data_7HYZ
# 
_entry.id   7HYZ 
# 
_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   7HYZ         pdb_00007hyz 10.2210/pdb7hyz/pdb 
WWPDB D_1001408107 ?            ?                   
# 
_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                        7HYZ 
_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)-N~1~-(1-methyl-1H-1,3-benzimidazol-4-yl)piperidine-1,3-dicarboxamide' 301.344   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                  65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                        78.133    4   ?         ? ? ? 
5 water       nat water                                                                       18.015    341 ?         ? ? ? 
# 
_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)-N~1~-(1-methyl-1H-1,3-benzimidazol-4-yl)piperidine-1,3-dicarboxamide' A1BN0 
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 
A1BN0 non-polymer         . '(3S)-N~1~-(1-methyl-1H-1,3-benzimidazol-4-yl)piperidine-1,3-dicarboxamide' ? 'C15 H19 N5 O2'  301.344 
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        A1BN0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BN0 
_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 A1BN0 1   201 201 A1BN0 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 2   DMS   DMS A . 
F 4 DMS   1   204 6   DMS   DMS A . 
G 2 A1BN0 1   201 201 A1BN0 LIG C . 
H 3 ZN    1   202 1   ZN    ZN  C . 
I 4 DMS   1   203 2   DMS   DMS C . 
J 4 DMS   1   204 6   DMS   DMS C . 
K 5 HOH   1   301 95  HOH   HOH A . 
K 5 HOH   2   302 64  HOH   HOH A . 
K 5 HOH   3   303 65  HOH   HOH A . 
K 5 HOH   4   304 25  HOH   HOH A . 
K 5 HOH   5   305 237 HOH   HOH A . 
K 5 HOH   6   306 84  HOH   HOH A . 
K 5 HOH   7   307 149 HOH   HOH A . 
K 5 HOH   8   308 150 HOH   HOH A . 
K 5 HOH   9   309 61  HOH   HOH A . 
K 5 HOH   10  310 63  HOH   HOH A . 
K 5 HOH   11  311 93  HOH   HOH A . 
K 5 HOH   12  312 178 HOH   HOH A . 
K 5 HOH   13  313 103 HOH   HOH A . 
K 5 HOH   14  314 66  HOH   HOH A . 
K 5 HOH   15  315 109 HOH   HOH A . 
K 5 HOH   16  316 28  HOH   HOH A . 
K 5 HOH   17  317 7   HOH   HOH A . 
K 5 HOH   18  318 62  HOH   HOH A . 
K 5 HOH   19  319 171 HOH   HOH A . 
K 5 HOH   20  320 190 HOH   HOH A . 
K 5 HOH   21  321 246 HOH   HOH A . 
K 5 HOH   22  322 34  HOH   HOH A . 
K 5 HOH   23  323 30  HOH   HOH A . 
K 5 HOH   24  324 5   HOH   HOH A . 
K 5 HOH   25  325 59  HOH   HOH A . 
K 5 HOH   26  326 14  HOH   HOH A . 
K 5 HOH   27  327 241 HOH   HOH A . 
K 5 HOH   28  328 116 HOH   HOH A . 
K 5 HOH   29  329 85  HOH   HOH A . 
K 5 HOH   30  330 84  HOH   HOH A . 
K 5 HOH   31  331 33  HOH   HOH A . 
K 5 HOH   32  332 22  HOH   HOH A . 
K 5 HOH   33  333 27  HOH   HOH A . 
K 5 HOH   34  334 13  HOH   HOH A . 
K 5 HOH   35  335 22  HOH   HOH A . 
K 5 HOH   36  336 133 HOH   HOH A . 
K 5 HOH   37  337 152 HOH   HOH A . 
K 5 HOH   38  338 140 HOH   HOH A . 
K 5 HOH   39  339 72  HOH   HOH A . 
K 5 HOH   40  340 163 HOH   HOH A . 
K 5 HOH   41  341 114 HOH   HOH A . 
K 5 HOH   42  342 48  HOH   HOH A . 
K 5 HOH   43  343 60  HOH   HOH A . 
K 5 HOH   44  344 53  HOH   HOH A . 
K 5 HOH   45  345 23  HOH   HOH A . 
K 5 HOH   46  346 60  HOH   HOH A . 
K 5 HOH   47  347 17  HOH   HOH A . 
K 5 HOH   48  348 4   HOH   HOH A . 
K 5 HOH   49  349 66  HOH   HOH A . 
K 5 HOH   50  350 21  HOH   HOH A . 
K 5 HOH   51  351 176 HOH   HOH A . 
K 5 HOH   52  352 45  HOH   HOH A . 
K 5 HOH   53  353 88  HOH   HOH A . 
K 5 HOH   54  354 49  HOH   HOH A . 
K 5 HOH   55  355 19  HOH   HOH A . 
K 5 HOH   56  356 70  HOH   HOH A . 
K 5 HOH   57  357 3   HOH   HOH A . 
K 5 HOH   58  358 71  HOH   HOH A . 
K 5 HOH   59  359 56  HOH   HOH A . 
K 5 HOH   60  360 86  HOH   HOH A . 
K 5 HOH   61  361 115 HOH   HOH A . 
K 5 HOH   62  362 119 HOH   HOH A . 
K 5 HOH   63  363 10  HOH   HOH A . 
K 5 HOH   64  364 99  HOH   HOH A . 
K 5 HOH   65  365 79  HOH   HOH A . 
K 5 HOH   66  366 10  HOH   HOH A . 
K 5 HOH   67  367 53  HOH   HOH A . 
K 5 HOH   68  368 119 HOH   HOH A . 
K 5 HOH   69  369 26  HOH   HOH A . 
K 5 HOH   70  370 55  HOH   HOH A . 
K 5 HOH   71  371 35  HOH   HOH A . 
K 5 HOH   72  372 18  HOH   HOH A . 
K 5 HOH   73  373 32  HOH   HOH A . 
K 5 HOH   74  374 122 HOH   HOH A . 
K 5 HOH   75  375 29  HOH   HOH A . 
K 5 HOH   76  376 63  HOH   HOH A . 
K 5 HOH   77  377 102 HOH   HOH A . 
K 5 HOH   78  378 111 HOH   HOH A . 
K 5 HOH   79  379 149 HOH   HOH A . 
K 5 HOH   80  380 235 HOH   HOH A . 
K 5 HOH   81  381 92  HOH   HOH A . 
K 5 HOH   82  382 91  HOH   HOH A . 
K 5 HOH   83  383 231 HOH   HOH A . 
K 5 HOH   84  384 75  HOH   HOH A . 
K 5 HOH   85  385 19  HOH   HOH A . 
K 5 HOH   86  386 42  HOH   HOH A . 
K 5 HOH   87  387 153 HOH   HOH A . 
K 5 HOH   88  388 146 HOH   HOH A . 
K 5 HOH   89  389 197 HOH   HOH A . 
K 5 HOH   90  390 128 HOH   HOH A . 
K 5 HOH   91  391 115 HOH   HOH A . 
K 5 HOH   92  392 12  HOH   HOH A . 
K 5 HOH   93  393 38  HOH   HOH A . 
K 5 HOH   94  394 47  HOH   HOH A . 
K 5 HOH   95  395 23  HOH   HOH A . 
K 5 HOH   96  396 107 HOH   HOH A . 
K 5 HOH   97  397 26  HOH   HOH A . 
K 5 HOH   98  398 223 HOH   HOH A . 
K 5 HOH   99  399 96  HOH   HOH A . 
K 5 HOH   100 400 35  HOH   HOH A . 
K 5 HOH   101 401 114 HOH   HOH A . 
K 5 HOH   102 402 14  HOH   HOH A . 
K 5 HOH   103 403 40  HOH   HOH A . 
K 5 HOH   104 404 101 HOH   HOH A . 
K 5 HOH   105 405 52  HOH   HOH A . 
K 5 HOH   106 406 49  HOH   HOH A . 
K 5 HOH   107 407 36  HOH   HOH A . 
K 5 HOH   108 408 12  HOH   HOH A . 
K 5 HOH   109 409 112 HOH   HOH A . 
K 5 HOH   110 410 106 HOH   HOH A . 
K 5 HOH   111 411 16  HOH   HOH A . 
K 5 HOH   112 412 102 HOH   HOH A . 
K 5 HOH   113 413 228 HOH   HOH A . 
K 5 HOH   114 414 125 HOH   HOH A . 
K 5 HOH   115 415 73  HOH   HOH A . 
K 5 HOH   116 416 153 HOH   HOH A . 
K 5 HOH   117 417 208 HOH   HOH A . 
K 5 HOH   118 418 214 HOH   HOH A . 
K 5 HOH   119 419 209 HOH   HOH A . 
K 5 HOH   120 420 132 HOH   HOH A . 
K 5 HOH   121 421 113 HOH   HOH A . 
K 5 HOH   122 422 15  HOH   HOH A . 
K 5 HOH   123 423 183 HOH   HOH A . 
K 5 HOH   124 424 61  HOH   HOH A . 
K 5 HOH   125 425 157 HOH   HOH A . 
K 5 HOH   126 426 100 HOH   HOH A . 
K 5 HOH   127 427 238 HOH   HOH A . 
K 5 HOH   128 428 151 HOH   HOH A . 
K 5 HOH   129 429 130 HOH   HOH A . 
K 5 HOH   130 430 177 HOH   HOH A . 
K 5 HOH   131 431 202 HOH   HOH A . 
K 5 HOH   132 432 77  HOH   HOH A . 
K 5 HOH   133 433 99  HOH   HOH A . 
K 5 HOH   134 434 21  HOH   HOH A . 
K 5 HOH   135 435 100 HOH   HOH A . 
K 5 HOH   136 436 104 HOH   HOH A . 
K 5 HOH   137 437 94  HOH   HOH A . 
K 5 HOH   138 438 161 HOH   HOH A . 
K 5 HOH   139 439 126 HOH   HOH A . 
K 5 HOH   140 440 181 HOH   HOH A . 
K 5 HOH   141 441 82  HOH   HOH A . 
K 5 HOH   142 442 154 HOH   HOH A . 
K 5 HOH   143 443 201 HOH   HOH A . 
K 5 HOH   144 444 57  HOH   HOH A . 
K 5 HOH   145 445 136 HOH   HOH A . 
K 5 HOH   146 446 172 HOH   HOH A . 
K 5 HOH   147 447 92  HOH   HOH A . 
K 5 HOH   148 448 138 HOH   HOH A . 
K 5 HOH   149 449 217 HOH   HOH A . 
K 5 HOH   150 450 72  HOH   HOH A . 
K 5 HOH   151 451 24  HOH   HOH A . 
K 5 HOH   152 452 216 HOH   HOH A . 
K 5 HOH   153 453 58  HOH   HOH A . 
K 5 HOH   154 454 135 HOH   HOH A . 
K 5 HOH   155 455 129 HOH   HOH A . 
K 5 HOH   156 456 187 HOH   HOH A . 
K 5 HOH   157 457 132 HOH   HOH A . 
K 5 HOH   158 458 221 HOH   HOH A . 
K 5 HOH   159 459 219 HOH   HOH A . 
K 5 HOH   160 460 82  HOH   HOH A . 
K 5 HOH   161 461 67  HOH   HOH A . 
K 5 HOH   162 462 59  HOH   HOH A . 
K 5 HOH   163 463 226 HOH   HOH A . 
K 5 HOH   164 464 90  HOH   HOH A . 
K 5 HOH   165 465 206 HOH   HOH A . 
L 5 HOH   1   301 56  HOH   HOH C . 
L 5 HOH   2   302 120 HOH   HOH C . 
L 5 HOH   3   303 110 HOH   HOH C . 
L 5 HOH   4   304 134 HOH   HOH C . 
L 5 HOH   5   305 194 HOH   HOH C . 
L 5 HOH   6   306 137 HOH   HOH C . 
L 5 HOH   7   307 89  HOH   HOH C . 
L 5 HOH   8   308 32  HOH   HOH C . 
L 5 HOH   9   309 33  HOH   HOH C . 
L 5 HOH   10  310 64  HOH   HOH C . 
L 5 HOH   11  311 70  HOH   HOH C . 
L 5 HOH   12  312 233 HOH   HOH C . 
L 5 HOH   13  313 8   HOH   HOH C . 
L 5 HOH   14  314 28  HOH   HOH C . 
L 5 HOH   15  315 174 HOH   HOH C . 
L 5 HOH   16  316 121 HOH   HOH C . 
L 5 HOH   17  317 97  HOH   HOH C . 
L 5 HOH   18  318 139 HOH   HOH C . 
L 5 HOH   19  319 50  HOH   HOH C . 
L 5 HOH   20  320 124 HOH   HOH C . 
L 5 HOH   21  321 2   HOH   HOH C . 
L 5 HOH   22  322 155 HOH   HOH C . 
L 5 HOH   23  323 51  HOH   HOH C . 
L 5 HOH   24  324 43  HOH   HOH C . 
L 5 HOH   25  325 123 HOH   HOH C . 
L 5 HOH   26  326 98  HOH   HOH C . 
L 5 HOH   27  327 42  HOH   HOH C . 
L 5 HOH   28  328 133 HOH   HOH C . 
L 5 HOH   29  329 69  HOH   HOH C . 
L 5 HOH   30  330 97  HOH   HOH C . 
L 5 HOH   31  331 15  HOH   HOH C . 
L 5 HOH   32  332 71  HOH   HOH C . 
L 5 HOH   33  333 46  HOH   HOH C . 
L 5 HOH   34  334 80  HOH   HOH C . 
L 5 HOH   35  335 244 HOH   HOH C . 
L 5 HOH   36  336 138 HOH   HOH C . 
L 5 HOH   37  337 130 HOH   HOH C . 
L 5 HOH   38  338 74  HOH   HOH C . 
L 5 HOH   39  339 67  HOH   HOH C . 
L 5 HOH   40  340 38  HOH   HOH C . 
L 5 HOH   41  341 204 HOH   HOH C . 
L 5 HOH   42  342 98  HOH   HOH C . 
L 5 HOH   43  343 111 HOH   HOH C . 
L 5 HOH   44  344 122 HOH   HOH C . 
L 5 HOH   45  345 126 HOH   HOH C . 
L 5 HOH   46  346 39  HOH   HOH C . 
L 5 HOH   47  347 239 HOH   HOH C . 
L 5 HOH   48  348 249 HOH   HOH C . 
L 5 HOH   49  349 31  HOH   HOH C . 
L 5 HOH   50  350 30  HOH   HOH C . 
L 5 HOH   51  351 118 HOH   HOH C . 
L 5 HOH   52  352 248 HOH   HOH C . 
L 5 HOH   53  353 73  HOH   HOH C . 
L 5 HOH   54  354 65  HOH   HOH C . 
L 5 HOH   55  355 79  HOH   HOH C . 
L 5 HOH   56  356 37  HOH   HOH C . 
L 5 HOH   57  357 78  HOH   HOH C . 
L 5 HOH   58  358 158 HOH   HOH C . 
L 5 HOH   59  359 229 HOH   HOH C . 
L 5 HOH   60  360 110 HOH   HOH C . 
L 5 HOH   61  361 103 HOH   HOH C . 
L 5 HOH   62  362 6   HOH   HOH C . 
L 5 HOH   63  363 243 HOH   HOH C . 
L 5 HOH   64  364 20  HOH   HOH C . 
L 5 HOH   65  365 212 HOH   HOH C . 
L 5 HOH   66  366 234 HOH   HOH C . 
L 5 HOH   67  367 1   HOH   HOH C . 
L 5 HOH   68  368 191 HOH   HOH C . 
L 5 HOH   69  369 83  HOH   HOH C . 
L 5 HOH   70  370 91  HOH   HOH C . 
L 5 HOH   71  371 57  HOH   HOH C . 
L 5 HOH   72  372 86  HOH   HOH C . 
L 5 HOH   73  373 69  HOH   HOH C . 
L 5 HOH   74  374 4   HOH   HOH C . 
L 5 HOH   75  375 148 HOH   HOH C . 
L 5 HOH   76  376 205 HOH   HOH C . 
L 5 HOH   77  377 247 HOH   HOH C . 
L 5 HOH   78  378 18  HOH   HOH C . 
L 5 HOH   79  379 48  HOH   HOH C . 
L 5 HOH   80  380 142 HOH   HOH C . 
L 5 HOH   81  381 37  HOH   HOH C . 
L 5 HOH   82  382 9   HOH   HOH C . 
L 5 HOH   83  383 141 HOH   HOH C . 
L 5 HOH   84  384 80  HOH   HOH C . 
L 5 HOH   85  385 7   HOH   HOH C . 
L 5 HOH   86  386 124 HOH   HOH C . 
L 5 HOH   87  387 50  HOH   HOH C . 
L 5 HOH   88  388 54  HOH   HOH C . 
L 5 HOH   89  389 11  HOH   HOH C . 
L 5 HOH   90  390 232 HOH   HOH C . 
L 5 HOH   91  391 62  HOH   HOH C . 
L 5 HOH   92  392 144 HOH   HOH C . 
L 5 HOH   93  393 89  HOH   HOH C . 
L 5 HOH   94  394 136 HOH   HOH C . 
L 5 HOH   95  395 85  HOH   HOH C . 
L 5 HOH   96  396 16  HOH   HOH C . 
L 5 HOH   97  397 195 HOH   HOH C . 
L 5 HOH   98  398 108 HOH   HOH C . 
L 5 HOH   99  399 210 HOH   HOH C . 
L 5 HOH   100 400 240 HOH   HOH C . 
L 5 HOH   101 401 29  HOH   HOH C . 
L 5 HOH   102 402 127 HOH   HOH C . 
L 5 HOH   103 403 40  HOH   HOH C . 
L 5 HOH   104 404 83  HOH   HOH C . 
L 5 HOH   105 405 11  HOH   HOH C . 
L 5 HOH   106 406 44  HOH   HOH C . 
L 5 HOH   107 407 120 HOH   HOH C . 
L 5 HOH   108 408 13  HOH   HOH C . 
L 5 HOH   109 409 87  HOH   HOH C . 
L 5 HOH   110 410 107 HOH   HOH C . 
L 5 HOH   111 411 230 HOH   HOH C . 
L 5 HOH   112 412 31  HOH   HOH C . 
L 5 HOH   113 413 54  HOH   HOH C . 
L 5 HOH   114 414 140 HOH   HOH C . 
L 5 HOH   115 415 45  HOH   HOH C . 
L 5 HOH   116 416 78  HOH   HOH C . 
L 5 HOH   117 417 3   HOH   HOH C . 
L 5 HOH   118 418 146 HOH   HOH C . 
L 5 HOH   119 419 68  HOH   HOH C . 
L 5 HOH   120 420 87  HOH   HOH C . 
L 5 HOH   121 421 41  HOH   HOH C . 
L 5 HOH   122 422 44  HOH   HOH C . 
L 5 HOH   123 423 137 HOH   HOH C . 
L 5 HOH   124 424 105 HOH   HOH C . 
L 5 HOH   125 425 41  HOH   HOH C . 
L 5 HOH   126 426 43  HOH   HOH C . 
L 5 HOH   127 427 94  HOH   HOH C . 
L 5 HOH   128 428 236 HOH   HOH C . 
L 5 HOH   129 429 106 HOH   HOH C . 
L 5 HOH   130 430 90  HOH   HOH C . 
L 5 HOH   131 431 135 HOH   HOH C . 
L 5 HOH   132 432 74  HOH   HOH C . 
L 5 HOH   133 433 105 HOH   HOH C . 
L 5 HOH   134 434 20  HOH   HOH C . 
L 5 HOH   135 435 250 HOH   HOH C . 
L 5 HOH   136 436 118 HOH   HOH C . 
L 5 HOH   137 437 145 HOH   HOH C . 
L 5 HOH   138 438 104 HOH   HOH C . 
L 5 HOH   139 439 144 HOH   HOH C . 
L 5 HOH   140 440 117 HOH   HOH C . 
L 5 HOH   141 441 148 HOH   HOH C . 
L 5 HOH   142 442 116 HOH   HOH C . 
L 5 HOH   143 443 242 HOH   HOH C . 
L 5 HOH   144 444 188 HOH   HOH C . 
L 5 HOH   145 445 96  HOH   HOH C . 
L 5 HOH   146 446 5   HOH   HOH C . 
L 5 HOH   147 447 200 HOH   HOH C . 
L 5 HOH   148 448 47  HOH   HOH C . 
L 5 HOH   149 449 147 HOH   HOH C . 
L 5 HOH   150 450 117 HOH   HOH C . 
L 5 HOH   151 451 251 HOH   HOH C . 
L 5 HOH   152 452 143 HOH   HOH C . 
L 5 HOH   153 453 95  HOH   HOH C . 
L 5 HOH   154 454 131 HOH   HOH C . 
L 5 HOH   155 455 185 HOH   HOH C . 
L 5 HOH   156 456 198 HOH   HOH C . 
L 5 HOH   157 457 139 HOH   HOH C . 
L 5 HOH   158 458 17  HOH   HOH C . 
L 5 HOH   159 459 142 HOH   HOH C . 
L 5 HOH   160 460 93  HOH   HOH C . 
L 5 HOH   161 461 151 HOH   HOH C . 
L 5 HOH   162 462 199 HOH   HOH C . 
L 5 HOH   163 463 152 HOH   HOH C . 
L 5 HOH   164 464 166 HOH   HOH C . 
L 5 HOH   165 465 81  HOH   HOH C . 
L 5 HOH   166 466 123 HOH   HOH C . 
L 5 HOH   167 467 222 HOH   HOH C . 
L 5 HOH   168 468 141 HOH   HOH C . 
L 5 HOH   169 469 245 HOH   HOH C . 
L 5 HOH   170 470 218 HOH   HOH C . 
L 5 HOH   171 471 25  HOH   HOH C . 
L 5 HOH   172 472 170 HOH   HOH C . 
L 5 HOH   173 473 196 HOH   HOH C . 
L 5 HOH   174 474 207 HOH   HOH C . 
L 5 HOH   175 475 150 HOH   HOH C . 
L 5 HOH   176 476 213 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           7HYZ 
_cell.length_a           72.635 
_cell.length_b           61.785 
_cell.length_c           65.161 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.84 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HYZ 
_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          7HYZ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.30 
_exptl_crystal.density_percent_sol   46.46 
_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   2024-12-11 
_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   0.92199 
_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        0.92199 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HYZ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.04 
_reflns.d_resolution_high            1.52 
_reflns.number_obs                   44192 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.109 
_reflns.pdbx_netI_over_sigmaI        8.2 
_reflns.pdbx_redundancy              5.4 
_reflns.pdbx_Rrim_I_all              0.121 
_reflns.pdbx_Rpim_I_all              0.051 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     240332 
_reflns.pdbx_chi_squared             0.88 
_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                  1.52 
_reflns_shell.d_res_low                   1.60 
_reflns_shell.number_measured_all         29342 
_reflns_shell.number_unique_obs           6413 
_reflns_shell.Rmerge_I_obs                1.334 
_reflns_shell.pdbx_chi_squared            0.77 
_reflns_shell.pdbx_redundancy             4.6 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.1 
_reflns_shell.pdbx_Rrim_I_all             1.508 
_reflns_shell.pdbx_Rpim_I_all             0.691 
_reflns_shell.pdbx_CC_half                0.459 
_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                                 7HYZ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     44148 
_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                             47.04 
_refine.ls_d_res_high                            1.522 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_R_factor_obs                          0.1889 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1878 
_refine.ls_R_factor_R_free                       0.2123 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.940 
_refine.ls_number_reflns_R_free                  2183 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.953 
_refine.B_iso_mean                               23.79 
_refine.aniso_B[1][1]                            -0.42460 
_refine.aniso_B[2][2]                            0.60760 
_refine.aniso_B[3][3]                            -0.18310 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.63120 
_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             0.078 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.077 
_refine.pdbx_overall_SU_R_Blow_DPI               0.084 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.081 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HYZ 
_refine_analyze.Luzzati_coordinate_error_obs    0.20 
_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         54 
_refine_hist.number_atoms_solvent             341 
_refine_hist.number_atoms_total               2543 
_refine_hist.d_res_high                       1.522 
_refine_hist.d_res_low                        47.04 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  2268 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.97  ? 2.00  3086 '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  420  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2262 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.27  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.39 ? ?     ?    '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  2069 '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                       1.52 
_refine_ls_shell.d_res_low                        1.53 
_refine_ls_shell.number_reflns_R_work             840 
_refine_ls_shell.R_factor_R_work                  0.2880 
_refine_ls_shell.percent_reflns_obs               98.63 
_refine_ls_shell.R_factor_R_free                  0.3272 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.87 
_refine_ls_shell.number_reflns_R_free             43 
_refine_ls_shell.number_reflns_all                883 
_refine_ls_shell.R_factor_all                     0.2899 
# 
_struct.entry_id                  7HYZ 
_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-0032645-001 (A71EV2A-x4447)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HYZ 
_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 4 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
K N N 5 ? 
L 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 7HYZ A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HYZ 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,F,K 
2 1 B,G,H,I,J,L 
# 
_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 ? ? ? ? ? ? ? 2.349 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.350 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.311 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 H ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.121 ? ? 
# 
_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_555 111.1 ? 
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_555 105.4 ? 
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_555 107.4 ? 
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_555 102.4 ? 
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_555 114.7 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.5 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.3 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? H ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 116.7 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 108.2 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? H ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.3 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? H ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.5 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
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 
AA1 3 4 ? 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 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
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 ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
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 GLN B 89  ? O GLN C 95  N ILE B 76  ? N ILE C 82  
# 
_pdbx_entry_details.entry_id                   7HYZ 
_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 A HOH 347 ? ? O A HOH 357 ? ? 1.47 
2  1 O A HOH 357 ? ? O A HOH 363 ? ? 1.65 
3  1 O A HOH 303 ? ? O A HOH 304 ? ? 1.86 
4  1 O C HOH 336 ? ? O C HOH 424 ? ? 1.89 
5  1 O A HOH 360 ? ? O A HOH 370 ? ? 2.06 
6  1 O A HOH 323 ? ? O A HOH 352 ? ? 2.07 
7  1 O C HOH 440 ? ? O C HOH 453 ? ? 2.08 
8  1 O C HOH 303 ? ? O C HOH 423 ? ? 2.09 
9  1 O A HOH 348 ? ? O A HOH 372 ? ? 2.11 
10 1 O A HOH 404 ? ? O A HOH 449 ? ? 2.16 
11 1 O C HOH 301 ? ? O C HOH 405 ? ? 2.18 
12 1 O A HOH 370 ? ? O A HOH 373 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     362 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     317 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_555 
_pdbx_validate_symm_contact.dist              1.92 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    C 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -133.22 
_pdbx_validate_torsion.psi             -31.82 
# 
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 19.6777 6.7583   18.2380 -0.0287 -0.0334 0.0028  -0.0009 0.0111 -0.0008 1.0210 1.2322 0.6234 
-0.5966 -0.1818 0.1186 -0.0210 -0.0160 0.1158 0.0163 0.0469 0.0256  0.0345  0.0562  -0.0260 
'X-RAY DIFFRACTION' 2 ? refined 15.2813 -23.9715 14.1832 -0.0228 -0.0227 -0.0012 0.0018  0.0045 -0.0066 0.7212 1.1809 0.5289 
0.5223  0.1761  0.0221 -0.0362 0.0182  0.0434 0.0080 0.0596 -0.0312 -0.0017 -0.0068 -0.0233 
# 
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|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      C 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       476 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.16 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
11 1 N 0 A DMS 203 ? E DMS ?   
12 1 N 0 C DMS 203 ? I DMS ?   
