data_7HZ6
# 
_entry.id   7HZ6 
# 
_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   7HZ6         pdb_00007hz6 10.2210/pdb7hz6/pdb 
WWPDB D_1001408114 ?            ?                   
# 
_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                        7HZ6 
_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 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(2-aminopyridin-3-yl)acetyl]piperidine-3-carboxamide' 262.308   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                     65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                           78.133    2   ?         ? ? ? 
5 water       nat water                                                          18.015    339 ?         ? ? ? 
# 
_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,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[(2-aminopyridin-3-yl)acetyl]piperidine-3-carboxamide' A1BQG 
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 
A1BQG non-polymer         . '(3S)-1-[(2-aminopyridin-3-yl)acetyl]piperidine-3-carboxamide' ? 'C13 H18 N4 O2'  262.308 
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 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 ?   ?   ?   C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BQG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BQG 
_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 
C 2 A1BQG 1   201 201 A1BQG LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 6   DMS   DMS A . 
F 2 A1BQG 1   201 201 A1BQG LIG C . 
G 3 ZN    1   202 1   ZN    ZN  C . 
H 4 DMS   1   203 2   DMS   DMS C . 
I 5 HOH   1   301 75  HOH   HOH A . 
I 5 HOH   2   302 95  HOH   HOH A . 
I 5 HOH   3   303 25  HOH   HOH A . 
I 5 HOH   4   304 65  HOH   HOH A . 
I 5 HOH   5   305 3   HOH   HOH A . 
I 5 HOH   6   306 239 HOH   HOH A . 
I 5 HOH   7   307 36  HOH   HOH A . 
I 5 HOH   8   308 142 HOH   HOH A . 
I 5 HOH   9   309 176 HOH   HOH A . 
I 5 HOH   10  310 84  HOH   HOH A . 
I 5 HOH   11  311 23  HOH   HOH A . 
I 5 HOH   12  312 61  HOH   HOH A . 
I 5 HOH   13  313 34  HOH   HOH A . 
I 5 HOH   14  314 84  HOH   HOH A . 
I 5 HOH   15  315 66  HOH   HOH A . 
I 5 HOH   16  316 238 HOH   HOH A . 
I 5 HOH   17  317 152 HOH   HOH A . 
I 5 HOH   18  318 152 HOH   HOH A . 
I 5 HOH   19  319 103 HOH   HOH A . 
I 5 HOH   20  320 266 HOH   HOH A . 
I 5 HOH   21  321 7   HOH   HOH A . 
I 5 HOH   22  322 93  HOH   HOH A . 
I 5 HOH   23  323 13  HOH   HOH A . 
I 5 HOH   24  324 234 HOH   HOH A . 
I 5 HOH   25  325 113 HOH   HOH A . 
I 5 HOH   26  326 17  HOH   HOH A . 
I 5 HOH   27  327 22  HOH   HOH A . 
I 5 HOH   28  328 48  HOH   HOH A . 
I 5 HOH   29  329 56  HOH   HOH A . 
I 5 HOH   30  330 59  HOH   HOH A . 
I 5 HOH   31  331 85  HOH   HOH A . 
I 5 HOH   32  332 140 HOH   HOH A . 
I 5 HOH   33  333 270 HOH   HOH A . 
I 5 HOH   34  334 49  HOH   HOH A . 
I 5 HOH   35  335 70  HOH   HOH A . 
I 5 HOH   36  336 109 HOH   HOH A . 
I 5 HOH   37  337 27  HOH   HOH A . 
I 5 HOH   38  338 63  HOH   HOH A . 
I 5 HOH   39  339 116 HOH   HOH A . 
I 5 HOH   40  340 32  HOH   HOH A . 
I 5 HOH   41  341 256 HOH   HOH A . 
I 5 HOH   42  342 171 HOH   HOH A . 
I 5 HOH   43  343 30  HOH   HOH A . 
I 5 HOH   44  344 14  HOH   HOH A . 
I 5 HOH   45  345 24  HOH   HOH A . 
I 5 HOH   46  346 19  HOH   HOH A . 
I 5 HOH   47  347 5   HOH   HOH A . 
I 5 HOH   48  348 235 HOH   HOH A . 
I 5 HOH   49  349 22  HOH   HOH A . 
I 5 HOH   50  350 63  HOH   HOH A . 
I 5 HOH   51  351 66  HOH   HOH A . 
I 5 HOH   52  352 71  HOH   HOH A . 
I 5 HOH   53  353 56  HOH   HOH A . 
I 5 HOH   54  354 72  HOH   HOH A . 
I 5 HOH   55  355 60  HOH   HOH A . 
I 5 HOH   56  356 10  HOH   HOH A . 
I 5 HOH   57  357 272 HOH   HOH A . 
I 5 HOH   58  358 119 HOH   HOH A . 
I 5 HOH   59  359 265 HOH   HOH A . 
I 5 HOH   60  360 45  HOH   HOH A . 
I 5 HOH   61  361 76  HOH   HOH A . 
I 5 HOH   62  362 169 HOH   HOH A . 
I 5 HOH   63  363 26  HOH   HOH A . 
I 5 HOH   64  364 18  HOH   HOH A . 
I 5 HOH   65  365 99  HOH   HOH A . 
I 5 HOH   66  366 102 HOH   HOH A . 
I 5 HOH   67  367 35  HOH   HOH A . 
I 5 HOH   68  368 29  HOH   HOH A . 
I 5 HOH   69  369 33  HOH   HOH A . 
I 5 HOH   70  370 53  HOH   HOH A . 
I 5 HOH   71  371 230 HOH   HOH A . 
I 5 HOH   72  372 4   HOH   HOH A . 
I 5 HOH   73  373 10  HOH   HOH A . 
I 5 HOH   74  374 229 HOH   HOH A . 
I 5 HOH   75  375 128 HOH   HOH A . 
I 5 HOH   76  376 42  HOH   HOH A . 
I 5 HOH   77  377 21  HOH   HOH A . 
I 5 HOH   78  378 115 HOH   HOH A . 
I 5 HOH   79  379 79  HOH   HOH A . 
I 5 HOH   80  380 115 HOH   HOH A . 
I 5 HOH   81  381 86  HOH   HOH A . 
I 5 HOH   82  382 19  HOH   HOH A . 
I 5 HOH   83  383 242 HOH   HOH A . 
I 5 HOH   84  384 12  HOH   HOH A . 
I 5 HOH   85  385 255 HOH   HOH A . 
I 5 HOH   86  386 106 HOH   HOH A . 
I 5 HOH   87  387 101 HOH   HOH A . 
I 5 HOH   88  388 75  HOH   HOH A . 
I 5 HOH   89  389 149 HOH   HOH A . 
I 5 HOH   90  390 245 HOH   HOH A . 
I 5 HOH   91  391 119 HOH   HOH A . 
I 5 HOH   92  392 23  HOH   HOH A . 
I 5 HOH   93  393 60  HOH   HOH A . 
I 5 HOH   94  394 14  HOH   HOH A . 
I 5 HOH   95  395 240 HOH   HOH A . 
I 5 HOH   96  396 258 HOH   HOH A . 
I 5 HOH   97  397 150 HOH   HOH A . 
I 5 HOH   98  398 254 HOH   HOH A . 
I 5 HOH   99  399 197 HOH   HOH A . 
I 5 HOH   100 400 88  HOH   HOH A . 
I 5 HOH   101 401 111 HOH   HOH A . 
I 5 HOH   102 402 125 HOH   HOH A . 
I 5 HOH   103 403 101 HOH   HOH A . 
I 5 HOH   104 404 223 HOH   HOH A . 
I 5 HOH   105 405 127 HOH   HOH A . 
I 5 HOH   106 406 96  HOH   HOH A . 
I 5 HOH   107 407 228 HOH   HOH A . 
I 5 HOH   108 408 73  HOH   HOH A . 
I 5 HOH   109 409 47  HOH   HOH A . 
I 5 HOH   110 410 55  HOH   HOH A . 
I 5 HOH   111 411 40  HOH   HOH A . 
I 5 HOH   112 412 52  HOH   HOH A . 
I 5 HOH   113 413 12  HOH   HOH A . 
I 5 HOH   114 414 92  HOH   HOH A . 
I 5 HOH   115 415 16  HOH   HOH A . 
I 5 HOH   116 416 49  HOH   HOH A . 
I 5 HOH   117 417 144 HOH   HOH A . 
I 5 HOH   118 418 253 HOH   HOH A . 
I 5 HOH   119 419 53  HOH   HOH A . 
I 5 HOH   120 420 36  HOH   HOH A . 
I 5 HOH   121 421 26  HOH   HOH A . 
I 5 HOH   122 422 85  HOH   HOH A . 
I 5 HOH   123 423 102 HOH   HOH A . 
I 5 HOH   124 424 35  HOH   HOH A . 
I 5 HOH   125 425 267 HOH   HOH A . 
I 5 HOH   126 426 77  HOH   HOH A . 
I 5 HOH   127 427 91  HOH   HOH A . 
I 5 HOH   128 428 21  HOH   HOH A . 
I 5 HOH   129 429 262 HOH   HOH A . 
I 5 HOH   130 430 100 HOH   HOH A . 
I 5 HOH   131 431 112 HOH   HOH A . 
I 5 HOH   132 432 151 HOH   HOH A . 
I 5 HOH   133 433 209 HOH   HOH A . 
I 5 HOH   134 434 38  HOH   HOH A . 
I 5 HOH   135 435 202 HOH   HOH A . 
I 5 HOH   136 436 153 HOH   HOH A . 
I 5 HOH   137 437 61  HOH   HOH A . 
I 5 HOH   138 438 15  HOH   HOH A . 
I 5 HOH   139 439 208 HOH   HOH A . 
I 5 HOH   140 440 126 HOH   HOH A . 
I 5 HOH   141 441 149 HOH   HOH A . 
I 5 HOH   142 442 177 HOH   HOH A . 
I 5 HOH   143 443 8   HOH   HOH A . 
I 5 HOH   144 444 181 HOH   HOH A . 
I 5 HOH   145 445 157 HOH   HOH A . 
I 5 HOH   146 446 154 HOH   HOH A . 
I 5 HOH   147 447 145 HOH   HOH A . 
I 5 HOH   148 448 24  HOH   HOH A . 
I 5 HOH   149 449 150 HOH   HOH A . 
I 5 HOH   150 450 154 HOH   HOH A . 
I 5 HOH   151 451 136 HOH   HOH A . 
I 5 HOH   152 452 172 HOH   HOH A . 
I 5 HOH   153 453 178 HOH   HOH A . 
I 5 HOH   154 454 72  HOH   HOH A . 
I 5 HOH   155 455 138 HOH   HOH A . 
I 5 HOH   156 456 216 HOH   HOH A . 
I 5 HOH   157 457 92  HOH   HOH A . 
I 5 HOH   158 458 67  HOH   HOH A . 
I 5 HOH   159 459 82  HOH   HOH A . 
I 5 HOH   160 460 90  HOH   HOH A . 
I 5 HOH   161 461 99  HOH   HOH A . 
I 5 HOH   162 462 59  HOH   HOH A . 
I 5 HOH   163 463 187 HOH   HOH A . 
I 5 HOH   164 464 221 HOH   HOH A . 
J 5 HOH   1   301 192 HOH   HOH C . 
J 5 HOH   2   302 120 HOH   HOH C . 
J 5 HOH   3   303 128 HOH   HOH C . 
J 5 HOH   4   304 89  HOH   HOH C . 
J 5 HOH   5   305 34  HOH   HOH C . 
J 5 HOH   6   306 184 HOH   HOH C . 
J 5 HOH   7   307 64  HOH   HOH C . 
J 5 HOH   8   308 174 HOH   HOH C . 
J 5 HOH   9   309 134 HOH   HOH C . 
J 5 HOH   10  310 137 HOH   HOH C . 
J 5 HOH   11  311 117 HOH   HOH C . 
J 5 HOH   12  312 8   HOH   HOH C . 
J 5 HOH   13  313 51  HOH   HOH C . 
J 5 HOH   14  314 248 HOH   HOH C . 
J 5 HOH   15  315 121 HOH   HOH C . 
J 5 HOH   16  316 103 HOH   HOH C . 
J 5 HOH   17  317 231 HOH   HOH C . 
J 5 HOH   18  318 65  HOH   HOH C . 
J 5 HOH   19  319 69  HOH   HOH C . 
J 5 HOH   20  320 70  HOH   HOH C . 
J 5 HOH   21  321 249 HOH   HOH C . 
J 5 HOH   22  322 97  HOH   HOH C . 
J 5 HOH   23  323 155 HOH   HOH C . 
J 5 HOH   24  324 32  HOH   HOH C . 
J 5 HOH   25  325 43  HOH   HOH C . 
J 5 HOH   26  326 2   HOH   HOH C . 
J 5 HOH   27  327 50  HOH   HOH C . 
J 5 HOH   28  328 28  HOH   HOH C . 
J 5 HOH   29  329 271 HOH   HOH C . 
J 5 HOH   30  330 97  HOH   HOH C . 
J 5 HOH   31  331 123 HOH   HOH C . 
J 5 HOH   32  332 33  HOH   HOH C . 
J 5 HOH   33  333 264 HOH   HOH C . 
J 5 HOH   34  334 80  HOH   HOH C . 
J 5 HOH   35  335 210 HOH   HOH C . 
J 5 HOH   36  336 39  HOH   HOH C . 
J 5 HOH   37  337 138 HOH   HOH C . 
J 5 HOH   38  338 195 HOH   HOH C . 
J 5 HOH   39  339 46  HOH   HOH C . 
J 5 HOH   40  340 212 HOH   HOH C . 
J 5 HOH   41  341 204 HOH   HOH C . 
J 5 HOH   42  342 20  HOH   HOH C . 
J 5 HOH   43  343 11  HOH   HOH C . 
J 5 HOH   44  344 130 HOH   HOH C . 
J 5 HOH   45  345 133 HOH   HOH C . 
J 5 HOH   46  346 98  HOH   HOH C . 
J 5 HOH   47  347 247 HOH   HOH C . 
J 5 HOH   48  348 259 HOH   HOH C . 
J 5 HOH   49  349 121 HOH   HOH C . 
J 5 HOH   50  350 122 HOH   HOH C . 
J 5 HOH   51  351 260 HOH   HOH C . 
J 5 HOH   52  352 241 HOH   HOH C . 
J 5 HOH   53  353 111 HOH   HOH C . 
J 5 HOH   54  354 126 HOH   HOH C . 
J 5 HOH   55  355 74  HOH   HOH C . 
J 5 HOH   56  356 67  HOH   HOH C . 
J 5 HOH   57  357 124 HOH   HOH C . 
J 5 HOH   58  358 30  HOH   HOH C . 
J 5 HOH   59  359 38  HOH   HOH C . 
J 5 HOH   60  360 118 HOH   HOH C . 
J 5 HOH   61  361 73  HOH   HOH C . 
J 5 HOH   62  362 269 HOH   HOH C . 
J 5 HOH   63  363 15  HOH   HOH C . 
J 5 HOH   64  364 252 HOH   HOH C . 
J 5 HOH   65  365 98  HOH   HOH C . 
J 5 HOH   66  366 136 HOH   HOH C . 
J 5 HOH   67  367 64  HOH   HOH C . 
J 5 HOH   68  368 243 HOH   HOH C . 
J 5 HOH   69  369 257 HOH   HOH C . 
J 5 HOH   70  370 4   HOH   HOH C . 
J 5 HOH   71  371 37  HOH   HOH C . 
J 5 HOH   72  372 110 HOH   HOH C . 
J 5 HOH   73  373 79  HOH   HOH C . 
J 5 HOH   74  374 6   HOH   HOH C . 
J 5 HOH   75  375 1   HOH   HOH C . 
J 5 HOH   76  376 263 HOH   HOH C . 
J 5 HOH   77  377 78  HOH   HOH C . 
J 5 HOH   78  378 57  HOH   HOH C . 
J 5 HOH   79  379 39  HOH   HOH C . 
J 5 HOH   80  380 148 HOH   HOH C . 
J 5 HOH   81  381 9   HOH   HOH C . 
J 5 HOH   82  382 37  HOH   HOH C . 
J 5 HOH   83  383 13  HOH   HOH C . 
J 5 HOH   84  384 7   HOH   HOH C . 
J 5 HOH   85  385 29  HOH   HOH C . 
J 5 HOH   86  386 86  HOH   HOH C . 
J 5 HOH   87  387 71  HOH   HOH C . 
J 5 HOH   88  388 191 HOH   HOH C . 
J 5 HOH   89  389 108 HOH   HOH C . 
J 5 HOH   90  390 246 HOH   HOH C . 
J 5 HOH   91  391 233 HOH   HOH C . 
J 5 HOH   92  392 80  HOH   HOH C . 
J 5 HOH   93  393 11  HOH   HOH C . 
J 5 HOH   94  394 237 HOH   HOH C . 
J 5 HOH   95  395 54  HOH   HOH C . 
J 5 HOH   96  396 62  HOH   HOH C . 
J 5 HOH   97  397 124 HOH   HOH C . 
J 5 HOH   98  398 251 HOH   HOH C . 
J 5 HOH   99  399 87  HOH   HOH C . 
J 5 HOH   100 400 232 HOH   HOH C . 
J 5 HOH   101 401 50  HOH   HOH C . 
J 5 HOH   102 402 83  HOH   HOH C . 
J 5 HOH   103 403 48  HOH   HOH C . 
J 5 HOH   104 404 146 HOH   HOH C . 
J 5 HOH   105 405 45  HOH   HOH C . 
J 5 HOH   106 406 52  HOH   HOH C . 
J 5 HOH   107 407 40  HOH   HOH C . 
J 5 HOH   108 408 261 HOH   HOH C . 
J 5 HOH   109 409 31  HOH   HOH C . 
J 5 HOH   110 410 41  HOH   HOH C . 
J 5 HOH   111 411 44  HOH   HOH C . 
J 5 HOH   112 412 91  HOH   HOH C . 
J 5 HOH   113 413 16  HOH   HOH C . 
J 5 HOH   114 414 89  HOH   HOH C . 
J 5 HOH   115 415 54  HOH   HOH C . 
J 5 HOH   116 416 139 HOH   HOH C . 
J 5 HOH   117 417 140 HOH   HOH C . 
J 5 HOH   118 418 244 HOH   HOH C . 
J 5 HOH   119 419 132 HOH   HOH C . 
J 5 HOH   120 420 120 HOH   HOH C . 
J 5 HOH   121 421 68  HOH   HOH C . 
J 5 HOH   122 422 268 HOH   HOH C . 
J 5 HOH   123 423 47  HOH   HOH C . 
J 5 HOH   124 424 127 HOH   HOH C . 
J 5 HOH   125 425 3   HOH   HOH C . 
J 5 HOH   126 426 20  HOH   HOH C . 
J 5 HOH   127 427 137 HOH   HOH C . 
J 5 HOH   128 428 44  HOH   HOH C . 
J 5 HOH   129 429 110 HOH   HOH C . 
J 5 HOH   130 430 144 HOH   HOH C . 
J 5 HOH   131 431 90  HOH   HOH C . 
J 5 HOH   132 432 200 HOH   HOH C . 
J 5 HOH   133 433 83  HOH   HOH C . 
J 5 HOH   134 434 105 HOH   HOH C . 
J 5 HOH   135 435 135 HOH   HOH C . 
J 5 HOH   136 436 43  HOH   HOH C . 
J 5 HOH   137 437 236 HOH   HOH C . 
J 5 HOH   138 438 41  HOH   HOH C . 
J 5 HOH   139 439 141 HOH   HOH C . 
J 5 HOH   140 440 104 HOH   HOH C . 
J 5 HOH   141 441 5   HOH   HOH C . 
J 5 HOH   142 442 95  HOH   HOH C . 
J 5 HOH   143 443 107 HOH   HOH C . 
J 5 HOH   144 444 131 HOH   HOH C . 
J 5 HOH   145 445 117 HOH   HOH C . 
J 5 HOH   146 446 148 HOH   HOH C . 
J 5 HOH   147 447 116 HOH   HOH C . 
J 5 HOH   148 448 158 HOH   HOH C . 
J 5 HOH   149 449 250 HOH   HOH C . 
J 5 HOH   150 450 185 HOH   HOH C . 
J 5 HOH   151 451 9   HOH   HOH C . 
J 5 HOH   152 452 109 HOH   HOH C . 
J 5 HOH   153 453 162 HOH   HOH C . 
J 5 HOH   154 454 27  HOH   HOH C . 
J 5 HOH   155 455 17  HOH   HOH C . 
J 5 HOH   156 456 147 HOH   HOH C . 
J 5 HOH   157 457 142 HOH   HOH C . 
J 5 HOH   158 458 93  HOH   HOH C . 
J 5 HOH   159 459 151 HOH   HOH C . 
J 5 HOH   160 460 198 HOH   HOH C . 
J 5 HOH   161 461 146 HOH   HOH C . 
J 5 HOH   162 462 189 HOH   HOH C . 
J 5 HOH   163 463 199 HOH   HOH C . 
J 5 HOH   164 464 132 HOH   HOH C . 
J 5 HOH   165 465 123 HOH   HOH C . 
J 5 HOH   166 466 222 HOH   HOH C . 
J 5 HOH   167 467 118 HOH   HOH C . 
J 5 HOH   168 468 218 HOH   HOH C . 
J 5 HOH   169 469 141 HOH   HOH C . 
J 5 HOH   170 470 196 HOH   HOH C . 
J 5 HOH   171 471 215 HOH   HOH C . 
J 5 HOH   172 472 129 HOH   HOH C . 
J 5 HOH   173 473 207 HOH   HOH C . 
J 5 HOH   174 474 147 HOH   HOH C . 
J 5 HOH   175 475 143 HOH   HOH C . 
# 
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           7HZ6 
_cell.length_a           72.519 
_cell.length_b           61.593 
_cell.length_c           65.184 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.70 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HZ6 
_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          7HZ6 
_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   46.23 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-12-13 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92203 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HZ6 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             37.52 
_reflns.d_resolution_high            1.30 
_reflns.number_obs                   68332 
_reflns.percent_possible_obs         97.1 
_reflns.pdbx_Rmerge_I_obs            0.072 
_reflns.pdbx_netI_over_sigmaI        12.9 
_reflns.pdbx_redundancy              5.7 
_reflns.pdbx_Rrim_I_all              0.079 
_reflns.pdbx_Rpim_I_all              0.031 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     391881 
_reflns.pdbx_chi_squared             0.82 
_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                  1.30 
_reflns_shell.d_res_low                   1.32 
_reflns_shell.number_measured_all         6462 
_reflns_shell.number_unique_obs           2531 
_reflns_shell.Rmerge_I_obs                1.202 
_reflns_shell.pdbx_chi_squared            0.40 
_reflns_shell.pdbx_redundancy             2.6 
_reflns_shell.percent_possible_obs        72.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             1.538 
_reflns_shell.pdbx_Rpim_I_all             0.935 
_reflns_shell.pdbx_CC_half                0.288 
_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                                 7HZ6 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     68293 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.02 
_refine.ls_d_res_high                            1.300 
_refine.ls_percent_reflns_obs                    97.0 
_refine.ls_R_factor_obs                          0.2000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1987 
_refine.ls_R_factor_R_free                       0.2267 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.860 
_refine.ls_number_reflns_R_free                  3322 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.B_iso_mean                               23.09 
_refine.aniso_B[1][1]                            -1.20680 
_refine.aniso_B[2][2]                            1.16690 
_refine.aniso_B[3][3]                            0.03990 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.34340 
_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             0.054 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.057 
_refine.pdbx_overall_SU_R_Blow_DPI               0.057 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.060 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HZ6 
_refine_analyze.Luzzati_coordinate_error_obs    0.18 
_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        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.number_atoms_solvent             339 
_refine_hist.number_atoms_total               2535 
_refine_hist.d_res_high                       1.300 
_refine_hist.d_res_low                        19.02 
# 
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  2254 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.07  ? 2.00  3066 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  752  '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  406  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2254 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.69  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.75 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  276  '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  2181 '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                       1.30 
_refine_ls_shell.d_res_low                        1.31 
_refine_ls_shell.number_reflns_R_work             1325 
_refine_ls_shell.R_factor_R_work                  0.3550 
_refine_ls_shell.percent_reflns_obs               67.93 
_refine_ls_shell.R_factor_R_free                  0.2885 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            3.00 
_refine_ls_shell.number_reflns_R_free             41 
_refine_ls_shell.number_reflns_all                1366 
_refine_ls_shell.R_factor_all                     0.3530 
# 
_struct.entry_id                  7HZ6 
_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-0036406-001 (A71EV2A-x4489)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HZ6 
_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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J 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 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HZ6 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HZ6 C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,I 
2 1 B,F,G,H,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 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 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.357 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.266 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.312 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.303 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 G ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
# 
_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 ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 108.8 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.5 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.7 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 107.9 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.6 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 115.1 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.0 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.8 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 116.9 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 108.4 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.8 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 113.7 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 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 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 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  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 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  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7HZ6 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O C HOH 301 ? ? O C HOH 381 ? ? 1.20 
2  1 O C HOH 427 ? ? O C HOH 429 ? ? 1.21 
3  1 O A HOH 305 ? ? O A HOH 326 ? ? 1.40 
4  1 O A HOH 336 ? ? O C HOH 306 ? ? 1.63 
5  1 O A HOH 303 ? ? O A HOH 304 ? ? 1.79 
6  1 O A HOH 305 ? ? O A HOH 373 ? ? 1.81 
7  1 O C HOH 311 ? ? O C HOH 448 ? ? 1.82 
8  1 O A HOH 364 ? ? O A HOH 372 ? ? 1.92 
9  1 O A HOH 357 ? ? O A HOH 386 ? ? 2.04 
10 1 O A HOH 343 ? ? O A HOH 360 ? ? 2.04 
11 1 O A HOH 381 ? ? O A HOH 410 ? ? 2.07 
12 1 O A HOH 357 ? ? O A HOH 376 ? ? 2.10 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 19.6436 6.7522   18.3336 -0.0336 -0.0197 0.0007  0.0017  0.0056  -0.0007 1.1208 2.4297 0.5131 
-1.0972 -0.4495 0.5864  -0.0469 -0.0190 0.1106 0.0106 0.0862 0.0349  0.0328  0.0489  -0.0393 
'X-RAY DIFFRACTION' 2 ? refined 15.2473 -23.9302 14.1545 -0.0241 -0.0149 -0.0024 -0.0013 -0.0024 -0.0040 0.8375 2.1411 0.4446 
0.7432  -0.0340 -0.3175 -0.0395 0.0352  0.0708 0.0692 0.0622 -0.0481 -0.0183 -0.0314 -0.0227 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
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 
6  1 Y 1 C GLU 146 ? B GLU 140 
7  1 Y 1 C ALA 147 ? B ALA 141 
8  1 Y 1 C MET 148 ? B MET 142 
9  1 Y 1 C GLU 149 ? B GLU 143 
10 1 Y 1 C GLN 150 ? B 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 
A1BQG N1   N  N N 1   
A1BQG N3   N  N N 2   
A1BQG C4   C  N N 3   
A1BQG C5   C  N N 4   
A1BQG C6   C  N N 5   
A1BQG C7   C  Y N 6   
A1BQG C8   C  Y N 7   
A1BQG C10  C  Y N 8   
A1BQG O1   O  N N 9   
A1BQG C3   C  N N 10  
A1BQG C2   C  N N 11  
A1BQG C12  C  N N 12  
A1BQG C1   C  N S 13  
A1BQG C    C  N N 14  
A1BQG O    O  N N 15  
A1BQG N    N  N N 16  
A1BQG C11  C  Y N 17  
A1BQG N2   N  Y N 18  
A1BQG C9   C  Y N 19  
A1BQG H14  H  N N 20  
A1BQG H15  H  N N 21  
A1BQG H8   H  N N 22  
A1BQG H7   H  N N 23  
A1BQG H10  H  N N 24  
A1BQG H9   H  N N 25  
A1BQG H11  H  N N 26  
A1BQG H13  H  N N 27  
A1BQG H6   H  N N 28  
A1BQG H5   H  N N 29  
A1BQG H4   H  N N 30  
A1BQG H3   H  N N 31  
A1BQG H17  H  N N 32  
A1BQG H16  H  N N 33  
A1BQG H    H  N N 34  
A1BQG H1   H  N N 35  
A1BQG H2   H  N N 36  
A1BQG H12  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BQG N   C    sing N N 1   
A1BQG O   C    doub N N 2   
A1BQG C   C1   sing N N 3   
A1BQG C1  C2   sing N N 4   
A1BQG C2  C3   sing N N 5   
A1BQG C3  C4   sing N N 6   
A1BQG C4  N1   sing N N 7   
A1BQG N1  C5   sing N N 8   
A1BQG C5  O1   doub N N 9   
A1BQG C6  C5   sing N N 10  
A1BQG C7  C6   sing N N 11  
A1BQG C7  C8   doub Y N 12  
A1BQG C8  C9   sing Y N 13  
A1BQG C9  C10  doub Y N 14  
A1BQG C10 N2   sing Y N 15  
A1BQG N2  C11  doub Y N 16  
A1BQG C11 C7   sing Y N 17  
A1BQG N3  C11  sing N N 18  
A1BQG C12 N1   sing N N 19  
A1BQG C1  C12  sing N N 20  
A1BQG N3  H14  sing N N 21  
A1BQG N3  H15  sing N N 22  
A1BQG C4  H8   sing N N 23  
A1BQG C4  H7   sing N N 24  
A1BQG C6  H10  sing N N 25  
A1BQG C6  H9   sing N N 26  
A1BQG C8  H11  sing N N 27  
A1BQG C10 H13  sing N N 28  
A1BQG C3  H6   sing N N 29  
A1BQG C3  H5   sing N N 30  
A1BQG C2  H4   sing N N 31  
A1BQG C2  H3   sing N N 32  
A1BQG C12 H17  sing N N 33  
A1BQG C12 H16  sing N N 34  
A1BQG C1  H    sing N N 35  
A1BQG N   H1   sing N N 36  
A1BQG N   H2   sing N N 37  
A1BQG C9  H12  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HZ6 
_atom_sites.fract_transf_matrix[1][1]   0.013789 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000650 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016236 
_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]   0.015358 
_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   ? 16.296 6.437   8.183  1.00 20.72  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.066 6.513   8.993  1.00 20.62  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 14.938 5.371   9.962  1.00 20.20  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.618 4.347   9.806  1.00 20.02  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 13.837 6.579   8.077  1.00 24.27  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.700 5.357   7.370  1.00 27.37  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.088 5.547   10.991 1.00 18.29  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.801 4.508   11.960 1.00 17.21  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.434 5.053   13.325 1.00 16.50  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.804 6.179   13.665 1.00 16.94  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.684 4.281   14.095 1.00 14.69  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.286 4.668   15.421 1.00 15.87  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.243 3.471   16.383 1.00 16.23  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.213 2.297   15.933 1.00 16.78  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.892 5.289   15.336 1.00 17.44  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.231 3.748   17.704 1.00 13.88  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 12.001 2.766   18.766 1.00 14.98  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.598 2.987   19.280 1.00 15.17  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.231 4.119   19.590 1.00 15.64  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 13.000 2.934   19.951 1.00 14.86  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.463 2.892   19.446 1.00 14.77  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.797 1.853   21.007 1.00 17.23  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.419 3.475   20.548 1.00 14.93  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.811  1.899   19.394 1.00 16.38  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.453  1.994   19.934 1.00 18.38  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.372  1.225   21.230 1.00 18.80  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.460  0.005   21.210 1.00 20.73  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.462  1.404   18.923 1.00 18.37  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.390  2.224   17.660 1.00 19.58  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.574  3.340   17.581 1.00 20.56  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.185  1.922   16.569 1.00 21.19  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.521  4.117   16.433 1.00 21.77  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.152  2.695   15.421 1.00 22.01  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.302  3.784   15.351 1.00 22.55  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.288  4.593   14.243 1.00 26.15  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.327  1.920   22.364 1.00 18.65  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.313  1.294   23.690 1.00 19.71  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.175  1.899   24.500 1.00 21.04  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 7.096  3.113   24.615 1.00 21.33  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.690  1.468   24.408 1.00 22.86  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.187 2.914   24.350 1.00 23.28  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.620  0.988   25.849 1.00 25.12  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.215  1.075   24.966 1.00 22.45  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 5.085  1.588   25.727 1.00 23.08  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.276  2.556   24.894 1.00 23.63  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 4.060  2.290   23.703 1.00 24.61  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 3.975  3.725   25.440 1.00 23.53  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.285  4.747   24.661 1.00 23.06  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.248  5.819   24.168 1.00 20.44  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.866  6.976   24.012 1.00 21.24  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 2.139  5.370   25.445 1.00 26.66  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 1.002  4.418   25.590 1.00 35.45  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.368  4.023   24.598 1.00 38.62  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.773  3.993   26.815 1.00 36.74  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.477  5.413   23.825 1.00 18.60  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.487  6.371   23.358 1.00 18.08  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 7.066  5.928   22.016 1.00 16.49  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.207  4.719   21.762 1.00 16.83  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.656  6.426   24.368 1.00 18.55  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.268  6.961   25.728 1.00 19.64  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.642  8.189   25.858 1.00 21.16  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.559  6.250   26.887 1.00 22.33  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.321  8.704   27.103 1.00 22.44  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.216  6.746   28.140 1.00 23.28  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.563  7.962   28.236 1.00 24.46  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.256  8.514   29.461 1.00 28.27  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.491  6.924   21.210 1.00 15.39  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.191  6.738   19.958 1.00 15.21  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.507  7.547   20.116 1.00 15.06  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.465  8.738   20.427 1.00 15.73  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.350  7.240   18.770 1.00 15.30  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.094  7.498   17.456 1.00 18.27  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.147  7.865   16.299 1.00 18.74  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.735  8.852   15.388 1.00 21.28  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.219  8.607   14.182 1.00 23.40  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.332  7.347   13.743 1.00 24.01  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.705  9.597   13.445 1.00 23.73  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.672 6.872   19.963 1.00 14.47  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 11.974 7.546   20.084 1.00 14.15  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.531 7.663   18.681 1.00 14.11  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.716 6.640   17.996 1.00 13.68  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 12.968 6.720   20.960 1.00 14.58  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.256 7.554   21.200 1.00 14.43  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.327 6.224   22.273 1.00 15.82  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.858 8.886   18.256 1.00 12.26  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.398 9.152   16.914 1.00 12.70  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.634 10.048  17.011 1.00 11.49  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.848 10.734  18.024 1.00 12.97  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.343 9.825   15.984 1.00 14.88  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.243 8.833   15.639 1.00 19.05  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.786 11.125  16.617 1.00 15.45  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.408 10.149  15.914 1.00 11.04  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.453 11.178  15.832 1.00 11.36  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.743 12.530  15.828 1.00 13.23  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.798 12.751  15.031 1.00 13.18  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.261 11.073  14.508 1.00 11.96  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.060 9.805   14.420 1.00 13.04  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.564 8.771   13.890 1.00 14.20  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.260 9.839   14.959 1.00 13.25  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.214 13.479  16.666 1.00 11.51  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.545 14.796  16.749 1.00 11.73  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.542 15.477  15.376 1.00 13.71  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.525 16.084  15.000 1.00 14.67  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.240 15.643  17.798 1.00 12.45  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.436 16.933  18.130 1.00 13.16  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.364 17.792  18.982 1.00 14.48  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.735 19.033  19.483 1.00 14.79  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.750 20.183  18.825 1.00 15.43  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.185 20.233  17.575 1.00 15.93  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.235 21.284  19.384 1.00 15.91  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.632 15.304  14.580 1.00 13.14  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.714 15.974  13.261 1.00 14.78  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.779 15.372  12.210 1.00 15.76  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.560 16.006  11.162 1.00 19.16  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.184 16.065  12.746 1.00 15.00  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.769 14.770  12.239 1.00 15.56  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.367 13.851  13.094 1.00 15.13  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 18.898 14.326  10.963 1.00 16.40  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.792 12.845  12.321 1.00 16.35  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.557 13.099  11.023 1.00 16.62  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.200 14.204  12.476 1.00 14.92  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.258 13.569  11.557 1.00 15.18  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.806 13.590  12.114 1.00 15.83  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 11.905 13.020  11.494 1.00 17.47  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.697 12.117  11.281 1.00 14.93  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.053 12.000  10.587 1.00 16.43  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.387 10.539  10.348 1.00 16.87  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.066 12.795  9.257  1.00 16.69  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.572 14.246  13.292 1.00 16.00  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.229 14.251  13.868 1.00 15.62  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.243 14.951  12.913 1.00 17.01  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.582 15.916  12.251 1.00 17.64  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.222 14.982  15.209 1.00 16.45  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.035  14.418  12.876 1.00 17.66  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 7.993  14.946  11.967 1.00 19.10  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.171  16.027  12.664 1.00 20.76  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.284  16.213  13.885 1.00 20.37  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.057  13.781  11.550 1.00 20.98  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.343  13.337  12.709 1.00 20.59  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.792  12.618  10.926 1.00 22.27  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.217  16.662  11.919 1.00 21.86  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.308  17.610  12.546 1.00 22.93  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.495  16.922  13.641 1.00 20.21  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.321  17.477  14.723 1.00 21.63  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.316  18.189  11.499 1.00 27.37  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 4.969  19.010  10.437 1.00 37.65  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.759  20.103  10.753 1.00 41.96  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 4.900  18.893  9.088  1.00 41.05  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.177  20.592  9.593  1.00 43.07  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.674  19.904  8.560  1.00 43.10  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.051  15.665  13.377 1.00 21.10  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.273  14.949  14.378 1.00 20.13  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.101  14.623  15.621 1.00 19.49  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.583  14.653  16.748 1.00 19.55  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.686  13.680  13.805 1.00 23.97  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.432  13.972  13.067 1.00 31.59  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.622  14.830  13.480 1.00 32.33  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 1.283  13.321  11.919 1.00 33.90  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.411  14.288  15.450 1.00 17.35  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.257  14.081  16.642 1.00 17.18  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.277  15.327  17.532 1.00 16.80  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.157  15.232  18.774 1.00 16.68  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.694  13.742  16.227 1.00 16.36  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.858  12.329  15.727 1.00 17.81  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.228  11.441  16.291 1.00 19.25  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.577  12.142  14.703 1.00 19.30  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.481  16.499  16.900 1.00 16.15  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.547  17.747  17.665 1.00 16.62  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.209  18.120  18.303 1.00 19.09  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.185  18.642  19.425 1.00 19.18  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.092  18.883  16.806 1.00 16.04  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.590  18.871  16.722 1.00 16.19  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.351  18.458  15.666 1.00 17.58  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.500  19.418  17.689 1.00 15.29  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.685 18.686  15.928 1.00 16.46  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.806 19.212  17.193 1.00 16.75  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.341  19.953  18.972 1.00 17.08  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 11.945 19.657  17.889 1.00 17.68  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.478 20.377  19.669 1.00 17.60  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.752 20.193  19.141 1.00 18.10  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.099  17.765  17.647 1.00 19.41  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.764  18.042  18.217 1.00 21.13  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.438  17.126  19.410 1.00 22.08  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.528  17.408  20.200 1.00 22.95  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.701  17.865  17.154 1.00 22.12  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.118  15.970  19.507 1.00 19.90  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 2.924  15.042  20.613 1.00 19.83  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.233  14.921  21.439 1.00 18.16  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.541  13.870  21.988 1.00 17.46  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.502  13.691  20.055 1.00 20.64  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.140  13.759  19.418 1.00 24.59  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.149  13.791  20.131 1.00 26.84  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 1.076  13.770  18.086 1.00 24.61  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 4.987  16.020  21.540 1.00 16.97  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.279  16.012  22.231 1.00 17.00  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.213  15.614  23.710 1.00 18.31  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.376  16.118  24.466 1.00 20.28  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 6.867  17.413  22.119 1.00 16.80  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.230  17.625  22.807 1.00 18.32  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.310  16.741  22.175 1.00 19.13  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.651  19.116  22.741 1.00 18.55  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.127  14.721  24.144 1.00 17.95  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.284  14.359  25.543 1.00 18.88  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.617  14.950  26.083 1.00 19.74  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.678  15.555  27.171 1.00 21.33  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.287  12.806  25.685 1.00 20.18  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.722  12.391  27.094 1.00 20.97  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 5.897  12.234  25.364 1.00 20.94  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.700  14.799  25.290 1.00 17.40  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 11.030 15.255  25.693 1.00 17.29  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 11.922 15.319  24.440 1.00 14.98  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.766 14.496  23.526 1.00 15.27  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.632 14.257  26.721 1.00 18.62  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 13.100 14.425  27.038 1.00 19.24  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.668 15.294  27.927 1.00 20.37  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.177 13.677  26.463 1.00 18.40  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 15.047 15.181  27.886 1.00 20.79  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.382 14.171  27.018 1.00 19.19  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.241 12.676  25.498 1.00 17.68  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.629 13.613  26.718 1.00 19.19  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.474 12.131  25.189 1.00 19.28  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.655 12.634  25.758 1.00 18.87  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.796 16.292  24.394 1.00 14.86  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.785 16.385  23.312 1.00 15.20  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 15.077 16.980  23.841 1.00 14.77  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 15.056 17.769  24.796 1.00 15.68  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.274 17.145  22.080 1.00 16.51  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.690 18.521  22.390 1.00 15.77  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.682 19.643  22.648 1.00 18.67  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.347 20.533  23.475 1.00 21.78  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.764 19.671  22.024 1.00 17.70  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.189 16.608  23.202 1.00 14.59  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.476 17.142  23.630 1.00 14.14  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.343 17.254  22.385 1.00 14.53  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.786 16.254  21.815 1.00 14.04  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 18.073 16.217  24.707 1.00 15.52  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.368 16.716  25.299 1.00 23.19  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.082 17.452  24.606 1.00 24.54  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.693 16.317  26.452 1.00 23.47  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.572 18.497  21.943 1.00 14.42  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.355 18.755  20.762 0.50 15.44  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.365 18.729  20.743 0.50 15.35  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.796 18.245  20.950 1.00 16.05  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.422 17.777  19.989 1.00 17.46  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.323 20.258  20.469 0.50 18.33  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.350 20.210  20.348 0.50 18.10  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 20.180 20.619  19.410 0.50 21.01  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 20.045 20.988  21.306 0.50 21.15  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.336 18.357  22.196 1.00 16.71  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.720 17.891  22.413 1.00 17.34  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 22.844 16.381  22.242 1.00 17.00  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 23.957 15.896  22.107 1.00 18.91  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.267 18.293  23.781 1.00 20.85  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.712 17.518  24.828 1.00 26.28  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.727 15.632  22.311 1.00 14.76  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.774 14.166  22.129 1.00 13.68  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.218 13.716  20.763 1.00 13.99  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.267 12.518  20.449 1.00 13.52  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 20.953 13.453  23.231 1.00 13.86  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.555 13.667  24.630 1.00 14.82  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.743 13.021  25.745 1.00 16.11  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.755 11.559  25.613 1.00 15.18  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.545 10.713  26.625 1.00 15.36  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.423 11.170  27.876 1.00 16.95  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.592 9.393   26.419 1.00 15.69  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.670 14.609  19.961 1.00 13.09  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 19.939 14.292  18.733 1.00 11.96  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.782 13.326  19.015 1.00 12.39  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.472 12.483  18.159 1.00 13.38  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 20.858 13.722  17.633 1.00 13.23  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.165 13.495  16.306 1.00 13.02  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.373 14.373  15.879 1.00 13.50  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.446 12.449  15.662 1.00 13.27  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.104 13.468  20.184 1.00 11.41  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 16.937 12.614  20.456 1.00 11.45  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.641 13.413  20.628 1.00 11.56  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.639 14.501  21.216 1.00 12.73  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.121 11.792  21.746 1.00 12.19  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.174 10.674  21.659 1.00 12.00  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.228 9.960   23.014 1.00 13.86  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.815 9.637   20.558 1.00 12.63  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.531 12.789  20.259 1.00 11.15  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.208 13.345  20.542 1.00 12.51  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.305 12.145  20.828 1.00 12.88  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.396 11.107  20.142 1.00 13.23  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.688 14.165  19.346 1.00 12.48  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.290 14.823  19.541 1.00 13.93  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.231 16.164  18.789 1.00 14.80  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.171 13.906  19.036 1.00 15.00  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.449 12.285  21.841 1.00 13.13  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.468 11.250  22.201 1.00 13.59  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 9.080  11.879  22.101 1.00 14.82  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 8.856  12.974  22.648 1.00 15.92  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.706 10.734  23.625 1.00 14.67  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.630  9.698   24.005 1.00 15.80  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 12.103 10.104  23.729 1.00 14.90  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.181  11.185  21.401 1.00 15.47  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.797  11.660  21.254 1.00 15.71  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.856  10.553  21.810 1.00 17.60  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.242  9.407   21.967 1.00 17.30  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.480  11.957  19.788 1.00 17.68  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.622  10.824  18.936 1.00 18.65  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.608  10.954  22.112 1.00 18.12  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.634  9.979   22.640 1.00 20.23  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 2.867  9.304   21.509 1.00 22.33  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.666  9.886   20.454 1.00 22.89  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.682  10.675  23.607 1.00 22.88  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 2.047  11.741  22.932 1.00 25.77  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.411  8.071   21.735 1.00 23.32  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.674  7.288   20.737 1.00 25.29  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.346  6.805   21.347 1.00 29.28  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.250  6.639   22.570 1.00 30.36  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.477  6.021   20.320 1.00 26.71  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.590  5.163   21.453 1.00 26.22  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.866  6.335   19.826 1.00 26.08  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.632 6.495   20.495 1.00 31.38  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -1.893 5.926   20.970 1.00 34.15  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.769 4.400   21.091 1.00 35.80  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.360 3.795   21.997 1.00 37.74  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -3.052 6.363   20.049 1.00 36.97  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.684 6.046   18.695 1.00 38.71  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.339 7.857   20.150 1.00 37.97  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -1.004 3.768   20.186 1.00 34.43  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.855 2.316   20.207 1.00 34.53  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.321  1.920   21.100 1.00 34.20  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.295  2.659   21.223 1.00 32.89  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.637 1.793   18.794 1.00 34.96  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.248  0.743   21.672 1.00 35.05  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.276  0.206   22.543 1.00 35.88  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.435  -0.349  21.744 1.00 35.63  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.253  -1.137  20.821 1.00 36.57  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.653  -0.892  23.425 1.00 39.18  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.660  -1.641  24.306 1.00 46.70  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 2.021  -0.892  25.563 1.00 54.83  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 1.365  0.090   25.949 1.00 57.24  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 3.075  -1.348  26.241 1.00 56.11  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.626  0.088   22.092 1.00 34.16  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 4.838  -0.418  21.485 1.00 35.27  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.342  -1.582  22.320 1.00 36.82  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 5.096  -1.654  23.541 1.00 37.77  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.085  -2.462  21.684 1.00 36.36  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.579  -3.634  22.407 1.00 36.62  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 8.084  -3.833  22.290 1.00 33.78  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.566  -4.908  22.671 1.00 34.37  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 5.798  -4.891  22.033 1.00 40.13  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 5.483  -5.056  20.260 1.00 52.61  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.845  -2.806  21.827 1.00 30.45  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.322 -2.889  21.828 1.00 26.90  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.713 -2.894  23.371 1.00 25.95  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 9.931  -2.378  24.200 1.00 29.44  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 11.008 -1.674  21.042 1.00 25.06  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.237 -1.784  19.512 1.00 28.62  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 11.769 -2.835  19.068 1.00 28.99  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 10.974 -0.734  18.739 1.00 22.70  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 11.813 -3.522  23.747 1.00 23.11  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 12.390 -3.650  25.102 1.00 23.24  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.678 -2.818  25.104 1.00 21.63  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.462 -2.973  24.185 1.00 20.48  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 12.829 -5.146  25.350 1.00 27.14  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 11.661 -5.896  25.626 1.00 31.50  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 13.812 -5.322  26.571 1.00 26.66  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 13.888 -1.951  26.103 1.00 19.74  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 15.133 -1.186  26.177 1.00 17.35  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 16.129 -1.934  27.052 1.00 18.22  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.773 -2.438  28.151 1.00 19.37  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 14.871 0.199   26.792 1.00 16.10  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.727 0.951   26.076 1.00 18.35  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 16.179 1.027   26.806 1.00 16.13  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 14.048 1.251   24.572 1.00 18.43  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.358 -2.080  26.591 1.00 16.32  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.436 -2.726  27.361 1.00 16.52  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.783 -1.837  28.569 1.00 17.73  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.816 -0.618  28.483 1.00 17.25  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.690 -2.894  26.466 1.00 15.47  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 19.059 -2.493  29.720 1.00 18.65  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.497 -1.745  30.920 1.00 19.35  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.775 -2.507  31.321 1.00 21.63  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.719 -3.486  32.069 1.00 23.03  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.431 -1.778  32.052 1.00 21.00  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.078 -1.221  31.624 1.00 20.56  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.110 0.261   31.248 1.00 20.71  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.770 0.697   30.865 1.00 19.64  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.503 1.861   30.279 1.00 21.67  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.486 2.703   29.980 1.00 18.61  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 14.256 2.178   29.964 1.00 22.12  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 21.909 -2.075  30.771 1.00 20.86  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 23.154 -2.847  30.867 1.00 21.53  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.338 -1.929  30.495 1.00 22.25  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 24.159 -0.789  30.071 1.00 22.94  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 23.068 -4.030  29.897 1.00 21.03  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 23.056 -3.525  28.138 1.00 18.13  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.563 -2.507  30.533 1.00 24.30  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.756 -1.775  30.112 1.00 24.11  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.427 -2.530  28.956 1.00 24.21  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.646 -2.427  28.792 1.00 24.57  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 27.757 -1.605  31.287 1.00 28.71  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 28.278 -2.901  31.882 1.00 37.12  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 27.768 -3.980  31.510 1.00 37.23  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 29.197 -2.837  32.734 1.00 44.21  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.638 -3.238  28.095 1.00 21.84  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 27.260 -3.933  26.941 1.00 19.43  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 27.996 -2.912  26.067 1.00 18.95  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.523 -1.761  25.889 1.00 18.59  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 26.208 -4.647  26.097 1.00 18.94  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.486 -6.145  26.810 1.00 19.28  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 29.103 -3.336  25.478 1.00 18.39  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 29.868 -2.574  24.501 1.00 17.65  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 30.015 -3.346  23.187 1.00 15.94  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 30.870 -3.036  22.359 1.00 15.36  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 31.258 -2.153  25.024 1.00 21.32  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 31.290 -0.967  25.985 1.00 25.89  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.738 -0.555  26.271 1.00 30.00  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 33.255 -0.755  27.379 1.00 32.11  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.437 0.002   25.285 1.00 26.88  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 29.195 -4.428  22.988 1.00 14.36  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 29.099 -5.135  21.716 1.00 14.42  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.593 -5.327  21.441 1.00 13.22  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.744 -5.396  22.365 1.00 14.79  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 29.807 -6.511  21.717 1.00 16.54  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 29.143 -7.402  22.618 1.00 18.96  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 31.288 -6.429  22.061 1.00 18.46  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.264 -5.353  20.152 1.00 12.92  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 25.879 -5.541  19.717 1.00 12.76  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 25.820 -5.607  18.198 1.00 11.39  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 26.833 -5.886  17.551 1.00 12.02  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.594 -5.483  17.675 1.00 11.01  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.334 -5.615  16.237 1.00 10.48  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.464 -4.435  15.853 1.00 10.47  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.494 -4.131  16.539 1.00 10.90  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.603 -6.972  15.965 1.00 11.15  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.175 -7.073  14.493 1.00 12.24  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.540 -8.143  16.319 1.00 12.94  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 23.812 -3.763  14.734 1.00 9.98   ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 22.955 -2.678  14.250 1.00 10.32  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.440 -2.949  12.851 1.00 10.78  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 23.049 -3.688  12.070 1.00 10.94  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.671 -1.277  14.313 1.00 10.36  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.658 -1.004  13.188 1.00 10.15  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 25.933 -1.564  13.206 1.00 11.87  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.340 -0.145  12.146 1.00 12.11  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 26.866 -1.277  12.214 1.00 12.23  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.276 0.146   11.146 1.00 12.99  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.529 -0.441  11.183 1.00 13.56  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.469 -0.203  10.190 1.00 15.50  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.294 -2.319  12.538 1.00 9.89   ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.720 -2.413  11.199 1.00 10.94  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.225 -1.220  10.342 1.00 11.23  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.086 -0.063  10.724 1.00 12.03  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.179 -2.446  11.237 1.00 12.24  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.626 -2.550  9.830  1.00 13.45  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 18.826 -3.688  9.081  1.00 14.40  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.941 -1.488  9.248  1.00 15.21  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.355 -3.785  7.778  1.00 15.69  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.490 -1.555  7.941  1.00 16.46  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.675 -2.715  7.218  1.00 17.69  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.217 -2.836  5.914  1.00 20.84  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.783 -1.536  9.160  1.00 11.94  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.323 -0.544  8.226  1.00 11.66  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.415 -0.536  6.967  1.00 13.25  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.551 -1.420  6.096  1.00 13.55  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.752 -0.936  7.878  1.00 12.80  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.504 0.110   6.592  1.00 15.06  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.545 0.474   6.848  1.00 13.90  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.619 0.532   5.727  1.00 14.64  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.288 0.671   4.362  1.00 14.49  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.842 0.060   3.387  1.00 16.72  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.577 1.634   5.929  1.00 18.38  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.192 2.909   5.952  1.00 25.76  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.461 1.335   4.319  1.00 14.52  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.190 1.505   3.054  1.00 15.10  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 22.874 0.241   2.552  1.00 14.87  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.399 0.249   1.434  1.00 16.45  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.207 2.626   3.139  1.00 16.56  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.252 2.349   4.056  1.00 16.06  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.819 -0.853  3.337  1.00 14.44  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.299 -2.161  2.900  1.00 14.52  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.190 -3.229  3.024  1.00 15.10  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.440 -4.417  2.750  1.00 16.67  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.519 -2.562  3.741  1.00 15.18  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.746 -1.682  3.504  1.00 15.00  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.385 -2.000  2.151  1.00 16.80  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.579 -1.175  1.903  1.00 19.81  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.560 0.015   1.320  1.00 19.45  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.414 0.532   0.881  1.00 19.18  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.696 0.692   1.128  1.00 20.00  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 20.996 -2.845  3.546  1.00 16.79  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 19.927 -3.811  3.855  1.00 18.39  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.492 -5.001  4.682  1.00 18.66  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.211 -6.181  4.388  1.00 20.45  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.209 -4.302  2.586  1.00 22.54  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 17.942 -3.547  2.306  1.00 28.40  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.282 -4.134  1.079  1.00 31.89  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.699 -3.093  0.246  1.00 33.63  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 16.969 -2.931  -1.053 1.00 35.32  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.820 -3.754  -1.673 1.00 36.40  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.416 -1.932  -1.732 1.00 33.69  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.333 -4.696  5.696  1.00 16.45  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 22.002 -5.764  6.439  1.00 17.04  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.217 -5.367  7.873  1.00 14.95  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.370 -4.187  8.162  1.00 14.24  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.413 -5.996  5.826  1.00 20.45  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.478 -6.992  4.665  1.00 29.88  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 24.915 -7.127  4.203  1.00 37.18  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 25.770 -7.853  5.230  1.00 44.53  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 27.051 -8.347  4.646  1.00 49.00  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.365 -6.362  8.745  1.00 13.56  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 22.764 -6.126  10.124 1.00 12.32  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.247 -6.439  10.269 1.00 13.70  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 24.786 -7.362  9.645  1.00 15.38  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 22.003 -7.064  11.070 1.00 12.63  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.528 -6.828  11.064 1.00 14.29  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 19.882 -6.101  12.064 1.00 17.25  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.599 -7.329  10.229 1.00 14.26  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.584 -6.191  11.778 1.00 16.32  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.373 -6.859  10.673 1.00 19.09  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 24.955 -5.633  11.073 1.00 11.69  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.394 -5.823  11.292 1.00 11.65  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.700 -5.903  12.788 1.00 11.84  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.195 -5.106  13.571 1.00 12.33  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.217 -4.631  10.716 1.00 12.68  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.224 -4.527  9.214  1.00 14.15  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 27.973 -5.408  8.431  1.00 15.93  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.501 -3.547  8.571  1.00 15.36  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 28.002 -5.294  7.038  1.00 16.62  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.529 -3.417  7.183  1.00 16.22  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.214 -4.344  6.417  1.00 17.89  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.232 -4.207  5.035  1.00 21.03  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.599 -6.790  13.199 1.00 11.33  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 28.046 -6.788  14.602 1.00 12.05  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 29.104 -5.696  14.830 1.00 14.63  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 29.931 -5.438  13.922 1.00 18.58  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.719 -8.169  14.750 1.00 13.32  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.220 -8.479  13.326 1.00 14.74  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.270 -7.836  12.380 1.00 12.20  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 29.089 -5.067  16.001 1.00 13.15  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 30.000 -3.955  16.324 1.00 13.77  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.471 -3.997  17.737 1.00 13.75  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 29.770 -4.448  18.643 1.00 14.23  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.299 -2.578  16.096 1.00 17.00  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.289 -2.228  14.604 1.00 18.53  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 27.886 -2.547  16.690 1.00 17.60  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.706 -3.478  17.942 1.00 13.97  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 32.210 -3.111  19.268 1.00 15.01  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 32.087 -1.570  19.340 1.00 15.13  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.457 -0.911  18.379 1.00 16.09  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.686 -3.461  19.397 1.00 17.03  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 33.826 -4.868  19.402 1.00 25.08  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.501 -1.006  20.394 1.00 13.08  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.296 0.449   20.450 1.00 14.04  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.805 1.017   21.749 1.00 14.58  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.872 0.341   22.793 1.00 15.26  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.811 0.812   20.184 1.00 13.77  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.775 0.047   21.003 1.00 11.98  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.309 -1.194  20.575 1.00 12.66  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.296 0.548   22.201 1.00 12.68  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.334 -1.882  21.297 1.00 12.83  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.337 -0.156  22.941 1.00 12.89  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.901 -1.387  22.494 1.00 13.52  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.159 2.326   21.711 1.00 14.92  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.647 2.998   22.893 1.00 16.34  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.514 3.347   23.864 1.00 17.17  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.347 3.319   23.495 1.00 16.82  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.424 4.260   22.508 1.00 18.05  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.568 5.159   21.807 1.00 19.81  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 31.842 3.562   25.142 1.00 17.69  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 30.839 3.978   26.140 1.00 18.58  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.281 5.356   25.776 1.00 19.45  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 30.976 6.174   25.176 1.00 19.62  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.453 3.995   27.559 1.00 21.78  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 31.802 2.589   28.032 1.00 24.56  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.239 2.662   29.525 1.00 30.89  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.609 1.275   29.988 1.00 37.25  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 33.148 1.291   31.367 1.00 42.26  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 29.024 5.648   26.174 1.00 18.27  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.438 6.964   25.831 1.00 18.92  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.292 8.109   26.328 1.00 19.76  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.679 8.152   27.509 1.00 20.61  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 27.059 6.959   26.514 1.00 20.61  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 26.788 5.527   26.908 1.00 22.61  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 28.101 4.775   26.930 1.00 19.52  ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.588 9.035   25.420 1.00 17.58  ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 30.480 10.139  25.789 1.00 19.69  ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 30.190 11.388  24.956 1.00 19.09  ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 29.285 11.388  24.109 1.00 18.27  ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 31.934 9.668   25.700 1.00 23.82  ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 32.363 9.644   24.361 1.00 28.90  ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 30.896 12.520  25.299 1.00 19.37  ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 30.740 13.792  24.586 1.00 21.13  ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 31.723 13.746  23.436 1.00 21.91  ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 32.956 13.718  23.692 1.00 23.17  ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 31.156 14.957  25.515 1.00 22.91  ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 30.083 15.597  26.297 1.00 27.32  ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 30.681 16.532  27.367 1.00 29.97  ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 29.148 16.427  25.396 1.00 28.10  ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 31.220 13.832  22.199 1.00 21.65  ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 32.006 13.697  20.975 1.00 22.88  ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 31.756 14.861  20.060 1.00 24.04  ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 30.601 15.204  19.818 1.00 23.02  ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 31.668 12.330  20.298 1.00 23.97  ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 32.144 11.180  21.203 1.00 26.62  ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 32.241 12.250  18.882 1.00 24.79  ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 31.852 9.853   20.752 1.00 27.93  ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 32.832 15.476  19.512 1.00 23.52  ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 32.655 16.574  18.573 1.00 25.54  ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 32.007 16.086  17.274 1.00 25.84  ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 32.422 15.072  16.723 1.00 27.87  ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 34.023 17.208  18.244 1.00 27.64  ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 33.928 18.334  17.244 1.00 30.73  ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 34.120 18.099  15.892 1.00 33.39  ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 33.574 19.602  17.642 1.00 32.72  ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 34.032 19.133  14.974 1.00 35.28  ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 33.501 20.644  16.718 1.00 34.66  ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 33.744 20.397  15.391 1.00 34.28  ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 30.962 16.799  16.804 1.00 23.91  ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 30.268 16.500  15.553 1.00 23.33  ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 30.311 17.760  14.686 1.00 24.27  ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 29.859 18.861  15.105 1.00 24.47  ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 28.793 16.036  15.801 1.00 22.67  ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 28.095 15.739  14.473 1.00 23.22  ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 28.736 14.810  16.718 1.00 22.15  ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 30.844 17.599  13.472 1.00 24.40  ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 31.011 18.712  12.521 1.00 25.03  ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 29.633 19.282  12.158 1.00 25.94  ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 28.625 18.572  12.283 1.00 25.23  ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 31.734 18.220  11.246 1.00 28.95  ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 32.318 19.337  10.390 1.00 39.32  ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 33.095 18.856  9.179  1.00 50.97  ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 33.925 19.635  8.656  1.00 54.05  ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 32.885 17.693  8.761  1.00 53.83  ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 29.577 20.557  11.728 1.00 27.15  ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 28.331 21.225  11.336 1.00 26.76  ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 27.682 20.450  10.190 1.00 26.73  ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 28.392 19.868  9.358  1.00 27.09  ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 28.644 22.651  10.865 1.00 27.11  ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 26.342 20.446  10.161 1.00 26.35  ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 25.545 19.819  9.112  1.00 25.46  ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 24.403 20.806  8.826  1.00 26.30  ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 24.340 21.892  9.438  1.00 27.59  ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 24.960 18.472  9.594  1.00 25.63  ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 23.971 18.647  10.600 1.00 24.59  ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 23.505 20.441  7.890  1.00 26.88  ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 22.325 21.287  7.658  1.00 28.12  ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 21.408 21.357  8.880  1.00 27.54  ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 20.585 22.277  8.997  1.00 28.48  ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 21.557 20.841  6.381  1.00 35.22  ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 20.184 20.182  6.558  1.00 46.42  ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 18.999 21.138  6.632  1.00 57.42  ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 17.911 20.708  7.086  1.00 59.31  ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 19.166 22.324  6.261  1.00 59.64  ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 21.527 20.365  9.792  1.00 25.89  ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 20.639 20.273  10.930 1.00 24.18  ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 21.161 20.919  12.189 1.00 22.09  ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 20.365 21.349  13.019 1.00 22.95  ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 20.332 18.797  11.212 1.00 23.82  ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 19.825 18.029  10.009 1.00 24.38  ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 20.690 17.280  9.222  1.00 25.99  ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 18.478 18.030  9.674  1.00 24.07  ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 20.222 16.528  8.151  1.00 27.19  ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 18.005 17.306  8.582  1.00 25.54  ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 18.876 16.552  7.830  1.00 27.56  ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 18.416 15.849  6.732  1.00 30.81  ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 22.499 20.964  12.361 1.00 21.30  ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 23.058 21.537  13.600 1.00 21.40  ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 24.362 22.251  13.307 1.00 24.15  ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 25.100 21.827  12.413 1.00 24.62  ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 23.452 20.417  14.612 1.00 20.03  ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 22.340 19.506  15.084 1.00 18.37  ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 21.452 19.912  16.069 1.00 18.87  ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 22.192 18.234  14.560 1.00 18.16  ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 20.484 19.050  16.573 1.00 18.10  ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 21.224 17.353  15.057 1.00 16.62  ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 20.365 17.775  16.052 1.00 16.53  ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 19.371 16.943  16.545 1.00 16.04  ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 24.704 23.294  14.085 1.00 26.45  ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 26.066 23.862  13.955 1.00 26.79  ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 27.077 22.865  14.557 1.00 26.38  ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 26.673 21.907  15.240 1.00 25.83  ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 25.978 25.137  14.813 1.00 28.06  ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 25.010 24.765  15.896 1.00 29.11  ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 23.967 23.887  15.228 1.00 27.00  ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 28.395 23.102  14.395 1.00 26.50  ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 29.435 22.244  14.991 1.00 27.14  ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 29.252 22.287  16.515 1.00 26.38  ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 28.959 23.344  17.064 1.00 26.79  ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 30.829 22.768  14.608 1.00 28.04  ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 29.258 21.102  17.164 1.00 24.66  ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 28.981 21.062  18.607 1.00 23.94  ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 29.470 19.731  19.201 1.00 23.36  ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 29.870 18.857  18.459 1.00 24.46  ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 27.451 21.205  18.812 1.00 23.16  ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 26.710 19.896  18.390 1.00 23.15  ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 25.308 20.123  17.919 1.00 21.51  ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 24.394 19.024  18.278 1.00 21.59  ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 24.361 17.847  17.662 1.00 19.65  ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 23.461 16.928  18.016 1.00 19.58  ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 25.240 17.567  16.708 1.00 20.02  ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 29.409 19.588  20.515 1.00 22.95  ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 29.662 18.306  21.142 1.00 23.25  ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 28.299 17.642  21.293 1.00 21.37  ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 27.375 18.248  21.844 1.00 22.54  ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 30.269 18.482  22.518 1.00 25.16  ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 31.714 18.908  22.418 1.00 27.61  ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 32.728 17.967  22.316 1.00 28.52  ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 32.058 20.249  22.334 1.00 30.13  ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 34.066 18.353  22.196 1.00 31.17  ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 33.384 20.647  22.199 1.00 32.09  ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 34.384 19.695  22.114 1.00 32.87  ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? 35.706 20.119  21.996 1.00 37.34  ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 28.171 16.425  20.800 1.00 18.35  ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 26.961 15.624  20.973 1.00 16.66  ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 27.238 14.700  22.162 1.00 16.01  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 28.298 14.041  22.234 1.00 17.89  ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 26.583 14.866  19.715 1.00 16.06  ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 25.340 13.967  19.948 1.00 15.62  ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 24.716 13.497  18.660 1.00 15.53  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 24.590 14.222  17.657 1.00 17.33  ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 24.237 12.234  18.641 1.00 14.25  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 26.373 14.727  23.136 1.00 15.34  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 26.494 13.917  24.331 1.00 15.59  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 25.828 12.546  24.163 1.00 16.88  ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 25.010 12.364  23.236 1.00 16.13  ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 25.922 14.671  25.522 1.00 18.78  ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 24.530 14.913  25.369 1.00 19.31  ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 26.228 11.591  25.039 1.00 15.99  ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 25.656 10.243  25.105 1.00 16.05  ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 25.831 9.515   23.777 1.00 15.36  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 24.982 8.708   23.401 1.00 14.16  ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 24.176 10.341  25.518 1.00 16.92  ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 23.990 10.954  26.883 1.00 19.21  ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 23.910 10.156  28.024 1.00 22.42  ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 23.956 12.253  27.261 1.00 20.66  ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 23.784 11.013  29.051 1.00 22.29  ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 23.808 12.268  28.636 1.00 22.77  ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 26.938 9.806   23.059 1.00 14.77  ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 27.185 9.202   21.744 1.00 15.36  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 28.226 8.085   21.863 1.00 14.66  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 29.194 8.198   22.623 1.00 14.92  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 27.703 10.292  20.774 1.00 16.47  ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 27.916 9.902   19.298 1.00 17.44  ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 26.600 9.469   18.599 1.00 16.49  ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 28.499 11.127  18.511 1.00 20.32  ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 27.974 6.998   21.125 1.00 13.88  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 28.875 5.827   21.137 1.00 13.33  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 29.371 5.582   19.726 1.00 14.45  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 28.551 5.520   18.790 1.00 15.09  ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 28.081 4.597   21.589 1.00 14.14  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 27.570 4.733   23.024 1.00 15.45  ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 26.426 3.470   23.549 1.00 18.50  ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 25.075 3.706   22.352 1.00 20.64  ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 30.689 5.434   19.538 1.00 14.41  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 31.207 5.215   18.188 1.00 14.32  ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 31.636 3.766   17.971 1.00 14.09  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 32.132 3.098   18.887 1.00 15.02  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 32.460 6.102   17.853 1.00 16.35  ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 32.246 7.580   17.894 1.00 21.18  ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 33.500 8.326   17.332 1.00 22.36  ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 31.073 8.010   17.065 1.00 21.14  ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 31.542 3.356   16.742 1.00 13.45  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 32.023 2.021   16.332 1.00 13.14  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 32.517 2.072   14.898 1.00 13.48  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 32.220 3.018   14.169 1.00 14.75  ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 30.858 1.006   16.374 1.00 14.55  ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 33.363 1.101   14.528 1.00 12.89  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 33.788 0.983   13.146 1.00 13.75  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 32.715 0.214   12.357 1.00 15.20  ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 32.353 -0.908  12.724 1.00 16.82  ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? 35.146 0.261   13.098 1.00 14.84  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? 35.571 0.024   11.642 1.00 15.85  ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? 36.179 1.098   13.857 1.00 16.31  ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 32.213 0.869   11.305 1.00 15.25  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 31.136 0.269   10.526 1.00 17.13  ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 30.647 1.252   9.490  1.00 17.27  ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 30.965 2.454   9.523  1.00 18.27  ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 29.943 0.727   8.496  1.00 16.71  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 29.389 1.545   7.448  1.00 15.35  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 28.159 2.340   7.869  1.00 15.40  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 27.233 1.782   8.477  1.00 14.98  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 29.066 0.711   6.203  1.00 16.54  ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 28.556 1.540   5.068  1.00 17.07  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 29.368 2.462   4.424  1.00 19.14  ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 27.283 1.680   4.601  1.00 16.94  ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 28.582 3.079   3.541  1.00 19.49  ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 27.326 2.607   3.599  1.00 18.37  ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 28.110 3.581   7.477  1.00 16.70  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 26.941 4.397   7.656  1.00 17.20  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 26.975 5.550   6.642  1.00 19.87  ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 28.078 5.948   6.203  1.00 22.16  ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 26.838 4.910   9.085  1.00 18.71  ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 27.846 5.864   9.347  1.00 24.65  ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 25.777 5.928   6.194  1.00 17.76  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 25.420 7.033   5.292  1.00 18.71  ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 24.291 7.827   6.003  1.00 20.48  ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 23.643 7.357   6.944  1.00 21.10  ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 24.908 6.483   3.945  1.00 20.98  ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 26.049 5.832   3.209  1.00 22.36  ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 25.703 5.186   1.872  1.00 22.52  ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 24.923 5.783   1.092  1.00 25.01  ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 26.212 4.070   1.613  1.00 21.18  ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 24.091 9.115   5.646  1.00 22.64  ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 23.096 9.950   6.387  1.00 22.05  ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 21.695 9.334   6.581  1.00 21.58  ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 21.127 9.347   7.702  1.00 22.85  ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 23.043 11.246  5.564  1.00 23.46  ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 24.399 11.295  4.863  1.00 24.64  ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 24.825 9.862   4.614  1.00 23.45  ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 21.195 8.703   5.533  1.00 19.04  ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 19.898 8.021   5.557  1.00 17.68  ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 19.848 6.806   6.491  1.00 17.11  ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 18.787 6.222   6.725  1.00 17.08  ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 21.020 6.371   7.021  1.00 16.09  ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 21.055 5.266   7.968  1.00 14.49  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 20.623 5.659   9.377  1.00 14.21  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 20.390 4.789   10.202 1.00 14.06  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 22.455 4.612   8.040  1.00 14.25  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 22.736 3.797   6.807  1.00 14.80  ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 21.782 3.180   6.287  1.00 16.16  ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 23.919 3.803   6.337  1.00 14.86  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 20.450 6.971   9.634  1.00 13.94  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 20.057 7.431   10.972 1.00 13.42  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 18.712 6.794   11.345 1.00 13.49  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.814 6.728   10.521 1.00 15.75  ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 19.997 8.965   11.039 1.00 13.58  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 21.626 9.740   11.130 1.00 17.32  ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 18.597 6.322   12.576 1.00 12.13  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.360 5.689   13.033 1.00 12.65  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.441 4.174   13.096 1.00 12.69  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 16.596 3.523   13.734 1.00 13.33  ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 18.459 3.596   12.453 1.00 11.79  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 18.665 2.138   12.562 1.00 12.47  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 18.946 1.740   14.008 1.00 11.31  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 19.715 2.415   14.691 1.00 11.62  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 18.339 0.650   14.468 1.00 10.96  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 18.543 0.244   15.845 1.00 10.61  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 19.834 -0.544  16.077 1.00 10.76  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 20.181 -1.435  15.287 1.00 11.51  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.305 -0.575  16.277 1.00 13.14  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 16.128 0.386   16.525 1.00 14.93  ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.537 -1.458  17.519 1.00 15.98  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 14.729 -0.393  16.831 1.00 18.27  ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 20.474 -0.269  17.198 1.00 9.69   ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 21.587 -1.049  17.765 1.00 9.86   ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 20.966 -1.842  18.935 1.00 10.87  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 20.333 -1.227  19.831 1.00 11.94  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 22.653 -0.077  18.321 1.00 11.08  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 23.805 -0.742  19.114 1.00 11.94  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 24.634 -1.701  18.230 1.00 12.83  ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 24.765 0.345   19.718 1.00 13.58  ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 21.197 -3.177  18.941 1.00 11.23  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 20.677 -4.047  19.993 1.00 12.00  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 21.794 -4.917  20.518 1.00 12.76  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 22.649 -5.411  19.779 1.00 13.43  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 19.655 -5.040  19.356 1.00 16.16  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 18.432 -4.451  18.741 1.00 23.81  ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.592 -5.609  18.162 1.00 25.66  ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 16.911 -6.226  19.289 1.00 28.09  ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 15.733 -5.827  19.742 1.00 28.48  ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 15.017 -4.952  19.057 1.00 25.58  ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 15.254 -6.318  20.871 1.00 25.06  ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 21.662 -5.250  21.801 1.00 13.03  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 22.507 -6.311  22.425 1.00 14.20  ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 21.551 -7.423  22.893 1.00 15.90  ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 20.359 -7.378  22.614 1.00 17.42  ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 23.269 -5.710  23.598 1.00 14.99  ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 22.166 -5.184  24.972 1.00 15.98  ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 22.060 -8.461  23.583 1.00 17.70  ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 21.210 -9.557  24.073 1.00 19.23  ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 20.136 -9.100  25.068 1.00 20.46  ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 19.166 -9.851  25.296 1.00 21.73  ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 22.078 -10.669 24.720 1.00 21.36  ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 22.743 -10.194 26.016 1.00 28.58  ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 23.743 -11.198 26.562 1.00 39.03  ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 24.975 -11.000 26.499 1.00 42.42  ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 23.230 -12.278 27.125 1.00 38.28  ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 20.229 -7.872  25.616 1.00 18.64  ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 19.260 -7.380  26.609 1.00 19.09  ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 18.132 -6.555  26.031 1.00 18.24  ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.139 -6.275  26.727 1.00 19.93  ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 19.959 -6.561  27.702 1.00 18.97  ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 21.087 -7.329  28.344 1.00 21.14  ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 22.424 -7.004  28.107 1.00 22.26  ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 21.047 -8.381  29.212 1.00 24.84  ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 23.147 -7.899  28.775 1.00 25.09  ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 22.371 -8.773  29.422 1.00 26.31  ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 18.312 -6.075  24.794 1.00 16.00  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.318 -5.226  24.175 1.00 15.76  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 17.930 -4.094  23.374 1.00 14.00  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 19.112 -4.141  23.008 1.00 14.50  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.110 -3.069  23.131 1.00 12.89  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.565 -1.919  22.343 1.00 12.74  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 18.545 -1.064  23.119 1.00 12.25  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 18.249 -0.641  24.263 1.00 13.78  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 16.345 -1.091  21.898 1.00 13.51  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 16.809 0.213   21.225 1.00 14.11  ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 15.474 -1.918  20.954 1.00 15.24  ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 19.660 -0.733  22.501 1.00 13.10  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 20.713 0.076   23.104 1.00 13.20  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 20.609 1.567   22.670 1.00 13.40  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 20.858 2.500   23.446 1.00 13.02  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 22.090 -0.513  22.731 1.00 13.88  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 23.256 0.406   23.180 1.00 14.61  ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 22.266 -1.904  23.335 1.00 14.12  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 20.337 1.775   21.381 1.00 11.70  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 20.302 3.123   20.828 1.00 13.11  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 20.010 3.125   19.349 1.00 11.17  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 19.618 2.096   18.777 1.00 11.40  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 20.146 4.304   18.727 1.00 11.01  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 19.844 4.437   17.300 1.00 10.33  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 20.981 5.111   16.563 1.00 10.43  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 21.642 6.004   17.137 1.00 10.50  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 18.515 5.202   17.022 1.00 11.73  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 18.483 6.534   17.797 1.00 13.64  ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.293 4.306   17.313 1.00 13.72  ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.235 7.410   17.294 1.00 14.35  ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 21.204 4.779   15.271 1.00 10.29  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 22.242 5.486   14.502 1.00 10.66  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 21.953 6.994   14.478 1.00 11.18  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 20.814 7.372   14.227 1.00 11.44  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 22.277 4.955   13.060 1.00 11.32  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 23.299 5.747   12.222 1.00 12.12  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 22.670 3.461   13.023 1.00 12.67  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 22.981 7.821   14.708 1.00 11.58  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 22.848 9.263   14.723 1.00 11.94  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 23.975 9.960   13.946 1.00 13.66  ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 23.754 11.068  13.487 1.00 14.84  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 22.855 9.717   16.180 1.00 12.19  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 22.754 11.138  16.326 1.00 14.00  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 25.160 9.339   13.819 1.00 13.88  ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 26.282 10.003  13.108 1.00 15.08  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 27.043 8.953   12.266 1.00 16.19  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 26.793 7.761   12.405 1.00 15.15  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 27.267 10.719  14.085 1.00 17.53  ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 28.085 9.750   14.736 1.00 19.48  ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 26.609 11.677  15.065 1.00 18.25  ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 27.941 9.412   11.400 1.00 18.23  ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 28.742 8.486   10.634 1.00 19.77  ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 29.740 9.209   9.762  1.00 22.25  ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 29.935 10.413  9.906  1.00 23.46  ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 30.286 8.453   8.828  1.00 24.88  ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 31.249 8.896   7.829  1.00 26.12  ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 32.586 8.243   8.085  1.00 26.67  ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 32.862 7.832   9.203  1.00 26.84  ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 33.463 8.236   7.095  1.00 27.51  ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 34.825 7.717   7.247  1.00 29.05  ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 34.980 6.293   7.809  1.00 25.81  ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? 36.020 6.011   8.408  1.00 26.59  ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? 35.608 8.713   8.151  1.00 33.86  ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? 35.615 10.167  7.675  1.00 41.65  ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? 35.771 10.447  6.479  1.00 44.35  ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? 35.511 11.127  8.611  1.00 42.71  ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 34.023 5.361   7.581  1.00 22.52  ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 34.103 4.008   8.125  1.00 20.84  ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 33.730 3.949   9.603  1.00 18.25  ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 33.958 2.924   10.252 1.00 19.96  ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 33.128 5.023   10.123 1.00 16.62  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 32.636 5.067   11.508 1.00 16.07  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 31.092 5.155   11.511 1.00 16.41  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 30.502 5.663   10.568 1.00 17.72  ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 33.217 6.269   12.264 1.00 16.98  ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 34.726 6.173   12.483 1.00 20.32  ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? 35.324 7.543   12.755 1.00 22.70  ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? 