# 
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 
A1BN0 N1   N  Y N 1   
A1BN0 N3   N  N N 2   
A1BN0 C4   C  N N 3   
A1BN0 C5   C  N N 4   
A1BN0 C6   C  N N 5   
A1BN0 C7   C  N N 6   
A1BN0 C8   C  N S 7   
A1BN0 C10  C  N N 8   
A1BN0 C13  C  Y N 9   
A1BN0 O1   O  N N 10  
A1BN0 C9   C  N N 11  
A1BN0 N4   N  N N 12  
A1BN0 O    O  N N 13  
A1BN0 N2   N  N N 14  
A1BN0 C3   C  Y N 15  
A1BN0 C11  C  Y N 16  
A1BN0 C12  C  Y N 17  
A1BN0 C14  C  Y N 18  
A1BN0 N    N  Y N 19  
A1BN0 C    C  N N 20  
A1BN0 C2   C  Y N 21  
A1BN0 C1   C  Y N 22  
A1BN0 H6   H  N N 23  
A1BN0 H7   H  N N 24  
A1BN0 H8   H  N N 25  
A1BN0 H9   H  N N 26  
A1BN0 H10  H  N N 27  
A1BN0 H11  H  N N 28  
A1BN0 H    H  N N 29  
A1BN0 H14  H  N N 30  
A1BN0 H15  H  N N 31  
A1BN0 H18  H  N N 32  
A1BN0 H12  H  N N 33  
A1BN0 H13  H  N N 34  
A1BN0 H5   H  N N 35  
A1BN0 H16  H  N N 36  
A1BN0 H17  H  N N 37  
A1BN0 H3   H  N N 38  
A1BN0 H1   H  N N 39  
A1BN0 H2   H  N N 40  
A1BN0 H4   H  N N 41  
ALA   N    N  N N 42  
ALA   CA   C  N S 43  
ALA   C    C  N N 44  
ALA   O    O  N N 45  
ALA   CB   C  N N 46  
ALA   OXT  O  N N 47  
ALA   H    H  N N 48  
ALA   H2   H  N N 49  
ALA   HA   H  N N 50  
ALA   HB1  H  N N 51  
ALA   HB2  H  N N 52  
ALA   HB3  H  N N 53  
ALA   HXT  H  N N 54  
ARG   N    N  N N 55  
ARG   CA   C  N S 56  
ARG   C    C  N N 57  
ARG   O    O  N N 58  
ARG   CB   C  N N 59  
ARG   CG   C  N N 60  
ARG   CD   C  N N 61  
ARG   NE   N  N N 62  
ARG   CZ   C  N N 63  
ARG   NH1  N  N N 64  
ARG   NH2  N  N N 65  
ARG   OXT  O  N N 66  
ARG   H    H  N N 67  
ARG   H2   H  N N 68  
ARG   HA   H  N N 69  
ARG   HB2  H  N N 70  
ARG   HB3  H  N N 71  
ARG   HG2  H  N N 72  
ARG   HG3  H  N N 73  
ARG   HD2  H  N N 74  
ARG   HD3  H  N N 75  
ARG   HE   H  N N 76  
ARG   HH11 H  N N 77  
ARG   HH12 H  N N 78  
ARG   HH21 H  N N 79  
ARG   HH22 H  N N 80  
ARG   HXT  H  N N 81  
ASN   N    N  N N 82  
ASN   CA   C  N S 83  
ASN   C    C  N N 84  
ASN   O    O  N N 85  
ASN   CB   C  N N 86  
ASN   CG   C  N N 87  
ASN   OD1  O  N N 88  
ASN   ND2  N  N N 89  
ASN   OXT  O  N N 90  
ASN   H    H  N N 91  
ASN   H2   H  N N 92  
ASN   HA   H  N N 93  
ASN   HB2  H  N N 94  
ASN   HB3  H  N N 95  
ASN   HD21 H  N N 96  
ASN   HD22 H  N N 97  
ASN   HXT  H  N N 98  
ASP   N    N  N N 99  
ASP   CA   C  N S 100 
ASP   C    C  N N 101 
ASP   O    O  N N 102 
ASP   CB   C  N N 103 
ASP   CG   C  N N 104 
ASP   OD1  O  N N 105 
ASP   OD2  O  N N 106 
ASP   OXT  O  N N 107 
ASP   H    H  N N 108 
ASP   H2   H  N N 109 
ASP   HA   H  N N 110 
ASP   HB2  H  N N 111 
ASP   HB3  H  N N 112 
ASP   HD2  H  N N 113 
ASP   HXT  H  N N 114 
CYS   N    N  N N 115 
CYS   CA   C  N R 116 
CYS   C    C  N N 117 
CYS   O    O  N N 118 
CYS   CB   C  N N 119 
CYS   SG   S  N N 120 
CYS   OXT  O  N N 121 
CYS   H    H  N N 122 
CYS   H2   H  N N 123 
CYS   HA   H  N N 124 
CYS   HB2  H  N N 125 
CYS   HB3  H  N N 126 
CYS   HG   H  N N 127 
CYS   HXT  H  N N 128 
DMS   S    S  N N 129 
DMS   O    O  N N 130 
DMS   C1   C  N N 131 
DMS   C2   C  N N 132 
DMS   H11  H  N N 133 
DMS   H12  H  N N 134 
DMS   H13  H  N N 135 
DMS   H21  H  N N 136 
DMS   H22  H  N N 137 
DMS   H23  H  N N 138 
GLN   N    N  N N 139 
GLN   CA   C  N S 140 
GLN   C    C  N N 141 
GLN   O    O  N N 142 
GLN   CB   C  N N 143 
GLN   CG   C  N N 144 
GLN   CD   C  N N 145 
GLN   OE1  O  N N 146 
GLN   NE2  N  N N 147 
GLN   OXT  O  N N 148 
GLN   H    H  N N 149 
GLN   H2   H  N N 150 
GLN   HA   H  N N 151 
GLN   HB2  H  N N 152 
GLN   HB3  H  N N 153 
GLN   HG2  H  N N 154 
GLN   HG3  H  N N 155 
GLN   HE21 H  N N 156 
GLN   HE22 H  N N 157 
GLN   HXT  H  N N 158 
GLU   N    N  N N 159 
GLU   CA   C  N S 160 
GLU   C    C  N N 161 
GLU   O    O  N N 162 
GLU   CB   C  N N 163 
GLU   CG   C  N N 164 
GLU   CD   C  N N 165 
GLU   OE1  O  N N 166 
GLU   OE2  O  N N 167 
GLU   OXT  O  N N 168 
GLU   H    H  N N 169 
GLU   H2   H  N N 170 
GLU   HA   H  N N 171 
GLU   HB2  H  N N 172 
GLU   HB3  H  N N 173 
GLU   HG2  H  N N 174 
GLU   HG3  H  N N 175 
GLU   HE2  H  N N 176 
GLU   HXT  H  N N 177 
GLY   N    N  N N 178 
GLY   CA   C  N N 179 
GLY   C    C  N N 180 
GLY   O    O  N N 181 
GLY   OXT  O  N N 182 
GLY   H    H  N N 183 
GLY   H2   H  N N 184 
GLY   HA2  H  N N 185 
GLY   HA3  H  N N 186 
GLY   HXT  H  N N 187 
HIS   N    N  N N 188 
HIS   CA   C  N S 189 
HIS   C    C  N N 190 
HIS   O    O  N N 191 
HIS   CB   C  N N 192 
HIS   CG   C  Y N 193 
HIS   ND1  N  Y N 194 
HIS   CD2  C  Y N 195 
HIS   CE1  C  Y N 196 
HIS   NE2  N  Y N 197 
HIS   OXT  O  N N 198 
HIS   H    H  N N 199 
HIS   H2   H  N N 200 
HIS   HA   H  N N 201 
HIS   HB2  H  N N 202 
HIS   HB3  H  N N 203 
HIS   HD1  H  N N 204 
HIS   HD2  H  N N 205 
HIS   HE1  H  N N 206 
HIS   HE2  H  N N 207 
HIS   HXT  H  N N 208 
HOH   O    O  N N 209 
HOH   H1   H  N N 210 
HOH   H2   H  N N 211 
ILE   N    N  N N 212 
ILE   CA   C  N S 213 
ILE   C    C  N N 214 
ILE   O    O  N N 215 
ILE   CB   C  N S 216 
ILE   CG1  C  N N 217 
ILE   CG2  C  N N 218 
ILE   CD1  C  N N 219 
ILE   OXT  O  N N 220 
ILE   H    H  N N 221 
ILE   H2   H  N N 222 
ILE   HA   H  N N 223 
ILE   HB   H  N N 224 
ILE   HG12 H  N N 225 
ILE   HG13 H  N N 226 
ILE   HG21 H  N N 227 
ILE   HG22 H  N N 228 
ILE   HG23 H  N N 229 
ILE   HD11 H  N N 230 
ILE   HD12 H  N N 231 
ILE   HD13 H  N N 232 
ILE   HXT  H  N N 233 
LEU   N    N  N N 234 
LEU   CA   C  N S 235 
LEU   C    C  N N 236 
LEU   O    O  N N 237 
LEU   CB   C  N N 238 
LEU   CG   C  N N 239 
LEU   CD1  C  N N 240 
LEU   CD2  C  N N 241 
LEU   OXT  O  N N 242 
LEU   H    H  N N 243 
LEU   H2   H  N N 244 
LEU   HA   H  N N 245 
LEU   HB2  H  N N 246 
LEU   HB3  H  N N 247 
LEU   HG   H  N N 248 
LEU   HD11 H  N N 249 
LEU   HD12 H  N N 250 
LEU   HD13 H  N N 251 
LEU   HD21 H  N N 252 
LEU   HD22 H  N N 253 
LEU   HD23 H  N N 254 
LEU   HXT  H  N N 255 
LYS   N    N  N N 256 
LYS   CA   C  N S 257 
LYS   C    C  N N 258 
LYS   O    O  N N 259 
LYS   CB   C  N N 260 
LYS   CG   C  N N 261 
LYS   CD   C  N N 262 
LYS   CE   C  N N 263 
LYS   NZ   N  N N 264 
LYS   OXT  O  N N 265 
LYS   H    H  N N 266 
LYS   H2   H  N N 267 
LYS   HA   H  N N 268 
LYS   HB2  H  N N 269 
LYS   HB3  H  N N 270 
LYS   HG2  H  N N 271 
LYS   HG3  H  N N 272 
LYS   HD2  H  N N 273 
LYS   HD3  H  N N 274 
LYS   HE2  H  N N 275 
LYS   HE3  H  N N 276 
LYS   HZ1  H  N N 277 
LYS   HZ2  H  N N 278 
LYS   HZ3  H  N N 279 
LYS   HXT  H  N N 280 
MET   N    N  N N 281 
MET   CA   C  N S 282 
MET   C    C  N N 283 
MET   O    O  N N 284 
MET   CB   C  N N 285 
MET   CG   C  N N 286 
MET   SD   S  N N 287 
MET   CE   C  N N 288 
MET   OXT  O  N N 289 
MET   H    H  N N 290 
MET   H2   H  N N 291 
MET   HA   H  N N 292 
MET   HB2  H  N N 293 
MET   HB3  H  N N 294 
MET   HG2  H  N N 295 
MET   HG3  H  N N 296 
MET   HE1  H  N N 297 
MET   HE2  H  N N 298 
MET   HE3  H  N N 299 
MET   HXT  H  N N 300 
PHE   N    N  N N 301 
PHE   CA   C  N S 302 
PHE   C    C  N N 303 
PHE   O    O  N N 304 
PHE   CB   C  N N 305 
PHE   CG   C  Y N 306 
PHE   CD1  C  Y N 307 
PHE   CD2  C  Y N 308 
PHE   CE1  C  Y N 309 
PHE   CE2  C  Y N 310 
PHE   CZ   C  Y N 311 
PHE   OXT  O  N N 312 
PHE   H    H  N N 313 
PHE   H2   H  N N 314 
PHE   HA   H  N N 315 
PHE   HB2  H  N N 316 
PHE   HB3  H  N N 317 
PHE   HD1  H  N N 318 
PHE   HD2  H  N N 319 
PHE   HE1  H  N N 320 
PHE   HE2  H  N N 321 
PHE   HZ   H  N N 322 
PHE   HXT  H  N N 323 
PRO   N    N  N N 324 
PRO   CA   C  N S 325 
PRO   C    C  N N 326 
PRO   O    O  N N 327 
PRO   CB   C  N N 328 
PRO   CG   C  N N 329 
PRO   CD   C  N N 330 
PRO   OXT  O  N N 331 
PRO   H    H  N N 332 
PRO   HA   H  N N 333 
PRO   HB2  H  N N 334 
PRO   HB3  H  N N 335 
PRO   HG2  H  N N 336 
PRO   HG3  H  N N 337 
PRO   HD2  H  N N 338 
PRO   HD3  H  N N 339 
PRO   HXT  H  N N 340 
SER   N    N  N N 341 
SER   CA   C  N S 342 
SER   C    C  N N 343 
SER   O    O  N N 344 
SER   CB   C  N N 345 
SER   OG   O  N N 346 
SER   OXT  O  N N 347 
SER   H    H  N N 348 
SER   H2   H  N N 349 
SER   HA   H  N N 350 
SER   HB2  H  N N 351 
SER   HB3  H  N N 352 
SER   HG   H  N N 353 
SER   HXT  H  N N 354 
THR   N    N  N N 355 
THR   CA   C  N S 356 
THR   C    C  N N 357 
THR   O    O  N N 358 
THR   CB   C  N R 359 
THR   OG1  O  N N 360 
THR   CG2  C  N N 361 
THR   OXT  O  N N 362 
THR   H    H  N N 363 
THR   H2   H  N N 364 
THR   HA   H  N N 365 
THR   HB   H  N N 366 
THR   HG1  H  N N 367 
THR   HG21 H  N N 368 
THR   HG22 H  N N 369 
THR   HG23 H  N N 370 
THR   HXT  H  N N 371 
TRP   N    N  N N 372 
TRP   CA   C  N S 373 
TRP   C    C  N N 374 
TRP   O    O  N N 375 
TRP   CB   C  N N 376 
TRP   CG   C  Y N 377 
TRP   CD1  C  Y N 378 
TRP   CD2  C  Y N 379 
TRP   NE1  N  Y N 380 
TRP   CE2  C  Y N 381 
TRP   CE3  C  Y N 382 
TRP   CZ2  C  Y N 383 
TRP   CZ3  C  Y N 384 
TRP   CH2  C  Y N 385 
TRP   OXT  O  N N 386 
TRP   H    H  N N 387 
TRP   H2   H  N N 388 
TRP   HA   H  N N 389 
TRP   HB2  H  N N 390 
TRP   HB3  H  N N 391 
TRP   HD1  H  N N 392 
TRP   HE1  H  N N 393 
TRP   HE3  H  N N 394 
TRP   HZ2  H  N N 395 
TRP   HZ3  H  N N 396 
TRP   HH2  H  N N 397 
TRP   HXT  H  N N 398 
TYR   N    N  N N 399 
TYR   CA   C  N S 400 
TYR   C    C  N N 401 
TYR   O    O  N N 402 
TYR   CB   C  N N 403 
TYR   CG   C  Y N 404 
TYR   CD1  C  Y N 405 
TYR   CD2  C  Y N 406 
TYR   CE1  C  Y N 407 
TYR   CE2  C  Y N 408 
TYR   CZ   C  Y N 409 
TYR   OH   O  N N 410 
TYR   OXT  O  N N 411 
TYR   H    H  N N 412 
TYR   H2   H  N N 413 
TYR   HA   H  N N 414 
TYR   HB2  H  N N 415 
TYR   HB3  H  N N 416 
TYR   HD1  H  N N 417 
TYR   HD2  H  N N 418 
TYR   HE1  H  N N 419 
TYR   HE2  H  N N 420 
TYR   HH   H  N N 421 
TYR   HXT  H  N N 422 
VAL   N    N  N N 423 
VAL   CA   C  N S 424 
VAL   C    C  N N 425 
VAL   O    O  N N 426 
VAL   CB   C  N N 427 
VAL   CG1  C  N N 428 
VAL   CG2  C  N N 429 
VAL   OXT  O  N N 430 
VAL   H    H  N N 431 
VAL   H2   H  N N 432 
VAL   HA   H  N N 433 
VAL   HB   H  N N 434 
VAL   HG11 H  N N 435 
VAL   HG12 H  N N 436 
VAL   HG13 H  N N 437 
VAL   HG21 H  N N 438 
VAL   HG22 H  N N 439 
VAL   HG23 H  N N 440 
VAL   HXT  H  N N 441 
ZN    ZN   ZN N N 442 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BN0 C   N    sing N N 1   
A1BN0 N   C1   sing Y N 2   
A1BN0 C1  N1   doub Y N 3   
A1BN0 N1  C2   sing Y N 4   
A1BN0 C2  C3   doub Y N 5   
A1BN0 C3  N2   sing N N 6   
A1BN0 N2  C4   sing N N 7   
A1BN0 O   C4   doub N N 8   
A1BN0 C4  N3   sing N N 9   
A1BN0 N3  C5   sing N N 10  
A1BN0 C5  C6   sing N N 11  
A1BN0 C6  C7   sing N N 12  
A1BN0 C7  C8   sing N N 13  
A1BN0 C8  C9   sing N N 14  
A1BN0 N4  C9   sing N N 15  
A1BN0 C9  O1   doub N N 16  
A1BN0 C10 C8   sing N N 17  
A1BN0 N3  C10  sing N N 18  
A1BN0 C11 C3   sing Y N 19  
A1BN0 C12 C11  doub Y N 20  
A1BN0 C13 C12  sing Y N 21  
A1BN0 C14 C13  doub Y N 22  
A1BN0 C2  C14  sing Y N 23  
A1BN0 N   C14  sing Y N 24  
A1BN0 C5  H6   sing N N 25  
A1BN0 C5  H7   sing N N 26  
A1BN0 C6  H8   sing N N 27  
A1BN0 C6  H9   sing N N 28  
A1BN0 C7  H10  sing N N 29  
A1BN0 C7  H11  sing N N 30  
A1BN0 C8  H    sing N N 31  
A1BN0 C10 H14  sing N N 32  
A1BN0 C10 H15  sing N N 33  
A1BN0 C13 H18  sing N N 34  
A1BN0 N4  H12  sing N N 35  
A1BN0 N4  H13  sing N N 36  
A1BN0 N2  H5   sing N N 37  
A1BN0 C11 H16  sing N N 38  
A1BN0 C12 H17  sing N N 39  
A1BN0 C   H3   sing N N 40  
A1BN0 C   H1   sing N N 41  
A1BN0 C   H2   sing N N 42  
A1BN0 C1  H4   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
DMS   S   O    doub N N 126 
DMS   S   C1   sing N N 127 
DMS   S   C2   sing N N 128 
DMS   C1  H11  sing N N 129 
DMS   C1  H12  sing N N 130 
DMS   C1  H13  sing N N 131 
DMS   C2  H21  sing N N 132 
DMS   C2  H22  sing N N 133 
DMS   C2  H23  sing N N 134 
GLN   N   CA   sing N N 135 
GLN   N   H    sing N N 136 
GLN   N   H2   sing N N 137 
GLN   CA  C    sing N N 138 
GLN   CA  CB   sing N N 139 
GLN   CA  HA   sing N N 140 
GLN   C   O    doub N N 141 
GLN   C   OXT  sing N N 142 
GLN   CB  CG   sing N N 143 
GLN   CB  HB2  sing N N 144 
GLN   CB  HB3  sing N N 145 
GLN   CG  CD   sing N N 146 
GLN   CG  HG2  sing N N 147 
GLN   CG  HG3  sing N N 148 
GLN   CD  OE1  doub N N 149 
GLN   CD  NE2  sing N N 150 
GLN   NE2 HE21 sing N N 151 
GLN   NE2 HE22 sing N N 152 
GLN   OXT HXT  sing N N 153 
GLU   N   CA   sing N N 154 
GLU   N   H    sing N N 155 
GLU   N   H2   sing N N 156 
GLU   CA  C    sing N N 157 
GLU   CA  CB   sing N N 158 
GLU   CA  HA   sing N N 159 
GLU   C   O    doub N N 160 
GLU   C   OXT  sing N N 161 
GLU   CB  CG   sing N N 162 
GLU   CB  HB2  sing N N 163 
GLU   CB  HB3  sing N N 164 
GLU   CG  CD   sing N N 165 
GLU   CG  HG2  sing N N 166 
GLU   CG  HG3  sing N N 167 
GLU   CD  OE1  doub N N 168 
GLU   CD  OE2  sing N N 169 
GLU   OE2 HE2  sing N N 170 
GLU   OXT HXT  sing N N 171 
GLY   N   CA   sing N N 172 
GLY   N   H    sing N N 173 
GLY   N   H2   sing N N 174 
GLY   CA  C    sing N N 175 
GLY   CA  HA2  sing N N 176 
GLY   CA  HA3  sing N N 177 
GLY   C   O    doub N N 178 
GLY   C   OXT  sing N N 179 
GLY   OXT HXT  sing N N 180 
HIS   N   CA   sing N N 181 
HIS   N   H    sing N N 182 
HIS   N   H2   sing N N 183 
HIS   CA  C    sing N N 184 
HIS   CA  CB   sing N N 185 
HIS   CA  HA   sing N N 186 
HIS   C   O    doub N N 187 
HIS   C   OXT  sing N N 188 
HIS   CB  CG   sing N N 189 
HIS   CB  HB2  sing N N 190 
HIS   CB  HB3  sing N N 191 
HIS   CG  ND1  sing Y N 192 
HIS   CG  CD2  doub Y N 193 
HIS   ND1 CE1  doub Y N 194 
HIS   ND1 HD1  sing N N 195 
HIS   CD2 NE2  sing Y N 196 
HIS   CD2 HD2  sing N N 197 
HIS   CE1 NE2  sing Y N 198 
HIS   CE1 HE1  sing N N 199 
HIS   NE2 HE2  sing N N 200 
HIS   OXT HXT  sing N N 201 
HOH   O   H1   sing N N 202 
HOH   O   H2   sing N N 203 
ILE   N   CA   sing N N 204 
ILE   N   H    sing N N 205 
ILE   N   H2   sing N N 206 
ILE   CA  C    sing N N 207 
ILE   CA  CB   sing N N 208 
ILE   CA  HA   sing N N 209 
ILE   C   O    doub N N 210 
ILE   C   OXT  sing N N 211 
ILE   CB  CG1  sing N N 212 
ILE   CB  CG2  sing N N 213 
ILE   CB  HB   sing N N 214 
ILE   CG1 CD1  sing N N 215 
ILE   CG1 HG12 sing N N 216 
ILE   CG1 HG13 sing N N 217 
ILE   CG2 HG21 sing N N 218 
ILE   CG2 HG22 sing N N 219 
ILE   CG2 HG23 sing N N 220 
ILE   CD1 HD11 sing N N 221 
ILE   CD1 HD12 sing N N 222 
ILE   CD1 HD13 sing N N 223 
ILE   OXT HXT  sing N N 224 
LEU   N   CA   sing N N 225 
LEU   N   H    sing N N 226 
LEU   N   H2   sing N N 227 
LEU   CA  C    sing N N 228 
LEU   CA  CB   sing N N 229 
LEU   CA  HA   sing N N 230 
LEU   C   O    doub N N 231 
LEU   C   OXT  sing N N 232 
LEU   CB  CG   sing N N 233 
LEU   CB  HB2  sing N N 234 
LEU   CB  HB3  sing N N 235 
LEU   CG  CD1  sing N N 236 
LEU   CG  CD2  sing N N 237 
LEU   CG  HG   sing N N 238 
LEU   CD1 HD11 sing N N 239 
LEU   CD1 HD12 sing N N 240 
LEU   CD1 HD13 sing N N 241 
LEU   CD2 HD21 sing N N 242 
LEU   CD2 HD22 sing N N 243 
LEU   CD2 HD23 sing N N 244 
LEU   OXT HXT  sing N N 245 
LYS   N   CA   sing N N 246 
LYS   N   H    sing N N 247 
LYS   N   H2   sing N N 248 
LYS   CA  C    sing N N 249 
LYS   CA  CB   sing N N 250 
LYS   CA  HA   sing N N 251 
LYS   C   O    doub N N 252 
LYS   C   OXT  sing N N 253 
LYS   CB  CG   sing N N 254 
LYS   CB  HB2  sing N N 255 
LYS   CB  HB3  sing N N 256 
LYS   CG  CD   sing N N 257 
LYS   CG  HG2  sing N N 258 
LYS   CG  HG3  sing N N 259 
LYS   CD  CE   sing N N 260 
LYS   CD  HD2  sing N N 261 
LYS   CD  HD3  sing N N 262 
LYS   CE  NZ   sing N N 263 
LYS   CE  HE2  sing N N 264 
LYS   CE  HE3  sing N N 265 
LYS   NZ  HZ1  sing N N 266 
LYS   NZ  HZ2  sing N N 267 
LYS   NZ  HZ3  sing N N 268 
LYS   OXT HXT  sing N N 269 
MET   N   CA   sing N N 270 
MET   N   H    sing N N 271 
MET   N   H2   sing N N 272 
MET   CA  C    sing N N 273 
MET   CA  CB   sing N N 274 
MET   CA  HA   sing N N 275 
MET   C   O    doub N N 276 
MET   C   OXT  sing N N 277 
MET   CB  CG   sing N N 278 
MET   CB  HB2  sing N N 279 
MET   CB  HB3  sing N N 280 
MET   CG  SD   sing N N 281 
MET   CG  HG2  sing N N 282 
MET   CG  HG3  sing N N 283 
MET   SD  CE   sing N N 284 
MET   CE  HE1  sing N N 285 
MET   CE  HE2  sing N N 286 
MET   CE  HE3  sing N N 287 
MET   OXT HXT  sing N N 288 
PHE   N   CA   sing N N 289 
PHE   N   H    sing N N 290 
PHE   N   H2   sing N N 291 
PHE   CA  C    sing N N 292 
PHE   CA  CB   sing N N 293 
PHE   CA  HA   sing N N 294 
PHE   C   O    doub N N 295 
PHE   C   OXT  sing N N 296 
PHE   CB  CG   sing N N 297 
PHE   CB  HB2  sing N N 298 
PHE   CB  HB3  sing N N 299 
PHE   CG  CD1  doub Y N 300 
PHE   CG  CD2  sing Y N 301 
PHE   CD1 CE1  sing Y N 302 
PHE   CD1 HD1  sing N N 303 
PHE   CD2 CE2  doub Y N 304 
PHE   CD2 HD2  sing N N 305 
PHE   CE1 CZ   doub Y N 306 
PHE   CE1 HE1  sing N N 307 
PHE   CE2 CZ   sing Y N 308 
PHE   CE2 HE2  sing N N 309 
PHE   CZ  HZ   sing N N 310 
PHE   OXT HXT  sing N N 311 
PRO   N   CA   sing N N 312 
PRO   N   CD   sing N N 313 
PRO   N   H    sing N N 314 
PRO   CA  C    sing N N 315 
PRO   CA  CB   sing N N 316 
PRO   CA  HA   sing N N 317 
PRO   C   O    doub N N 318 
PRO   C   OXT  sing N N 319 
PRO   CB  CG   sing N N 320 
PRO   CB  HB2  sing N N 321 
PRO   CB  HB3  sing N N 322 
PRO   CG  CD   sing N N 323 
PRO   CG  HG2  sing N N 324 
PRO   CG  HG3  sing N N 325 
PRO   CD  HD2  sing N N 326 
PRO   CD  HD3  sing N N 327 
PRO   OXT HXT  sing N N 328 
SER   N   CA   sing N N 329 
SER   N   H    sing N N 330 
SER   N   H2   sing N N 331 
SER   CA  C    sing N N 332 
SER   CA  CB   sing N N 333 
SER   CA  HA   sing N N 334 
SER   C   O    doub N N 335 
SER   C   OXT  sing N N 336 
SER   CB  OG   sing N N 337 
SER   CB  HB2  sing N N 338 
SER   CB  HB3  sing N N 339 
SER   OG  HG   sing N N 340 
SER   OXT HXT  sing N N 341 
THR   N   CA   sing N N 342 
THR   N   H    sing N N 343 
THR   N   H2   sing N N 344 
THR   CA  C    sing N N 345 
THR   CA  CB   sing N N 346 
THR   CA  HA   sing N N 347 
THR   C   O    doub N N 348 
THR   C   OXT  sing N N 349 
THR   CB  OG1  sing N N 350 
THR   CB  CG2  sing N N 351 
THR   CB  HB   sing N N 352 
THR   OG1 HG1  sing N N 353 
THR   CG2 HG21 sing N N 354 
THR   CG2 HG22 sing N N 355 
THR   CG2 HG23 sing N N 356 
THR   OXT HXT  sing N N 357 
TRP   N   CA   sing N N 358 
TRP   N   H    sing N N 359 
TRP   N   H2   sing N N 360 
TRP   CA  C    sing N N 361 
TRP   CA  CB   sing N N 362 
TRP   CA  HA   sing N N 363 
TRP   C   O    doub N N 364 
TRP   C   OXT  sing N N 365 
TRP   CB  CG   sing N N 366 
TRP   CB  HB2  sing N N 367 
TRP   CB  HB3  sing N N 368 
TRP   CG  CD1  doub Y N 369 
TRP   CG  CD2  sing Y N 370 
TRP   CD1 NE1  sing Y N 371 
TRP   CD1 HD1  sing N N 372 
TRP   CD2 CE2  doub Y N 373 
TRP   CD2 CE3  sing Y N 374 
TRP   NE1 CE2  sing Y N 375 
TRP   NE1 HE1  sing N N 376 
TRP   CE2 CZ2  sing Y N 377 
TRP   CE3 CZ3  doub Y N 378 
TRP   CE3 HE3  sing N N 379 
TRP   CZ2 CH2  doub Y N 380 
TRP   CZ2 HZ2  sing N N 381 
TRP   CZ3 CH2  sing Y N 382 
TRP   CZ3 HZ3  sing N N 383 
TRP   CH2 HH2  sing N N 384 
TRP   OXT HXT  sing N N 385 
TYR   N   CA   sing N N 386 
TYR   N   H    sing N N 387 
TYR   N   H2   sing N N 388 
TYR   CA  C    sing N N 389 
TYR   CA  CB   sing N N 390 
TYR   CA  HA   sing N N 391 
TYR   C   O    doub N N 392 
TYR   C   OXT  sing N N 393 
TYR   CB  CG   sing N N 394 
TYR   CB  HB2  sing N N 395 
TYR   CB  HB3  sing N N 396 
TYR   CG  CD1  doub Y N 397 
TYR   CG  CD2  sing Y N 398 
TYR   CD1 CE1  sing Y N 399 
TYR   CD1 HD1  sing N N 400 
TYR   CD2 CE2  doub Y N 401 
TYR   CD2 HD2  sing N N 402 
TYR   CE1 CZ   doub Y N 403 
TYR   CE1 HE1  sing N N 404 
TYR   CE2 CZ   sing Y N 405 
TYR   CE2 HE2  sing N N 406 
TYR   CZ  OH   sing N N 407 
TYR   OH  HH   sing N N 408 
TYR   OXT HXT  sing N N 409 
VAL   N   CA   sing N N 410 
VAL   N   H    sing N N 411 
VAL   N   H2   sing N N 412 
VAL   CA  C    sing N N 413 
VAL   CA  CB   sing N N 414 
VAL   CA  HA   sing N N 415 
VAL   C   O    doub N N 416 
VAL   C   OXT  sing N N 417 
VAL   CB  CG1  sing N N 418 
VAL   CB  CG2  sing N N 419 
VAL   CB  HB   sing N N 420 
VAL   CG1 HG11 sing N N 421 
VAL   CG1 HG12 sing N N 422 
VAL   CG1 HG13 sing N N 423 
VAL   CG2 HG21 sing N N 424 
VAL   CG2 HG22 sing N N 425 
VAL   CG2 HG23 sing N N 426 
VAL   OXT HXT  sing N N 427 
# 
_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                    7HYZ 
_atom_sites.fract_transf_matrix[1][1]   0.013767 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000683 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016185 
_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]   0.015365 
_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   ? 16.384 6.453   8.100  1.00 20.38  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.149 6.572   8.885  1.00 20.55  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 14.985 5.424   9.875  1.00 20.63  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.607 4.371   9.709  1.00 21.38  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 13.945 6.663   7.947  1.00 23.61  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.835 5.439   7.239  1.00 27.42  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.146 5.618   10.895 1.00 19.32  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.879 4.572   11.871 1.00 18.25  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.469 5.119   13.230 1.00 17.52  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.829 6.251   13.589 1.00 18.29  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.744 4.310   14.007 1.00 15.64  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.309 4.730   15.326 1.00 16.03  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.238 3.520   16.261 1.00 16.30  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.177 2.363   15.795 1.00 16.74  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.915 5.354   15.213 1.00 16.65  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.256 3.791   17.588 1.00 14.54  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 12.030 2.783   18.617 1.00 14.83  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.610 3.014   19.107 1.00 15.50  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.250 4.153   19.413 1.00 15.63  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 13.001 2.977   19.805 1.00 14.74  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.475 2.927   19.307 1.00 14.72  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.764 1.920   20.893 1.00 15.95  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.428 3.489   20.337 1.00 15.74  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.814  1.948   19.238 1.00 16.24  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.444  2.077   19.743 1.00 17.50  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.336  1.308   21.043 1.00 17.58  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.348  0.090   20.994 1.00 18.46  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.448  1.503   18.711 1.00 18.09  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.387  2.349   17.462 1.00 19.67  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.565  3.467   17.395 1.00 21.32  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.182  2.059   16.363 1.00 21.91  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.522  4.264   16.259 1.00 22.35  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.168  2.864   15.233 1.00 23.12  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.323  3.954   15.180 1.00 24.09  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.298  4.757   14.068 1.00 27.07  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.312  1.980   22.199 1.00 17.62  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.270  1.309   23.501 1.00 18.24  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.136  1.895   24.318 1.00 19.73  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 7.048  3.109   24.473 1.00 20.74  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.641  1.438   24.238 1.00 19.37  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.158 2.880   24.233 1.00 19.24  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.572  0.892   25.657 1.00 20.62  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.191  1.050   24.761 1.00 20.32  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 5.051  1.535   25.525 1.00 20.62  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.252  2.522   24.694 1.00 21.21  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 4.041  2.277   23.503 1.00 21.05  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 3.958  3.702   25.262 1.00 21.47  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.271  4.737   24.493 1.00 21.98  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.227  5.830   24.034 1.00 20.35  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.839  6.998   23.944 1.00 20.71  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 2.104  5.322   25.262 1.00 25.24  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 1.014  4.297   25.417 1.00 32.68  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.354  3.912   24.448 1.00 35.67  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.855  3.801   26.626 1.00 34.46  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.467  5.442   23.689 1.00 18.33  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.483  6.391   23.232 1.00 17.44  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 7.075  5.961   21.894 1.00 15.70  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.207  4.748   21.621 1.00 15.47  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.649  6.449   24.237 1.00 18.09  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.252  6.973   25.594 1.00 19.43  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.589  8.187   25.727 1.00 20.82  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.528  6.256   26.743 1.00 20.70  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.245  8.690   26.978 1.00 22.28  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.178  6.745   27.999 1.00 21.96  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.515  7.954   28.108 1.00 23.94  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.176  8.477   29.327 1.00 26.51  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.493  6.967   21.087 1.00 14.40  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.195  6.785   19.828 1.00 14.04  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.503  7.581   19.972 1.00 14.68  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.453  8.765   20.265 1.00 15.37  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.346  7.325   18.648 1.00 15.17  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.106  7.521   17.340 1.00 18.47  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.188  7.868   16.175 1.00 18.52  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.750  8.907   15.297 1.00 21.26  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.278  8.683   14.102 1.00 24.77  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.375  7.439   13.634 1.00 25.80  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.751  9.694   13.376 1.00 23.29  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.661 6.909   19.846 1.00 14.29  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 11.967 7.580   19.961 1.00 14.37  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.550 7.725   18.559 1.00 15.31  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.705 6.719   17.866 1.00 14.93  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 12.954 6.743   20.833 1.00 14.64  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.251 7.558   21.109 1.00 14.23  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.301 6.293   22.150 1.00 14.15  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.895 8.944   18.151 1.00 14.50  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.470 9.174   16.826 1.00 15.04  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.697 10.073  16.938 1.00 14.14  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.887 10.782  17.950 1.00 14.36  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.433 9.848   15.880 1.00 15.75  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.313 8.890   15.531 1.00 18.12  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.878 11.135  16.510 1.00 16.02  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.490 10.163  15.835 1.00 13.54  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.548 11.184  15.786 1.00 13.13  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.857 12.561  15.790 1.00 13.96  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.920 12.780  15.002 1.00 14.51  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.323 11.081  14.480 1.00 13.13  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.133 9.833   14.401 1.00 15.47  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.685 8.833   13.824 1.00 16.11  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.349 9.882   14.953 1.00 16.02  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.302 13.476  16.644 1.00 13.58  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.663 14.810  16.727 1.00 13.19  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.671 15.516  15.338 1.00 14.38  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.662 16.129  14.949 1.00 15.66  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.343 15.657  17.791 1.00 13.84  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.574 16.939  18.139 1.00 14.50  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.491 17.794  18.995 1.00 16.00  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.868 19.027  19.497 1.00 16.89  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.841 20.179  18.834 1.00 18.25  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.314 20.251  17.592 1.00 17.76  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.342 21.273  19.408 1.00 17.88  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.764 15.345  14.558 1.00 14.61  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.849 16.025  13.248 1.00 15.56  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.897 15.450  12.195 1.00 16.89  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.673 16.095  11.165 1.00 18.99  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.316 16.091  12.729 1.00 16.39  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.882 14.792  12.239 1.00 16.50  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.440 13.861  13.107 1.00 17.33  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 18.995 14.332  10.967 1.00 18.01  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.870 12.865  12.339 1.00 18.38  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.611 13.099  11.043 1.00 18.86  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.324 14.251  12.454 1.00 16.30  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.362 13.617  11.540 1.00 16.58  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.918 13.655  12.071 1.00 16.93  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 12.025 13.062  11.453 1.00 16.70  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.792 12.164  11.228 1.00 16.51  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.179 12.014  10.561 1.00 17.54  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.482 10.544  10.310 1.00 18.03  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.258 12.822  9.237  1.00 17.75  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.674 14.302  13.233 1.00 16.46  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.312 14.315  13.806 1.00 16.26  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.343 15.014  12.843 1.00 16.89  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.710 15.986  12.204 1.00 16.30  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.310 15.042  15.144 1.00 16.33  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.120  14.504  12.751 1.00 17.82  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 8.091  15.054  11.866 1.00 19.53  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.264  16.140  12.570 1.00 20.23  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.409  16.333  13.784 1.00 19.19  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.156  13.892  11.421 1.00 21.34  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.420  13.423  12.563 1.00 22.02  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.921  12.754  10.785 1.00 22.20  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.318  16.808  11.831 1.00 21.53  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.410  17.768  12.457 1.00 23.69  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.577  17.053  13.549 1.00 21.57  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.362  17.608  14.624 1.00 21.58  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.430  18.370  11.415 1.00 28.58  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 5.079  19.131  10.303 1.00 37.65  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.911  20.208  10.553 1.00 41.41  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 4.951  18.977  8.961  1.00 40.66  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.294  20.647  9.364  1.00 42.63  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.733  19.941  8.375  1.00 42.59  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.157  15.796  13.287 1.00 21.62  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.373  15.051  14.274 1.00 21.09  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.181  14.711  15.536 1.00 19.14  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.634  14.764  16.645 1.00 19.06  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.787  13.784  13.673 1.00 23.44  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.495  14.032  12.949 1.00 29.95  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.642  14.830  13.392 1.00 31.04  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 1.360  13.400  11.797 1.00 31.20  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.481  14.389  15.397 1.00 17.52  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.330  14.151  16.564 1.00 16.07  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.377  15.410  17.448 1.00 16.41  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.223  15.303  18.665 1.00 17.30  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.768  13.825  16.106 1.00 14.77  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.921  12.422  15.573 1.00 19.33  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.269  11.509  16.123 1.00 20.19  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.698  12.240  14.593 1.00 19.87  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.582  16.597  16.833 1.00 16.40  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.656  17.839  17.596 1.00 17.17  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.299  18.194  18.222 1.00 19.22  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.256  18.741  19.334 1.00 19.92  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.197  18.973  16.722 1.00 17.07  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.703  18.983  16.614 1.00 18.25  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.457  18.536  15.568 1.00 19.19  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.627  19.495  17.585 1.00 18.18  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.804 18.729  15.836 1.00 19.18  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.932 19.295  17.079 1.00 19.13  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.483  20.021  18.864 1.00 19.14  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 12.079 19.696  17.784 1.00 19.62  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.616 20.449  19.540 1.00 19.95  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.896 20.229  19.028 1.00 19.97  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.189  17.855  17.547 1.00 19.76  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.850  18.133  18.105 1.00 20.65  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.481  17.203  19.287 1.00 21.17  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.521  17.472  20.044 1.00 21.96  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.799  18.002  17.015 1.00 21.63  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.178  16.061  19.405 1.00 19.69  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 2.945  15.116  20.489 1.00 20.17  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.239  14.957  21.316 1.00 19.43  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.535  13.882  21.819 1.00 18.27  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.493  13.774  19.902 1.00 21.87  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.134  13.859  19.252 1.00 26.09  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.111  13.864  19.947 1.00 26.39  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 1.092  13.923  17.917 1.00 26.70  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 5.009  16.046  21.465 1.00 18.62  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.301  16.031  22.143 1.00 18.74  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.228  15.646  23.618 1.00 18.52  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.366  16.151  24.356 1.00 19.10  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 6.912  17.418  22.010 1.00 19.20  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.272  17.641  22.692 1.00 19.41  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.374  16.771  22.060 1.00 19.95  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.703  19.121  22.585 1.00 19.19  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.129  14.747  24.043 1.00 17.84  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.282  14.356  25.443 1.00 18.99  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.610  14.951  25.967 1.00 19.70  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.672  15.568  27.041 1.00 20.88  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.283  12.800  25.584 1.00 19.82  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.683  12.374  26.995 1.00 20.74  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 5.912  12.228  25.219 1.00 20.26  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.692  14.783  25.177 1.00 18.06  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 11.019 15.245  25.581 1.00 18.50  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 11.908 15.322  24.362 1.00 17.06  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.782 14.491  23.463 1.00 17.24  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.620 14.211  26.578 1.00 19.64  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 13.076 14.384  26.929 1.00 20.35  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.614 15.213  27.876 1.00 21.77  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.166 13.641  26.383 1.00 19.88  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 14.988 15.067  27.906 1.00 21.95  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.350 14.111  26.992 1.00 20.61  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.265 12.670  25.389 1.00 19.44  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.604 13.567  26.703 1.00 21.03  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.509 12.141  25.094 1.00 20.26  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.663 12.601  25.739 1.00 20.90  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.813 16.286  24.337 1.00 16.73  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.818 16.356  23.259 1.00 16.70  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 15.118 16.923  23.817 1.00 16.48  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 15.108 17.725  24.765 1.00 16.89  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.315 17.143  22.026 1.00 17.40  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.731 18.524  22.328 1.00 18.98  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.745 19.627  22.610 1.00 21.87  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.420 20.535  23.413 1.00 26.97  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.864 19.579  22.053 1.00 20.62  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.252 16.536  23.206 1.00 16.11  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.537 17.048  23.636 1.00 16.33  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.414 17.200  22.400 1.00 16.84  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.876 16.204  21.830 1.00 16.30  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 18.149 16.117  24.691 1.00 19.26  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.410 16.643  25.358 1.00 26.75  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.132 17.448  24.722 1.00 29.08  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.699 16.215  26.490 1.00 27.43  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.644 18.452  21.974 1.00 18.04  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.462 18.745  20.806 0.50 19.08  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.460 18.704  20.790 0.50 18.77  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.905 18.218  20.989 1.00 18.83  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.524 17.747  20.028 1.00 19.61  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.451 20.250  20.535 0.50 21.04  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.427 20.184  20.407 0.50 19.91  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 20.367 20.622  19.523 0.50 23.86  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 20.086 20.965  21.388 0.50 21.18  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.441 18.277  22.239 1.00 18.25  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.811 17.782  22.467 1.00 19.86  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 22.936 16.266  22.294 1.00 19.11  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 24.034 15.794  22.090 1.00 20.14  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.353 18.189  23.834 1.00 23.18  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.787 17.404  24.867 1.00 27.71  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.832 15.523  22.354 1.00 16.74  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.858 14.066  22.178 1.00 15.68  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.308 13.627  20.799 1.00 15.62  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.355 12.426  20.483 1.00 14.75  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 20.991 13.401  23.283 1.00 16.26  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.567 13.601  24.681 1.00 17.08  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.749 12.917  25.775 1.00 16.61  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.713 11.454  25.630 1.00 15.99  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.499 10.605  26.632 1.00 18.34  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.345 11.059  27.882 1.00 18.65  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.508 9.288   26.410 1.00 16.25  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.732 14.574  20.010 1.00 15.03  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 20.050 14.277  18.744 1.00 14.26  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.880 13.308  18.993 1.00 14.61  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.612 12.454  18.146 1.00 14.94  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 20.988 13.708  17.659 1.00 15.79  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.289 13.481  16.313 1.00 15.86  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.488 14.346  15.910 1.00 16.27  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.574 12.433  15.651 1.00 15.74  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.152 13.460  20.119 1.00 13.89  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 16.997 12.596  20.420 1.00 13.45  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.710 13.396  20.608 1.00 13.94  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.729 14.481  21.189 1.00 14.83  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.210 11.782  21.719 1.00 13.84  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.221 10.618  21.639 1.00 14.92  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.280 9.873   22.986 1.00 16.35  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.838 9.619   20.529 1.00 14.39  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.598 12.787  20.230 1.00 12.88  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.267 13.341  20.473 1.00 12.77  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.352 12.153  20.768 1.00 13.63  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.450 11.101  20.116 1.00 13.77  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.766 14.174  19.268 1.00 13.47  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.400 14.851  19.474 1.00 15.11  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.351 16.189  18.743 1.00 17.46  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.249 13.952  18.932 1.00 14.38  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.449 12.317  21.730 1.00 13.76  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.481 11.272  22.096 1.00 14.18  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 9.102  11.917  22.008 1.00 14.91  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 8.874  13.005  22.554 1.00 15.92  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.724 10.749  23.544 1.00 15.54  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.631  9.736   23.943 1.00 15.60  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 12.111 10.103  23.663 1.00 15.83  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.195  11.243  21.315 1.00 14.84  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.821  11.708  21.173 1.00 15.91  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.865  10.619  21.685 1.00 17.97  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.263  9.443   21.832 1.00 17.19  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.509  12.052  19.719 1.00 17.44  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.635  10.925  18.860 1.00 19.21  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.620  11.010  21.974 1.00 18.77  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.644  10.030  22.485 1.00 19.29  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 2.861  9.332   21.374 1.00 20.78  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.638  9.904   20.316 1.00 21.40  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.711  10.704  23.491 1.00 20.99  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 2.081  11.807  22.876 1.00 23.99  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.424  8.092   21.607 1.00 21.60  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.669  7.333   20.604 1.00 23.88  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.352  6.843   21.224 1.00 27.11  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.241  6.765   22.450 1.00 28.20  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.480  6.106   20.109 1.00 24.54  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.596  5.183   21.190 1.00 26.15  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.863  6.459   19.614 1.00 23.68  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.615 6.489   20.391 1.00 28.89  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -1.881 5.937   20.879 1.00 31.29  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.778 4.400   20.979 1.00 32.94  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.379 3.795   21.876 1.00 34.76  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -3.042 6.408   19.996 1.00 33.72  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.712 6.138   18.627 1.00 35.51  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.328 7.889   20.165 1.00 34.31  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -1.013 3.771   20.078 1.00 31.95  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.835 2.320   20.075 1.00 31.94  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.363  1.888   20.947 1.00 32.13  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.320  2.646   21.112 1.00 31.59  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.638 1.838   18.651 1.00 31.92  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.307  0.664   21.487 1.00 32.27  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.385  0.121   22.318 1.00 32.95  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.520  -0.337  21.417 1.00 31.91  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.259  -0.974  20.395 1.00 32.33  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.870  -1.066  23.133 1.00 36.94  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.784  -1.434  24.297 1.00 44.18  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 1.558  -0.554  25.511 1.00 52.98  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 0.565  0.185   25.623 1.00 55.75  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 2.474  -0.634  26.470 1.00 55.10  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.757  0.026   21.744 1.00 30.59  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 4.905  -0.288  20.893 1.00 29.67  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.376  -1.726  20.915 1.00 29.37  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 5.065  -2.456  21.852 1.00 31.04  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.204  -2.102  19.916 1.00 26.70  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.764  -3.436  19.713 1.00 25.38  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 8.126  -3.691  20.422 1.00 24.79  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.508  -4.844  20.599 1.00 24.60  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 6.891  -3.689  18.210 1.00 25.74  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 7.949  -2.490  17.330 1.00 27.68  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.856  -2.647  20.806 1.00 23.45  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.219 -2.789  21.353 1.00 21.78  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.351 -2.796  22.883 1.00 21.10  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 9.438  -2.318  23.574 1.00 22.16  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 11.097 -1.650  20.782 1.00 21.26  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.241 -1.695  19.268 1.00 23.70  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 11.673 -2.751  18.748 1.00 24.28  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 10.963 -0.654  18.600 1.00 20.18  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 11.509 -3.334  23.410 1.00 20.15  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 11.945 -3.337  24.815 1.00 21.31  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.415 -2.754  24.909 1.00 20.17  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.211 -2.951  23.994 1.00 20.55  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 11.727 -4.706  25.497 1.00 25.68  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 12.661 -5.642  24.971 1.00 28.26  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 10.311 -5.255  25.307 1.00 26.15  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 13.737 -1.984  25.966 1.00 18.44  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 15.021 -1.270  26.088 1.00 17.04  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 15.987 -2.024  26.965 1.00 17.72  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.598 -2.528  28.022 1.00 18.41  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 14.793 0.154   26.705 1.00 17.22  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.683 0.947   25.961 1.00 18.64  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 16.114 0.981   26.731 1.00 17.02  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 13.984 1.192   24.446 1.00 19.87  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.232 -2.155  26.514 1.00 16.18  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.282 -2.810  27.296 1.00 16.87  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.616 -1.934  28.518 1.00 16.95  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.676 -0.725  28.405 1.00 16.76  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.547 -2.967  26.431 1.00 16.42  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 18.912 -2.567  29.666 1.00 17.48  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.319 -1.838  30.892 1.00 17.59  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.590 -2.589  31.296 1.00 18.74  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.541 -3.582  32.018 1.00 19.08  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.218 -1.903  31.974 1.00 17.92  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.876 -1.302  31.532 1.00 18.68  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.938 0.196   31.187 1.00 20.13  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.605 0.702   30.832 1.00 20.07  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.386 1.840   30.172 1.00 22.36  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.395 2.628   29.841 1.00 20.98  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 14.151 2.208   29.865 1.00 22.45  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 21.712 -2.212  30.677 1.00 18.95  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 22.956 -2.986  30.779 1.00 19.88  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.171 -2.099  30.444 1.00 21.02  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 24.014 -0.935  30.074 1.00 22.06  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 22.869 -4.149  29.794 1.00 19.41  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 22.894 -3.612  28.060 1.00 19.07  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.388 -2.697  30.503 1.00 22.13  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.596 -1.987  30.094 1.00 23.28  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.273 -2.710  28.922 1.00 23.38  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.498 -2.674  28.810 1.00 24.19  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 27.591 -1.812  31.258 1.00 27.49  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 28.110 -3.101  31.871 1.00 35.47  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 27.626 -4.183  31.484 1.00 34.89  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 29.013 -3.025  32.731 1.00 42.33  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.495 -3.383  28.046 1.00 21.80  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 27.089 -4.059  26.877 1.00 19.65  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 27.844 -3.048  26.005 1.00 19.28  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.415 -1.895  25.869 1.00 19.00  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 26.015 -4.749  26.041 1.00 19.77  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.346 -6.296  26.737 1.00 19.30  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 28.978 -3.477  25.459 1.00 17.12  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 29.774 -2.713  24.492 1.00 17.40  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 29.930 -3.485  23.176 1.00 16.69  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 30.803 -3.156  22.377 1.00 17.15  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 31.142 -2.323  25.021 1.00 20.40  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 31.085 -1.218  26.026 1.00 26.19  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.500 -0.828  26.408 1.00 31.49  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 32.923 -1.028  27.549 1.00 32.97  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.278 -0.268  25.465 1.00 29.62  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 29.099 -4.537  22.959 1.00 15.66  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 29.013 -5.253  21.693 1.00 15.38  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.518 -5.429  21.390 1.00 15.20  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.670 -5.496  22.295 1.00 15.91  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 29.736 -6.609  21.682 1.00 16.90  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 29.056 -7.498  22.570 1.00 17.95  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 31.196 -6.494  22.059 1.00 18.52  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.202 -5.436  20.119 1.00 13.72  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 25.820 -5.589  19.691 1.00 13.69  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 25.763 -5.681  18.175 1.00 13.42  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 26.792 -5.904  17.510 1.00 14.62  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.559 -5.567  17.646 1.00 13.67  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.306 -5.676  16.209 1.00 14.34  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.426 -4.487  15.801 1.00 14.03  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.423 -4.211  16.458 1.00 14.74  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.604 -7.019  15.902 1.00 16.18  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.220 -7.099  14.423 1.00 17.60  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.490 -8.200  16.288 1.00 16.52  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 23.763 -3.818  14.679 1.00 13.26  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 22.939 -2.710  14.196 1.00 13.21  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.421 -2.953  12.789 1.00 12.93  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 23.050 -3.667  12.002 1.00 12.56  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.675 -1.339  14.288 1.00 12.78  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.697 -1.073  13.193 1.00 12.69  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 25.958 -1.649  13.232 1.00 13.33  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.430 -0.177  12.158 1.00 13.62  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 26.926 -1.349  12.272 1.00 13.77  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.381 0.095   11.166 1.00 14.48  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.629 -0.490  11.229 1.00 14.88  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.580 -0.268  10.251 1.00 17.56  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.282 -2.319  12.455 1.00 13.21  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.745 -2.423  11.112 1.00 14.19  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.252 -1.250  10.261 1.00 14.14  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.116 -0.083  10.658 1.00 13.71  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.196 -2.432  11.111 1.00 14.78  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.669 -2.552  9.704  1.00 15.22  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 18.872 -3.704  8.967  1.00 15.35  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 18.006 -1.490  9.094  1.00 15.69  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.423 -3.809  7.658  1.00 17.22  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.546 -1.581  7.786  1.00 16.29  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.763 -2.740  7.074  1.00 18.33  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.318 -2.840  5.783  1.00 22.50  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.841 -1.568  9.094  1.00 13.85  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.401 -0.568  8.175  1.00 13.56  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.511 -0.536  6.893  1.00 14.17  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.627 -1.421  6.040  1.00 15.13  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.846 -0.940  7.850  1.00 14.33  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.627 0.097   6.579  1.00 16.64  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.597 0.460   6.783  1.00 13.55  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.693 0.518   5.641  1.00 15.05  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.400 0.675   4.296  1.00 14.98  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.927 0.107   3.292  1.00 15.86  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.634 1.606   5.822  1.00 19.55  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.238 2.882   5.961  1.00 25.97  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.561 1.366   4.268  1.00 13.68  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.319 1.557   3.003  1.00 14.90  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 22.994 0.277   2.485  1.00 15.07  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.563 0.287   1.392  1.00 16.23  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.369 2.655   3.140  1.00 16.70  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.367 2.325   4.094  1.00 17.05  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.936 -0.811  3.278  1.00 14.35  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.422 -2.112  2.842  1.00 14.42  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.302 -3.198  2.963  1.00 16.39  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.559 -4.367  2.649  1.00 17.81  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.628 -2.517  3.711  1.00 15.56  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.866 -1.648  3.464  1.00 17.20  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.496 -1.992  2.110  1.00 19.09  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.688 -1.175  1.820  1.00 19.67  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.649 0.018   1.239  1.00 19.77  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.487 0.550   0.872  1.00 19.33  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.776 0.688   1.003  1.00 18.25  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 21.090 -2.831  3.473  1.00 16.85  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 20.008 -3.784  3.762  1.00 19.35  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.549 -4.976  4.584  1.00 20.05  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.313 -6.143  4.237  1.00 21.30  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.313 -4.283  2.501  1.00 23.44  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 18.567 -3.244  1.760  1.00 29.11  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.409 -3.956  1.070  1.00 30.76  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.745 -3.051  0.154  1.00 32.57  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.031 -2.947  -1.139 1.00 34.81  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.954 -3.740  -1.693 1.00 34.80  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.412 -2.047  -1.888 1.00 33.63  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.403 -4.682  5.575  1.00 18.65  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 22.065 -5.756  6.332  1.00 18.28  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.286 -5.366  7.780  1.00 17.12  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.400 -4.182  8.084  1.00 16.76  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.487 -5.992  5.762  1.00 21.45  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.619 -7.047  4.678  1.00 30.72  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 25.110 -7.282  4.416  1.00 37.47  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 25.370 -8.404  3.434  1.00 43.38  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 25.264 -7.949  2.021  1.00 46.89  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.436 -6.375  8.645  1.00 16.32  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 22.809 -6.159  10.039 1.00 15.06  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.291 -6.460  10.193 1.00 15.65  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 24.820 -7.399  9.564  1.00 17.91  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 22.020 -7.102  10.963 1.00 14.83  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.536 -6.864  10.960 1.00 15.41  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 19.906 -6.144  11.964 1.00 19.11  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.594 -7.348  10.126 1.00 16.62  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.613 -6.200  11.693 1.00 18.72  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.378 -6.885  10.587 1.00 19.51  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 24.980 -5.650  11.004 1.00 14.02  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.404 -5.861  11.234 1.00 13.74  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.712 -5.924  12.729 1.00 14.10  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.193 -5.125  13.512 1.00 14.09  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.212 -4.655  10.675 1.00 14.04  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.238 -4.564  9.165  1.00 15.05  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 28.023 -5.427  8.404  1.00 17.55  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.537 -3.569  8.501  1.00 15.57  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 28.047 -5.349  7.011  1.00 18.96  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.566 -3.468  7.116  1.00 16.54  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.335 -4.352  6.368  1.00 19.07  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.372 -4.235  4.990  1.00 21.40  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.620 -6.819  13.139 1.00 14.15  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 28.059 -6.828  14.550 1.00 15.10  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 29.078 -5.687  14.799 1.00 16.69  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 29.896 -5.379  13.911 1.00 19.28  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.764 -8.187  14.699 1.00 15.95  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.221 -8.518  13.307 1.00 16.41  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.279 -7.867  12.331 1.00 14.25  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 29.049 -5.070  15.998 1.00 14.88  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 29.938 -3.943  16.316 1.00 15.36  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.444 -4.008  17.741 1.00 16.13  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 29.767 -4.547  18.616 1.00 15.53  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.222 -2.555  16.150 1.00 16.91  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.193 -2.130  14.675 1.00 17.79  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 27.820 -2.571  16.756 1.00 16.57  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.645 -3.434  17.966 1.00 16.38  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 32.199 -3.170  19.302 1.00 17.11  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 32.089 -1.647  19.379 1.00 15.17  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.534 -0.959  18.442 1.00 15.36  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.666 -3.558  19.385 1.00 20.83  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 33.742 -4.972  19.372 1.00 26.52  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.467 -1.128  20.439 1.00 13.74  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.228 0.300   20.515 1.00 14.27  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.706 0.887   21.818 1.00 15.47  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.760 0.192   22.842 1.00 16.65  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.737 0.634   20.222 1.00 14.74  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.684 -0.120  21.024 1.00 14.13  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.194 -1.343  20.589 1.00 14.66  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.178 0.402   22.214 1.00 14.31  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.207 -2.020  21.322 1.00 15.12  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.208 -0.296  22.955 1.00 14.99  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.725 -1.490  22.501 1.00 15.20  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.115 2.185   21.764 1.00 15.28  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.617 2.877   22.947 1.00 16.02  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.482 3.219   23.943 1.00 16.73  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.317 3.204   23.580 1.00 17.48  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.391 4.129   22.542 1.00 17.83  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.528 5.063   21.907 1.00 20.58  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 31.807 3.501   25.221 1.00 17.30  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 30.800 3.884   26.227 1.00 19.11  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.195 5.242   25.865 1.00 19.73  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 30.874 6.060   25.251 1.00 20.42  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.462 3.951   27.622 1.00 22.79  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 31.864 2.566   28.117 1.00 28.86  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.221 2.599   29.586 1.00 33.59  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.554 1.216   30.067 1.00 38.31  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 33.003 1.238   31.481 1.00 42.18  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 28.947 5.520   26.282 1.00 19.56  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.343 6.824   25.955 1.00 19.61  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.202 7.990   26.425 1.00 19.50  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.630 7.991   27.576 1.00 20.13  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 26.994 6.815   26.687 1.00 20.93  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 26.743 5.378   27.056 1.00 21.93  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 28.038 4.640   27.049 1.00 19.63  ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.517 8.925   25.517 1.00 18.63  ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 30.419 10.012  25.879 1.00 20.25  ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 