35.043 5.159   13.651 1.00 20.13  ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 30.480 4.696   12.603 1.00 13.99  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 29.051 4.852   12.792 1.00 12.75  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 28.854 5.245   14.283 1.00 12.50  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 29.545 4.698   15.136 1.00 14.20  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 28.250 3.586   12.402 1.00 12.94  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 28.753 2.305   13.083 1.00 15.37  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 26.768 3.819   12.678 1.00 13.67  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 28.038 6.259   14.527 1.00 11.40  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 27.777 6.725   15.888 1.00 12.69  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 26.338 6.484   16.287 1.00 12.43  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 25.437 6.697   15.476 1.00 12.66  ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 26.130 6.056   17.528 1.00 11.64  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 24.783 5.699   18.015 1.00 11.35  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 24.437 6.588   19.222 1.00 11.79  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 25.241 6.717   20.158 1.00 11.98  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 24.767 4.241   18.498 1.00 11.06  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 25.261 3.249   17.472 1.00 11.69  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 24.411 2.777   16.479 1.00 11.57  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 26.586 2.804   17.490 1.00 13.63  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 24.853 1.840   15.549 1.00 11.87  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 27.030 1.842   16.572 1.00 13.42  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 26.169 1.381   15.587 1.00 12.62  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 23.221 7.141   19.211 1.00 11.17  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 22.708 7.877   20.365 1.00 11.15  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 22.216 6.826   21.368 1.00 11.26  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 21.279 6.060   21.067 1.00 11.97  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 21.561 8.758   19.920 1.00 11.74  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 22.804 6.784   22.571 1.00 11.25  ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 22.408 5.840   23.611 1.00 12.61  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 21.029 6.215   24.179 1.00 12.72  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 20.695 7.411   24.317 1.00 13.20  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 23.427 5.878   24.764 1.00 15.75  ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 23.177 4.858   25.853 1.00 21.63  ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 22.974 3.694   25.529 1.00 19.88  ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 23.101 5.265   27.057 1.00 25.84  ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 20.202 5.182   24.500 1.00 11.78  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 18.934 5.411   25.174 1.00 12.96  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 18.844 4.648   26.509 1.00 14.37  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.817 4.729   27.178 1.00 16.07  ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.700 5.096   24.310 1.00 13.89  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.688 5.954   23.025 1.00 14.62  ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.647 3.596   23.964 1.00 13.74  ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 19.892 3.892   26.888 1.00 13.78  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 19.802 3.018   28.072 1.00 14.39  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 19.663 3.720   29.382 1.00 17.36  ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 19.166 3.121   30.352 1.00 19.03  ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 21.013 2.058   28.124 1.00 15.45  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 21.071 1.064   26.968 1.00 16.02  ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 22.354 0.264   27.062 1.00 16.31  ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 23.485 1.125   26.743 1.00 15.41  ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 24.732 0.683   26.591 1.00 17.94  ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 25.042 -0.587  26.900 1.00 17.61  ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 25.695 1.519   26.205 1.00 17.98  ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 20.061 5.004   29.434 1.00 16.46  ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 19.933 5.768   30.678 1.00 17.52  ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 18.541 6.373   30.855 1.00 18.65  ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 18.270 6.896   31.943 1.00 20.13  ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 20.974 6.898   30.722 1.00 17.94  ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 20.796 7.932   29.620 1.00 21.77  ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 20.617 7.530   28.458 1.00 20.65  ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 20.864 9.160   29.923 1.00 24.32  ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.663 6.318   29.837 1.00 17.63  ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 16.306 6.928   29.909 1.00 16.53  ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 15.340 5.975   30.564 1.00 16.48  ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 14.561 5.248   29.917 1.00 16.42  ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 15.855 7.329   28.513 1.00 15.61  ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 16.824 8.276   27.783 1.00 16.82  ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 16.385 8.479   26.348 1.00 16.26  ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 16.998 9.599   28.507 1.00 17.77  ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 15.448 5.900   31.894 1.00 17.52  ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 14.690 4.888   32.638 1.00 20.38  ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 13.185 5.044   32.548 1.00 21.48  ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 12.442 4.041   32.601 1.00 21.62  ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 15.150 4.820   34.099 1.00 21.60  ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 16.662 4.748   34.329 1.00 23.34  ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 16.955 4.530   35.840 1.00 25.36  ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.334 3.609   33.491 1.00 23.83  ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 12.730 6.304   32.383 1.00 20.68  ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 11.310 6.619   32.304 1.00 21.12  ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 10.641 6.031   31.052 1.00 22.17  ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 9.406  5.957   31.014 1.00 23.86  ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 11.092 8.132   32.414 1.00 20.81  ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 11.907 8.934   31.423 1.00 19.71  ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 13.148 9.480   31.608 1.00 19.45  ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 11.524 9.249   30.083 1.00 19.08  ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 13.533 10.166  30.479 1.00 18.92  ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 12.537 10.067  29.539 1.00 18.99  ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 10.370 8.999   29.327 1.00 20.05  ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 12.474 10.561  28.237 1.00 19.52  ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 10.289 9.525   28.049 1.00 20.09  ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 11.322 10.329  27.537 1.00 19.43  ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 11.428 5.570   30.026 1.00 20.74  ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 10.799 5.004   28.828 1.00 21.64  ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 9.937  3.769   29.169 1.00 26.27  ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 9.060  3.411   28.376 1.00 26.68  ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 11.859 4.600   27.784 1.00 19.93  ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 12.542 5.761   27.073 1.00 19.03  ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 13.646 5.217   26.171 1.00 19.39  ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 11.522 6.555   26.208 1.00 19.14  ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 10.236 3.079   30.295 1.00 31.20  ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 9.442  1.896   30.649 1.00 36.68  ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 8.974  1.871   32.092 1.00 41.86  ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 8.699  0.784   32.608 1.00 43.24  ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 10.147 0.582   30.287 1.00 40.39  ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 11.601 0.515   30.676 1.00 48.13  ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 12.415 0.093   29.834 1.00 50.62  ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 11.931 0.913   31.807 1.00 51.20  ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 8.904  3.044   32.754 1.00 44.14  ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 8.419  3.168   34.135 1.00 47.39  ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 8.074  4.616   34.487 1.00 48.97  ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 8.841  5.315   35.152 1.00 50.00  ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 9.344  2.513   35.195 1.00 51.66  ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 10.843 2.624   34.961 1.00 58.68  ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 11.600 3.402   36.023 1.00 66.13  ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 11.197 4.554   36.315 1.00 67.03  ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 12.605 2.868   36.550 1.00 67.79  ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 19.409 -24.678 24.049 1.00 24.85  ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 20.540 -24.536 23.117 1.00 25.12  ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 20.563 -25.692 22.103 1.00 23.65  ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 19.906 -26.724 22.312 1.00 24.25  ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 21.867 -24.471 23.879 1.00 27.49  ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 22.086 -25.700 24.555 1.00 30.46  ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 21.316 -25.518 21.023 1.00 21.61  ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 21.509 -26.530 19.998 1.00 19.77  ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 21.784 -25.941 18.632 1.00 17.86  ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 21.383 -24.808 18.355 1.00 18.66  ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 22.415 -26.700 17.762 1.00 17.24  ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 22.738 -26.281 16.404 1.00 17.47  ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 22.690 -27.441 15.408 1.00 16.56  ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 22.715 -28.609 15.813 1.00 18.20  ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 24.160 -25.682 16.400 1.00 18.43  ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 22.617 -27.126 14.104 1.00 15.50  ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 22.757 -28.076 13.005 1.00 14.87  ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 24.112 -27.841 12.332 1.00 15.60  ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 24.494 -26.714 12.068 1.00 15.66  ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 21.645 -27.830 11.965 1.00 14.93  ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 20.255 -27.908 12.596 1.00 14.98  ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 21.773 -28.836 10.804 1.00 16.93  ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 19.210 -27.271 11.634 1.00 14.74  ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 24.875 -28.919 12.100 1.00 17.05  ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 26.189 -28.854 11.462 1.00 18.20  ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 26.124 -29.586 10.140 1.00 18.48  ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 25.953 -30.817 10.122 1.00 19.79  ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 27.209 -29.539 12.386 1.00 19.06  ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 27.400 -28.766 13.679 1.00 18.21  ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 28.247 -27.667 13.736 1.00 18.96  ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 26.666 -29.077 14.818 1.00 19.95  ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 28.394 -26.923 14.909 1.00 21.11  ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 26.799 -28.335 15.992 1.00 20.99  ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 27.674 -27.268 16.037 1.00 22.61  ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 27.757 -26.498 17.186 1.00 24.77  ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 26.205 -28.886 9.037  1.00 19.25  ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 26.084 -29.478 7.708  1.00 20.38  ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 27.165 -28.854 6.829  1.00 21.25  ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 27.257 -27.630 6.721  1.00 20.53  ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 24.641 -29.271 7.119  1.00 22.08  ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 24.172 -27.829 7.275  1.00 22.19  ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 24.578 -29.728 5.660  1.00 23.71  ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 28.070 -29.679 6.274  1.00 22.16  ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 29.138 -29.158 5.425  1.00 23.36  ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 30.026 -28.225 6.220  1.00 24.24  ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 30.321 -28.520 7.381  1.00 25.91  ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 30.313 -27.037 5.690  1.00 23.57  ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 31.084 -26.057 6.456  1.00 24.00  ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 30.185 -24.978 7.063  1.00 21.55  ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 30.622 -23.839 7.228  1.00 21.49  ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 32.183 -25.434 5.625  1.00 28.03  ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 33.293 -26.428 5.382  1.00 36.67  ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 33.965 -26.897 6.318  1.00 39.15  ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 33.466 -26.807 4.132  1.00 39.12  ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 28.980 -25.369 7.484  1.00 19.98  ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 28.027 -24.417 8.065  1.00 18.76  ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 27.521 -24.897 9.423  1.00 17.57  ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 27.372 -26.113 9.649  1.00 17.95  ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 26.771 -24.322 7.168  1.00 18.95  ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 27.060 -23.751 5.796  1.00 20.51  ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 27.719 -22.534 5.651  1.00 22.39  ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 26.659 -24.422 4.643  1.00 21.55  ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 27.988 -22.009 4.392  1.00 23.78  ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 26.918 -23.897 3.379  1.00 23.07  ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 27.587 -22.694 3.262  1.00 25.31  ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 27.823 -22.143 2.023  1.00 28.17  ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 27.198 -23.928 10.308 1.00 16.13  ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 26.572 -24.143 11.615 1.00 15.91  ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 25.289 -23.297 11.606 1.00 14.21  ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 25.342 -22.095 11.349 1.00 15.31  ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 27.508 -23.713 12.745 1.00 17.12  ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 26.876 -23.449 14.117 1.00 17.76  ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 27.900 -23.168 15.219 1.00 20.02  ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 27.470 -22.167 16.210 1.00 21.36  ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 27.002 -22.435 17.432 1.00 22.82  ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 26.793 -23.694 17.810 1.00 22.42  ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 26.649 -21.446 18.249 1.00 20.75  ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 24.118 -23.939 11.819 1.00 14.21  ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 22.832 -23.245 11.834 1.00 13.93  ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 22.368 -23.155 13.301 1.00 14.20  ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 22.208 -24.192 13.985 1.00 14.47  ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 21.757 -24.040 11.040 1.00 15.82  ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 20.480 -23.185 10.920 1.00 15.91  ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 22.278 -24.502 9.670  1.00 15.95  ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 22.110 -21.927 13.777 1.00 12.89  ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 21.665 -21.719 15.162 1.00 13.33  ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 20.437 -20.793 15.196 1.00 12.31  ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 20.182 -20.051 14.227 1.00 12.42  ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 22.807 -21.081 16.025 1.00 16.16  ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 23.909 -22.102 16.240 1.00 19.98  ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 23.347 -19.780 15.397 1.00 15.56  ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 19.738 -20.719 16.349 1.00 11.81  ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 18.720 -19.680 16.541 1.00 12.26  ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 19.489 -18.324 16.505 1.00 13.42  ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 20.498 -18.145 17.246 1.00 13.86  ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 18.038 -19.780 17.919 1.00 12.78  ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.210 -21.042 18.059 1.00 15.03  ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 17.713 -22.085 18.530 1.00 14.35  ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 15.961 -20.981 17.608 1.00 13.21  ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 18.966 -17.356 15.723 1.00 12.59  ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 19.647 -16.041 15.623 1.00 12.20  ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 19.770 -15.392 16.989 1.00 14.77  ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 20.827 -14.811 17.299 1.00 15.26  ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 18.891 -15.155 14.639 1.00 12.60  ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 19.673 -13.861 14.267 1.00 11.97  ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 18.725 -12.974 13.507 1.00 14.06  ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 19.344 -11.730 12.983 1.00 13.78  ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 19.391 -10.590 13.654 1.00 17.66  ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 19.060 -10.554 14.935 1.00 17.63  ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 19.909 -9.497  13.085 1.00 16.74  ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 18.748 -15.550 17.859 1.00 14.07  ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 18.825 -14.911 19.186 1.00 15.14  ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 19.864 -15.557 20.141 1.00 16.61  ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 20.221 -14.938 21.162 1.00 18.07  ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.425 -14.813 19.830 1.00 14.48  ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 16.857 -16.103 20.361 1.00 15.45  ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 16.159 -16.992 19.546 1.00 15.92  ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 16.825 -16.564 21.635 1.00 15.77  ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 15.760 -17.998 20.342 1.00 15.74  ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 16.126 -17.779 21.613 1.00 17.09  ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 20.357 -16.742 19.823 1.00 16.02  ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 21.382 -17.408 20.646 1.00 16.37  ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 22.776 -17.370 20.008 1.00 17.58  ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 23.712 -17.995 20.539 1.00 18.30  ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 20.937 -18.872 20.903 1.00 16.63  ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 19.629 -18.967 21.709 1.00 16.91  ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 19.268 -20.453 21.963 1.00 17.53  ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 19.734 -18.184 23.090 1.00 17.77  ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 22.925 -16.689 18.830 1.00 16.55  ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 24.217 -16.695 18.137 1.00 17.56  ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 25.290 -16.049 19.011 1.00 17.04  ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 25.012 -15.097 19.718 1.00 18.54  ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 24.123 -15.951 16.815 1.00 16.45  ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 26.500 -16.596 18.958 1.00 17.62  ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 27.617 -16.104 19.772 1.00 18.48  ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 28.418 -15.007 19.034 1.00 19.00  ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 28.225 -14.815 17.828 1.00 18.26  ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 28.546 -17.296 20.083 1.00 19.49  ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 29.162 -17.728 18.861 1.00 21.73  ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 27.850 -18.434 20.757 1.00 21.21  ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 29.439 -14.383 19.704 1.00 19.85  ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 30.317 -13.450 19.006 1.00 19.17  ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 31.020 -14.159 17.848 1.00 19.36  ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 31.135 -13.584 16.766 1.00 20.66  ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 31.404 -12.954 19.998 1.00 23.26  ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 30.858 -12.095 21.089 1.00 31.18  ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 30.135 -10.945 20.810 1.00 35.13  ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 31.008 -12.202 22.435 1.00 34.92  ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 29.864 -10.389 21.986 1.00 36.17  ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 30.352 -11.115 22.994 1.00 36.45  ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 31.440 -15.434 18.061 1.00 18.65  ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 32.126 -16.157 16.979 1.00 20.06  ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 31.177 -16.380 15.806 1.00 19.10  ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 31.609 -16.310 14.644 1.00 19.21  ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 32.676 -17.487 17.462 1.00 23.12  ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 33.532 -18.176 16.423 1.00 30.31  ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? 34.604 -17.661 16.046 1.00 32.22  ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 33.076 -19.334 15.921 1.00 30.66  ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 29.883 -16.726 16.074 1.00 18.87  ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 28.945 -16.877 14.951 1.00 18.72  ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 28.833 -15.587 14.116 1.00 17.68  ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 28.877 -15.631 12.884 1.00 18.68  ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 27.545 -17.217 15.486 1.00 17.55  ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 27.411 -18.648 15.991 1.00 18.85  ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 28.020 -19.562 15.368 1.00 19.16  ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 26.749 -18.836 17.034 1.00 17.32  ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 28.724 -14.439 14.789 1.00 17.95  ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 28.609 -13.164 14.083 1.00 18.31  ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 29.916 -12.761 13.359 1.00 19.61  ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 29.853 -12.166 12.288 1.00 19.62  ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 28.155 -12.049 15.044 1.00 18.13  ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 26.666 -12.034 15.221 1.00 16.26  ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 25.973 -12.459 16.310 1.00 16.82  ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 25.706 -11.438 14.328 1.00 15.65  ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 24.623 -12.219 16.131 1.00 17.59  ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 24.435 -11.604 14.914 1.00 16.76  ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 25.796 -10.842 13.062 1.00 16.78  ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 23.263 -11.127 14.305 1.00 17.30  ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 24.625 -10.400 12.441 1.00 17.32  ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 23.380 -10.580 13.054 1.00 16.95  ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 31.069 -13.183 13.891 1.00 18.55  ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 32.353 -12.865 13.236 1.00 20.68  ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 32.591 -13.751 11.997 1.00 22.46  ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 33.490 -13.461 11.200 1.00 23.99  ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 33.493 -13.074 14.218 1.00 21.17  ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 31.877 -14.895 11.906 1.00 20.28  ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 31.987 -15.838 10.779 1.00 19.67  ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 30.613 -15.946 10.080 1.00 19.44  ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 30.232 -17.005 9.612  1.00 18.79  ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 32.461 -17.193 11.291 1.00 18.97  ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 33.899 -17.083 11.784 1.00 24.88  ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? 34.836 -17.029 10.978 1.00 25.71  ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 34.079 -17.009 13.105 1.00 24.06  ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 29.889 -14.840 10.027 1.00 18.92  ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 28.545 -14.815 9.459  1.00 18.24  ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 28.474 -15.188 7.976  1.00 19.55  ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 29.225 -14.660 7.160  1.00 22.03  ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 27.986 -13.399 9.667  1.00 18.24  ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 26.562 -13.172 9.117  1.00 18.71  ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 25.533 -14.091 9.843  1.00 19.33  ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 26.170 -11.705 9.263  1.00 19.72  ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 27.522 -16.078 7.616  1.00 17.42  ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 27.241 -16.429 6.229  1.00 18.69  ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 25.899 -15.791 5.813  1.00 19.50  ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 25.781 -15.168 4.745  1.00 21.14  ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 27.199 -17.966 6.043  1.00 20.24  ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 26.646 -18.330 4.653  1.00 21.04  ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 28.591 -18.563 6.270  1.00 22.13  ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 24.876 -15.939 6.675  1.00 16.64  ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 23.535 -15.457 6.383  1.00 16.35  ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 22.756 -15.397 7.699  1.00 15.65  ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 22.944 -16.250 8.586  1.00 15.70  ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 22.849 -16.423 5.359  1.00 17.17  ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 21.368 -16.228 5.159  1.00 17.76  ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 20.747 -15.346 4.322  1.00 19.77  ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 20.321 -16.961 5.818  1.00 17.06  ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 19.369 -15.458 4.456  1.00 20.27  ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 19.087 -16.465 5.343  1.00 18.89  ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 20.309 -17.989 6.775  1.00 16.95  ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 17.851 -17.013 5.748  1.00 17.98  ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 19.088 -18.525 7.164  1.00 17.00  ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 17.884 -18.014 6.685  1.00 16.58  ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 21.890 -14.401 7.826  1.00 15.35  ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 20.990 -14.336 8.973  1.00 15.86  ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 19.673 -13.718 8.543  1.00 15.15  ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 19.632 -12.915 7.591  1.00 15.33  ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 21.583 -13.599 10.183 1.00 16.83  ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 22.154 -12.222 9.856  1.00 16.61  ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 21.162 -11.088 9.702  1.00 19.45  ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 21.442 -10.159 8.903  1.00 21.77  ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 20.118 -11.080 10.391 1.00 18.46  ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 18.601 -14.093 9.239  1.00 14.41  ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.284 -13.538 8.910  1.00 13.79  ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 16.515 -13.427 10.220 1.00 14.11  ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 16.090 -14.429 10.799 1.00 13.60  ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 16.593 -14.435 7.863  1.00 14.03  ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 15.268 -13.914 7.387  1.00 18.69  ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 14.614 -13.216 8.149  1.00 22.58  ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 14.851 -14.280 6.247  1.00 19.64  ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 16.335 -12.190 10.683 1.00 14.09  ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 15.640 -11.928 11.920 0.50 14.64  ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 15.632 -11.954 11.937 0.50 14.80  ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 14.171 -12.412 11.839 1.00 15.55  ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 13.635 -12.897 12.838 1.00 16.53  ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 15.723 -10.431 12.232 0.50 17.16  ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 15.707 -10.480 12.343 0.50 17.83  ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 14.945 -10.091 13.360 0.50 19.16  ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 14.949 -9.690  11.445 0.50 20.57  ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 13.546 -12.287 10.653 1.00 14.29  ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 12.150 -12.716 10.543 1.00 14.89  ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 12.007 -14.213 10.715 1.00 15.15  ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 10.889 -14.660 10.985 1.00 17.44  ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 11.533 -12.283 9.213  1.00 18.71  ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 11.970 -13.079 8.119  1.00 23.23  ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 13.095 -14.981 10.552 1.00 13.20  ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 13.040 -16.458 10.717 1.00 13.12  ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 13.673 -16.938 12.022 1.00 12.51  ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 13.632 -18.145 12.313 1.00 12.18  ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 13.778 -17.175 9.551  1.00 13.78  ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 13.065 -16.912 8.220  1.00 14.64  ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 13.813 -17.556 7.033  1.00 14.94  ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 13.768 -19.022 7.135  1.00 13.54  ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 13.896 -19.834 6.078  1.00 14.10  ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 13.930 -19.334 4.837  1.00 16.40  ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 13.791 -21.155 6.234  1.00 14.80  ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 14.315 -16.059 12.778 1.00 13.40  ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 15.120 -16.429 13.939 1.00 12.62  ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 16.231 -17.402 13.569 1.00 12.11  ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 16.576 -18.268 14.375 1.00 12.20  ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 14.277 -16.969 15.119 1.00 12.59  ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 15.072 -17.247 16.389 1.00 12.88  ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 15.921 -16.399 16.775 1.00 14.24  ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 14.814 -18.301 17.051 1.00 13.84  ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 16.817 -17.249 12.359 1.00 11.55  ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 17.961 -18.116 11.994 1.00 11.59  ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 19.253 -17.335 11.745 1.00 12.59  ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 19.230 -16.247 11.165 1.00 13.28  ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 17.668 -18.932 10.719 1.00 12.78  ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 16.587 -20.025 10.851 1.00 12.59  ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 16.450 -20.721 9.484  1.00 13.58  ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 17.018 -21.082 11.914 1.00 12.76  ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 20.379 -18.002 12.021 1.00 11.56  ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 21.686 -17.430 11.655 1.00 12.54  ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 22.576 -18.628 11.279 1.00 12.17  ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 22.473 -19.691 11.903 1.00 13.73  ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 22.284 -16.637 12.816 1.00 13.76  ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 23.674 -15.985 12.533 1.00 13.92  ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 23.813 -14.638 13.315 1.00 15.16  ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 24.851 -16.951 12.924 1.00 16.27  ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 23.354 -18.484 10.206 1.00 12.14  ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 24.279 -19.524 9.741  1.00 12.98  ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 25.672 -18.915 9.750  1.00 14.37  ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 25.878 -17.805 9.221  1.00 15.13  ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 23.909 -19.996 8.309  1.00 14.20  ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 24.937 -21.020 7.796  1.00 16.19  ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 22.503 -20.630 8.309  1.00 14.06  ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 26.608 -19.643 10.369 1.00 14.78  ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 28.014 -19.218 10.403 1.00 16.26  ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 28.895 -20.308 9.753  1.00 18.39  ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 28.469 -21.456 9.571  1.00 18.10  ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 28.440 -18.947 11.836 1.00 17.03  ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 28.300 -20.095 12.670 1.00 18.66  ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 30.121 -19.924 9.377  1.00 19.67  ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 31.019 -20.884 8.737  1.00 21.70  ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 31.860 -21.616 9.791  1.00 23.49  ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 32.147 -21.058 10.858 1.00 23.75  ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 31.921 -20.167 7.744  1.00 23.68  ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 32.650 -19.165 8.421  1.00 28.21  ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 32.242 -22.865 9.487  1.00 25.20  ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 33.040 -23.714 10.384 1.00 27.88  ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 34.276 -24.224 9.647  1.00 31.88  ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 34.263 -24.336 8.417  1.00 32.39  ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 32.217 -24.980 10.801 1.00 28.75  ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 31.992 -25.783 9.642  1.00 30.07  ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 30.864 -24.632 11.422 1.00 29.06  ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? 35.308 -24.603 10.389 1.00 34.59  ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? 36.497 -25.219 9.784  1.00 37.41  ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? 36.296 -26.742 9.661  1.00 38.67  ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? 36.784 -27.354 8.704  1.00 40.66  ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? 37.750 -24.848 10.582 1.00 40.60  ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? 37.510 -25.134 11.965 1.00 43.54  ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? 38.127 -23.371 10.417 1.00 41.62  ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? 35.574 -27.357 10.613 1.00 37.34  ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? 35.334 -28.798 10.590 1.00 37.34  ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 34.105 -29.139 9.757  1.00 36.94  ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 33.168 -28.350 9.674  1.00 36.36  ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? 35.161 -29.328 12.008 1.00 37.68  ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 34.093 -30.322 9.179  1.00 36.27  ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 33.006 -30.790 8.335  1.00 36.26  ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 31.847 -31.330 9.179  1.00 34.71  ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 32.049 -32.181 10.045 1.00 35.47  ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 33.535 -31.890 7.399  1.00 39.39  ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 32.474 -32.557 6.533  1.00 45.23  ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 32.110 -31.727 5.313  1.00 52.74  ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 32.792 -30.751 4.934  1.00 54.73  ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 31.020 -32.115 4.660  1.00 54.06  ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 30.638 -30.850 8.899  1.00 31.37  ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 29.437 -31.303 9.589  1.00 29.18  ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 28.790 -32.436 8.827  1.00 27.84  ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 28.855 -32.478 7.596  1.00 29.14  ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 28.173 -33.352 9.546  1.00 25.73  ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 27.580 -34.525 8.943  1.00 25.46  ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 26.083 -34.651 9.091  1.00 23.66  ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 25.577 -35.772 8.883  1.00 24.38  ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 28.265 -35.784 9.454  1.00 28.32  ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 30.028 -35.846 9.105  1.00 33.42  ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 25.355 -33.588 9.480  1.00 19.77  ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 23.892 -33.729 9.576  1.00 19.44  ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 23.322 -33.717 8.172  1.00 20.46  ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 23.845 -33.029 7.278  1.00 23.04  ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 23.250 -32.559 10.381 1.00 20.51  ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 23.576 -32.571 11.871 1.00 27.05  ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 23.901 -33.649 12.398 1.00 29.36  ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 23.520 -31.487 12.513 1.00 27.78  ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 22.300 -34.486 7.956  1.00 19.87  ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 21.606 -34.527 6.672  1.00 21.26  ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 20.374 -33.637 6.816  1.00 18.85  ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 19.625 -33.844 7.752  1.00 19.33  ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 21.126 -35.965 6.391  1.00 25.09  ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 22.291 -36.760 6.088  1.00 28.52  ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 20.143 -36.029 5.209  1.00 25.71  ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 20.140 -32.722 5.883  1.00 17.94  ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 18.953 -31.887 5.912  1.00 16.44  ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 17.850 -32.553 5.092  1.00 16.75  ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 18.084 -33.013 3.949  1.00 16.39  ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 19.237 -30.498 5.319  1.00 17.02  ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 20.488 -29.833 5.945  1.00 19.58  ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 17.998 -29.588 5.424  1.00 16.26  ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 20.313 -29.520 7.460  1.00 21.59  ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 16.651 -32.630 5.646  1.00 15.34  ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 15.510 -33.198 4.927  1.00 14.23  ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 15.090 -32.274 3.789  1.00 14.30  ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 15.121 -31.060 3.924  1.00 14.10  ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 14.345 -33.310 5.921  1.00 13.23  ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 14.655 -32.863 2.646  1.00 14.27  ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 14.177 -32.070 1.485  1.00 14.11  ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 12.822 -32.755 1.192  1.00 14.50  ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 12.757 -33.714 0.403  1.00 16.80  ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 15.155 -32.198 0.295  1.00 14.71  ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 16.563 -31.702 0.629  1.00 16.42  ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 16.631 -30.211 1.018  1.00 18.36  ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 18.026 -29.818 1.334  1.00 18.45  ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 18.373 -28.680 1.927  1.00 19.90  ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.450 -27.826 2.319  1.00 16.95  ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 19.652 -28.409 2.166  1.00 21.20  ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 11.737 -32.228 1.797  1.00 14.41  ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 10.449 -32.900 1.796  1.00 14.49  ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 9.334  -31.954 2.281  1.00 15.15  ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 9.617  -30.863 2.729  1.00 15.41  ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 10.543 -34.107 2.723  1.00 15.43  ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 10.710 -33.638 4.486  1.00 14.13  ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 8.073  -32.468 2.320  1.00 15.46  ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 6.955  -31.722 2.908  1.00 17.47  ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 6.338  -32.534 4.057  1.00 17.23  ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 5.132  -32.446 4.312  1.00 17.59  ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 5.886  -31.370 1.850  1.00 20.79  ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 5.226  -32.569 1.212  1.00 23.86  ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 5.602  -33.729 1.548  1.00 25.01  ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 4.295  -32.365 0.383  1.00 29.92  ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 7.156  -33.322 4.787  1.00 15.81  ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 6.649  -34.075 5.962  1.00 14.50  ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 5.988  -33.136 6.949  1.00 13.89  ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 6.427  -31.980 7.140  1.00 13.38  ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 7.786  -34.800 6.684  1.00 14.33  ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 8.383  -36.280 5.832  1.00 15.93  ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 4.975  -33.680 7.609  1.00 13.20  ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 4.294  -33.031 8.726  1.00 13.75  ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 4.290  -33.940 9.944  1.00 12.53  ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 3.481  -33.712 10.872 1.00 13.52  ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 2.874  -32.608 8.356  1.00 14.55  ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 2.890  -31.366 7.425  1.00 16.55  ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 1.471  -30.958 7.127  1.00 18.35  ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 0.948  -31.171 6.009  1.00 21.14  ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 0.780  -30.431 8.141  1.00 17.76  ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 5.156  -35.002 9.970  1.00 12.64  ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 5.323  -35.823 11.172 1.00 13.50  ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 6.833  -36.003 11.380 1.00 13.48  ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 7.609  -36.089 10.427 1.00 14.63  ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 4.609  -37.164 11.118 1.00 18.43  ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 5.234  -37.990 10.122 1.00 21.81  ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 3.108  -37.032 10.828 1.00 20.22  ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 7.234  -35.998 12.661 1.00 11.96  ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 8.657  -36.145 12.992 1.00 12.19  ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 8.838  -36.268 14.499 1.00 10.66  ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 7.875  -36.546 15.213 1.00 11.92  ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 10.099 -36.156 14.937 1.00 10.78  ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 10.438 -36.310 16.361 1.00 10.07  ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 11.335 -35.127 16.736 1.00 11.09  ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 12.274 -34.843 16.000 1.00 11.01  ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 11.190 -37.645 16.568 1.00 10.95  ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 11.703 -37.788 18.019 1.00 12.53  ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 10.299 -38.830 16.203 1.00 12.83  ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 11.066 -34.479 17.885 1.00 10.54  ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 11.966 -33.411 18.339 1.00 10.72  ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 12.551 -33.692 19.714 1.00 11.00  ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 11.968 -34.440 20.519 1.00 11.36  ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 11.288 -31.990 18.327 1.00 11.03  ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 10.358 -31.716 19.501 1.00 10.64  ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 9.074  -32.256 19.540 1.00 12.41  ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 10.744 -30.872 20.540 1.00 11.82  ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 8.190  -31.957 20.576 1.00 14.08  ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 9.875  -30.586 21.600 1.00 13.91  ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 8.601  -31.142 21.613 1.00 14.65  ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 7.712  -30.886 22.638 1.00 16.23  ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 13.725 -33.082 19.977 1.00 11.03  ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 14.376 -33.227 21.266 1.00 11.50  ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 13.951 -32.065 22.162 1.00 12.73  ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 14.111 -30.908 21.804 1.00 13.15  ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 15.909 -33.304 21.129 1.00 12.89  ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 16.547 -33.455 22.493 1.00 14.47  ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 16.375 -34.617 23.229 1.00 15.64  ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.299 -32.429 23.049 1.00 17.35  ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 16.927 -34.759 24.504 1.00 17.05  ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 17.847 -32.558 24.324 1.00 18.30  ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 17.677 -33.732 25.028 1.00 18.86  ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 18.216 -33.903 26.300 1.00 22.25  ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 13.454 -32.413 23.359 1.00 12.76  ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 13.024 -31.439 24.353 1.00 12.48  ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 13.997 -31.494 25.567 1.00 14.69  ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 13.893 -32.409 26.405 1.00 16.06  ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 11.601 -31.758 24.755 1.00 12.85  ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 10.974 -30.701 26.092 1.00 16.85  ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 14.924 -30.504 25.664 1.00 14.71  ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 15.918 -30.546 26.721 1.00 17.67  ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 15.326 -30.429 28.108 1.00 18.58  ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 15.834 -31.098 29.023 1.00 20.54  ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 16.998 -29.493 26.495 1.00 22.25  ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 16.464 -28.189 26.534 1.00 29.42  ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 14.217 -29.703 28.257 1.00 17.35  ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 13.570 -29.544 29.584 1.00 18.50  ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 12.870 -30.779 30.084 1.00 19.91  ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 12.433 -30.794 31.245 1.00 21.20  ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 12.626 -28.359 29.585 1.00 18.76  ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 11.528 -28.553 28.719 1.00 17.84  ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 12.812 -31.837 29.270 1.00 17.72  ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 12.284 -33.126 29.684 1.00 16.75  ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 13.330 -34.240 29.477 1.00 17.50  ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 13.045 -35.411 29.770 1.00 18.58  ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 10.997 -33.467 28.898 1.00 17.62  ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 9.844  -32.533 29.174 1.00 19.16  ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 9.256  -32.828 30.561 1.00 20.43  ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 8.119  -31.968 30.863 1.00 24.56  ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 8.196  -30.790 31.463 1.00 28.20  ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 9.374  -30.316 31.875 1.00 27.73  ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 7.096  -30.088 31.694 1.00 29.66  ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 14.532 -33.902 28.903 1.00 18.33  ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 15.560 -34.897 28.526 1.00 19.09  ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 14.920 -36.034 27.723 1.00 20.00  ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 15.126 -37.211 27.990 1.00 21.56  ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 16.319 -35.401 29.786 1.00 23.20  ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 17.693 -34.705 29.928 1.00 32.42  ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 17.931 -33.567 30.875 1.00 41.77  ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 18.159 -32.348 30.102 1.00 47.27  ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 18.710 -31.237 30.566 1.00 50.55  ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 19.163 -31.184 31.812 1.00 52.57  ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 18.821 -30.171 29.787 1.00 50.02  ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 14.026 -35.656 26.751 1.00 18.14  ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 13.281 -36.680 26.027 1.00 18.00  ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 13.014 -36.247 24.615 1.00 15.69  ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 12.877 -35.050 24.367 1.00 15.14  ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 11.872 -36.868 26.698 1.00 23.27  ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 11.810 -37.887 27.819 1.00 33.87  ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 10.395 -37.946 28.365 1.00 40.02  ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 9.459  -38.606 27.397 1.00 44.53  ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 8.224  -39.066 28.092 1.00 47.65  ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 12.796 -37.217 23.743 1.00 14.45  ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 12.331 -36.946 22.386 1.00 13.02  ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 10.839 -37.209 22.315 1.00 14.72  ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 10.323 -38.152 22.945 1.00 17.32  ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 13.016 -37.871 21.379 1.00 12.81  ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 14.491 -37.653 21.300 1.00 13.90  ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 15.098 -36.906 20.284 1.00 17.07  ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 15.461 -38.180 22.089 1.00 14.42  ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 16.413 -37.028 20.500 1.00 15.40  ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 16.668 -37.713 21.584 1.00 18.50  ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 10.098 -36.380 21.547 1.00 12.01  ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 8.647  -36.555 21.402 1.00 11.85  ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 8.279  -36.630 19.923 1.00 12.17  ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 8.712  -35.810 19.117 1.00 12.74  ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 7.874  -35.357 21.998 1.00 13.44  ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 7.936  -35.235 23.504 1.00 14.34  ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 7.221  -36.109 24.323 1.00 16.26  ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 8.733  -34.267 24.120 1.00 16.44  ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 7.250  -35.973 25.714 1.00 17.03  ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 8.782  -34.151 25.510 1.00 17.16  ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 8.078  -35.041 26.291 1.00 18.49  ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 8.103  -34.884 27.669 1.00 21.97  ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 7.420  -37.597 19.555 1.00 12.01  ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 6.916  -37.644 18.181 1.00 11.96  ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 5.758  -36.637 18.063 1.00 13.72  ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 4.918  -36.568 19.010 1.00 15.69  ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 6.387  -39.084 18.053 1.00 13.09  ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 6.010  -39.470 19.445 1.00 13.98  ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 6.887  -38.700 20.398 1.00 12.93  ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 5.728  -35.878 16.984 1.00 12.91  ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 4.671  -34.863 16.811 1.00 13.93  ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 4.246  -34.771 15.361 1.00 12.56  ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 5.016  -35.042 14.426 1.00 14.22  ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 5.149  -33.463 17.261 1.00 15.71  ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 5.248  -33.361 18.800 1.00 17.12  ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 6.439  -33.049 16.566 1.00 16.44  ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 2.979  -34.286 15.174 1.00 12.47  ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 2.522  -33.779 13.900 1.00 12.91  ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 2.789  -32.226 13.934 1.00 13.23  ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 2.725  -31.588 15.021 1.00 14.23  ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 1.021  -33.979 13.691 1.00 16.16  ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 0.746  -35.366 13.683 1.00 21.80  ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 3.215  -31.643 12.802 1.00 12.31  ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 3.532  -30.216 12.786 1.00 12.80  ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 2.982  -29.579 11.529 1.00 13.42  ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 2.730  -30.247 10.506 1.00 14.03  ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 5.045  -29.947 12.954 1.00 12.50  ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 5.946  -30.687 11.983 1.00 11.10  ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 6.429  -31.948 12.289 1.00 11.09  ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 6.378  -30.078 10.818 1.00 11.72  ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 7.315  -32.608 11.422 1.00 11.63  ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 7.269  -30.714 9.957  1.00 11.63  ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 7.721  -31.994 10.244 1.00 11.42  ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 2.731  -28.253 11.607 1.00 12.20  ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 2.083  -27.566 10.502 1.00 14.26  ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 3.024  -27.240 9.326  1.00 15.36  ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 4.222  -27.540 9.378  1.00 14.77  ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 1.404  -26.294 11.022 1.00 15.70  ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 2.360  -25.340 11.466 1.00 16.53  ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 2.482  -26.649 8.277  1.00 16.01  ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 3.316  -26.198 7.158  1.00 16.36  ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 4.009  -24.876 7.509  1.00 15.94  ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 3.410  -24.053 8.217  1.00 19.70  ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 2.412  -26.000 5.919  1.00 19.83  ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 1.799  -27.336 5.494  1.00 24.61  ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 1.406  -27.334 3.997  1.00 35.27  ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 0.938  -28.712 3.558  1.00 44.68  ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? 