30.164 11.286  25.068 1.00 19.67  ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 29.266 11.302  24.214 1.00 18.44  ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 31.871 9.532   25.767 1.00 24.73  ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 32.198 9.302   24.417 1.00 30.22  ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 30.887 12.396  25.420 1.00 19.79  ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 30.754 13.701  24.749 1.00 20.98  ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 31.756 13.686  23.600 1.00 22.15  ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 32.971 13.661  23.849 1.00 22.70  ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 31.171 14.836  25.709 1.00 22.89  ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 30.120 15.652  26.404 1.00 27.47  ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 30.776 16.718  27.311 1.00 29.08  ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 29.170 16.345  25.422 1.00 28.27  ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 31.264 13.723  22.361 1.00 22.06  ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 32.105 13.638  21.180 1.00 23.19  ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 31.859 14.807  20.243 1.00 23.43  ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 30.697 15.153  19.988 1.00 23.43  ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 31.805 12.279  20.482 1.00 24.55  ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 32.283 11.117  21.368 1.00 26.60  ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 32.436 12.204  19.099 1.00 26.18  ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 31.924 9.776   20.892 1.00 28.64  ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 32.943 15.419  19.711 1.00 23.44  ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 32.780 16.529  18.784 1.00 24.61  ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 32.178 16.052  17.465 1.00 25.37  ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 32.620 15.051  16.909 1.00 25.91  ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 34.136 17.234  18.534 1.00 25.67  ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 34.010 18.456  17.655 1.00 28.27  ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 34.321 18.397  16.306 1.00 29.71  ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 33.488 19.629  18.152 1.00 30.75  ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 34.199 19.521  15.496 1.00 31.27  ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 33.337 20.742  17.332 1.00 32.36  ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 33.717 20.682  16.015 1.00 31.90  ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 31.127 16.756  16.992 1.00 25.46  ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 30.475 16.444  15.725 1.00 25.36  ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 30.510 17.699  14.865 1.00 26.73  ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 30.042 18.770  15.285 1.00 27.24  ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 29.019 15.970  15.935 1.00 25.47  ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 28.342 15.705  14.594 1.00 26.77  ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 28.964 14.726  16.823 1.00 25.20  ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 31.057 17.573  13.668 1.00 27.33  ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 31.210 18.698  12.735 1.00 28.15  ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 29.836 19.278  12.330 1.00 28.15  ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 28.828 18.577  12.422 1.00 27.31  ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 31.975 18.199  11.483 1.00 32.13  ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 32.680 19.286  10.683 1.00 41.57  ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 33.326 18.800  9.395  1.00 51.79  ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 33.687 19.653  8.552  1.00 54.16  ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 33.469 17.566  9.224  1.00 54.81  ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 29.790 20.564  11.904 1.00 28.32  ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 28.541 21.200  11.485 1.00 28.77  ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 27.909 20.446  10.329 1.00 29.74  ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 28.615 19.876  9.491  1.00 30.60  ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 28.787 22.648  11.062 1.00 29.21  ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 26.579 20.408  10.320 1.00 28.82  ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 25.790 19.804  9.260  1.00 28.15  ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 24.653 20.805  8.943  1.00 29.35  ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 24.560 21.863  9.580  1.00 30.23  ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 25.207 18.464  9.741  1.00 27.92  ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 24.266 18.664  10.783 1.00 26.93  ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 23.783 20.474  7.985  1.00 29.68  ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 22.613 21.305  7.705  1.00 30.68  ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 21.651 21.356  8.917  1.00 29.95  ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 20.818 22.257  9.022  1.00 30.50  ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 21.873 20.710  6.486  1.00 35.91  ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 21.477 21.734  5.425  1.00 46.18  ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 22.049 21.624  4.020  1.00 58.86  ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 21.741 20.639  3.306  1.00 61.13  ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 22.791 22.555  3.627  1.00 63.12  ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 21.746 20.356  9.818  1.00 28.66  ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 20.857 20.190  10.954 1.00 27.97  ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 21.341 20.819  12.256 1.00 27.20  ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 20.522 21.211  13.077 1.00 28.03  ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 20.592 18.691  11.163 1.00 27.66  ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 20.065 17.977  9.933  1.00 28.12  ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 20.899 17.193  9.147  1.00 29.53  ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 18.722 18.033  9.595  1.00 28.32  ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 20.398 16.452  8.078  1.00 30.43  ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 18.219 17.335  8.502  1.00 29.12  ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 19.060 16.552  7.741  1.00 31.37  ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 18.552 15.864  6.655  1.00 34.24  ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 22.654 20.914  12.452 1.00 26.24  ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 23.212 21.465  13.687 1.00 25.14  ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 24.486 22.236  13.431 1.00 26.41  ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 25.266 21.879  12.542 1.00 26.15  ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 23.617 20.320  14.657 1.00 23.66  ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 22.496 19.421  15.139 1.00 22.35  ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 21.562 19.873  16.056 1.00 22.38  ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 22.415 18.100  14.731 1.00 22.42  ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 20.558 19.041  16.539 1.00 21.13  ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 21.407 17.255  15.197 1.00 21.30  ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 20.483 17.722  16.111 1.00 20.86  ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 19.472 16.904  16.576 1.00 18.59  ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 24.775 23.230  14.287 1.00 27.73  ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 26.096 23.872  14.205 1.00 29.17  ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 27.155 22.899  14.761 1.00 30.31  ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 26.812 21.899  15.414 1.00 31.38  ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 25.942 25.083  15.133 1.00 30.02  ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 24.947 24.634  16.161 1.00 30.57  ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 23.981 23.733  15.431 1.00 27.64  ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 28.454 23.223  14.615 1.00 29.96  ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 29.539 22.411  15.190 1.00 30.38  ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 29.345 22.364  16.716 1.00 29.19  ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 29.099 23.414  17.314 1.00 29.44  ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 30.892 23.044  14.858 1.00 31.63  ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 29.298 21.151  17.316 1.00 27.62  ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 29.025 21.058  18.758 1.00 25.96  ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 29.526 19.719  19.347 1.00 25.02  ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 29.967 18.849  18.605 1.00 25.92  ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 27.489 21.200  18.978 1.00 24.93  ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 26.719 19.868  18.704 1.00 25.17  ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 25.356 20.031  18.088 1.00 24.86  ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 24.453 18.913  18.411 1.00 24.50  ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 24.456 17.738  17.786 1.00 24.48  ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 23.567 16.803  18.111 1.00 22.33  ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 25.372 17.473  16.859 1.00 23.83  ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 29.439 19.554  20.668 1.00 23.91  ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 29.718 18.262  21.282 1.00 23.86  ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 28.381 17.560  21.444 1.00 22.17  ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 27.455 18.128  22.032 1.00 22.58  ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 30.375 18.405  22.646 1.00 25.11  ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 31.799 18.873  22.524 1.00 27.29  ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 32.838 17.968  22.400 1.00 29.20  ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 32.098 20.227  22.465 1.00 28.77  ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 34.152 18.398  22.256 1.00 31.21  ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 33.400 20.670  22.309 1.00 30.93  ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 34.423 19.754  22.203 1.00 32.82  ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? 35.694 20.248  22.070 1.00 36.71  ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 28.261 16.360  20.892 1.00 19.62  ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 27.048 15.567  21.067 1.00 17.98  ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 27.305 14.670  22.271 1.00 18.27  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 28.371 14.021  22.355 1.00 19.80  ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 26.716 14.736  19.818 1.00 17.90  ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 25.488 13.813  20.010 1.00 17.58  ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 24.854 13.386  18.714 1.00 18.71  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 24.802 14.144  17.743 1.00 20.86  ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 24.294 12.163  18.682 1.00 14.70  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 26.374 14.643  23.219 1.00 17.29  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 26.521 13.835  24.430 1.00 16.89  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 25.856 12.455  24.277 1.00 17.69  ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 25.054 12.261  23.352 1.00 18.11  ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 25.929 14.572  25.623 1.00 18.78  ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 24.540 14.821  25.448 1.00 20.22  ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 26.227 11.492  25.165 1.00 16.52  ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 25.633 10.151  25.196 1.00 15.66  ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 25.814 9.419   23.829 1.00 15.84  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 24.971 8.609   23.446 1.00 16.50  ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 24.138 10.229  25.621 1.00 16.94  ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 23.951 10.821  26.994 1.00 19.63  ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 23.869 10.011  28.121 1.00 22.41  ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 23.826 12.115  27.376 1.00 20.63  ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 23.697 10.841  29.156 1.00 21.64  ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 23.688 12.114  28.758 1.00 21.99  ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 26.927 9.714   23.124 1.00 15.75  ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 27.188 9.110   21.804 1.00 15.38  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 28.207 7.966   21.944 1.00 14.96  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 29.183 8.090   22.697 1.00 14.69  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 27.778 10.209  20.869 1.00 15.90  ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 27.980 9.832   19.376 1.00 17.19  ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 26.647 9.455   18.688 1.00 18.00  ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 28.635 11.034  18.609 1.00 19.17  ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 28.004 6.892   21.184 1.00 14.88  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 28.901 5.725   21.218 1.00 15.14  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 29.396 5.485   19.827 1.00 15.77  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 28.579 5.436   18.910 1.00 17.22  ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 28.093 4.501   21.679 1.00 16.08  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 27.514 4.685   23.081 1.00 17.35  ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 26.420 3.357   23.640 1.00 19.18  ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 25.108 3.498   22.466 1.00 20.65  ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 30.730 5.365   19.624 1.00 15.13  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 31.248 5.143   18.280 1.00 15.48  ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 31.673 3.716   18.069 1.00 15.30  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 32.168 3.057   18.997 1.00 15.57  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 32.498 6.027   17.986 1.00 17.32  ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 32.292 7.502   18.032 1.00 21.75  ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 33.603 8.256   17.657 1.00 23.83  ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 31.170 7.953   17.091 1.00 23.03  ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 31.635 3.319   16.801 1.00 14.86  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 32.110 1.991   16.404 1.00 15.12  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 32.640 2.062   14.991 1.00 14.79  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 32.310 2.989   14.257 1.00 15.40  ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 30.931 1.000   16.446 1.00 16.81  ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 33.449 1.071   14.595 1.00 13.83  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 33.883 0.967   13.212 1.00 14.81  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 32.767 0.189   12.475 1.00 16.55  ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 32.366 -0.907  12.888 1.00 17.90  ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? 35.227 0.198   13.158 1.00 15.90  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? 35.663 -0.069  11.710 1.00 16.95  ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? 36.284 0.977   13.915 1.00 17.56  ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 32.300 0.760   11.381 1.00 17.27  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 31.248 0.162   10.575 1.00 17.59  ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 30.759 1.148   9.525  1.00 17.44  ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 31.087 2.344   9.568  1.00 17.75  ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 30.012 0.649   8.551  1.00 16.26  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 29.483 1.481   7.490  1.00 16.00  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 28.226 2.259   7.880  1.00 16.43  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 27.259 1.704   8.407  1.00 15.86  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 29.194 0.634   6.239  1.00 16.57  ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 28.702 1.461   5.088  1.00 17.60  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 29.547 2.312   4.397  1.00 19.89  ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 27.439 1.609   4.611  1.00 18.82  ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 28.780 2.946   3.518  1.00 21.34  ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 27.506 2.517   3.586  1.00 20.18  ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 28.203 3.541   7.517  1.00 17.23  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 27.017 4.353   7.686  1.00 17.35  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 27.052 5.512   6.688  1.00 19.42  ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 28.136 5.991   6.330  1.00 21.18  ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 26.871 4.869   9.112  1.00 17.73  ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 27.959 5.721   9.433  1.00 22.80  ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 25.879 5.878   6.193  1.00 18.09  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 25.557 7.001   5.302  1.00 19.58  ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 24.460 7.846   5.978  1.00 20.74  ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 23.775 7.361   6.872  1.00 20.37  ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 25.081 6.478   3.940  1.00 21.75  ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 26.217 5.793   3.224  1.00 23.41  ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 25.842 5.157   1.896  1.00 24.22  ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 25.047 5.759   1.133  1.00 24.24  ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 26.350 4.047   1.623  1.00 21.79  ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 24.312 9.136   5.625  1.00 21.54  ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 23.323 9.991   6.331  1.00 21.95  ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 21.918 9.385   6.534  1.00 21.87  ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 21.350 9.466   7.631  1.00 23.22  ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 23.297 11.263  5.474  1.00 22.80  ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 24.706 11.331  4.903  1.00 22.76  ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 25.104 9.893   4.631  1.00 21.35  ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 21.401 8.720   5.512  1.00 19.90  ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 20.104 8.055   5.531  1.00 18.91  ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 20.022 6.842   6.452  1.00 17.60  ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 18.935 6.287   6.673  1.00 18.06  ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 21.156 6.410   7.012  1.00 16.17  ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 21.146 5.291   7.949  1.00 14.86  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 20.685 5.682   9.352  1.00 14.73  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 20.411 4.796   10.177 1.00 14.44  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 22.549 4.670   8.042  1.00 15.62  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 22.850 3.812   6.832  1.00 17.43  ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 21.906 3.169   6.308  1.00 16.85  ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 24.037 3.799   6.384  1.00 16.08  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 20.584 6.976   9.651  1.00 15.18  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 20.146 7.431   10.984 1.00 14.71  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 18.788 6.827   11.334 1.00 14.05  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.924 6.726   10.454 1.00 15.42  ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 20.097 8.956   11.037 1.00 15.53  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 21.727 9.741   11.083 1.00 18.42  ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 18.653 6.354   12.555 1.00 13.74  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.407 5.713   12.981 1.00 14.09  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.488 4.196   12.990 1.00 14.49  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 16.639 3.527   13.586 1.00 14.58  ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 18.533 3.628   12.371 1.00 13.74  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 18.751 2.181   12.446 1.00 12.89  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 19.009 1.760   13.892 1.00 12.80  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 19.755 2.431   14.607 1.00 13.67  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 18.375 0.664   14.333 1.00 12.75  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 18.504 0.243   15.720 1.00 12.95  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 19.777 -0.564  15.983 1.00 12.78  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 20.129 -1.454  15.200 1.00 14.48  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.210 -0.510  16.160 1.00 14.97  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 16.078 0.523   16.388 1.00 15.97  ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.427 -1.385  17.419 1.00 16.73  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 14.678 -0.180  16.630 1.00 18.18  ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 20.407 -0.291  17.140 1.00 12.09  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 21.526 -1.071  17.702 1.00 11.95  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 20.919 -1.888  18.872 1.00 12.93  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 20.253 -1.310  19.748 1.00 12.65  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 22.627 -0.133  18.245 1.00 12.38  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 23.771 -0.816  19.056 1.00 13.87  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 24.575 -1.781  18.187 1.00 13.43  ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 24.716 0.248   19.671 1.00 15.25  ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 21.101 -3.210  18.857 1.00 13.65  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 20.570 -4.096  19.895 1.00 15.03  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 21.680 -4.964  20.463 1.00 16.01  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 22.591 -5.380  19.732 1.00 16.63  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 19.495 -5.049  19.287 1.00 16.80  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 18.126 -4.447  19.033 1.00 21.11  ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.074 -5.475  18.492 1.00 24.42  ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 15.662 -5.019  18.680 1.00 24.65  ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 14.897 -5.363  19.710 1.00 24.81  ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 15.368 -6.163  20.657 1.00 21.72  ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 13.643 -4.916  19.800 1.00 27.16  ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 21.530 -5.346  21.729 1.00 15.53  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 22.394 -6.363  22.328 1.00 15.70  ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 21.438 -7.513  22.769 1.00 16.78  ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 20.223 -7.466  22.494 1.00 17.65  ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 23.144 -5.785  23.524 1.00 17.43  ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 22.032 -5.285  24.869 1.00 15.99  ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 21.946 -8.513  23.493 1.00 16.54  ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 21.085 -9.616  23.969 1.00 17.23  ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 19.975 -9.168  24.942 1.00 17.63  ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 19.025 -9.929  25.190 1.00 18.85  ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 21.941 -10.722 24.625 1.00 19.95  ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 22.559 -10.250 25.945 1.00 26.02  ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 23.609 -11.217 26.437 1.00 34.70  ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 24.827 -10.997 26.292 1.00 38.50  ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 23.159 -12.296 27.044 1.00 33.48  ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 20.065 -7.952  25.487 1.00 16.93  ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 19.108 -7.452  26.497 1.00 17.02  ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 18.010 -6.568  25.942 1.00 16.89  ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.031 -6.312  26.657 1.00 17.89  ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 19.815 -6.700  27.642 1.00 17.88  ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 20.928 -7.482  28.291 1.00 21.28  ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 22.264 -7.146  28.075 1.00 22.44  ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 20.876 -8.574  29.108 1.00 22.52  ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 22.984 -8.031  28.755 1.00 23.31  ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 22.202 -8.920  29.391 1.00 23.39  ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 18.176 -6.105  24.698 1.00 15.88  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.173 -5.258  24.079 1.00 15.16  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 17.800 -4.134  23.268 1.00 14.19  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 18.962 -4.220  22.843 1.00 15.39  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.018 -3.099  23.029 1.00 13.98  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.466 -1.945  22.255 1.00 13.65  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 18.441 -1.097  23.074 1.00 14.12  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 18.120 -0.699  24.204 1.00 14.71  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 16.249 -1.076  21.844 1.00 14.55  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 16.724 0.230   21.182 1.00 15.32  ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 15.330 -1.875  20.914 1.00 15.78  ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 19.591 -0.781  22.473 1.00 14.20  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 20.647 0.017   23.082 1.00 14.73  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 20.570 1.491   22.624 1.00 15.05  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 20.785 2.418   23.411 1.00 14.24  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 22.032 -0.585  22.717 1.00 15.76  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 23.195 0.347   23.130 1.00 17.02  ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 22.218 -1.984  23.322 1.00 15.98  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 20.342 1.687   21.330 1.00 13.89  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 20.295 3.048   20.781 1.00 14.72  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 19.983 3.091   19.301 1.00 14.86  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 19.624 2.073   18.718 1.00 14.88  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 20.162 4.270   18.680 1.00 14.23  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 19.889 4.395   17.238 1.00 13.92  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 21.046 5.103   16.537 1.00 13.39  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 21.681 5.985   17.112 1.00 13.46  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 18.573 5.184   16.978 1.00 13.94  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 18.524 6.495   17.782 1.00 14.93  ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.339 4.318   17.222 1.00 15.50  ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.311 7.402   17.301 1.00 16.97  ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 21.280 4.769   15.255 1.00 12.17  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 22.326 5.459   14.460 1.00 11.72  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 22.034 6.975   14.448 1.00 12.76  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 20.888 7.380   14.236 1.00 12.73  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 22.347 4.927   13.010 1.00 12.45  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 23.348 5.735   12.172 1.00 13.62  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 22.746 3.445   12.989 1.00 12.59  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 23.058 7.789   14.720 1.00 13.23  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 22.915 9.245   14.761 1.00 14.33  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 24.034 9.950   13.978 1.00 15.73  ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 23.812 11.039  13.483 1.00 16.50  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 22.924 9.709   16.218 1.00 15.40  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 22.832 11.119  16.373 1.00 16.33  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 25.244 9.345   13.891 1.00 15.02  ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 26.351 10.003  13.142 1.00 16.10  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 27.085 8.927   12.294 1.00 16.86  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 26.856 7.736   12.460 1.00 15.66  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 27.367 10.718  14.131 1.00 19.15  ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 28.186 9.742   14.788 1.00 20.73  ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 26.715 11.633  15.143 1.00 20.16  ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 28.001 9.369   11.448 1.00 17.91  ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 28.830 8.441   10.708 1.00 20.95  ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 29.859 9.158   9.884  1.00 24.85  ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 30.133 10.338  10.094 1.00 25.06  ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 30.369 8.408   8.934  1.00 27.94  ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 31.361 8.842   7.970  1.00 30.08  ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 32.690 8.186   8.243  1.00 31.00  ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 32.927 7.713   9.349  1.00 32.88  ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 33.585 8.208   7.264  1.00 29.99  ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 34.945 7.710   7.403  1.00 29.60  ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 35.120 6.247   7.893  1.00 25.49  ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? 36.155 5.953   8.491  1.00 24.73  ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? 35.704 8.665   8.365  1.00 33.77  ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? 35.676 10.133  7.966  1.00 39.90  ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? 35.899 10.479  6.796  1.00 42.55  ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? 35.466 11.031  8.935  1.00 39.84  ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 34.172 5.329   7.646  1.00 21.91  ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 34.263 3.969   8.186  1.00 20.27  ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 33.886 3.903   9.670  1.00 19.45  ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 34.201 2.923   10.370 1.00 19.99  ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 33.173 4.932   10.157 1.00 17.59  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 32.696 5.003   11.525 1.00 17.72  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 31.158 5.073   11.522 1.00 16.98  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 30.542 5.514   10.540 1.00 18.17  ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 33.243 6.252   12.239 1.00 18.40  ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 34.765 6.210   12.547 1.00 21.69  ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? 35.304 7.599   12.915 1.00 23.62  ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? 