1.456  -29.108 2.195  1.00 51.17  ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 5.223  -24.611 7.009  1.00 15.61  ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 5.908  -23.342 7.343  1.00 15.58  ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 5.082  -22.124 6.945  1.00 17.33  ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 4.561  -22.024 5.822  1.00 20.06  ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 7.220  -23.383 6.548  1.00 17.15  ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 7.407  -24.780 6.140  1.00 18.95  ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 6.035  -25.452 6.115  1.00 14.71  ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 4.924  -21.223 7.910  1.00 16.51  ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 4.035  -20.085 7.668  1.00 18.38  ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 4.397  -18.909 8.565  1.00 18.21  ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 5.358  -18.975 9.363  1.00 16.69  ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 2.585  -20.552 7.878  1.00 24.22  ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 2.260  -20.673 9.259  1.00 29.76  ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 3.695  -17.761 8.358  1.00 17.77  ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 3.897  -16.543 9.126  1.00 19.78  ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 2.999  -16.670 10.349 1.00 20.87  ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 1.754  -16.725 10.208 1.00 23.47  ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 3.400  -15.349 8.291  1.00 21.11  ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 4.412  -14.719 7.395  1.00 24.54  ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 3.715  -13.846 6.323  1.00 27.42  ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 5.416  -13.907 8.197  1.00 24.77  ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 3.591  -16.623 11.546 1.00 19.61  ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 2.912  -16.802 12.828 1.00 20.85  ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 3.295  -15.702 13.799 1.00 22.07  ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 4.464  -15.372 13.927 1.00 20.18  ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 3.269  -18.188 13.393 1.00 23.13  ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 2.712  -19.274 12.448 1.00 25.91  ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 2.828  -18.334 14.872 1.00 25.18  ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 2.999  -20.626 12.817 1.00 28.40  ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 2.302  -15.115 14.494 1.00 23.09  ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 2.574  -14.051 15.444 1.00 24.75  ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 3.348  -14.573 16.654 1.00 23.86  ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 2.996  -15.607 17.218 1.00 25.63  ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 1.225  -13.431 15.918 1.00 26.91  ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 1.401  -12.325 16.930 1.00 29.75  ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 1.331  -12.590 18.290 1.00 32.62  ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 1.729  -11.052 16.529 1.00 32.04  ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 1.520  -11.573 19.222 1.00 34.34  ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 1.902  -10.029 17.464 1.00 34.01  ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 1.795  -10.301 18.801 1.00 33.71  ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 4.396  -13.854 17.045 1.00 22.94  ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 5.224  -14.166 18.209 1.00 23.42  ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 5.292  -12.913 19.109 1.00 25.01  ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 5.687  -11.826 18.670 1.00 24.48  ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 6.658  -14.632 17.787 1.00 21.67  ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 7.504  -14.953 19.036 1.00 21.11  ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 6.570  -15.846 16.866 1.00 21.27  ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 5.013  -13.111 20.402 1.00 27.09  ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 5.056  -12.056 21.415 1.00 28.42  ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 6.447  -11.463 21.566 1.00 27.85  ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 7.442  -12.146 21.350 1.00 26.62  ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 4.643  -12.644 22.777 1.00 32.24  ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 3.287  -13.322 22.793 1.00 39.31  ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 2.121  -12.399 23.095 1.00 46.90  ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 0.968  -12.886 23.047 1.00 47.63  ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 2.349  -11.198 23.375 1.00 48.06  ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 6.523  -10.213 22.004 1.00 27.19  ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 7.775  -9.509  22.232 1.00 26.48  ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 8.620  -10.252 23.285 1.00 25.23  ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 8.092  -10.852 24.219 1.00 25.84  ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 7.480  -8.083  22.751 1.00 27.63  ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 9.951  -10.172 23.141 1.00 23.46  ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 10.894 -10.734 24.095 1.00 21.81  ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 12.031 -9.690  24.192 1.00 22.96  ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 11.989 -8.636  23.517 1.00 24.39  ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 11.404 -12.112 23.608 1.00 21.65  ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 12.158 -11.975 22.412 1.00 20.57  ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 13.055 -9.981  24.998 1.00 23.09  ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 14.214 -9.084  25.039 1.00 23.97  ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 14.997 -9.180  23.706 1.00 24.45  ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 15.807 -8.295  23.427 1.00 24.72  ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 15.096 -9.422  26.236 1.00 27.77  ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 15.656 -10.827 26.167 1.00 34.24  ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 14.898 -11.950 26.869 1.00 45.31  ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 15.563 -12.730 27.592 1.00 49.52  ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 13.660 -12.074 26.686 1.00 44.22  ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 14.738 -10.216 22.859 1.00 24.40  ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 15.440 -10.403 21.605 1.00 24.89  ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 14.726 -9.760  20.400 1.00 24.10  ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 15.391 -9.353  19.443 1.00 26.77  ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 15.625 -11.914 21.373 1.00 24.32  ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 16.235 -12.664 22.544 1.00 23.73  ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 17.610 -12.649 22.773 1.00 26.14  ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 15.450 -13.427 23.384 1.00 24.63  ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 18.176 -13.365 23.826 1.00 27.25  ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 16.002 -14.167 24.423 1.00 26.43  ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 17.366 -14.123 24.654 1.00 29.19  ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 17.915 -14.876 25.678 1.00 33.74  ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 13.399 -9.689  20.410 1.00 22.01  ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 12.639 -9.115  19.281 1.00 21.95  ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 11.407 -8.381  19.746 1.00 25.23  ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 10.795 -8.789  20.729 1.00 24.48  ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 12.100 -10.253 18.362 1.00 20.85  ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 13.126 -11.194 17.794 1.00 19.27  ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 13.324 -12.451 18.348 1.00 19.28  ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 13.897 -10.838 16.689 1.00 18.33  ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 14.225 -13.346 17.803 1.00 18.06  ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 14.797 -11.725 16.126 1.00 16.85  ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 14.965 -12.986 16.681 1.00 17.65  ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 15.894 -13.836 16.137 1.00 16.85  ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 10.929 -7.348  19.000 1.00 27.71  ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 9.603  -6.801  19.319 1.00 28.68  ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 8.527  -7.814  18.879 1.00 28.66  ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 8.862  -8.783  18.148 1.00 27.48  ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 9.528  -5.539  18.448 1.00 29.44  ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 10.372 -5.863  17.284 1.00 29.67  ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 11.482 -6.788  17.745 1.00 28.36  ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 7.252  -7.626  19.235 1.00 28.69  ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 6.147  -8.480  18.767 1.00 29.43  ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 6.117  -8.396  17.227 1.00 28.52  ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 6.340  -7.309  16.665 1.00 29.67  ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 4.806  -8.008  19.344 1.00 30.05  ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 6.037  -9.559  16.556 1.00 26.44  ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 6.145  -9.564  15.102 1.00 25.08  ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 5.632  -10.876 14.543 1.00 25.11  ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 5.328  -11.796 15.305 1.00 25.63  ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 7.645  -9.417  14.732 1.00 23.84  ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 8.462  -10.722 15.048 1.00 20.91  ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 9.913  -10.501 15.283 1.00 21.26  ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 10.789 -11.595 14.823 1.00 19.65  ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 10.877 -12.788 15.416 1.00 20.42  ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 11.731 -13.705 14.960 1.00 17.96  ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 10.115 -13.072 16.477 1.00 20.74  ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 5.551  -10.972 13.210 1.00 24.64  ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 5.249  -12.239 12.590 1.00 25.20  ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 6.602  -12.886 12.261 1.00 21.17  ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 7.465  -12.267 11.603 1.00 21.78  ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 4.509  -12.004 11.282 1.00 28.06  ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 3.080  -11.606 11.550 1.00 31.88  ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 2.097  -12.563 11.743 1.00 33.84  ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 2.729  -10.275 11.710 1.00 34.95  ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 0.777  -12.202 12.005 1.00 36.66  ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 1.423  -9.905  12.004 1.00 36.75  ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 0.454  -10.874 12.164 1.00 38.52  ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? -0.853 -10.511 12.403 1.00 42.55  ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 6.785  -14.117 12.736 1.00 17.84  ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 7.969  -14.889 12.378 1.00 16.20  ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 7.586  -15.768 11.189 1.00 16.07  ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 6.524  -16.436 11.199 1.00 18.01  ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 8.461  -15.698 13.579 1.00 15.67  ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 9.659  -16.619 13.195 1.00 15.20  ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 10.383 -17.103 14.418 1.00 14.55  ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 10.598 -16.403 15.403 1.00 15.58  ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 10.845 -18.390 14.341 1.00 13.13  ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 8.399  -15.728 10.139 1.00 15.23  ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 8.161  -16.504 8.945  1.00 14.13  ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 8.814  -17.916 9.005  1.00 14.50  ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 9.701  -18.166 9.839  1.00 14.28  ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 8.656  -15.754 7.701  1.00 16.92  ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 10.065 -15.561 7.763  1.00 19.43  ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 8.340  -18.824 8.112  1.00 14.41  ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 8.868  -20.168 7.935  1.00 14.45  ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 8.757  -20.962 9.258  1.00 14.47  ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 9.621  -21.804 9.545  1.00 13.93  ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 10.320 -20.108 7.416  1.00 14.70  ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 10.428 -19.458 6.070  1.00 16.10  ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 10.416 -20.216 4.906  1.00 19.19  ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 10.450 -18.141 5.742  1.00 18.18  ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 10.503 -19.334 3.898  1.00 19.81  ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 10.515 -18.078 4.354  1.00 20.01  ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 7.737  -20.655 10.080 1.00 14.45  ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 7.557  -21.286 11.406 1.00 13.85  ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 6.476  -22.385 11.337 1.00 14.49  ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 5.459  -22.217 10.653 1.00 14.58  ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 7.148  -20.220 12.459 1.00 15.15  ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 7.048  -20.644 13.909 1.00 16.24  ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 8.426  -21.059 14.460 1.00 15.93  ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 6.579  -19.464 14.800 1.00 20.02  ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 6.734  -23.504 12.021 1.00 13.31  ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 5.793  -24.649 12.041 1.00 12.97  ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 5.402  -24.933 13.485 1.00 14.09  ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 6.298  -24.940 14.364 1.00 14.59  ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 6.498  -25.893 11.467 1.00 13.29  ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 6.880  -25.661 10.031 1.00 15.53  ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 7.937  -26.938 9.399  1.00 16.94  ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 9.465  -26.789 10.525 1.00 16.26  ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 4.092  -25.161 13.766 1.00 13.16  ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 3.703  -25.408 15.161 1.00 12.61  ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 3.318  -26.870 15.367 1.00 12.92  ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 2.818  -27.523 14.447 1.00 13.26  ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 2.465  -24.560 15.592 1.00 14.67  ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 2.660  -23.074 15.519 1.00 15.40  ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 1.370  -22.317 15.965 1.00 16.85  ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 3.902  -22.601 16.314 1.00 16.80  ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 3.514  -27.340 16.590 1.00 13.38  ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 3.047  -28.660 17.009 1.00 13.17  ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 2.486  -28.532 18.418 1.00 13.54  ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 2.846  -27.611 19.147 1.00 14.71  ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 4.228  -29.660 17.046 1.00 14.16  ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 1.647  -29.493 18.848 1.00 13.49  ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 1.200  -29.569 20.235 1.00 14.87  ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 2.310  -30.294 21.002 1.00 16.86  ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 2.579  -31.475 20.742 1.00 18.78  ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? -0.165 -30.311 20.324 1.00 16.71  ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? -0.610 -30.414 21.786 1.00 17.42  ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? -1.204 -29.527 19.516 1.00 17.49  ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 2.926  -29.595 21.928 1.00 17.76  ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 3.994  -30.187 22.714 1.00 19.44  ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 4.610  -29.218 23.675 1.00 20.68  ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 4.373  -27.995 23.621 1.00 20.45  ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 5.416  -29.763 24.584 1.00 20.41  ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 6.064  -28.960 25.583 1.00 21.22  ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 7.321  -28.274 25.058 1.00 21.02  ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 8.143  -28.900 24.373 1.00 19.42  ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 6.424  -29.859 26.776 1.00 21.67  ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 7.090  -29.098 27.865 1.00 22.01  ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 6.392  -28.123 28.593 1.00 23.78  ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 8.397  -29.083 28.252 1.00 23.79  ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 7.276  -27.587 29.411 1.00 24.98  ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 8.491  -28.152 29.269 1.00 25.80  ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 7.526  -27.020 25.456 1.00 21.53  ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 8.685  -26.199 25.156 1.00 24.14  ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 8.851  -25.207 26.340 1.00 24.67  ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 7.887  -24.811 26.994 1.00 27.17  ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 8.445  -25.418 23.855 1.00 28.93  ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 9.540  -24.627 23.401 1.00 38.36  ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 10.094 -24.875 26.647 1.00 22.61  ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 10.538 -23.818 27.586 1.00 23.50  ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 11.641 -23.039 26.863 1.00 23.39  ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 12.193 -23.537 25.879 1.00 22.85  ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 11.052 -24.409 28.890 1.00 25.53  ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 9.905  -25.013 29.652 1.00 30.30  ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 10.266 -25.689 30.960 1.00 37.21  ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 11.106 -25.140 31.702 1.00 42.38  ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 9.706  -26.770 31.241 1.00 37.97  ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 11.966 -21.792 27.261 1.00 24.03  ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 12.937 -21.004 26.449 1.00 23.79  ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 14.289 -21.690 26.179 1.00 22.92  ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 14.825 -21.615 25.047 1.00 23.92  ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 13.109 -19.711 27.243 1.00 25.43  ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 11.835 -19.596 28.069 1.00 26.25  ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 11.355 -21.002 28.348 1.00 24.63  ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 14.803 -22.415 27.193 1.00 20.53  ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 16.061 -23.150 27.079 1.00 20.32  ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 15.998 -24.322 26.094 1.00 19.18  ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 17.035 -24.927 25.763 1.00 19.03  ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 14.789 -24.657 25.616 1.00 17.30  ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 14.615 -25.723 24.626 1.00 16.59  ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 14.938 -25.270 23.215 1.00 15.25  ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 15.060 -26.121 22.332 1.00 15.45  ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 13.173 -26.288 24.636 1.00 16.02  ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 12.910 -27.147 25.862 1.00 17.93  ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 13.860 -27.802 26.332 1.00 18.39  ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 11.778 -27.092 26.387 1.00 18.91  ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 15.116 -23.937 22.969 1.00 14.07  ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 15.446 -23.473 21.622 1.00 14.89  ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 16.718 -24.127 21.146 1.00 14.97  ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 17.671 -24.259 21.922 1.00 16.29  ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 15.557 -21.947 21.576 1.00 16.19  ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 13.948 -21.103 21.628 1.00 19.80  ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 16.719 -24.555 19.902 1.00 12.84  ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 17.882 -25.214 19.320 1.00 13.27  ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 17.742 -26.723 19.236 1.00 13.42  ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 18.517 -27.383 18.534 1.00 13.82  ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 16.742 -27.276 19.945 1.00 12.19  ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 16.492 -28.720 19.847 1.00 11.64  ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 16.099 -29.102 18.410 1.00 11.68  ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 15.296 -28.387 17.790 1.00 11.68  ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 16.623 -30.215 17.905 1.00 11.49  ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 16.312 -30.567 16.519 1.00 11.64  ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 15.008 -31.308 16.351 1.00 10.73  ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 14.699 -32.205 17.153 1.00 11.86  ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.522 -31.389 15.959 1.00 15.31  ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 18.718 -30.423 15.671 1.00 18.06  ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.186 -32.217 14.699 1.00 18.00  ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 20.047 -31.220 15.221 1.00 21.57  ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 14.316 -30.997 15.261 1.00 10.16  ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 13.140 -31.754 14.764 1.00 9.51   ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 13.661 -32.529 13.538 1.00 10.70  ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 14.247 -31.921 12.609 1.00 11.13  ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 12.044 -30.739 14.319 1.00 10.56  ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 10.846 -31.361 13.599 1.00 11.74  ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 10.067 -32.336 14.510 1.00 12.66  ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 9.884  -30.240 13.069 1.00 12.46  ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 13.400 -33.861 13.521 1.00 10.97  ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 13.834 -34.731 12.424 1.00 12.34  ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 12.662 -35.525 11.920 1.00 12.93  ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 11.839 -36.004 12.712 1.00 14.13  ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 14.855 -35.758 12.971 1.00 15.82  ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 16.130 -35.204 13.510 1.00 22.05  ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 16.996 -36.374 14.044 1.00 26.83  ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 17.549 -37.030 12.870 1.00 32.65  ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 18.706 -36.680 12.309 1.00 34.99  ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 19.530 -35.843 12.932 1.00 35.78  ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 19.063 -37.198 11.154 1.00 35.09  ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 12.668 -35.784 10.635 1.00 12.23  ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 11.694 -36.711 10.007 1.00 13.23  ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 12.490 -37.871 9.439  1.00 16.21  ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 13.696 -37.989 9.650  1.00 15.62  ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 10.874 -36.009 8.925  1.00 12.52  ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 11.865 -35.481 7.486  1.00 13.44  ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 11.785 -38.793 8.724  1.00 17.96  ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 12.474 -39.928 8.135  1.00 19.48  ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 13.546 -39.520 7.093  1.00 20.53  ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 14.419 -40.319 6.756  1.00 23.42  ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 11.444 -40.877 7.506  1.00 21.86  ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 10.758 -40.285 6.276  1.00 23.15  ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 9.747  -41.256 5.677  1.00 32.89  ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 8.540  -41.013 5.750  1.00 36.77  ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 10.217 -42.355 5.075  1.00 34.49  ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 13.532 -38.263 6.608  1.00 17.87  ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 14.487 -37.797 5.591  1.00 18.68  ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 15.687 -37.059 6.181  1.00 18.88  ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 16.631 -36.787 5.444  1.00 21.54  ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 13.775 -36.875 4.581  1.00 18.50  ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 12.573 -37.545 3.967  1.00 17.83  ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 11.289 -37.143 4.270  1.00 18.29  ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 12.515 -38.530 3.032  1.00 20.59  ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 10.475 -37.945 3.599  1.00 20.02  ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 11.161 -38.795 2.815  1.00 22.21  ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 15.638 -36.703 7.479  1.00 16.13  ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 16.753 -35.959 8.077  1.00 15.23  ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 16.291 -34.792 8.943  1.00 13.53  ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 15.156 -34.766 9.406  1.00 14.02  ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 17.158 -33.771 9.082  1.00 13.22  ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 16.825 -32.603 9.915  1.00 12.69  ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 15.827 -31.687 9.228  1.00 12.85  ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 16.062 -31.249 8.089  1.00 13.41  ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 18.114 -31.831 10.267 1.00 14.53  ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 17.774 -30.517 10.989 1.00 14.53  ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 19.035 -32.714 11.121 1.00 15.28  ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 14.755 -31.327 9.926  1.00 11.82  ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 13.708 -30.467 9.414  1.00 11.68  ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 13.883 -29.024 9.866  1.00 11.87  ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 13.627 -28.069 9.117  1.00 11.78  ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 12.319 -31.014 9.881  1.00 11.56  ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 11.179 -30.061 9.516  1.00 12.65  ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 12.064 -32.375 9.250  1.00 12.90  ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 14.246 -28.857 11.134 1.00 11.24  ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 14.372 -27.520 11.697 1.00 13.38  ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 14.744 -27.564 13.158 1.00 11.26  ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 15.143 -28.622 13.688 1.00 11.55  ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 14.657 -26.394 13.813 1.00 11.03  ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 15.048 -26.316 15.226 1.00 10.68  ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 13.988 -25.618 16.045 1.00 10.93  ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 13.319 -24.700 15.542 1.00 11.16  ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 16.406 -25.589 15.430 1.00 12.14  ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 16.420 -24.228 14.687 1.00 13.63  ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.605 -26.496 15.048 1.00 14.00  ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 17.740 -23.388 15.078 1.00 14.83  ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 13.832 -25.978 17.339 1.00 10.11  ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 12.875 -25.253 18.200 1.00 10.67  ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 13.218 -23.757 18.233 1.00 11.26  ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 14.392 -23.405 18.423 1.00 11.70  ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 12.929 -25.810 19.624 1.00 11.60  ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 12.031 -25.000 20.564 1.00 13.12  ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 12.506 -27.292 19.646 1.00 12.10  ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 12.196 -22.893 18.084 1.00 11.89  ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 12.387 -21.455 18.079 1.00 11.67  ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 11.379 -20.710 18.960 1.00 14.17  ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 11.715 -19.630 19.487 1.00 14.80  ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 12.307 -20.980 16.621 1.00 12.67  ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 12.421 -19.550 16.542 1.00 12.89  ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 10.186 -21.260 19.167 1.00 14.31  ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 9.165  -20.584 20.006 1.00 14.93  ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 8.432  -21.592 20.862 1.00 15.17  ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 8.497  -22.805 20.612 1.00 14.16  ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 8.123  -19.821 19.107 1.00 16.17  ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 7.238  -20.745 18.432 1.00 17.93  ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 8.744  -18.892 18.117 1.00 16.73  ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 7.708  -21.097 21.860 1.00 17.38  ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 6.892  -21.958 22.698 1.00 19.66  ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 5.903  -21.164 23.505 1.00 21.45  ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 6.031  -19.958 23.644 1.00 21.83  ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 4.951  -21.863 24.089 1.00 23.13  ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 3.935  -21.225 24.928 1.00 24.65  ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 2.585  -21.888 24.729 1.00 25.69  ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 2.292  -22.384 23.639 1.00 24.87  ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 1.758  -21.895 25.799 1.00 26.75  ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 0.419  -22.467 25.727 1.00 27.76  ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 0.331  -23.916 25.253 1.00 26.30  ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? -0.691 -24.315 24.668 1.00 27.45  ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? -0.446 -21.591 24.825 1.00 30.01  ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? -0.652 -20.184 25.310 1.00 35.57  ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? -0.690 -19.908 26.513 1.00 37.15  ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? -0.849 -19.287 24.367 1.00 36.49  ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 1.373  -24.707 25.506 1.00 23.11  ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 1.353  -26.089 25.075 1.00 21.48  ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 1.585  -26.261 23.578 1.00 19.56  ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 1.261  -27.309 23.044 1.00 20.05  ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 2.143  -25.266 22.917 1.00 17.26  ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 2.495  -25.344 21.520 1.00 17.20  ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 4.027  -25.195 21.439 1.00 18.79  ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 4.603  -24.470 22.254 1.00 23.63  ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 1.757  -24.246 20.754 1.00 18.53  ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 0.215  -24.449 20.684 1.00 21.20  ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? -0.505 -23.133 20.372 1.00 24.27  ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? -0.154 -25.466 19.629 1.00 21.38  ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 4.666  -25.828 20.484 1.00 15.64  ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 6.087  -25.617 20.237 1.00 14.28  ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 6.233  -25.195 18.771 1.00 13.85  ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 5.557  -25.770 17.892 1.00 13.46  ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 6.868  -26.917 20.534 1.00 14.91  ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 6.298  -28.144 19.839 1.00 17.71  ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 8.378  -26.734 20.244 1.00 15.75  ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 7.112  -24.227 18.527 1.00 11.92  ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 7.317  -23.763 17.174 1.00 13.11  ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 8.722  -24.076 16.700 1.00 11.64  ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 9.665  -23.911 17.463 1.00 12.69  ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 8.815  -24.510 15.439 1.00 11.19  ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 10.111 -24.898 14.836 1.00 11.13  ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 10.404 -24.005 13.640 1.00 11.55  ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 9.542  -23.883 12.751 1.00 11.78  ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 10.057 -26.356 14.328 1.00 12.26  ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 9.602  -27.345 15.377 1.00 12.51  ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 10.498 -27.866 16.290 1.00 11.52  ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 8.272  -27.749 15.455 1.00 13.59  ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 10.084 -28.788 17.244 1.00 12.57  ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 7.867  -28.705 16.390 1.00 14.09  ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 8.778  -29.232 17.268 1.00 13.54  ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 11.643 -23.482 13.583 1.00 11.33  ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 12.093 -22.756 12.402 1.00 10.22  ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 12.488 -23.774 11.357 1.00 10.47  ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 13.419 -24.559 11.568 1.00 10.68  ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 13.300 -21.911 12.786 1.00 10.98  ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 11.818 -23.766 10.203 1.00 10.62  ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 12.126 -24.697 9.125  1.00 11.24  ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 13.465 -24.370 8.451  1.00 12.30  ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 13.816 -23.180 8.287  1.00 12.42  ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 11.017 -24.558 8.033  1.00 13.35  ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 11.136 -25.564 6.912  1.00 18.48  ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 11.289 -26.743 7.200  1.00 17.26  ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 11.156 -25.138 5.723  1.00 21.82  ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 14.244 -25.414 8.066  1.00 11.52  ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 15.469 -25.194 7.282  1.00 12.49  ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 15.428 -25.946 5.943  1.00 13.61  ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 16.393 -25.871 5.187  1.00 14.27  ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 16.761 -25.565 8.046  1.00 12.74  ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 16.895 -24.735 9.341  1.00 12.75  ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 16.816 -27.070 8.365  1.00 13.10  ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 14.326 -26.667 5.633  1.00 12.67  ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 14.268 -27.505 4.449  1.00 12.49  ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 14.348 -26.748 3.140  1.00 14.48  ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 14.711 -27.357 2.127  1.00 16.33  ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 12.999 -28.378 4.479  1.00 12.17  ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 12.987 -29.380 5.621  1.00 13.65  ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 11.658 -30.098 5.635  1.00 11.90  ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 10.565 -29.202 6.031  1.00 12.67  ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 9.318  -29.596 6.289  1.00 12.93  ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 8.928  -30.837 6.004  1.00 14.24  ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 8.420  -28.728 6.749  1.00 14.55  ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 13.969 -25.475 3.133  1.00 14.43  ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 14.037 -24.686 1.900  1.00 14.89  ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 15.412 -24.113 1.642  1.00 15.89  ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 15.599 -23.583 0.543  1.00 17.44  ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 13.033 -23.536 1.939  1.00 15.60  ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 13.311 -22.519 3.045  1.00 19.60  ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 13.595 -22.951 4.188  1.00 18.65  ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 13.246 -21.266 2.753  1.00 19.58  ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 16.388 -24.213 2.590  1.00 15.27  ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.719 -23.615 2.419  1.00 15.90  ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 18.612 -24.572 1.677  1.00 16.33  ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 19.458 -25.289 2.249  1.00 15.84  ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 18.302 -23.268 3.804  1.00 14.90  ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.422 -22.332 4.635  1.00 15.82  ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 17.977 -22.162 6.019  1.00 16.91  ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.226 -20.995 3.969  1.00 16.98  ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 18.369 -24.635 0.346  1.00 16.26  ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 19.033 -25.662 -0.474 1.00 17.60  ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 20.534 -25.488 -0.523 1.00 19.41  ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 21.265 -26.476 -0.677 1.00 21.00  ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 18.434 -25.712 -1.875 1.00 17.66  ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 16.915 -25.755 -1.988 1.00 18.60  ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 16.484 -25.865 -3.471 1.00 20.40  ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 16.293 -26.878 -1.130 1.00 19.06  ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 21.007 -24.221 -0.379 1.00 19.65  ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 22.443 -23.922 -0.437 1.00 20.31  ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 23.227 -24.524 0.750  1.00 21.21  ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 24.455 -24.586 0.682  1.00 22.39  ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 22.661 -22.398 -0.518 1.00 20.07  ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 21.962 -21.631 0.568  1.00 19.07  ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 20.722 -21.065 0.517  1.00 19.46  ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 22.487 -21.342 1.881  1.00 18.31  ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 20.450 -20.425 1.720  1.00 19.05  ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 21.542 -20.545 2.546  1.00 18.53  ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 23.703 -21.625 2.523  1.00 18.91  ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 21.742 -20.095 3.859  1.00 19.55  ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 23.932 -21.112 3.797  1.00 20.29  ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 22.970 -20.333 4.437  1.00 19.47  ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 22.547 -25.011 1.818  1.00 20.26  ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 23.289 -25.618 2.944  1.00 20.37  ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 24.101 -26.853 2.485  1.00 24.95  ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 25.082 -27.190 3.152  1.00 25.68  ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 22.301 -26.066 4.068  1.00 19.23  ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 21.703 -24.924 4.889  1.00 18.33  ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 20.680 -25.485 5.868  1.00 18.17  ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 22.801 -24.163 5.687  1.00 18.14  ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 23.633 -27.549 1.418  1.00 27.82  ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 24.212 -28.765 0.820  1.00 32.95  ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 25.305 -28.509 -0.196 1.00 36.99  ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 25.852 -29.487 -0.710 1.00 38.35  ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 23.131 -29.509 0.034  1.00 36.66  ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 22.080 -30.181 0.864  1.00 43.42  ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 22.381 -30.544 2.013  1.00 45.30  ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 20.955 -30.362 0.353  1.00 48.16  ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 25.539 -27.256 -0.589 1.00 38.56  ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 26.565 -26.931 -1.576 1.00 41.54  ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 27.575 -25.939 -0.975 1.00 43.63  ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 28.442 -25.399 -1.682 1.00 45.07  ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 25.916 -26.369 -2.856 1.00 44.92  ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 25.225 -25.030 -2.672 1.00 51.51  ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 24.269 -24.645 -3.790 1.00 60.13  ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 24.238 -23.448 -4.164 1.00 60.18  ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 23.541 -25.539 -4.282 1.00 62.97  ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1BQG C 2 .   ? 25.190 13.880  10.530 1.00 22.06  ? 201 A1BQG A N1  1 
HETATM 2156 N  N3  . A1BQG C 2 .   ? 24.971 9.365   9.455  1.00 35.90  ? 201 A1BQG A N3  1 
HETATM 2157 C  C4  . A1BQG C 2 .   ? 24.157 14.563  9.735  1.00 22.03  ? 201 A1BQG A C4  1 
HETATM 2158 C  C5  . A1BQG C 2 .   ? 25.879 12.797  10.123 1.00 24.08  ? 201 A1BQG A C5  1 
HETATM 2159 C  C6  . A1BQG C 2 .   ? 25.419 12.202  8.807  1.00 28.41  ? 201 A1BQG A C6  1 
HETATM 2160 C  C7  . A1BQG C 2 .   ? 26.286 11.062  8.336  1.00 32.99  ? 201 A1BQG A C7  1 
HETATM 2161 C  C8  . A1BQG C 2 .   ? 27.327 11.306  7.449  1.00 34.70  ? 201 A1BQG A C8  1 
HETATM 2162 C  C10 . A1BQG C 2 .   ? 27.659 8.981   7.211  1.00 35.90  ? 201 A1BQG A C10 1 
HETATM 2163 O  O1  . A1BQG C 2 .   ? 26.809 12.344  10.767 1.00 23.20  ? 201 A1BQG A O1  1 
HETATM 2164 C  C3  . A1BQG C 2 .   ? 22.797 14.488  10.407 1.00 22.06  ? 201 A1BQG A C3  1 
HETATM 2165 C  C2  . A1BQG C 2 .   ? 22.878 14.945  11.864 1.00 20.76  ? 201 A1BQG A C2  1 
HETATM 2166 C  C12 . A1BQG C 2 .   ? 25.332 14.372  11.902 1.00 20.90  ? 201 A1BQG A C12 1 
HETATM 2167 C  C1  . A1BQG C 2 .   ? 23.988 14.196  12.612 1.00 19.59  ? 201 A1BQG A C1  1 
HETATM 2168 C  C   . A1BQG C 2 .   ? 24.081 14.653  14.057 1.00 19.33  ? 201 A1BQG A C   1 
HETATM 2169 O  O   . A1BQG C 2 .   ? 24.456 15.792  14.345 1.00 19.95  ? 201 A1BQG A O   1 
HETATM 2170 N  N   . A1BQG C 2 .   ? 23.754 13.750  14.966 1.00 16.87  ? 201 A1BQG A N   1 
HETATM 2171 C  C11 . A1BQG C 2 .   ? 25.986 9.696   8.640  1.00 35.18  ? 201 A1BQG A C11 1 
HETATM 2172 N  N2  . A1BQG C 2 .   ? 26.680 8.684   8.079  1.00 35.82  ? 201 A1BQG A N2  1 
HETATM 2173 C  C9  . A1BQG C 2 .   ? 28.015 10.259  6.875  1.00 35.58  ? 201 A1BQG A C9  1 
HETATM 2174 ZN ZN  . ZN    D 3 .   ? 23.216 -5.526  26.951 1.00 18.41  2 202 ZN    A ZN  1 
HETATM 2175 S  S   . DMS   E 4 .   ? 15.097 -0.330  12.287 1.00 38.57  ? 203 DMS   A S   1 
HETATM 2176 O  O   . DMS   E 4 .   ? 16.410 -0.732  12.885 1.00 32.64  ? 203 DMS   A O   1 
HETATM 2177 C  C1  . DMS   E 4 .   ? 15.210 0.448   10.655 1.00 38.60  ? 203 DMS   A C1  1 
HETATM 2178 C  C2  . DMS   E 4 .   ? 14.410 1.116   13.215 1.00 37.70  ? 203 DMS   A C2  1 
HETATM 2179 N  N1  . A1BQG F 2 .   ? 10.659 -16.804 22.599 1.00 20.15  ? 201 A1BQG C N1  1 
HETATM 2180 N  N3  . A1BQG F 2 .   ? 10.762 -21.352 23.513 1.00 35.60  ? 201 A1BQG C N3  1 
HETATM 2181 C  C4  . A1BQG F 2 .   ? 11.744 -16.112 23.313 1.00 20.18  ? 201 A1BQG C C4  1 
HETATM 2182 C  C5  . A1BQG F 2 .   ? 9.967  -17.875 23.044 1.00 23.20  ? 201 A1BQG C C5  1 
HETATM 2183 C  C6  . A1BQG F 2 .   ? 10.517 -18.516 24.307 1.00 27.45  ? 201 A1BQG C C6  1 
HETATM 2184 C  C7  . A1BQG F 2 .   ? 9.648  -19.646 24.808 1.00 31.81  ? 201 A1BQG C C7  1 
HETATM 2185 C  C8  . A1BQG F 2 .   ? 8.690  -19.392 25.784 1.00 33.08  ? 201 A1BQG C C8  1 
HETATM 2186 C  C10 . A1BQG F 2 .   ? 8.246  -21.705 25.941 1.00 34.60  ? 201 A1BQG C C10 1 
HETATM 2187 O  O1  . A1BQG F 2 .   ? 8.960  -18.290 22.473 1.00 20.82  ? 201 A1BQG C O1  1 
HETATM 2188 C  C3  . A1BQG F 2 .   ? 13.045 -16.194 22.527 1.00 19.53  ? 201 A1BQG C C3  1 
HETATM 2189 C  C2  . A1BQG F 2 .   ? 12.845 -15.717 21.088 1.00 18.32  ? 201 A1BQG C C2  1 
HETATM 2190 C  C12 . A1BQG F 2 .   ? 10.411 -16.287 21.252 1.00 18.06  ? 201 A1BQG C C12 1 
HETATM 2191 C  C1  . A1BQG F 2 .   ? 11.679 -16.467 20.420 1.00 16.88  ? 201 A1BQG C C1  1 
HETATM 2192 C  C   . A1BQG F 2 .   ? 11.461 -16.000 18.993 1.00 16.49  ? 201 A1BQG C C   1 
HETATM 2193 O  O   . A1BQG F 2 .   ? 11.080 -14.845 18.756 1.00 15.72  ? 201 A1BQG C O   1 
HETATM 2194 N  N   . A1BQG F 2 .   ? 11.677 -16.914 18.043 1.00 15.80  ? 201 A1BQG C N   1 
HETATM 2195 C  C11 . A1BQG F 2 .   ? 9.845  -21.009 24.422 1.00 34.15  ? 201 A1BQG C C11 1 
HETATM 2196 N  N2  . A1BQG F 2 .   ? 9.136  -22.011 24.984 1.00 34.69  ? 201 A1BQG C N2  1 
HETATM 2197 C  C9  . A1BQG F 2 .   ? 7.992  -20.430 26.365 1.00 33.98  ? 201 A1BQG C C9  1 
HETATM 2198 ZN ZN  . ZN    G 3 .   ? 10.605 -35.679 5.568  1.00 14.46  2 202 ZN    C ZN  1 
HETATM 2199 S  S   . DMS   H 4 .   ? 14.265 -10.725 7.052  1.00 69.67  ? 203 DMS   C S   1 
HETATM 2200 O  O   . DMS   H 4 .   ? 14.298 -10.115 8.438  1.00 69.13  ? 203 DMS   C O   1 
HETATM 2201 C  C1  . DMS   H 4 .   ? 12.705 -10.263 6.229  1.00 69.69  ? 203 DMS   C C1  1 
HETATM 2202 C  C2  . DMS   H 4 .   ? 15.357 -9.742  5.981  1.00 69.66  ? 203 DMS   C C2  1 
HETATM 2203 O  O   . HOH   I 5 .   ? 8.128  16.154  19.475 1.00 247.12 ? 301 HOH   A O   1 
HETATM 2204 O  O   . HOH   I 5 .   ? 14.786 22.194  24.487 1.00 23.73  ? 302 HOH   A O   1 
HETATM 2205 O  O   . HOH   I 5 .   ? 23.867 7.384   28.159 1.00 23.08  ? 303 HOH   A O   1 
HETATM 2206 O  O   . HOH   I 5 .   ? 22.610 7.810   26.951 1.00 222.30 ? 304 HOH   A O   1 
HETATM 2207 O  O   . HOH   I 5 .   ? 23.010 10.920  22.688 1.00 109.92 ? 305 HOH   A O   1 
HETATM 2208 O  O   . HOH   I 5 .   ? 31.844 7.328   23.099 1.00 36.07  ? 306 HOH   A O   1 
HETATM 2209 O  O   . HOH   I 5 .   ? 19.573 10.265  17.591 1.00 244.70 ? 307 HOH   A O   1 
HETATM 2210 O  O   . HOH   I 5 .   ? 12.748 -4.696  20.530 1.00 40.39  ? 308 HOH   A O   1 
HETATM 2211 O  O   . HOH   I 5 .   ? 34.899 15.037  24.722 1.00 42.56  ? 309 HOH   A O   1 
HETATM 2212 O  O   . HOH   I 5 .   ? 11.183 21.401  24.570 1.00 26.09  ? 310 HOH   A O   1 
HETATM 2213 O  O   . HOH   I 5 .   ? 29.787 7.120   4.636  1.00 38.41  ? 311 HOH   A O   1 
HETATM 2214 O  O   . HOH   I 5 .   ? 11.673 -1.654  28.016 1.00 26.90  ? 312 HOH   A O   1 
HETATM 2215 O  O   . HOH   I 5 .   ? 14.953 8.579   13.411 1.00 14.35  ? 313 HOH   A O   1 
HETATM 2216 O  O   . HOH   I 5 .   ? 29.184 -7.519  25.278 1.00 56.16  ? 314 HOH   A O   1 
HETATM 2217 O  O   . HOH   I 5 .   ? 19.853 10.539  31.966 1.00 50.76  ? 315 HOH   A O   1 
HETATM 2218 O  O   . HOH   I 5 .   ? 30.894 -5.300  11.439 1.00 29.88  ? 316 HOH   A O   1 
HETATM 2219 O  O   . HOH   I 5 .   ? 2.523  1.203   28.090 1.00 39.43  ? 317 HOH   A O   1 
HETATM 2220 O  O   . HOH   I 5 .   ? 0.014  14.474  22.721 1.00 60.41  ? 318 HOH   A O   1 
HETATM 2221 O  O   . HOH   I 5 .   ? 22.386 6.507   1.605  1.00 26.31  ? 319 HOH   A O   1 
HETATM 2222 O  O   . HOH   I 5 .   ? 33.836 -3.154  12.872 1.00 39.51  ? 320 HOH   A O   1 
HETATM 2223 O  O   . HOH   I 5 .   ? 24.123 3.981   29.207 1.00 26.11  ? 321 HOH   A O   1 
HETATM 2224 O  O   . HOH   I 5 .   ? 17.077 20.708  22.981 1.00 20.82  ? 322 HOH   A O   1 
HETATM 2225 O  O   . HOH   I 5 .   ? 34.368 -0.825  16.453 1.00 14.95  ? 323 HOH   A O   1 
HETATM 2226 O  O   . HOH   I 5 .   ? -1.851 15.626  20.330 1.00 26.75  ? 324 HOH   A O   1 
HETATM 2227 O  O   . HOH   I 5 .   ? 17.982 16.554  28.566 1.00 48.98  ? 325 HOH   A O   1 
HETATM 2228 O  O   . HOH   I 5 .   ? 23.531 11.002  21.386 1.00 13.92  ? 326 HOH   A O   1 
HETATM 2229 O  O   . HOH   I 5 .   ? 7.141  15.522  29.431 1.00 40.82  ? 327 HOH   A O   1 
HETATM 2230 O  O   . HOH   I 5 .   ? 11.157 -0.224  15.957 1.00 25.09  ? 328 HOH   A O   1 
HETATM 2231 O  O   . HOH   I 5 .   ? 31.998 2.951   4.997  1.00 32.91  ? 329 HOH   A O   1 
HETATM 2232 O  O   . HOH   I 5 .   ? 28.440 -6.155  3.538  1.00 26.91  ? 330 HOH   A O   1 
HETATM 2233 O  O   . HOH   I 5 .   ? 8.811  3.835   12.098 1.00 36.63  ? 331 HOH   A O   1 
HETATM 2234 O  O   . HOH   I 5 .   ? 23.854 16.650  27.381 1.00 46.65  ? 332 HOH   A O   1 
HETATM 2235 O  O   . HOH   I 5 .   ? 34.880 13.912  16.340 1.00 38.88  ? 333 HOH   A O   1 
HETATM 2236 O  O   . HOH   I 5 .   ? 20.085 2.102   9.354  1.00 14.43  ? 334 HOH   A O   1 
HETATM 2237 O  O   . HOH   I 5 .   ? 27.905 3.078   -0.315 1.00 23.01  ? 335 HOH   A O   1 
HETATM 2238 O  O   . HOH   I 5 .   ? 17.831 -7.702  21.566 1.00 23.64  ? 336 HOH   A O   1 
HETATM 2239 O  O   . HOH   I 5 .   ? 22.001 8.712   2.892  1.00 29.04  ? 337 HOH   A O   1 
HETATM 2240 O  O   . HOH   I 5 .   ? 11.351 10.750  10.021 1.00 46.21  ? 338 HOH   A O   1 
HETATM 2241 O  O   . HOH   I 5 .   ? 15.910 -0.607  4.931  1.00 32.63  ? 339 HOH   A O   1 
HETATM 2242 O  O   . HOH   I 5 .   ? 16.251 -3.303  13.910 1.00 34.28  ? 340 HOH   A O   1 
HETATM 2243 O  O   . HOH   I 5 .   ? 16.570 -7.328  29.228 1.00 30.40  ? 341 HOH   A O   1 
HETATM 2244 O  O   . HOH   I 5 .   ? 16.481 18.590  27.030 1.00 37.28  ? 342 HOH   A O   1 
HETATM 2245 O  O   . HOH   I 5 .   ? 12.320 17.818  13.280 1.00 34.02  ? 343 HOH   A O   1 
HETATM 2246 O  O   . HOH   I 5 .   ? 25.430 17.916  12.844 1.00 19.43  ? 344 HOH   A O   1 
HETATM 2247 O  O   . HOH   I 5 .   ? 6.404  3.072   29.104 1.00 40.98  ? 345 HOH   A O   1 
HETATM 2248 O  O   . HOH   I 5 .   ? 20.073 11.890  8.575  1.00 21.05  ? 346 HOH   A O   1 
HETATM 2249 O  O   . HOH   I 5 .   ? 7.324  7.584   31.875 1.00 38.95  ? 347 HOH   A O   1 
HETATM 2250 O  O   . HOH   I 5 .   ? 29.298 13.498  11.232 1.00 38.84  ? 348 HOH   A O   1 
HETATM 2251 O  O   . HOH   I 5 .   ? 23.552 1.794   -0.876 1.00 16.65  ? 349 HOH   A O   1 
HETATM 2252 O  O   . HOH   I 5 .   ? 18.641 -11.649 27.366 1.00 34.52  ? 350 HOH   A O   1 
HETATM 2253 O  O   . HOH   I 5 .   ? 17.204 2.094   9.338  1.00 19.21  ? 351 HOH   A O   1 
HETATM 2254 O  O   . HOH   I 5 .   ? 5.096  3.003   21.117 1.00 22.16  ? 352 HOH   A O   1 
HETATM 2255 O  O   . HOH   I 5 .   ? 22.388 -6.076  0.496  1.00 45.63  ? 353 HOH   A O   1 
HETATM 2256 O  O   . HOH   I 5 .   ? 4.134  9.906   18.022 1.00 36.14  ? 354 HOH   A O   1 
HETATM 2257 O  O   . HOH   I 5 .   ? 27.001 19.126  15.011 1.00 21.28  ? 355 HOH   A O   1 
HETATM 2258 O  O   . HOH   I 5 .   ? 25.579 1.625   29.846 1.00 25.90  ? 356 HOH   A O   1 
HETATM 2259 O  O   . HOH   I 5 .   ? 24.941 -8.697  24.889 1.00 36.52  ? 357 HOH   A O   1 
HETATM 2260 O  O   . HOH   I 5 .   ? 16.730 4.445   5.995  1.00 28.56  ? 358 HOH   A O   1 
HETATM 2261 O  O   . HOH   I 5 .   ? 11.540 -7.712  27.779 1.00 39.32  ? 359 HOH   A O   1 
HETATM 2262 O  O   . HOH   I 5 .   ? 13.481 18.689  14.711 1.00 27.10  ? 360 HOH   A O   1 
HETATM 2263 O  O   . HOH   I 5 .   ? 30.740 5.084   7.814  1.00 25.88  ? 361 HOH   A O   1 
HETATM 2264 O  O   . HOH   I 5 .   ? 23.210 3.703   0.209  1.00 139.80 ? 362 HOH   A O   1 
HETATM 2265 O  O   . HOH   I 5 .   ? 4.446  4.120   28.210 1.00 33.52  ? 363 HOH   A O   1 
HETATM 2266 O  O   . HOH   I 5 .   ? 28.380 0.830   26.833 1.00 22.36  ? 364 HOH   A O   1 
HETATM 2267 O  O   . HOH   I 5 .   ? 34.816 -6.407  21.584 1.00 42.79  ? 365 HOH   A O   1 
HETATM 2268 O  O   . HOH   I 5 .   ? 4.166  20.232  15.434 1.00 37.49  ? 366 HOH   A O   1 
HETATM 2269 O  O   . HOH   I 5 .   ? 30.410 -5.739  26.287 1.00 29.03  ? 367 HOH   A O   1 
HETATM 2270 O  O   . HOH   I 5 .   ? 29.573 -2.099  8.370  1.00 20.91  ? 368 HOH   A O   1 
HETATM 2271 O  O   . HOH   I 5 .   ? 5.032  10.801  12.648 1.00 33.66  ? 369 HOH   A O   1 
HETATM 2272 O  O   . HOH   I 5 .   ? 17.139 18.439  15.568 1.00 15.00  ? 370 HOH   A O   1 
HETATM 2273 O  O   . HOH   I 5 .   ? 28.018 16.288  10.678 1.00 27.55  ? 371 HOH   A O   1 
HETATM 2274 O  O   . HOH   I 5 .   ? 29.264 1.284   25.188 1.00 45.32  ? 372 HOH   A O   1 
HETATM 2275 O  O   . HOH   I 5 .   ? 21.631 9.922   23.301 1.00 13.28  ? 373 HOH   A O   1 
HETATM 2276 O  O   . HOH   I 5 .   ? 4.021  19.957  21.692 1.00 27.08  ? 374 HOH   A O   1 
HETATM 2277 O  O   . HOH   I 5 .   ? 29.644 25.954  16.078 1.00 40.31  ? 375 HOH   A O   1 
HETATM 2278 O  O   . HOH   I 5 .   ? 24.749 -9.163  22.853 1.00 36.22  ? 376 HOH   A O   1 
HETATM 2279 O  O   . HOH   I 5 .   ? 22.874 20.852  20.390 1.00 25.96  ? 377 HOH   A O   1 
HETATM 2280 O  O   . HOH   I 5 .   ? 16.475 8.944   6.783  1.00 24.24  ? 378 HOH   A O   1 
HETATM 2281 O  O   . HOH   I 5 .   ? 24.959 4.180   -1.319 1.00 21.84  ? 379 HOH   A O   1 
HETATM 2282 O  O   . HOH   I 5 .   ? 3.451  18.105  23.610 1.00 29.13  ? 380 HOH   A O   1 
HETATM 2283 O  O   . HOH   I 5 .   ? 19.972 -4.854  15.311 1.00 25.19  ? 381 HOH   A O   1 
HETATM 2284 O  O   . HOH   I 5 .   ? 32.475 8.977   4.473  1.00 56.90  ? 382 HOH   A O   1 
HETATM 2285 O  O   . HOH   I 5 .   ? 27.118 -8.681  8.519  1.00 35.53  ? 383 HOH   A O   1 
HETATM 2286 O  O   . HOH   I 5 .   ? 18.340 -5.196  30.524 1.00 28.80  ? 384 HOH   A O   1 
HETATM 2287 O  O   . HOH   I 5 .   ? 25.500 20.459  22.123 1.00 38.56  ? 385 HOH   A O   1 
HETATM 2288 O  O   . HOH   I 5 .   ? 26.532 -7.813  23.977 1.00 34.67  ? 386 HOH   A O   1 
HETATM 2289 O  O   . HOH   I 5 .   ? 20.139 23.368  15.107 1.00 42.90  ? 387 HOH   A O   1 
HETATM 2290 O  O   . HOH   I 5 .   ? 35.495 14.552  20.261 1.00 30.65  ? 388 HOH   A O   1 
HETATM 2291 O  O   . HOH   I 5 .   ? 34.548 3.126   26.154 1.00 33.75  ? 389 HOH   A O   1 
HETATM 2292 O  O   . HOH   I 5 .   ? 23.690 18.063  6.202  1.00 41.45  ? 390 HOH   A O   1 
HETATM 2293 O  O   . HOH   I 5 .   ? 17.049 0.420   2.597  1.00 33.09  ? 391 HOH   A O   1 
HETATM 2294 O  O   . HOH   I 5 .   ? 30.540 -2.946  11.652 1.00 32.86  ? 392 HOH   A O   1 
HETATM 2295 O  O   . HOH   I 5 .   ? 28.294 17.152  8.232  1.00 41.16  ? 393 HOH   A O   1 
HETATM 2296 O  O   . HOH   I 5 .   ? 17.769 20.072  13.553 1.00 30.06  ? 394 HOH   A O   1 
HETATM 2297 O  O   . HOH   I 5 .   ? 26.992 -6.265  29.812 1.00 43.59  ? 395 HOH   A O   1 
HETATM 2298 O  O   . HOH   I 5 .   ? 19.663 -6.164  32.735 1.00 45.46  ? 396 HOH   A O   1 
HETATM 2299 O  O   . HOH   I 5 .   ? 26.794 19.044  24.630 1.00 41.46  ? 397 HOH   A O   1 
HETATM 2300 O  O   . HOH   I 5 .   ? 20.456 20.369  24.302 1.00 34.31  ? 398 HOH   A O   1 
HETATM 2301 O  O   . HOH   I 5 .   ? 29.158 25.764  13.333 1.00 30.63  ? 399 HOH   A O   1 
HETATM 2302 O  O   . HOH   I 5 .   ? 23.928 15.071  29.605 1.00 60.43  ? 400 HOH   A O   1 
HETATM 2303 O  O   . HOH   I 5 .   ? 2.731  8.599   26.241 1.00 38.07  ? 401 HOH   A O   1 
HETATM 2304 O  O   . HOH   I 5 .   ? 4.705  10.632  14.922 1.00 37.65  ? 402 HOH   A O   1 
HETATM 2305 O  O   . HOH   I 5 .   ? 22.331 -8.352  19.398 1.00 29.30  ? 403 HOH   A O   1 
HETATM 2306 O  O   . HOH   I 5 .   ? 4.814  6.101   13.494 1.00 52.43  ? 404 HOH   A O   1 
HETATM 2307 O  O   . HOH   I 5 .   ? 15.752 -5.354  5.226  1.00 51.98  ? 405 HOH   A O   1 
HETATM 2308 O  O   . HOH   I 5 .   ? 20.082 13.897  29.069 1.00 29.79  ? 406 HOH   A O   1 
HETATM 2309 O  O   . HOH   I 5 .   ? 27.961 11.989  27.459 1.00 24.38  ? 407 HOH   A O   1 
HETATM 2310 O  O   . HOH   I 5 .   ? 29.904 6.363   29.919 1.00 33.42  ? 408 HOH   A O   1 
HETATM 2311 O  O   . HOH   I 5 .   ? 15.825 12.099  30.751 1.00 38.16  ? 409 HOH   A O   1 
HETATM 2312 O  O   . HOH   I 5 .   ? 18.317 -3.754  14.715 1.00 35.49  ? 410 HOH   A O   1 
HETATM 2313 O  O   . HOH   I 5 .   ? 3.379  2.398   19.020 1.00 32.44  ? 411 HOH   A O   1 
HETATM 2314 O  O   . HOH   I 5 .   ? 30.037 -2.016  3.503  1.00 43.17  ? 412 HOH   A O   1 
HETATM 2315 O  O   . HOH   I 5 .   ? 12.197 18.466  26.463 1.00 25.63  ? 413 HOH   A O   1 
HETATM 2316 O  O   . HOH   I 5 .   ? 28.770 22.098  22.152 1.00 33.11  ? 414 HOH   A O   1 
HETATM 2317 O  O   . HOH   I 5 .   ? 15.179 23.203  16.980 1.00 22.66  ? 415 HOH   A O   1 
HETATM 2318 O  O   . HOH   I 5 .   ? 32.062 22.353  11.396 1.00 33.26  ? 416 HOH   A O   1 
HETATM 2319 O  O   . HOH   I 5 .   ? 14.477 -4.039  16.160 1.00 34.18  ? 417 HOH   A O   1 
HETATM 2320 O  O   . HOH   I 5 .   ? 17.633 22.295  15.774 1.00 35.12  ? 418 HOH   A O   1 
HETATM 2321 O  O   . HOH   I 5 .   ? 23.074 -11.545 30.615 1.00 52.41  ? 419 HOH   A O   1 
HETATM 2322 O  O   . HOH   I 5 .   ? 13.198 8.513   11.128 1.00 20.62  ? 420 HOH   A O   1 
HETATM 2323 O  O   . HOH   I 5 .   ? 33.047 -2.847  15.219 1.00 25.97  ? 421 HOH   A O   1 
HETATM 2324 O  O   . HOH   I 5 .   ? 32.897 12.205  27.663 1.00 39.30  ? 422 HOH   A O   1 
HETATM 2325 O  O   . HOH   I 5 .   ? 11.099 2.131   12.471 1.00 28.51  ? 423 HOH   A O   1 
HETATM 2326 O  O   . HOH   I 5 .   ? 3.891  14.712  10.398 1.00 28.29  ? 424 HOH   A O   1 
HETATM 2327 O  O   . HOH   I 5 .   ? 17.012 18.934  4.665  1.00 61.39  ? 425 HOH   A O   1 
HETATM 2328 O  O   . HOH   I 5 .   ? 32.381 5.715   4.932  1.00 49.54  ? 426 HOH   A O   1 
HETATM 2329 O  O   . HOH   I 5 .   ? 31.757 14.682  12.766 1.00 36.58  ? 427 HOH   A O   1 
HETATM 2330 O  O   . HOH   I 5 .   ? 31.083 9.949   13.828 1.00 45.64  ? 428 HOH   A O   1 
HETATM 2331 O  O   . HOH   I 5 .   ? 20.595 13.593  6.501  1.00 42.75  ? 429 HOH   A O   1 
HETATM 2332 O  O   . HOH   I 5 .   ? 32.099 -7.011  17.866 1.00 38.21  ? 430 HOH   A O   1 
HETATM 2333 O  O   . HOH   I 5 .   ? 6.597  16.118  8.832  1.00 36.17  ? 431 HOH   A O   1 
HETATM 2334 O  O   . HOH   I 5 .   ? 0.783  17.466  23.275 1.00 57.60  ? 432 HOH   A O   1 
HETATM 2335 O  O   . HOH   I 5 .   ? 10.611 6.792   11.586 1.00 40.16  ? 433 HOH   A O   1 
HETATM 2336 O  O   . HOH   I 5 .   ? 12.121 -2.674  15.847 1.00 44.01  ? 434 HOH   A O   1 
HETATM 2337 O  O   . HOH   I 5 .   ? 2.320  14.088  25.200 1.00 52.68  ? 435 HOH   A O   1 
HETATM 2338 O  O   . HOH   I 5 .   ? 16.183 -5.277  12.580 1.00 39.01  ? 436 HOH   A O   1 
HETATM 2339 O  O   . HOH   I 5 .   ? 19.794 23.786  23.068 1.00 69.93  ? 437 HOH   A O   1 
HETATM 2340 O  O   . HOH   I 5 .   ? 15.696 8.361   34.150 1.00 37.92  ? 438 HOH   A O   1 
HETATM 2341 O  O   . HOH   I 5 .   ? 19.573 -9.884  20.454 1.00 33.71  ? 439 HOH   A O   1 
HETATM 2342 O  O   . HOH   I 5 .   ? 18.085 10.899  6.644  1.00 34.77  ? 440 HOH   A O   1 
HETATM 2343 O  O   . HOH   I 5 .   ? 8.037  -2.446  17.368 1.00 20.83  ? 441 HOH   A O   1 
HETATM 2344 O  O   . HOH   I 5 .   ? 26.190 22.131  5.995  1.00 52.25  ? 442 HOH   A O   1 
HETATM 2345 O  O   . HOH   I 5 .   ? 31.173 11.973  15.131 1.00 55.87  ? 443 HOH   A O   1 
HETATM 2346 O  O   . HOH   I 5 .   ? 6.648  19.024  26.445 1.00 44.28  ? 444 HOH   A O   1 
HETATM 2347 O  O   . HOH   I 5 .   ? 24.633 -5.533  32.995 1.00 43.43  ? 445 HOH   A O   1 
HETATM 2348 O  O   . HOH   I 5 .   ? 8.881  17.865  8.711  1.00 60.12  ? 446 HOH   A O   1 
HETATM 2349 O  O   . HOH   I 5 .   ? 32.920 0.897   6.107  1.00 36.27  ? 447 HOH   A O   1 
HETATM 2350 O  O   . HOH   I 5 .   ? 2.401  21.051  12.335 1.00 45.46  ? 448 HOH   A O   1 
HETATM 2351 O  O   . HOH   I 5 .   ? 23.278 22.852  18.808 1.00 37.52  ? 449 HOH   A O   1 
HETATM 2352 O  O   . HOH   I 5 .   ? 30.791 -2.886  5.869  1.00 39.72  ? 450 HOH   A O   1 
HETATM 2353 O  O   . HOH   I 5 .   ? 13.863 21.654  14.792 1.00 26.25  ? 451 HOH   A O   1 
HETATM 2354 O  O   . HOH   I 5 .   ? 2.044  21.409  8.624  1.00 56.19  ? 452 HOH   A O   1 
HETATM 2355 O  O   . HOH   I 5 .   ? 6.987  -0.775  28.362 1.00 60.78  ? 453 HOH   A O   1 
HETATM 2356 O  O   . HOH   I 5 .   ? 28.146 1.815   29.328 1.00 31.92  ? 454 HOH   A O   1 
HETATM 2357 O  O   . HOH   I 5 .   ? 33.617 -2.180  9.080  1.00 30.47  ? 455 HOH   A O   1 
HETATM 2358 O  O   . HOH   I 5 .   ? -4.967 5.964   15.343 1.00 53.49  ? 456 HOH   A O   1 
HETATM 2359 O  O   . HOH   I 5 .   ? 20.446 -6.767  -0.646 1.00 48.03  ? 457 HOH   A O   1 
HETATM 2360 O  O   . HOH   I 5 .   ? 3.161  10.940  27.570 1.00 47.57  ? 458 HOH   A O   1 
HETATM 2361 O  O   . HOH   I 5 .   ? 31.290 -3.891  9.634  1.00 30.93  ? 459 HOH   A O   1 
HETATM 2362 O  O   . HOH   I 5 .   ? 11.566 -4.352  29.834 1.00 52.63  ? 460 HOH   A O   1 
HETATM 2363 O  O   . HOH   I 5 .   ? 25.049 14.566  6.063  1.00 49.13  ? 461 HOH   A O   1 
HETATM 2364 O  O   . HOH   I 5 .   ? 28.527 4.244   30.452 1.00 43.04  ? 462 HOH   A O   1 
HETATM 2365 O  O   . HOH   I 5 .   ? 2.823  4.029   17.049 1.00 37.59  ? 463 HOH   A O   1 
HETATM 2366 O  O   . HOH   I 5 .   ? 33.539 10.822  14.523 1.00 54.97  ? 464 HOH   A O   1 
HETATM 2367 O  O   . HOH   J 5 .   ? 5.893  -28.202 7.944  1.00 272.55 ? 301 HOH   C O   1 
HETATM 2368 O  O   . HOH   J 5 .   ? 20.227 -8.465  7.827  1.00 26.75  ? 302 HOH   C O   1 
HETATM 2369 O  O   . HOH   J 5 .   ? 10.525 -28.820 1.953  1.00 131.55 ? 303 HOH   C O   1 
HETATM 2370 O  O   . HOH   J 5 .   ? 12.835 -14.353 4.967  1.00 43.41  ? 304 HOH   C O   1 
HETATM 2371 O  O   . HOH   J 5 .   ? 13.351 -24.596 31.009 1.00 39.81  ? 305 HOH   C O   1 
HETATM 2372 O  O   . HOH   J 5 .   ? 18.154 -8.622  22.867 1.00 107.34 ? 306 HOH   C O   1 
HETATM 2373 O  O   . HOH   J 5 .   ? 24.875 -37.363 10.625 1.00 46.25  ? 307 HOH   C O   1 
HETATM 2374 O  O   . HOH   J 5 .   ? 35.553 -15.364 15.879 1.00 35.80  ? 308 HOH   C O   1 
HETATM 2375 O  O   . HOH   J 5 .   ? 2.655  -23.064 10.399 1.00 29.65  ? 309 HOH   C O   1 
HETATM 2376 O  O   . HOH   J 5 .   ? 30.888 -10.646 10.547 1.00 33.88  ? 310 HOH   C O   1 
HETATM 2377 O  O   . HOH   J 5 .   ? 17.578 -10.037 18.325 1.00 39.37  ? 311 HOH   C O   1 
HETATM 2378 O  O   . HOH   J 5 .   ? 10.244 -22.920 4.776  1.00 20.99  ? 312 HOH   C O   1 
HETATM 2379 O  O   . HOH   J 5 .   ? 26.592 -22.897 -0.124 1.00 39.75  ? 313 HOH   C O   1 
HETATM 2380 O  O   . HOH   J 5 .   ? 11.836 -20.469 0.726  1.00 40.57  ? 314 HOH   C O   1 
HETATM 2381 O  O   . HOH   J 5 .   ? 23.670 -9.264  7.913  1.00 23.14  ? 315 HOH   C O   1 
HETATM 2382 O  O   . HOH   J 5 .   ? 10.499 -27.290 33.667 1.00 31.57  ? 316 HOH   C O   1 
HETATM 2383 O  O   . HOH   J 5 .   ? 4.303  -36.019 21.492 1.00 26.53  ? 317 HOH   C O   1 
HETATM 2384 O  O   . HOH   J 5 .   ? 30.855 -21.233 13.132 1.00 35.99  ? 318 HOH   C O   1 
HETATM 2385 O  O   . HOH   J 5 .   ? 22.841 -36.051 12.233 1.00 40.94  ? 319 HOH   C O   1 
HETATM 2386 O  O   . HOH   J 5 .   ? 5.530  -17.942 25.262 1.00 42.38  ? 320 HOH   C O   1 
HETATM 2387 O  O   . HOH   J 5 .   ? 2.669  -31.645 3.811  1.00 39.47  ? 321 HOH   C O   1 
HETATM 2388 O  O   . HOH   J 5 .   ? 5.191  -25.379 24.661 1.00 38.82  ? 322 HOH   C O   1 
HETATM 2389 O  O   . HOH   J 5 .   ? 14.301 -19.741 0.868  1.00 37.30  ? 323 HOH   C O   1 
HETATM 2390 O  O   . HOH   J 5 .   ? 20.395 -22.368 18.744 1.00 15.50  ? 324 HOH   C O   1 
HETATM 2391 O  O   . HOH   J 5 .   ? 10.467 -12.741 20.500 1.00 19.37  ? 325 HOH   C O   1 
HETATM 2392 O  O   . HOH   J 5 .   ? 23.577 -31.248 15.169 1.00 26.19  ? 326 HOH   C O   1 
HETATM 2393 O  O   . HOH   J 5 .   ? 9.938  -26.200 3.594  1.00 18.75  ? 327 HOH   C O   1 
HETATM 2394 O  O   . HOH   J 5 .   ? 12.252 -29.373 33.504 1.00 23.63  ? 328 HOH   C O   1 
HETATM 2395 O  O   . HOH   J 5 .   ? 30.103 -25.375 17.831 1.00 37.67  ? 329 HOH   C O   1 
HETATM 2396 O  O   . HOH   J 5 .   ? 20.820 -28.522 -2.365 1.00 45.73  ? 330 HOH   C O   1 
HETATM 2397 O  O   . HOH   J 5 .   ? 22.135 -32.542 3.797  1.00 27.13  ? 331 HOH   C O   1 
HETATM 2398 O  O   . HOH   J 5 .   ? 17.433 -37.856 3.106  1.00 37.80  ? 332 HOH   C O   1 
HETATM 2399 O  O   . HOH   J 5 .   ? 17.332 -17.466 26.151 1.00 51.24  ? 333 HOH   C O   1 
HETATM 2400 O  O   . HOH   J 5 .   ? 6.865  -36.970 29.112 1.00 33.37  ? 334 HOH   C O   1 
HETATM 2401 O  O   . HOH   J 5 .   ? 16.504 -14.143 4.096  1.00 42.25  ? 335 HOH   C O   1 
HETATM 2402 O  O   . HOH   J 5 .   ? 11.314 -19.593 11.496 1.00 14.22  ? 336 HOH   C O   1 
HETATM 2403 O  O   . HOH   J 5 .   ? 23.590 -12.851 19.142 1.00 36.28  ? 337 HOH   C O   1 
HETATM 2404 O  O   . HOH   J 5 .   ? 29.366 -27.930 10.025 1.00 25.31  ? 338 HOH   C O   1 
HETATM 2405 O  O   . HOH   J 5 .   ? 0.846  -31.591 16.993 1.00 14.84  ? 339 HOH   C O   1 
HETATM 2406 O  O   . HOH   J 5 .   ? 21.329 -27.108 -4.538 1.00 54.21  ? 340 HOH   C O   1 
HETATM 2407 O  O   . HOH   J 5 .   ? 21.426 -36.542 9.968  1.00 27.27  ? 341 HOH   C O   1 
HETATM 2408 O  O   . HOH   J 5 .   ? 8.444  -28.419 3.005  1.00 19.64  ? 342 HOH   C O   1 
HETATM 2409 O  O   . HOH   J 5 .   ? 11.773 -35.927 -0.849 1.00 30.34  ? 343 HOH   C O   1 
HETATM 2410 O  O   . HOH   J 5 .   ? 0.717  -16.863 18.045 1.00 33.67  ? 344 HOH   C O   1 
HETATM 2411 O  O   . HOH   J 5 .   ? 27.638 -27.621 2.291  1.00 40.06  ? 345 HOH   C O   1 
HETATM 2412 O  O   . HOH   J 5 .   ? 27.450 -15.201 2.583  1.00 38.41  ? 346 HOH   C O   1 
HETATM 2413 O  O   . HOH   J 5 .   ? 7.202  -39.081 7.155  1.00 42.28  ? 347 HOH   C O   1 
HETATM 2414 O  O   . HOH   J 5 .   ? 4.904  -30.745 -1.744 1.00 39.82  ? 348 HOH   C O   1 
HETATM 2415 O  O   . HOH   J 5 .   ? 12.669 -28.694 22.540 1.00 237.44 ? 349 HOH   C O   1 
HETATM 2416 O  O   . HOH   J 5 .   ? 17.777 -10.012 9.432  1.00 20.21  ? 350 HOH   C O   1 
HETATM 2417 O  O   . HOH   J 5 .   ? -1.524 -31.622 4.897  1.00 43.04  ? 351 HOH   C O   1 
HETATM 2418 O  O   . HOH   J 5 .   ? 6.715  -16.714 22.729 1.00 31.85  ? 352 HOH   C O   1 
HETATM 2419 O  O   . HOH   J 5 .   ? 34.688 -11.005 10.845 1.00 45.88  ? 353 HOH   C O   1 
HETATM 2420 O  O   . HOH   J 5 .   ? 18.102 -11.908 5.531  1.00 33.28  ? 354 HOH   C O   1 
HETATM 2421 O  O   . HOH   J 5 .   ? 15.334 -28.853 23.179 1.00 15.35  ? 355 HOH   C O   1 
HETATM 2422 O  O   . HOH   J 5 .   ? 15.876 -18.912 24.118 1.00 22.57  ? 356 HOH   C O   1 
HETATM 2423 O  O   . HOH   J 5 .   ? 3.751  -23.549 3.649  1.00 30.71  ? 357 HOH   C O   1 
HETATM 2424 O  O   . HOH   J 5 .   ? 8.580  -11.530 18.464 1.00 20.20  ? 358 HOH   C O   1 
HETATM 2425 O  O   . HOH   J 5 .   ? 30.389 -20.208 19.149 1.00 31.10  ? 359 HOH   C O   1 
HETATM 2426 O  O   . HOH   J 5 .   ? -0.043 -18.908 21.721 1.00 44.83  ? 360 HOH   C O   1 
HETATM 2427 O  O   . HOH   J 5 .   ? 18.184 -28.807 23.013 1.00 22.11  ? 361 HOH   C O   1 
HETATM 2428 O  O   . HOH   J 5 .   ? 3.894  -27.053 27.925 1.00 48.05  ? 362 HOH   C O   1 
HETATM 2429 O  O   . HOH   J 5 .   ? 10.670 -13.845 5.619  1.00 49.43  ? 363 HOH   C O   1 
HETATM 2430 O  O   . HOH   J 5 .   ? 11.003 -36.325 31.478 1.00 32.90  ? 364 HOH   C O   1 
HETATM 2431 O  O   . HOH   J 5 .   ? 21.967 -12.237 17.279 1.00 26.07  ? 365 HOH   C O   1 
HETATM 2432 O  O   . HOH   J 5 .   ? 7.199  -27.552 32.930 1.00 52.69  ? 366 HOH   C O   1 
HETATM 2433 O  O   . HOH   J 5 .   ? 26.351 -32.864 5.977  1.00 43.59  ? 367 HOH   C O   1 
HETATM 2434 O  O   . HOH   J 5 .   ? 21.782 -14.869 23.529 1.00 37.43  ? 368 HOH   C O   1 
HETATM 2435 O  O   . HOH   J 5 .   ? 30.388 -20.426 16.678 1.00 34.56  ? 369 HOH   C O   1 
HETATM 2436 O  O   . HOH   J 5 .   ? 13.028 -20.697 9.423  1.00 12.52  ? 370 HOH   C O   1 
HETATM 2437 O  O   . HOH   J 5 .   ? 18.263 -12.395 16.955 1.00 16.64  ? 371 HOH   C O   1 
HETATM 2438 O  O   . HOH   J 5 .   ? 31.169 -10.749 16.483 1.00 25.09  ? 372 HOH   C O   1 
HETATM 2439 O  O   . HOH   J 5 .   ? 19.477 -22.259 25.561 1.00 29.54  ? 373 HOH   C O   1 
HETATM 2440 O  O   . HOH   J 5 .   ? 12.667 -6.213  22.166 1.00 26.81  ? 374 HOH   C O   1 
HETATM 2441 O  O   . HOH   J 5 .   ? 7.968  -34.990 0.545  1.00 19.71  ? 375 HOH   C O   1 
HETATM 2442 O  O   . HOH   J 5 .   ? 29.757 -26.469 2.936  1.00 40.18  ? 376 HOH   C O   1 
HETATM 2443 O  O   . HOH   J 5 .   ? 1.015  -33.859 20.398 1.00 30.09  ? 377 HOH   C O   1 
HETATM 2444 O  O   . HOH   J 5 .   ? 32.659 -16.813 6.772  1.00 49.64  ? 378 HOH   C O   1 
HETATM 2445 O  O   . HOH   J 5 .   ? 29.310 -34.319 5.357  1.00 59.24  ? 379 HOH   C O   1 
HETATM 2446 O  O   . HOH   J 5 .   ? 8.181  -39.543 24.267 1.00 34.59  ? 380 HOH   C O   1 
HETATM 2447 O  O   . HOH   J 5 .   ? 5.605  -29.231 7.389  1.00 16.46  ? 381 HOH   C O   1 
HETATM 2448 O  O   . HOH   J 5 .   ? -0.445 -15.906 14.138 1.00 33.52  ? 382 HOH   C O   1 
HETATM 2449 O  O   . HOH   J 5 .   ? 3.918  -8.853  22.790 1.00 37.03  ? 383 HOH   C O   1 
HETATM 2450 O  O   . HOH   J 5 .   ? 3.755  -36.164 6.789  1.00 25.04  ? 384 HOH   C O   1 
HETATM 2451 O  O   . HOH   J 5 .   ? 0.960  -29.549 24.851 1.00 41.16  ? 385 HOH   C O   1 
HETATM 2452 O  O   . HOH   J 5 .   ? 14.812 -35.750 17.055 1.00 21.09  ? 386 HOH   C O   1 
HETATM 2453 O  O   . HOH   J 5 .   ? 19.778 -31.575 27.049 1.00 32.10  ? 387 HOH   C O   1 
HETATM 2454 O  O   . HOH   J 5 .   ? 19.258 -27.103 25.636 1.00 45.94  ? 388 HOH   C O   1 
HETATM 2455 O  O   . HOH   J 5 .   ? 28.623 -33.245 12.411 1.00 34.35  ? 389 HOH   C O   1 
HETATM 2456 O  O   . HOH   J 5 .   ? 26.351 -27.387 19.565 1.00 42.94  ? 390 HOH   C O   1 
HETATM 2457 O  O   . HOH   J 5 .   ? 8.102  -14.431 23.017 1.00 29.22  ? 391 HOH   C O   1 
HETATM 2458 O  O   . HOH   J 5 .   ? 14.346 -22.420 30.070 1.00 33.29  ? 392 HOH   C O   1 
HETATM 2459 O  O   . HOH   J 5 .   ? 5.636  -32.668 24.433 1.00 21.04  ? 393 HOH   C O   1 
HETATM 2460 O  O   . HOH   J 5 .   ? 2.269  -37.709 14.530 1.00 43.99  ? 394 HOH   C O   1 
HETATM 2461 O  O   . HOH   J 5 .   ? 5.830  -33.130 29.463 1.00 51.73  ? 395 HOH   C O   1 
HETATM 2462 O  O   . HOH   J 5 .   ? 6.550  -18.339 5.848  1.00 22.58  ? 396 HOH   C O   1 
HETATM 2463 O  O   . HOH   J 5 .   ? 18.324 -18.408 1.670  1.00 41.41  ? 397 HOH   C O   1 
HETATM 2464 O  O   . HOH   J 5 .   ? 18.807 -31.549 19.337 1.00 21.49  ? 398 HOH   C O   1 
HETATM 2465 O  O   . HOH   J 5 .   ? 8.756  -38.638 9.524  1.00 24.37  ? 399 HOH   C O   1 
HETATM 2466 O  O   . HOH   J 5 .   ? 32.112 -16.688 20.640 1.00 26.84  ? 400 HOH   C O   1 
HETATM 2467 O  O   . HOH   J 5 .   ? 1.774  -17.693 6.126  1.00 35.64  ? 401 HOH   C O   1 
HETATM 2468 O  O   . HOH   J 5 .   ? 14.316 -16.625 3.719  1.00 26.70  ? 402 HOH   C O   1 
HETATM 2469 O  O   . HOH   J 5 .   ? 36.509 -32.030 9.147  1.00 46.26  ? 403 HOH   C O   1 
HETATM 2470 O  O   . HOH   J 5 .   ? 20.828 -12.041 21.158 1.00 32.95  ? 404 HOH   C O   1 
HETATM 2471 O  O   . HOH   J 5 .   ? 31.311 -22.089 4.941  1.00 37.40  ? 405 HOH   C O   1 
HETATM 2472 O  O   . HOH   J 5 .   ? 31.175 -28.645 11.849 1.00 31.85  ? 406 HOH   C O   1 
HETATM 2473 O  O   . HOH   J 5 .   ? 26.460 -33.094 13.794 1.00 31.10  ? 407 HOH   C O   1 
HETATM 2474 O  O   . HOH   J 5 .   ? 4.119  -24.342 26.598 1.00 37.91  ? 408 HOH   C O   1 
HETATM 2475 O  O   . HOH   J 5 .   ? 19.489 -7.440  15.198 1.00 21.98  ? 409 HOH   C O   1 
HETATM 2476 O  O   . HOH   J 5 .   ? 22.401 -12.193 5.884  1.00 24.82  ? 410 HOH   C O   1 
HETATM 2477 O  O   . HOH   J 5 .   ? 15.260 -35.644 1.739  1.00 22.64  ? 411 HOH   C O   1 
HETATM 2478 O  O   . HOH   J 5 .   ? 16.534 -38.666 10.532 1.00 42.92  ? 412 HOH   C O   1 
HETATM 2479 O  O   . HOH   J 5 .   ? 9.478  -10.116 11.090 1.00 43.59  ? 413 HOH   C O   1 
HETATM 2480 O  O   . HOH   J 5 .   ? -2.206 -30.293 8.444  1.00 21.14  ? 414 HOH   C O   1 
HETATM 2481 O  O   . HOH   J 5 .   ? 5.929  -8.563  11.450 1.00 39.11  ? 415 HOH   C O   1 
HETATM 2482 O  O   . HOH   J 5 .   ? 35.572 -29.095 5.001  1.00 49.97  ? 416 HOH   C O   1 
HETATM 2483 O  O   . HOH   J 5 .   ? 24.725 -23.939 20.030 1.00 36.94  ? 417 HOH   C O   1 
HETATM 2484 O  O   . HOH   J 5 .   ? 4.250  -33.554 22.215 1.00 38.15  ? 418 HOH   C O   1 
HETATM 2485 O  O   . HOH   J 5 .   ? 4.837  -38.370 7.124  1.00 59.75  ? 419 HOH   C O   1 
HETATM 2486 O  O   . HOH   J 5 .   ? 10.789 -15.202 3.378  1.00 40.29  ? 420 HOH   C O   1 
HETATM 2487 O  O   . HOH   J 5 .   ? 29.167 -14.872 22.702 1.00 35.51  ? 421 HOH   C O   1 
HETATM 2488 O  O   . HOH   J 5 .   ? 31.377 -12.455 8.829  1.00 41.87  ? 422 HOH   C O   1 
HETATM 2489 O  O   . HOH   J 5 .   ? 11.986 -39.046 12.973 1.00 30.70  ? 423 HOH   C O   1 
HETATM 2490 O  O   . HOH   J 5 .   ? 16.651 -7.859  14.579 1.00 35.36  ? 424 HOH   C O   1 
HETATM 2491 O  O   . HOH   J 5 .   ? 11.998 -9.824  12.517 1.00 28.57  ? 425 HOH   C O   1 
HETATM 2492 O  O   . HOH   J 5 .   ? 4.365  -20.631 19.550 1.00 36.24  ? 426 HOH   C O   1 
HETATM 2493 O  O   . HOH   J 5 .   ? 1.127  -34.533 17.641 1.00 22.99  ? 427 HOH   C O   1 
HETATM 2494 O  O   . HOH   J 5 .   ? 24.124 -28.976 19.077 1.00 28.33  ? 428 HOH   C O   1 
HETATM 2495 O  O   . HOH   J 5 .   ? 1.773  -33.570 17.999 1.00 26.97  ? 429 HOH   C O   1 
HETATM 2496 O  O   . HOH   J 5 .   ? 16.822 -8.522  16.755 1.00 40.17  ? 430 HOH   C O   1 
HETATM 2497 O  O   . HOH   J 5 .   ? -0.521 -35.878 16.537 1.00 36.42  ? 431 HOH   C O   1 
HETATM 2498 O  O   . HOH   J 5 .   ? 17.638 -38.832 24.389 1.00 40.26  ? 432 HOH   C O   1 
HETATM 2499 O  O   . HOH   J 5 .   ? 7.855  -5.395  14.596 1.00 39.42  ? 433 HOH   C O   1 
HETATM 2500 O  O   . HOH   J 5 .   ? 22.345 -22.478 20.832 1.00 22.12  ? 434 HOH   C O   1 
HETATM 2501 O  O   . HOH   J 5 .   ? 28.074 -9.566  18.719 1.00 48.94  ? 435 HOH   C O   1 
HETATM 2502 O  O   . HOH   J 5 .   ? 31.439 -26.444 -2.462 1.00 64.13  ? 436 HOH   C O   1 
HETATM 2503 O  O   . HOH   J 5 .   ? 6.959  -20.331 4.286  1.00 41.95  ? 437 HOH   C O   1 
HETATM 2504 O  O   . HOH   J 5 .   ? 4.592  -16.244 21.418 1.00 34.46  ? 438 HOH   C O   1 
HETATM 2505 O  O   . HOH   J 5 .   ? 6.937  -36.445 2.920  1.00 26.13  ? 439 HOH   C O   1 
HETATM 2506 O  O   . HOH   J 5 .   ? 32.858 -9.461  19.578 1.00 63.35  ? 440 HOH   C O   1 
HETATM 2507 O  O   . HOH   J 5 .   ? 4.089  -18.574 18.577 1.00 43.60  ? 441 HOH   C O   1 
HETATM 2508 O  O   . HOH   J 5 .   ? 20.520 -8.969  17.621 1.00 37.10  ? 442 HOH   C O   1 
HETATM 2509 O  O   . HOH   J 5 .   ? 30.711 -8.722  18.240 1.00 48.39  ? 443 HOH   C O   1 
HETATM 2510 O  O   . HOH   J 5 .   ? 12.365 -16.763 1.748  1.00 66.30  ? 444 HOH   C O   1 
HETATM 2511 O  O   . HOH   J 5 .   ? 13.606 -42.607 4.252  1.00 58.29  ? 445 HOH   C O   1 
HETATM 2512 O  O   . HOH   J 5 .   ? 16.798 -20.260 0.138  1.00 38.39  ? 446 HOH   C O   1 
HETATM 2513 O  O   . HOH   J 5 .   ? 5.059  -28.907 4.764  1.00 49.56  ? 447 HOH   C O   1 
HETATM 2514 O  O   . HOH   J 5 .   ? 18.318 -11.393 19.291 1.00 36.38  ? 448 HOH   C O   1 
HETATM 2515 O  O   . HOH   J 5 .   ? 2.439  -34.836 4.092  1.00 57.26  ? 449 HOH   C O   1 
HETATM 2516 O  O   . HOH   J 5 .   ? 30.607 -31.216 13.220 1.00 38.83  ? 450 HOH   C O   1 
HETATM 2517 O  O   . HOH   J 5 .   ? 17.373 -9.918  29.110 1.00 51.20  ? 451 HOH   C O   1 
HETATM 2518 O  O   . HOH   J 5 .   ? 29.104 -22.132 20.899 1.00 40.88  ? 452 HOH   C O   1 
HETATM 2519 O  O   . HOH   J 5 .   ? 17.269 -34.688 18.061 1.00 36.38  ? 453 HOH   C O   1 
HETATM 2520 O  O   . HOH   J 5 .   ? 8.637  -8.031  26.615 1.00 49.99  ? 454 HOH   C O   1 
HETATM 2521 O  O   . HOH   J 5 .   ? 24.447 -15.950 23.788 1.00 59.52  ? 455 HOH   C O   1 
HETATM 2522 O  O   . HOH   J 5 .   ? 32.134 -19.357 21.010 1.00 36.98  ? 456 HOH   C O   1 
HETATM 2523 O  O   . HOH   J 5 .   ? 16.128 -17.677 1.883  1.00 55.67  ? 457 HOH   C O   1 
HETATM 2524 O  O   . HOH   J 5 .   ? 8.679  -23.814 2.778  1.00 30.73  ? 458 HOH   C O   1 
HETATM 2525 O  O   . HOH   J 5 .   ? 32.781 -9.526  14.569 1.00 31.21  ? 459 HOH   C O   1 
HETATM 2526 O  O   . HOH   J 5 .   ? 2.442  -28.930 27.303 1.00 41.47  ? 460 HOH   C O   1 
HETATM 2527 O  O   . HOH   J 5 .   ? 34.517 -11.265 17.721 1.00 38.60  ? 461 HOH   C O   1 
HETATM 2528 O  O   . HOH   J 5 .   ? 26.707 -21.489 22.467 1.00 55.78  ? 462 HOH   C O   1 
HETATM 2529 O  O   . HOH   J 5 .   ? 32.935 -9.281  11.755 1.00 39.06  ? 463 HOH   C O   1 
HETATM 2530 O  O   . HOH   J 5 .   ? 9.478  -39.601 12.276 1.00 32.47  ? 464 HOH   C O   1 
HETATM 2531 O  O   . HOH   J 5 .   ? 31.978 -27.150 13.850 1.00 39.48  ? 465 HOH   C O   1 
HETATM 2532 O  O   . HOH   J 5 .   ? 31.814 -36.207 12.282 1.00 40.52  ? 466 HOH   C O   1 
HETATM 2533 O  O   . HOH   J 5 .   ? 19.405 -33.871 18.634 1.00 36.40  ? 467 HOH   C O   1 
HETATM 2534 O  O   . HOH   J 5 .   ? 5.296  -39.556 23.287 1.00 29.39  ? 468 HOH   C O   1 
HETATM 2535 O  O   . HOH   J 5 .   ? 29.621 -8.602  9.130  1.00 26.73  ? 469 HOH   C O   1 
HETATM 2536 O  O   . HOH   J 5 .   ? 1.963  -19.615 19.601 1.00 63.64  ? 470 HOH   C O   1 
HETATM 2537 O  O   . HOH   J 5 .   ? 20.669 -21.848 6.416  1.00 221.03 ? 471 HOH   C O   1 
HETATM 2538 O  O   . HOH   J 5 .   ? 26.382 -14.864 -0.255 1.00 64.61  ? 472 HOH   C O   1 
HETATM 2539 O  O   . HOH   J 5 .   ? 35.356 -9.484  8.548  1.00 63.08  ? 473 HOH   C O   1 
HETATM 2540 O  O   . HOH   J 5 .   ? 19.689 -23.204 8.079  1.00 294.73 ? 474 HOH   C O   1 
HETATM 2541 O  O   . HOH   J 5 .   ? 35.496 -10.239 15.583 1.00 33.65  ? 475 HOH   C 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   ? 0.2790 0.2550 0.2535 0.0164  -0.0260 0.0118  7   SER   A N   
2    C CA  . SER   A 1   ? 0.2682 0.2523 0.2628 0.0140  -0.0314 0.0085  7   SER   A CA  
3    C C   . SER   A 1   ? 0.2553 0.2473 0.2649 0.0087  -0.0301 0.0043  7   SER   A C   
4    O O   . SER   A 1   ? 0.2553 0.2465 0.2587 0.0078  -0.0283 0.0027  7   SER   A O   
5    C CB  . SER   A 1   ? 0.3162 0.2973 0.3089 0.0201  -0.0441 0.0052  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3577 0.3373 0.3449 0.0225  -0.0514 -0.0005 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2227 0.2210 0.2513 0.0056  -0.0295 0.0030  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2027 0.2059 0.2453 0.0017  -0.0262 -0.0001 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1880 0.1950 0.2438 -0.0009 -0.0197 0.0015  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1947 0.2016 0.2473 -0.0007 -0.0165 0.0047  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1593 0.1686 0.2302 -0.0028 -0.0168 -0.0009 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1705 0.1811 0.2515 -0.0040 -0.0091 0.0007  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1741 0.1827 0.2600 -0.0050 -0.0008 0.0003  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1807 0.1881 0.2689 -0.0058 -0.0020 -0.0023 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1833 0.1966 0.2827 -0.0039 -0.0127 -0.0009 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1448 0.1515 0.2310 -0.0042 0.0081  0.0027  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1595 0.1610 0.2488 -0.0033 0.0184  0.0036  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1551 0.1561 0.2652 -0.0041 0.0239  0.0033  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1594 0.1623 0.2726 -0.0035 0.0237  0.0042  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1655 0.1627 0.2364 0.0008  0.0249  0.0064  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1691 0.1684 0.2236 0.0015  0.0190  0.0057  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1992 0.1877 0.2679 0.0039  0.0363  0.0084  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1764 0.1740 0.2169 0.0061  0.0214  0.0059  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1658 0.1640 0.2925 -0.0055 0.0299  0.0018  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1832 0.1804 0.3346 -0.0065 0.0377  0.0012  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1931 0.1794 0.3418 -0.0038 0.0550  0.0054  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2182 0.1996 0.3697 -0.0043 0.0603  0.0052  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1720 0.1747 0.3515 -0.0102 0.0308  -0.0053 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1844 0.1955 0.3640 -0.0104 0.0136  -0.0093 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1911 0.2068 0.3834 -0.0100 0.0094  -0.0103 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2096 0.2221 0.3736 -0.0100 0.0025  -0.0113 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2058 0.2268 0.3946 -0.0084 -0.0058 -0.0129 11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2201 0.2370 0.3791 -0.0082 -0.0117 -0.0137 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2216 0.2424 0.3927 -0.0071 -0.0160 -0.0145 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2695 0.2921 0.4320 -0.0037 -0.0293 -0.0158 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1962 0.1769 0.3354 0.0001  0.0640  0.0094  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2177 0.1845 0.3468 0.0054  0.0815  0.0145  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2309 0.1935 0.3749 0.0067  0.0933  0.0162  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2340 0.2012 0.3752 0.0074  0.0882  0.0157  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2716 0.2327 0.3643 0.0124  0.0805  0.0174  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2778 0.2464 0.3603 0.0130  0.0698  0.0156  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3111 0.2555 0.3879 0.0207  0.0979  0.0228  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2448 0.1990 0.4091 0.0063  0.1094  0.0178  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2488 0.1981 0.4302 0.0075  0.1230  0.0195  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2415 0.2059 0.4506 0.0018  0.1108  0.0138  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2435 0.2192 0.4725 -0.0038 0.0975  0.0078  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2413 0.2057 0.4470 0.0044  0.1126  0.0151  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2232 0.2012 0.4517 0.0003  0.1000  0.0102  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1958 0.1809 0.4001 0.0011  0.0831  0.0097  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2017 0.1926 0.4127 0.0009  0.0772  0.0084  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2634 0.2378 0.5118 0.0017  0.1134  0.0113  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3637 0.3346 0.6485 -0.0011 0.1281  0.0099  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3892 0.3710 0.7073 -0.0067 0.1189  0.0030  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3876 0.3422 0.6660 0.0036  0.1513  0.0160  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1808 0.1658 0.3603 0.0018  0.0754  0.0103  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1791 0.1698 0.3378 0.0023  0.0616  0.0097  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1571 0.1551 0.3143 -0.0011 0.0475  0.0069  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1615 0.1575 0.3205 -0.0024 0.0492  0.0062  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1987 0.1810 0.3251 0.0081  0.0664  0.0127  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2180 0.1908 0.3374 0.0138  0.0791  0.0151  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2327 0.2089 0.3623 0.0134  0.0781  0.0142  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2632 0.2222 0.3630 0.0207  0.0922  0.0185  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2550 0.2216 0.3760 0.0194  0.0898  0.0160  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2825 0.2305 0.3715 0.0278  0.1041  0.0208  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2921 0.2442 0.3928 0.0267  0.1031  0.0193  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3484 0.2892 0.4366 0.0342  0.1145  0.0209  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1431 0.1477 0.2939 -0.0019 0.0349  0.0057  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1419 0.1511 0.2848 -0.0035 0.0225  0.0040  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1483 0.1566 0.2672 -0.0017 0.0200  0.0061  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1568 0.1658 0.2749 -0.0007 0.0198  0.0069  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1354 0.1511 0.2948 -0.0047 0.0109  0.0008  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1772 0.1950 0.3219 -0.0040 -0.0016 0.0002  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1772 0.1992 0.3357 -0.0027 -0.0139 -0.0035 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2157 0.2363 0.3566 0.0002  -0.0220 -0.0011 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2480 0.2666 0.3747 0.0026  -0.0309 -0.0019 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2556 0.2744 0.3821 0.0018  -0.0339 -0.0056 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2588 0.2735 0.3692 0.0060  -0.0351 0.0015  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1469 0.1538 0.2492 -0.0013 0.0188  0.0064  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1486 0.1556 0.2335 0.0001  0.0164  0.0068  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1484 0.1585 0.2292 -0.0017 0.0077  0.0065  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1438 0.1538 0.2221 -0.0026 0.0051  0.0057  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1606 0.1633 0.2300 0.0032  0.0215  0.0068  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1623 0.1665 0.2196 0.0050  0.0182  0.0051  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1788 0.1743 0.2480 0.0069  0.0322  0.0082  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1253 0.1366 0.2038 -0.0018 0.0042  0.0073  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1332 0.1444 0.2049 -0.0021 -0.0018 0.0082  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1206 0.1312 0.1847 -0.0021 0.0004  0.0088  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1383 0.1495 0.2052 -0.0017 0.0038  0.0075  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1584 0.1695 0.2375 -0.0011 -0.0079 0.0091  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2069 0.2198 0.2969 -0.0011 -0.0122 0.0064  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1626 0.1741 0.2504 -0.0007 -0.0056 0.0101  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1183 0.1268 0.1742 -0.0020 -0.0014 0.0103  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1233 0.1304 0.1778 -0.0024 0.0020  0.0109  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1453 0.1506 0.2068 -0.0019 0.0022  0.0128  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1458 0.1483 0.2067 -0.0001 -0.0018 0.0155  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1359 0.1383 0.1802 -0.0018 0.0026  0.0135  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1513 0.1551 0.1890 -0.0022 0.0029  0.0116  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1682 0.1711 0.2001 -0.0014 -0.0010 0.0116  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1521 0.1586 0.1926 -0.0033 0.0068  0.0089  19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1209 0.1274 0.1893 -0.0027 0.0059  0.0108  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1217 0.1262 0.1979 -0.0022 0.0067  0.0124  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1509 0.1483 0.2219 -0.0007 0.0071  0.0178  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1634 0.1579 0.2361 0.0016  0.0044  0.0207  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1275 0.1338 0.2117 -0.0032 0.0104  0.0079  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1341 0.1385 0.2275 -0.0027 0.0115  0.0087  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1475 0.1531 0.2494 -0.0036 0.0145  0.0029  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1489 0.1527 0.2602 -0.0031 0.0161  0.0021  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1566 0.1553 0.2745 -0.0038 0.0194  0.0053  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1661 0.1597 0.2797 -0.0041 0.0220  0.0108  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1599 0.1571 0.2873 -0.0033 0.0209  0.0038  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1475 0.1410 0.2109 -0.0008 0.0105  0.0194  21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1748 0.1579 0.2290 0.0023  0.0133  0.0256  21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1932 0.1721 0.2337 0.0072  0.0058  0.0287  21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2433 0.2118 0.2727 0.0123  0.0062  0.0341  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1799 0.1584 0.2316 0.0011  0.0220  0.0267  21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1905 0.1696 0.2311 0.0014  0.0209  0.0261  21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.1799 0.1683 0.2265 -0.0018 0.0194  0.0202  21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2099 0.1802 0.2329 0.0054  0.0217  0.0306  21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2002 0.1861 0.2348 -0.0005 0.0192  0.0213  21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2122 0.1871 0.2321 0.0037  0.0208  0.0272  21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1801 0.1656 0.2211 0.0065  -0.0011 0.0251  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1871 0.1701 0.2197 0.0110  -0.0102 0.0254  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1882 0.1775 0.2356 0.0112  -0.0171 0.0224  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2091 0.1988 0.2560 0.0146  -0.0261 0.0203  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1856 0.1707 0.2108 0.0101  -0.0125 0.0225  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2116 0.1901 0.2226 0.0108  -0.0058 0.0253  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2186 0.1993 0.2231 0.0101  -0.0086 0.0220  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2253 0.1901 0.2188 0.0177  -0.0046 0.0312  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1839 0.1781 0.2459 0.0079  -0.0127 0.0214  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1721 0.1716 0.2498 0.0080  -0.0168 0.0187  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1912 0.1865 0.2687 0.0138  -0.0245 0.0206  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2053 0.1926 0.2723 0.0174  -0.0232 0.0252  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1777 0.1804 0.2669 0.0050  -0.0098 0.0179  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1934 0.1938 0.2839 0.0152  -0.0321 0.0165  24  THR   A N   
135  C CA  . THR   A 18  ? 0.2118 0.2096 0.3042 0.0222  -0.0425 0.0163  24  THR   A CA  
136  C C   . THR   A 18  ? 0.2264 0.2267 0.3356 0.0222  -0.0404 0.0169  24  THR   A C   
137  O O   . THR   A 18  ? 0.2165 0.2209 0.3367 0.0167  -0.0313 0.0166  24  THR   A O   
138  C CB  . THR   A 18  ? 0.2301 0.2336 0.3336 0.0238  -0.0534 0.0092  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2134 0.2261 0.3428 0.0181  -0.0489 0.0052  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2521 0.2536 0.3407 0.0236  -0.0557 0.0075  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2401 0.2380 0.3523 0.0293  -0.0500 0.0168  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2465 0.2473 0.3775 0.0298  -0.0488 0.0166  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.1993 0.2110 0.3574 0.0242  -0.0458 0.0108  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2127 0.2265 0.3825 0.0207  -0.0368 0.0116  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3037 0.3010 0.4350 0.0398  -0.0621 0.0160  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4482 0.4313 0.5510 0.0475  -0.0631 0.0231  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.5084 0.4837 0.6023 0.0456  -0.0510 0.0303  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.5014 0.4754 0.5831 0.0578  -0.0741 0.0239  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.5356 0.4968 0.6042 0.0542  -0.0528 0.0362  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.5402 0.4993 0.5981 0.0625  -0.0667 0.0330  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2056 0.2228 0.3732 0.0235  -0.0521 0.0049  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.1815 0.2070 0.3762 0.0184  -0.0467 0.0000  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1755 0.2002 0.3647 0.0119  -0.0316 0.0028  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1701 0.1973 0.3755 0.0091  -0.0222 0.0020  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2240 0.2547 0.4321 0.0188  -0.0557 -0.0073 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3125 0.3474 0.5402 0.0251  -0.0698 -0.0133 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3151 0.3526 0.5605 0.0265  -0.0687 -0.0134 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3433 0.3783 0.5666 0.0301  -0.0845 -0.0189 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1578 0.1782 0.3232 0.0103  -0.0290 0.0058  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1583 0.1776 0.3167 0.0059  -0.0167 0.0076  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1535 0.1709 0.3137 0.0059  -0.0096 0.0098  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1501 0.1677 0.3159 0.0042  -0.0002 0.0091  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1571 0.1726 0.2921 0.0051  -0.0163 0.0098  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.1760 0.1928 0.3080 0.0042  -0.0199 0.0072  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.1883 0.2083 0.3347 0.0022  -0.0169 0.0041  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2015 0.2150 0.3170 0.0060  -0.0252 0.0083  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1489 0.1627 0.3022 0.0086  -0.0133 0.0128  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1548 0.1663 0.3105 0.0085  -0.0070 0.0143  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1778 0.1925 0.3550 0.0095  -0.0051 0.0124  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1782 0.1918 0.3590 0.0085  0.0034  0.0120  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1532 0.1585 0.2979 0.0112  -0.0097 0.0184  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1618 0.1633 0.2901 0.0090  -0.0054 0.0199  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.1856 0.1833 0.2989 0.0101  -0.0083 0.0222  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1511 0.1517 0.2782 0.0061  0.0023  0.0184  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.1749 0.1701 0.2805 0.0073  -0.0017 0.0225  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1746 0.1725 0.2894 0.0048  0.0038  0.0194  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1705 0.1725 0.3058 0.0051  0.0078  0.0153  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1866 0.1841 0.3012 0.0023  0.0095  0.0166  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.1788 0.1797 0.3103 0.0034  0.0124  0.0123  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1884 0.1879 0.3114 0.0018  0.0126  0.0124  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1754 0.1941 0.3679 0.0117  -0.0128 0.0103  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1874 0.2101 0.4054 0.0125  -0.0105 0.0078  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.1948 0.2195 0.4245 0.0090  0.0009  0.0054  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.1993 0.2251 0.4478 0.0092  0.0081  0.0042  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1930 0.2202 0.4274 0.0165  -0.0233 0.0044  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1710 0.1951 0.3901 0.0065  0.0033  0.0051  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1685 0.1912 0.3937 0.0044  0.0155  0.0041  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1581 0.1749 0.3569 0.0040  0.0228  0.0065  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1522 0.1662 0.3450 0.0034  0.0296  0.0065  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1732 0.1997 0.4114 0.0027  0.0121  0.0008  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2106 0.2439 0.4798 0.0037  0.0046  -0.0039 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2306 0.2651 0.5241 0.0033  0.0133  -0.0055 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2098 0.2468 0.4785 0.0060  -0.0114 -0.0066 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1487 0.1630 0.3332 0.0051  0.0214  0.0079  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1578 0.1678 0.3203 0.0054  0.0253  0.0081  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1781 0.1825 0.3353 0.0078  0.0372  0.0074  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2007 0.2025 0.3673 0.0098  0.0444  0.0072  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1577 0.1664 0.3142 0.0060  0.0224  0.0083  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1839 0.1894 0.3228 0.0066  0.0245  0.0063  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1977 0.2046 0.3245 0.0049  0.0203  0.0064  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1870 0.1910 0.3269 0.0068  0.0230  0.0054  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1803 0.1814 0.3202 0.0088  0.0396  0.0070  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1992 0.1922 0.3261 0.0136  0.0500  0.0066  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2177 0.2083 0.3239 0.0167  0.0463  0.0033  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2428 0.2275 0.3402 0.0217  0.0509  0.0009  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2182 0.2078 0.3409 0.0140  0.0556  0.0083  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2391 0.2175 0.3400 0.0212  0.0655  0.0085  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2187 0.2099 0.3668 0.0113  0.0610  0.0097  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1886 0.1840 0.2887 0.0140  0.0377  0.0023  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1920 0.1868 0.2783 0.0163  0.0334  -0.0023 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1597 0.1609 0.2487 0.0114  0.0253  -0.0021 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1617 0.1653 0.2532 0.0084  0.0233  0.0012  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2174 0.2060 0.2841 0.0225  0.0369  -0.0041 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2291 0.2187 0.2834 0.0255  0.0300  -0.0102 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2462 0.2336 0.2940 0.0306  0.0273  -0.0172 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2186 0.2123 0.2681 0.0239  0.0245  -0.0112 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2521 0.2432 0.2948 0.0318  0.0195  -0.0231 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2305 0.2252 0.2736 0.0279  0.0184  -0.0191 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2077 0.2045 0.2595 0.0197  0.0237  -0.0070 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2304 0.2291 0.2697 0.0280  0.0126  -0.0225 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2291 0.2289 0.2745 0.0198  0.0186  -0.0096 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2250 0.2262 0.2657 0.0235  0.0133  -0.0171 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1575 0.1602 0.2471 0.0109  0.0215  -0.0059 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1598 0.1663 0.2513 0.0071  0.0166  -0.0057 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1545 0.1620 0.2448 0.0084  0.0142  -0.0129 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1662 0.1718 0.2577 0.0115  0.0147  -0.0180 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1727 0.1800 0.2747 0.0034  0.0153  -0.0009 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1606 0.1661 0.2725 0.0039  0.0171  -0.0015 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.1961 0.2009 0.3125 0.0034  0.0171  -0.0065 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2344 0.2373 0.3558 0.0052  0.0189  -0.0100 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.1833 0.1891 0.3002 0.0012  0.0160  -0.0073 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1514 0.1619 0.2411 0.0063  0.0115  -0.0140 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1434 0.1563 0.2377 0.0073  0.0087  -0.0223 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1448 0.1600 0.2474 0.0023  0.0093  -0.0203 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1402 0.1567 0.2365 0.0015  0.0087  -0.0180 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1652 0.1782 0.2464 0.0134  0.0054  -0.0283 35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2591 0.2755 0.3466 0.0161  -0.0001 -0.0395 35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2693 0.2893 0.3737 0.0111  0.0000  -0.0418 35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2672 0.2819 0.3426 0.0239  -0.0044 -0.0463 35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1390 0.1531 0.2556 -0.0007 0.0118  -0.0209 36  SER   A N   
241  C CA  A SER   A 30  ? 0.1497 0.1630 0.2740 -0.0046 0.0154  -0.0180 36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1486 0.1619 0.2727 -0.0046 0.0154  -0.0179 36  SER   A CA  
243  C C   . SER   A 30  ? 0.1541 0.1723 0.2835 -0.0047 0.0136  -0.0254 36  SER   A C   
244  O O   . SER   A 30  ? 0.1722 0.1900 0.3013 -0.0069 0.0167  -0.0219 36  SER   A O   
245  C CB  A SER   A 30  ? 0.1825 0.1918 0.3220 -0.0069 0.0202  -0.0176 36  SER   A CB  
246  C CB  B SER   A 30  ? 0.1799 0.1889 0.3188 -0.0071 0.0206  -0.0169 36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2147 0.2208 0.3627 -0.0100 0.0266  -0.0149 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2125 0.2246 0.3666 -0.0068 0.0192  -0.0277 36  SER   A OG  
249  N N   . SER   A 31  ? 0.1594 0.1819 0.2935 -0.0013 0.0082  -0.0364 37  SER   A N   
250  C CA  . SER   A 31  ? 0.1630 0.1913 0.3047 -0.0003 0.0047  -0.0451 37  SER   A CA  
251  C C   . SER   A 31  ? 0.1640 0.1934 0.2886 0.0018  0.0025  -0.0415 37  SER   A C   
252  O O   . SER   A 31  ? 0.1846 0.2185 0.3155 0.0019  0.0008  -0.0464 37  SER   A O   
253  C CB  . SER   A 31  ? 0.2039 0.2361 0.3524 0.0049  -0.0032 -0.0591 37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2806 0.3110 0.4069 0.0123  -0.0088 -0.0602 37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1430 0.1688 0.2489 0.0036  0.0026  -0.0340 38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1344 0.1602 0.2253 0.0054  0.0015  -0.0304 38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1408 0.1636 0.2270 0.0010  0.0060  -0.0201 38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1385 0.1611 0.2143 0.0016  0.0054  -0.0173 38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1435 0.1659 0.2174 0.0115  -0.0006 -0.0301 38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1564 0.1795 0.2273 0.0189  -0.0064 -0.0407 38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1819 0.1981 0.2323 0.0266  -0.0059 -0.0392 38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1756 0.1893 0.2120 0.0287  -0.0044 -0.0344 38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1868 0.1933 0.2035 0.0374  -0.0038 -0.0343 38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2123 0.2133 0.2183 0.0460  -0.0056 -0.0397 38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1955 0.1991 0.2017 0.0387  -0.0014 -0.0296 38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1286 0.1483 0.2206 -0.0024 0.0097  -0.0149 39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1181 0.1335 0.2027 -0.0043 0.0119  -0.0060 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1273 0.1421 0.2014 -0.0024 0.0091  -0.0030 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1427 0.1560 0.2095 -0.0030 0.0084  0.0013  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1356 0.1499 0.2172 -0.0058 0.0144  -0.0038 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1385 0.1466 0.2098 -0.0059 0.0156  0.0043  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1459 0.1494 0.2179 -0.0056 0.0165  0.0086  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1451 0.1523 0.2068 -0.0055 0.0150  0.0060  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1147 0.1299 0.1889 0.0000  0.0084  -0.0054 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1177 0.1312 0.1861 0.0014  0.0086  -0.0023 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1173 0.1291 0.1928 0.0013  0.0098  0.0001  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1305 0.1419 0.2115 0.0020  0.0108  -0.0024 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1302 0.1428 0.1900 0.0059  0.0093  -0.0058 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1302 0.1440 0.1818 0.0072  0.0077  -0.0076 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1589 0.1689 0.1987 0.0139  0.0088  -0.0103 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1391 0.1523 0.1884 0.0043  0.0080  -0.0026 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1119 0.1229 0.1888 0.0009  0.0098  0.0037  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1262 0.1365 0.2125 0.0013  0.0113  0.0052  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1305 0.1400 0.2188 0.0019  0.0137  0.0061  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1354 0.1457 0.2214 0.0007  0.0115  0.0069  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1237 0.1339 0.2167 -0.0001 0.0075  0.0083  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1378 0.1480 0.2434 0.0008  0.0079  0.0094  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1485 0.1566 0.2573 0.0011  0.0056  0.0118  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1482 0.1602 0.2617 0.0007  0.0050  0.0101  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1327 0.1399 0.2263 0.0039  0.0194  0.0059  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1370 0.1421 0.2373 0.0044  0.0249  0.0070  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1459 0.1524 0.2650 0.0035  0.0261  0.0077  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1594 0.1649 0.2806 0.0050  0.0282  0.0073  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1569 0.1552 0.2452 0.0091  0.0337  0.0066  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1697 0.1635 0.2672 0.0096  0.0429  0.0087  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1661 0.1635 0.2366 0.0110  0.0309  0.0050  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1481 0.1574 0.2823 0.0015  0.0241  0.0076  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1427 0.1547 0.2995 0.0010  0.0241  0.0070  43  SER   A CA  
299  C C   . SER   A 37  ? 0.1619 0.1719 0.3349 0.0005  0.0334  0.0063  43  SER   A C   
300  O O   . SER   A 37  ? 0.1611 0.1681 0.3279 0.0002  0.0373  0.0065  43  SER   A O   
301  C CB  . SER   A 37  ? 0.1633 0.1807 0.3278 0.0001  0.0113  0.0059  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1751 0.1942 0.3392 -0.0011 0.0056  0.0041  43  SER   A OG  
303  N N   . SER   A 38  ? 0.1604 0.1716 0.3562 0.0006  0.0380  0.0054  44  SER   A N   
304  C CA  . SER   A 38  ? 0.1811 0.1898 0.3978 -0.0001 0.0493  0.0046  44  SER   A CA  
305  C C   . SER   A 38  ? 0.1965 0.2129 0.4392 -0.0032 0.0402  -0.0003 44  SER   A C   
306  O O   . SER   A 38  ? 0.1992 0.2226 0.4478 -0.0032 0.0259  -0.0031 44  SER   A O   
307  C CB  . SER   A 38  ? 0.2111 0.2165 0.4419 0.0018  0.0609  0.0055  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2398 0.2529 0.4865 0.0013  0.0509  0.0032  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2044 0.2185 0.4630 -0.0050 0.0487  -0.0018 45  THR   A N   
310  C CA  . THR   A 39  ? 0.2176 0.2390 0.5044 -0.0079 0.0401  -0.0085 45  THR   A CA  
311  C C   . THR   A 39  ? 0.2556 0.2763 0.5808 -0.0096 0.0538  -0.0113 45  THR   A C   
312  O O   . THR   A 39  ? 0.2734 0.2844 0.5957 -0.0084 0.0731  -0.0062 45  THR   A O   
313  C CB  . THR   A 39  ? 0.2406 0.2596 0.5146 -0.0094 0.0381  -0.0091 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2388 0.2476 0.5097 -0.0092 0.0571  -0.0050 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2450 0.2633 0.4827 -0.0079 0.0283  -0.0061 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2672 0.2971 0.6282 -0.0116 0.0442  -0.0197 46  THR   A N   
317  C CA  . THR   A 40  ? 0.2875 0.3178 0.6923 -0.0141 0.0573  -0.0239 46  THR   A CA  
318  C C   . THR   A 40  ? 0.3073 0.3321 0.7210 -0.0171 0.0672  -0.0252 46  THR   A C   
319  O O   . THR   A 40  ? 0.3275 0.3445 0.7620 -0.0184 0.0884  -0.0233 46  THR   A O   
320  C CB  . THR   A 40  ? 0.3056 0.3493 0.7497 -0.0142 0.0415  -0.0341 46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3276 0.3783 0.7650 -0.0134 0.0190  -0.0407 46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3188 0.3657 0.7583 -0.0108 0.0366  -0.0318 46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2944 0.3216 0.6921 -0.0178 0.0534  -0.0279 47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2946 0.3166 0.7008 -0.0206 0.0614  -0.0297 47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3086 0.3170 0.6739 -0.0185 0.0755  -0.0191 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3053 0.3120 0.6325 -0.0153 0.0703  -0.0133 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2961 0.3268 0.7055 -0.0216 0.0395  -0.0388 47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3197 0.3183 0.6938 -0.0198 0.0925  -0.0173 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3473 0.3315 0.6846 -0.0163 0.1063  -0.0078 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3521 0.3385 0.6634 -0.0165 0.0922  -0.0089 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3557 0.3478 0.6863 -0.0201 0.0831  -0.0164 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3864 0.3571 0.7452 -0.0167 0.1319  -0.0050 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5002 0.4534 0.8209 -0.0114 0.1468  0.0047  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6184 0.5594 0.9056 -0.0037 0.1594  0.0141  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6450 0.5882 0.9418 -0.0029 0.1626  0.0144  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6526 0.5799 0.8994 0.0030  0.1665  0.0215  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3489 0.3310 0.6180 -0.0123 0.0899  -0.0024 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3716 0.3544 0.6142 -0.0118 0.0793  -0.0023 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4005 0.3690 0.6294 -0.0091 0.0958  0.0032  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4185 0.3743 0.6423 -0.0049 0.1147  0.0096  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3978 0.3666 0.6173 -0.0101 0.0890  0.0013  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4102 0.3648 0.6165 -0.0068 0.1042  0.0066  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3872 0.3402 0.5561 -0.0030 0.0964  0.0094  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4018 0.3441 0.5600 -0.0002 0.1058  0.0127  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4441 0.3961 0.6845 -0.0115 0.1114  0.0018  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.5874 0.5568 0.8547 -0.0185 0.0876  -0.0114 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3482 0.3107 0.4979 -0.0024 0.0809  0.0084  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3147 0.2759 0.4313 0.0016  0.0748  0.0107  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3153 0.2626 0.4081 0.0102  0.0892  0.0179  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3594 0.3013 0.4577 0.0124  0.0995  0.0206  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.2912 0.2647 0.3963 0.0003  0.0576  0.0081  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3313 0.3143 0.4419 -0.0042 0.0425  0.0026  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3382 0.3190 0.4443 -0.0046 0.0414  0.0012  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.2518 0.2434 0.3672 -0.0062 0.0313  -0.0001 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2900 0.2303 0.3576 0.0158  0.0905  0.0206  52  THR   A N   