35.072 5.188   13.672 1.00 21.61  ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 30.557 4.646   12.640 1.00 14.63  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 29.131 4.781   12.860 1.00 13.61  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 28.928 5.177   14.333 1.00 13.87  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 29.616 4.627   15.186 1.00 14.59  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 28.307 3.542   12.428 1.00 13.66  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 28.832 2.241   13.046 1.00 15.43  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 26.828 3.743   12.713 1.00 13.49  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 28.114 6.216   14.599 1.00 13.16  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 27.858 6.714   15.955 1.00 13.67  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 26.412 6.476   16.343 1.00 13.23  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 25.513 6.647   15.502 1.00 13.35  ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 26.181 5.984   17.559 1.00 13.09  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 24.831 5.645   18.042 1.00 13.25  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 24.467 6.524   19.248 1.00 13.68  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 25.246 6.663   20.181 1.00 13.54  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 24.743 4.175   18.510 1.00 12.59  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 25.257 3.179   17.483 1.00 12.51  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 24.420 2.693   16.488 1.00 12.72  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 26.571 2.706   17.538 1.00 13.08  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 24.882 1.759   15.548 1.00 13.39  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 27.040 1.771   16.582 1.00 13.34  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 26.195 1.323   15.582 1.00 13.21  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 23.252 7.046   19.238 1.00 12.90  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 22.734 7.798   20.365 1.00 13.14  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 22.219 6.748   21.376 1.00 13.14  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 21.297 5.987   21.060 1.00 13.89  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 21.576 8.672   19.913 1.00 13.29  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 22.793 6.724   22.577 1.00 13.21  ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 22.361 5.770   23.608 1.00 14.51  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 20.995 6.133   24.170 1.00 14.41  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 20.682 7.324   24.323 1.00 14.81  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 23.391 5.790   24.746 1.00 16.57  ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 23.148 4.757   25.833 1.00 21.77  ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 22.882 3.609   25.496 1.00 20.82  ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 23.168 5.136   27.035 1.00 26.98  ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 20.166 5.101   24.509 1.00 13.12  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 18.868 5.356   25.160 1.00 13.79  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 18.760 4.565   26.486 1.00 15.22  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.721 4.630   27.117 1.00 16.34  ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.627 5.052   24.261 1.00 15.23  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.629 5.924   22.992 1.00 15.00  ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.563 3.565   23.883 1.00 15.68  ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 19.807 3.806   26.888 1.00 15.24  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 19.707 2.930   28.074 1.00 14.31  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 19.560 3.645   29.388 1.00 16.03  ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 19.041 3.051   30.344 1.00 16.67  ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 20.907 1.948   28.152 1.00 14.81  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 20.976 1.015   26.954 1.00 15.83  ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 22.248 0.201   27.059 1.00 16.39  ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 23.399 1.026   26.696 1.00 15.42  ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 24.642 0.565   26.590 1.00 17.62  ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 24.916 -0.700  26.900 1.00 16.36  ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 25.624 1.372   26.189 1.00 17.74  ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 19.988 4.916   29.449 1.00 16.69  ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 19.840 5.680   30.699 1.00 17.26  ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 18.440 6.290   30.882 1.00 17.57  ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 18.149 6.788   31.969 1.00 19.06  ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 20.872 6.820   30.747 1.00 18.43  ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 20.690 7.850   29.653 1.00 23.53  ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 20.541 7.446   28.478 1.00 23.60  ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 20.691 9.068   29.968 1.00 26.80  ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.591 6.288   29.836 1.00 16.29  ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 16.248 6.884   29.875 1.00 15.52  ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 15.268 5.913   30.528 1.00 16.13  ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 14.470 5.241   29.848 1.00 16.00  ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 15.819 7.250   28.435 1.00 15.74  ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 16.796 8.222   27.696 1.00 17.32  ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 16.333 8.488   26.236 1.00 16.96  ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 16.981 9.521   28.476 1.00 18.91  ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 15.353 5.810   31.865 1.00 16.52  ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 14.561 4.796   32.571 1.00 18.20  ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 13.069 4.991   32.465 1.00 18.75  ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 12.305 4.000   32.525 1.00 20.05  ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 14.986 4.684   34.036 1.00 18.56  ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 16.495 4.593   34.295 1.00 20.28  ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 16.727 4.246   35.764 1.00 20.94  ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.215 3.555   33.380 1.00 20.75  ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 12.636 6.266   32.303 1.00 18.15  ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 11.225 6.591   32.205 1.00 18.80  ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 10.540 6.026   30.949 1.00 20.18  ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 9.308  5.999   30.889 1.00 21.76  ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 11.035 8.109   32.306 1.00 18.60  ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 11.871 8.904   31.329 1.00 18.31  ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 13.111 9.436   31.540 1.00 18.52  ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 11.502 9.257   29.992 1.00 18.53  ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 13.524 10.129  30.423 1.00 19.13  ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 12.557 10.026  29.453 1.00 19.02  ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 10.359 9.039   29.216 1.00 18.90  ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 12.507 10.561  28.164 1.00 19.15  ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 10.311 9.571   27.935 1.00 19.69  ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 11.365 10.345  27.439 1.00 19.44  ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 11.317 5.564   29.947 1.00 20.43  ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 10.724 4.985   28.738 1.00 21.87  ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 9.907  3.725   29.073 1.00 25.82  ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 8.985  3.411   28.332 1.00 25.50  ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 11.807 4.609   27.721 1.00 20.58  ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 12.423 5.781   26.946 1.00 19.57  ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 13.564 5.282   26.043 1.00 19.93  ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 11.368 6.497   26.059 1.00 19.76  ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 10.290 2.996   30.156 1.00 29.39  ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 9.702  1.737   30.635 1.00 34.19  ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 8.464  1.896   31.484 1.00 38.23  ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 7.956  0.880   31.948 1.00 39.00  ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 10.704 1.000   31.546 1.00 37.26  ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 11.922 0.436   30.893 1.00 44.81  ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 11.905 0.269   29.662 1.00 46.27  ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 12.906 0.153   31.616 1.00 48.43  ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 8.035  3.124   31.787 1.00 40.69  ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 6.853  3.339   32.622 1.00 44.03  ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 5.926  4.355   31.963 1.00 46.30  ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 4.863  4.665   32.509 1.00 48.00  ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 7.267  3.824   34.023 1.00 46.73  ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 8.005  5.149   33.983 1.00 52.76  ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 9.007  5.367   35.097 1.00 60.15  ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 9.180  6.535   35.519 1.00 60.99  ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 9.635  4.375   35.534 1.00 62.67  ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 19.542 -24.802 24.055 1.00 26.32  ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 20.671 -24.642 23.120 1.00 26.49  ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 20.707 -25.795 22.092 1.00 25.06  ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 20.082 -26.846 22.307 1.00 24.45  ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 21.988 -24.578 23.887 1.00 28.89  ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 22.144 -25.783 24.621 1.00 33.02  ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 21.420 -25.581 20.987 1.00 23.48  ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 21.564 -26.585 19.940 1.00 21.91  ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 21.844 -26.015 18.560 1.00 20.89  ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 21.493 -24.869 18.266 1.00 21.98  ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 22.483 -26.803 17.699 1.00 18.88  ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 22.835 -26.348 16.338 1.00 17.99  ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 22.781 -27.512 15.358 1.00 18.43  ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 22.852 -28.679 15.768 1.00 19.62  ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 24.258 -25.769 16.328 1.00 18.12  ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 22.676 -27.194 14.053 1.00 17.31  ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 22.769 -28.166 12.972 1.00 16.46  ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 24.129 -27.952 12.308 1.00 17.38  ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 24.496 -26.828 12.013 1.00 17.95  ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 21.654 -27.921 11.938 1.00 16.23  ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 20.282 -27.973 12.606 1.00 17.34  ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 21.750 -28.913 10.763 1.00 16.37  ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 19.189 -27.307 11.690 1.00 18.80  ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 24.880 -29.025 12.053 1.00 18.29  ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 26.183 -28.951 11.426 1.00 18.92  ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 26.121 -29.687 10.096 1.00 21.17  ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 26.014 -30.910 10.086 1.00 22.01  ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 27.235 -29.606 12.358 1.00 19.41  ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 27.443 -28.798 13.628 1.00 19.41  ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 28.302 -27.707 13.651 1.00 20.17  ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 26.731 -29.084 14.785 1.00 20.49  ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 28.466 -26.940 14.801 1.00 22.11  ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 26.882 -28.317 15.938 1.00 21.47  ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 27.761 -27.254 15.946 1.00 22.97  ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 27.889 -26.482 17.082 1.00 24.85  ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 26.144 -28.964 8.980  1.00 21.49  ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 26.025 -29.581 7.658  1.00 21.85  ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 27.105 -29.003 6.755  1.00 22.78  ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 27.219 -27.792 6.638  1.00 21.44  ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 24.588 -29.392 7.071  1.00 22.85  ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 24.125 -27.947 7.177  1.00 22.96  ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 24.494 -29.899 5.637  1.00 23.84  ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 27.978 -29.852 6.196  1.00 24.15  ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 29.061 -29.366 5.336  1.00 25.45  ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 29.960 -28.422 6.108  1.00 26.34  ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 30.274 -28.704 7.266  1.00 27.64  ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 30.244 -27.233 5.558  1.00 25.37  ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 31.032 -26.247 6.303  1.00 25.35  ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 30.152 -25.145 6.892  1.00 23.05  ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 30.587 -23.990 6.988  1.00 22.98  ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 32.137 -25.665 5.457  1.00 28.60  ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 33.177 -26.705 5.161  1.00 36.65  ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 33.917 -27.151 6.056  1.00 39.57  ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 33.215 -27.157 3.919  1.00 38.09  ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 28.939 -25.514 7.326  1.00 21.45  ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 27.996 -24.568 7.916  1.00 20.56  ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 27.514 -25.029 9.291  1.00 19.20  ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 27.352 -26.239 9.546  1.00 19.08  ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 26.747 -24.450 7.026  1.00 21.11  ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 27.025 -23.910 5.641  1.00 23.00  ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 27.719 -22.720 5.467  1.00 24.84  ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 26.598 -24.590 4.509  1.00 24.81  ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 27.955 -22.202 4.201  1.00 26.60  ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 26.843 -24.093 3.233  1.00 26.59  ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 27.515 -22.892 3.085  1.00 28.26  ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 27.753 -22.380 1.824  1.00 31.20  ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 27.216 -24.026 10.162 1.00 16.58  ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 26.632 -24.234 11.488 1.00 16.31  ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 25.346 -23.403 11.517 1.00 15.96  ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 25.411 -22.208 11.249 1.00 16.47  ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 27.596 -23.790 12.600 1.00 17.39  ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 26.965 -23.601 13.983 1.00 18.31  ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 28.002 -23.308 15.084 1.00 19.50  ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 27.596 -22.260 16.038 1.00 21.20  ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 27.133 -22.494 17.266 1.00 23.77  ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 26.951 -23.742 17.688 1.00 23.65  ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 26.793 -21.479 18.063 1.00 22.89  ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 24.182 -24.041 11.726 1.00 15.56  ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 22.879 -23.348 11.759 1.00 15.17  ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 22.443 -23.229 13.217 1.00 15.13  ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 22.326 -24.256 13.896 1.00 16.00  ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 21.783 -24.127 10.970 1.00 16.17  ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 20.506 -23.280 10.851 1.00 16.67  ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 22.297 -24.548 9.586  1.00 15.43  ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 22.173 -22.012 13.698 1.00 14.01  ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 21.750 -21.825 15.082 1.00 14.96  ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 20.547 -20.876 15.134 1.00 14.25  ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 20.294 -20.117 14.180 1.00 14.44  ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 22.904 -21.205 15.931 1.00 17.31  ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 24.021 -22.199 16.145 1.00 20.72  ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 23.440 -19.916 15.286 1.00 16.19  ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 19.857 -20.822 16.292 1.00 13.37  ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 18.830 -19.772 16.497 1.00 13.36  ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 19.584 -18.404 16.450 1.00 13.88  ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 20.621 -18.242 17.133 1.00 15.03  ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 18.212 -19.885 17.891 1.00 14.41  ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.339 -21.098 18.047 1.00 16.32  ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 17.790 -22.139 18.523 1.00 16.18  ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 16.080 -20.972 17.623 1.00 15.19  ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 19.097 -17.465 15.646 1.00 14.26  ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 19.783 -16.151 15.534 1.00 13.97  ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 19.950 -15.471 16.918 1.00 14.21  ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 21.023 -14.898 17.189 1.00 14.97  ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 19.030 -15.239 14.562 1.00 14.49  ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 19.794 -13.957 14.156 1.00 16.09  ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 18.827 -13.054 13.410 1.00 17.01  ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 19.423 -11.813 12.873 1.00 15.42  ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 19.529 -10.678 13.548 1.00 18.36  ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 19.222 -10.634 14.840 1.00 18.11  ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 19.992 -9.584  12.949 1.00 18.42  ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 18.943 -15.599 17.806 1.00 14.57  ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 19.028 -14.974 19.132 1.00 15.04  ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 20.054 -15.626 20.068 1.00 16.22  ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 20.434 -15.005 21.076 1.00 18.21  ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.638 -14.872 19.804 1.00 14.70  ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 17.069 -16.151 20.351 1.00 15.81  ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 16.391 -17.055 19.536 1.00 15.91  ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 17.073 -16.621 21.625 1.00 17.09  ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 15.999 -18.047 20.338 1.00 17.42  ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 16.397 -17.837 21.602 1.00 18.35  ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 20.560 -16.833 19.719 1.00 15.35  ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 21.575 -17.508 20.534 1.00 16.09  ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 22.956 -17.504 19.836 1.00 17.19  ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 23.894 -18.127 20.348 1.00 18.53  ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 21.138 -18.978 20.825 1.00 16.06  ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 19.812 -19.102 21.637 1.00 17.29  ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 19.475 -20.591 21.896 1.00 16.83  ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 19.887 -18.306 22.997 1.00 18.91  ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 23.097 -16.817 18.665 1.00 15.62  ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 24.400 -16.799 17.968 1.00 16.17  ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 25.459 -16.139 18.835 1.00 16.94  ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 25.164 -15.170 19.529 1.00 16.94  ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 24.280 -16.023 16.663 1.00 15.76  ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 26.683 -16.659 18.789 1.00 16.98  ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 27.813 -16.147 19.580 1.00 17.79  ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 28.593 -15.052 18.823 1.00 17.99  ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 28.363 -14.845 17.631 1.00 17.28  ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 28.748 -17.331 19.901 1.00 19.23  ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 29.361 -17.779 18.691 1.00 20.69  ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 28.031 -18.463 20.606 1.00 19.38  ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 29.612 -14.416 19.479 1.00 18.31  ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 30.470 -13.449 18.778 1.00 20.51  ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 31.178 -14.151 17.586 1.00 20.33  ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 31.306 -13.566 16.503 1.00 21.16  ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 31.538 -12.911 19.754 1.00 23.80  ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 30.983 -12.081 20.872 1.00 30.35  ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 30.216 -10.945 20.628 1.00 33.94  ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 31.164 -12.202 22.209 1.00 33.36  ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 29.939 -10.431 21.818 1.00 34.73  ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 30.479 -11.153 22.800 1.00 34.85  ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 31.578 -15.426 17.767 1.00 19.35  ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 32.246 -16.170 16.695 1.00 19.74  ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 31.305 -16.444 15.521 1.00 19.13  ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 31.735 -16.387 14.367 1.00 18.96  ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 32.834 -17.476 17.226 1.00 22.45  ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 33.680 -18.221 16.224 1.00 28.43  ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? 34.739 -17.750 15.814 1.00 31.43  ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 33.233 -19.411 15.819 1.00 30.08  ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 30.011 -16.750 15.798 1.00 18.45  ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 29.048 -16.950 14.712 1.00 18.44  ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 28.924 -15.662 13.870 1.00 19.02  ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 28.948 -15.724 12.643 1.00 19.88  ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 27.664 -17.290 15.303 1.00 17.11  ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 27.548 -18.714 15.837 1.00 18.26  ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 28.119 -19.625 15.212 1.00 18.39  ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 26.874 -18.904 16.888 1.00 18.40  ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 28.823 -14.500 14.527 1.00 19.35  ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 28.690 -13.235 13.812 1.00 19.39  ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 29.989 -12.869 13.055 1.00 19.48  ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 29.920 -12.273 11.974 1.00 19.95  ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 28.269 -12.109 14.783 1.00 19.24  ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 26.790 -12.070 15.034 1.00 18.07  ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 26.120 -12.545 16.122 1.00 18.73  ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 25.804 -11.509 14.160 1.00 17.46  ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 24.766 -12.337 15.968 1.00 18.84  ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 24.547 -11.702 14.768 1.00 18.12  ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 25.858 -10.914 12.894 1.00 17.77  ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 23.365 -11.227 14.198 1.00 18.42  ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 24.679 -10.448 12.331 1.00 18.79  ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 23.448 -10.673 12.955 1.00 18.39  ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 31.145 -13.248 13.593 1.00 19.18  ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 32.423 -12.952 12.929 1.00 20.38  ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 32.668 -13.859 11.695 1.00 22.05  ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 33.566 -13.572 10.886 1.00 23.06  ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 33.575 -13.123 13.917 1.00 19.41  ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 31.955 -15.001 11.613 1.00 21.05  ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 32.072 -15.942 10.498 1.00 20.97  ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 30.689 -16.091 9.817  1.00 20.95  ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 30.313 -17.171 9.400  1.00 20.70  ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 32.569 -17.295 11.026 1.00 22.44  ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 33.991 -17.200 11.526 1.00 27.31  ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? 34.947 -17.169 10.739 1.00 28.79  ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 34.174 -17.102 12.849 1.00 27.54  ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 29.945 -14.993 9.727  1.00 20.73  ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 28.601 -14.972 9.192  1.00 20.31  ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 28.507 -15.346 7.717  1.00 20.99  ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 29.270 -14.826 6.896  1.00 22.22  ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 28.020 -13.572 9.404  1.00 19.99  ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 26.598 -13.318 8.897  1.00 20.34  ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 25.566 -14.204 9.656  1.00 20.45  ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 26.239 -11.852 9.115  1.00 21.23  ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 27.551 -16.233 7.380  1.00 19.22  ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 27.238 -16.598 6.001  1.00 19.46  ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 25.892 -15.946 5.621  1.00 20.42  ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 25.755 -15.318 4.554  1.00 21.20  ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 27.181 -18.136 5.833  1.00 20.25  ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 26.634 -18.518 4.454  1.00 21.09  ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 28.564 -18.753 6.070  1.00 20.67  ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 24.888 -16.098 6.506  1.00 19.25  ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 23.546 -15.590 6.259  1.00 19.17  ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 22.796 -15.514 7.569  1.00 17.93  ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 22.973 -16.371 8.430  1.00 18.28  ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 22.818 -16.579 5.311  1.00 19.34  ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 21.341 -16.357 5.106  1.00 19.75  ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 20.739 -15.499 4.229  1.00 21.29  ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 20.278 -17.081 5.757  1.00 19.17  ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 19.355 -15.624 4.324  1.00 20.87  ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 19.055 -16.567 5.276  1.00 20.07  ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 20.250 -18.072 6.746  1.00 19.67  ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 17.816 -17.084 5.686  1.00 20.03  ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 19.023 -18.580 7.152  1.00 19.69  ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 17.825 -18.075 6.641  1.00 19.63  ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 21.918 -14.537 7.708  1.00 17.96  ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 21.035 -14.460 8.876  1.00 17.50  ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 19.693 -13.842 8.454  1.00 17.19  ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 19.646 -13.024 7.514  1.00 17.09  ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 21.661 -13.714 10.078 1.00 17.79  ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 22.242 -12.338 9.742  1.00 18.93  ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 21.242 -11.201 9.585  1.00 22.12  ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 21.530 -10.260 8.805  1.00 26.34  ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 20.177 -11.233 10.240 1.00 19.13  ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 18.617 -14.222 9.149  1.00 16.16  ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.312 -13.648 8.869  1.00 16.34  ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 16.561 -13.513 10.203 1.00 16.02  ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 16.128 -14.501 10.792 1.00 15.66  ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 16.555 -14.537 7.869  1.00 17.45  ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 15.254 -13.972 7.369  1.00 23.03  ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 14.627 -13.188 8.103  1.00 24.18  ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 14.832 -14.357 6.262  1.00 24.44  ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 16.417 -12.259 10.676 1.00 16.00  ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 15.736 -11.965 11.924 0.50 16.30  ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 15.739 -12.005 11.940 0.50 16.35  ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 14.273 -12.448 11.892 1.00 16.80  ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 13.768 -12.924 12.901 1.00 18.12  ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 15.817 -10.467 12.214 0.50 18.30  ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 15.847 -10.533 12.334 0.50 18.51  ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 15.018 -10.095 13.320 0.50 21.60  ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 15.100 -9.732  11.436 0.50 22.09  ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 13.605 -12.348 10.716 1.00 16.24  ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 12.205 -12.784 10.631 1.00 16.53  ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 12.045 -14.289 10.806 1.00 16.45  ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 10.949 -14.716 11.156 1.00 17.93  ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 11.534 -12.339 9.336  1.00 19.61  ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 11.950 -13.124 8.227  1.00 23.32  ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 13.106 -15.067 10.599 1.00 14.75  ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 13.049 -16.530 10.757 1.00 14.07  ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 13.716 -17.011 12.075 1.00 14.83  ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 13.675 -18.219 12.375 1.00 14.84  ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 13.766 -17.201 9.559  1.00 13.70  ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 13.054 -16.921 8.223  1.00 14.57  ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 13.754 -17.601 7.047  1.00 14.87  ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 13.761 -19.064 7.158  1.00 14.56  ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 13.828 -19.891 6.112  1.00 16.56  ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 13.873 -19.406 4.869  1.00 17.51  ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 13.768 -21.208 6.295  1.00 17.54  ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 14.414 -16.108 12.791 1.00 14.85  ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 15.209 -16.459 13.978 1.00 14.01  ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 16.302 -17.469 13.584 1.00 13.81  ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 16.633 -18.350 14.381 1.00 14.13  ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 14.360 -17.024 15.161 1.00 14.47  ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 15.179 -17.302 16.431 1.00 14.83  ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 16.099 -16.496 16.746 1.00 15.29  ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 14.922 -18.337 17.112 1.00 14.48  ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 16.920 -17.311 12.388 1.00 13.25  ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 18.013 -18.201 11.967 1.00 13.52  ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 19.297 -17.436 11.649 1.00 13.60  ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 19.252 -16.352 11.083 1.00 14.39  ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 17.642 -18.970 10.681 1.00 13.99  ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 16.587 -20.081 10.844 1.00 14.89  ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 16.373 -20.802 9.480  1.00 15.43  ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 17.041 -21.120 11.872 1.00 15.82  ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 20.439 -18.079 11.899 1.00 13.04  ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 21.742 -17.550 11.535 1.00 13.85  ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 22.609 -18.759 11.127 1.00 14.69  ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 22.535 -19.829 11.745 1.00 15.14  ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 22.366 -16.751 12.692 1.00 14.03  ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 23.743 -16.107 12.388 1.00 14.99  ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 23.884 -14.771 13.120 1.00 15.93  ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 24.917 -17.049 12.793 1.00 15.94  ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 23.418 -18.590 10.088 1.00 13.77  ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 24.317 -19.632 9.592  1.00 14.30  ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 25.715 -19.020 9.567  1.00 15.39  ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 25.917 -17.918 9.024  1.00 15.95  ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 23.912 -20.117 8.168  1.00 14.82  ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 24.934 -21.137 7.634  1.00 16.33  ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 22.497 -20.720 8.175  1.00 14.09  ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 26.671 -19.729 10.164 1.00 15.84  ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 28.063 -19.302 10.172 1.00 16.48  ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 28.930 -20.411 9.554  1.00 17.56  ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 28.484 -21.566 9.417  1.00 18.47  ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 28.522 -19.009 11.592 1.00 17.67  ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 28.422 -20.153 12.435 1.00 21.40  ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 30.168 -20.042 9.154  1.00 18.07  ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 31.040 -21.027 8.531  1.00 20.61  ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 31.904 -21.774 9.567  1.00 23.14  ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 32.252 -21.218 10.612 1.00 23.72  ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 31.903 -20.354 7.474  1.00 22.58  ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 32.639 -19.298 8.059  1.00 25.32  ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 32.229 -23.048 9.275  1.00 24.68  ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 33.052 -23.864 10.168 1.00 27.83  ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 34.282 -24.376 9.397  1.00 31.13  ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 34.284 -24.410 8.157  1.00 31.72  ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 32.242 -25.083 10.666 1.00 29.13  ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 31.992 -25.947 9.558  1.00 30.81  ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 30.920 -24.703 11.297 1.00 28.62  ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? 35.307 -24.805 10.127 1.00 32.83  ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? 36.495 -25.389 9.507  1.00 35.37  ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? 36.312 -26.907 9.343  1.00 36.62  ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? 36.795 -27.479 8.363  1.00 37.73  ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? 37.746 -25.008 10.311 1.00 38.00  ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? 37.513 -25.316 11.691 1.00 40.60  ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? 38.070 -23.532 10.192 1.00 38.45  ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? 35.603 -27.558 10.290 1.00 36.04  ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? 35.354 -28.998 10.261 1.00 36.51  ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 34.093 -29.343 9.471  1.00 37.03  ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 33.156 -28.546 9.409  1.00 37.04  ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? 35.228 -29.527 11.680 1.00 36.86  ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 34.059 -30.547 8.893  1.00 36.92  ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 32.929 -31.014 8.110  1.00 37.26  ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 31.830 -31.490 9.040  1.00 35.85  ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 32.094 -32.222 9.990  1.00 36.66  ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 33.359 -32.165 7.188  1.00 40.84  ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 32.349 -32.461 6.078  1.00 46.66  ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 32.482 -31.522 4.898  1.00 53.82  ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 33.480 -30.803 4.738  1.00 55.54  ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 31.483 -31.534 4.023  1.00 55.57  ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 30.608 -31.044 8.758  1.00 33.22  ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 29.410 -31.424 9.494  1.00 31.30  ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 28.738 -32.583 8.788  1.00 29.80  ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 28.746 -32.653 7.553  1.00 29.92  ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 28.151 -33.483 9.555  1.00 28.28  ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 27.565 -34.687 8.984  1.00 27.87  ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 26.059 -34.789 9.111  1.00 26.04  ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 25.532 -35.893 8.905  1.00 26.52  ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 28.246 -35.928 9.545  1.00 30.66  ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 30.021 -36.008 9.191  1.00 37.39  ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 25.360 -33.693 9.466  1.00 22.79  ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 23.900 -33.771 9.541  1.00 22.20  ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 23.342 -33.761 8.113  1.00 22.32  ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 23.909 -33.095 7.238  1.00 22.50  ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 23.317 -32.571 10.333 1.00 23.70  ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 23.605 -32.617 11.826 1.00 30.07  ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 23.994 -33.695 12.326 1.00 32.62  ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 23.465 -31.570 12.494 1.00 29.33  ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 22.285 -34.522 7.863  1.00 21.13  ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 21.596 -34.527 6.573  1.00 22.17  ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 20.333 -33.667 6.718  1.00 20.45  ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 19.572 -33.908 7.637  1.00 20.89  ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 21.177 -35.962 6.226  1.00 26.81  ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 22.374 -36.707 5.939  1.00 29.85  ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 20.219 -36.029 5.032  1.00 28.06  ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 20.099 -32.712 5.810  1.00 19.08  ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 18.887 -31.899 5.854  1.00 18.57  ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 17.796 -32.589 5.053  1.00 18.39  ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 18.042 -33.067 3.930  1.00 18.77  ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 19.130 -30.491 5.242  1.00 19.32  ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 20.355 -29.780 5.879  1.00 21.47  ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 17.857 -29.612 5.371  1.00 19.29  ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 20.227 -29.560 7.409  1.00 24.06  ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 16.588 -32.662 5.627  1.00 16.83  ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 15.449 -33.240 4.935  1.00 16.33  ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 15.031 -32.322 3.773  1.00 15.62  ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 15.026 -31.107 3.942  1.00 16.19  ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 14.281 -33.378 5.918  1.00 15.90  ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 14.602 -32.897 2.629  1.00 14.62  ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 14.112 -32.127 1.471  1.00 14.59  ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 12.762 -32.806 1.179  1.00 15.41  ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 12.692 -33.797 0.438  1.00 16.32  ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 15.101 -32.241 0.300  1.00 15.35  ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 16.498 -31.721 0.626  1.00 15.97  ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 16.533 -30.220 1.001  1.00 16.58  ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 17.912 -29.769 1.230  1.00 18.59  ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 18.245 -28.673 1.904  1.00 20.68  ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.307 -27.869 2.378  1.00 19.44  ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 19.523 -28.359 2.087  1.00 21.81  ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 11.709 -32.316 1.838  1.00 14.93  ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 10.410 -32.982 1.845  1.00 15.02  ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 9.288  -32.039 2.338  1.00 16.37  ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 9.568  -30.926 2.751  1.00 16.43  ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 10.524 -34.178 2.780  1.00 15.07  ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 10.701 -33.695 4.521  1.00 15.46  ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 8.034  -32.545 2.366  1.00 16.27  ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 6.907  -31.821 2.947  1.00 17.46  ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 6.298  -32.612 4.121  1.00 17.66  ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 5.100  -32.502 4.372  1.00 18.14  ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 5.831  -31.473 1.907  1.00 19.27  ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 5.136  -32.655 1.284  1.00 25.84  ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 5.533  -33.811 1.576  1.00 27.04  ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 4.192  -32.433 0.492  1.00 30.20  ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 7.109  -33.395 4.859  1.00 15.75  ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 6.643  -34.163 6.039  1.00 14.53  ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 5.981  -33.244 7.026  1.00 14.00  ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 6.393  -32.073 7.181  1.00 13.97  ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 7.804  -34.877 6.727  1.00 15.11  ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 8.344  -36.378 5.885  1.00 17.31  ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 4.951  -33.771 7.678  1.00 13.18  ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 4.265  -33.129 8.784  1.00 14.02  ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 4.256  -33.986 10.044 1.00 15.06  ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 3.467  -33.730 10.963 1.00 15.30  ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 2.847  -32.675 8.428  1.00 14.59  ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 2.824  -31.417 7.519  1.00 15.91  ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 1.396  -31.017 7.264  1.00 18.83  ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 0.870  -31.209 6.142  1.00 19.95  ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 0.743  -30.506 8.307  1.00 19.30  ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 5.106  -35.028 10.099 1.00 14.33  ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 5.281  -35.842 11.314 1.00 16.06  ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 6.789  -36.024 11.491 1.00 15.63  ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 7.541  -36.121 10.511 1.00 16.50  ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 4.587  -37.205 11.269 1.00 20.49  ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 5.174  -38.015 10.237 1.00 22.61  ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 3.097  -37.101 10.998 1.00 21.81  ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 7.216  -36.052 12.745 1.00 13.61  ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 8.639  -36.184 13.050 1.00 13.77  ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 8.854  -36.325 14.543 1.00 13.22  ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 7.911  -36.587 15.287 1.00 14.57  ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 10.105 -36.229 14.967 1.00 12.30  ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 10.483 -36.390 16.366 1.00 12.94  ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 11.398 -35.223 16.736 1.00 13.81  ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 12.374 -34.949 16.016 1.00 13.26  ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 11.239 -37.735 16.550 1.00 13.77  ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 11.739 -37.886 18.001 1.00 15.11  ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 10.356 -38.918 16.145 1.00 14.51  ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 11.149 -34.585 17.908 1.00 13.84  ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 12.041 -33.500 18.356 1.00 14.30  ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 12.668 -33.783 19.710 1.00 14.08  ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 12.080 -34.506 20.520 1.00 13.12  ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 11.348 -32.097 18.366 1.00 14.13  ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 10.418 -31.850 19.535 1.00 14.62  ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 9.147  -32.404 19.565 1.00 16.76  ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 10.781 -30.993 20.574 1.00 15.98  ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 8.249  -32.113 20.594 1.00 18.09  ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 9.908  -30.736 21.639 1.00 17.10  ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 8.642  -31.298 21.638 1.00 18.83  ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 7.743  -31.066 22.665 1.00 20.84  ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 13.851 -33.201 19.963 1.00 13.99  ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 14.503 -33.357 21.243 1.00 14.47  ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 14.085 -32.217 22.162 1.00 15.36  ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 14.231 -31.044 21.803 1.00 14.91  ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 16.041 -33.400 21.120 1.00 14.99  ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 16.673 -33.583 22.489 1.00 16.38  ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 16.494 -34.760 23.210 1.00 17.37  ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.405 -32.563 23.081 1.00 18.31  ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 17.042 -34.927 24.481 1.00 18.72  ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 17.967 -32.723 24.350 1.00 19.34  ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 17.778 -33.901 25.046 1.00 20.67  ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 18.328 -34.048 26.305 1.00 23.58  ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 13.577 -32.571 23.365 1.00 15.21  ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 13.120 -31.607 24.370 1.00 15.15  ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 14.100 -31.639 25.579 1.00 16.86  ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 14.025 -32.555 26.416 1.00 18.14  ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 11.698 -31.955 24.790 1.00 14.95  ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 11.051 -30.923 26.130 1.00 17.92  ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 15.043 -30.667 25.644 1.00 16.24  ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 16.034 -30.701 26.724 1.00 18.74  ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 15.440 -30.588 28.124 1.00 19.27  ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 15.946 -31.238 29.056 1.00 20.32  ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 17.131 -29.661 26.516 1.00 23.34  ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 16.588 -28.366 26.426 1.00 29.78  ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 14.324 -29.867 28.271 1.00 18.66  ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 13.705 -29.703 29.602 1.00 18.81  ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 13.020 -30.965 30.134 1.00 19.54  ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 12.562 -30.984 31.288 1.00 20.87  ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 12.721 -28.545 29.599 1.00 18.60  ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 11.647 -28.769 28.699 1.00 19.37  ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 12.933 -32.013 29.301 1.00 17.88  ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 12.424 -33.312 29.705 1.00 18.19  ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 13.490 -34.428 29.473 1.00 19.52  ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 13.224 -35.589 29.788 1.00 20.88  ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 11.145 -33.626 28.910 1.00 19.24  ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 9.980  -32.708 29.250 1.00 21.62  ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 9.422  -33.027 30.634 1.00 23.93  ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 8.296  -32.165 30.986 1.00 27.30  ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 8.413  -30.986 31.587 1.00 31.79  ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 9.613  -30.512 31.916 1.00 31.56  ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 7.332  -30.270 31.870 1.00 32.20  ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 14.678 -34.089 28.889 1.00 19.29  ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 15.728 -35.055 28.476 1.00 21.54  ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 15.101 -36.189 27.679 1.00 22.13  ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 15.312 -37.373 27.979 1.00 23.19  ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 16.541 -35.606 29.674 1.00 24.88  ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 17.220 -34.552 30.522 1.00 30.95  ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 18.647 -34.167 30.204 1.00 37.96  ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 18.994 -32.956 30.954 1.00 43.81  ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 18.839 -31.715 30.496 1.00 47.77  ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 18.432 -31.506 29.257 1.00 47.60  ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 19.139 -30.675 31.263 1.00 49.75  ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 14.187 -35.827 26.757 1.00 20.78  ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 13.441 -36.843 26.022 1.00 20.35  ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 13.151 -36.388 24.607 1.00 18.25  ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 13.036 -35.190 24.354 1.00 17.33  ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 12.041 -37.051 26.682 1.00 24.30  ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 11.933 -38.149 27.717 1.00 34.86  ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 10.455 -38.347 28.053 1.00 42.04  ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 10.211 -39.500 29.007 1.00 47.89  ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 10.374 -39.095 30.433 1.00 50.32  ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 12.907 -37.350 23.731 1.00 16.79  ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 12.449 -37.083 22.366 1.00 15.76  ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 10.964 -37.331 22.331 1.00 17.33  ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 10.463 -38.285 22.956 1.00 19.43  ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 13.156 -38.017 21.360 1.00 15.73  ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 14.635 -37.803 21.253 1.00 18.09  ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 15.192 -37.056 20.228 1.00 19.92  ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 15.633 -38.315 22.006 1.00 18.18  ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 16.505 -37.129 20.400 1.00 18.63  ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 16.815 -37.855 21.463 1.00 19.96  ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 10.226 -36.490 21.595 1.00 15.38  ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 8.782  -36.668 21.457 1.00 15.16  ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 8.371  -36.746 19.997 1.00 14.22  ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 8.812  -35.915 19.190 1.00 14.08  ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 8.026  -35.472 22.078 1.00 16.15  ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 8.107  -35.419 23.586 1.00 18.50  ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 7.354  -36.285 24.372 1.00 19.75  ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 8.884  -34.462 24.230 1.00 19.93  ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 7.393  -36.213 25.762 1.00 21.16  ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 8.948  -34.400 25.614 1.00 21.51  ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 8.186  -35.265 26.379 1.00 23.25  ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 8.236  -35.209 27.767 1.00 25.82  ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 7.531  -37.733 19.641 1.00 14.51  ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 6.993  -37.782 18.262 1.00 14.55  ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 5.843  -36.749 18.169 1.00 15.92  ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 4.994  -36.707 19.076 1.00 16.92  ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 6.458  -39.225 18.157 1.00 15.70  ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 6.147  -39.613 19.548 1.00 16.59  ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 6.997  -38.821 20.494 1.00 14.81  ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 5.780  -35.958 17.093 1.00 14.88  ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 4.700  -34.978 16.932 1.00 16.19  ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 4.270  -34.842 15.476 1.00 16.03  ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 5.057  -35.104 14.557 1.00 16.69  ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 5.156  -33.563 17.421 1.00 17.85  ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 5.370  -33.515 18.941 1.00 20.26  ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 6.382  -33.053 16.656 1.00 16.76  ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 3.026  -34.358 15.281 1.00 15.03  ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 2.544  -33.851 13.999 1.00 15.35  ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 2.875  -32.322 14.081 1.00 14.98  ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 2.796  -31.702 15.163 1.00 14.62  ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 1.020  -34.008 13.854 1.00 17.68  ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 0.650  -35.377 13.791 1.00 22.17  ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 3.187  -31.700 12.944 1.00 13.64  ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 3.501  -30.259 12.925 1.00 13.92  ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 2.933  -29.592 11.686 1.00 13.92  ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 2.677  -30.278 10.696 1.00 15.22  ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 5.004  -29.958 13.098 1.00 13.77  ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 5.919  -30.699 12.141 1.00 13.04  ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 6.397  -31.958 12.448 1.00 13.03  ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 6.323  -30.114 10.955 1.00 13.29  ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 7.256  -32.634 11.584 1.00 13.28  ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 7.166  -30.786 10.083 1.00 13.43  ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 7.654  -32.037 10.412 1.00 13.24  ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 2.708  -28.284 11.745 1.00 12.98  ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 2.054  -27.596 10.637 1.00 13.93  ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 2.993  -27.309 9.459  1.00 15.57  ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 4.183  -27.664 9.483  1.00 15.78  ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 1.395  -26.313 11.164 1.00 14.42  ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 2.396  -25.375 11.533 1.00 16.45  ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 2.453  -26.701 8.398  1.00 15.13  ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 3.285  -26.278 7.286  1.00 16.41  ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 3.984  -24.933 7.628  1.00 16.55  ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 3.434  -24.116 8.382  1.00 18.03  ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 2.410  -26.126 6.030  1.00 19.10  ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 1.729  -27.452 5.654  1.00 23.83  ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 1.193  -27.410 4.250  1.00 33.26  ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 0.458  -28.675 3.905  1.00 40.56  ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? -0.370 -28.485 2.688  1.00 45.41  ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 5.171  -24.656 7.064  1.00 16.51  ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 5.880  -23.393 7.404  1.00 17.59  ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 5.032  -22.174 7.091  1.00 19.57  ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 4.446  -22.098 6.007  1.00 20.30  ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 7.146  -23.428 6.535  1.00 18.50  ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 7.309  -24.852 6.132  1.00 19.24  ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 5.961  -25.517 6.154  1.00 16.91  ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 4.898  -21.261 8.066  1.00 19.28  ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 4.002  -20.129 7.867  1.00 20.98  ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 4.384  -18.921 8.719  1.00 19.52  ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 5.364  -18.982 9.481  1.00 18.47  ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 2.562  -20.568 8.116  1.00 25.12  ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 2.353  -20.855 9.488  1.00 29.45  ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 3.676  -17.781 8.509  1.00 18.95  ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 3.904  -16.534 9.220  1.00 19.64  ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 3.040  -16.590 10.490 1.00 19.83  ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 1.793  -16.626 10.401 1.00 19.80  ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 3.405  -15.367 8.351  1.00 21.56  ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 4.404  -14.597 7.515  1.00 26.95  ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 3.670  -13.523 6.682  1.00 29.52  ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 5.466  -13.922 8.386  1.00 27.31  ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 3.684  -16.581 11.663 1.00 18.56  ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 2.986  -16.686 12.937 1.00 19.93  ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 3.382  -15.557 13.890 1.00 19.75  ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 4.563  -15.253 14.017 1.00 18.68  ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 3.296  -18.085 13.545 1.00 22.18  ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 2.674  -19.195 12.649 1.00 25.44  ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 2.840  -18.185 15.019 1.00 23.63  ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 3.025  -20.571 13.003 1.00 29.28  ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 2.399  -14.930 14.563 1.00 19.98  ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 2.699  -13.839 15.481 1.00 21.32  ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 3.455  -14.336 16.712 1.00 21.97  ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 3.076  -15.338 17.314 1.00 23.15  ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 1.403  -13.110 15.912 1.00 22.97  ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 1.656  -11.884 16.753 1.00 25.02  ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 1.482  -11.919 18.121 1.00 27.06  ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 2.172  -10.730 16.188 1.00 26.83  ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 1.710  -10.789 18.896 1.00 28.36  ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 2.428  -9.604  16.973 1.00 28.45  ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 2.203  -9.648  18.321 1.00 28.43  ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 4.543  -13.639 17.069 1.00 21.88  ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 5.341  -13.954 18.257 1.00 22.02  ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 5.464  -12.688 19.124 1.00 23.12  ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 5.879  -11.638 18.626 1.00 22.70  ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 6.752  -14.482 17.870 1.00 21.61  ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 7.580  -14.782 19.127 1.00 22.39  ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 6.656  -15.741 16.986 1.00 21.31  ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 5.148  -12.793 20.429 1.00 24.69  ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 5.210  -11.671 21.374 1.00 25.19  ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 6.619  -11.131 21.539 1.00 23.58  ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 7.581  -11.884 21.373 1.00 22.25  ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 4.735  -12.132 22.758 1.00 29.84  ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 3.401  -12.844 22.754 1.00 38.67  ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 2.199  -11.938 22.893 1.00 47.82  ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 1.066  -12.467 22.816 1.00 50.31  ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 2.377  -10.711 23.082 1.00 49.12  ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 6.750  -9.848  21.934 1.00 23.59  ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 8.069  -9.246  22.158 1.00 23.23  ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 8.834  -10.010 23.233 1.00 22.71  ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 8.250  -10.607 24.145 1.00 22.92  ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 7.930  -7.777  22.591 1.00 23.93  ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 10.143 -10.029 23.097 1.00 21.01  ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 11.047 -10.631 24.064 1.00 20.29  ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 12.250 -9.659  24.162 1.00 21.95  ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 12.282 -8.622  23.472 1.00 22.87  ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 11.521 -12.009 23.578 1.00 19.72  ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 12.284 -11.879 22.388 1.00 18.90  ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 13.226 -9.974  25.008 1.00 21.42  ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 14.464 -9.173  25.096 1.00 22.83  ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 15.233 -9.209  23.739 1.00 22.58  ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 16.017 -8.295  23.452 1.00 22.63  ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 15.424 -9.768  26.145 1.00 26.93  ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 15.184 -9.381  27.592 1.00 34.43  ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 16.187 -10.139 28.442 1.00 44.90  ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 17.198 -9.527  28.854 1.00 45.19  ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 16.013 -11.367 28.625 1.00 49.73  ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 15.008 -10.267 22.933 1.00 21.98  ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 15.702 -10.514 21.686 1.00 21.91  ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 15.063 -9.892  20.441 1.00 21.86  ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 15.777 -9.623  19.464 1.00 22.91  ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 15.844 -12.034 21.486 1.00 22.73  ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 16.448 -12.766 22.663 1.00 25.11  ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 17.825 -12.807 22.853 1.00 26.94  ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 15.654 -13.507 23.523 1.00 26.45  ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 18.386 -13.499 23.923 1.00 28.43  ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 16.206 -14.241 24.568 1.00 28.19  ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 17.576 -14.247 24.758 1.00 29.95  ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 18.130 -14.977 25.790 1.00 33.33  ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 13.737 -9.749  20.427 1.00 20.86  ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 13.018 -9.252  19.256 1.00 20.74  ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 11.851 -8.398  19.649 1.00 22.14  ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 11.176 -8.669  20.654 1.00 22.41  ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 12.405 -10.431 18.439 1.00 19.21  ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 13.410 -11.358 17.823 1.00 18.65  ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 13.584 -12.648 18.311 1.00 18.59  ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 14.183 -10.955 16.743 1.00 18.83  ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 14.487 -13.517 17.737 1.00 17.74  ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 15.072 -11.826 16.142 1.00 18.96  ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 15.218 -13.108 16.644 1.00 18.65  ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 16.150 -13.944 16.088 1.00 18.63  ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 11.483 -7.426  18.787 1.00 23.03  ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 10.214 -6.753  19.001 1.00 22.68  ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 9.055  -7.729  18.693 1.00 22.80  ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 9.251  -8.734  18.009 1.00 22.51  ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 10.233 -5.633  17.932 1.00 23.67  ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 11.077 -6.196  16.827 1.00 24.54  ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 12.108 -7.051  17.493 1.00 22.46  ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 7.830  -7.405  19.099 1.00 22.60  ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 6.623  -8.153  18.715 1.00 23.50  ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 6.566  -8.133  17.154 1.00 23.50  ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 6.923  -7.099  16.554 1.00 23.31  ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 5.371  -7.471  19.290 1.00 24.08  ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 6.305  -9.288  16.521 1.00 22.89  ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 6.432  -9.377  15.060 1.00 22.19  ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 5.857  -10.697 14.526 1.00 23.16  ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 5.594  -11.618 15.304 1.00 24.14  ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 7.954  -9.330  14.715 1.00 22.01  ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 8.691  -10.667 15.035 1.00 19.16  ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 10.174 -10.512 15.248 1.00 20.03  ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 10.979 -11.647 14.789 1.00 19.75  ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 11.070 -12.813 15.423 1.00 21.38  ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 11.862 -13.771 14.952 1.00 19.60  ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 10.357 -13.034 16.531 1.00 21.05  ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 5.783  -10.837 13.188 1.00 23.11  ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 5.414  -12.115 12.609 1.00 23.41  ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 6.719  -12.840 12.280 1.00 20.23  ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 7.574  -12.284 11.582 1.00 20.54  ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 4.598  -11.924 11.335 1.00 25.84  ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 3.196  -11.464 11.640 1.00 29.79  ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 2.187  -12.377 11.901 1.00 31.92  ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 2.895  -10.116 11.747 1.00 32.59  ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 0.897  -11.961 12.212 1.00 34.22  ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 1.610  -9.688  12.073 1.00 34.33  ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 0.617  -10.618 12.315 1.00 35.87  ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? -0.671 -10.237 12.626 1.00 39.50  ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 6.888  -14.047 12.818 1.00 17.16  ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 8.047  -14.865 12.476 1.00 16.11  ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 7.634  -15.735 11.281 1.00 15.97  ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 