356  C CA  . THR   A 46  ? 0.3060 0.2321 0.3449 0.0265  0.1006  0.0263  52  THR   A CA  
357  C C   . THR   A 46  ? 0.2909 0.2245 0.3065 0.0303  0.0863  0.0239  52  THR   A C   
358  O O   . THR   A 46  ? 0.2733 0.2161 0.2885 0.0266  0.0748  0.0205  52  THR   A O   
359  C CB  . THR   A 46  ? 0.3629 0.2763 0.3920 0.0309  0.1098  0.0297  52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4146 0.3175 0.4646 0.0291  0.1270  0.0326  52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3740 0.2734 0.3655 0.0445  0.1146  0.0345  52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2742 0.2035 0.2723 0.0375  0.0875  0.0251  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2476 0.1839 0.2276 0.0413  0.0743  0.0212  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2717 0.1967 0.2238 0.0529  0.0765  0.0228  53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2973 0.2051 0.2337 0.0624  0.0897  0.0278  53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2322 0.1704 0.2093 0.0437  0.0724  0.0197  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2486 0.1958 0.2529 0.0339  0.0718  0.0189  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2339 0.1806 0.1984 0.0466  0.0581  0.0140  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2393 0.2021 0.2589 0.0244  0.0581  0.0149  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2474 0.1800 0.1925 0.0534  0.0648  0.0188  54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2614 0.1852 0.1809 0.0653  0.0636  0.0187  54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2854 0.2040 0.1842 0.0767  0.0604  0.0161  54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2735 0.2021 0.1798 0.0733  0.0526  0.0114  54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2428 0.1793 0.1657 0.0619  0.0504  0.0134  54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.3122 0.2135 0.1828 0.0915  0.0666  0.0190  55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.3315 0.2260 0.1776 0.1052  0.0616  0.0151  55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3694 0.2591 0.1932 0.1175  0.0537  0.0122  55  ARG   A C   
378  O O   . ARG   A 49  ? 0.4016 0.2721 0.2012 0.1297  0.0635  0.0182  55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3653 0.2389 0.1937 0.1145  0.0785  0.0221  55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.3497 0.2275 0.2041 0.1022  0.0882  0.0255  55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3406 0.2355 0.2109 0.0946  0.0757  0.0182  55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.3181 0.2158 0.2125 0.0843  0.0852  0.0218  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3322 0.2446 0.2468 0.0750  0.0773  0.0176  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2888 0.2141 0.2041 0.0737  0.0613  0.0099  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.3300 0.2441 0.2664 0.0670  0.0857  0.0207  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3507 0.2574 0.1846 0.1143  0.0369  0.0031  56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3633 0.2699 0.1850 0.1231  0.0281  -0.0006 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3609 0.2871 0.1974 0.1205  0.0094  -0.0130 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3590 0.2977 0.2149 0.1110  0.0050  -0.0172 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3525 0.2600 0.1864 0.1144  0.0351  0.0054  56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2951 0.2261 0.1677 0.0926  0.0294  0.0023  56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3877 0.3169 0.2186 0.1281  -0.0006 -0.0184 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3726 0.3206 0.2229 0.1250  -0.0167 -0.0306 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.3645 0.3226 0.2326 0.1161  -0.0175 -0.0300 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3620 0.3311 0.2405 0.1185  -0.0293 -0.0394 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.4384 0.3829 0.2696 0.1439  -0.0310 -0.0413 57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.5583 0.4891 0.3629 0.1596  -0.0314 -0.0389 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5649 0.4861 0.3635 0.1563  -0.0182 -0.0277 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.6537 0.5827 0.4435 0.1759  -0.0455 -0.0488 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3333 0.2885 0.2081 0.1053  -0.0052 -0.0202 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2947 0.2586 0.1850 0.0970  -0.0058 -0.0202 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2735 0.2563 0.1904 0.0871  -0.0144 -0.0282 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2630 0.2518 0.1916 0.0800  -0.0147 -0.0295 58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2882 0.2473 0.1842 0.0863  0.0069  -0.0105 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.3076 0.2444 0.1805 0.0954  0.0206  -0.0006 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2601 0.2512 0.1875 0.0863  -0.0195 -0.0327 59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2366 0.2434 0.1905 0.0766  -0.0239 -0.0389 59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2111 0.2204 0.1740 0.0675  -0.0177 -0.0344 59  GLN   A C   
409  O O   . GLN   A 53  ? 0.1941 0.2137 0.1757 0.0619  -0.0195 -0.0389 59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2765 0.2928 0.2405 0.0847  -0.0365 -0.0516 59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3330 0.3521 0.2985 0.0904  -0.0450 -0.0599 59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3748 0.4060 0.3590 0.0965  -0.0584 -0.0747 59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4069 0.4351 0.3780 0.1116  -0.0694 -0.0825 59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3203 0.3649 0.3359 0.0858  -0.0575 -0.0794 59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1992 0.1977 0.1489 0.0666  -0.0093 -0.0256 60  THR   A N   
416  C CA  . THR   A 54  ? 0.1975 0.1967 0.1539 0.0578  -0.0035 -0.0215 60  THR   A CA  
417  C C   . THR   A 54  ? 0.1864 0.1775 0.1384 0.0516  0.0047  -0.0137 60  THR   A C   
418  O O   . THR   A 54  ? 0.2130 0.1950 0.1538 0.0563  0.0083  -0.0100 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2284 0.2230 0.1771 0.0639  -0.0029 -0.0212 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2704 0.2505 0.1994 0.0719  0.0019  -0.0157 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2480 0.2506 0.2028 0.0714  -0.0119 -0.0299 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1782 0.1726 0.1401 0.0417  0.0076  -0.0117 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1778 0.1667 0.1405 0.0355  0.0132  -0.0065 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1564 0.1491 0.1274 0.0271  0.0133  -0.0065 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1626 0.1589 0.1353 0.0269  0.0119  -0.0090 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1509 0.1414 0.1261 0.0214  0.0153  -0.0039 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1425 0.1340 0.1218 0.0153  0.0143  -0.0044 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1393 0.1338 0.1246 0.0110  0.0121  -0.0036 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1441 0.1370 0.1329 0.0108  0.0133  -0.0020 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1534 0.1375 0.1327 0.0145  0.0174  -0.0036 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.1661 0.1506 0.1484 0.0095  0.0142  -0.0056 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.1797 0.1598 0.1520 0.0195  0.0200  -0.0038 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1319 0.1295 0.1177 0.0081  0.0098  -0.0044 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1345 0.1333 0.1242 0.0050  0.0075  -0.0032 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1427 0.1380 0.1289 0.0032  0.0046  -0.0037 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1479 0.1405 0.1274 0.0040  0.0050  -0.0050 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1324 0.1360 0.1250 0.0047  0.0077  -0.0032 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1309 0.1342 0.1206 0.0041  0.0096  -0.0033 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1521 0.1570 0.1419 0.0059  0.0121  -0.0055 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1577 0.1580 0.1445 0.0028  0.0098  -0.0011 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1572 0.1611 0.1464 0.0055  0.0163  -0.0054 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1712 0.1685 0.1537 0.0033  0.0145  -0.0002 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1771 0.1763 0.1618 0.0042  0.0184  -0.0024 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.2039 0.1992 0.1859 0.0048  0.0252  -0.0013 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1302 0.1252 0.1204 0.0016  0.0010  -0.0033 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1464 0.1376 0.1316 0.0018  -0.0042 -0.0048 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1537 0.1432 0.1298 0.0032  -0.0040 -0.0023 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1615 0.1534 0.1420 0.0025  -0.0030 0.0001  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1591 0.1506 0.1553 0.0007  -0.0094 -0.0069 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.1779 0.1654 0.1678 0.0028  -0.0175 -0.0103 64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.1933 0.1766 0.1772 0.0041  -0.0200 -0.0144 64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2009 0.1877 0.1891 0.0046  -0.0233 -0.0099 64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2142 0.1926 0.1892 0.0078  -0.0288 -0.0187 64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2219 0.2034 0.2001 0.0090  -0.0321 -0.0134 64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2412 0.2185 0.2125 0.0108  -0.0354 -0.0183 64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.2873 0.2582 0.2462 0.0167  -0.0456 -0.0232 64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1692 0.1528 0.1319 0.0057  -0.0040 -0.0027 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1713 0.1495 0.1224 0.0083  -0.0009 0.0007  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.1986 0.1687 0.1360 0.0128  -0.0085 -0.0005 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2086 0.1726 0.1338 0.0160  -0.0109 -0.0034 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.1886 0.1644 0.1334 0.0092  0.0068  0.0013  65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2258 0.1911 0.1552 0.0132  0.0148  0.0062  65  CYS   A SG  
463  N N   . SER   A 60  ? 0.2069 0.1761 0.1452 0.0142  -0.0128 0.0011  66  SER   A N   
464  C CA  . SER   A 60  ? 0.2230 0.1847 0.1485 0.0202  -0.0224 -0.0011 66  SER   A CA  
465  C C   . SER   A 60  ? 0.2346 0.1829 0.1332 0.0275  -0.0196 0.0014  66  SER   A C   
466  O O   . SER   A 60  ? 0.2701 0.2112 0.1540 0.0335  -0.0280 -0.0030 66  SER   A O   
467  C CB  . SER   A 60  ? 0.2674 0.2310 0.2001 0.0209  -0.0275 0.0003  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3635 0.3238 0.2914 0.0215  -0.0190 0.0071  66  SER   A OG  
469  N N   . SER   A 61  ? 0.2380 0.1825 0.1312 0.0271  -0.0068 0.0076  67  SER   A N   
470  C CA  . SER   A 61  ? 0.2589 0.1883 0.1264 0.0344  -0.0001 0.0113  67  SER   A CA  
471  C C   . SER   A 61  ? 0.2606 0.1864 0.1181 0.0359  0.0017  0.0079  67  SER   A C   
472  O O   . SER   A 61  ? 0.2934 0.2050 0.1267 0.0431  0.0071  0.0104  67  SER   A O   
473  C CB  . SER   A 61  ? 0.2781 0.2038 0.1473 0.0332  0.0151  0.0187  67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2617 0.1977 0.1510 0.0259  0.0233  0.0178  67  SER   A OG  
475  N N   . ARG   A 62  ? 0.2458 0.1827 0.1201 0.0301  -0.0024 0.0023  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.2504 0.1842 0.1170 0.0314  -0.0026 -0.0020 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2537 0.1920 0.1281 0.0306  -0.0161 -0.0102 68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2752 0.2118 0.1465 0.0311  -0.0174 -0.0150 68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2512 0.1928 0.1326 0.0256  0.0080  -0.0008 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.2515 0.1888 0.1299 0.0263  0.0222  0.0053  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.2876 0.2097 0.1410 0.0334  0.0290  0.0068  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.3274 0.2442 0.1813 0.0338  0.0455  0.0128  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.3300 0.2361 0.1731 0.0378  0.0527  0.0191  68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.3338 0.2332 0.1615 0.0428  0.0434  0.0203  68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.3369 0.2380 0.1852 0.0376  0.0699  0.0240  68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2680 0.2130 0.1569 0.0285  -0.0249 -0.0123 69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2809 0.2317 0.1861 0.0260  -0.0352 -0.0203 69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2780 0.2345 0.1966 0.0203  -0.0292 -0.0219 69  ARG   A C   
489  O O   . ARG   A 63  ? 0.3004 0.2552 0.2216 0.0206  -0.0342 -0.0287 69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3411 0.2835 0.2320 0.0336  -0.0480 -0.0282 69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.4171 0.3574 0.3046 0.0389  -0.0589 -0.0298 69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4661 0.4005 0.3452 0.0467  -0.0751 -0.0407 69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.4969 0.4232 0.3576 0.0564  -0.0842 -0.0402 69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.5354 0.4459 0.3606 0.0685  -0.0880 -0.0404 69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.5584 0.4602 0.3644 0.0716  -0.0835 -0.0417 69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.5238 0.4257 0.3307 0.0786  -0.0957 -0.0388 69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2455 0.2076 0.1720 0.0159  -0.0189 -0.0163 70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2489 0.2145 0.1840 0.0127  -0.0132 -0.0171 70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2148 0.1886 0.1647 0.0085  -0.0076 -0.0133 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2046 0.1810 0.1555 0.0081  -0.0053 -0.0093 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.2988 0.2594 0.2189 0.0153  -0.0058 -0.0152 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.4260 0.3778 0.3315 0.0195  -0.0092 -0.0202 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.5242 0.4713 0.4173 0.0218  0.0007  -0.0173 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.6103 0.5644 0.5173 0.0182  0.0070  -0.0170 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6715 0.6209 0.5691 0.0209  0.0152  -0.0165 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.1933 0.1694 0.1525 0.0067  -0.0046 -0.0144 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.1728 0.1544 0.1409 0.0052  0.0009  -0.0112 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.1918 0.1741 0.1546 0.0069  0.0065  -0.0102 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2165 0.1949 0.1729 0.0084  0.0076  -0.0122 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.1731 0.1543 0.1525 0.0039  0.0020  -0.0123 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.1902 0.1717 0.1810 0.0018  -0.0023 -0.0141 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2234 0.2081 0.2237 0.0006  -0.0003 -0.0114 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.1889 0.1680 0.1851 0.0012  -0.0086 -0.0194 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2076 0.1920 0.2203 -0.0012 -0.0046 -0.0148 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2440 0.2258 0.2554 -0.0008 -0.0107 -0.0201 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1631 0.1508 0.1301 0.0072  0.0096  -0.0080 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1618 0.1521 0.1288 0.0092  0.0138  -0.0086 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.1605 0.1553 0.1341 0.0113  0.0141  -0.0088 72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1643 0.1618 0.1423 0.0110  0.0126  -0.0078 72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.1738 0.1662 0.1416 0.0088  0.0171  -0.0075 72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.1989 0.1839 0.1549 0.0093  0.0190  -0.0065 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2254 0.2058 0.1738 0.0113  0.0226  -0.0078 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2172 0.1986 0.1678 0.0090  0.0176  -0.0041 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2423 0.2135 0.1757 0.0135  0.0250  -0.0068 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2365 0.2084 0.1715 0.0117  0.0194  -0.0028 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2628 0.2291 0.1879 0.0143  0.0228  -0.0043 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.3130 0.2675 0.2185 0.0187  0.0251  -0.0029 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.1542 0.1491 0.1270 0.0148  0.0156  -0.0103 73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.1615 0.1595 0.1370 0.0194  0.0146  -0.0112 73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.1885 0.1946 0.1729 0.0203  0.0135  -0.0142 73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2361 0.2446 0.2253 0.0184  0.0162  -0.0156 73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.1801 0.1746 0.1512 0.0237  0.0162  -0.0122 73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.1987 0.1923 0.1689 0.0208  0.0185  -0.0134 73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.1680 0.1594 0.1361 0.0158  0.0179  -0.0118 73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1675 0.1771 0.1551 0.0234  0.0103  -0.0156 74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1684 0.1864 0.1685 0.0242  0.0080  -0.0203 74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1673 0.1878 0.1672 0.0320  0.0023  -0.0247 74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1795 0.1940 0.1673 0.0366  0.0011  -0.0224 74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2070 0.2266 0.2124 0.0191  0.0085  -0.0186 74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2267 0.2442 0.2332 0.0134  0.0137  -0.0158 74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2191 0.2337 0.2159 0.0189  0.0074  -0.0148 74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1624 0.1915 0.1768 0.0344  -0.0011 -0.0318 75  SER   A N   
543  C CA  . SER   A 69  ? 0.1731 0.2066 0.1905 0.0425  -0.0093 -0.0388 75  SER   A CA  
544  C C   . SER   A 69  ? 0.1680 0.2073 0.1995 0.0382  -0.0105 -0.0419 75  SER   A C   
545  O O   . SER   A 69  ? 0.1737 0.2172 0.2206 0.0312  -0.0056 -0.0423 75  SER   A O   
546  C CB  . SER   A 69  ? 0.1919 0.2327 0.2223 0.0479  -0.0138 -0.0470 75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3004 0.3351 0.3173 0.0528  -0.0129 -0.0441 75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1447 0.1824 0.1698 0.0423  -0.0153 -0.0433 76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1509 0.1933 0.1893 0.0379  -0.0159 -0.0461 76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1548 0.2016 0.1976 0.0464  -0.0260 -0.0561 76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1702 0.2127 0.1968 0.0571  -0.0323 -0.0584 76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1533 0.1888 0.1810 0.0324  -0.0106 -0.0373 76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1410 0.1670 0.1470 0.0376  -0.0104 -0.0322 76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1558 0.1749 0.1501 0.0370  -0.0057 -0.0257 76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1534 0.1765 0.1517 0.0436  -0.0139 -0.0341 76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1667 0.1759 0.1448 0.0413  -0.0029 -0.0207 76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1663 0.1785 0.1450 0.0488  -0.0107 -0.0284 76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1794 0.1848 0.1495 0.0476  -0.0047 -0.0218 76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1494 0.2037 0.2138 0.0426  -0.0276 -0.0626 77  SER   A N   
560  C CA  . SER   A 71  ? 0.1634 0.2226 0.2350 0.0505  -0.0385 -0.0742 77  SER   A CA  
561  C C   . SER   A 71  ? 0.1834 0.2346 0.2342 0.0551  -0.0407 -0.0714 77  SER   A C   
562  O O   . SER   A 71  ? 0.1855 0.2295 0.2240 0.0497  -0.0327 -0.0608 77  SER   A O   
563  C CB  . SER   A 71  ? 0.1701 0.2397 0.2758 0.0443  -0.0385 -0.0830 77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1926 0.2590 0.3013 0.0346  -0.0292 -0.0753 77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1920 0.2432 0.2369 0.0666  -0.0519 -0.0811 78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2131 0.2555 0.2375 0.0725  -0.0533 -0.0793 78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2173 0.2632 0.2583 0.0627  -0.0492 -0.0790 78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2067 0.2625 0.2764 0.0557  -0.0495 -0.0851 78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2577 0.2987 0.2711 0.0888  -0.0675 -0.0916 78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.3033 0.3368 0.2931 0.1008  -0.0707 -0.0898 78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3913 0.4198 0.3627 0.1198  -0.0854 -0.1014 78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4831 0.5026 0.4296 0.1331  -0.0883 -0.0991 78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.5555 0.5689 0.4812 0.1540  -0.1039 -0.1107 78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2110 0.2480 0.2353 0.0628  -0.0444 -0.0719 79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2133 0.2530 0.2527 0.0541  -0.0405 -0.0711 79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2139 0.2619 0.2748 0.0563  -0.0496 -0.0856 79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2280 0.2750 0.2802 0.0682  -0.0605 -0.0959 79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2462 0.2745 0.2623 0.0575  -0.0360 -0.0637 79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2833 0.3020 0.2737 0.0651  -0.0335 -0.0573 79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2418 0.2653 0.2344 0.0709  -0.0411 -0.0641 79  PRO   A CD  
581  N N   . SER   A 74  ? 0.1745 0.2298 0.2635 0.0456  -0.0450 -0.0868 80  SER   A N   
582  C CA  . SER   A 74  ? 0.1892 0.2532 0.3059 0.0462  -0.0524 -0.1016 80  SER   A CA  
583  C C   . SER   A 74  ? 0.1732 0.2391 0.3130 0.0345  -0.0432 -0.0985 80  SER   A C   
584  O O   . SER   A 74  ? 0.1676 0.2277 0.2988 0.0272  -0.0325 -0.0850 80  SER   A O   
585  C CB  . SER   A 74  ? 0.2318 0.3053 0.3679 0.0491  -0.0592 -0.1123 80  SER   A CB  
586  O OG  . SER   A 74  ? 0.2881 0.3655 0.4444 0.0382  -0.0483 -0.1066 80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1649 0.2377 0.3335 0.0340  -0.0483 -0.1121 81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.1788 0.2522 0.3719 0.0238  -0.0389 -0.1103 81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.1781 0.2565 0.3978 0.0162  -0.0302 -0.1097 81  LEU   A C   
590  O O   . LEU   A 75  ? 0.1825 0.2702 0.4277 0.0186  -0.0366 -0.1234 81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.1922 0.2706 0.4075 0.0272  -0.0481 -0.1269 81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2561 0.3278 0.4542 0.0306  -0.0505 -0.1258 81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2813 0.3583 0.4990 0.0368  -0.0632 -0.1456 81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2667 0.3324 0.4685 0.0203  -0.0364 -0.1128 81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.1781 0.2502 0.3943 0.0077  -0.0159 -0.0953 82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.1876 0.2604 0.4215 0.0013  -0.0044 -0.0914 82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.1994 0.2660 0.4481 -0.0068 0.0097  -0.0847 82  ILE   A C   
598  O O   . ILE   A 76  ? 0.1955 0.2539 0.4251 -0.0083 0.0134  -0.0742 82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2124 0.2804 0.4179 0.0020  -0.0011 -0.0793 82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2477 0.3213 0.4426 0.0106  -0.0138 -0.0869 82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2201 0.2850 0.4366 -0.0044 0.0132  -0.0723 82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2740 0.3433 0.4439 0.0120  -0.0119 -0.0774 82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.1801 0.2496 0.4640 -0.0116 0.0187  -0.0903 83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2044 0.2649 0.5013 -0.0183 0.0350  -0.0825 83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2217 0.2698 0.4901 -0.0202 0.0470  -0.0642 83  PHE   A C   
606  O O   . PHE   A 77  ? 0.2506 0.2987 0.5096 -0.0194 0.0493  -0.0606 83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2143 0.2792 0.5568 -0.0227 0.0446  -0.0922 83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2527 0.3057 0.6091 -0.0290 0.0644  -0.0833 83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.2928 0.3343 0.6415 -0.0315 0.0823  -0.0701 83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.2734 0.3242 0.6457 -0.0312 0.0656  -0.0870 83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.3185 0.3460 0.6759 -0.0354 0.1017  -0.0608 83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.2983 0.3360 0.6825 -0.0361 0.0851  -0.0780 83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3003 0.3259 0.6763 -0.0377 0.1034  -0.0647 83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.2058 0.2431 0.4594 -0.0219 0.0533  -0.0533 84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.2120 0.2363 0.4382 -0.0221 0.0631  -0.0370 84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.2237 0.2359 0.4625 -0.0254 0.0797  -0.0304 84  VAL   A C   
617  O O   . VAL   A 78  ? 0.2233 0.2338 0.4724 -0.0266 0.0798  -0.0321 84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.2159 0.2376 0.4080 -0.0189 0.0531  -0.0297 84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.2359 0.2447 0.4015 -0.0180 0.0608  -0.0151 84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.2102 0.2415 0.3900 -0.0151 0.0391  -0.0356 84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.2295 0.2316 0.4659 -0.0260 0.0949  -0.0223 85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.2395 0.2263 0.4852 -0.0277 0.1144  -0.0142 85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.2642 0.2391 0.4821 -0.0248 0.1137  -0.0027 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.2644 0.2411 0.4531 -0.0215 0.1009  0.0010  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.2953 0.2707 0.5339 -0.0266 0.1309  -0.0060 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.4257 0.3852 0.6829 -0.0283 0.1549  0.0000  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.5798 0.5266 0.8301 -0.0264 0.1732  0.0079  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.6138 0.5502 0.8896 -0.0286 0.1949  0.0096  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.6263 0.5726 0.8463 -0.0225 0.1669  0.0122  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.2801 0.2426 0.5090 -0.0258 0.1275  0.0024  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.2872 0.2372 0.4923 -0.0222 0.1278  0.0132  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.3049 0.2424 0.4683 -0.0157 0.1284  0.0262  86  ALA   A C   
633  O O   . ALA   A 80  ? 0.3142 0.2448 0.4703 -0.0142 0.1383  0.0302  86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.2900 0.2254 0.5144 -0.0235 0.1469  0.0177  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.3097 0.2444 0.4473 -0.0115 0.1176  0.0318  87  SER   A N   
636  C CA  . SER   A 81  ? 0.3151 0.2383 0.4140 -0.0043 0.1149  0.0424  87  SER   A CA  
637  C C   . SER   A 81  ? 0.3339 0.2458 0.4197 0.0004  0.1142  0.0501  87  SER   A C   
638  O O   . SER   A 81  ? 0.3426 0.2558 0.4500 -0.0028 0.1173  0.0475  87  SER   A O   
639  C CB  . SER   A 81  ? 0.3174 0.2545 0.4020 -0.0040 0.0963  0.0376  87  SER   A CB  
640  O OG  . SER   A 81  ? 0.2993 0.2470 0.3881 -0.0053 0.0826  0.0330  87  SER   A OG  
641  N N   . GLU   A 82  ? 0.3564 0.2570 0.4077 0.0086  0.1094  0.0589  88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.3795 0.2710 0.4181 0.0142  0.1056  0.0652  88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.3619 0.2704 0.4143 0.0101  0.0899  0.0575  88  GLU   A C   
644  O O   . GLU   A 82  ? 0.3749 0.2790 0.4281 0.0125  0.0882  0.0604  88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.4879 0.3639 0.4865 0.0256  0.1013  0.0743  88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.6313 0.5165 0.6160 0.0290  0.0801  0.0715  88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.7728 0.6538 0.7552 0.0335  0.0740  0.0747  88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.7926 0.6852 0.7756 0.0337  0.0576  0.0700  88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.8059 0.6718 0.7882 0.0368  0.0866  0.0817  88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.3316 0.2584 0.3935 0.0048  0.0790  0.0481  89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.3023 0.2432 0.3731 0.0022  0.0654  0.0416  89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.2627 0.2140 0.3626 -0.0042 0.0670  0.0327  89  TYR   A C   
653  O O   . TYR   A 83  ? 0.2694 0.2264 0.3761 -0.0049 0.0601  0.0294  89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.2974 0.2494 0.3584 0.0019  0.0532  0.0373  89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.3164 0.2596 0.3501 0.0083  0.0493  0.0435  89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.3425 0.2805 0.3646 0.0097  0.0547  0.0454  89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.3176 0.2583 0.3385 0.0136  0.0393  0.0464  89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.3691 0.2989 0.3649 0.0164  0.0497  0.0496  89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.3469 0.2800 0.3436 0.0206  0.0333  0.0499  89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.3789 0.3062 0.3619 0.0221  0.0383  0.0514  89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.4315 0.3502 0.3888 0.0301  0.0316  0.0539  89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.2459 0.1997 0.3639 -0.0084 0.0754  0.0276  90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.2338 0.1984 0.3810 -0.0136 0.0744  0.0164  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.2622 0.2219 0.4335 -0.0170 0.0892  0.0141  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.2719 0.2251 0.4386 -0.0164 0.0985  0.0185  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.2097 0.1902 0.3609 -0.0154 0.0632  0.0060  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.1931 0.1796 0.3251 -0.0129 0.0502  0.0065  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.1970 0.1881 0.3318 -0.0124 0.0431  0.0031  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.1967 0.1836 0.3096 -0.0109 0.0462  0.0101  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.1902 0.1863 0.3112 -0.0102 0.0336  0.0031  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.1796 0.1720 0.2797 -0.0092 0.0357  0.0096  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.1755 0.1722 0.2803 -0.0089 0.0303  0.0064  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.1713 0.1721 0.2662 -0.0072 0.0227  0.0064  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.2807 0.2440 0.4804 -0.0206 0.0917  0.0061  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.2750 0.2368 0.5060 -0.0249 0.1050  0.0006  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.2605 0.2374 0.5045 -0.0271 0.0978  -0.0111 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.2548 0.2425 0.4841 -0.0253 0.0826  -0.0153 91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.2815 0.2455 0.5393 -0.0277 0.1051  -0.0074 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.2953 0.2705 0.5402 -0.0257 0.0868  -0.0127 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.2825 0.2531 0.4901 -0.0211 0.0818  -0.0007 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.2516 0.2296 0.5259 -0.0309 0.1086  -0.0174 92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.2490 0.2420 0.5402 -0.0324 0.1012  -0.0301 92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2310 0.2391 0.5323 -0.0317 0.0827  -0.0448 92  ALA   A C   
684  O O   . ALA   A 86  ? 0.2313 0.2389 0.5476 -0.0329 0.0820  -0.0497 92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.2478 0.2393 0.5783 -0.0368 0.1170  -0.0359 92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2104 0.2295 0.4970 -0.0285 0.0680  -0.0502 93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.1973 0.2274 0.4849 -0.0254 0.0508  -0.0625 93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.1895 0.2301 0.4679 -0.0214 0.0383  -0.0696 93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2065 0.2461 0.4768 -0.0218 0.0429  -0.0639 93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.1990 0.2233 0.4576 -0.0228 0.0462  -0.0535 93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.2115 0.2338 0.4343 -0.0198 0.0423  -0.0426 93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.2014 0.2146 0.4013 -0.0188 0.0441  -0.0301 93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.2105 0.2262 0.3838 -0.0152 0.0345  -0.0267 93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.1919 0.2070 0.3476 -0.0142 0.0339  -0.0209 93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.1973 0.2139 0.3327 -0.0113 0.0264  -0.0182 93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.1964 0.2086 0.3557 -0.0158 0.0416  -0.0182 93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.1819 0.2310 0.4592 -0.0166 0.0232  -0.0814 94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.1887 0.2448 0.4498 -0.0107 0.0112  -0.0861 94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.1797 0.2299 0.4023 -0.0074 0.0077  -0.0748 94  TYR   A C   
700  O O   . TYR   A 88  ? 0.1983 0.2452 0.4128 -0.0059 0.0052  -0.0739 94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2050 0.2706 0.4805 -0.0049 -0.0036 -0.1048 94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2192 0.2931 0.5368 -0.0076 -0.0024 -0.1186 94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2257 0.3070 0.5511 -0.0055 -0.0060 -0.1241 94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2395 0.3133 0.5920 -0.0127 0.0040  -0.1256 94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2418 0.3316 0.6109 -0.0083 -0.0041 -0.1376 94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2469 0.3284 0.6439 -0.0160 0.0068  -0.1388 94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2510 0.3409 0.6571 -0.0139 0.0029  -0.1448 94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.2883 0.3867 0.7438 -0.0172 0.0060  -0.1592 94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1488 0.1977 0.3506 -0.0063 0.0082  -0.0668 95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1396 0.1839 0.3093 -0.0031 0.0049  -0.0577 95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1337 0.1829 0.2919 0.0047  -0.0068 -0.0660 95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1532 0.2082 0.3184 0.0069  -0.0105 -0.0726 95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1392 0.1778 0.2932 -0.0060 0.0123  -0.0446 95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1441 0.1790 0.2703 -0.0029 0.0083  -0.0371 95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.1496 0.1781 0.2625 -0.0057 0.0143  -0.0252 95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.1729 0.1958 0.2898 -0.0089 0.0217  -0.0193 95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1397 0.1674 0.2343 -0.0035 0.0112  -0.0214 95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1315 0.1779 0.2736 0.0098  -0.0122 -0.0667 96  SER   A N   
719  C CA  . SER   A 90  ? 0.1399 0.1871 0.2653 0.0193  -0.0219 -0.0731 96  SER   A CA  
720  C C   . SER   A 90  ? 0.1668 0.2088 0.2659 0.0215  -0.0197 -0.0627 96  SER   A C   
721  O O   . SER   A 90  ? 0.1605 0.1985 0.2539 0.0157  -0.0121 -0.0512 96  SER   A O   
722  C CB  . SER   A 90  ? 0.1832 0.2275 0.3030 0.0250  -0.0272 -0.0793 96  SER   A CB  
723  O OG  . SER   A 90  ? 0.1965 0.2337 0.3037 0.0225  -0.0205 -0.0685 96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1607 0.2022 0.2447 0.0305  -0.0268 -0.0676 97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1717 0.2069 0.2312 0.0340  -0.0245 -0.0591 97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1612 0.1981 0.2245 0.0268  -0.0185 -0.0512 97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1526 0.1839 0.2017 0.0253  -0.0135 -0.0417 97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1909 0.2175 0.2345 0.0350  -0.0194 -0.0512 97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2240 0.2467 0.2591 0.0438  -0.0244 -0.0587 97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2756 0.2903 0.2858 0.0558  -0.0272 -0.0602 97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2377 0.2624 0.2848 0.0433  -0.0270 -0.0654 97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2765 0.2880 0.2823 0.0627  -0.0317 -0.0678 97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2728 0.2909 0.3015 0.0551  -0.0321 -0.0715 97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1445 0.1883 0.2281 0.0225  -0.0184 -0.0558 98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1512 0.1951 0.2373 0.0163  -0.0118 -0.0487 98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1418 0.1892 0.2260 0.0209  -0.0157 -0.0532 98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1400 0.1931 0.2340 0.0264  -0.0234 -0.0644 98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1565 0.2032 0.2659 0.0089  -0.0055 -0.0492 98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1696 0.2136 0.2795 0.0033  0.0033  -0.0412 98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1671 0.2032 0.2564 0.0013  0.0069  -0.0294 98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.1983 0.2424 0.3314 -0.0024 0.0116  -0.0420 98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1374 0.1809 0.2089 0.0191  -0.0114 -0.0451 99  MET   A N   
743  C CA  . MET   A 93  ? 0.1308 0.1765 0.1990 0.0233  -0.0140 -0.0478 99  MET   A CA  
744  C C   . MET   A 93  ? 0.1420 0.1885 0.2187 0.0166  -0.0065 -0.0436 99  MET   A C   
745  O O   . MET   A 93  ? 0.1547 0.1955 0.2232 0.0115  -0.0002 -0.0345 99  MET   A O   
746  C CB  . MET   A 93  ? 0.1521 0.1901 0.1952 0.0282  -0.0143 -0.0418 99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1745 0.2082 0.2042 0.0367  -0.0194 -0.0446 99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2263 0.2478 0.2289 0.0418  -0.0150 -0.0357 99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2526 0.2718 0.2597 0.0303  -0.0063 -0.0255 99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1338 0.1868 0.2269 0.0174  -0.0072 -0.0505 100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1306 0.1826 0.2308 0.0118  0.0019  -0.0462 100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1317 0.1828 0.2210 0.0150  0.0012  -0.0450 100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1430 0.1975 0.2300 0.0220  -0.0067 -0.0511 100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1436 0.2025 0.2753 0.0088  0.0060  -0.0539 100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.1993 0.2585 0.3469 0.0047  0.0090  -0.0555 100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2013 0.2653 0.3828 0.0007  0.0172  -0.0617 100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2073 0.2568 0.3393 0.0002  0.0166  -0.0436 100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1272 0.1731 0.2106 0.0108  0.0094  -0.0378 101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1266 0.1711 0.2017 0.0130  0.0105  -0.0367 101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1305 0.1714 0.2104 0.0084  0.0213  -0.0328 101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1470 0.1837 0.2298 0.0041  0.0283  -0.0286 101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1554 0.1922 0.2053 0.0144  0.0086  -0.0297 101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1223 0.1641 0.2034 0.0103  0.0234  -0.0344 102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1353 0.1712 0.2159 0.0073  0.0348  -0.0300 102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1665 0.1919 0.2191 0.0069  0.0357  -0.0217 102 VAL   A C   
766  O O   . VAL   A 96  ? 0.1916 0.2161 0.2315 0.0096  0.0299  -0.0215 102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1425 0.1839 0.2376 0.0097  0.0369  -0.0360 102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1594 0.1925 0.2505 0.0076  0.0503  -0.0308 102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1464 0.1993 0.2739 0.0103  0.0345  -0.0463 102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1728 0.1895 0.2171 0.0043  0.0428  -0.0154 103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.2081 0.2152 0.2275 0.0048  0.0415  -0.0093 103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.2159 0.2135 0.2268 0.0038  0.0480  -0.0033 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2240 0.2221 0.2481 0.0020  0.0537  -0.0029 103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2196 0.2071 0.2081 0.0058  0.0475  0.0009  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.2110 0.1870 0.1853 0.0073  0.0520  0.0068  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.2115 0.1886 0.1849 0.0063  0.0447  0.0086  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2053 0.1871 0.1767 0.0057  0.0345  0.0065  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2386 0.2025 0.1874 0.0118  0.0521  0.0092  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2565 0.2061 0.1860 0.0160  0.0563  0.0152  104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2857 0.2262 0.2154 0.0175  0.0711  0.0200  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2628 0.2060 0.1748 0.0194  0.0474  0.0169  104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.3020 0.2290 0.2097 0.0229  0.0711  0.0254  104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2909 0.2197 0.1873 0.0244  0.0557  0.0231  104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.2297 0.2010 0.2039 0.0066  0.0509  0.0126  105 SER   A N   
785  C CA  . SER   A 99  ? 0.2373 0.2076 0.2085 0.0066  0.0450  0.0150  105 SER   A CA  
786  C C   . SER   A 99  ? 0.2788 0.2357 0.2405 0.0097  0.0546  0.0217  105 SER   A C   
787  O O   . SER   A 99  ? 0.3077 0.2594 0.2750 0.0097  0.0681  0.0236  105 SER   A O   
788  C CB  . SER   A 99  ? 0.2451 0.2279 0.2378 0.0024  0.0405  0.0110  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.3133 0.2985 0.3247 0.0002  0.0494  0.0099  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.2594 0.2096 0.2058 0.0131  0.0481  0.0250  106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.2810 0.2168 0.2132 0.0182  0.0538  0.0320  106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.2985 0.2402 0.2394 0.0165  0.0450  0.0317  106 GLU   A C   
793  O O   . GLU   A 100 ? 0.2986 0.2525 0.2504 0.0129  0.0343  0.0267  106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.3256 0.2464 0.2252 0.0269  0.0504  0.0349  106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.3489 0.2618 0.2387 0.0292  0.0614  0.0359  106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.3678 0.2647 0.2230 0.0390  0.0585  0.0376  106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.4114 0.2949 0.2442 0.0472  0.0552  0.0418  106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.3526 0.2499 0.2023 0.0394  0.0587  0.0342  106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.3298 0.2622 0.2681 0.0190  0.0511  0.0374  107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.3166 0.2550 0.2660 0.0171  0.0439  0.0370  107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.3106 0.2547 0.2545 0.0186  0.0276  0.0336  107 PRO   A C   
802  O O   . PRO   A 101 ? 0.3168 0.2732 0.2782 0.0138  0.0210  0.0295  107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.3434 0.2658 0.2822 0.0224  0.0534  0.0450  107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.3631 0.2750 0.2982 0.0235  0.0704  0.0487  107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.3497 0.2650 0.2763 0.0237  0.0669  0.0448  107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.2889 0.2241 0.2102 0.0254  0.0213  0.0343  108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2709 0.2110 0.1900 0.0273  0.0057  0.0296  108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.2538 0.2079 0.1886 0.0208  0.0003  0.0227  108 GLY   A C   
809  O O   . GLY   A 102 ? 0.2496 0.2093 0.1900 0.0207  -0.0106 0.0182  108 GLY   A O   
810  N N   . ASP   A 103 ? 0.2365 0.1955 0.1793 0.0161  0.0085  0.0217  109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.2082 0.1785 0.1637 0.0113  0.0048  0.0163  109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1946 0.1754 0.1699 0.0065  0.0033  0.0144  109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1877 0.1755 0.1712 0.0040  0.0002  0.0107  109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.2046 0.1761 0.1607 0.0094  0.0127  0.0153  109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.2212 0.1833 0.1577 0.0141  0.0129  0.0156  109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.2426 0.2017 0.1695 0.0172  0.0034  0.0132  109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.2253 0.1824 0.1569 0.0149  0.0229  0.0176  109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1893 0.1696 0.1708 0.0061  0.0060  0.0171  110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1741 0.1631 0.1726 0.0025  0.0050  0.0151  110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1724 0.1651 0.1750 0.0025  -0.0032 0.0126  110 CYS   A C   
821  O O   . CYS   A 104 ? 0.2044 0.1930 0.2011 0.0055  -0.0095 0.0130  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1751 0.1616 0.1792 0.0025  0.0089  0.0181  110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.2202 0.2057 0.2321 0.0004  0.0205  0.0185  110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1494 0.1489 0.1625 -0.0001 -0.0029 0.0098  111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1526 0.1547 0.1733 -0.0006 -0.0073 0.0077  111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.1535 0.1560 0.1727 -0.0010 -0.0080 0.0050  111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1579 0.1621 0.1865 -0.0019 -0.0084 0.0032  111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1465 0.1465 0.1551 -0.0002 -0.0067 0.0049  112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1556 0.1555 0.1626 -0.0005 -0.0065 0.0024  112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1379 0.1409 0.1508 -0.0011 -0.0017 0.0019  112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1411 0.1465 0.1541 -0.0007 0.0014  0.0024  112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1322 0.1341 0.1499 -0.0014 -0.0008 0.0005  113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1276 0.1292 0.1464 0.0001  0.0048  0.0010  113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1329 0.1336 0.1424 0.0024  0.0070  0.0004  113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1442 0.1432 0.1498 0.0020  0.0060  -0.0007 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1573 0.1557 0.1862 -0.0006 0.0075  0.0008  113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.1754 0.1757 0.2161 -0.0019 0.0070  0.0013  113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.1961 0.1896 0.2214 0.0026  0.0154  0.0022  113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2128 0.2105 0.2709 -0.0033 0.0107  0.0001  113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1201 0.1216 0.1264 0.0057  0.0094  0.0003  114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1253 0.1257 0.1237 0.0099  0.0109  -0.0010 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1416 0.1351 0.1363 0.0140  0.0161  0.0009  114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1555 0.1472 0.1510 0.0159  0.0184  0.0020  114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1392 0.1446 0.1373 0.0125  0.0086  -0.0038 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1523 0.1575 0.1436 0.0188  0.0080  -0.0067 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1641 0.1697 0.1538 0.0180  0.0081  -0.0074 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1695 0.1809 0.1655 0.0216  0.0038  -0.0120 114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1496 0.1379 0.1393 0.0160  0.0190  0.0015  115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1641 0.1428 0.1490 0.0208  0.0265  0.0043  115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.1795 0.1541 0.1511 0.0279  0.0273  0.0040  115 ARG   A C   
851  O O   . ARG   A 109 ? 0.1871 0.1651 0.1582 0.0268  0.0239  0.0019  115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2148 0.1891 0.2103 0.0162  0.0308  0.0054  115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3051 0.2831 0.3163 0.0100  0.0290  0.0045  115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3256 0.2995 0.3497 0.0065  0.0320  0.0032  115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.3585 0.3226 0.3862 0.0095  0.0439  0.0067  115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.3595 0.3218 0.4007 0.0079  0.0493  0.0078  115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.3154 0.2861 0.3705 0.0030  0.0422  0.0047  115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.3200 0.2711 0.3609 0.0120  0.0626  0.0121  115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.1900 0.1550 0.1502 0.0359  0.0330  0.0066  116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2124 0.1695 0.1575 0.0449  0.0352  0.0075  116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2397 0.1821 0.1824 0.0471  0.0478  0.0133  116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2548 0.1958 0.2114 0.0407  0.0534  0.0151  116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2279 0.1838 0.1578 0.0554  0.0308  0.0052  116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2480 0.1920 0.1671 0.0621  0.0390  0.0094  116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.2716 0.2025 0.1986 0.0564  0.0528  0.0160  117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.2971 0.2114 0.2220 0.0593  0.0675  0.0222  117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.3172 0.2212 0.2389 0.0628  0.0780  0.0269  117 GLN   A C   
868  O O   . GLN   A 111 ? 0.3352 0.2267 0.2637 0.0620  0.0924  0.0319  117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.3352 0.2369 0.2393 0.0710  0.0710  0.0250  117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.4376 0.3328 0.3156 0.0858  0.0678  0.0253  117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.5806 0.4652 0.4371 0.0988  0.0676  0.0266  117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.6222 0.5161 0.4733 0.1034  0.0544  0.0206  117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.5816 0.4459 0.4270 0.1055  0.0828  0.0344  117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.2950 0.2039 0.2095 0.0659  0.0721  0.0249  118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.3059 0.2043 0.2152 0.0703  0.0823  0.0291  118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.2837 0.1913 0.2179 0.0587  0.0830  0.0279  118 HIS   A C   
877  O O   . HIS   A 112 ? 0.3075 0.2063 0.2433 0.0606  0.0941  0.0317  118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.3136 0.2091 0.1979 0.0826  0.0760  0.0271  118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.3529 0.2390 0.2114 0.0964  0.0733  0.0272  118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.3641 0.2628 0.2190 0.0989  0.0568  0.0196  118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.4143 0.2791 0.2504 0.1088  0.0853  0.0339  118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.4116 0.2980 0.2436 0.1124  0.0575  0.0212  118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.4386 0.3039 0.2571 0.1190  0.0745  0.0302  118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2436 0.1685 0.1957 0.0480  0.0711  0.0225  119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2303 0.1643 0.2042 0.0384  0.0692  0.0207  119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2011 0.1512 0.1794 0.0332  0.0545  0.0154  119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2083 0.1641 0.1787 0.0345  0.0461  0.0124  119 GLY   A O   
888  N N   . VAL   A 114 ? 0.1805 0.1369 0.1724 0.0279  0.0527  0.0144  120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1726 0.1421 0.1694 0.0231  0.0409  0.0104  120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1706 0.1418 0.1530 0.0294  0.0360  0.0082  120 VAL   A C   
891  O O   . VAL   A 114 ? 0.1951 0.1598 0.1687 0.0357  0.0405  0.0093  120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.1747 0.1489 0.1898 0.0168  0.0405  0.0102  120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.1781 0.1628 0.1953 0.0134  0.0303  0.0073  120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.1905 0.1653 0.2233 0.0106  0.0415  0.0096  120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1788 0.1586 0.1604 0.0279  0.0271  0.0044  121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1813 0.1649 0.1552 0.0331  0.0209  -0.0001 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1769 0.1694 0.1628 0.0277  0.0159  -0.0027 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1725 0.1661 0.1561 0.0316  0.0133  -0.0060 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1899 0.1775 0.1599 0.0351  0.0155  -0.0035 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.1970 0.1914 0.1667 0.0393  0.0074  -0.0104 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2010 0.1785 0.1568 0.0424  0.0203  -0.0009 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1496 0.1476 0.1474 0.0196  0.0143  -0.0016 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1620 0.1664 0.1698 0.0150  0.0106  -0.0029 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1342 0.1412 0.1491 0.0085  0.0091  -0.0010 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1382 0.1427 0.1523 0.0071  0.0102  0.0008  122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1287 0.1395 0.1500 0.0054  0.0068  -0.0013 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1193 0.1302 0.1429 0.0015  0.0052  0.0009  123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1198 0.1326 0.1440 0.0004  0.0052  0.0001  123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1178 0.1335 0.1477 0.0009  0.0059  -0.0025 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1350 0.1452 0.1655 -0.0003 0.0041  0.0032  123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1568 0.1687 0.1927 0.0002  0.0051  0.0024  123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1597 0.1676 0.1942 -0.0003 0.0050  0.0038  123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.1637 0.1748 0.2069 -0.0015 0.0035  0.0050  123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1204 0.1307 0.1397 -0.0009 0.0052  0.0020  124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1250 0.1348 0.1452 -0.0016 0.0083  0.0024  124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1295 0.1387 0.1566 -0.0027 0.0098  0.0039  124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1341 0.1408 0.1598 -0.0026 0.0074  0.0066  124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1389 0.1428 0.1483 -0.0012 0.0088  0.0051  124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1503 0.1506 0.1596 -0.0013 0.0153  0.0069  124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1579 0.1620 0.1615 -0.0003 0.0080  0.0032  124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1306 0.1420 0.1673 -0.0035 0.0137  0.0015  125 SER   A N   
922  C CA  . SER   A 119 ? 0.1326 0.1429 0.1782 -0.0047 0.0164  0.0025  125 SER   A CA  
923  C C   . SER   A 119 ? 0.1531 0.1603 0.2057 -0.0059 0.0243  0.0031  125 SER   A C   
924  O O   . SER   A 119 ? 0.1687 0.1706 0.2244 -0.0065 0.0288  0.0066  125 SER   A O   
925  C CB  . SER   A 119 ? 0.1303 0.1467 0.1862 -0.0042 0.0134  -0.0032 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1497 0.1654 0.2167 -0.0056 0.0158  -0.0036 125 SER   A OG  
927  N N   . THR   A 120 ? 0.1539 0.1635 0.2102 -0.0061 0.0273  0.0000  126 THR   A N   
928  C CA  . THR   A 120 ? 0.1666 0.1728 0.2337 -0.0075 0.0374  0.0004  126 THR   A CA  
929  C C   . THR   A 120 ? 0.1843 0.1876 0.2431 -0.0064 0.0415  0.0017  126 THR   A C   
930  O O   . THR   A 120 ? 0.1742 0.1798 0.2217 -0.0049 0.0353  0.0009  126 THR   A O   
931  C CB  . THR   A 120 ? 0.1860 0.2008 0.2792 -0.0093 0.0382  -0.0084 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.2063 0.2294 0.3046 -0.0079 0.0333  -0.0156 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.1913 0.2093 0.2927 -0.0097 0.0333  -0.0115 126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.2101 0.2074 0.2751 -0.0070 0.0531  0.0039  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.2329 0.2270 0.2914 -0.0057 0.0585  0.0047  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.2636 0.2496 0.3324 -0.0064 0.0745  0.0075  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.2737 0.2583 0.3594 -0.0085 0.0811  0.0073  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.3030 0.2820 0.3603 -0.0042 0.0815  0.0104  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.3207 0.2887 0.3829 -0.0035 0.0996  0.0144  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.3175 0.2945 0.4015 -0.0054 0.1038  0.0073  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.3088 0.3012 0.4097 -0.0074 0.0928  -0.0018 128 GLY   A O   
942  N N   . ASN   A 123 ? 0.3312 0.2977 0.4163 -0.0042 0.1205  0.0109  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.3395 0.3141 0.4500 -0.0059 0.1268  0.0039  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.2959 0.2825 0.4023 -0.0049 0.1130  -0.0025 129 ASN   A C   
945  O O   . ASN   A 123 ? 0.2924 0.2912 0.4269 -0.0065 0.1124  -0.0115 129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.3817 0.3684 0.5366 -0.0110 0.1293  -0.0053 129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.4803 0.4554 0.6466 -0.0128 0.1452  0.0001  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.5251 0.4819 0.6779 -0.0102 0.1635  0.0099  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.4822 0.4666 0.6739 -0.0165 0.1395  -0.0065 129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.2665 0.2492 0.3401 -0.0017 0.1027  0.0014  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.2436 0.2356 0.3128 -0.0005 0.0909  -0.0039 130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.2020 0.2087 0.2827 -0.0017 0.0749  -0.0110 130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2209 0.2355 0.3020 -0.0001 0.0660  -0.0162 130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1787 0.1871 0.2657 -0.0037 0.0717  -0.0109 131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1661 0.1854 0.2591 -0.0036 0.0575  -0.0168 131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1800 0.1937 0.2496 -0.0032 0.0508  -0.0106 131 LEU   A C   
957  O O   . LEU   A 125 ? 0.2046 0.2077 0.2611 -0.0034 0.0566  -0.0033 131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1647 0.1921 0.2882 -0.0059 0.0583  -0.0240 131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.1940 0.2303 0.3477 -0.0061 0.0619  -0.0333 131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2117 0.2521 0.3987 -0.0095 0.0677  -0.0394 131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.1872 0.2351 0.3426 -0.0017 0.0469  -0.0423 131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1486 0.1688 0.2142 -0.0018 0.0390  -0.0139 132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1391 0.1558 0.1897 -0.0018 0.0331  -0.0095 132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1296 0.1547 0.1906 -0.0009 0.0250  -0.0154 132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1466 0.1784 0.2143 0.0018  0.0203  -0.0219 132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1501 0.1621 0.1794 -0.0001 0.0288  -0.0059 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1795 0.1964 0.2083 0.0024  0.0243  -0.0103 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1630 0.1728 0.1835 -0.0003 0.0229  -0.0028 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1156 0.1393 0.1780 -0.0023 0.0241  -0.0135 133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1277 0.1573 0.1973 -0.0008 0.0173  -0.0189 133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1304 0.1566 0.1851 0.0002  0.0128  -0.0147 133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1380 0.1584 0.1847 -0.0017 0.0149  -0.0083 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1207 0.1497 0.1718 0.0041  0.0069  -0.0184 134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1224 0.1474 0.1615 0.0054  0.0049  -0.0145 134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1261 0.1527 0.1693 0.0079  0.0020  -0.0182 134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1259 0.1562 0.1731 0.0122  -0.0019 -0.0254 134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1234 0.1464 0.1506 0.0094  0.0031  -0.0145 134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1331 0.1548 0.1563 0.0080  0.0052  -0.0125 134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1355 0.1524 0.1519 0.0051  0.0070  -0.0073 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1550 0.1804 0.1823 0.0102  0.0048  -0.0170 134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1418 0.1564 0.1528 0.0046  0.0085  -0.0063 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1546 0.1780 0.1774 0.0093  0.0073  -0.0152 134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1494 0.1670 0.1630 0.0065  0.0094  -0.0097 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1198 0.1432 0.1613 0.0061  0.0032  -0.0140 135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1193 0.1425 0.1620 0.0089  0.0015  -0.0167 135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1268 0.1457 0.1555 0.0146  0.0011  -0.0161 135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1390 0.1537 0.1620 0.0134  0.0042  -0.0105 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1262 0.1470 0.1729 0.0052  0.0039  -0.0119 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1285 0.1472 0.1518 0.0217  -0.0024 -0.0221 136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1539 0.1653 0.1601 0.0293  -0.0011 -0.0209 136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1586 0.1637 0.1609 0.0300  0.0039  -0.0167 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1613 0.1685 0.1717 0.0281  0.0032  -0.0185 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.1960 0.2075 0.1948 0.0391  -0.0077 -0.0294 136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2815 0.2825 0.2577 0.0495  -0.0058 -0.0276 136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2632 0.2598 0.2325 0.0492  -0.0012 -0.0219 136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3406 0.3361 0.3049 0.0586  -0.0081 -0.0317 136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1530 0.1498 0.1450 0.0325  0.0103  -0.0111 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1711 0.1608 0.1604 0.0342  0.0171  -0.0074 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2000 0.1774 0.1686 0.0453  0.0225  -0.0063 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2257 0.1947 0.1903 0.0481  0.0307  -0.0027 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1788 0.1685 0.1805 0.0266  0.0227  -0.0013 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1798 0.1787 0.1971 0.0182  0.0173  -0.0017 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1795 0.1651 0.1776 0.0264  0.0266  0.0021  137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.1979 0.1729 0.1526 0.0525  0.0187  -0.0091 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.2186 0.1788 0.1495 0.0647  0.0248  -0.0066 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.2645 0.2162 0.1789 0.0754  0.0250  -0.0097 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2979 0.2336 0.1914 0.0854  0.0344  -0.0051 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.2360 0.1957 0.1553 0.0710  0.0192  -0.0093 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2382 0.2019 0.1684 0.0626  0.0216  -0.0052 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2452 0.2093 0.1653 0.0693  0.0153  -0.0088 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2255 0.2032 0.1570 0.0675  0.0031  -0.0178 138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2557 0.2385 0.1874 0.0710  -0.0043 -0.0231 138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2595 0.2338 0.1756 0.0786  -0.0021 -0.0204 138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2465 0.2421 0.1947 0.0678  -0.0134 -0.0315 138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2472 0.2079 0.1702 0.0740  0.0159  -0.0173 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2686 0.2213 0.1760 0.0847  0.0147  -0.0219 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2829 0.2303 0.1955 0.0810  0.0254  -0.0164 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.3102 0.2479 0.2067 0.0908  0.0273  -0.0187 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2667 0.2310 0.1841 0.0851  0.0001  -0.0340 139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.3006 0.2786 0.2478 0.0705  -0.0015 -0.0347 139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2796 0.2637 0.2411 0.0600  0.0018  -0.0289 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3290 0.3108 0.2844 0.0704  -0.0064 -0.0415 139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2609 0.2141 0.1950 0.0684  0.0317  -0.0099 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.2444 0.1947 0.1888 0.0643  0.0411  -0.0055 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.2529 0.1875 0.1859 0.0697  0.0567  0.0024  140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.2470 0.1818 0.1949 0.0625  0.0649  0.0085  140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.2190 0.1825 0.1917 0.0500  0.0387  -0.0036 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2259 0.2027 0.2103 0.0446  0.0261  -0.0101 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2086 0.1947 0.2146 0.0328  0.0250  -0.0067 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2383 0.2154 0.2217 0.0484  0.0219  -0.0166 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2803 0.1997 0.1858 0.0839  0.0615  0.0019  141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.3281 0.2284 0.2179 0.0917  0.0789  0.0103  141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.3368 0.2336 0.2458 0.0852  0.0941  0.0166  141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.3408 0.2274 0.2534 0.0850  0.1094  0.0240  141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.3627 0.2446 0.2136 0.1107  0.0810  0.0086  141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.3896 0.2751 0.2221 0.1193  0.0638  0.0001  141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.4369 0.3002 0.2265 0.1412  0.0667  -0.0009 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.3913 0.2832 0.2307 0.1142  0.0602  0.0022  141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.3185 0.2242 0.2430 0.0798  0.0900  0.0131  142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.3175 0.2217 0.2632 0.0741  0.1027  0.0176  142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.3164 0.2313 0.2948 0.0606  0.1042  0.0208  142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.3319 0.2442 0.3305 0.0567  0.1163  0.0245  142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.3088 0.2199 0.2620 0.0723  0.0963  0.0126  142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2839 0.2138 0.2511 0.0638  0.0778  0.0060  142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2835 0.2178 0.2378 0.0678  0.0641  -0.0017 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2610 0.2060 0.2581 0.0505  0.0720  0.0065  142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2641 0.2148 0.2400 0.0572  0.0526  -0.0051 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2552 0.2117 0.2547 0.0472  0.0571  0.0003  142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2633 0.2126 0.2861 0.0421  0.0779  0.0108  142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2501 0.2197 0.2719 0.0366  0.0495  0.0000  142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2518 0.2153 0.2964 0.0323  0.0676  0.0092  142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2414 0.2137 0.2831 0.0301  0.0544  0.0047  142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.2923 0.2188 0.2769 0.0541  0.0920  0.0186  143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.2911 0.2269 0.3043 0.0429  0.0919  0.0202  143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.3518 0.2751 0.3713 0.0442  0.1094  0.0260  143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.3452 0.2746 0.3940 0.0356  0.1118  0.0263  143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2659 0.2125 0.2789 0.0379  0.0780  0.0172  143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2484 0.2088 0.2657 0.0333  0.0626  0.0121  143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2515 0.2193 0.2660 0.0302  0.0525  0.0100  143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2380 0.2076 0.2818 0.0248  0.0601  0.0119  143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.4293 0.3346 0.4218 0.0556  0.1211  0.0301  144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.5013 0.3922 0.5001 0.0573  0.1407  0.0365  144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.5816 0.4502 0.5588 0.0699  0.1603  0.0423  144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.6071 0.4584 0.5774 0.0753  0.1778  0.0487  144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.5518 0.4397 0.5433 0.0578  0.1398  0.0381  144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.6622 0.5475 0.6189 0.0670  0.1289  0.0362  144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.6895 0.5852 0.6488 0.0624  0.1166  0.0332  144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.7150 0.5880 0.6424 0.0795  0.1320  0.0369  144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.6151 0.4821 0.5801 0.0752  0.1584  0.0402  145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.6714 0.5161 0.6131 0.0883  0.1769  0.0452  145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.6896 0.5388 0.6323 0.0891  0.1727  0.0411  145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.7138 0.5592 0.6269 0.0989  0.1637  0.0370  145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.7482 0.5720 0.6426 0.1056  0.1810  0.0482  145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.8407 0.6744 0.7145 0.1088  0.1580  0.0414  145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.9505 0.7755 0.7865 0.1242  0.1497  0.0364  145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.9598 0.7878 0.7992 0.1241  0.1479  0.0328  145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.9856 0.8011 0.7891 0.1368  0.1440  0.0353  145 GLU   A OE2 
1078 N N   . SER   B 1   ? 0.3518 0.2866 0.3056 -0.0111 -0.0438 -0.0099 7   SER   C N   
1079 C CA  . SER   B 1   ? 0.3444 0.2894 0.3206 -0.0097 -0.0480 -0.0084 7   SER   C CA  
1080 C C   . SER   B 1   ? 0.3162 0.2736 0.3089 -0.0068 -0.0448 -0.0068 7   SER   C C   
1081 O O   . SER   B 1   ? 0.3260 0.2828 0.3127 -0.0066 -0.0427 -0.0060 7   SER   C O   
1082 C CB  . SER   B 1   ? 0.3763 0.3139 0.3542 -0.0135 -0.0613 -0.0059 7   SER   C CB  
1083 O OG  . SER   B 1   ? 0.4168 0.3497 0.3910 -0.0155 -0.0683 -0.0026 7   SER   C OG  
1084 N N   . GLY   B 2   ? 0.2804 0.2478 0.2928 -0.0052 -0.0438 -0.0065 8   GLY   C N   
1085 C CA  . GLY   B 2   ? 0.2487 0.2260 0.2765 -0.0032 -0.0398 -0.0059 8   GLY   C CA  
1086 C C   . GLY   B 2   ? 0.2170 0.2036 0.2581 -0.0020 -0.0333 -0.0072 8   GLY   C C   
1087 O O   . GLY   B 2   ? 0.2284 0.2154 0.2650 -0.0020 -0.0302 -0.0083 8   GLY   C O   
1088 N N   . ALA   B 3   ? 0.2017 0.1949 0.2585 -0.0013 -0.0304 -0.0072 9   ALA   C N   
1089 C CA  . ALA   B 3   ? 0.1985 0.1991 0.2660 -0.0013 -0.0231 -0.0085 9   ALA   C CA  
1090 C C   . ALA   B 3   ? 0.1834 0.1884 0.2574 -0.0010 -0.0159 -0.0098 9   ALA   C C   
1091 O O   . ALA   B 3   ? 0.2040 0.2072 0.2802 -0.0003 -0.0177 -0.0094 9   ALA   C O   
1092 C CB  . ALA   B 3   ? 0.2046 0.2065 0.2893 -0.0020 -0.0270 -0.0076 9   ALA   C CB  
1093 N N   . ILE   B 4   ? 0.1680 0.1773 0.2436 -0.0023 -0.0077 -0.0114 10  ILE   C N   
1094 C CA  . ILE   B 4   ? 0.1576 0.1691 0.2383 -0.0033 0.0006  -0.0136 10  ILE   C CA  
1095 C C   . ILE   B 4   ? 0.1599 0.1741 0.2590 -0.0041 0.0052  -0.0148 10  ILE   C C   
1096 O O   . ILE   B 4   ? 0.1592 0.1750 0.2608 -0.0052 0.0054  -0.0141 10  ILE   C O   
1097 C CB  . ILE   B 4   ? 0.1631 0.1754 0.2287 -0.0058 0.0064  -0.0143 10  ILE   C CB  
1098 C CG1 . ILE   B 4   ? 0.1691 0.1800 0.2202 -0.0050 0.0026  -0.0126 10  ILE   C CG1 
1099 C CG2 . ILE   B 4   ? 0.1883 0.2001 0.2547 -0.0083 0.0153  -0.0172 10  ILE   C CG2 
1100 C CD1 . ILE   B 4   ? 0.1692 0.1816 0.2093 -0.0076 0.0057  -0.0115 10  ILE   C CD1 
1101 N N   . TYR   B 5   ? 0.1730 0.1875 0.2872 -0.0034 0.0092  -0.0164 11  TYR   C N   
1102 C CA  . TYR   B 5   ? 0.1796 0.1966 0.3152 -0.0039 0.0157  -0.0178 11  TYR   C CA  
1103 C C   . TYR   B 5   ? 0.1845 0.2000 0.3177 -0.0063 0.0293  -0.0222 11  TYR   C C   
1104 O O   . TYR   B 5   ? 0.2014 0.2144 0.3361 -0.0054 0.0321  -0.0241 11  TYR   C O   
1105 C CB  . TYR   B 5   ? 0.1824 0.2000 0.3417 -0.0010 0.0091  -0.0157 11  TYR   C CB  
1106 C CG  . TYR   B 5   ? 0.1718 0.1887 0.3313 -0.0002 -0.0051 -0.0114 11  TYR   C CG  
1107 C CD1 . TYR   B 5   ? 0.1766 0.1960 0.3478 -0.0012 -0.0080 -0.0098 11  TYR   C CD1 
1108 C CD2 . TYR   B 5   ? 0.2002 0.2125 0.3453 0.0006  -0.0150 -0.0091 11  TYR   C CD2 
1109 C CE1 . TYR   B 5   ? 0.2058 0.2224 0.3739 -0.0015 -0.0212 -0.0063 11  TYR   C CE1 
1110 C CE2 . TYR   B 5   ? 0.2162 0.2249 0.3565 0.0000  -0.0272 -0.0058 11  TYR   C CE2 
1111 C CZ  . TYR   B 5   ? 0.2322 0.2428 0.3839 -0.0011 -0.0306 -0.0045 11  TYR   C CZ  
1112 O OH  . TYR   B 5   ? 0.2641 0.2692 0.4077 -0.0026 -0.0427 -0.0018 11  TYR   C OH  
1113 N N   . VAL   B 6   ? 0.1962 0.2117 0.3235 -0.0100 0.0379  -0.0239 12  VAL   C N   
1114 C CA  . VAL   B 6   ? 0.2147 0.2260 0.3335 -0.0141 0.0513  -0.0284 12  VAL   C CA  
1115 C C   . VAL   B 6   ? 0.2217 0.2336 0.3522 -0.0169 0.0618  -0.0302 12  VAL   C C   
1116 O O   . VAL   B 6   ? 0.2128 0.2269 0.3403 -0.0185 0.0592  -0.0277 12  VAL   C O   
1117 C CB  . VAL   B 6   ? 0.2475 0.2553 0.3363 -0.0181 0.0504  -0.0280 12  VAL   C CB  
1118 C CG1 . VAL   B 6   ? 0.2511 0.2616 0.3307 -0.0188 0.0433  -0.0238 12  VAL   C CG1 
1119 C CG2 . VAL   B 6   ? 0.2746 0.2756 0.3505 -0.0244 0.0635  -0.0324 12  VAL   C CG2 
1120 N N   . GLY   B 7   ? 0.2284 0.2382 0.3754 -0.0173 0.0740  -0.0345 13  GLY   C N   
1121 C CA  . GLY   B 7   ? 0.2392 0.2492 0.3993 -0.0202 0.0863  -0.0366 13  GLY   C CA  
1122 C C   . GLY   B 7   ? 0.2399 0.2577 0.4236 -0.0171 0.0781  -0.0321 13  GLY   C C   
1123 O O   . GLY   B 7   ? 0.2538 0.2757 0.4549 -0.0121 0.0668  -0.0291 13  GLY   C O   
1124 N N   . ASN   B 8   ? 0.2321 0.2509 0.4125 -0.0206 0.0811  -0.0309 14  ASN   C N   
1125 C CA  . ASN   B 8   ? 0.2286 0.2541 0.4293 -0.0184 0.0720  -0.0264 14  ASN   C CA  
1126 C C   . ASN   B 8   ? 0.2041 0.2300 0.3847 -0.0183 0.0581  -0.0221 14  ASN   C C   
1127 O O   . ASN   B 8   ? 0.2005 0.2289 0.3873 -0.0192 0.0540  -0.0192 14  ASN   C O   
1128 C CB  . ASN   B 8   ? 0.2737 0.3006 0.4907 -0.0218 0.0843  -0.0274 14  ASN   C CB  
1129 C CG  . ASN   B 8   ? 0.3725 0.4007 0.6202 -0.0202 0.0965  -0.0309 14  ASN   C CG  
1130 O OD1 . ASN   B 8   ? 0.3924 0.4259 0.6691 -0.0152 0.0888  -0.0285 14  ASN   C OD1 
1131 N ND2 . ASN   B 8   ? 0.4076 0.4298 0.6490 -0.0247 0.1156  -0.0364 14  ASN   C ND2 
1132 N N   . TYR   B 9   ? 0.1921 0.2154 0.3517 -0.0169 0.0508  -0.0217 15  TYR   C N   
1133 C CA  . TYR   B 9   ? 0.1828 0.2057 0.3244 -0.0165 0.0394  -0.0182 15  TYR   C CA  
1134 C C   . TYR   B 9   ? 0.1682 0.1911 0.3084 -0.0120 0.0271  -0.0165 15  TYR   C C   
1135 O O   . TYR   B 9   ? 0.1726 0.1945 0.3148 -0.0102 0.0278  -0.0181 15  TYR   C O   
1136 C CB  . TYR   B 9   ? 0.1959 0.2146 0.3094 -0.0203 0.0432  -0.0187 15  TYR   C CB  
1137 C CG  . TYR   B 9   ? 0.2188 0.2349 0.3257 -0.0263 0.0541  -0.0195 15  TYR   C CG  
1138 C CD1 . TYR   B 9   ? 0.2394 0.2573 0.3541 -0.0279 0.0540  -0.0172 15  TYR   C CD1 
1139 C CD2 . TYR   B 9   ? 0.2393 0.2495 0.3299 -0.0314 0.0643  -0.0225 15  TYR   C CD2 
1140 C CE1 . TYR   B 9   ? 0.2607 0.2751 0.3676 -0.0343 0.0643  -0.0175 15  TYR   C CE1 
1141 C CE2 . TYR   B 9   ? 0.2635 0.2690 0.3439 -0.0383 0.0744  -0.0231 15  TYR   C CE2 
1142 C CZ  . TYR   B 9   ? 0.2884 0.2962 0.3773 -0.0397 0.0746  -0.0205 15  TYR   C CZ  
1143 O OH  . TYR   B 9   ? 0.3304 0.3325 0.4074 -0.0472 0.0845  -0.0204 15  TYR   C OH  
1144 N N   . ARG   B 10  ? 0.1518 0.1745 0.2864 -0.0108 0.0163  -0.0135 16  ARG   C N   
1145 C CA  . ARG   B 10  ? 0.1524 0.1727 0.2793 -0.0079 0.0052  -0.0120 16  ARG   C CA  
1146 C C   . ARG   B 10  ? 0.1390 0.1569 0.2439 -0.0085 0.0031  -0.0110 16  ARG   C C   
1147 O O   . ARG   B 10  ? 0.1536 0.1715 0.2568 -0.0100 0.0027  -0.0098 16  ARG   C O   
1148 C CB  . ARG   B 10  ? 0.1630 0.1830 0.3047 -0.0067 -0.0052 -0.0096 16  ARG   C CB  
1149 C CG  . ARG   B 10  ? 0.1774 0.1920 0.3053 -0.0055 -0.0169 -0.0079 16  ARG   C CG  
1150 C CD  . ARG   B 10  ? 0.2025 0.2148 0.3435 -0.0059 -0.0284 -0.0053 16  ARG   C CD  
1151 N NE  . ARG   B 10  ? 0.2271 0.2323 0.3522 -0.0069 -0.0371 -0.0045 16  ARG   C NE  
1152 C CZ  . ARG   B 10  ? 0.2529 0.2504 0.3637 -0.0070 -0.0455 -0.0039 16  ARG   C CZ  
1153 N NH1 . ARG   B 10  ? 0.2486 0.2452 0.3581 -0.0058 -0.0471 -0.0033 16  ARG   C NH1 
1154 N NH2 . ARG   B 10  ? 0.2347 0.2240 0.3300 -0.0085 -0.0512 -0.0041 16  ARG   C NH2 
1155 N N   . VAL   B 11  ? 0.1446 0.1606 0.2346 -0.0075 0.0023  -0.0113 17  VAL   C N   
1156 C CA  . VAL   B 11  ? 0.1472 0.1616 0.2205 -0.0077 0.0008  -0.0100 17  VAL   C CA  
1157 C C   . VAL   B 11  ? 0.1539 0.1644 0.2213 -0.0050 -0.0073 -0.0093 17  VAL   C C   
1158 O O   . VAL   B 11  ? 0.1583 0.1672 0.2241 -0.0036 -0.0097 -0.0098 17  VAL   C O   
1159 C CB  . VAL   B 11  ? 0.1748 0.1897 0.2364 -0.0091 0.0057  -0.0104 17  VAL   C CB  
1160 C CG1 . VAL   B 11  ? 0.1802 0.1946 0.2297 -0.0095 0.0039  -0.0079 17  VAL   C CG1 
1161 C CG2 . VAL   B 11  ? 0.1755 0.1913 0.2393 -0.0128 0.0145  -0.0122 17  VAL   C CG2 
1162 N N   . VAL   B 12  ? 0.1397 0.1474 0.2026 -0.0047 -0.0108 -0.0084 18  VAL   C N   
1163 C CA  . VAL   B 12  ? 0.1504 0.1517 0.2044 -0.0031 -0.0167 -0.0086 18  VAL   C CA  
1164 C C   . VAL   B 12  ? 0.1416 0.1407 0.1853 -0.0024 -0.0148 -0.0082 18  VAL   C C   
1165 O O   . VAL   B 12  ? 0.1413 0.1436 0.1872 -0.0032 -0.0115 -0.0068 18  VAL   C O   
1166 C CB  . VAL   B 12  ? 0.1856 0.1824 0.2459 -0.0039 -0.0240 -0.0086 18  VAL   C CB  
1167 C CG1 . VAL   B 12  ? 0.2291 0.2277 0.3022 -0.0043 -0.0276 -0.0080 18  VAL   C CG1 
1168 C CG2 . VAL   B 12  ? 0.1752 0.1735 0.2427 -0.0053 -0.0230 -0.0080 18  VAL   C CG2 
1169 N N   . ASN   B 13  ? 0.1410 0.1336 0.1742 -0.0011 -0.0168 -0.0091 19  ASN   C N   
1170 C CA  . ASN   B 13  ? 0.1498 0.1389 0.1771 0.0000  -0.0142 -0.0092 19  ASN   C CA  
1171 C C   . ASN   B 13  ? 0.1639 0.1500 0.1959 -0.0010 -0.0167 -0.0093 19  ASN   C C   
1172 O O   . ASN   B 13  ? 0.1712 0.1520 0.2034 -0.0023 -0.0222 -0.0106 19  ASN   C O   
1173 C CB  . ASN   B 13  ? 0.1637 0.1438 0.1783 0.0008  -0.0144 -0.0112 19  ASN   C CB  
1174 C CG  . ASN   B 13  ? 0.1931 0.1754 0.2028 0.0015  -0.0119 -0.0108 19  ASN   C CG  
1175 O OD1 . ASN   B 13  ? 0.1858 0.1666 0.1927 0.0006  -0.0152 -0.0110 19  ASN   C OD1 
1176 N ND2 . ASN   B 13  ? 0.1683 0.1545 0.1790 0.0029  -0.0065 -0.0095 19  ASN   C ND2 
1177 N N   . ARG   B 14  ? 0.1514 0.1398 0.1872 -0.0006 -0.0136 -0.0076 20  ARG   C N   
1178 C CA  . ARG   B 14  ? 0.1459 0.1311 0.1866 -0.0017 -0.0156 -0.0074 20  ARG   C CA  
1179 C C   . ARG   B 14  ? 0.1849 0.1587 0.2177 -0.0016 -0.0187 -0.0106 20  ARG   C C   
1180 O O   . ARG   B 14  ? 0.1915 0.1612 0.2270 -0.0036 -0.0235 -0.0114 20  ARG   C O   
1181 C CB  . ARG   B 14  ? 0.1484 0.1367 0.1936 -0.0014 -0.0123 -0.0043 20  ARG   C CB  
1182 C CG  . ARG   B 14  ? 0.1389 0.1251 0.1907 -0.0031 -0.0142 -0.0032 20  ARG   C CG  
1183 C CD  . ARG   B 14  ? 0.1638 0.1511 0.2191 -0.0025 -0.0119 0.0005  20  ARG   C CD  
1184 N NE  . ARG   B 14  ? 0.1587 0.1442 0.2206 -0.0045 -0.0134 0.0026  20  ARG   C NE  
1185 C CZ  . ARG   B 14  ? 0.2102 0.1876 0.2732 -0.0035 -0.0146 0.0010  20  ARG   C CZ  
1186 N NH1 . ARG   B 14  ? 0.2148 0.1840 0.2709 -0.0012 -0.0143 -0.0035 20  ARG   C NH1 
1187 N NH2 . ARG   B 14  ? 0.1969 0.1729 0.2664 -0.0055 -0.0160 0.0035  20  ARG   C NH2 
1188 N N   . HIS   B 15  ? 0.1816 0.1491 0.2038 0.0001  -0.0158 -0.0127 21  HIS   C N   
1189 C CA  . HIS   B 15  ? 0.2038 0.1573 0.2141 -0.0009 -0.0174 -0.0165 21  HIS   C CA  
1190 C C   . HIS   B 15  ? 0.2273 0.1743 0.2293 -0.0041 -0.0252 -0.0179 21  HIS   C C   
1191 O O   . HIS   B 15  ? 0.2540 0.1879 0.2449 -0.0067 -0.0289 -0.0207 21  HIS   C O   
1192 C CB  . HIS   B 15  ? 0.2006 0.1477 0.2020 0.0014  -0.0099 -0.0188 21  HIS   C CB  
1193 C CG  . HIS   B 15  ? 0.2157 0.1631 0.2082 0.0016  -0.0080 -0.0192 21  HIS   C CG  
1194 N ND1 . HIS   B 15  ? 0.2152 0.1743 0.2154 0.0035  -0.0050 -0.0161 21  HIS   C ND1 
1195 C CD2 . HIS   B 15  ? 0.2293 0.1651 0.2048 -0.0004 -0.0086 -0.0223 21  HIS   C CD2 
1196 C CE1 . HIS   B 15  ? 0.2178 0.1731 0.2072 0.0030  -0.0037 -0.0174 21  HIS   C CE1 
1197 N NE2 . HIS   B 15  ? 0.2447 0.1860 0.2186 0.0006  -0.0056 -0.0209 21  HIS   C NE2 
1198 N N   . LEU   B 16  ? 0.2155 0.1704 0.2230 -0.0044 -0.0282 -0.0158 22  LEU   C N   
1199 C CA  . LEU   B 16  ? 0.2226 0.1725 0.2268 -0.0074 -0.0370 -0.0156 22  LEU   C CA  
1200 C C   . LEU   B 16  ? 0.2296 0.1867 0.2518 -0.0088 -0.0428 -0.0132 22  LEU   C C   
1201 O O   . LEU   B 16  ? 0.2381 0.1935 0.2638 -0.0110 -0.0509 -0.0118 22  LEU   C O   
1202 C CB  . LEU   B 16  ? 0.2269 0.1791 0.2259 -0.0066 -0.0363 -0.0148 22  LEU   C CB  
1203 C CG  . LEU   B 16  ? 0.2393 0.1830 0.2203 -0.0060 -0.0305 -0.0172 22  LEU   C CG  
1204 C CD1 . LEU   B 16  ? 0.2479 0.1937 0.2245 -0.0058 -0.0304 -0.0158 22  LEU   C CD1 
1205 C CD2 . LEU   B 16  ? 0.2626 0.1881 0.2242 -0.0097 -0.0337 -0.0205 22  LEU   C CD2 
1206 N N   . ALA   B 17  ? 0.2093 0.1749 0.2447 -0.0078 -0.0384 -0.0121 23  ALA   C N   
1207 C CA  . ALA   B 17  ? 0.2135 0.1864 0.2674 -0.0092 -0.0413 -0.0099 23  ALA   C CA  
1208 C C   . ALA   B 17  ? 0.2088 0.1738 0.2647 -0.0127 -0.0511 -0.0098 23  ALA   C C   
1209 O O   . ALA   B 17  ? 0.2355 0.1898 0.2791 -0.0141 -0.0533 -0.0118 23  ALA   C O   
1210 C CB  . ALA   B 17  ? 0.1939 0.1743 0.2570 -0.0087 -0.0345 -0.0087 23  ALA   C CB  
1211 N N   . THR   B 18  ? 0.2091 0.1789 0.2814 -0.0143 -0.0569 -0.0074 24  THR   C N   
1212 C CA  . THR   B 18  ? 0.2205 0.1836 0.2980 -0.0184 -0.0685 -0.0061 24  THR   C CA  
1213 C C   . THR   B 18  ? 0.2202 0.1877 0.3141 -0.0199 -0.0677 -0.0050 24  THR   C C   
1214 O O   . THR   B 18  ? 0.2050 0.1815 0.3073 -0.0179 -0.0580 -0.0048 24  THR   C O   
1215 C CB  . THR   B 18  ? 0.2273 0.1941 0.3193 -0.0193 -0.0760 -0.0029 24  THR   C CB  
1216 O OG1 . THR   B 18  ? 0.2426 0.2235 0.3595 -0.0173 -0.0691 -0.0014 24  THR   C OG1 
1217 C CG2 . THR   B 18  ? 0.2553 0.2180 0.3327 -0.0182 -0.0773 -0.0032 24  THR   C CG2 
1218 N N   . HIS   B 19  ? 0.2308 0.1923 0.3311 -0.0242 -0.0786 -0.0036 25  HIS   C N   
1219 C CA  . HIS   B 19  ? 0.2142 0.1808 0.3333 -0.0261 -0.0781 -0.0019 25  HIS   C CA  
1220 C C   . HIS   B 19  ? 0.2029 0.1847 0.3481 -0.0244 -0.0712 0.0006  25  HIS   C C   
1221 O O   . HIS   B 19  ? 0.2141 0.2024 0.3685 -0.0241 -0.0626 0.0008  25  HIS   C O   
1222 C CB  . HIS   B 19  ? 0.2670 0.2252 0.3915 -0.0316 -0.0931 0.0000  25  HIS   C CB  
1223 C CG  . HIS   B 19  ? 0.3821 0.3227 0.4798 -0.0347 -0.0991 -0.0032 25  HIS   C CG  
1224 N ND1 . HIS   B 19  ? 0.4379 0.3731 0.5239 -0.0338 -0.0919 -0.0065 25  HIS   C ND1 
1225 C CD2 . HIS   B 19  ? 0.4399 0.3659 0.5209 -0.0394 -0.1115 -0.0035 25  HIS   C CD2 
1226 C CE1 . HIS   B 19  ? 0.4645 0.3821 0.5278 -0.0375 -0.0986 -0.0095 25  HIS   C CE1 
1227 N NE2 . HIS   B 19  ? 0.4723 0.3830 0.5295 -0.0414 -0.1104 -0.0080 25  HIS   C NE2 
1228 N N   . ASN   B 20  ? 0.1887 0.1751 0.3447 -0.0234 -0.0741 0.0022  26  ASN   C N   
1229 C CA  . ASN   B 20  ? 0.1937 0.1932 0.3754 -0.0218 -0.0657 0.0037  26  ASN   C CA  
1230 C C   . ASN   B 20  ? 0.1830 0.1877 0.3550 -0.0189 -0.0507 0.0011  26  ASN   C C   
1231 O O   . ASN   B 20  ? 0.1771 0.1895 0.3633 -0.0192 -0.0407 0.0013  26  ASN   C O   
1232 C CB  . ASN   B 20  ? 0.2268 0.2290 0.4226 -0.0209 -0.0714 0.0059  26  ASN   C CB  
1233 C CG  . ASN   B 20  ? 0.3038 0.3181 0.5298 -0.0195 -0.0621 0.0070  26  ASN   C CG  
1234 O OD1 . ASN   B 20  ? 0.3181 0.3376 0.5687 -0.0216 -0.0618 0.0091  26  ASN   C OD1 
1235 N ND2 . ASN   B 20  ? 0.3073 0.3256 0.5322 -0.0163 -0.0533 0.0052  26  ASN   C ND2 
1236 N N   . ASP   B 21  ? 0.1896 0.1896 0.3376 -0.0166 -0.0487 -0.0011 27  ASP   C N   
1237 C CA  . ASP   B 21  ? 0.1893 0.1937 0.3281 -0.0147 -0.0364 -0.0027 27  ASP   C CA  
1238 C C   . ASP   B 21  ? 0.1766 0.1813 0.3139 -0.0164 -0.0313 -0.0023 27  ASP   C C   
1239 O O   . ASP   B 21  ? 0.1857 0.1962 0.3278 -0.0172 -0.0216 -0.0019 27  ASP   C O   
1240 C CB  . ASP   B 21  ? 0.1843 0.1832 0.2995 -0.0124 -0.0366 -0.0045 27  ASP   C CB  
1241 C CG  . ASP   B 21  ? 0.2009 0.2002 0.3149 -0.0107 -0.0385 -0.0048 27  ASP   C CG  
1242 O OD1 . ASP   B 21  ? 0.1973 0.2036 0.3270 -0.0103 -0.0343 -0.0044 27  ASP   C OD1 
1243 O OD2 . ASP   B 21  ? 0.1894 0.1813 0.2874 -0.0102 -0.0439 -0.0055 27  ASP   C OD2 
1244 N N   . TRP   B 22  ? 0.1848 0.1821 0.3149 -0.0176 -0.0377 -0.0022 28  TRP   C N   
1245 C CA  . TRP   B 22  ? 0.1899 0.1865 0.3193 -0.0192 -0.0340 -0.0013 28  TRP   C CA  
1246 C C   . TRP   B 22  ? 0.1972 0.1996 0.3484 -0.0224 -0.0317 0.0009  28  TRP   C C   
1247 O O   . TRP   B 22  ? 0.1961 0.2011 0.3483 -0.0240 -0.0244 0.0022  28  TRP   C O   
1248 C CB  . TRP   B 22  ? 0.1956 0.1812 0.3122 -0.0195 -0.0407 -0.0025 28  TRP   C CB  
1249 C CG  . TRP   B 22  ? 0.1798 0.1609 0.2772 -0.0165 -0.0374 -0.0042 28  TRP   C CG  
1250 C CD1 . TRP   B 22  ? 0.1941 0.1681 0.2770 -0.0148 -0.0406 -0.0067 28  TRP   C CD1 
1251 C CD2 . TRP   B 22  ? 0.1733 0.1558 0.2655 -0.0154 -0.0306 -0.0029 28  TRP   C CD2 
1252 N NE1 . TRP   B 22  ? 0.2084 0.1804 0.2796 -0.0121 -0.0349 -0.0075 28  TRP   C NE1 
1253 C CE2 . TRP   B 22  ? 0.1938 0.1713 0.2715 -0.0124 -0.0296 -0.0048 28  TRP   C CE2 
1254 C CE3 . TRP   B 22  ? 0.1839 0.1711 0.2825 -0.0171 -0.0254 0.0002  28  TRP   C CE3 
1255 C CZ2 . TRP   B 22  ? 0.2022 0.1800 0.2751 -0.0106 -0.0246 -0.0032 28  TRP   C CZ2 
1256 C CZ3 . TRP   B 22  ? 0.1936 0.1803 0.2844 -0.0160 -0.0215 0.0020  28  TRP   C CZ3 
1257 C CH2 . TRP   B 22  ? 0.1938 0.1766 0.2737 -0.0125 -0.0214 0.0005  28  TRP   C CH2 
1258 N N   . ALA   B 23  ? 0.1770 0.1817 0.3462 -0.0235 -0.0377 0.0017  29  ALA   C N   
1259 C CA  . ALA   B 23  ? 0.1935 0.2046 0.3876 -0.0265 -0.0347 0.0040  29  ALA   C CA  
1260 C C   . ALA   B 23  ? 0.2096 0.2295 0.4142 -0.0262 -0.0212 0.0037  29  ALA   C C   
1261 O O   . ALA   B 23  ? 0.2213 0.2462 0.4440 -0.0289 -0.0143 0.0050  29  ALA   C O   
1262 C CB  . ALA   B 23  ? 0.1933 0.2044 0.4068 -0.0280 -0.0463 0.0058  29  ALA   C CB  
1263 N N   . ASN   B 24  ? 0.1851 0.2060 0.3794 -0.0233 -0.0172 0.0016  30  ASN   C N   
1264 C CA  . ASN   B 24  ? 0.1737 0.2003 0.3736 -0.0234 -0.0040 0.0003  30  ASN   C CA  
1265 C C   . ASN   B 24  ? 0.1805 0.2043 0.3540 -0.0230 0.0023  -0.0011 30  ASN   C C   
1266 O O   . ASN   B 24  ? 0.1734 0.1988 0.3418 -0.0222 0.0090  -0.0030 30  ASN   C O   
1267 C CB  . ASN   B 24  ? 0.1587 0.1887 0.3732 -0.0208 -0.0058 -0.0006 30  ASN   C CB  
1268 C CG  . ASN   B 24  ? 0.2221 0.2559 0.4675 -0.0218 -0.0117 0.0020  30  ASN   C CG  
1269 O OD1 . ASN   B 24  ? 0.2233 0.2627 0.4907 -0.0237 -0.0024 0.0024  30  ASN   C OD1 
1270 N ND2 . ASN   B 24  ? 0.2123 0.2424 0.4595 -0.0213 -0.0272 0.0040  30  ASN   C ND2 
1271 N N   . LEU   B 25  ? 0.1803 0.1998 0.3388 -0.0240 -0.0005 0.0003  31  LEU   C N   
1272 C CA  . LEU   B 25  ? 0.1799 0.1968 0.3163 -0.0238 0.0029  0.0004  31  LEU   C CA  
1273 C C   . LEU   B 25  ? 0.1976 0.2163 0.3290 -0.0275 0.0149  0.0004  31  LEU   C C   
1274 O O   . LEU   B 25  ? 0.2263 0.2457 0.3651 -0.0316 0.0213  0.0016  31  LEU   C O   
1275 C CB  . LEU   B 25  ? 0.1845 0.1963 0.3121 -0.0243 -0.0024 0.0026  31  LEU   C CB  
1276 C CG  . LEU   B 25  ? 0.1977 0.2069 0.3064 -0.0241 -0.0007 0.0041  31  LEU   C CG  
1277 C CD1 . LEU   B 25  ? 0.2093 0.2178 0.3076 -0.0200 -0.0036 0.0021  31  LEU   C CD1 
1278 C CD2 . LEU   B 25  ? 0.2132 0.2174 0.3187 -0.0245 -0.0052 0.0067  31  LEU   C CD2 
1279 N N   . VAL   B 26  ? 0.1758 0.1937 0.2924 -0.0269 0.0179  -0.0007 32  VAL   C N   
1280 C CA  . VAL   B 26  ? 0.1961 0.2127 0.3012 -0.0317 0.0279  -0.0007 32  VAL   C CA  
1281 C C   . VAL   B 26  ? 0.2143 0.2272 0.2994 -0.0332 0.0242  0.0028  32  VAL   C C   
1282 O O   . VAL   B 26  ? 0.2391 0.2488 0.3153 -0.0387 0.0280  0.0058  32  VAL   C O   
1283 C CB  . VAL   B 26  ? 0.2158 0.2335 0.3197 -0.0309 0.0339  -0.0045 32  VAL   C CB  
1284 C CG1 . VAL   B 26  ? 0.2336 0.2470 0.3187 -0.0368 0.0429  -0.0047 32  VAL   C CG1 
1285 C CG2 . VAL   B 26  ? 0.2305 0.2520 0.3583 -0.0298 0.0389  -0.0072 32  VAL   C CG2 
1286 N N   . TRP   B 27  ? 0.1802 0.1928 0.2592 -0.0288 0.0165  0.0030  33  TRP   C N   
1287 C CA  . TRP   B 27  ? 0.1821 0.1921 0.2470 -0.0294 0.0126  0.0067  33  TRP   C CA  
1288 C C   . TRP   B 27  ? 0.1730 0.1830 0.2385 -0.0233 0.0051  0.0060  33  TRP   C C   
1289 O O   . TRP   B 27  ? 0.1720 0.1833 0.2412 -0.0199 0.0038  0.0026  33  TRP   C O   
1290 C CB  . TRP   B 27  ? 0.1977 0.2067 0.2481 -0.0333 0.0173  0.0070  33  TRP   C CB  
1291 C CG  . TRP   B 27  ? 0.2095 0.2171 0.2482 -0.0337 0.0117  0.0112  33  TRP   C CG  
1292 C CD1 . TRP   B 27  ? 0.2386 0.2431 0.2695 -0.0380 0.0090  0.0170  33  TRP   C CD1 
1293 C CD2 . TRP   B 27  ? 0.2011 0.2104 0.2368 -0.0297 0.0079  0.0105  33  TRP   C CD2 
1294 N NE1 . TRP   B 27  ? 0.2464 0.2513 0.2724 -0.0365 0.0031  0.0203  33  TRP   C NE1 
1295 C CE2 . TRP   B 27  ? 0.2270 0.2350 0.2556 -0.0316 0.0031  0.0161  33  TRP   C CE2 
1296 C CE3 . TRP   B 27  ? 0.1978 0.2093 0.2370 -0.0251 0.0078  0.0062  33  TRP   C CE3 
1297 C CZ2 . TRP   B 27  ? 0.2157 0.2255 0.2420 -0.0290 -0.0007 0.0172  33  TRP   C CZ2 
1298 C CZ3 . TRP   B 27  ? 0.1997 0.2122 0.2339 -0.0228 0.0044  0.0071  33  TRP   C CZ3 
1299 C CH2 . TRP   B 27  ? 0.1964 0.2084 0.2253 -0.0245 0.0006  0.0123  33  TRP   C CH2 
1300 N N   . GLU   B 28  ? 0.1712 0.1787 0.2334 -0.0224 0.0006  0.0093  34  GLU   C N   
1301 C CA  . GLU   B 28  ? 0.1785 0.1845 0.2397 -0.0172 -0.0041 0.0084  34  GLU   C CA  
1302 C C   . GLU   B 28  ? 0.1714 0.1763 0.2281 -0.0173 -0.0062 0.0131  34  GLU   C C   
1303 O O   . GLU   B 28  ? 0.1742 0.1780 0.2304 -0.0211 -0.0065 0.0177  34  GLU   C O   
1304 C CB  . GLU   B 28  ? 0.1898 0.1921 0.2576 -0.0143 -0.0079 0.0059  34  GLU   C CB  
1305 C CG  . GLU   B 28  ? 0.1859 0.1854 0.2596 -0.0164 -0.0091 0.0082  34  GLU   C CG  
1306 C CD  . GLU   B 28  ? 0.2236 0.2195 0.2959 -0.0157 -0.0110 0.0119  34  GLU   C CD  
1307 O OE1 . GLU   B 28  ? 0.2525 0.2472 0.3277 -0.0189 -0.0110 0.0157  34  GLU   C OE1 
1308 O OE2 . GLU   B 28  ? 0.2128 0.2064 0.2823 -0.0119 -0.0123 0.0112  34  GLU   C OE2 
1309 N N   . ASP   B 29  ? 0.1625 0.1676 0.2174 -0.0135 -0.0077 0.0125  35  ASP   C N   
1310 C CA  . ASP   B 29  ? 0.1546 0.1594 0.2101 -0.0130 -0.0099 0.0175  35  ASP   C CA  
1311 C C   . ASP   B 29  ? 0.1583 0.1608 0.2171 -0.0073 -0.0100 0.0149  35  ASP   C C   
1312 O O   . ASP   B 29  ? 0.1525 0.1565 0.2077 -0.0053 -0.0087 0.0122  35  ASP   C O   
1313 C CB  . ASP   B 29  ? 0.1588 0.1671 0.2073 -0.0169 -0.0099 0.0210  35  ASP   C CB  
1314 C CG  . ASP   B 29  ? 0.2165 0.2253 0.2681 -0.0175 -0.0140 0.0278  35  ASP   C CG  
1315 O OD1 . ASP   B 29  ? 0.2631 0.2708 0.3239 -0.0128 -0.0150 0.0284  35  ASP   C OD1 
1316 O OD2 . ASP   B 29  ? 0.2306 0.2403 0.2754 -0.0231 -0.0162 0.0326  35  ASP   C OD2 
1317 N N   . SER   B 30  ? 0.1576 0.1553 0.2226 -0.0050 -0.0109 0.0155  36  SER   C N   
1318 C CA  A SER   B 30  ? 0.1654 0.1584 0.2323 -0.0002 -0.0090 0.0122  36  SER   C CA  
1319 C CA  B SER   B 30  ? 0.1675 0.1605 0.2343 -0.0002 -0.0090 0.0121  36  SER   C CA  
1320 C C   . SER   B 30  ? 0.1745 0.1712 0.2450 0.0018  -0.0077 0.0152  36  SER   C C   
1321 O O   . SER   B 30  ? 0.1883 0.1831 0.2568 0.0049  -0.0043 0.0114  36  SER   C O   
1322 C CB  A SER   B 30  ? 0.1974 0.1834 0.2710 0.0012  -0.0094 0.0124  36  SER   C CB  
1323 C CB  B SER   B 30  ? 0.2063 0.1919 0.2794 0.0015  -0.0091 0.0118  36  SER   C CB  
1324 O OG  A SER   B 30  ? 0.2245 0.2040 0.2996 0.0055  -0.0057 0.0089  36  SER   C OG  
1325 O OG  B SER   B 30  ? 0.2372 0.2246 0.3200 0.0010  -0.0108 0.0187  36  SER   C OG  
1326 N N   . SER   B 31  ? 0.1552 0.1568 0.2308 -0.0008 -0.0107 0.0223  37  SER   C N   
1327 C CA  . SER   B 31  ? 0.1593 0.1651 0.2415 0.0005  -0.0108 0.0261  37  SER   C CA  
1328 C C   . SER   B 31  ? 0.1642 0.1739 0.2377 -0.0002 -0.0093 0.0234  37  SER   C C   
1329 O O   . SER   B 31  ? 0.1904 0.2029 0.2695 0.0017  -0.0081 0.0250  37  SER   C O   
1330 C CB  . SER   B 31  ? 0.2043 0.2134 0.2931 -0.0033 -0.0166 0.0354  37  SER   C CB  
1331 O OG  . SER   B 31  ? 0.2646 0.2766 0.3414 -0.0097 -0.0197 0.0376  37  SER   C OG  
1332 N N   . ARG   B 32  ? 0.1430 0.1530 0.2053 -0.0028 -0.0091 0.0198  38  ARG   C N   
1333 C CA  . ARG   B 32  ? 0.1436 0.1565 0.1982 -0.0035 -0.0077 0.0171  38  ARG   C CA  
1334 C C   . ARG   B 32  ? 0.1389 0.1481 0.1884 -0.0004 -0.0048 0.0102  38  ARG   C C   
1335 O O   . ARG   B 32  ? 0.1361 0.1467 0.1800 -0.0005 -0.0037 0.0080  38  ARG   C O   
1336 C CB  . ARG   B 32  ? 0.1540 0.1692 0.2003 -0.0091 -0.0088 0.0178  38  ARG   C CB  
1337 C CG  . ARG   B 32  ? 0.1644 0.1814 0.2106 -0.0140 -0.0128 0.0251  38  ARG   C CG  
1338 C CD  . ARG   B 32  ? 0.1724 0.1887 0.2067 -0.0207 -0.0122 0.0251  38  ARG   C CD  
1339 N NE  . ARG   B 32  ? 0.1565 0.1742 0.1839 -0.0214 -0.0098 0.0213  38  ARG   C NE  
1340 C CZ  . ARG   B 32  ? 0.1678 0.1840 0.1839 -0.0277 -0.0091 0.0217  38  ARG   C CZ  
1341 N NH1 . ARG   B 32  ? 0.2005 0.2136 0.2090 -0.0345 -0.0113 0.0263  38  ARG   C NH1 
1342 N NH2 . ARG   B 32  ? 0.1782 0.1949 0.1892 -0.0279 -0.0069 0.0181  38  ARG   C NH2 
1343 N N   . ASP   B 33  ? 0.1519 0.1552 0.2019 0.0014  -0.0044 0.0072  39  ASP   C N   
1344 C CA  . ASP   B 33  ? 0.1461 0.1441 0.1893 0.0026  -0.0040 0.0015  39  ASP   C CA  
1345 C C   . ASP   B 33  ? 0.1396 0.1407 0.1797 0.0001  -0.0057 0.0002  39  ASP   C C   
1346 O O   . ASP   B 33  ? 0.1431 0.1421 0.1783 0.0007  -0.0062 -0.0029 39  ASP   C O   
1347 C CB  . ASP   B 33  ? 0.1487 0.1429 0.1868 0.0053  -0.0008 -0.0012 39  ASP   C CB  
1348 C CG  . ASP   B 33  ? 0.1584 0.1445 0.1864 0.0053  -0.0019 -0.0062 39  ASP   C CG  
1349 O OD1 . ASP   B 33  ? 0.1781 0.1581 0.2049 0.0047  -0.0043 -0.0082 39  ASP   C OD1 
1350 O OD2 . ASP   B 33  ? 0.1734 0.1582 0.1941 0.0055  -0.0009 -0.0079 39  ASP   C OD2 
1351 N N   . LEU   B 34  ? 0.1301 0.1351 0.1735 -0.0031 -0.0062 0.0026  40  LEU   C N   
1352 C CA  . LEU   B 34  ? 0.1299 0.1372 0.1732 -0.0053 -0.0058 0.0007  40  LEU   C CA  
1353 C C   . LEU   B 34  ? 0.1409 0.1471 0.1902 -0.0070 -0.0066 0.0003  40  LEU   C C   
1354 O O   . LEU   B 34  ? 0.1490 0.1546 0.2009 -0.0084 -0.0068 0.0029  40  LEU   C O   
1355 C CB  . LEU   B 34  ? 0.1445 0.1563 0.1847 -0.0087 -0.0033 0.0027  40  LEU   C CB  
1356 C CG  . LEU   B 34  ? 0.1432 0.1567 0.1783 -0.0081 -0.0028 0.0029  40  LEU   C CG  
1357 C CD1 . LEU   B 34  ? 0.1567 0.1725 0.1867 -0.0130 -0.0009 0.0046  40  LEU   C CD1 
1358 C CD2 . LEU   B 34  ? 0.1462 0.1583 0.1802 -0.0056 -0.0028 -0.0011 40  LEU   C CD2 
1359 N N   . LEU   B 35  ? 0.1263 0.1331 0.1797 -0.0074 -0.0069 -0.0023 41  LEU   C N   
1360 C CA  . LEU   B 35  ? 0.1354 0.1428 0.1981 -0.0096 -0.0068 -0.0023 41  LEU   C CA  
1361 C C   . LEU   B 35  ? 0.1274 0.1384 0.1965 -0.0108 -0.0036 -0.0041 41  LEU   C C   
1362 O O   . LEU   B 35  ? 0.1475 0.1585 0.2155 -0.0089 -0.0049 -0.0058 41  LEU   C O   
1363 C CB  . LEU   B 35  ? 0.1514 0.1537 0.2177 -0.0083 -0.0124 -0.0036 41  LEU   C CB  
1364 C CG  . LEU   B 35  ? 0.1491 0.1522 0.2278 -0.0107 -0.0134 -0.0032 41  LEU   C CG  
1365 C CD1 . LEU   B 35  ? 0.1671 0.1634 0.2455 -0.0106 -0.0187 -0.0033 41  LEU   C CD1 
1366 C CD2 . LEU   B 35  ? 0.1743 0.1798 0.2642 -0.0109 -0.0153 -0.0046 41  LEU   C CD2 
1367 N N   . VAL   B 36  ? 0.1241 0.1376 0.1994 -0.0141 0.0015  -0.0036 42  VAL   C N   
1368 C CA  . VAL   B 36  ? 0.1309 0.1471 0.2151 -0.0153 0.0070  -0.0058 42  VAL   C CA  
1369 C C   . VAL   B 36  ? 0.1426 0.1601 0.2435 -0.0165 0.0073  -0.0057 42  VAL   C C   
1370 O O   . VAL   B 36  ? 0.1522 0.1691 0.2535 -0.0190 0.0085  -0.0038 42  VAL   C O   
1371 C CB  . VAL   B 36  ? 0.1493 0.1658 0.2244 -0.0195 0.0155  -0.0058 42  VAL   C CB  
1372 C CG1 . VAL   B 36  ? 0.1707 0.1885 0.2561 -0.0209 0.0237  -0.0091 42  VAL   C CG1 
1373 C CG2 . VAL   B 36  ? 0.1529 0.1683 0.2132 -0.0188 0.0138  -0.0053 42  VAL   C CG2 
1374 N N   . SER   B 37  ? 0.1421 0.1615 0.2581 -0.0148 0.0056  -0.0071 43  SER   C N   
1375 C CA  . SER   B 37  ? 0.1531 0.1749 0.2899 -0.0160 0.0055  -0.0065 43  SER   C CA  
1376 C C   . SER   B 37  ? 0.1734 0.1990 0.3264 -0.0166 0.0146  -0.0086 43  SER   C C   
1377 O O   . SER   B 37  ? 0.1715 0.1968 0.3195 -0.0155 0.0186  -0.0106 43  SER   C O   
1378 C CB  . SER   B 37  ? 0.1611 0.1808 0.3051 -0.0139 -0.0067 -0.0054 43  SER   C CB  
1379 O OG  . SER   B 37  ? 0.1821 0.2009 0.3262 -0.0113 -0.0114 -0.0061 43  SER   C OG  
1380 N N   . SER   B 38  ? 0.1817 0.2104 0.3553 -0.0185 0.0188  -0.0081 44  SER   C N   
1381 C CA  . SER   B 38  ? 0.2001 0.2320 0.3926 -0.0190 0.0296  -0.0103 44  SER   C CA  
1382 C C   . SER   B 38  ? 0.2134 0.2484 0.4306 -0.0155 0.0218  -0.0093 44  SER   C C   
1383 O O   . SER   B 38  ? 0.2148 0.2496 0.4381 -0.0145 0.0087  -0.0062 44  SER   C O   
1384 C CB  . SER   B 38  ? 0.2205 0.2542 0.4250 -0.0231 0.0400  -0.0102 44  SER   C CB  
1385 O OG  . SER   B 38  ? 0.2720 0.3081 0.4920 -0.0232 0.0311  -0.0069 44  SER   C OG  
1386 N N   . THR   B 39  ? 0.2302 0.2667 0.4607 -0.0141 0.0295  -0.0117 45  THR   C N   
1387 C CA  . THR   B 39  ? 0.2544 0.2937 0.5111 -0.0108 0.0223  -0.0099 45  THR   C CA  
1388 C C   . THR   B 39  ? 0.2928 0.3367 0.5820 -0.0111 0.0352  -0.0114 45  THR   C C   
1389 O O   . THR   B 39  ? 0.3013 0.3440 0.5855 -0.0136 0.0519  -0.0155 45  THR   C O   
1390 C CB  . THR   B 39  ? 0.2706 0.3067 0.5150 -0.0079 0.0198  -0.0114 45  THR   C CB  
1391 O OG1 . THR   B 39  ? 0.2894 0.3241 0.5291 -0.0088 0.0359  -0.0161 45  THR   C OG1 
1392 C CG2 . THR   B 39  ? 0.2869 0.3182 0.4990 -0.0076 0.0105  -0.0106 45  THR   C CG2 
1393 N N   . THR   B 40  ? 0.3146 0.3628 0.6368 -0.0088 0.0278  -0.0081 46  THR   C N   
1394 C CA  . THR   B 40  ? 0.3364 0.3895 0.6956 -0.0082 0.0404  -0.0093 46  THR   C CA  
1395 C C   . THR   B 40  ? 0.3515 0.4023 0.7154 -0.0051 0.0470  -0.0125 46  THR   C C   
1396 O O   . THR   B 40  ? 0.3716 0.4227 0.7507 -0.0053 0.0651  -0.0169 46  THR   C O   
1397 C CB  . THR   B 40  ? 0.3620 0.4213 0.7592 -0.0077 0.0288  -0.0033 46  THR   C CB  
1398 O OG1 . THR   B 40  ? 0.4011 0.4582 0.7952 -0.0057 0.0078  0.0015  46  THR   C OG1 
1399 C CG2 . THR   B 40  ? 0.3743 0.4357 0.7715 -0.0115 0.0271  -0.0013 46  THR   C CG2 
1400 N N   . ALA   B 41  ? 0.3404 0.3880 0.6904 -0.0025 0.0335  -0.0105 47  ALA   C N   
1401 C CA  . ALA   B 41  ? 0.3400 0.3849 0.6938 0.0004  0.0380  -0.0129 47  ALA   C CA  
1402 C C   . ALA   B 41  ? 0.3493 0.3879 0.6664 -0.0012 0.0490  -0.0189 47  ALA   C C   
1403 O O   . ALA   B 41  ? 0.3533 0.3895 0.6386 -0.0036 0.0456  -0.0190 47  ALA   C O   
1404 C CB  . ALA   B 41  ? 0.3440 0.3875 0.7000 0.0031  0.0180  -0.0073 47  ALA   C CB  
1405 N N   . GLN   B 42  ? 0.3400 0.3754 0.6625 -0.0002 0.0611  -0.0234 48  GLN   C N   
1406 C CA  . GLN   B 42  ? 0.3532 0.3816 0.6429 -0.0026 0.0715  -0.0291 48  GLN   C CA  
1407 C C   . GLN   B 42  ? 0.3423 0.3674 0.6090 -0.0008 0.0583  -0.0271 48  GLN   C C   
1408 O O   . GLN   B 42  ? 0.3467 0.3721 0.6290 0.0029  0.0497  -0.0243 48  GLN   C O   
1409 C CB  . GLN   B 42  ? 0.3888 0.4133 0.6944 -0.0027 0.0908  -0.0354 48  GLN   C CB  
1410 C CG  . GLN   B 42  ? 0.4769 0.4922 0.7493 -0.0060 0.1010  -0.0415 48  GLN   C CG  
1411 C CD  . GLN   B 42  ? 0.5826 0.5934 0.8276 -0.0127 0.1128  -0.0452 48  GLN   C CD  
1412 O OE1 . GLN   B 42  ? 0.6039 0.6180 0.8577 -0.0150 0.1179  -0.0444 48  GLN   C OE1 
1413 N NE2 . GLN   B 42  ? 0.6136 0.6161 0.8245 -0.0167 0.1166  -0.0488 48  GLN   C NE2 
1414 N N   . GLY   B 43  ? 0.3130 0.3349 0.5441 -0.0037 0.0570  -0.0280 49  GLY   C N   
1415 C CA  . GLY   B 43  ? 0.2940 0.3128 0.5021 -0.0026 0.0468  -0.0265 49  GLY   C CA  
1416 C C   . GLY   B 43  ? 0.2834 0.2961 0.4783 -0.0040 0.0573  -0.0316 49  GLY   C C   
1417 O O   . GLY   B 43  ? 0.3033 0.3124 0.4914 -0.0079 0.0720  -0.0366 49  GLY   C O   
1418 N N   . CYS   B 44  ? 0.2591 0.2695 0.4489 -0.0018 0.0500  -0.0304 50  CYS   C N   
1419 C CA  . CYS   B 44  ? 0.2615 0.2655 0.4405 -0.0031 0.0585  -0.0349 50  CYS   C CA  
1420 C C   . CYS   B 44  ? 0.2499 0.2511 0.3981 -0.0049 0.0524  -0.0341 50  CYS   C C   
1421 O O   . CYS   B 44  ? 0.2630 0.2589 0.4046 -0.0055 0.0559  -0.0367 50  CYS   C O   
1422 C CB  . CYS   B 44  ? 0.2894 0.2921 0.4946 0.0009  0.0585  -0.0350 50  CYS   C CB  
1423 S SG  . CYS   B 44  ? 0.3386 0.3447 0.5866 0.0032  0.0683  -0.0363 50  CYS   C SG  
1424 N N   . ASP   B 45  ? 0.2053 0.2094 0.3365 -0.0057 0.0436  -0.0304 51  ASP   C N   
1425 C CA  . ASP   B 45  ? 0.2104 0.2124 0.3160 -0.0074 0.0390  -0.0294 51  ASP   C CA  
1426 C C   . ASP   B 45  ? 0.2310 0.2287 0.3178 -0.0132 0.0491  -0.0333 51  ASP   C C   
1427 O O   . ASP   B 45  ? 0.2638 0.2612 0.3505 -0.0163 0.0568  -0.0352 51  ASP   C O   
1428 C CB  . ASP   B 45  ? 0.2262 0.2319 0.3210 -0.0065 0.0281  -0.0247 51  ASP   C CB  
1429 C CG  . ASP   B 45  ? 0.3052 0.3122 0.4102 -0.0025 0.0166  -0.0207 51  ASP   C CG  
1430 O OD1 . ASP   B 45  ? 0.3317 0.3366 0.4474 -0.0005 0.0143  -0.0203 51  ASP   C OD1 
1431 O OD2 . ASP   B 45  ? 0.3151 0.3239 0.4165 -0.0019 0.0095  -0.0178 51  ASP   C OD2 
1432 N N   . THR   B 46  ? 0.2301 0.2237 0.3010 -0.0154 0.0490  -0.0343 52  THR   C N   
1433 C CA  . THR   B 46  ? 0.2567 0.2447 0.3062 -0.0222 0.0559  -0.0370 52  THR   C CA  
1434 C C   . THR   B 46  ? 0.2309 0.2223 0.2632 -0.0238 0.0468  -0.0321 52  THR   C C   
1435 O O   . THR   B 46  ? 0.2363 0.2305 0.2675 -0.0208 0.0384  -0.0289 52  THR   C O   
1436 C CB  . THR   B 46  ? 0.3099 0.2908 0.3527 -0.0242 0.0598  -0.0406 52  THR   C CB  
1437 O OG1 . THR   B 46  ? 0.3491 0.3255 0.4091 -0.0230 0.0706  -0.0459 52  THR   C OG1 
1438 C CG2 . THR   B 46  ? 0.3289 0.3029 0.3451 -0.0323 0.0630  -0.0422 52  THR   C CG2 
1439 N N   . ILE   B 47  ? 0.2240 0.2143 0.2434 -0.0288 0.0490  -0.0313 53  ILE   C N   
1440 C CA  . ILE   B 47  ? 0.2084 0.2016 0.2145 -0.0306 0.0406  -0.0262 53  ILE   C CA  
1441 C C   . ILE   B 47  ? 0.2206 0.2082 0.2076 -0.0370 0.0406  -0.0263 53  ILE   C C   
1442 O O   . ILE   B 47  ? 0.2227 0.2018 0.1981 -0.0435 0.0486  -0.0303 53  ILE   C O   
1443 C CB  . ILE   B 47  ? 0.2164 0.2110 0.2194 -0.0332 0.0412  -0.0240 53  ILE   C CB  
1444 C CG1 . ILE   B 47  ? 0.2408 0.2400 0.2631 -0.0282 0.0422  -0.0243 53  ILE   C CG1 
1445 C CG2 . ILE   B 47  ? 0.2087 0.2067 0.2023 -0.0341 0.0319  -0.0179 53  ILE   C CG2 
1446 C CD1 . ILE   B 47  ? 0.2607 0.2658 0.2937 -0.0213 0.0324  -0.0211 53  ILE   C CD1 
1447 N N   . ALA   B 48  ? 0.2030 0.1939 0.1860 -0.0360 0.0321  -0.0221 54  ALA   C N   
1448 C CA  . ALA   B 48  ? 0.1958 0.1823 0.1626 -0.0424 0.0298  -0.0210 54  ALA   C CA  
1449 C C   . ALA   B 48  ? 0.2024 0.1861 0.1546 -0.0498 0.0280  -0.0178 54  ALA   C C   
1450 O O   . ALA   B 48  ? 0.1969 0.1856 0.1534 -0.0480 0.0245  -0.0138 54  ALA   C O   
1451 C CB  . ALA   B 48  ? 0.1797 0.1724 0.1507 -0.0388 0.0211  -0.0162 54  ALA   C CB  
1452 N N   . ARG   B 49  ? 0.2115 0.1860 0.1448 -0.0589 0.0297  -0.0191 55  ARG   C N   
1453 C CA  . ARG   B 49  ? 0.2170 0.1866 0.1327 -0.0678 0.0262  -0.0149 55  ARG   C CA  
1454 C C   . ARG   B 49  ? 0.2266 0.1934 0.1311 -0.0735 0.0181  -0.0115 55  ARG   C C   
1455 O O   . ARG   B 49  ? 0.2648 0.2206 0.1528 -0.0811 0.0217  -0.0155 55  ARG   C O   
1456 C CB  . ARG   B 49  ? 0.2337 0.1912 0.1340 -0.0753 0.0375  -0.0207 55  ARG   C CB  
1457 C CG  . ARG   B 49  ? 0.2491 0.2098 0.1648 -0.0694 0.0466  -0.0245 55  ARG   C CG  
1458 C CD  . ARG   B 49  ? 0.2675 0.2371 0.1932 -0.0655 0.0405  -0.0185 55  ARG   C CD  
1459 N NE  . ARG   B 49  ? 0.2624 0.2348 0.2038 -0.0605 0.0490  -0.0223 55  ARG   C NE  
1460 C CZ  . ARG   B 49  ? 0.2737 0.2539 0.2285 -0.0553 0.0452  -0.0188 55  ARG   C CZ  
1461 N NH1 . ARG   B 49  ? 0.2342 0.2201 0.1896 -0.0537 0.0344  -0.0121 55  ARG   C NH1 
1462 N NH2 . ARG   B 49  ? 0.2845 0.2668 0.2542 -0.0518 0.0523  -0.0220 55  ARG   C NH2 
1463 N N   . CYS   B 50  ? 0.2191 0.1953 0.1332 -0.0704 0.0074  -0.0040 56  CYS   C N   
1464 C CA  . CYS   B 50  ? 0.2209 0.1975 0.1321 -0.0739 -0.0005 -0.0002 56  CYS   C CA  
1465 C C   . CYS   B 50  ? 0.2214 0.2085 0.1458 -0.0710 -0.0111 0.0090  56  CYS   C C   
1466 O O   . CYS   B 50  ? 0.2188 0.2122 0.1543 -0.0655 -0.0113 0.0113  56  CYS   C O   
1467 C CB  . CYS   B 50  ? 0.2293 0.2075 0.1495 -0.0681 0.0035  -0.0050 56  CYS   C CB  
1468 S SG  . CYS   B 50  ? 0.2001 0.1914 0.1454 -0.0547 0.0034  -0.0037 56  CYS   C SG  
1469 N N   . ASP   B 51  ? 0.2239 0.2133 0.1502 -0.0739 -0.0190 0.0138  57  ASP   C N   
1470 C CA  . ASP   B 51  ? 0.2398 0.2399 0.1839 -0.0702 -0.0273 0.0222  57  ASP   C CA  
1471 C C   . ASP   B 51  ? 0.2300 0.2366 0.1880 -0.0642 -0.0263 0.0215  57  ASP   C C   
1472 O O   . ASP   B 51  ? 0.2285 0.2415 0.1984 -0.0643 -0.0330 0.0281  57  ASP   C O   
1473 C CB  . ASP   B 51  ? 0.2847 0.2827 0.2226 -0.0800 -0.0392 0.0310  57  ASP   C CB  
1474 C CG  . ASP   B 51  ? 0.3303 0.3212 0.2550 -0.0892 -0.0438 0.0312  57  ASP   C CG  
1475 O OD1 . ASP   B 51  ? 0.3478 0.3348 0.2676 -0.0878 -0.0368 0.0239  57  ASP   C OD1 
1476 O OD2 . ASP   B 51  ? 0.4093 0.3981 0.3292 -0.0981 -0.0554 0.0392  57  ASP   C OD2 
1477 N N   . CYS   B 52  ? 0.2125 0.2174 0.1707 -0.0589 -0.0180 0.0141  58  CYS   C N   
1478 C CA  . CYS   B 52  ? 0.1905 0.2003 0.1601 -0.0533 -0.0167 0.0137  58  CYS   C CA  
1479 C C   . CYS   B 52  ? 0.1736 0.1932 0.1611 -0.0466 -0.0184 0.0186  58  CYS   C C   
1480 O O   . CYS   B 52  ? 0.1645 0.1867 0.1570 -0.0427 -0.0173 0.0192  58  CYS   C O   
1481 C CB  . CYS   B 52  ? 0.1898 0.1961 0.1587 -0.0480 -0.0086 0.0061  58  CYS   C CB  
1482 S SG  . CYS   B 52  ? 0.2192 0.2137 0.1724 -0.0544 -0.0041 -0.0007 58  CYS   C SG  
1483 N N   . GLN   B 53  ? 0.1601 0.1841 0.1571 -0.0454 -0.0198 0.0215  59  GLN   C N   
1484 C CA  . GLN   B 53  ? 0.1588 0.1906 0.1728 -0.0388 -0.0184 0.0248  59  GLN   C CA  
1485 C C   . GLN   B 53  ? 0.1429 0.1743 0.1590 -0.0345 -0.0128 0.0215  59  GLN   C C   
1486 O O   . GLN   B 53  ? 0.1497 0.1861 0.1780 -0.0308 -0.0107 0.0243  59  GLN   C O   
1487 C CB  . GLN   B 53  ? 0.1622 0.2006 0.1899 -0.0420 -0.0251 0.0333  59  GLN   C CB  
1488 C CG  . GLN   B 53  ? 0.1869 0.2262 0.2159 -0.0446 -0.0309 0.0380  59  GLN   C CG  
1489 C CD  . GLN   B 53  ? 0.2014 0.2477 0.2482 -0.0474 -0.0386 0.0475  59  GLN   C CD  
1490 O OE1 . GLN   B 53  ? 0.2389 0.2833 0.2811 -0.0561 -0.0483 0.0529  59  GLN   C OE1 
1491 N NE2 . GLN   B 53  ? 0.1844 0.2380 0.2523 -0.0407 -0.0346 0.0499  59  GLN   C NE2 
1492 N N   . THR   B 54  ? 0.1503 0.1750 0.1550 -0.0352 -0.0101 0.0158  60  THR   C N   
1493 C CA  . THR   B 54  ? 0.1615 0.1844 0.1670 -0.0312 -0.0057 0.0131  60  THR   C CA  
1494 C C   . THR   B 54  ? 0.1656 0.1826 0.1639 -0.0282 -0.0023 0.0070  60  THR   C C   
1495 O O   . THR   B 54  ? 0.1838 0.1969 0.1753 -0.0311 -0.0023 0.0040  60  THR   C O   
1496 C CB  . THR   B 54  ? 0.2250 0.2462 0.2292 -0.0352 -0.0069 0.0140  60  THR   C CB  
1497 O OG1 . THR   B 54  ? 0.2740 0.2881 0.2666 -0.0402 -0.0079 0.0101  60  THR   C OG1 
1498 C CG2 . THR   B 54  ? 0.2421 0.2698 0.2565 -0.0389 -0.0112 0.0207  60  THR   C CG2 
1499 N N   . GLY   B 55  ? 0.1461 0.1620 0.1464 -0.0229 0.0005  0.0056  61  GLY   C N   
1500 C CA  . GLY   B 55  ? 0.1517 0.1627 0.1489 -0.0200 0.0021  0.0012  61  GLY   C CA  
1501 C C   . GLY   B 55  ? 0.1331 0.1416 0.1305 -0.0159 0.0031  0.0013  61  GLY   C C   
1502 O O   . GLY   B 55  ? 0.1486 0.1579 0.1465 -0.0159 0.0040  0.0038  61  GLY   C O   
1503 N N   . VAL   B 56  ? 0.1360 0.1407 0.1329 -0.0131 0.0026  -0.0014 62  VAL   C N   
1504 C CA  . VAL   B 56  ? 0.1295 0.1293 0.1237 -0.0105 0.0017  -0.0010 62  VAL   C CA  
1505 C C   . VAL   B 56  ? 0.1426 0.1416 0.1373 -0.0078 0.0005  -0.0021 62  VAL   C C   
1506 O O   . VAL   B 56  ? 0.1397 0.1399 0.1389 -0.0075 -0.0001 -0.0041 62  VAL   C O   
1507 C CB  . VAL   B 56  ? 0.1423 0.1366 0.1369 -0.0108 -0.0001 -0.0021 62  VAL   C CB  
1508 C CG1 . VAL   B 56  ? 0.1659 0.1536 0.1565 -0.0090 -0.0033 -0.0007 62  VAL   C CG1 
1509 C CG2 . VAL   B 56  ? 0.1667 0.1606 0.1602 -0.0139 0.0011  -0.0012 62  VAL   C CG2 
1510 N N   . TYR   B 57  ? 0.1382 0.1342 0.1279 -0.0063 0.0007  -0.0011 63  TYR   C N   
1511 C CA  . TYR   B 57  ? 0.1418 0.1352 0.1305 -0.0044 -0.0013 -0.0024 63  TYR   C CA  
1512 C C   . TYR   B 57  ? 0.1512 0.1353 0.1316 -0.0045 -0.0050 -0.0020 63  TYR   C C   
1513 O O   . TYR   B 57  ? 0.1599 0.1391 0.1326 -0.0058 -0.0044 -0.0004 63  TYR   C O   
1514 C CB  . TYR   B 57  ? 0.1447 0.1408 0.1336 -0.0033 0.0020  -0.0022 63  TYR   C CB  
1515 C CG  . TYR   B 57  ? 0.1439 0.1351 0.1252 -0.0032 0.0058  -0.0015 63  TYR   C CG  
1516 C CD1 . TYR   B 57  ? 0.1650 0.1589 0.1477 -0.0042 0.0102  0.0005  63  TYR   C CD1 
1517 C CD2 . TYR   B 57  ? 0.1643 0.1477 0.1372 -0.0025 0.0059  -0.0030 63  TYR   C CD2 
1518 C CE1 . TYR   B 57  ? 0.1895 0.1788 0.1667 -0.0041 0.0161  0.0007  63  TYR   C CE1 
1519 C CE2 . TYR   B 57  ? 0.1959 0.1727 0.1598 -0.0030 0.0116  -0.0033 63  TYR   C CE2 
1520 C CZ  . TYR   B 57  ? 0.2033 0.1834 0.1700 -0.0036 0.0175  -0.0015 63  TYR   C CZ  
1521 O OH  . TYR   B 57  ? 0.2280 0.2016 0.1873 -0.0042 0.0254  -0.0020 63  TYR   C OH  
1522 N N   . TYR   B 58  ? 0.1521 0.1332 0.1338 -0.0036 -0.0096 -0.0029 64  TYR   C N   
1523 C CA  . TYR   B 58  ? 0.1643 0.1354 0.1373 -0.0047 -0.0154 -0.0017 64  TYR   C CA  
1524 C C   . TYR   B 58  ? 0.1861 0.1510 0.1464 -0.0054 -0.0135 -0.0026 64  TYR   C C   
1525 O O   . TYR   B 58  ? 0.1894 0.1570 0.1532 -0.0041 -0.0121 -0.0043 64  TYR   C O   
1526 C CB  . TYR   B 58  ? 0.1786 0.1492 0.1619 -0.0042 -0.0226 -0.0015 64  TYR   C CB  
1527 C CG  . TYR   B 58  ? 0.2055 0.1649 0.1794 -0.0064 -0.0311 0.0009  64  TYR   C CG  
1528 C CD1 . TYR   B 58  ? 0.2247 0.1775 0.1919 -0.0084 -0.0346 0.0039  64  TYR   C CD1 
1529 C CD2 . TYR   B 58  ? 0.2447 0.1992 0.2152 -0.0073 -0.0364 0.0008  64  TYR   C CD2 
1530 C CE1 . TYR   B 58  ? 0.2505 0.1911 0.2063 -0.0117 -0.0437 0.0071  64  TYR   C CE1 
1531 C CE2 . TYR   B 58  ? 0.2648 0.2070 0.2236 -0.0108 -0.0457 0.0035  64  TYR   C CE2 
1532 C CZ  . TYR   B 58  ? 0.2766 0.2119 0.2281 -0.0131 -0.0497 0.0069  64  TYR   C CZ  
1533 O OH  . TYR   B 58  ? 0.3286 0.2502 0.2664 -0.0177 -0.0604 0.0107  64  TYR   C OH  
1534 N N   . CYS   B 59  ? 0.1951 0.1499 0.1397 -0.0078 -0.0131 -0.0016 65  CYS   C N   
1535 C CA  . CYS   B 59  ? 0.2000 0.1454 0.1290 -0.0094 -0.0097 -0.0032 65  CYS   C CA  
1536 C C   . CYS   B 59  ? 0.2379 0.1688 0.1514 -0.0133 -0.0189 -0.0020 65  CYS   C C   
1537 O O   . CYS   B 59  ? 0.2624 0.1845 0.1635 -0.0166 -0.0217 0.0005  65  CYS   C O   
1538 C CB  . CYS   B 59  ? 0.2077 0.1514 0.1292 -0.0103 -0.0003 -0.0031 65  CYS   C CB  
1539 S SG  . CYS   B 59  ? 0.2703 0.1993 0.1706 -0.0128 0.0073  -0.0060 65  CYS   C SG  
1540 N N   . SER   B 60  ? 0.2390 0.1669 0.1528 -0.0135 -0.0242 -0.0033 66  SER   C N   
1541 C CA  . SER   B 60  ? 0.2852 0.1998 0.1862 -0.0179 -0.0353 -0.0013 66  SER   C CA  
1542 C C   . SER   B 60  ? 0.3123 0.2092 0.1843 -0.0233 -0.0332 -0.0019 66  SER   C C   
1543 O O   . SER   B 60  ? 0.3456 0.2307 0.2040 -0.0282 -0.0425 0.0017  66  SER   C O   
1544 C CB  . SER   B 60  ? 0.3405 0.2558 0.2491 -0.0175 -0.0417 -0.0024 66  SER   C CB  
1545 O OG  . SER   B 60  ? 0.4344 0.3472 0.3361 -0.0169 -0.0341 -0.0066 66  SER   C OG  
1546 N N   . SER   B 61  ? 0.3004 0.1951 0.1637 -0.0227 -0.0206 -0.0059 67  SER   C N   
1547 C CA  . SER   B 61  ? 0.3309 0.2071 0.1650 -0.0282 -0.0150 -0.0076 67  SER   C CA  
1548 C C   . SER   B 61  ? 0.3534 0.2255 0.1777 -0.0309 -0.0120 -0.0047 67  SER   C C   
1549 O O   . SER   B 61  ? 0.3845 0.2393 0.1819 -0.0367 -0.0080 -0.0055 67  SER   C O   
1550 C CB  . SER   B 61  ? 0.3356 0.2104 0.1670 -0.0263 -0.0009 -0.0130 67  SER   C CB  
1551 O OG  . SER   B 61  ? 0.3126 0.2024 0.1629 -0.0212 0.0098  -0.0132 67  SER   C OG  
1552 N N   . ARG   B 62  ? 0.3147 0.2006 0.1581 -0.0275 -0.0141 -0.0014 68  ARG   C N   
1553 C CA  . ARG   B 62  ? 0.3059 0.1883 0.1421 -0.0302 -0.0132 0.0021  68  ARG   C CA  
1554 C C   . ARG   B 62  ? 0.3113 0.1962 0.1574 -0.0305 -0.0273 0.0074  68  ARG   C C   
1555 O O   . ARG   B 62  ? 0.3273 0.2092 0.1696 -0.0326 -0.0287 0.0111  68  ARG   C O   
1556 C CB  . ARG   B 62  ? 0.3074 0.2034 0.1587 -0.0261 -0.0007 0.0012  68  ARG   C CB  
1557 C CG  . ARG   B 62  ? 0.3297 0.2233 0.1750 -0.0258 0.0140  -0.0029 68  ARG   C CG  
1558 C CD  . ARG   B 62  ? 0.3614 0.2365 0.1785 -0.0322 0.0204  -0.0029 68  ARG   C CD  