6.558  -16.359 11.298 1.00 17.68  ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 8.487  -15.737 13.667 1.00 16.17  ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 9.636  -16.718 13.297 1.00 16.65  ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 10.417 -17.175 14.510 1.00 17.67  ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 10.615 -16.422 15.475 1.00 18.21  ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 10.921 -18.407 14.450 1.00 15.10  ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 8.468  -15.768 10.236 1.00 14.56  ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 8.160  -16.540 9.034  1.00 14.45  ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 8.789  -17.932 9.071  1.00 14.78  ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 9.678  -18.193 9.904  1.00 15.74  ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 8.649  -15.801 7.788  1.00 16.22  ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 10.054 -15.576 7.825  1.00 17.87  ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 8.295  -18.841 8.165  1.00 14.56  ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 8.835  -20.203 8.013  1.00 14.28  ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 8.760  -20.991 9.361  1.00 15.88  ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 9.607  -21.835 9.635  1.00 15.87  ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 10.281 -20.154 7.450  1.00 14.75  ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 10.374 -19.514 6.090  1.00 17.65  ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 10.303 -20.269 4.937  1.00 20.57  ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 10.493 -18.205 5.749  1.00 19.98  ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 10.437 -19.411 3.926  1.00 21.69  ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 10.535 -18.155 4.364  1.00 21.64  ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 7.738  -20.695 10.186 1.00 15.96  ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 7.564  -21.331 11.505 1.00 15.43  ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 6.499  -22.448 11.438 1.00 15.56  ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 5.456  -22.282 10.798 1.00 16.15  ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 7.162  -20.252 12.545 1.00 15.89  ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 7.090  -20.679 14.008 1.00 18.21  ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 8.476  -21.049 14.531 1.00 18.21  ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 6.591  -19.509 14.902 1.00 20.22  ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 6.745  -23.561 12.125 1.00 14.14  ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 5.801  -24.699 12.137 1.00 14.13  ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 5.428  -24.977 13.574 1.00 14.96  ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 6.324  -25.031 14.398 1.00 15.43  ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 6.496  -25.944 11.547 1.00 13.56  ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 6.902  -25.706 10.116 1.00 16.17  ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 7.905  -26.995 9.456  1.00 18.66  ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 9.367  -26.939 10.520 1.00 19.64  ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 4.133  -25.172 13.883 1.00 13.80  ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 3.727  -25.439 15.260 1.00 14.15  ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 3.321  -26.884 15.473 1.00 14.43  ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 2.807  -27.542 14.567 1.00 13.69  ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 2.517  -24.572 15.681 1.00 15.75  ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 2.735  -23.062 15.635 1.00 17.87  ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 1.438  -22.310 16.082 1.00 18.59  ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 3.925  -22.655 16.518 1.00 19.24  ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 3.589  -27.383 16.686 1.00 14.37  ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 3.122  -28.700 17.137 1.00 14.45  ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 2.552  -28.563 18.553 1.00 15.57  ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 2.897  -27.630 19.278 1.00 16.20  ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 4.292  -29.706 17.168 1.00 14.07  ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 1.672  -29.501 18.939 1.00 16.22  ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 1.185  -29.587 20.304 1.00 17.34  ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 2.286  -30.343 21.075 1.00 19.38  ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 2.575  -31.499 20.765 1.00 19.78  ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? -0.176 -30.335 20.367 1.00 18.33  ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? -0.644 -30.471 21.822 1.00 18.73  ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? -1.225 -29.595 19.520 1.00 18.66  ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 2.886  -29.687 22.052 1.00 21.19  ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 3.950  -30.323 22.822 1.00 22.79  ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 4.563  -29.412 23.845 1.00 23.82  ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 4.349  -28.190 23.820 1.00 24.70  ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 5.345  -30.008 24.752 1.00 23.04  ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 6.004  -29.230 25.788 1.00 22.62  ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 7.280  -28.578 25.304 1.00 22.09  ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 8.062  -29.181 24.554 1.00 21.01  ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 6.313  -30.120 27.012 1.00 23.17  ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 7.105  -29.403 28.060 1.00 24.74  ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 6.531  -28.398 28.835 1.00 26.55  ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 8.432  -29.473 28.347 1.00 25.53  ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 7.508  -27.939 29.607 1.00 26.85  ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 8.669  -28.570 29.358 1.00 26.51  ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 7.514  -27.343 25.774 1.00 23.07  ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 8.757  -26.608 25.589 1.00 24.38  ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 8.911  -25.527 26.685 1.00 25.04  ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 7.922  -25.049 27.241 1.00 26.03  ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 8.875  -26.009 24.193 1.00 27.21  ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 7.822  -25.103 23.925 1.00 31.16  ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 10.159 -25.203 27.026 1.00 23.92  ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 10.577 -24.156 27.968 1.00 24.29  ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 11.599 -23.294 27.176 1.00 24.13  ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 12.147 -23.768 26.170 1.00 23.23  ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 11.283 -24.760 29.197 1.00 26.43  ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 10.476 -25.727 30.051 1.00 33.41  ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 9.792  -25.111 31.253 1.00 40.22  ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 9.963  -23.891 31.483 1.00 42.35  ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 9.071  -25.847 31.960 1.00 41.13  ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 11.894 -22.036 27.577 1.00 24.83  ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 12.839 -21.215 26.776 1.00 24.74  ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 14.200 -21.860 26.432 1.00 23.25  ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 14.693 -21.739 25.300 1.00 24.76  ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 13.007 -19.955 27.630 1.00 26.70  ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 11.690 -19.840 28.378 1.00 27.34  ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 11.311 -21.269 28.706 1.00 25.52  ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 14.769 -22.601 27.384 1.00 21.48  ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 16.041 -23.290 27.180 1.00 20.11  ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 16.027 -24.425 26.162 1.00 18.70  ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 17.078 -24.999 25.814 1.00 18.25  ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 14.814 -24.783 25.694 1.00 16.84  ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 14.676 -25.823 24.673 1.00 16.68  ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 15.018 -25.354 23.252 1.00 16.08  ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 15.085 -26.214 22.359 1.00 16.16  ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 13.263 -26.454 24.676 1.00 17.10  ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 13.032 -27.310 25.907 1.00 20.24  ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 13.988 -27.948 26.367 1.00 20.50  ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 11.886 -27.336 26.412 1.00 21.31  ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 15.185 -24.016 23.005 1.00 15.27  ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 15.534 -23.512 21.647 1.00 15.89  ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 16.804 -24.177 21.151 1.00 15.46  ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 17.722 -24.366 21.959 1.00 15.76  ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 15.683 -21.992 21.644 1.00 18.22  ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 14.109 -21.133 21.831 1.00 20.78  ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 16.816 -24.583 19.891 1.00 15.07  ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 17.976 -25.263 19.330 1.00 15.53  ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 17.825 -26.777 19.267 1.00 15.59  ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 18.585 -27.453 18.560 1.00 15.99  ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 16.813 -27.323 19.960 1.00 14.88  ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 16.518 -28.755 19.883 1.00 14.29  ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 16.099 -29.116 18.457 1.00 14.28  ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 15.320 -28.392 17.830 1.00 15.06  ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 16.647 -30.222 17.932 1.00 13.97  ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 16.381 -30.574 16.540 1.00 14.79  ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 15.091 -31.348 16.360 1.00 14.57  ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 14.771 -32.242 17.159 1.00 15.64  ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.622 -31.325 15.944 1.00 17.57  ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 18.782 -30.332 15.657 1.00 19.81  ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.282 -32.130 14.671 1.00 18.70  ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 20.109 -31.070 15.256 1.00 22.69  ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 14.374 -31.021 15.279 1.00 13.27  ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 13.186 -31.761 14.808 1.00 13.23  ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 13.656 -32.546 13.560 1.00 14.19  ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 14.260 -31.956 12.656 1.00 13.76  ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 12.058 -30.775 14.419 1.00 13.13  ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 10.842 -31.392 13.695 1.00 14.50  ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 10.064 -32.391 14.597 1.00 15.60  ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 9.869  -30.282 13.196 1.00 14.27  ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 13.424 -33.867 13.538 1.00 14.45  ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 13.838 -34.720 12.421 1.00 14.69  ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 12.660 -35.537 11.911 1.00 15.31  ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 11.799 -35.929 12.702 1.00 16.15  ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 14.896 -35.746 12.914 1.00 17.70  ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 16.292 -35.182 13.115 1.00 25.94  ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 17.289 -36.256 13.590 1.00 34.28  ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 18.680 -35.870 13.303 1.00 42.36  ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 19.341 -36.218 12.207 1.00 46.07  ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 18.756 -36.967 11.278 1.00 43.95  ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 20.591 -35.819 12.028 1.00 49.03  ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 12.676 -35.857 10.622 1.00 15.55  ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 11.696 -36.782 10.055 1.00 15.82  ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 12.504 -37.976 9.483  1.00 17.44  ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 13.727 -38.060 9.665  1.00 17.27  ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 10.861 -36.105 8.971  1.00 15.47  ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 11.850 -35.558 7.553  1.00 16.22  ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 11.823 -38.881 8.750  1.00 19.14  ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 12.518 -40.014 8.145  1.00 20.55  ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 13.595 -39.584 7.110  1.00 21.30  ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 14.460 -40.380 6.764  1.00 22.40  ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 11.492 -40.970 7.505  1.00 22.92  ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 10.838 -40.380 6.263  1.00 27.11  ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 9.772  -41.308 5.725  1.00 34.47  ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 8.579  -41.068 5.911  1.00 37.65  ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 10.189 -42.374 5.047  1.00 35.18  ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 13.567 -38.324 6.642  1.00 19.35  ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 14.484 -37.839 5.604  1.00 19.05  ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 15.684 -37.049 6.121  1.00 19.99  ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 16.586 -36.768 5.345  1.00 21.53  ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 13.740 -36.977 4.571  1.00 19.46  ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 12.540 -37.649 3.965  1.00 19.89  ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 11.254 -37.252 4.285  1.00 19.72  ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 12.480 -38.647 3.051  1.00 20.36  ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 10.442 -38.038 3.588  1.00 20.22  ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 11.127 -38.896 2.819  1.00 21.01  ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 15.682 -36.676 7.404  1.00 19.34  ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 16.782 -35.900 7.964  1.00 18.17  ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 16.289 -34.779 8.868  1.00 16.23  ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 15.167 -34.819 9.387  1.00 16.42  ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 17.130 -33.767 9.045  1.00 15.42  ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 16.794 -32.606 9.880  1.00 14.97  ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 15.784 -31.706 9.196  1.00 14.65  ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 15.996 -31.291 8.049  1.00 15.07  ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 18.083 -31.806 10.197 1.00 16.51  ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 17.735 -30.510 10.932 1.00 16.83  ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 19.064 -32.678 11.015 1.00 16.71  ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 14.705 -31.348 9.921  1.00 13.51  ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 13.633 -30.493 9.431  1.00 13.61  ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 13.805 -29.056 9.912  1.00 13.60  ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 13.571 -28.105 9.163  1.00 13.17  ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 12.254 -31.058 9.906  1.00 14.43  ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 11.118 -30.067 9.622  1.00 15.40  ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 11.984 -32.409 9.248  1.00 13.85  ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 14.161 -28.912 11.186 1.00 13.16  ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 14.297 -27.569 11.757 1.00 14.47  ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 14.720 -27.578 13.207 1.00 14.12  ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 15.115 -28.625 13.724 1.00 14.63  ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 14.627 -26.421 13.876 1.00 12.44  ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 15.045 -26.332 15.280 1.00 13.53  ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 14.021 -25.593 16.107 1.00 13.68  ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 13.387 -24.665 15.623 1.00 13.88  ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 16.415 -25.616 15.417 1.00 15.72  ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 16.429 -24.277 14.661 1.00 16.95  ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.600 -26.531 15.021 1.00 17.11  ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 17.769 -23.459 14.987 1.00 18.51  ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 13.874 -25.970 17.401 1.00 12.12  ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 12.933 -25.263 18.299 1.00 12.61  ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 13.297 -23.755 18.334 1.00 13.21  ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 14.471 -23.407 18.474 1.00 13.10  ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 13.016 -25.842 19.740 1.00 13.16  ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 12.150 -25.021 20.696 1.00 14.17  ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 12.561 -27.308 19.760 1.00 13.74  ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 12.283 -22.889 18.195 1.00 13.32  ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 12.490 -21.442 18.164 1.00 13.69  ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 11.503 -20.700 19.076 1.00 14.86  ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 11.854 -19.654 19.622 1.00 15.84  ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 12.377 -20.935 16.723 1.00 14.59  ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 12.535 -19.518 16.633 1.00 14.66  ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 10.294 -21.199 19.252 1.00 14.75  ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 9.267  -20.531 20.082 1.00 16.71  ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 8.494  -21.580 20.929 1.00 17.88  ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 8.523  -22.775 20.631 1.00 16.24  ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 8.228  -19.773 19.174 1.00 18.94  ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 7.356  -20.704 18.521 1.00 20.74  ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 8.852  -18.862 18.145 1.00 19.61  ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 7.721  -21.115 21.904 1.00 19.44  ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 6.874  -22.005 22.700 1.00 21.36  ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 5.943  -21.220 23.599 1.00 22.86  ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 6.197  -20.048 23.865 1.00 22.32  ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 4.863  -21.869 24.040 1.00 24.89  ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 3.836  -21.281 24.910 1.00 26.20  ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 2.489  -21.922 24.676 1.00 27.37  ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 2.232  -22.393 23.572 1.00 27.23  ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 1.630  -21.984 25.721 1.00 27.59  ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 0.282  -22.555 25.620 1.00 27.94  ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 0.220  -24.014 25.184 1.00 27.12  ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? -0.768 -24.431 24.560 1.00 28.09  ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? -0.561 -21.694 24.690 1.00 29.85  ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? -0.748 -20.283 25.192 1.00 34.08  ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? -0.934 -20.040 26.383 1.00 34.94  ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? -0.720 -19.325 24.291 1.00 36.46  ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 1.257  -24.778 25.518 1.00 24.49  ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 1.299  -26.164 25.104 1.00 23.11  ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 1.568  -26.318 23.617 1.00 20.84  ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 1.283  -27.379 23.068 1.00 21.26  ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 2.186  -25.295 22.969 1.00 20.08  ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 2.559  -25.370 21.563 1.00 18.95  ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 4.064  -25.146 21.462 1.00 18.53  ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 4.624  -24.340 22.218 1.00 19.88  ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 1.830  -24.299 20.743 1.00 19.92  ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 0.298  -24.415 20.805 1.00 22.67  ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? -0.341 -23.085 20.479 1.00 24.63  ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? -0.190 -25.473 19.845 1.00 22.79  ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 4.706  -25.854 20.537 1.00 15.17  ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 6.137  -25.692 20.303 1.00 15.77  ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 6.279  -25.208 18.855 1.00 14.73  ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 5.620  -25.756 17.957 1.00 15.62  ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 6.940  -26.993 20.578 1.00 17.20  ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 6.369  -28.211 19.845 1.00 19.88  ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 8.443  -26.801 20.279 1.00 17.21  ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 7.154  -24.233 18.635 1.00 13.70  ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 7.362  -23.738 17.281 1.00 13.67  ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 8.765  -24.048 16.791 1.00 13.71  ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 9.731  -23.895 17.539 1.00 14.18  ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 8.868  -24.535 15.542 1.00 13.60  ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 10.147 -24.922 14.939 1.00 13.63  ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 10.433 -24.059 13.720 1.00 13.73  ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 9.569  -23.870 12.856 1.00 13.05  ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 10.120 -26.386 14.452 1.00 13.56  ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 9.674  -27.381 15.506 1.00 14.27  ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 10.582 -27.926 16.394 1.00 13.49  ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 8.352  -27.802 15.572 1.00 15.23  ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 10.175 -28.853 17.349 1.00 13.89  ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 7.945  -28.723 16.528 1.00 15.99  ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 8.857  -29.223 17.430 1.00 14.81  ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 11.659 -23.544 13.647 1.00 12.22  ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 12.107 -22.784 12.484 1.00 12.41  ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 12.491 -23.800 11.397 1.00 12.22  ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 13.401 -24.610 11.595 1.00 12.17  ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 13.331 -21.950 12.850 1.00 12.05  ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 11.802 -23.765 10.250 1.00 12.86  ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 12.090 -24.717 9.165  1.00 12.74  ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 13.423 -24.405 8.487  1.00 13.36  ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 13.767 -23.229 8.334  1.00 13.70  ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 10.959 -24.582 8.118  1.00 14.25  ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 11.040 -25.599 6.996  1.00 20.20  ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 11.274 -26.770 7.285  1.00 19.04  ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 10.924 -25.196 5.834  1.00 22.91  ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 14.175 -25.450 8.060  1.00 13.01  ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 15.419 -25.225 7.278  1.00 13.26  ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 15.361 -25.980 5.941  1.00 14.47  ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 16.340 -25.936 5.201  1.00 15.67  ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 16.726 -25.590 8.050  1.00 14.04  ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 16.874 -24.747 9.323  1.00 14.20  ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 16.759 -27.089 8.391  1.00 14.60  ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 14.252 -26.694 5.633  1.00 13.93  ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 14.171 -27.532 4.438  1.00 13.75  ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 14.216 -26.777 3.123  1.00 15.42  ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 14.583 -27.375 2.106  1.00 17.86  ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 12.932 -28.429 4.479  1.00 12.95  ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 12.926 -29.388 5.657  1.00 13.38  ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 11.599 -30.140 5.652  1.00 13.60  ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 10.522 -29.263 6.129  1.00 14.13  ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 9.276  -29.660 6.361  1.00 16.14  ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 8.889  -30.889 6.036  1.00 14.93  ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 8.387  -28.815 6.868  1.00 15.16  ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 13.847 -25.494 3.125  1.00 14.94  ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 13.881 -24.689 1.898  1.00 15.11  ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 15.270 -24.123 1.602  1.00 16.56  ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 15.474 -23.610 0.504  1.00 17.66  ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 12.873 -23.546 1.976  1.00 15.93  ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 13.224 -22.535 3.065  1.00 21.50  ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 13.514 -22.971 4.208  1.00 20.75  ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 13.221 -21.296 2.766  1.00 22.71  ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 16.227 -24.200 2.552  1.00 16.00  ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.579 -23.649 2.386  1.00 16.45  ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 18.456 -24.625 1.617  1.00 17.13  ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 19.322 -25.309 2.185  1.00 17.62  ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 18.182 -23.322 3.783  1.00 16.70  ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.324 -22.356 4.634  1.00 18.47  ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 17.948 -22.159 6.037  1.00 19.46  ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.084 -21.043 3.920  1.00 18.85  ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 18.223 -24.691 0.298  1.00 17.35  ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 18.889 -25.706 -0.519 1.00 18.69  ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 20.384 -25.546 -0.598 1.00 20.21  ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 21.098 -26.547 -0.783 1.00 22.07  ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 18.282 -25.782 -1.927 1.00 18.69  ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 16.768 -25.811 -2.022 1.00 19.76  ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 16.313 -25.995 -3.452 1.00 20.99  ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 16.119 -26.839 -1.069 1.00 19.05  ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 20.875 -24.287 -0.441 1.00 20.31  ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 22.308 -23.998 -0.517 1.00 21.32  ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 23.120 -24.619 0.641  1.00 22.89  ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 24.348 -24.684 0.554  1.00 23.50  ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 22.532 -22.487 -0.587 1.00 20.51  ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 21.844 -21.711 0.499  1.00 19.80  ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 20.606 -21.139 0.453  1.00 19.83  ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 22.386 -21.400 1.797  1.00 19.39  ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 20.334 -20.510 1.654  1.00 20.16  ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 21.427 -20.633 2.479  1.00 19.96  ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 23.608 -21.681 2.433  1.00 20.26  ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 21.634 -20.173 3.781  1.00 20.87  ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 23.828 -21.180 3.706  1.00 21.16  ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 22.860 -20.411 4.353  1.00 20.96  ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 22.446 -25.094 1.709  1.00 22.80  ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 23.159 -25.724 2.827  1.00 23.35  ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 23.893 -27.001 2.357  1.00 26.81  ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 24.889 -27.360 2.972  1.00 27.40  ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 22.180 -26.098 3.960  1.00 21.26  ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 21.689 -24.934 4.834  1.00 20.30  ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 20.632 -25.434 5.840  1.00 19.43  ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 22.874 -24.284 5.616  1.00 19.78  ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 23.360 -27.678 1.318  1.00 29.25  ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 23.838 -28.938 0.730  1.00 32.96  ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 24.984 -28.786 -0.254 1.00 36.73  ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 25.409 -29.798 -0.806 1.00 37.58  ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 22.708 -29.619 -0.069 1.00 35.12  ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 21.548 -30.169 0.718  1.00 38.93  ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 21.698 -30.367 1.946  1.00 39.58  ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 20.473 -30.401 0.104  1.00 41.45  ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 25.400 -27.559 -0.580 1.00 38.33  ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 26.486 -27.350 -1.537 1.00 40.99  ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 27.520 -26.380 -0.962 1.00 42.94  ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 28.513 -26.071 -1.631 1.00 44.41  ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 25.925 -26.810 -2.859 1.00 44.43  ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 25.243 -25.465 -2.699 1.00 50.89  ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 24.121 -25.193 -3.684 1.00 59.91  ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 23.933 -24.012 -4.059 1.00 61.39  ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 23.423 -26.158 -4.071 1.00 62.56  ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1BN0 C 2 .   ? 27.740 12.150  7.349  1.00 40.79  ? 201 A1BN0 A N1  1 
HETATM 2156 N  N3  . A1BN0 C 2 .   ? 25.351 14.129  10.618 1.00 28.98  ? 201 A1BN0 A N3  1 
HETATM 2157 C  C4  . A1BN0 C 2 .   ? 25.956 12.957  10.272 1.00 31.46  ? 201 A1BN0 A C4  1 
HETATM 2158 C  C5  . A1BN0 C 2 .   ? 24.235 14.737  9.868  1.00 27.77  ? 201 A1BN0 A C5  1 
HETATM 2159 C  C6  . A1BN0 C 2 .   ? 22.897 14.501  10.559 1.00 26.47  ? 201 A1BN0 A C6  1 
HETATM 2160 C  C7  . A1BN0 C 2 .   ? 22.972 14.917  12.028 1.00 25.96  ? 201 A1BN0 A C7  1 
HETATM 2161 C  C8  . A1BN0 C 2 .   ? 24.124 14.191  12.734 1.00 25.11  ? 201 A1BN0 A C8  1 
HETATM 2162 C  C10 . A1BN0 C 2 .   ? 25.437 14.524  12.025 1.00 27.46  ? 201 A1BN0 A C10 1 
HETATM 2163 C  C13 . A1BN0 C 2 .   ? 27.057 8.658   7.878  1.00 40.33  ? 201 A1BN0 A C13 1 
HETATM 2164 O  O1  . A1BN0 C 2 .   ? 24.694 15.721  14.489 1.00 23.00  ? 201 A1BN0 A O1  1 
HETATM 2165 C  C9  . A1BN0 C 2 .   ? 24.242 14.615  14.187 1.00 23.09  ? 201 A1BN0 A C9  1 
HETATM 2166 N  N4  . A1BN0 C 2 .   ? 23.875 13.712  15.084 1.00 20.66  ? 201 A1BN0 A N4  1 
HETATM 2167 O  O   . A1BN0 C 2 .   ? 26.899 12.491  10.899 1.00 29.47  ? 201 A1BN0 A O   1 
HETATM 2168 N  N2  . A1BN0 C 2 .   ? 25.436 12.318  9.213  1.00 35.55  ? 201 A1BN0 A N2  1 
HETATM 2169 C  C3  . A1BN0 C 2 .   ? 25.964 11.091  8.804  1.00 38.23  ? 201 A1BN0 A C3  1 
HETATM 2170 C  C11 . A1BN0 C 2 .   ? 25.462 9.860   9.238  1.00 39.37  ? 201 A1BN0 A C11 1 
HETATM 2171 C  C12 . A1BN0 C 2 .   ? 26.009 8.665   8.788  1.00 39.98  ? 201 A1BN0 A C12 1 
HETATM 2172 C  C14 . A1BN0 C 2 .   ? 27.538 9.880   7.442  1.00 40.55  ? 201 A1BN0 A C14 1 
HETATM 2173 N  N   . A1BN0 C 2 .   ? 28.525 10.211  6.542  1.00 41.50  ? 201 A1BN0 A N   1 
HETATM 2174 C  C   . A1BN0 C 2 .   ? 29.207 9.290   5.643  1.00 42.35  ? 201 A1BN0 A C   1 
HETATM 2175 C  C2  . A1BN0 C 2 .   ? 27.041 11.088  7.906  1.00 39.74  ? 201 A1BN0 A C2  1 
HETATM 2176 C  C1  . A1BN0 C 2 .   ? 28.608 11.568  6.556  1.00 41.20  ? 201 A1BN0 A C1  1 
HETATM 2177 ZN ZN  . ZN    D 3 .   ? 23.105 -5.633  26.882 1.00 18.98  2 202 ZN    A ZN  1 
HETATM 2178 S  S   . DMS   E 4 .   ? 20.325 21.282  26.138 0.00 39.09  ? 203 DMS   A S   1 
HETATM 2179 O  O   . DMS   E 4 .   ? 21.263 20.602  25.185 0.00 30.92  ? 203 DMS   A O   1 
HETATM 2180 C  C1  . DMS   E 4 .   ? 19.797 20.049  27.357 0.00 35.62  ? 203 DMS   A C1  1 
HETATM 2181 C  C2  . DMS   E 4 .   ? 21.331 22.259  27.288 0.00 35.56  ? 203 DMS   A C2  1 
HETATM 2182 S  S   . DMS   F 4 .   ? 15.117 -0.321  12.192 1.00 40.56  ? 204 DMS   A S   1 
HETATM 2183 O  O   . DMS   F 4 .   ? 16.460 -0.693  12.735 1.00 37.69  ? 204 DMS   A O   1 
HETATM 2184 C  C1  . DMS   F 4 .   ? 15.153 0.334   10.505 1.00 40.68  ? 204 DMS   A C1  1 
HETATM 2185 C  C2  . DMS   F 4 .   ? 14.425 1.158   13.035 1.00 39.93  ? 204 DMS   A C2  1 
HETATM 2186 N  N1  . A1BN0 G 2 .   ? 8.895  -18.880 26.101 1.00 31.76  ? 201 A1BN0 C N1  1 
HETATM 2187 N  N3  . A1BN0 G 2 .   ? 10.985 -16.567 22.711 1.00 23.48  ? 201 A1BN0 C N3  1 
HETATM 2188 C  C4  . A1BN0 G 2 .   ? 10.385 -17.741 23.071 1.00 26.35  ? 201 A1BN0 C C4  1 