1559 N NE  . ARG   B 62  ? 0.4159 0.2879 0.2293 -0.0318 0.0370  -0.0074 68  ARG   C NE  
1560 C CZ  . ARG   B 62  ? 0.4707 0.3308 0.2699 -0.0334 0.0421  -0.0122 68  ARG   C CZ  
1561 N NH1 . ARG   B 62  ? 0.4731 0.3225 0.2580 -0.0364 0.0307  -0.0128 68  ARG   C NH1 
1562 N NH2 . ARG   B 62  ? 0.4898 0.3476 0.2895 -0.0324 0.0589  -0.0163 68  ARG   C NH2 
1563 N N   . ARG   B 63  ? 0.3146 0.2055 0.1765 -0.0281 -0.0371 0.0078  69  ARG   C N   
1564 C CA  . ARG   B 63  ? 0.3170 0.2125 0.1957 -0.0271 -0.0488 0.0124  69  ARG   C CA  
1565 C C   . ARG   B 63  ? 0.3200 0.2264 0.2134 -0.0239 -0.0431 0.0132  69  ARG   C C   
1566 O O   . ARG   B 63  ? 0.3406 0.2434 0.2350 -0.0255 -0.0488 0.0175  69  ARG   C O   
1567 C CB  . ARG   B 63  ? 0.3805 0.2589 0.2422 -0.0337 -0.0627 0.0179  69  ARG   C CB  
1568 C CG  . ARG   B 63  ? 0.4956 0.3715 0.3645 -0.0347 -0.0759 0.0195  69  ARG   C CG  
1569 C CD  . ARG   B 63  ? 0.6267 0.4882 0.4723 -0.0400 -0.0794 0.0178  69  ARG   C CD  
1570 N NE  . ARG   B 63  ? 0.6888 0.5600 0.5473 -0.0357 -0.0745 0.0127  69  ARG   C NE  
1571 C CZ  . ARG   B 63  ? 0.7370 0.5991 0.5847 -0.0390 -0.0795 0.0110  69  ARG   C CZ  
1572 N NH1 . ARG   B 63  ? 0.7774 0.6199 0.6002 -0.0472 -0.0906 0.0141  69  ARG   C NH1 
1573 N NH2 . ARG   B 63  ? 0.7226 0.5942 0.5835 -0.0348 -0.0740 0.0066  69  ARG   C NH2 
1574 N N   . LYS   B 64  ? 0.2889 0.2078 0.1926 -0.0198 -0.0315 0.0093  70  LYS   C N   
1575 C CA  . LYS   B 64  ? 0.2807 0.2082 0.1950 -0.0180 -0.0261 0.0099  70  LYS   C CA  
1576 C C   . LYS   B 64  ? 0.2404 0.1829 0.1730 -0.0137 -0.0199 0.0066  70  LYS   C C   
1577 O O   . LYS   B 64  ? 0.2321 0.1779 0.1653 -0.0122 -0.0161 0.0039  70  LYS   C O   
1578 C CB  . LYS   B 64  ? 0.3545 0.2769 0.2530 -0.0208 -0.0167 0.0100  70  LYS   C CB  
1579 C CG  . LYS   B 64  ? 0.4986 0.4078 0.3805 -0.0258 -0.0207 0.0143  70  LYS   C CG  
1580 C CD  . LYS   B 64  ? 0.5823 0.4875 0.4508 -0.0284 -0.0090 0.0138  70  LYS   C CD  
1581 C CE  . LYS   B 64  ? 0.6294 0.5477 0.5148 -0.0258 -0.0023 0.0139  70  LYS   C CE  
1582 N NZ  . LYS   B 64  ? 0.6744 0.5876 0.5486 -0.0293 0.0072  0.0152  70  LYS   C NZ  
1583 N N   . HIS   B 65  ? 0.2180 0.1679 0.1630 -0.0124 -0.0185 0.0071  71  HIS   C N   
1584 C CA  . HIS   B 65  ? 0.1914 0.1537 0.1497 -0.0099 -0.0125 0.0045  71  HIS   C CA  
1585 C C   . HIS   B 65  ? 0.2130 0.1783 0.1680 -0.0111 -0.0050 0.0051  71  HIS   C C   
1586 O O   . HIS   B 65  ? 0.2499 0.2100 0.1981 -0.0134 -0.0044 0.0074  71  HIS   C O   
1587 C CB  . HIS   B 65  ? 0.1822 0.1492 0.1551 -0.0088 -0.0150 0.0041  71  HIS   C CB  
1588 C CG  . HIS   B 65  ? 0.1935 0.1594 0.1754 -0.0073 -0.0212 0.0036  71  HIS   C CG  
1589 N ND1 . HIS   B 65  ? 0.2275 0.2005 0.2206 -0.0053 -0.0194 0.0008  71  HIS   C ND1 
1590 C CD2 . HIS   B 65  ? 0.2021 0.1606 0.1853 -0.0079 -0.0295 0.0064  71  HIS   C CD2 
1591 C CE1 . HIS   B 65  ? 0.2041 0.1744 0.2065 -0.0045 -0.0257 0.0016  71  HIS   C CE1 
1592 N NE2 . HIS   B 65  ? 0.2478 0.2098 0.2454 -0.0059 -0.0325 0.0052  71  HIS   C NE2 
1593 N N   . TYR   B 66  ? 0.1737 0.1475 0.1351 -0.0098 0.0006  0.0036  72  TYR   C N   
1594 C CA  . TYR   B 66  ? 0.1695 0.1478 0.1327 -0.0108 0.0072  0.0050  72  TYR   C CA  
1595 C C   . TYR   B 66  ? 0.1658 0.1546 0.1419 -0.0106 0.0076  0.0048  72  TYR   C C   
1596 O O   . TYR   B 66  ? 0.1696 0.1630 0.1515 -0.0092 0.0065  0.0033  72  TYR   C O   
1597 C CB  . TYR   B 66  ? 0.1912 0.1686 0.1508 -0.0101 0.0139  0.0044  72  TYR   C CB  
1598 C CG  . TYR   B 66  ? 0.2127 0.1773 0.1550 -0.0118 0.0159  0.0042  72  TYR   C CG  
1599 C CD1 . TYR   B 66  ? 0.2420 0.2005 0.1754 -0.0148 0.0196  0.0062  72  TYR   C CD1 
1600 C CD2 . TYR   B 66  ? 0.2448 0.2019 0.1777 -0.0114 0.0137  0.0020  72  TYR   C CD2 
1601 C CE1 . TYR   B 66  ? 0.2629 0.2075 0.1765 -0.0177 0.0221  0.0060  72  TYR   C CE1 
1602 C CE2 . TYR   B 66  ? 0.2654 0.2081 0.1783 -0.0145 0.0152  0.0016  72  TYR   C CE2 
1603 C CZ  . TYR   B 66  ? 0.2881 0.2241 0.1903 -0.0179 0.0191  0.0037  72  TYR   C CZ  
1604 O OH  . TYR   B 66  ? 0.3455 0.2651 0.2242 -0.0221 0.0212  0.0032  72  TYR   C OH  
1605 N N   . PRO   B 67  ? 0.1616 0.1533 0.1412 -0.0129 0.0090  0.0066  73  PRO   C N   
1606 C CA  . PRO   B 67  ? 0.1551 0.1550 0.1441 -0.0143 0.0086  0.0070  73  PRO   C CA  
1607 C C   . PRO   B 67  ? 0.1729 0.1794 0.1690 -0.0140 0.0124  0.0092  73  PRO   C C   
1608 O O   . PRO   B 67  ? 0.1984 0.2036 0.1940 -0.0138 0.0175  0.0108  73  PRO   C O   
1609 C CB  . PRO   B 67  ? 0.1699 0.1685 0.1590 -0.0175 0.0080  0.0085  73  PRO   C CB  
1610 C CG  . PRO   B 67  ? 0.1855 0.1781 0.1677 -0.0177 0.0107  0.0103  73  PRO   C CG  
1611 C CD  . PRO   B 67  ? 0.1771 0.1633 0.1508 -0.0152 0.0102  0.0088  73  PRO   C CD  
1612 N N   . VAL   B 68  ? 0.1583 0.1710 0.1613 -0.0140 0.0106  0.0094  74  VAL   C N   
1613 C CA  . VAL   B 68  ? 0.1656 0.1849 0.1790 -0.0134 0.0131  0.0124  74  VAL   C CA  
1614 C C   . VAL   B 68  ? 0.1434 0.1694 0.1645 -0.0166 0.0084  0.0150  74  VAL   C C   
1615 O O   . VAL   B 68  ? 0.1667 0.1912 0.1823 -0.0187 0.0044  0.0131  74  VAL   C O   
1616 C CB  . VAL   B 68  ? 0.1887 0.2065 0.2017 -0.0096 0.0154  0.0106  74  VAL   C CB  
1617 C CG1 . VAL   B 68  ? 0.2123 0.2220 0.2162 -0.0077 0.0207  0.0087  74  VAL   C CG1 
1618 C CG2 . VAL   B 68  ? 0.1996 0.2163 0.2087 -0.0091 0.0108  0.0080  74  VAL   C CG2 
1619 N N   . SER   B 69  ? 0.1355 0.1683 0.1700 -0.0174 0.0092  0.0197  75  SER   C N   
1620 C CA  . SER   B 69  ? 0.1363 0.1750 0.1791 -0.0204 0.0034  0.0236  75  SER   C CA  
1621 C C   . SER   B 69  ? 0.1379 0.1783 0.1863 -0.0165 0.0046  0.0238  75  SER   C C   
1622 O O   . SER   B 69  ? 0.1503 0.1890 0.2015 -0.0120 0.0111  0.0222  75  SER   C O   
1623 C CB  . SER   B 69  ? 0.1698 0.2156 0.2286 -0.0232 0.0021  0.0299  75  SER   C CB  
1624 O OG  . SER   B 69  ? 0.2435 0.2874 0.2976 -0.0270 0.0009  0.0299  75  SER   C OG  
1625 N N   . PHE   B 70  ? 0.1265 0.1678 0.1734 -0.0187 -0.0011 0.0249  76  PHE   C N   
1626 C CA  . PHE   B 70  ? 0.1307 0.1729 0.1826 -0.0155 -0.0005 0.0252  76  PHE   C CA  
1627 C C   . PHE   B 70  ? 0.1342 0.1812 0.1945 -0.0193 -0.0078 0.0313  76  PHE   C C   
1628 O O   . PHE   B 70  ? 0.1433 0.1905 0.1992 -0.0256 -0.0142 0.0340  76  PHE   C O   
1629 C CB  . PHE   B 70  ? 0.1334 0.1695 0.1719 -0.0134 0.0007  0.0193  76  PHE   C CB  
1630 C CG  . PHE   B 70  ? 0.1208 0.1537 0.1473 -0.0176 -0.0028 0.0169  76  PHE   C CG  
1631 C CD1 . PHE   B 70  ? 0.1249 0.1535 0.1428 -0.0183 -0.0014 0.0132  76  PHE   C CD1 
1632 C CD2 . PHE   B 70  ? 0.1297 0.1625 0.1533 -0.0207 -0.0066 0.0180  76  PHE   C CD2 
1633 C CE1 . PHE   B 70  ? 0.1363 0.1609 0.1448 -0.0217 -0.0027 0.0101  76  PHE   C CE1 
1634 C CE2 . PHE   B 70  ? 0.1341 0.1623 0.1456 -0.0248 -0.0074 0.0148  76  PHE   C CE2 
1635 C CZ  . PHE   B 70  ? 0.1349 0.1591 0.1398 -0.0251 -0.0049 0.0105  76  PHE   C CZ  
1636 N N   . SER   B 71  ? 0.1138 0.1634 0.1862 -0.0162 -0.0072 0.0341  77  SER   C N   
1637 C CA  . SER   B 71  ? 0.1348 0.1889 0.2183 -0.0199 -0.0152 0.0416  77  SER   C CA  
1638 C C   . SER   B 71  ? 0.1549 0.2049 0.2239 -0.0244 -0.0213 0.0414  77  SER   C C   
1639 O O   . SER   B 71  ? 0.1546 0.1990 0.2074 -0.0241 -0.0182 0.0349  77  SER   C O   
1640 C CB  . SER   B 71  ? 0.1445 0.2026 0.2493 -0.0147 -0.0121 0.0451  77  SER   C CB  
1641 O OG  . SER   B 71  ? 0.1587 0.2120 0.2575 -0.0102 -0.0077 0.0403  77  SER   C OG  
1642 N N   . LYS   B 72  ? 0.1603 0.2125 0.2356 -0.0291 -0.0299 0.0488  78  LYS   C N   
1643 C CA  . LYS   B 72  ? 0.1713 0.2183 0.2319 -0.0341 -0.0349 0.0493  78  LYS   C CA  
1644 C C   . LYS   B 72  ? 0.1649 0.2110 0.2297 -0.0287 -0.0313 0.0477  78  LYS   C C   
1645 O O   . LYS   B 72  ? 0.2049 0.2551 0.2885 -0.0231 -0.0289 0.0501  78  LYS   C O   
1646 C CB  . LYS   B 72  ? 0.2135 0.2618 0.2782 -0.0423 -0.0470 0.0592  78  LYS   C CB  
1647 C CG  . LYS   B 72  ? 0.2766 0.3241 0.3343 -0.0490 -0.0515 0.0604  78  LYS   C CG  
1648 C CD  . LYS   B 72  ? 0.4165 0.4596 0.4641 -0.0605 -0.0645 0.0680  78  LYS   C CD  
1649 C CE  . LYS   B 72  ? 0.5404 0.5802 0.5769 -0.0680 -0.0685 0.0677  78  LYS   C CE  
1650 N NZ  . LYS   B 72  ? 0.6363 0.6643 0.6438 -0.0796 -0.0744 0.0672  78  LYS   C NZ  
1651 N N   . PRO   B 73  ? 0.1679 0.2084 0.2170 -0.0306 -0.0304 0.0439  79  PRO   C N   
1652 C CA  . PRO   B 73  ? 0.1664 0.2057 0.2199 -0.0260 -0.0275 0.0426  79  PRO   C CA  
1653 C C   . PRO   B 73  ? 0.1819 0.2243 0.2520 -0.0261 -0.0336 0.0512  79  PRO   C C   
1654 O O   . PRO   B 73  ? 0.2168 0.2592 0.2862 -0.0330 -0.0428 0.0588  79  PRO   C O   
1655 C CB  . PRO   B 73  ? 0.1946 0.2278 0.2294 -0.0303 -0.0269 0.0388  79  PRO   C CB  
1656 C CG  . PRO   B 73  ? 0.2231 0.2534 0.2434 -0.0351 -0.0261 0.0354  79  PRO   C CG  
1657 C CD  . PRO   B 73  ? 0.1657 0.2000 0.1934 -0.0373 -0.0310 0.0404  79  PRO   C CD  
1658 N N   . SER   B 74  ? 0.1660 0.2101 0.2513 -0.0187 -0.0286 0.0502  80  SER   C N   
1659 C CA  . SER   B 74  ? 0.1815 0.2289 0.2878 -0.0176 -0.0333 0.0584  80  SER   C CA  
1660 C C   . SER   B 74  ? 0.1770 0.2221 0.2927 -0.0103 -0.0265 0.0549  80  SER   C C   
1661 O O   . SER   B 74  ? 0.1630 0.2037 0.2673 -0.0068 -0.0192 0.0464  80  SER   C O   
1662 C CB  . SER   B 74  ? 0.2468 0.3009 0.3724 -0.0171 -0.0352 0.0640  80  SER   C CB  
1663 O OG  . SER   B 74  ? 0.3132 0.3687 0.4489 -0.0097 -0.0245 0.0585  80  SER   C OG  
1664 N N   . LEU   B 75  ? 0.1639 0.2109 0.3005 -0.0086 -0.0299 0.0620  81  LEU   C N   
1665 C CA  . LEU   B 75  ? 0.1867 0.2304 0.3343 -0.0021 -0.0237 0.0593  81  LEU   C CA  
1666 C C   . LEU   B 75  ? 0.1945 0.2401 0.3585 0.0044  -0.0141 0.0564  81  LEU   C C   
1667 O O   . LEU   B 75  ? 0.2179 0.2698 0.4041 0.0047  -0.0162 0.0633  81  LEU   C O   
1668 C CB  . LEU   B 75  ? 0.1973 0.2420 0.3628 -0.0034 -0.0318 0.0693  81  LEU   C CB  
1669 C CG  . LEU   B 75  ? 0.2473 0.2869 0.3982 -0.0080 -0.0377 0.0709  81  LEU   C CG  
1670 C CD1 . LEU   B 75  ? 0.2781 0.3191 0.4447 -0.0120 -0.0494 0.0837  81  LEU   C CD1 
1671 C CD2 . LEU   B 75  ? 0.2539 0.2874 0.4000 -0.0030 -0.0296 0.0630  81  LEU   C CD2 
1672 N N   . ILE   B 76  ? 0.1836 0.2232 0.3383 0.0091  -0.0037 0.0468  82  ILE   C N   
1673 C CA  . ILE   B 76  ? 0.1970 0.2352 0.3601 0.0142  0.0077  0.0421  82  ILE   C CA  
1674 C C   . ILE   B 76  ? 0.2152 0.2443 0.3791 0.0193  0.0166  0.0358  82  ILE   C C   
1675 O O   . ILE   B 76  ? 0.1992 0.2218 0.3458 0.0187  0.0159  0.0308  82  ILE   C O   
1676 C CB  . ILE   B 76  ? 0.2328 0.2701 0.3760 0.0127  0.0110  0.0360  82  ILE   C CB  
1677 C CG1 . ILE   B 76  ? 0.2648 0.3102 0.4093 0.0075  0.0029  0.0422  82  ILE   C CG1 
1678 C CG2 . ILE   B 76  ? 0.2602 0.2923 0.4043 0.0171  0.0241  0.0296  82  ILE   C CG2 
1679 C CD1 . ILE   B 76  ? 0.3022 0.3470 0.4299 0.0056  0.0049  0.0376  82  ILE   C CD1 
1680 N N   . PHE   B 77  ? 0.2215 0.2494 0.4064 0.0241  0.0257  0.0358  83  PHE   C N   
1681 C CA  . PHE   B 77  ? 0.2460 0.2632 0.4311 0.0285  0.0355  0.0292  83  PHE   C CA  
1682 C C   . PHE   B 77  ? 0.2474 0.2543 0.4049 0.0284  0.0434  0.0185  83  PHE   C C   
1683 O O   . PHE   B 77  ? 0.2719 0.2796 0.4222 0.0277  0.0482  0.0161  83  PHE   C O   
1684 C CB  . PHE   B 77  ? 0.2630 0.2809 0.4787 0.0335  0.0456  0.0313  83  PHE   C CB  
1685 C CG  . PHE   B 77  ? 0.3034 0.3079 0.5191 0.0378  0.0578  0.0235  83  PHE   C CG  
1686 C CD1 . PHE   B 77  ? 0.3478 0.3417 0.5499 0.0393  0.0723  0.0139  83  PHE   C CD1 
1687 C CD2 . PHE   B 77  ? 0.3305 0.3312 0.5557 0.0394  0.0545  0.0254  83  PHE   C CD2 
1688 C CE1 . PHE   B 77  ? 0.3759 0.3549 0.5741 0.0421  0.0838  0.0059  83  PHE   C CE1 
1689 C CE2 . PHE   B 77  ? 0.3605 0.3472 0.5846 0.0429  0.0660  0.0177  83  PHE   C CE2 
1690 C CZ  . PHE   B 77  ? 0.3652 0.3408 0.5750 0.0441  0.0807  0.0077  83  PHE   C CZ  
1691 N N   . VAL   B 78  ? 0.2442 0.2410 0.3866 0.0285  0.0440  0.0127  84  VAL   C N   
1692 C CA  . VAL   B 78  ? 0.2631 0.2479 0.3789 0.0275  0.0493  0.0033  84  VAL   C CA  
1693 C C   . VAL   B 78  ? 0.2880 0.2587 0.4036 0.0302  0.0586  -0.0029 84  VAL   C C   
1694 O O   . VAL   B 78  ? 0.2796 0.2481 0.4023 0.0311  0.0550  -0.0016 84  VAL   C O   
1695 C CB  . VAL   B 78  ? 0.2476 0.2329 0.3427 0.0235  0.0388  0.0023  84  VAL   C CB  
1696 C CG1 . VAL   B 78  ? 0.2533 0.2260 0.3229 0.0220  0.0423  -0.0062 84  VAL   C CG1 
1697 C CG2 . VAL   B 78  ? 0.2386 0.2359 0.3336 0.0206  0.0312  0.0076  84  VAL   C CG2 
1698 N N   . GLU   B 79  ? 0.3223 0.2815 0.4255 0.0307  0.0704  -0.0103 85  GLU   C N   
1699 C CA  . GLU   B 79  ? 0.3468 0.2890 0.4441 0.0321  0.0812  -0.0180 85  GLU   C CA  
1700 C C   . GLU   B 79  ? 0.3497 0.2820 0.4267 0.0293  0.0740  -0.0221 85  GLU   C C   
1701 O O   . GLU   B 79  ? 0.3384 0.2738 0.3991 0.0257  0.0636  -0.0216 85  GLU   C O   
1702 C CB  . GLU   B 79  ? 0.4053 0.3352 0.4846 0.0308  0.0944  -0.0254 85  GLU   C CB  
1703 C CG  . GLU   B 79  ? 0.4855 0.4243 0.5837 0.0330  0.1032  -0.0220 85  GLU   C CG  
1704 C CD  . GLU   B 79  ? 0.5744 0.5092 0.6984 0.0378  0.1185  -0.0231 85  GLU   C CD  
1705 O OE1 . GLU   B 79  ? 0.5738 0.5173 0.7188 0.0398  0.1257  -0.0195 85  GLU   C OE1 
1706 O OE2 . GLU   B 79  ? 0.5925 0.5157 0.7177 0.0395  0.1234  -0.0276 85  GLU   C OE2 
1707 N N   . ALA   B 80  ? 0.3449 0.2645 0.4235 0.0307  0.0800  -0.0267 86  ALA   C N   
1708 C CA  . ALA   B 80  ? 0.3456 0.2540 0.4067 0.0278  0.0739  -0.0309 86  ALA   C CA  
1709 C C   . ALA   B 80  ? 0.3450 0.2416 0.3721 0.0225  0.0723  -0.0374 86  ALA   C C   
1710 O O   . ALA   B 80  ? 0.3597 0.2483 0.3738 0.0214  0.0815  -0.0417 86  ALA   C O   
1711 C CB  . ALA   B 80  ? 0.3630 0.2564 0.4306 0.0301  0.0840  -0.0361 86  ALA   C CB  
1712 N N   . SER   B 81  ? 0.3276 0.2223 0.3413 0.0188  0.0604  -0.0376 87  SER   C N   
1713 C CA  . SER   B 81  ? 0.3206 0.2034 0.3046 0.0132  0.0559  -0.0425 87  SER   C CA  
1714 C C   . SER   B 81  ? 0.3410 0.2137 0.3176 0.0104  0.0488  -0.0452 87  SER   C C   
1715 O O   . SER   B 81  ? 0.3523 0.2279 0.3466 0.0131  0.0487  -0.0432 87  SER   C O   
1716 C CB  . SER   B 81  ? 0.3149 0.2116 0.2960 0.0115  0.0456  -0.0375 87  SER   C CB  
1717 O OG  . SER   B 81  ? 0.2922 0.2023 0.2871 0.0119  0.0349  -0.0319 87  SER   C OG  
1718 N N   . GLU   B 82  ? 0.3548 0.2159 0.3066 0.0046  0.0417  -0.0487 88  GLU   C N   
1719 C CA  . GLU   B 82  ? 0.3705 0.2235 0.3169 0.0012  0.0330  -0.0503 88  GLU   C CA  
1720 C C   . GLU   B 82  ? 0.3634 0.2357 0.3297 0.0024  0.0215  -0.0428 88  GLU   C C   
1721 O O   . GLU   B 82  ? 0.3664 0.2361 0.3367 0.0009  0.0156  -0.0425 88  GLU   C O   
1722 C CB  . GLU   B 82  ? 0.4345 0.2702 0.3505 -0.0062 0.0266  -0.0549 88  GLU   C CB  
1723 C CG  . GLU   B 82  ? 0.5147 0.3604 0.4258 -0.0084 0.0168  -0.0505 88  GLU   C CG  
1724 C CD  . GLU   B 82  ? 0.6608 0.5032 0.5574 -0.0092 0.0230  -0.0516 88  GLU   C CD  
1725 O OE1 . GLU   B 82  ? 0.7231 0.5583 0.6002 -0.0147 0.0148  -0.0516 88  GLU   C OE1 
1726 O OE2 . GLU   B 82  ? 0.6421 0.4896 0.5484 -0.0047 0.0354  -0.0518 88  GLU   C OE2 
1727 N N   . TYR   B 83  ? 0.3528 0.2434 0.3311 0.0048  0.0194  -0.0369 89  TYR   C N   
1728 C CA  . TYR   B 83  ? 0.3483 0.2553 0.3422 0.0052  0.0106  -0.0306 89  TYR   C CA  
1729 C C   . TYR   B 83  ? 0.3270 0.2451 0.3437 0.0093  0.0137  -0.0254 89  TYR   C C   
1730 O O   . TYR   B 83  ? 0.3548 0.2805 0.3820 0.0086  0.0076  -0.0213 89  TYR   C O   
1731 C CB  . TYR   B 83  ? 0.3383 0.2561 0.3297 0.0044  0.0064  -0.0276 89  TYR   C CB  
1732 C CG  . TYR   B 83  ? 0.3413 0.2486 0.3117 0.0002  0.0022  -0.0311 89  TYR   C CG  
1733 C CD1 . TYR   B 83  ? 0.3748 0.2785 0.3399 -0.0040 -0.0084 -0.0311 89  TYR   C CD1 
1734 C CD2 . TYR   B 83  ? 0.3592 0.2604 0.3162 0.0000  0.0081  -0.0335 89  TYR   C CD2 
1735 C CE1 . TYR   B 83  ? 0.3982 0.2920 0.3450 -0.0084 -0.0144 -0.0329 89  TYR   C CE1 
1736 C CE2 . TYR   B 83  ? 0.3923 0.2831 0.3287 -0.0046 0.0031  -0.0356 89  TYR   C CE2 
1737 C CZ  . TYR   B 83  ? 0.4304 0.3171 0.3615 -0.0089 -0.0089 -0.0351 89  TYR   C CZ  
1738 O OH  . TYR   B 83  ? 0.4981 0.3742 0.4098 -0.0141 -0.0159 -0.0358 89  TYR   C OH  
1739 N N   . TYR   B 84  ? 0.2972 0.2165 0.3225 0.0131  0.0227  -0.0250 90  TYR   C N   
1740 C CA  . TYR   B 84  ? 0.2853 0.2150 0.3338 0.0166  0.0240  -0.0187 90  TYR   C CA  
1741 C C   . TYR   B 84  ? 0.3257 0.2484 0.3844 0.0206  0.0349  -0.0206 90  TYR   C C   
1742 O O   . TYR   B 84  ? 0.3218 0.2369 0.3714 0.0213  0.0435  -0.0256 90  TYR   C O   
1743 C CB  . TYR   B 84  ? 0.2630 0.2092 0.3200 0.0172  0.0216  -0.0124 90  TYR   C CB  
1744 C CG  . TYR   B 84  ? 0.2427 0.1972 0.2925 0.0138  0.0131  -0.0104 90  TYR   C CG  
1745 C CD1 . TYR   B 84  ? 0.2469 0.2018 0.2837 0.0124  0.0126  -0.0128 90  TYR   C CD1 
1746 C CD2 . TYR   B 84  ? 0.2262 0.1874 0.2827 0.0117  0.0064  -0.0059 90  TYR   C CD2 
1747 C CE1 . TYR   B 84  ? 0.2301 0.1926 0.2636 0.0097  0.0060  -0.0109 90  TYR   C CE1 
1748 C CE2 . TYR   B 84  ? 0.2067 0.1751 0.2585 0.0088  0.0010  -0.0045 90  TYR   C CE2 
1749 C CZ  . TYR   B 84  ? 0.2200 0.1892 0.2615 0.0080  0.0008  -0.0071 90  TYR   C CZ  
1750 O OH  . TYR   B 84  ? 0.2083 0.1840 0.2479 0.0055  -0.0037 -0.0060 90  TYR   C OH  
1751 N N   . PRO   B 85  ? 0.3491 0.2748 0.4289 0.0234  0.0354  -0.0161 91  PRO   C N   
1752 C CA  . PRO   B 85  ? 0.3571 0.2791 0.4535 0.0280  0.0464  -0.0166 91  PRO   C CA  
1753 C C   . PRO   B 85  ? 0.3481 0.2839 0.4570 0.0300  0.0481  -0.0111 91  PRO   C C   
1754 O O   . PRO   B 85  ? 0.3304 0.2783 0.4353 0.0275  0.0395  -0.0064 91  PRO   C O   
1755 C CB  . PRO   B 85  ? 0.3591 0.2827 0.4768 0.0299  0.0430  -0.0110 91  PRO   C CB  
1756 C CG  . PRO   B 85  ? 0.3586 0.2941 0.4748 0.0263  0.0302  -0.0042 91  PRO   C CG  
1757 C CD  . PRO   B 85  ? 0.3507 0.2848 0.4422 0.0222  0.0261  -0.0090 91  PRO   C CD  
1758 N N   . ALA   B 86  ? 0.3433 0.2779 0.4689 0.0341  0.0588  -0.0112 92  ALA   C N   
1759 C CA  . ALA   B 86  ? 0.3425 0.2909 0.4847 0.0358  0.0597  -0.0049 92  ALA   C CA  
1760 C C   . ALA   B 86  ? 0.3203 0.2834 0.4798 0.0349  0.0468  0.0063  92  ALA   C C   
1761 O O   . ALA   B 86  ? 0.3317 0.2932 0.5026 0.0355  0.0426  0.0098  92  ALA   C O   
1762 C CB  . ALA   B 86  ? 0.3445 0.2888 0.5085 0.0408  0.0739  -0.0062 92  ALA   C CB  
1763 N N   . ARG   B 87  ? 0.2909 0.2664 0.4473 0.0322  0.0396  0.0113  93  ARG   C N   
1764 C CA  . ARG   B 87  ? 0.2670 0.2537 0.4323 0.0294  0.0270  0.0211  93  ARG   C CA  
1765 C C   . ARG   B 87  ? 0.2636 0.2619 0.4286 0.0269  0.0225  0.0259  93  ARG   C C   
1766 O O   . ARG   B 87  ? 0.2729 0.2709 0.4302 0.0275  0.0288  0.0214  93  ARG   C O   
1767 C CB  . ARG   B 87  ? 0.2589 0.2426 0.4041 0.0253  0.0196  0.0191  93  ARG   C CB  
1768 C CG  . ARG   B 87  ? 0.2295 0.2144 0.3506 0.0221  0.0182  0.0141  93  ARG   C CG  
1769 C CD  . ARG   B 87  ? 0.2420 0.2203 0.3455 0.0196  0.0153  0.0090  93  ARG   C CD  
1770 N NE  . ARG   B 87  ? 0.2244 0.2084 0.3138 0.0156  0.0095  0.0091  93  ARG   C NE  
1771 C CZ  . ARG   B 87  ? 0.2380 0.2226 0.3154 0.0151  0.0113  0.0053  93  ARG   C CZ  
1772 N NH1 . ARG   B 87  ? 0.2085 0.1978 0.2760 0.0118  0.0064  0.0054  93  ARG   C NH1 
1773 N NH2 . ARG   B 87  ? 0.2442 0.2240 0.3197 0.0176  0.0187  0.0014  93  ARG   C NH2 
1774 N N   . TYR   B 88  ? 0.2525 0.2597 0.4241 0.0233  0.0114  0.0351  94  TYR   C N   
1775 C CA  . TYR   B 88  ? 0.2581 0.2745 0.4247 0.0195  0.0059  0.0390  94  TYR   C CA  
1776 C C   . TYR   B 88  ? 0.2163 0.2314 0.3566 0.0149  0.0014  0.0352  94  TYR   C C   
1777 O O   . TYR   B 88  ? 0.2267 0.2397 0.3613 0.0123  -0.0038 0.0368  94  TYR   C O   
1778 C CB  . TYR   B 88  ? 0.2860 0.3102 0.4699 0.0164  -0.0046 0.0510  94  TYR   C CB  
1779 C CG  . TYR   B 88  ? 0.3230 0.3508 0.5376 0.0208  -0.0011 0.0561  94  TYR   C CG  
1780 C CD1 . TYR   B 88  ? 0.3424 0.3772 0.5662 0.0210  0.0010  0.0579  94  TYR   C CD1 
1781 C CD2 . TYR   B 88  ? 0.3560 0.3798 0.5922 0.0250  0.0017  0.0584  94  TYR   C CD2 
1782 C CE1 . TYR   B 88  ? 0.3661 0.4049 0.6220 0.0251  0.0052  0.0628  94  TYR   C CE1 
1783 C CE2 . TYR   B 88  ? 0.3670 0.3941 0.6352 0.0296  0.0065  0.0627  94  TYR   C CE2 
1784 C CZ  . TYR   B 88  ? 0.3833 0.4182 0.6619 0.0297  0.0086  0.0649  94  TYR   C CZ  
1785 O OH  . TYR   B 88  ? 0.4210 0.4603 0.7355 0.0342  0.0136  0.0700  94  TYR   C OH  
1786 N N   . GLN   B 89  ? 0.1785 0.1947 0.3047 0.0140  0.0041  0.0304  95  GLN   C N   
1787 C CA  . GLN   B 89  ? 0.1646 0.1807 0.2701 0.0100  0.0003  0.0274  95  GLN   C CA  
1788 C C   . GLN   B 89  ? 0.1608 0.1846 0.2653 0.0049  -0.0067 0.0337  95  GLN   C C   
1789 O O   . GLN   B 89  ? 0.1810 0.2098 0.2935 0.0050  -0.0065 0.0367  95  GLN   C O   
1790 C CB  . GLN   B 89  ? 0.1643 0.1757 0.2552 0.0115  0.0063  0.0190  95  GLN   C CB  
1791 C CG  . GLN   B 89  ? 0.1637 0.1760 0.2378 0.0077  0.0024  0.0164  95  GLN   C CG  
1792 C CD  . GLN   B 89  ? 0.1620 0.1677 0.2231 0.0091  0.0061  0.0090  95  GLN   C CD  
1793 O OE1 . GLN   B 89  ? 0.1786 0.1762 0.2372 0.0114  0.0098  0.0047  95  GLN   C OE1 
1794 N NE2 . GLN   B 89  ? 0.1466 0.1546 0.1977 0.0068  0.0045  0.0074  95  GLN   C NE2 
1795 N N   . SER   B 90  ? 0.1534 0.1773 0.2483 -0.0001 -0.0125 0.0359  96  SER   C N   
1796 C CA  . SER   B 90  ? 0.1400 0.1680 0.2289 -0.0064 -0.0189 0.0412  96  SER   C CA  
1797 C C   . SER   B 90  ? 0.1503 0.1784 0.2223 -0.0087 -0.0166 0.0354  96  SER   C C   
1798 O O   . SER   B 90  ? 0.1510 0.1759 0.2156 -0.0060 -0.0116 0.0282  96  SER   C O   
1799 C CB  . SER   B 90  ? 0.1773 0.2034 0.2623 -0.0119 -0.0253 0.0466  96  SER   C CB  
1800 O OG  . SER   B 90  ? 0.2145 0.2363 0.2875 -0.0124 -0.0221 0.0409  96  SER   C OG  
1801 N N   . HIS   B 91  ? 0.1501 0.1809 0.2165 -0.0142 -0.0211 0.0392  97  HIS   C N   
1802 C CA  . HIS   B 91  ? 0.1559 0.1860 0.2072 -0.0173 -0.0193 0.0346  97  HIS   C CA  
1803 C C   . HIS   B 91  ? 0.1555 0.1863 0.2081 -0.0120 -0.0134 0.0287  97  HIS   C C   
1804 O O   . HIS   B 91  ? 0.1529 0.1814 0.1949 -0.0121 -0.0103 0.0229  97  HIS   C O   
1805 C CB  . HIS   B 91  ? 0.1648 0.1905 0.2030 -0.0203 -0.0175 0.0306  97  HIS   C CB  
1806 C CG  . HIS   B 91  ? 0.1850 0.2084 0.2181 -0.0269 -0.0225 0.0364  97  HIS   C CG  
1807 N ND1 . HIS   B 91  ? 0.2299 0.2507 0.2486 -0.0350 -0.0250 0.0382  97  HIS   C ND1 
1808 C CD2 . HIS   B 91  ? 0.2097 0.2319 0.2492 -0.0272 -0.0256 0.0412  97  HIS   C CD2 
1809 C CE1 . HIS   B 91  ? 0.2402 0.2577 0.2548 -0.0405 -0.0295 0.0440  97  HIS   C CE1 
1810 N NE2 . HIS   B 91  ? 0.2379 0.2566 0.2658 -0.0359 -0.0304 0.0463  97  HIS   C NE2 
1811 N N   . LEU   B 92  ? 0.1501 0.1831 0.2160 -0.0076 -0.0114 0.0303  98  LEU   C N   
1812 C CA  . LEU   B 92  ? 0.1430 0.1748 0.2084 -0.0032 -0.0050 0.0250  98  LEU   C CA  
1813 C C   . LEU   B 92  ? 0.1484 0.1848 0.2173 -0.0049 -0.0057 0.0277  98  LEU   C C   
1814 O O   . LEU   B 92  ? 0.1441 0.1853 0.2246 -0.0072 -0.0102 0.0346  98  LEU   C O   
1815 C CB  . LEU   B 92  ? 0.1567 0.1860 0.2331 0.0025  0.0003  0.0238  98  LEU   C CB  
1816 C CG  . LEU   B 92  ? 0.1735 0.1983 0.2455 0.0061  0.0079  0.0179  98  LEU   C CG  
1817 C CD1 . LEU   B 92  ? 0.1773 0.1960 0.2321 0.0058  0.0082  0.0115  98  LEU   C CD1 
1818 C CD2 . LEU   B 92  ? 0.2195 0.2397 0.3014 0.0107  0.0144  0.0165  98  LEU   C CD2 
1819 N N   . MET   B 93  ? 0.1372 0.1717 0.1967 -0.0044 -0.0022 0.0229  99  MET   C N   
1820 C CA  . MET   B 93  ? 0.1310 0.1691 0.1927 -0.0063 -0.0024 0.0249  99  MET   C CA  
1821 C C   . MET   B 93  ? 0.1454 0.1813 0.2088 -0.0020 0.0052  0.0214  99  MET   C C   
1822 O O   . MET   B 93  ? 0.1573 0.1869 0.2099 0.0003  0.0088  0.0157  99  MET   C O   
1823 C CB  . MET   B 93  ? 0.1406 0.1769 0.1875 -0.0106 -0.0048 0.0223  99  MET   C CB  
1824 C CG  . MET   B 93  ? 0.1709 0.2070 0.2123 -0.0161 -0.0106 0.0251  99  MET   C CG  
1825 S SD  . MET   B 93  ? 0.1960 0.2275 0.2199 -0.0206 -0.0102 0.0201  99  MET   C SD  
1826 C CE  . MET   B 93  ? 0.1901 0.2173 0.2104 -0.0148 -0.0044 0.0125  99  MET   C CE  
1827 N N   . LEU   B 94  ? 0.1277 0.1679 0.2043 -0.0014 0.0077  0.0250  100 LEU   C N   
1828 C CA  . LEU   B 94  ? 0.1221 0.1586 0.1983 0.0020  0.0167  0.0214  100 LEU   C CA  
1829 C C   . LEU   B 94  ? 0.1274 0.1650 0.1985 -0.0006 0.0172  0.0214  100 LEU   C C   
1830 O O   . LEU   B 94  ? 0.1282 0.1716 0.2040 -0.0045 0.0113  0.0258  100 LEU   C O   
1831 C CB  . LEU   B 94  ? 0.1401 0.1796 0.2376 0.0052  0.0230  0.0246  100 LEU   C CB  
1832 C CG  . LEU   B 94  ? 0.1472 0.1848 0.2530 0.0083  0.0239  0.0248  100 LEU   C CG  
1833 C CD1 . LEU   B 94  ? 0.1565 0.1967 0.2869 0.0119  0.0316  0.0278  100 LEU   C CD1 
1834 C CD2 . LEU   B 94  ? 0.1745 0.2018 0.2618 0.0102  0.0272  0.0173  100 LEU   C CD2 
1835 N N   . ALA   B 95  ? 0.1389 0.1700 0.1996 0.0010  0.0237  0.0169  101 ALA   C N   
1836 C CA  . ALA   B 95  ? 0.1376 0.1686 0.1942 -0.0011 0.0256  0.0170  101 ALA   C CA  
1837 C C   . ALA   B 95  ? 0.1446 0.1698 0.2002 0.0012  0.0363  0.0147  101 ALA   C C   
1838 O O   . ALA   B 95  ? 0.1633 0.1816 0.2139 0.0039  0.0414  0.0110  101 ALA   C O   
1839 C CB  . ALA   B 95  ? 0.1581 0.1837 0.1961 -0.0030 0.0214  0.0134  101 ALA   C CB  
1840 N N   . VAL   B 96  ? 0.1427 0.1691 0.2008 -0.0004 0.0404  0.0163  102 VAL   C N   
1841 C CA  . VAL   B 96  ? 0.1648 0.1834 0.2170 0.0004  0.0517  0.0135  102 VAL   C CA  
1842 C C   . VAL   B 96  ? 0.2022 0.2099 0.2286 -0.0012 0.0497  0.0092  102 VAL   C C   
1843 O O   . VAL   B 96  ? 0.2283 0.2369 0.2485 -0.0039 0.0441  0.0103  102 VAL   C O   
1844 C CB  . VAL   B 96  ? 0.1809 0.2058 0.2483 -0.0012 0.0569  0.0178  102 VAL   C CB  
1845 C CG1 . VAL   B 96  ? 0.1960 0.2112 0.2548 -0.0011 0.0704  0.0146  102 VAL   C CG1 
1846 C CG2 . VAL   B 96  ? 0.1773 0.2135 0.2738 0.0003  0.0567  0.0232  102 VAL   C CG2 
1847 N N   . GLY   B 97  ? 0.2219 0.2187 0.2341 -0.0001 0.0537  0.0047  103 GLY   C N   
1848 C CA  . GLY   B 97  ? 0.2549 0.2403 0.2435 -0.0022 0.0501  0.0017  103 GLY   C CA  
1849 C C   . GLY   B 97  ? 0.2798 0.2525 0.2533 -0.0017 0.0535  -0.0029 103 GLY   C C   
1850 O O   . GLY   B 97  ? 0.2744 0.2471 0.2556 0.0008  0.0583  -0.0046 103 GLY   C O   
1851 N N   . HIS   B 98  ? 0.2879 0.2485 0.2392 -0.0047 0.0503  -0.0048 104 HIS   C N   
1852 C CA  . HIS   B 98  ? 0.3092 0.2551 0.2418 -0.0059 0.0518  -0.0090 104 HIS   C CA  
1853 C C   . HIS   B 98  ? 0.3061 0.2531 0.2394 -0.0045 0.0418  -0.0101 104 HIS   C C   
1854 O O   . HIS   B 98  ? 0.2824 0.2357 0.2200 -0.0045 0.0317  -0.0081 104 HIS   C O   
1855 C CB  . HIS   B 98  ? 0.3283 0.2596 0.2357 -0.0109 0.0504  -0.0093 104 HIS   C CB  
1856 C CG  . HIS   B 98  ? 0.3463 0.2599 0.2303 -0.0139 0.0506  -0.0133 104 HIS   C CG  
1857 N ND1 . HIS   B 98  ? 0.3745 0.2780 0.2509 -0.0144 0.0637  -0.0176 104 HIS   C ND1 
1858 C CD2 . HIS   B 98  ? 0.3768 0.2814 0.2458 -0.0166 0.0389  -0.0136 104 HIS   C CD2 
1859 C CE1 . HIS   B 98  ? 0.4028 0.2900 0.2563 -0.0180 0.0595  -0.0207 104 HIS   C CE1 
1860 N NE2 . HIS   B 98  ? 0.4148 0.3023 0.2633 -0.0196 0.0439  -0.0180 104 HIS   C NE2 
1861 N N   . SER   B 99  ? 0.3167 0.2562 0.2452 -0.0038 0.0451  -0.0137 105 SER   C N   
1862 C CA  . SER   B 99  ? 0.3504 0.2885 0.2782 -0.0031 0.0370  -0.0152 105 SER   C CA  
1863 C C   . SER   B 99  ? 0.3694 0.2898 0.2780 -0.0053 0.0420  -0.0201 105 SER   C C   
1864 O O   . SER   B 99  ? 0.4051 0.3182 0.3090 -0.0056 0.0544  -0.0228 105 SER   C O   
1865 C CB  . SER   B 99  ? 0.3985 0.3508 0.3499 0.0012  0.0369  -0.0137 105 SER   C CB  
1866 O OG  . SER   B 99  ? 0.5170 0.4698 0.4705 0.0019  0.0294  -0.0145 105 SER   C OG  
1867 N N   . GLU   B 100 ? 0.3500 0.2624 0.2468 -0.0076 0.0324  -0.0214 106 GLU   C N   
1868 C CA  . GLU   B 100 ? 0.3732 0.2683 0.2515 -0.0105 0.0336  -0.0261 106 GLU   C CA  
1869 C C   . GLU   B 100 ? 0.3663 0.2670 0.2554 -0.0089 0.0238  -0.0258 106 GLU   C C   
1870 O O   . GLU   B 100 ? 0.3495 0.2641 0.2546 -0.0068 0.0158  -0.0221 106 GLU   C O   
1871 C CB  . GLU   B 100 ? 0.4150 0.2916 0.2635 -0.0174 0.0289  -0.0268 106 GLU   C CB  
1872 C CG  . GLU   B 100 ? 0.4820 0.3511 0.3180 -0.0196 0.0410  -0.0276 106 GLU   C CG  
1873 C CD  . GLU   B 100 ? 0.5870 0.4363 0.3906 -0.0275 0.0371  -0.0275 106 GLU   C CD  
1874 O OE1 . GLU   B 100 ? 0.6649 0.4980 0.4475 -0.0326 0.0303  -0.0297 106 GLU   C OE1 
1875 O OE2 . GLU   B 100 ? 0.5981 0.4475 0.3969 -0.0293 0.0400  -0.0249 106 GLU   C OE2 
1876 N N   . PRO   B 101 ? 0.3804 0.2704 0.2622 -0.0099 0.0250  -0.0298 107 PRO   C N   
1877 C CA  . PRO   B 101 ? 0.3704 0.2675 0.2660 -0.0080 0.0166  -0.0290 107 PRO   C CA  
1878 C C   . PRO   B 101 ? 0.3572 0.2588 0.2550 -0.0100 0.0018  -0.0254 107 PRO   C C   
1879 O O   . PRO   B 101 ? 0.3585 0.2742 0.2763 -0.0071 -0.0029 -0.0228 107 PRO   C O   
1880 C CB  . PRO   B 101 ? 0.4017 0.2818 0.2827 -0.0105 0.0197  -0.0343 107 PRO   C CB  
1881 C CG  . PRO   B 101 ? 0.4198 0.2888 0.2887 -0.0110 0.0350  -0.0383 107 PRO   C CG  
1882 C CD  . PRO   B 101 ? 0.4004 0.2720 0.2634 -0.0124 0.0361  -0.0355 107 PRO   C CD  
1883 N N   . GLY   B 102 ? 0.3375 0.2270 0.2157 -0.0152 -0.0050 -0.0248 108 GLY   C N   
1884 C CA  . GLY   B 102 ? 0.3322 0.2249 0.2148 -0.0172 -0.0191 -0.0208 108 GLY   C CA  
1885 C C   . GLY   B 102 ? 0.3058 0.2155 0.2077 -0.0136 -0.0201 -0.0168 108 GLY   C C   
1886 O O   . GLY   B 102 ? 0.2985 0.2136 0.2108 -0.0139 -0.0300 -0.0136 108 GLY   C O   
1887 N N   . ASP   B 103 ? 0.2772 0.1949 0.1851 -0.0104 -0.0098 -0.0169 109 ASP   C N   
1888 C CA  . ASP   B 103 ? 0.2579 0.1903 0.1822 -0.0076 -0.0100 -0.0138 109 ASP   C CA  
1889 C C   . ASP   B 103 ? 0.2289 0.1757 0.1746 -0.0041 -0.0102 -0.0131 109 ASP   C C   
1890 O O   . ASP   B 103 ? 0.2239 0.1812 0.1818 -0.0028 -0.0115 -0.0109 109 ASP   C O   
1891 C CB  . ASP   B 103 ? 0.2502 0.1855 0.1731 -0.0065 0.0001  -0.0136 109 ASP   C CB  
1892 C CG  . ASP   B 103 ? 0.2853 0.2080 0.1881 -0.0105 0.0002  -0.0131 109 ASP   C CG  
1893 O OD1 . ASP   B 103 ? 0.2954 0.2123 0.1912 -0.0135 -0.0099 -0.0110 109 ASP   C OD1 
1894 O OD2 . ASP   B 103 ? 0.3021 0.2200 0.1966 -0.0110 0.0104  -0.0146 109 ASP   C OD2 
1895 N N   . CYS   B 104 ? 0.2128 0.1592 0.1624 -0.0031 -0.0089 -0.0149 110 CYS   C N   
1896 C CA  . CYS   B 104 ? 0.2130 0.1717 0.1809 -0.0007 -0.0093 -0.0137 110 CYS   C CA  
1897 C C   . CYS   B 104 ? 0.2094 0.1730 0.1863 -0.0015 -0.0170 -0.0120 110 CYS   C C   
1898 O O   . CYS   B 104 ? 0.2303 0.1864 0.2020 -0.0038 -0.0246 -0.0119 110 CYS   C O   
1899 C CB  . CYS   B 104 ? 0.2301 0.1855 0.1996 0.0000  -0.0078 -0.0156 110 CYS   C CB  
1900 S SG  . CYS   B 104 ? 0.2761 0.2303 0.2459 0.0025  0.0036  -0.0169 110 CYS   C SG  
1901 N N   . GLY   B 105 ? 0.1742 0.1492 0.1644 0.0000  -0.0151 -0.0106 111 GLY   C N   
1902 C CA  . GLY   B 105 ? 0.1743 0.1543 0.1757 -0.0005 -0.0196 -0.0096 111 GLY   C CA  
1903 C C   . GLY   B 105 ? 0.1750 0.1573 0.1775 -0.0006 -0.0196 -0.0085 111 GLY   C C   
1904 O O   . GLY   B 105 ? 0.1745 0.1618 0.1887 -0.0005 -0.0206 -0.0081 111 GLY   C O   
1905 N N   . GLY   B 106 ? 0.1647 0.1427 0.1557 -0.0009 -0.0175 -0.0082 112 GLY   C N   
1906 C CA  . GLY   B 106 ? 0.1569 0.1367 0.1487 -0.0011 -0.0173 -0.0070 112 GLY   C CA  
1907 C C   . GLY   B 106 ? 0.1509 0.1406 0.1524 -0.0005 -0.0122 -0.0071 112 GLY   C C   
1908 O O   . GLY   B 106 ? 0.1493 0.1433 0.1512 -0.0001 -0.0078 -0.0071 112 GLY   C O   
1909 N N   . ILE   B 107 ? 0.1453 0.1374 0.1540 -0.0008 -0.0129 -0.0070 113 ILE   C N   
1910 C CA  . ILE   B 107 ? 0.1431 0.1418 0.1573 -0.0014 -0.0078 -0.0078 113 ILE   C CA  
1911 C C   . ILE   B 107 ? 0.1331 0.1332 0.1413 -0.0025 -0.0048 -0.0069 113 ILE   C C   
1912 O O   . ILE   B 107 ? 0.1502 0.1464 0.1539 -0.0026 -0.0061 -0.0060 113 ILE   C O   
1913 C CB  . ILE   B 107 ? 0.1856 0.1850 0.2113 -0.0016 -0.0080 -0.0091 113 ILE   C CB  
1914 C CG1 . ILE   B 107 ? 0.2165 0.2176 0.2520 -0.0011 -0.0090 -0.0099 113 ILE   C CG1 
1915 C CG2 . ILE   B 107 ? 0.2181 0.2205 0.2452 -0.0034 -0.0022 -0.0107 113 ILE   C CG2 
1916 C CD1 . ILE   B 107 ? 0.2553 0.2571 0.3071 -0.0008 -0.0082 -0.0111 113 ILE   C CD1 
1917 N N   . LEU   B 108 ? 0.1240 0.1291 0.1328 -0.0039 -0.0014 -0.0065 114 LEU   C N   
1918 C CA  . LEU   B 108 ? 0.1161 0.1235 0.1219 -0.0060 0.0007  -0.0052 114 LEU   C CA  
1919 C C   . LEU   B 108 ? 0.1303 0.1381 0.1381 -0.0087 0.0025  -0.0072 114 LEU   C C   
1920 O O   . LEU   B 108 ? 0.1345 0.1438 0.1444 -0.0100 0.0041  -0.0083 114 LEU   C O   
1921 C CB  . LEU   B 108 ? 0.1278 0.1396 0.1338 -0.0066 0.0018  -0.0027 114 LEU   C CB  
1922 C CG  . LEU   B 108 ? 0.1418 0.1569 0.1473 -0.0097 0.0023  -0.0003 114 LEU   C CG  
1923 C CD1 . LEU   B 108 ? 0.1547 0.1682 0.1582 -0.0093 0.0030  0.0006  114 LEU   C CD1 
1924 C CD2 . LEU   B 108 ? 0.1479 0.1678 0.1577 -0.0104 0.0017  0.0034  114 LEU   C CD2 
1925 N N   . ARG   B 109 ? 0.1350 0.1407 0.1412 -0.0100 0.0032  -0.0077 115 ARG   C N   
1926 C CA  . ARG   B 109 ? 0.1530 0.1566 0.1595 -0.0130 0.0063  -0.0106 115 ARG   C CA  
1927 C C   . ARG   B 109 ? 0.1625 0.1660 0.1627 -0.0168 0.0066  -0.0095 115 ARG   C C   
1928 O O   . ARG   B 109 ? 0.1781 0.1818 0.1771 -0.0161 0.0047  -0.0072 115 ARG   C O   
1929 C CB  . ARG   B 109 ? 0.1961 0.1954 0.2095 -0.0109 0.0064  -0.0127 115 ARG   C CB  
1930 C CG  . ARG   B 109 ? 0.2720 0.2711 0.2947 -0.0077 0.0047  -0.0132 115 ARG   C CG  
1931 C CD  . ARG   B 109 ? 0.3308 0.3256 0.3630 -0.0059 0.0034  -0.0139 115 ARG   C CD  
1932 N NE  . ARG   B 109 ? 0.4032 0.3964 0.4412 -0.0077 0.0101  -0.0180 115 ARG   C NE  
1933 C CZ  . ARG   B 109 ? 0.4288 0.4227 0.4779 -0.0071 0.0141  -0.0205 115 ARG   C CZ  
1934 N NH1 . ARG   B 109 ? 0.4350 0.4313 0.4933 -0.0044 0.0100  -0.0187 115 ARG   C NH1 
1935 N NH2 . ARG   B 109 ? 0.4304 0.4215 0.4814 -0.0096 0.0226  -0.0249 115 ARG   C NH2 
1936 N N   . CYS   B 110 ? 0.1559 0.1575 0.1513 -0.0215 0.0091  -0.0113 116 CYS   C N   
1937 C CA  . CYS   B 110 ? 0.1718 0.1710 0.1599 -0.0265 0.0088  -0.0109 116 CYS   C CA  
1938 C C   . CYS   B 110 ? 0.2125 0.2043 0.1990 -0.0286 0.0136  -0.0161 116 CYS   C C   
1939 O O   . CYS   B 110 ? 0.2032 0.1929 0.1973 -0.0254 0.0171  -0.0193 116 CYS   C O   
1940 C CB  . CYS   B 110 ? 0.1646 0.1656 0.1455 -0.0320 0.0066  -0.0081 116 CYS   C CB  
1941 S SG  . CYS   B 110 ? 0.1806 0.1766 0.1534 -0.0367 0.0110  -0.0117 116 CYS   C SG  
1942 N N   . GLN   B 111 ? 0.2391 0.2262 0.2170 -0.0343 0.0140  -0.0170 117 GLN   C N   
1943 C CA  . GLN   B 111 ? 0.2622 0.2403 0.2377 -0.0367 0.0199  -0.0227 117 GLN   C CA  
1944 C C   . GLN   B 111 ? 0.2781 0.2515 0.2505 -0.0390 0.0272  -0.0277 117 GLN   C C   
1945 O O   . GLN   B 111 ? 0.3160 0.2822 0.2915 -0.0392 0.0345  -0.0333 117 GLN   C O   
1946 C CB  . GLN   B 111 ? 0.2979 0.2705 0.2622 -0.0435 0.0185  -0.0228 117 GLN   C CB  
1947 C CG  . GLN   B 111 ? 0.3197 0.2906 0.2694 -0.0516 0.0162  -0.0213 117 GLN   C CG  
1948 C CD  . GLN   B 111 ? 0.4489 0.4135 0.3873 -0.0593 0.0132  -0.0210 117 GLN   C CD  
1949 O OE1 . GLN   B 111 ? 0.4963 0.4663 0.4343 -0.0618 0.0054  -0.0148 117 GLN   C OE1 
1950 N NE2 . GLN   B 111 ? 0.4758 0.4286 0.4062 -0.0633 0.0193  -0.0275 117 GLN   C NE2 
1951 N N   . HIS   B 112 ? 0.2446 0.2217 0.2127 -0.0406 0.0260  -0.0255 118 HIS   C N   
1952 C CA  . HIS   B 112 ? 0.2580 0.2302 0.2215 -0.0437 0.0334  -0.0296 118 HIS   C CA  
1953 C C   . HIS   B 112 ? 0.2536 0.2309 0.2329 -0.0371 0.0359  -0.0303 118 HIS   C C   
1954 O O   . HIS   B 112 ? 0.2885 0.2620 0.2680 -0.0390 0.0436  -0.0341 118 HIS   C O   
1955 C CB  . HIS   B 112 ? 0.2612 0.2327 0.2089 -0.0509 0.0299  -0.0263 118 HIS   C CB  
1956 C CG  . HIS   B 112 ? 0.2594 0.2258 0.1922 -0.0585 0.0254  -0.0247 118 HIS   C CG  
1957 N ND1 . HIS   B 112 ? 0.2629 0.2361 0.1960 -0.0592 0.0153  -0.0175 118 HIS   C ND1 
1958 C CD2 . HIS   B 112 ? 0.3036 0.2579 0.2210 -0.0662 0.0298  -0.0294 118 HIS   C CD2 
1959 C CE1 . HIS   B 112 ? 0.2912 0.2578 0.2116 -0.0669 0.0125  -0.0173 118 HIS   C CE1 
1960 N NE2 . HIS   B 112 ? 0.3271 0.2812 0.2354 -0.0718 0.0207  -0.0245 118 HIS   C NE2 
1961 N N   . GLY   B 113 ? 0.2121 0.1971 0.2035 -0.0303 0.0296  -0.0264 119 GLY   C N   
1962 C CA  . GLY   B 113 ? 0.1946 0.1837 0.2002 -0.0249 0.0301  -0.0264 119 GLY   C CA  
1963 C C   . GLY   B 113 ? 0.1701 0.1665 0.1776 -0.0215 0.0226  -0.0212 119 GLY   C C   
1964 O O   . GLY   B 113 ? 0.1773 0.1760 0.1794 -0.0214 0.0173  -0.0177 119 GLY   C O   
1965 N N   . VAL   B 114 ? 0.1627 0.1619 0.1779 -0.0191 0.0228  -0.0210 120 VAL   C N   
1966 C CA  . VAL   B 114 ? 0.1538 0.1580 0.1705 -0.0160 0.0166  -0.0169 120 VAL   C CA  
1967 C C   . VAL   B 114 ? 0.1584 0.1647 0.1650 -0.0195 0.0148  -0.0138 120 VAL   C C   
1968 O O   . VAL   B 114 ? 0.1679 0.1725 0.1692 -0.0238 0.0182  -0.0145 120 VAL   C O   
1969 C CB  . VAL   B 114 ? 0.1725 0.1783 0.2013 -0.0130 0.0167  -0.0176 120 VAL   C CB  
1970 C CG1 . VAL   B 114 ? 0.1718 0.1808 0.1996 -0.0108 0.0111  -0.0142 120 VAL   C CG1 
1971 C CG2 . VAL   B 114 ? 0.1782 0.1823 0.2200 -0.0094 0.0157  -0.0189 120 VAL   C CG2 
1972 N N   . VAL   B 115 ? 0.1449 0.1544 0.1498 -0.0178 0.0098  -0.0101 121 VAL   C N   
1973 C CA  . VAL   B 115 ? 0.1439 0.1560 0.1439 -0.0203 0.0070  -0.0060 121 VAL   C CA  
1974 C C   . VAL   B 115 ? 0.1436 0.1585 0.1490 -0.0172 0.0050  -0.0039 121 VAL   C C   
1975 O O   . VAL   B 115 ? 0.1426 0.1587 0.1463 -0.0196 0.0039  -0.0012 121 VAL   C O   
1976 C CB  . VAL   B 115 ? 0.1422 0.1563 0.1408 -0.0203 0.0040  -0.0030 121 VAL   C CB  
1977 C CG1 . VAL   B 115 ? 0.1545 0.1725 0.1538 -0.0219 0.0003  0.0024  121 VAL   C CG1 
1978 C CG2 . VAL   B 115 ? 0.1625 0.1729 0.1545 -0.0246 0.0053  -0.0047 121 VAL   C CG2 
1979 N N   . GLY   B 116 ? 0.1339 0.1487 0.1447 -0.0122 0.0039  -0.0048 122 GLY   C N   
1980 C CA  . GLY   B 116 ? 0.1593 0.1750 0.1739 -0.0094 0.0022  -0.0036 122 GLY   C CA  
1981 C C   . GLY   B 116 ? 0.1329 0.1458 0.1491 -0.0054 0.0005  -0.0050 122 GLY   C C   
1982 O O   . GLY   B 116 ? 0.1375 0.1480 0.1534 -0.0048 0.0001  -0.0067 122 GLY   C O   
1983 N N   . ILE   B 117 ? 0.1301 0.1418 0.1472 -0.0033 -0.0007 -0.0043 123 ILE   C N   
1984 C CA  . ILE   B 117 ? 0.1283 0.1346 0.1429 -0.0009 -0.0028 -0.0059 123 ILE   C CA  
1985 C C   . ILE   B 117 ? 0.1336 0.1374 0.1443 0.0007  -0.0014 -0.0051 123 ILE   C C   
1986 O O   . ILE   B 117 ? 0.1344 0.1410 0.1489 0.0010  0.0003  -0.0033 123 ILE   C O   
1987 C CB  . ILE   B 117 ? 0.1461 0.1501 0.1651 -0.0005 -0.0057 -0.0073 123 ILE   C CB  
1988 C CG1 . ILE   B 117 ? 0.1629 0.1692 0.1857 -0.0010 -0.0046 -0.0062 123 ILE   C CG1 
1989 C CG2 . ILE   B 117 ? 0.1670 0.1721 0.1929 -0.0014 -0.0065 -0.0085 123 ILE   C CG2 
1990 C CD1 . ILE   B 117 ? 0.1776 0.1808 0.2051 -0.0007 -0.0079 -0.0075 123 ILE   C CD1 
1991 N N   . VAL   B 118 ? 0.1280 0.1253 0.1310 0.0015  -0.0016 -0.0063 124 VAL   C N   
1992 C CA  . VAL   B 118 ? 0.1381 0.1309 0.1365 0.0028  0.0022  -0.0066 124 VAL   C CA  
1993 C C   . VAL   B 118 ? 0.1457 0.1358 0.1463 0.0038  0.0021  -0.0075 124 VAL   C C   
1994 O O   . VAL   B 118 ? 0.1529 0.1395 0.1522 0.0031  -0.0022 -0.0090 124 VAL   C O   
1995 C CB  . VAL   B 118 ? 0.1573 0.1404 0.1429 0.0021  0.0019  -0.0082 124 VAL   C CB  
1996 C CG1 . VAL   B 118 ? 0.1813 0.1572 0.1601 0.0028  0.0080  -0.0097 124 VAL   C CG1 
1997 C CG2 . VAL   B 118 ? 0.1637 0.1488 0.1474 0.0011  0.0021  -0.0068 124 VAL   C CG2 
1998 N N   . SER   B 119 ? 0.1514 0.1430 0.1572 0.0053  0.0067  -0.0065 125 SER   C N   
1999 C CA  . SER   B 119 ? 0.1485 0.1371 0.1579 0.0064  0.0073  -0.0072 125 SER   C CA  
2000 C C   . SER   B 119 ? 0.1828 0.1647 0.1909 0.0083  0.0142  -0.0088 125 SER   C C   
2001 O O   . SER   B 119 ? 0.1944 0.1684 0.1995 0.0089  0.0152  -0.0114 125 SER   C O   
2002 C CB  . SER   B 119 ? 0.1542 0.1517 0.1756 0.0061  0.0055  -0.0034 125 SER   C CB  
2003 O OG  . SER   B 119 ? 0.1561 0.1510 0.1827 0.0072  0.0058  -0.0033 125 SER   C OG  
2004 N N   . THR   B 120 ? 0.1830 0.1671 0.1937 0.0092  0.0196  -0.0076 126 THR   C N   
2005 C CA  . THR   B 120 ? 0.1924 0.1702 0.2045 0.0111  0.0287  -0.0094 126 THR   C CA  
2006 C C   . THR   B 120 ? 0.1993 0.1737 0.2034 0.0103  0.0344  -0.0104 126 THR   C C   
2007 O O   . THR   B 120 ? 0.1857 0.1651 0.1872 0.0087  0.0308  -0.0085 126 THR   C O   
2008 C CB  . THR   B 120 ? 0.1981 0.1846 0.2318 0.0137  0.0314  -0.0050 126 THR   C CB  
2009 O OG1 . THR   B 120 ? 0.2134 0.2105 0.2572 0.0131  0.0307  -0.0002 126 THR   C OG1 
2010 C CG2 . THR   B 120 ? 0.2012 0.1915 0.2430 0.0138  0.0254  -0.0026 126 THR   C CG2 
2011 N N   . GLY   B 121 ? 0.2316 0.1968 0.2320 0.0112  0.0443  -0.0136 127 GLY   C N   
2012 C CA  . GLY   B 121 ? 0.2641 0.2253 0.2574 0.0101  0.0519  -0.0145 127 GLY   C CA  
2013 C C   . GLY   B 121 ? 0.2887 0.2416 0.2847 0.0117  0.0656  -0.0176 127 GLY   C C   
2014 O O   . GLY   B 121 ? 0.2947 0.2414 0.2932 0.0133  0.0688  -0.0204 127 GLY   C O   
2015 N N   . GLY   B 122 ? 0.3107 0.2622 0.3059 0.0110  0.0745  -0.0176 128 GLY   C N   
2016 C CA  . GLY   B 122 ? 0.3318 0.2745 0.3304 0.0123  0.0905  -0.0212 128 GLY   C CA  
2017 C C   . GLY   B 122 ? 0.3349 0.2879 0.3532 0.0136  0.0982  -0.0171 128 GLY   C C   
2018 O O   . GLY   B 122 ? 0.3128 0.2820 0.3500 0.0146  0.0902  -0.0107 128 GLY   C O   
2019 N N   . ASN   B 123 ? 0.3535 0.2961 0.3668 0.0128  0.1140  -0.0209 129 ASN   C N   
2020 C CA  . ASN   B 123 ? 0.3562 0.3080 0.3906 0.0138  0.1232  -0.0171 129 ASN   C CA  
2021 C C   . ASN   B 123 ? 0.3339 0.2968 0.3686 0.0113  0.1143  -0.0116 129 ASN   C C   
2022 O O   . ASN   B 123 ? 0.3353 0.3117 0.3958 0.0127  0.1159  -0.0060 129 ASN   C O   
2023 C CB  . ASN   B 123 ? 0.3675 0.3327 0.4402 0.0191  0.1253  -0.0125 129 ASN   C CB  
2024 C CG  . ASN   B 123 ? 0.4392 0.3939 0.5184 0.0223  0.1373  -0.0176 129 ASN   C CG  
2025 O OD1 . ASN   B 123 ? 0.4715 0.4085 0.5314 0.0206  0.1513  -0.0252 129 ASN   C OD1 
2026 N ND2 . ASN   B 123 ? 0.4382 0.4031 0.5450 0.0265  0.1325  -0.0134 129 ASN   C ND2 
2027 N N   . GLY   B 124 ? 0.3045 0.2613 0.3124 0.0076  0.1047  -0.0128 130 GLY   C N   
2028 C CA  . GLY   B 124 ? 0.2809 0.2465 0.2886 0.0052  0.0966  -0.0082 130 GLY   C CA  
2029 C C   . GLY   B 124 ? 0.2450 0.2272 0.2711 0.0068  0.0828  -0.0026 130 GLY   C C   
2030 O O   . GLY   B 124 ? 0.2460 0.2371 0.2784 0.0052  0.0778  0.0016  130 GLY   C O   
2031 N N   . LEU   B 125 ? 0.2127 0.1976 0.2453 0.0092  0.0770  -0.0028 131 LEU   C N   
2032 C CA  . LEU   B 125 ? 0.2038 0.2014 0.2485 0.0096  0.0644  0.0019  131 LEU   C CA  
2033 C C   . LEU   B 125 ? 0.2320 0.2237 0.2581 0.0086  0.0552  -0.0012 131 LEU   C C   
2034 O O   . LEU   B 125 ? 0.3017 0.2817 0.3144 0.0089  0.0585  -0.0060 131 LEU   C O   
2035 C CB  . LEU   B 125 ? 0.2088 0.2149 0.2802 0.0128  0.0656  0.0056  131 LEU   C CB  
2036 C CG  . LEU   B 125 ? 0.2315 0.2460 0.3280 0.0136  0.0729  0.0103  131 LEU   C CG  
2037 C CD1 . LEU   B 125 ? 0.2601 0.2786 0.3833 0.0176  0.0773  0.0129  131 LEU   C CD1 
2038 C CD2 . LEU   B 125 ? 0.2264 0.2533 0.3326 0.0108  0.0628  0.0169  131 LEU   C CD2 
2039 N N   . VAL   B 126 ? 0.1899 0.1886 0.2157 0.0071  0.0446  0.0012  132 VAL   C N   
2040 C CA  . VAL   B 126 ? 0.1776 0.1728 0.1920 0.0065  0.0366  -0.0010 132 VAL   C CA  
2041 C C   . VAL   B 126 ? 0.1641 0.1698 0.1925 0.0068  0.0297  0.0027  132 VAL   C C   
2042 O O   . VAL   B 126 ? 0.1526 0.1673 0.1914 0.0054  0.0270  0.0071  132 VAL   C O   
2043 C CB  . VAL   B 126 ? 0.1918 0.1836 0.1912 0.0038  0.0314  -0.0020 132 VAL   C CB  
2044 C CG1 . VAL   B 126 ? 0.2222 0.2224 0.2283 0.0021  0.0291  0.0016  132 VAL   C CG1 
2045 C CG2 . VAL   B 126 ? 0.2056 0.1950 0.1980 0.0034  0.0232  -0.0038 132 VAL   C CG2 
2046 N N   . GLY   B 127 ? 0.1409 0.1442 0.1677 0.0077  0.0265  0.0012  133 GLY   C N   
2047 C CA  . GLY   B 127 ? 0.1500 0.1611 0.1870 0.0071  0.0204  0.0047  133 GLY   C CA  
2048 C C   . GLY   B 127 ? 0.1348 0.1449 0.1623 0.0053  0.0140  0.0029  133 GLY   C C   
2049 O O   . GLY   B 127 ? 0.1539 0.1567 0.1715 0.0057  0.0136  -0.0010 133 GLY   C O   
2050 N N   . PHE   B 128 ? 0.1257 0.1426 0.1569 0.0027  0.0093  0.0059  134 PHE   C N   
2051 C CA  . PHE   B 128 ? 0.1273 0.1436 0.1519 0.0006  0.0051  0.0041  134 PHE   C CA  
2052 C C   . PHE   B 128 ? 0.1299 0.1495 0.1596 -0.0010 0.0022  0.0066  134 PHE   C C   
2053 O O   . PHE   B 128 ? 0.1292 0.1535 0.1649 -0.0031 0.0004  0.0112  134 PHE   C O   
2054 C CB  . PHE   B 128 ? 0.1422 0.1609 0.1629 -0.0023 0.0037  0.0044  134 PHE   C CB  
2055 C CG  . PHE   B 128 ? 0.1476 0.1636 0.1640 -0.0014 0.0062  0.0032  134 PHE   C CG  
2056 C CD1 . PHE   B 128 ? 0.1400 0.1497 0.1481 -0.0006 0.0057  -0.0002 134 PHE   C CD1 
2057 C CD2 . PHE   B 128 ? 0.1586 0.1779 0.1798 -0.0019 0.0084  0.0061  134 PHE   C CD2 
2058 C CE1 . PHE   B 128 ? 0.1565 0.1624 0.1587 -0.0007 0.0075  -0.0006 134 PHE   C CE1 
2059 C CE2 . PHE   B 128 ? 0.1676 0.1838 0.1839 -0.0018 0.0112  0.0052  134 PHE   C CE2 
2060 C CZ  . PHE   B 128 ? 0.1666 0.1757 0.1722 -0.0013 0.0107  0.0019  134 PHE   C CZ  
2061 N N   . ALA   B 129 ? 0.1290 0.1456 0.1559 -0.0010 0.0010  0.0042  135 ALA   C N   
2062 C CA  . ALA   B 129 ? 0.1133 0.1321 0.1429 -0.0035 -0.0012 0.0064  135 ALA   C CA  
2063 C C   . ALA   B 129 ? 0.1177 0.1382 0.1420 -0.0077 -0.0019 0.0063  135 ALA   C C   
2064 O O   . ALA   B 129 ? 0.1221 0.1407 0.1429 -0.0078 -0.0007 0.0025  135 ALA   C O   
2065 C CB  . ALA   B 129 ? 0.1242 0.1391 0.1537 -0.0021 -0.0015 0.0036  135 ALA   C CB  
2066 N N   . ASP   B 130 ? 0.1190 0.1420 0.1427 -0.0119 -0.0040 0.0105  136 ASP   C N   
2067 C CA  . ASP   B 130 ? 0.1298 0.1521 0.1452 -0.0172 -0.0038 0.0099  136 ASP   C CA  
2068 C C   . ASP   B 130 ? 0.1454 0.1649 0.1572 -0.0196 -0.0015 0.0074  136 ASP   C C   
2069 O O   . ASP   B 130 ? 0.1459 0.1651 0.1610 -0.0193 -0.0024 0.0091  136 ASP   C O   
2070 C CB  . ASP   B 130 ? 0.1566 0.1804 0.1702 -0.0225 -0.0083 0.0161  136 ASP   C CB  
2071 C CG  . ASP   B 130 ? 0.2268 0.2474 0.2280 -0.0295 -0.0083 0.0154  136 ASP   C CG  
2072 O OD1 . ASP   B 130 ? 0.2130 0.2324 0.2105 -0.0292 -0.0055 0.0114  136 ASP   C OD1 
2073 O OD2 . ASP   B 130 ? 0.2726 0.2904 0.2661 -0.0358 -0.0107 0.0185  136 ASP   C OD2 
2074 N N   . VAL   B 131 ? 0.1381 0.1550 0.1444 -0.0219 0.0023  0.0033  137 VAL   C N   
2075 C CA  . VAL   B 131 ? 0.1520 0.1662 0.1563 -0.0248 0.0064  0.0009  137 VAL   C CA  
2076 C C   . VAL   B 131 ? 0.1719 0.1816 0.1636 -0.0323 0.0096  0.0001  137 VAL   C C   
2077 O O   . VAL   B 131 ? 0.1826 0.1886 0.1708 -0.0357 0.0152  -0.0024 137 VAL   C O   
2078 C CB  . VAL   B 131 ? 0.1525 0.1664 0.1652 -0.0208 0.0099  -0.0041 137 VAL   C CB  
2079 C CG1 . VAL   B 131 ? 0.1491 0.1648 0.1704 -0.0151 0.0060  -0.0035 137 VAL   C CG1 
2080 C CG2 . VAL   B 131 ? 0.1577 0.1703 0.1699 -0.0200 0.0121  -0.0075 137 VAL   C CG2 
2081 N N   . ARG   B 132 ? 0.1627 0.1717 0.1469 -0.0354 0.0066  0.0021  138 ARG   C N   
2082 C CA  . ARG   B 132 ? 0.1676 0.1700 0.1370 -0.0432 0.0094  0.0006  138 ARG   C CA  
2083 C C   . ARG   B 132 ? 0.1987 0.1959 0.1555 -0.0512 0.0091  0.0036  138 ARG   C C   
2084 O O   . ARG   B 132 ? 0.2298 0.2188 0.1718 -0.0584 0.0144  0.0005  138 ARG   C O   
2085 C CB  . ARG   B 132 ? 0.1650 0.1677 0.1299 -0.0453 0.0045  0.0029  138 ARG   C CB  
2086 C CG  . ARG   B 132 ? 0.1799 0.1853 0.1533 -0.0392 0.0061  -0.0005 138 ARG   C CG  
2087 C CD  . ARG   B 132 ? 0.1584 0.1648 0.1288 -0.0416 0.0011  0.0026  138 ARG   C CD  
2088 N NE  . ARG   B 132 ? 0.1632 0.1761 0.1422 -0.0395 -0.0056 0.0093  138 ARG   C NE  
2089 C CZ  . ARG   B 132 ? 0.1640 0.1802 0.1470 -0.0400 -0.0103 0.0133  138 ARG   C CZ  
2090 N NH1 . ARG   B 132 ? 0.1840 0.1970 0.1599 -0.0440 -0.0105 0.0119  138 ARG   C NH1 
2091 N NH2 . ARG   B 132 ? 0.1785 0.2008 0.1735 -0.0370 -0.0144 0.0189  138 ARG   C NH2 
2092 N N   . ASP   B 133 ? 0.1955 0.1959 0.1568 -0.0506 0.0033  0.0096  139 ASP   C N   
2093 C CA  . ASP   B 133 ? 0.2074 0.2021 0.1562 -0.0587 0.0019  0.0136  139 ASP   C CA  
2094 C C   . ASP   B 133 ? 0.2208 0.2129 0.1702 -0.0589 0.0098  0.0101  139 ASP   C C   
2095 O O   . ASP   B 133 ? 0.2471 0.2326 0.1831 -0.0668 0.0105  0.0127  139 ASP   C O   
2096 C CB  . ASP   B 133 ? 0.2129 0.2117 0.1683 -0.0583 -0.0083 0.0225  139 ASP   C CB  
2097 C CG  . ASP   B 133 ? 0.2549 0.2605 0.2292 -0.0491 -0.0085 0.0228  139 ASP   C CG  
2098 O OD1 . ASP   B 133 ? 0.2381 0.2478 0.2226 -0.0417 -0.0052 0.0179  139 ASP   C OD1 
2099 O OD2 . ASP   B 133 ? 0.2535 0.2591 0.2313 -0.0500 -0.0124 0.0281  139 ASP   C OD2 
2100 N N   . LEU   B 134 ? 0.2065 0.2030 0.1707 -0.0513 0.0153  0.0048  140 LEU   C N   
2101 C CA  . LEU   B 134 ? 0.2131 0.2084 0.1824 -0.0512 0.0223  0.0020  140 LEU   C CA  
2102 C C   . LEU   B 134 ? 0.2234 0.2120 0.1850 -0.0558 0.0336  -0.0044 140 LEU   C C   
2103 O O   . LEU   B 134 ? 0.2124 0.2030 0.1863 -0.0511 0.0398  -0.0100 140 LEU   C O   
2104 C CB  . LEU   B 134 ? 0.1913 0.1939 0.1811 -0.0417 0.0212  0.0002  140 LEU   C CB  
2105 C CG  . LEU   B 134 ? 0.1989 0.2062 0.1958 -0.0368 0.0122  0.0052  140 LEU   C CG  
2106 C CD1 . LEU   B 134 ? 0.2065 0.2178 0.2183 -0.0290 0.0114  0.0024  140 LEU   C CD1 
2107 C CD2 . LEU   B 134 ? 0.2151 0.2210 0.2092 -0.0404 0.0088  0.0109  140 LEU   C CD2 
2108 N N   . LEU   B 135 ? 0.2327 0.2121 0.1729 -0.0660 0.0361  -0.0032 141 LEU   C N   
2109 C CA  . LEU   B 135 ? 0.2567 0.2267 0.1852 -0.0719 0.0483  -0.0101 141 LEU   C CA  
2110 C C   . LEU   B 135 ? 0.2757 0.2455 0.2162 -0.0703 0.0605  -0.0152 141 LEU   C C   
2111 O O   . LEU   B 135 ? 0.2962 0.2620 0.2397 -0.0704 0.0718  -0.0223 141 LEU   C O   
2112 C CB  . LEU   B 135 ? 0.2715 0.2291 0.1705 -0.0845 0.0480  -0.0078 141 LEU   C CB  
2113 C CG  . LEU   B 135 ? 0.2870 0.2446 0.1751 -0.0878 0.0342  -0.0009 141 LEU   C CG  
2114 C CD1 . LEU   B 135 ? 0.3255 0.2681 0.1816 -0.1023 0.0336  0.0013  141 LEU   C CD1 
2115 C CD2 . LEU   B 135 ? 0.2881 0.2509 0.1852 -0.0818 0.0310  -0.0034 141 LEU   C CD2 
2116 N N   . TRP   B 136 ? 0.2742 0.2484 0.2240 -0.0686 0.0586  -0.0115 142 TRP   C N   
2117 C CA  . TRP   B 136 ? 0.2777 0.2525 0.2417 -0.0675 0.0695  -0.0153 142 TRP   C CA  
2118 C C   . TRP   B 136 ? 0.2771 0.2603 0.2685 -0.0577 0.0714  -0.0196 142 TRP   C C   
2119 O O   . TRP   B 136 ? 0.2868 0.2705 0.2933 -0.0569 0.0814  -0.0234 142 TRP   C O   
2120 C CB  . TRP   B 136 ? 0.2726 0.2500 0.2400 -0.0684 0.0652  -0.0096 142 TRP   C CB  
2121 C CG  . TRP   B 136 ? 0.2533 0.2394 0.2320 -0.0610 0.0512  -0.0042 142 TRP   C CG  
2122 C CD1 . TRP   B 136 ? 0.2615 0.2477 0.2303 -0.0623 0.0400  0.0023  142 TRP   C CD1 
2123 C CD2 . TRP   B 136 ? 0.2327 0.2278 0.2354 -0.0517 0.0474  -0.0051 142 TRP   C CD2 
2124 N NE1 . TRP   B 136 ? 0.2480 0.2423 0.2334 -0.0539 0.0314  0.0048  142 TRP   C NE1 
2125 C CE2 . TRP   B 136 ? 0.2337 0.2326 0.2375 -0.0480 0.0355  0.0002  142 TRP   C CE2 
2126 C CE3 . TRP   B 136 ? 0.2319 0.2311 0.2555 -0.0469 0.0527  -0.0094 142 TRP   C CE3 
2127 C CZ2 . TRP   B 136 ? 0.2388 0.2439 0.2599 -0.0400 0.0296  0.0002  142 TRP   C CZ2 
2128 C CZ3 . TRP   B 136 ? 0.2412 0.2472 0.2824 -0.0395 0.0447  -0.0082 142 TRP   C CZ3 
2129 C CH2 . TRP   B 136 ? 0.2313 0.2393 0.2692 -0.0366 0.0338  -0.0038 142 TRP   C CH2 
2130 N N   . LEU   B 137 ? 0.2608 0.2499 0.2592 -0.0509 0.0619  -0.0188 143 LEU   C N   
2131 C CA  . LEU   B 137 ? 0.2522 0.2475 0.2744 -0.0428 0.0622  -0.0219 143 LEU   C CA  
2132 C C   . LEU   B 137 ? 0.3098 0.3004 0.3377 -0.0441 0.0752  -0.0287 143 LEU   C C   
2133 O O   . LEU   B 137 ? 0.3096 0.3047 0.3615 -0.0387 0.0778  -0.0309 143 LEU   C O   
2134 C CB  . LEU   B 137 ? 0.2358 0.2355 0.2591 -0.0370 0.0509  -0.0199 143 LEU   C CB  
2135 C CG  . LEU   B 137 ? 0.2220 0.2269 0.2475 -0.0332 0.0396  -0.0145 143 LEU   C CG  
2136 C CD1 . LEU   B 137 ? 0.2197 0.2271 0.2438 -0.0288 0.0315  -0.0133 143 LEU   C CD1 
2137 C CD2 . LEU   B 137 ? 0.2115 0.2210 0.2568 -0.0287 0.0379  -0.0143 143 LEU   C CD2 
2138 N N   . ASP   B 138 ? 0.3565 0.3375 0.3629 -0.0513 0.0823  -0.0317 144 ASP   C N   
2139 C CA  . ASP   B 138 ? 0.4240 0.3973 0.4305 -0.0540 0.0963  -0.0390 144 ASP   C CA  
2140 C C   . ASP   B 138 ? 0.4772 0.4440 0.4844 -0.0596 0.1125  -0.0431 144 ASP   C C   
2141 O O   . ASP   B 138 ? 0.4963 0.4557 0.5051 -0.0618 0.1264  -0.0500 144 ASP   C O   
2142 C CB  . ASP   B 138 ? 0.4841 0.4472 0.4618 -0.0612 0.0965  -0.0405 144 ASP   C CB  
2143 C CG  . ASP   B 138 ? 0.5686 0.5357 0.5456 -0.0568 0.0849  -0.0383 144 ASP   C CG  
2144 O OD1 . ASP   B 138 ? 0.5824 0.5574 0.5814 -0.0482 0.0808  -0.0383 144 ASP   C OD1 
2145 O OD2 . ASP   B 138 ? 0.6380 0.5997 0.5922 -0.0626 0.0796  -0.0363 144 ASP   C OD2 
2146 N N   . GLU   B 139 ? 0.4980 0.4657 0.5013 -0.0629 0.1120  -0.0393 145 GLU   C N   
2147 C CA  . GLU   B 139 ? 0.5381 0.4993 0.5410 -0.0691 0.1282  -0.0428 145 GLU   C CA  
2148 C C   . GLU   B 139 ? 0.5517 0.5233 0.5827 -0.0639 0.1270  -0.0398 145 GLU   C C   
2149 O O   . GLU   B 139 ? 0.5700 0.5384 0.6042 -0.0686 0.1389  -0.0411 145 GLU   C O   
2150 C CB  . GLU   B 139 ? 0.5971 0.5461 0.5635 -0.0811 0.1301  -0.0407 145 GLU   C CB  
2151 C CG  . GLU   B 139 ? 0.6814 0.6355 0.6403 -0.0815 0.1148  -0.0317 145 GLU   C CG  
2152 C CD  . GLU   B 139 ? 0.8066 0.7490 0.7290 -0.0929 0.1111  -0.0276 145 GLU   C CD  
2153 O OE1 . GLU   B 139 ? 0.8097 0.7515 0.7252 -0.0970 0.1070  -0.0217 145 GLU   C OE1 
2154 O OE2 . GLU   B 139 ? 0.8527 0.7862 0.7537 -0.0982 0.1112  -0.0299 145 GLU   C OE2 
2155 N N1  . A1BQG C .   ? 0.2694 0.2395 0.3292 -0.0052 0.0635  0.0224  201 A1BQG A N1  
2156 N N3  . A1BQG C .   ? 0.4602 0.4343 0.4694 0.0009  0.0450  0.0207  201 A1BQG A N3  
2157 C C4  . A1BQG C .   ? 0.2790 0.2366 0.3213 -0.0008 0.0643  0.0309  201 A1BQG A C4  
2158 C C5  . A1BQG C .   ? 0.2969 0.2678 0.3501 -0.0046 0.0648  0.0215  201 A1BQG A C5  
2159 C C6  . A1BQG C .   ? 0.3659 0.3239 0.3895 0.0010  0.0658  0.0291  201 A1BQG A C6  
2160 C C7  . A1BQG C .   ? 0.4261 0.3839 0.4435 0.0016  0.0689  0.0278  201 A1BQG A C7  
2161 C C8  . A1BQG C .   ? 0.4513 0.3985 0.4686 0.0030  0.0845  0.0315  201 A1BQG A C8  
2162 C C10 . A1BQG C .   ? 0.4702 0.4238 0.4701 0.0046  0.0752  0.0268  201 A1BQG A C10 
2163 O O1  . A1BQG C .   ? 0.2771 0.2578 0.3466 -0.0075 0.0646  0.0143  201 A1BQG A O1  
2164 C C3  . A1BQG C .   ? 0.2785 0.2427 0.3170 -0.0003 0.0507  0.0293  201 A1BQG A C3  
2165 C C2  . A1BQG C .   ? 0.2501 0.2268 0.3119 -0.0050 0.0471  0.0216  201 A1BQG A C2  
2166 C C12 . A1BQG C .   ? 0.2427 0.2252 0.3262 -0.0092 0.0588  0.0140  201 A1BQG A C12 
2167 C C1  . A1BQG C .   ? 0.2274 0.2148 0.3022 -0.0081 0.0463  0.0134  201 A1BQG A C1  
2168 C C   . A1BQG C .   ? 0.2141 0.2121 0.3081 -0.0105 0.0413  0.0048  201 A1BQG A C   
2169 O O   . A1BQG C .   ? 0.2161 0.2139 0.3281 -0.0124 0.0463  0.0021  201 A1BQG A O   
2170 N N   . A1BQG C .   ? 0.1817 0.1879 0.2713 -0.0096 0.0318  0.0002  201 A1BQG A N   
2171 C C11 . A1BQG C .   ? 0.4540 0.4197 0.4630 0.0018  0.0577  0.0237  201 A1BQG A C11 
2172 N N2  . A1BQG C .   ? 0.4656 0.4292 0.4664 0.0032  0.0607  0.0232  201 A1BQG A N2  
2173 C C9  . A1BQG C .   ? 0.4663 0.4112 0.4744 0.0046  0.0879  0.0312  201 A1BQG A C9  
2179 N N1  . A1BQG F .   ? 0.2828 0.2169 0.2659 0.0105  0.0365  -0.0250 201 A1BQG C N1  
2180 N N3  . A1BQG F .   ? 0.4863 0.4262 0.4400 0.0037  0.0284  -0.0209 201 A1BQG C N3  
2181 C C4  . A1BQG F .   ? 0.2932 0.2134 0.2604 0.0075  0.0322  -0.0294 201 A1BQG C C4  
2182 C C5  . A1BQG F .   ? 0.3230 0.2578 0.3006 0.0099  0.0410  -0.0247 201 A1BQG C C5  
2183 C C6  . A1BQG F .   ? 0.3905 0.3110 0.3415 0.0054  0.0397  -0.0287 201 A1BQG C C6  
2184 C C7  . A1BQG F .   ? 0.4477 0.3681 0.3928 0.0046  0.0459  -0.0281 201 A1BQG C C7  
2185 C C8  . A1BQG F .   ? 0.4706 0.3793 0.4071 0.0042  0.0592  -0.0321 201 A1BQG C C8  
2186 C C10 . A1BQG F .   ? 0.4895 0.4060 0.4190 0.0015  0.0568  -0.0273 201 A1BQG C C10 
2187 O O1  . A1BQG F .   ? 0.2842 0.2298 0.2771 0.0123  0.0450  -0.0211 201 A1BQG C O1  
2188 C C3  . A1BQG F .   ? 0.2807 0.2087 0.2525 0.0061  0.0199  -0.0264 201 A1BQG C C3  
2189 C C2  . A1BQG F .   ? 0.2530 0.1955 0.2474 0.0091  0.0186  -0.0215 201 A1BQG C C2  
2190 C C12 . A1BQG F .   ? 0.2441 0.1919 0.2502 0.0134  0.0340  -0.0199 201 A1BQG C C12 
2191 C C1  . A1BQG F .   ? 0.2267 0.1813 0.2334 0.0115  0.0227  -0.0173 201 A1BQG C C1  
2192 C C   . A1BQG F .   ? 0.2111 0.1781 0.2371 0.0130  0.0199  -0.0117 201 A1BQG C C   
2193 O O   . A1BQG F .   ? 0.1984 0.1639 0.2351 0.0149  0.0225  -0.0108 201 A1BQG C O   
2194 N N   . A1BQG F .   ? 0.1976 0.1756 0.2272 0.0116  0.0147  -0.0078 201 A1BQG C N   
2195 C C11 . A1BQG F .   ? 0.4739 0.4037 0.4197 0.0036  0.0392  -0.0241 201 A1BQG C C11 
2196 N N2  . A1BQG F .   ? 0.4840 0.4118 0.4224 0.0022  0.0443  -0.0237 201 A1BQG C N2  
2197 C C9  . A1BQG F .   ? 0.4855 0.3921 0.4137 0.0024  0.0651  -0.0318 201 A1BQG C C9  
# 