HETATM 2189 C  C5  . A1BN0 G 2 .   ? 12.166 -15.950 23.340 1.00 22.49  ? 201 A1BN0 C C5  1 
HETATM 2190 C  C6  . A1BN0 G 2 .   ? 13.416 -16.140 22.478 1.00 22.04  ? 201 A1BN0 C C6  1 
HETATM 2191 C  C7  . A1BN0 G 2 .   ? 13.157 -15.718 21.028 1.00 20.68  ? 201 A1BN0 C C7  1 
HETATM 2192 C  C8  . A1BN0 G 2 .   ? 11.928 -16.438 20.456 1.00 20.10  ? 201 A1BN0 C C8  1 
HETATM 2193 C  C10 . A1BN0 G 2 .   ? 10.723 -16.119 21.342 1.00 21.64  ? 201 A1BN0 C C10 1 
HETATM 2194 C  C13 . A1BN0 G 2 .   ? 9.345  -22.262 24.940 1.00 31.76  ? 201 A1BN0 C C13 1 
HETATM 2195 O  O1  . A1BN0 G 2 .   ? 11.171 -14.841 18.828 1.00 17.34  ? 201 A1BN0 C O1  1 
HETATM 2196 C  C9  . A1BN0 G 2 .   ? 11.621 -15.975 19.043 1.00 18.73  ? 201 A1BN0 C C9  1 
HETATM 2197 N  N4  . A1BN0 G 2 .   ? 11.785 -16.890 18.095 1.00 17.71  ? 201 A1BN0 C N4  1 
HETATM 2198 O  O   . A1BN0 G 2 .   ? 9.299  -18.097 22.604 1.00 25.61  ? 201 A1BN0 C O   1 
HETATM 2199 N  N2  . A1BN0 G 2 .   ? 11.026 -18.472 24.010 1.00 29.24  ? 201 A1BN0 C N2  1 
HETATM 2200 C  C3  . A1BN0 G 2 .   ? 10.501 -19.739 24.346 1.00 30.87  ? 201 A1BN0 C C3  1 
HETATM 2201 C  C11 . A1BN0 G 2 .   ? 10.891 -20.904 23.669 1.00 31.26  ? 201 A1BN0 C C11 1 
HETATM 2202 C  C12 . A1BN0 G 2 .   ? 10.321 -22.140 23.959 1.00 31.55  ? 201 A1BN0 C C12 1 
HETATM 2203 C  C14 . A1BN0 G 2 .   ? 8.956  -21.106 25.601 1.00 31.57  ? 201 A1BN0 C C14 1 
HETATM 2204 N  N   . A1BN0 G 2 .   ? 8.021  -20.888 26.586 1.00 31.47  ? 201 A1BN0 C N   1 
HETATM 2205 C  C   . A1BN0 G 2 .   ? 7.153  -21.894 27.180 1.00 31.57  ? 201 A1BN0 C C   1 
HETATM 2206 C  C2  . A1BN0 G 2 .   ? 9.495  -19.857 25.320 1.00 31.45  ? 201 A1BN0 C C2  1 
HETATM 2207 C  C1  . A1BN0 G 2 .   ? 8.039  -19.552 26.834 1.00 31.82  ? 201 A1BN0 C C1  1 
HETATM 2208 ZN ZN  . ZN    H 3 .   ? 10.592 -35.746 5.623  1.00 16.13  2 202 ZN    C ZN  1 
HETATM 2209 S  S   . DMS   I 4 .   ? 14.552 -10.233 7.691  0.00 39.09  ? 203 DMS   C S   1 
HETATM 2210 O  O   . DMS   I 4 .   ? 13.935 -9.829  8.997  0.00 30.92  ? 203 DMS   C O   1 
HETATM 2211 C  C1  . DMS   I 4 .   ? 13.224 -10.299 6.458  0.00 35.62  ? 203 DMS   C C1  1 
HETATM 2212 C  C2  . DMS   I 4 .   ? 15.372 -8.771  7.000  0.00 35.56  ? 203 DMS   C C2  1 
HETATM 2213 S  S   . DMS   J 4 .   ? 19.878 -31.413 19.597 1.00 47.59  ? 204 DMS   C S   1 
HETATM 2214 O  O   . DMS   J 4 .   ? 18.474 -31.700 19.314 1.00 45.39  ? 204 DMS   C O   1 
HETATM 2215 C  C1  . DMS   J 4 .   ? 20.098 -30.832 21.304 1.00 47.72  ? 204 DMS   C C1  1 
HETATM 2216 C  C2  . DMS   J 4 .   ? 20.526 -29.912 18.808 1.00 47.41  ? 204 DMS   C C2  1 
HETATM 2217 O  O   . HOH   K 5 .   ? 14.886 22.108  24.549 1.00 30.12  ? 301 HOH   A O   1 
HETATM 2218 O  O   . HOH   K 5 .   ? 24.832 24.101  10.539 1.00 52.77  ? 302 HOH   A O   1 
HETATM 2219 O  O   . HOH   K 5 .   ? 22.523 7.672   26.999 1.00 226.13 ? 303 HOH   A O   1 
HETATM 2220 O  O   . HOH   K 5 .   ? 23.830 7.217   28.247 1.00 23.80  ? 304 HOH   A O   1 
HETATM 2221 O  O   . HOH   K 5 .   ? 29.139 13.435  11.572 1.00 38.42  ? 305 HOH   A O   1 
HETATM 2222 O  O   . HOH   K 5 .   ? 11.195 21.328  24.410 1.00 32.04  ? 306 HOH   A O   1 
HETATM 2223 O  O   . HOH   K 5 .   ? 14.369 -5.484  26.936 1.00 29.06  ? 307 HOH   A O   1 
HETATM 2224 O  O   . HOH   K 5 .   ? 26.927 19.524  24.184 1.00 57.39  ? 308 HOH   A O   1 
HETATM 2225 O  O   . HOH   K 5 .   ? 11.577 -1.663  27.923 1.00 24.27  ? 309 HOH   A O   1 
HETATM 2226 O  O   . HOH   K 5 .   ? 18.631 -11.599 27.176 1.00 31.66  ? 310 HOH   A O   1 
HETATM 2227 O  O   . HOH   K 5 .   ? 17.106 20.687  22.910 1.00 23.80  ? 311 HOH   A O   1 
HETATM 2228 O  O   . HOH   K 5 .   ? 6.421  2.953   28.860 1.00 44.91  ? 312 HOH   A O   1 
HETATM 2229 O  O   . HOH   K 5 .   ? 22.599 6.705   1.553  1.00 27.70  ? 313 HOH   A O   1 
HETATM 2230 O  O   . HOH   K 5 .   ? 20.430 10.328  32.298 1.00 41.24  ? 314 HOH   A O   1 
HETATM 2231 O  O   . HOH   K 5 .   ? 17.762 -7.573  21.485 1.00 22.00  ? 315 HOH   A O   1 
HETATM 2232 O  O   . HOH   K 5 .   ? 6.713  -1.975  23.888 1.00 29.31  ? 316 HOH   A O   1 
HETATM 2233 O  O   . HOH   K 5 .   ? 24.104 3.802   29.150 1.00 26.13  ? 317 HOH   A O   1 
HETATM 2234 O  O   . HOH   K 5 .   ? 31.358 12.645  9.523  1.00 42.87  ? 318 HOH   A O   1 
HETATM 2235 O  O   . HOH   K 5 .   ? 16.317 18.513  27.016 1.00 46.61  ? 319 HOH   A O   1 
HETATM 2236 O  O   . HOH   K 5 .   ? 34.991 13.951  16.324 1.00 29.42  ? 320 HOH   A O   1 
HETATM 2237 O  O   . HOH   K 5 .   ? 31.044 -5.330  11.490 1.00 37.91  ? 321 HOH   A O   1 
HETATM 2238 O  O   . HOH   K 5 .   ? 15.046 8.625   13.322 1.00 15.57  ? 322 HOH   A O   1 
HETATM 2239 O  O   . HOH   K 5 .   ? 12.417 17.829  13.147 1.00 36.89  ? 323 HOH   A O   1 
HETATM 2240 O  O   . HOH   K 5 .   ? 7.229  7.571   31.627 1.00 36.42  ? 324 HOH   A O   1 
HETATM 2241 O  O   . HOH   K 5 .   ? 28.501 -6.169  3.503  1.00 30.48  ? 325 HOH   A O   1 
HETATM 2242 O  O   . HOH   K 5 .   ? 25.615 17.889  12.977 1.00 21.24  ? 326 HOH   A O   1 
HETATM 2243 O  O   . HOH   K 5 .   ? -1.803 15.742  20.200 1.00 28.72  ? 327 HOH   A O   1 
HETATM 2244 O  O   . HOH   K 5 .   ? 16.031 -0.769  4.621  1.00 30.63  ? 328 HOH   A O   1 
HETATM 2245 O  O   . HOH   K 5 .   ? 8.847  4.018   11.976 1.00 37.65  ? 329 HOH   A O   1 
HETATM 2246 O  O   . HOH   K 5 .   ? 28.943 -7.699  25.269 1.00 63.47  ? 330 HOH   A O   1 
HETATM 2247 O  O   . HOH   K 5 .   ? 5.081  11.068  12.524 1.00 35.96  ? 331 HOH   A O   1 
HETATM 2248 O  O   . HOH   K 5 .   ? 23.708 1.815   -0.859 1.00 17.12  ? 332 HOH   A O   1 
HETATM 2249 O  O   . HOH   K 5 .   ? 22.117 8.741   2.878  1.00 28.15  ? 333 HOH   A O   1 
HETATM 2250 O  O   . HOH   K 5 .   ? 34.494 -0.802  16.548 1.00 15.25  ? 334 HOH   A O   1 
HETATM 2251 O  O   . HOH   K 5 .   ? 6.841  15.711  29.069 1.00 44.69  ? 335 HOH   A O   1 
HETATM 2252 O  O   . HOH   K 5 .   ? 22.175 -6.137  0.596  1.00 45.14  ? 336 HOH   A O   1 
HETATM 2253 O  O   . HOH   K 5 .   ? -0.089 14.455  22.623 1.00 57.10  ? 337 HOH   A O   1 
HETATM 2254 O  O   . HOH   K 5 .   ? 23.517 16.593  27.396 1.00 46.73  ? 338 HOH   A O   1 
HETATM 2255 O  O   . HOH   K 5 .   ? 4.163  10.260  17.841 1.00 33.23  ? 339 HOH   A O   1 
HETATM 2256 O  O   . HOH   K 5 .   ? 27.931 24.814  19.384 1.00 46.40  ? 340 HOH   A O   1 
HETATM 2257 O  O   . HOH   K 5 .   ? 11.864 13.281  8.703  1.00 55.42  ? 341 HOH   A O   1 
HETATM 2258 O  O   . HOH   K 5 .   ? 11.150 -0.203  15.821 1.00 24.32  ? 342 HOH   A O   1 
HETATM 2259 O  O   . HOH   K 5 .   ? 27.182 19.165  15.230 1.00 22.27  ? 343 HOH   A O   1 
HETATM 2260 O  O   . HOH   K 5 .   ? 23.256 -11.157 30.635 1.00 52.46  ? 344 HOH   A O   1 
HETATM 2261 O  O   . HOH   K 5 .   ? 30.223 6.358   4.536  1.00 41.08  ? 345 HOH   A O   1 
HETATM 2262 O  O   . HOH   K 5 .   ? 28.722 17.343  8.355  1.00 41.70  ? 346 HOH   A O   1 
HETATM 2263 O  O   . HOH   K 5 .   ? 23.563 10.937  21.415 1.00 15.36  ? 347 HOH   A O   1 
HETATM 2264 O  O   . HOH   K 5 .   ? 29.517 0.989   25.065 1.00 53.86  ? 348 HOH   A O   1 
HETATM 2265 O  O   . HOH   K 5 .   ? 17.271 2.170   9.294  1.00 20.38  ? 349 HOH   A O   1 
HETATM 2266 O  O   . HOH   K 5 .   ? 22.959 20.825  20.545 1.00 25.69  ? 350 HOH   A O   1 
HETATM 2267 O  O   . HOH   K 5 .   ? 34.928 15.096  25.241 1.00 42.02  ? 351 HOH   A O   1 
HETATM 2268 O  O   . HOH   K 5 .   ? 13.569 18.686  14.637 1.00 30.05  ? 352 HOH   A O   1 
HETATM 2269 O  O   . HOH   K 5 .   ? 24.204 14.422  30.264 1.00 57.99  ? 353 HOH   A O   1 
HETATM 2270 O  O   . HOH   K 5 .   ? 20.148 2.166   9.230  1.00 15.30  ? 354 HOH   A O   1 
HETATM 2271 O  O   . HOH   K 5 .   ? 20.220 11.860  8.596  1.00 22.30  ? 355 HOH   A O   1 
HETATM 2272 O  O   . HOH   K 5 .   ? 28.076 3.142   -0.403 1.00 23.87  ? 356 HOH   A O   1 
HETATM 2273 O  O   . HOH   K 5 .   ? 22.864 10.631  22.676 1.00 109.13 ? 357 HOH   A O   1 
HETATM 2274 O  O   . HOH   K 5 .   ? 5.038  3.073   20.950 1.00 21.08  ? 358 HOH   A O   1 
HETATM 2275 O  O   . HOH   K 5 .   ? 32.280 2.411   5.100  1.00 39.31  ? 359 HOH   A O   1 
HETATM 2276 O  O   . HOH   K 5 .   ? 19.948 -4.939  15.309 1.00 27.62  ? 360 HOH   A O   1 
HETATM 2277 O  O   . HOH   K 5 .   ? 3.497  18.176  23.733 1.00 29.51  ? 361 HOH   A O   1 
HETATM 2278 O  O   . HOH   K 5 .   ? 17.200 0.250   2.568  1.00 35.84  ? 362 HOH   A O   1 
HETATM 2279 O  O   . HOH   K 5 .   ? 21.593 9.826   23.345 1.00 14.04  ? 363 HOH   A O   1 
HETATM 2280 O  O   . HOH   K 5 .   ? 34.736 -6.547  21.518 1.00 44.05  ? 364 HOH   A O   1 
HETATM 2281 O  O   . HOH   K 5 .   ? 25.119 4.265   -1.283 1.00 23.28  ? 365 HOH   A O   1 
HETATM 2282 O  O   . HOH   K 5 .   ? 25.496 1.475   29.805 1.00 31.06  ? 366 HOH   A O   1 
HETATM 2283 O  O   . HOH   K 5 .   ? 17.267 18.426  15.572 1.00 16.17  ? 367 HOH   A O   1 
HETATM 2284 O  O   . HOH   K 5 .   ? 16.841 4.490   5.913  1.00 29.42  ? 368 HOH   A O   1 
HETATM 2285 O  O   . HOH   K 5 .   ? 4.423  4.140   28.052 1.00 37.15  ? 369 HOH   A O   1 
HETATM 2286 O  O   . HOH   K 5 .   ? 18.436 -3.704  14.665 1.00 30.55  ? 370 HOH   A O   1 
HETATM 2287 O  O   . HOH   K 5 .   ? 30.326 -5.901  26.185 1.00 29.73  ? 371 HOH   A O   1 
HETATM 2288 O  O   . HOH   K 5 .   ? 28.360 0.650   26.800 1.00 21.97  ? 372 HOH   A O   1 
HETATM 2289 O  O   . HOH   K 5 .   ? 16.427 -3.329  13.876 1.00 32.92  ? 373 HOH   A O   1 
HETATM 2290 O  O   . HOH   K 5 .   ? 30.947 4.651   7.825  1.00 29.86  ? 374 HOH   A O   1 
HETATM 2291 O  O   . HOH   K 5 .   ? 29.721 -2.213  8.437  1.00 23.70  ? 375 HOH   A O   1 
HETATM 2292 O  O   . HOH   K 5 .   ? 11.277 10.621  10.117 1.00 48.68  ? 376 HOH   A O   1 
HETATM 2293 O  O   . HOH   K 5 .   ? 4.170  20.361  15.459 1.00 35.28  ? 377 HOH   A O   1 
HETATM 2294 O  O   . HOH   K 5 .   ? 2.715  8.591   26.097 1.00 33.91  ? 378 HOH   A O   1 
HETATM 2295 O  O   . HOH   K 5 .   ? 34.533 3.468   26.237 1.00 32.40  ? 379 HOH   A O   1 
HETATM 2296 O  O   . HOH   K 5 .   ? 3.290  11.677  10.457 1.00 50.83  ? 380 HOH   A O   1 
HETATM 2297 O  O   . HOH   K 5 .   ? 28.828 21.883  22.313 1.00 37.77  ? 381 HOH   A O   1 
HETATM 2298 O  O   . HOH   K 5 .   ? 31.960 14.916  12.874 1.00 34.63  ? 382 HOH   A O   1 
HETATM 2299 O  O   . HOH   K 5 .   ? 4.117  20.072  21.671 1.00 26.35  ? 383 HOH   A O   1 
HETATM 2300 O  O   . HOH   K 5 .   ? 35.640 14.547  20.431 1.00 27.64  ? 384 HOH   A O   1 
HETATM 2301 O  O   . HOH   K 5 .   ? 32.706 8.683   4.515  1.00 50.09  ? 385 HOH   A O   1 
HETATM 2302 O  O   . HOH   K 5 .   ? 24.703 -9.051  22.676 1.00 50.64  ? 386 HOH   A O   1 
HETATM 2303 O  O   . HOH   K 5 .   ? 27.209 -8.758  8.559  1.00 33.20  ? 387 HOH   A O   1 
HETATM 2304 O  O   . HOH   K 5 .   ? 14.696 -4.079  16.082 1.00 27.70  ? 388 HOH   A O   1 
HETATM 2305 O  O   . HOH   K 5 .   ? 29.205 25.846  13.550 1.00 34.10  ? 389 HOH   A O   1 
HETATM 2306 O  O   . HOH   K 5 .   ? 29.645 26.075  16.204 1.00 49.84  ? 390 HOH   A O   1 
HETATM 2307 O  O   . HOH   K 5 .   ? 16.630 9.060   6.768  1.00 23.94  ? 391 HOH   A O   1 
HETATM 2308 O  O   . HOH   K 5 .   ? 18.261 -5.317  30.498 1.00 30.99  ? 392 HOH   A O   1 
HETATM 2309 O  O   . HOH   K 5 .   ? 12.034 -2.743  15.819 1.00 34.22  ? 393 HOH   A O   1 
HETATM 2310 O  O   . HOH   K 5 .   ? 15.747 12.071  30.692 1.00 40.81  ? 394 HOH   A O   1 
HETATM 2311 O  O   . HOH   K 5 .   ? 30.658 -3.101  11.851 1.00 30.81  ? 395 HOH   A O   1 
HETATM 2312 O  O   . HOH   K 5 .   ? 28.373 16.202  10.696 1.00 38.82  ? 396 HOH   A O   1 
HETATM 2313 O  O   . HOH   K 5 .   ? 32.940 -2.682  15.213 1.00 23.56  ? 397 HOH   A O   1 
HETATM 2314 O  O   . HOH   K 5 .   ? 4.807  6.224   13.301 1.00 53.07  ? 398 HOH   A O   1 
HETATM 2315 O  O   . HOH   K 5 .   ? 19.969 13.803  29.014 1.00 31.94  ? 399 HOH   A O   1 
HETATM 2316 O  O   . HOH   K 5 .   ? 3.917  14.823  10.459 1.00 28.36  ? 400 HOH   A O   1 
HETATM 2317 O  O   . HOH   K 5 .   ? 24.049 17.891  6.447  1.00 46.68  ? 401 HOH   A O   1 
HETATM 2318 O  O   . HOH   K 5 .   ? 17.824 19.875  13.352 1.00 31.96  ? 402 HOH   A O   1 
HETATM 2319 O  O   . HOH   K 5 .   ? 3.439  2.587   18.940 1.00 35.45  ? 403 HOH   A O   1 
HETATM 2320 O  O   . HOH   K 5 .   ? 22.217 -8.386  19.284 1.00 35.56  ? 404 HOH   A O   1 
HETATM 2321 O  O   . HOH   K 5 .   ? 30.059 -2.136  3.504  1.00 40.63  ? 405 HOH   A O   1 
HETATM 2322 O  O   . HOH   K 5 .   ? 32.193 22.431  11.522 1.00 34.90  ? 406 HOH   A O   1 
HETATM 2323 O  O   . HOH   K 5 .   ? 13.311 8.574   11.048 1.00 21.84  ? 407 HOH   A O   1 
HETATM 2324 O  O   . HOH   K 5 .   ? 12.314 18.504  26.423 1.00 25.47  ? 408 HOH   A O   1 
HETATM 2325 O  O   . HOH   K 5 .   ? 6.773  16.335  8.813  1.00 37.63  ? 409 HOH   A O   1 
HETATM 2326 O  O   . HOH   K 5 .   ? 26.464 -8.092  24.154 1.00 47.70  ? 410 HOH   A O   1 
HETATM 2327 O  O   . HOH   K 5 .   ? 15.286 23.220  17.001 1.00 23.95  ? 411 HOH   A O   1 
HETATM 2328 O  O   . HOH   K 5 .   ? 11.146 2.209   12.381 1.00 25.27  ? 412 HOH   A O   1 
HETATM 2329 O  O   . HOH   K 5 .   ? 27.989 11.827  27.728 1.00 24.93  ? 413 HOH   A O   1 
HETATM 2330 O  O   . HOH   K 5 .   ? 4.513  10.548  14.923 1.00 49.82  ? 414 HOH   A O   1 
HETATM 2331 O  O   . HOH   K 5 .   ? 30.020 6.134   30.099 1.00 43.68  ? 415 HOH   A O   1 
HETATM 2332 O  O   . HOH   K 5 .   ? 18.758 22.944  6.729  1.00 50.51  ? 416 HOH   A O   1 
HETATM 2333 O  O   . HOH   K 5 .   ? 19.666 -9.570  20.192 1.00 46.87  ? 417 HOH   A O   1 
HETATM 2334 O  O   . HOH   K 5 .   ? -2.612 2.945   25.055 1.00 57.98  ? 418 HOH   A O   1 
HETATM 2335 O  O   . HOH   K 5 .   ? 10.501 6.796   11.351 1.00 47.39  ? 419 HOH   A O   1 
HETATM 2336 O  O   . HOH   K 5 .   ? 4.757  22.677  6.994  1.00 61.96  ? 420 HOH   A O   1 
HETATM 2337 O  O   . HOH   K 5 .   ? 17.518 16.828  28.845 1.00 50.02  ? 421 HOH   A O   1 
HETATM 2338 O  O   . HOH   K 5 .   ? 15.630 8.234   33.986 1.00 31.06  ? 422 HOH   A O   1 
HETATM 2339 O  O   . HOH   K 5 .   ? 31.394 -3.597  29.931 1.00 71.15  ? 423 HOH   A O   1 
HETATM 2340 O  O   . HOH   K 5 .   ? 19.742 23.609  23.274 1.00 60.15  ? 424 HOH   A O   1 
HETATM 2341 O  O   . HOH   K 5 .   ? 24.761 -5.398  32.486 1.00 38.05  ? 425 HOH   A O   1 
HETATM 2342 O  O   . HOH   K 5 .   ? 31.852 -7.124  17.791 1.00 45.17  ? 426 HOH   A O   1 
HETATM 2343 O  O   . HOH   K 5 .   ? 17.943 22.624  16.018 1.00 42.16  ? 427 HOH   A O   1 
HETATM 2344 O  O   . HOH   K 5 .   ? 0.906  17.340  23.278 1.00 53.85  ? 428 HOH   A O   1 
HETATM 2345 O  O   . HOH   K 5 .   ? 23.305 19.261  27.564 1.00 73.33  ? 429 HOH   A O   1 
HETATM 2346 O  O   . HOH   K 5 .   ? 25.599 22.183  5.783  1.00 57.22  ? 430 HOH   A O   1 
HETATM 2347 O  O   . HOH   K 5 .   ? 2.633  14.242  25.089 1.00 49.34  ? 431 HOH   A O   1 
HETATM 2348 O  O   . HOH   K 5 .   ? 32.700 5.152   4.616  1.00 53.50  ? 432 HOH   A O   1 
HETATM 2349 O  O   . HOH   K 5 .   ? 25.574 14.614  6.502  1.00 45.74  ? 433 HOH   A O   1 
HETATM 2350 O  O   . HOH   K 5 .   ? 31.472 10.223  13.939 1.00 51.65  ? 434 HOH   A O   1 
HETATM 2351 O  O   . HOH   K 5 .   ? 24.290 2.802   9.922  1.00 104.78 ? 435 HOH   A O   1 
HETATM 2352 O  O   . HOH   K 5 .   ? 5.329  2.577   12.129 1.00 59.46  ? 436 HOH   A O   1 
HETATM 2353 O  O   . HOH   K 5 .   ? 30.883 12.338  13.041 1.00 50.52  ? 437 HOH   A O   1 
HETATM 2354 O  O   . HOH   K 5 .   ? -2.747 -1.323  25.729 1.00 66.67  ? 438 HOH   A O   1 
HETATM 2355 O  O   . HOH   K 5 .   ? 18.177 10.986  6.585  1.00 33.01  ? 439 HOH   A O   1 
HETATM 2356 O  O   . HOH   K 5 .   ? 6.629  18.935  26.440 1.00 47.64  ? 440 HOH   A O   1 
HETATM 2357 O  O   . HOH   K 5 .   ? 1.938  16.227  9.273  1.00 49.34  ? 441 HOH   A O   1 
HETATM 2358 O  O   . HOH   K 5 .   ? 9.018  17.957  8.856  1.00 53.55  ? 442 HOH   A O   1 
HETATM 2359 O  O   . HOH   K 5 .   ? 26.145 18.613  26.405 1.00 44.92  ? 443 HOH   A O   1 
HETATM 2360 O  O   . HOH   K 5 .   ? 18.116 13.006  30.429 1.00 46.35  ? 444 HOH   A O   1 
HETATM 2361 O  O   . HOH   K 5 .   ? 13.983 21.667  14.743 1.00 33.05  ? 445 HOH   A O   1 
HETATM 2362 O  O   . HOH   K 5 .   ? 2.117  21.534  8.867  1.00 54.78  ? 446 HOH   A O   1 
HETATM 2363 O  O   . HOH   K 5 .   ? 20.177 -6.901  -0.717 1.00 56.87  ? 447 HOH   A O   1 
HETATM 2364 O  O   . HOH   K 5 .   ? 33.771 -2.216  9.161  1.00 33.41  ? 448 HOH   A O   1 
HETATM 2365 O  O   . HOH   K 5 .   ? 23.324 -10.060 20.074 1.00 57.51  ? 449 HOH   A O   1 
HETATM 2366 O  O   . HOH   K 5 .   ? 28.090 1.569   29.385 1.00 34.00  ? 450 HOH   A O   1 
HETATM 2367 O  O   . HOH   K 5 .   ? 2.319  21.111  12.308 1.00 42.62  ? 451 HOH   A O   1 
HETATM 2368 O  O   . HOH   K 5 .   ? -4.891 5.932   15.127 1.00 49.44  ? 452 HOH   A O   1 
HETATM 2369 O  O   . HOH   K 5 .   ? 26.773 20.017  5.162  1.00 47.31  ? 453 HOH   A O   1 
HETATM 2370 O  O   . HOH   K 5 .   ? 25.675 -9.428  19.404 1.00 38.83  ? 454 HOH   A O   1 
HETATM 2371 O  O   . HOH   K 5 .   ? 8.877  -2.264  27.832 1.00 45.96  ? 455 HOH   A O   1 
HETATM 2372 O  O   . HOH   K 5 .   ? 2.785  4.034   16.966 1.00 36.53  ? 456 HOH   A O   1 
HETATM 2373 O  O   . HOH   K 5 .   ? 9.486  21.937  12.452 1.00 33.17  ? 457 HOH   A O   1 
HETATM 2374 O  O   . HOH   K 5 .   ? 34.957 11.490  15.734 1.00 50.32  ? 458 HOH   A O   1 
HETATM 2375 O  O   . HOH   K 5 .   ? 3.475  8.132   16.137 1.00 63.55  ? 459 HOH   A O   1 
HETATM 2376 O  O   . HOH   K 5 .   ? 31.405 -3.804  9.659  1.00 33.72  ? 460 HOH   A O   1 
HETATM 2377 O  O   . HOH   K 5 .   ? 3.149  11.047  27.221 1.00 44.14  ? 461 HOH   A O   1 
HETATM 2378 O  O   . HOH   K 5 .   ? 28.663 3.994   30.642 1.00 48.27  ? 462 HOH   A O   1 
HETATM 2379 O  O   . HOH   K 5 .   ? 4.798  0.752   14.754 1.00 61.45  ? 463 HOH   A O   1 
HETATM 2380 O  O   . HOH   K 5 .   ? 11.331 -4.483  29.751 1.00 51.28  ? 464 HOH   A O   1 
HETATM 2381 O  O   . HOH   K 5 .   ? 29.633 20.989  25.240 1.00 67.90  ? 465 HOH   A O   1 
HETATM 2382 O  O   . HOH   L 5 .   ? 12.687 -36.148 0.798  1.00 150.88 ? 301 HOH   C O   1 
HETATM 2383 O  O   . HOH   L 5 .   ? 20.221 -8.568  7.705  1.00 27.64  ? 302 HOH   C O   1 
HETATM 2384 O  O   . HOH   L 5 .   ? 2.034  -32.671 18.687 1.00 89.09  ? 303 HOH   C O   1 
HETATM 2385 O  O   . HOH   L 5 .   ? 2.591  -23.108 10.562 1.00 35.87  ? 304 HOH   C O   1 
HETATM 2386 O  O   . HOH   L 5 .   ? 9.900  -21.684 32.692 1.00 61.58  ? 305 HOH   C O   1 
HETATM 2387 O  O   . HOH   L 5 .   ? 30.785 -10.516 10.389 1.00 39.29  ? 306 HOH   C O   1 
HETATM 2388 O  O   . HOH   L 5 .   ? 12.914 -13.927 4.671  1.00 48.07  ? 307 HOH   C O   1 
HETATM 2389 O  O   . HOH   L 5 .   ? 20.540 -22.545 18.604 1.00 14.28  ? 308 HOH   C O   1 
HETATM 2390 O  O   . HOH   L 5 .   ? 17.240 -37.907 3.128  1.00 40.09  ? 309 HOH   C O   1 
HETATM 2391 O  O   . HOH   L 5 .   ? 26.180 -33.071 6.020  1.00 42.76  ? 310 HOH   C O   1 
HETATM 2392 O  O   . HOH   L 5 .   ? 5.526  -17.814 24.976 1.00 38.75  ? 311 HOH   C O   1 
HETATM 2393 O  O   . HOH   L 5 .   ? 4.233  -36.160 21.484 1.00 37.17  ? 312 HOH   C O   1 
HETATM 2394 O  O   . HOH   L 5 .   ? 10.107 -22.920 4.916  1.00 23.26  ? 313 HOH   C O   1 
HETATM 2395 O  O   . HOH   L 5 .   ? 12.200 -29.589 33.440 1.00 23.83  ? 314 HOH   C O   1 
HETATM 2396 O  O   . HOH   L 5 .   ? 35.739 -15.351 15.679 1.00 40.77  ? 315 HOH   C O   1 
HETATM 2397 O  O   . HOH   L 5 .   ? 23.771 -9.316  7.861  1.00 24.80  ? 316 HOH   C O   1 
HETATM 2398 O  O   . HOH   L 5 .   ? 18.840 -29.086 -1.472 1.00 151.35 ? 317 HOH   C O   1 
HETATM 2399 O  O   . HOH   L 5 .   ? 35.666 -29.351 5.081  1.00 42.90  ? 318 HOH   C O   1 
HETATM 2400 O  O   . HOH   L 5 .   ? 9.934  -26.267 3.625  1.00 18.38  ? 319 HOH   C O   1 
HETATM 2401 O  O   . HOH   L 5 .   ? 3.922  -23.498 3.820  1.00 35.55  ? 320 HOH   C O   1 
HETATM 2402 O  O   . HOH   L 5 .   ? 23.598 -31.359 15.136 1.00 28.64  ? 321 HOH   C O   1 
HETATM 2403 O  O   . HOH   L 5 .   ? 14.069 -19.704 0.817  1.00 36.90  ? 322 HOH   C O   1 
HETATM 2404 O  O   . HOH   L 5 .   ? 26.521 -23.021 -0.446 1.00 45.14  ? 323 HOH   C O   1 
HETATM 2405 O  O   . HOH   L 5 .   ? 10.558 -12.653 20.511 1.00 17.80  ? 324 HOH   C O   1 
HETATM 2406 O  O   . HOH   L 5 .   ? 22.079 -32.328 3.714  1.00 29.38  ? 325 HOH   C O   1 
HETATM 2407 O  O   . HOH   L 5 .   ? 22.187 -12.489 17.269 1.00 23.95  ? 326 HOH   C O   1 
HETATM 2408 O  O   . HOH   L 5 .   ? 29.332 -28.034 9.792  1.00 26.06  ? 327 HOH   C O   1 
HETATM 2409 O  O   . HOH   L 5 .   ? 27.395 -27.993 2.215  1.00 43.02  ? 328 HOH   C O   1 
HETATM 2410 O  O   . HOH   L 5 .   ? 23.249 -36.282 12.120 1.00 42.90  ? 329 HOH   C O   1 
HETATM 2411 O  O   . HOH   L 5 .   ? 5.292  -25.633 24.725 1.00 31.38  ? 330 HOH   C O   1 
HETATM 2412 O  O   . HOH   L 5 .   ? 10.803 -13.950 5.793  1.00 49.28  ? 331 HOH   C O   1 
HETATM 2413 O  O   . HOH   L 5 .   ? 19.991 -31.879 27.060 1.00 33.36  ? 332 HOH   C O   1 
HETATM 2414 O  O   . HOH   L 5 .   ? 0.866  -31.603 17.084 1.00 17.23  ? 333 HOH   C O   1 
HETATM 2415 O  O   . HOH   L 5 .   ? 6.970  -37.192 29.147 1.00 35.78  ? 334 HOH   C O   1 
HETATM 2416 O  O   . HOH   L 5 .   ? 2.710  -31.310 3.807  1.00 38.29  ? 335 HOH   C O   1 
HETATM 2417 O  O   . HOH   L 5 .   ? 24.159 -12.711 18.886 1.00 41.79  ? 336 HOH   C O   1 
HETATM 2418 O  O   . HOH   L 5 .   ? 0.817  -16.718 18.003 1.00 33.27  ? 337 HOH   C O   1 
HETATM 2419 O  O   . HOH   L 5 .   ? 15.387 -28.962 23.149 1.00 18.73  ? 338 HOH   C O   1 
HETATM 2420 O  O   . HOH   L 5 .   ? 16.117 -18.888 24.113 1.00 24.98  ? 339 HOH   C O   1 
HETATM 2421 O  O   . HOH   L 5 .   ? 30.601 -20.210 18.910 1.00 33.48  ? 340 HOH   C O   1 
HETATM 2422 O  O   . HOH   L 5 .   ? 21.623 -36.829 9.699  1.00 40.96  ? 341 HOH   C O   1 
HETATM 2423 O  O   . HOH   L 5 .   ? 27.545 -15.460 2.472  1.00 43.42  ? 342 HOH   C O   1 
HETATM 2424 O  O   . HOH   L 5 .   ? 34.688 -11.074 10.514 1.00 42.20  ? 343 HOH   C O   1 
HETATM 2425 O  O   . HOH   L 5 .   ? 17.817 -10.088 9.361  1.00 20.27  ? 344 HOH   C O   1 
HETATM 2426 O  O   . HOH   L 5 .   ? 18.206 -11.973 5.389  1.00 41.90  ? 345 HOH   C O   1 
HETATM 2427 O  O   . HOH   L 5 .   ? 11.326 -19.642 11.602 1.00 16.08  ? 346 HOH   C O   1 
HETATM 2428 O  O   . HOH   L 5 .   ? 6.984  -16.576 22.867 1.00 37.05  ? 347 HOH   C O   1 
HETATM 2429 O  O   . HOH   L 5 .   ? 4.938  -30.961 -1.751 1.00 39.99  ? 348 HOH   C O   1 
HETATM 2430 O  O   . HOH   L 5 .   ? 9.918  -40.761 1.142  1.00 46.70  ? 349 HOH   C O   1 
HETATM 2431 O  O   . HOH   L 5 .   ? 8.845  -11.457 18.429 1.00 20.14  ? 350 HOH   C O   1 
HETATM 2432 O  O   . HOH   L 5 .   ? 0.007  -18.963 21.626 1.00 39.23  ? 351 HOH   C O   1 
HETATM 2433 O  O   . HOH   L 5 .   ? 7.320  -39.040 7.348  1.00 43.78  ? 352 HOH   C O   1 
HETATM 2434 O  O   . HOH   L 5 .   ? 18.209 -28.799 22.995 1.00 25.21  ? 353 HOH   C O   1 
HETATM 2435 O  O   . HOH   L 5 .   ? 30.875 -21.405 13.037 1.00 32.35  ? 354 HOH   C O   1 
HETATM 2436 O  O   . HOH   L 5 .   ? 19.471 -22.308 25.323 1.00 29.87  ? 355 HOH   C O   1 
HETATM 2437 O  O   . HOH   L 5 .   ? 18.455 -12.403 16.878 1.00 17.86  ? 356 HOH   C O   1 
HETATM 2438 O  O   . HOH   L 5 .   ? 1.099  -33.873 20.520 1.00 36.78  ? 357 HOH   C O   1 
HETATM 2439 O  O   . HOH   L 5 .   ? 18.252 -10.803 18.854 1.00 36.34  ? 358 HOH   C O   1 
HETATM 2440 O  O   . HOH   L 5 .   ? 11.066 -36.595 31.513 1.00 35.30  ? 359 HOH   C O   1 
HETATM 2441 O  O   . HOH   L 5 .   ? 31.315 -10.753 16.334 1.00 25.22  ? 360 HOH   C O   1 
HETATM 2442 O  O   . HOH   L 5 .   ? 10.583 -27.639 33.526 1.00 44.81  ? 361 HOH   C O   1 
HETATM 2443 O  O   . HOH   L 5 .   ? 12.607 -6.137  22.176 1.00 26.54  ? 362 HOH   C O   1 
HETATM 2444 O  O   . HOH   L 5 .   ? 30.665 -20.477 16.304 1.00 35.31  ? 363 HOH   C O   1 
HETATM 2445 O  O   . HOH   L 5 .   ? 8.340  -28.398 3.014  1.00 21.61  ? 364 HOH   C O   1 
HETATM 2446 O  O   . HOH   L 5 .   ? 20.992 -27.627 -4.052 1.00 60.68  ? 365 HOH   C O   1 
HETATM 2447 O  O   . HOH   L 5 .   ? 21.942 -14.839 23.481 1.00 40.54  ? 366 HOH   C O   1 
HETATM 2448 O  O   . HOH   L 5 .   ? 7.903  -35.066 0.622  1.00 21.25  ? 367 HOH   C O   1 
HETATM 2449 O  O   . HOH   L 5 .   ? 19.269 -27.165 25.621 1.00 37.24  ? 368 HOH   C O   1 
HETATM 2450 O  O   . HOH   L 5 .   ? 7.987  -5.436  14.489 1.00 37.47  ? 369 HOH   C O   1 
HETATM 2451 O  O   . HOH   L 5 .   ? 16.403 -38.605 10.510 1.00 42.28  ? 370 HOH   C O   1 
HETATM 2452 O  O   . HOH   L 5 .   ? 32.660 -16.810 6.647  1.00 42.17  ? 371 HOH   C O   1 
HETATM 2453 O  O   . HOH   L 5 .   ? 14.862 -35.918 17.062 1.00 22.78  ? 372 HOH   C O   1 
HETATM 2454 O  O   . HOH   L 5 .   ? 26.525 -27.302 19.475 1.00 38.19  ? 373 HOH   C O   1 
HETATM 2455 O  O   . HOH   L 5 .   ? 12.969 -20.708 9.465  1.00 15.25  ? 374 HOH   C O   1 
HETATM 2456 O  O   . HOH   L 5 .   ? 8.337  -39.711 24.268 1.00 44.65  ? 375 HOH   C O   1 
HETATM 2457 O  O   . HOH   L 5 .   ? 4.616  -30.763 31.034 1.00 47.36  ? 376 HOH   C O   1 
HETATM 2458 O  O   . HOH   L 5 .   ? 29.527 -26.603 2.826  1.00 39.96  ? 377 HOH   C O   1 
HETATM 2459 O  O   . HOH   L 5 .   ? 26.683 -34.762 12.464 1.00 56.94  ? 378 HOH   C O   1 
HETATM 2460 O  O   . HOH   L 5 .   ? 36.362 -32.302 9.049  1.00 46.40  ? 379 HOH   C O   1 
HETATM 2461 O  O   . HOH   L 5 .   ? 13.211 -12.239 26.829 1.00 37.43  ? 380 HOH   C O   1 
HETATM 2462 O  O   . HOH   L 5 .   ? -0.393 -15.658 14.207 1.00 26.13  ? 381 HOH   C O   1 
HETATM 2463 O  O   . HOH   L 5 .   ? 5.548  -29.206 7.359  1.00 16.42  ? 382 HOH   C O   1 
HETATM 2464 O  O   . HOH   L 5 .   ? 10.184 -16.433 27.000 1.00 43.95  ? 383 HOH   C O   1 
HETATM 2465 O  O   . HOH   L 5 .   ? 14.322 -22.673 30.268 1.00 30.62  ? 384 HOH   C O   1 
HETATM 2466 O  O   . HOH   L 5 .   ? 3.727  -36.306 6.901  1.00 26.96  ? 385 HOH   C O   1 
HETATM 2467 O  O   . HOH   L 5 .   ? 18.160 -18.561 1.479  1.00 45.61  ? 386 HOH   C O   1 
HETATM 2468 O  O   . HOH   L 5 .   ? 1.657  -17.821 6.391  1.00 32.74  ? 387 HOH   C O   1 
HETATM 2469 O  O   . HOH   L 5 .   ? 6.188  -8.469  11.507 1.00 35.45  ? 388 HOH   C O   1 
HETATM 2470 O  O   . HOH   L 5 .   ? 5.673  -32.912 24.502 1.00 23.73  ? 389 HOH   C O   1 
HETATM 2471 O  O   . HOH   L 5 .   ? 13.542 -37.233 32.196 1.00 39.96  ? 390 HOH   C O   1 
HETATM 2472 O  O   . HOH   L 5 .   ? 6.487  -18.404 5.892  1.00 22.86  ? 391 HOH   C O   1 
HETATM 2473 O  O   . HOH   L 5 .   ? 16.743 -8.480  16.933 1.00 39.96  ? 392 HOH   C O   1 
HETATM 2474 O  O   . HOH   L 5 .   ? -2.191 -30.383 8.521  1.00 24.66  ? 393 HOH   C O   1 
HETATM 2475 O  O   . HOH   L 5 .   ? 7.912  -24.519 34.325 1.00 53.98  ? 394 HOH   C O   1 
HETATM 2476 O  O   . HOH   L 5 .   ? -3.392 -18.879 27.549 1.00 32.20  ? 395 HOH   C O   1 
HETATM 2477 O  O   . HOH   L 5 .   ? 9.512  -10.105 11.089 1.00 42.48  ? 396 HOH   C O   1 
HETATM 2478 O  O   . HOH   L 5 .   ? 31.204 -28.777 11.625 1.00 35.78  ? 397 HOH   C O   1 
HETATM 2479 O  O   . HOH   L 5 .   ? 28.790 -33.297 12.447 1.00 42.43  ? 398 HOH   C O   1 
HETATM 2480 O  O   . HOH   L 5 .   ? 16.699 -13.931 3.993  1.00 49.61  ? 399 HOH   C O   1 
HETATM 2481 O  O   . HOH   L 5 .   ? 16.692 -22.122 -1.761 1.00 40.25  ? 400 HOH   C O   1 
HETATM 2482 O  O   . HOH   L 5 .   ? 0.748  -29.562 25.015 1.00 43.77  ? 401 HOH   C O   1 
HETATM 2483 O  O   . HOH   L 5 .   ? 16.551 -7.834  14.501 1.00 40.13  ? 402 HOH   C O   1 
HETATM 2484 O  O   . HOH   L 5 .   ? 26.423 -33.104 13.947 1.00 36.30  ? 403 HOH   C O   1 
HETATM 2485 O  O   . HOH   L 5 .   ? 14.226 -16.652 3.783  1.00 31.11  ? 404 HOH   C O   1 
HETATM 2486 O  O   . HOH   L 5 .   ? 10.918 -36.012 -0.476 1.00 34.51  ? 405 HOH   C O   1 
HETATM 2487 O  O   . HOH   L 5 .   ? 15.123 -35.677 1.662  1.00 22.31  ? 406 HOH   C O   1 
HETATM 2488 O  O   . HOH   L 5 .   ? 10.688 -15.304 3.478  1.00 46.93  ? 407 HOH   C O   1 
HETATM 2489 O  O   . HOH   L 5 .   ? 4.216  -8.389  22.654 1.00 34.48  ? 408 HOH   C O   1 
HETATM 2490 O  O   . HOH   L 5 .   ? 8.725  -38.714 9.599  1.00 29.85  ? 409 HOH   C O   1 
HETATM 2491 O  O   . HOH   L 5 .   ? 30.575 -9.225  18.194 1.00 46.91  ? 410 HOH   C O   1 
HETATM 2492 O  O   . HOH   L 5 .   ? 8.057  -14.210 23.236 1.00 33.62  ? 411 HOH   C O   1 
HETATM 2493 O  O   . HOH   L 5 .   ? 19.394 -7.559  15.111 1.00 21.89  ? 412 HOH   C O   1 
HETATM 2494 O  O   . HOH   L 5 .   ? 5.764  -33.112 29.616 1.00 54.58  ? 413 HOH   C O   1 
HETATM 2495 O  O   . HOH   L 5 .   ? 24.976 -23.875 19.988 1.00 30.85  ? 414 HOH   C O   1 
HETATM 2496 O  O   . HOH   L 5 .   ? 31.417 -22.164 4.707  1.00 41.57  ? 415 HOH   C O   1 
HETATM 2497 O  O   . HOH   L 5 .   ? 4.035  -24.307 26.697 1.00 30.42  ? 416 HOH   C O   1 
HETATM 2498 O  O   . HOH   L 5 .   ? 12.083 -9.901  12.457 1.00 31.20  ? 417 HOH   C O   1 
HETATM 2499 O  O   . HOH   L 5 .   ? 20.825 -11.963 21.202 1.00 39.76  ? 418 HOH   C O   1 
HETATM 2500 O  O   . HOH   L 5 .   ? 29.393 -14.964 22.492 1.00 40.84  ? 419 HOH   C O   1 
HETATM 2501 O  O   . HOH   L 5 .   ? 31.101 -15.787 4.617  1.00 67.86  ? 420 HOH   C O   1 
HETATM 2502 O  O   . HOH   L 5 .   ? 22.387 -12.316 5.618  1.00 27.47  ? 421 HOH   C O   1 
HETATM 2503 O  O   . HOH   L 5 .   ? 24.123 -29.142 18.880 1.00 31.34  ? 422 HOH   C O   1 
HETATM 2504 O  O   . HOH   L 5 .   ? 1.302  -34.446 17.855 1.00 24.30  ? 423 HOH   C O   1 
HETATM 2505 O  O   . HOH   L 5 .   ? 22.532 -13.133 19.752 1.00 56.67  ? 424 HOH   C O   1 
HETATM 2506 O  O   . HOH   L 5 .   ? 4.558  -15.679 21.430 1.00 38.26  ? 425 HOH   C O   1 
HETATM 2507 O  O   . HOH   L 5 .   ? 31.391 -26.208 -2.854 1.00 66.16  ? 426 HOH   C O   1 
HETATM 2508 O  O   . HOH   L 5 .   ? 13.876 -25.385 28.621 1.00 186.02 ? 427 HOH   C O   1 
HETATM 2509 O  O   . HOH   L 5 .   ? 32.226 -16.679 20.569 1.00 25.99  ? 428 HOH   C O   1 
HETATM 2510 O  O   . HOH   L 5 .   ? 28.091 -9.860  18.585 1.00 50.34  ? 429 HOH   C O   1 
HETATM 2511 O  O   . HOH   L 5 .   ? -0.560 -35.879 16.659 1.00 37.66  ? 430 HOH   C O   1 
HETATM 2512 O  O   . HOH   L 5 .   ? 16.590 -14.280 29.686 1.00 70.76  ? 431 HOH   C O   1 
HETATM 2513 O  O   . HOH   L 5 .   ? 0.787  -15.531 23.518 1.00 62.09  ? 432 HOH   C O   1 
HETATM 2514 O  O   . HOH   L 5 .   ? 22.444 -22.590 20.727 1.00 22.86  ? 433 HOH   C O   1 
HETATM 2515 O  O   . HOH   L 5 .   ? 4.270  -20.631 19.549 1.00 45.11  ? 434 HOH   C O   1 
HETATM 2516 O  O   . HOH   L 5 .   ? 16.332 -20.464 0.234  1.00 46.33  ? 435 HOH   C O   1 
HETATM 2517 O  O   . HOH   L 5 .   ? 17.064 -34.508 17.810 1.00 37.44  ? 436 HOH   C O   1 
HETATM 2518 O  O   . HOH   L 5 .   ? 19.508 -24.385 27.953 1.00 41.67  ? 437 HOH   C O   1 
HETATM 2519 O  O   . HOH   L 5 .   ? 32.835 -9.115  19.773 1.00 59.28  ? 438 HOH   C O   1 
HETATM 2520 O  O   . HOH   L 5 .   ? 2.570  -19.891 21.417 1.00 59.43  ? 439 HOH   C O   1 
HETATM 2521 O  O   . HOH   L 5 .   ? 20.077 -8.732  17.486 1.00 40.17  ? 440 HOH   C O   1 
HETATM 2522 O  O   . HOH   L 5 .   ? 7.012  -36.523 2.925  1.00 28.22  ? 441 HOH   C O   1 
HETATM 2523 O  O   . HOH   L 5 .   ? 4.967  -29.157 4.801  1.00 40.87  ? 442 HOH   C O   1 
HETATM 2524 O  O   . HOH   L 5 .   ? 19.218 -22.114 -2.424 1.00 42.51  ? 443 HOH   C O   1 
HETATM 2525 O  O   . HOH   L 5 .   ? 6.834  -23.625 30.229 1.00 69.80  ? 444 HOH   C O   1 
HETATM 2526 O  O   . HOH   L 5 .   ? -0.748 -7.403  14.525 1.00 39.69  ? 445 HOH   C O   1 
HETATM 2527 O  O   . HOH   L 5 .   ? 4.095  -18.101 19.088 1.00 56.56  ? 446 HOH   C O   1 
HETATM 2528 O  O   . HOH   L 5 .   ? 17.540 -39.028 24.618 1.00 44.68  ? 447 HOH   C O   1 
HETATM 2529 O  O   . HOH   L 5 .   ? 12.321 -39.356 12.880 1.00 38.54  ? 448 HOH   C O   1 
HETATM 2530 O  O   . HOH   L 5 .   ? 12.552 -7.716  14.040 1.00 40.04  ? 449 HOH   C O   1 
HETATM 2531 O  O   . HOH   L 5 .   ? 13.677 -42.130 3.782  1.00 53.24  ? 450 HOH   C O   1 
HETATM 2532 O  O   . HOH   L 5 .   ? 2.037  -34.297 4.129  1.00 62.14  ? 451 HOH   C O   1 
HETATM 2533 O  O   . HOH   L 5 .   ? 8.652  -8.273  26.809 1.00 45.93  ? 452 HOH   C O   1 
HETATM 2534 O  O   . HOH   L 5 .   ? 21.228 -10.437 17.800 1.00 53.91  ? 453 HOH   C O   1 
HETATM 2535 O  O   . HOH   L 5 .   ? 12.452 -16.811 1.485  1.00 55.84  ? 454 HOH   C O   1 
HETATM 2536 O  O   . HOH   L 5 .   ? 30.846 -31.027 13.289 1.00 46.96  ? 455 HOH   C O   1 
HETATM 2537 O  O   . HOH   L 5 .   ? 2.495  -29.172 27.300 1.00 39.61  ? 456 HOH   C O   1 
HETATM 2538 O  O   . HOH   L 5 .   ? -0.652 -35.015 10.064 1.00 79.21  ? 457 HOH   C O   1 
HETATM 2539 O  O   . HOH   L 5 .   ? 24.395 -16.144 23.749 1.00 65.86  ? 458 HOH   C O   1 
HETATM 2540 O  O   . HOH   L 5 .   ? 16.117 -17.616 2.026  1.00 48.71  ? 459 HOH   C O   1 
HETATM 2541 O  O   . HOH   L 5 .   ? 8.629  -23.855 2.716  1.00 37.44  ? 460 HOH   C O   1 
HETATM 2542 O  O   . HOH   L 5 .   ? 32.476 -19.358 20.845 1.00 35.34  ? 461 HOH   C O   1 
HETATM 2543 O  O   . HOH   L 5 .   ? 32.989 -9.461  11.703 1.00 40.54  ? 462 HOH   C O   1 
HETATM 2544 O  O   . HOH   L 5 .   ? 32.942 -9.459  14.360 1.00 31.17  ? 463 HOH   C O   1 
HETATM 2545 O  O   . HOH   L 5 .   ? 15.725 -40.145 2.653  1.00 53.65  ? 464 HOH   C O   1 
HETATM 2546 O  O   . HOH   L 5 .   ? 10.532 -14.096 26.263 1.00 45.83  ? 465 HOH   C O   1 
HETATM 2547 O  O   . HOH   L 5 .   ? 31.949 -27.272 13.739 1.00 40.19  ? 466 HOH   C O   1 
HETATM 2548 O  O   . HOH   L 5 .   ? 31.818 -36.226 12.186 1.00 40.06  ? 467 HOH   C O   1 
HETATM 2549 O  O   . HOH   L 5 .   ? 29.719 -8.574  9.076  1.00 43.43  ? 468 HOH   C O   1 
HETATM 2550 O  O   . HOH   L 5 .   ? 20.595 -19.630 -2.970 1.00 46.42  ? 469 HOH   C O   1 
HETATM 2551 O  O   . HOH   L 5 .   ? 5.382  -39.756 23.318 1.00 37.05  ? 470 HOH   C O   1 
HETATM 2552 O  O   . HOH   L 5 .   ? 26.129 -32.673 16.446 1.00 64.89  ? 471 HOH   C O   1 
HETATM 2553 O  O   . HOH   L 5 .   ? 7.440  -40.248 26.819 1.00 166.74 ? 472 HOH   C O   1 
HETATM 2554 O  O   . HOH   L 5 .   ? 0.517  -19.492 18.413 1.00 53.31  ? 473 HOH   C O   1 
HETATM 2555 O  O   . HOH   L 5 .   ? 35.629 -9.642  8.148  1.00 67.84  ? 474 HOH   C O   1 
HETATM 2556 O  O   . HOH   L 5 .   ? 35.578 -10.159 15.435 1.00 34.63  ? 475 HOH   C O   1 
HETATM 2557 O  O   . HOH   L 5 .   ? 6.405  -3.926  11.298 1.00 60.51  ? 476 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   ? 0.2605 0.2485 0.2652 0.0050  -0.0056 0.0165  7   SER   A N   
2    C CA  . SER   A 1   ? 0.2587 0.2481 0.2739 0.0027  -0.0080 0.0149  7   SER   A CA  
3    C C   . SER   A 1   ? 0.2586 0.2477 0.2774 0.0000  -0.0079 0.0107  7   SER   A C   
4    O O   . SER   A 1   ? 0.2711 0.2583 0.2831 0.0004  -0.0079 0.0085  7   SER   A O   
5    C CB  . SER   A 1   ? 0.2973 0.2874 0.3121 0.0048  -0.0142 0.0151  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3485 0.3374 0.3560 0.0059  -0.0187 0.0114  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2383 0.2287 0.2672 -0.0022 -0.0072 0.0100  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2239 0.2133 0.2564 -0.0042 -0.0060 0.0071  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2114 0.2019 0.2524 -0.0056 -0.0022 0.0075  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2202 0.2117 0.2629 -0.0052 0.0001  0.0091  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1861 0.1757 0.2323 -0.0071 -0.0010 0.0060  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1887 0.1790 0.2414 -0.0076 0.0033  0.0065  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1933 0.1805 0.2454 -0.0082 0.0068  0.0056  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2002 0.1850 0.2508 -0.0091 0.0051  0.0044  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1918 0.1851 0.2558 -0.0083 0.0019  0.0073  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1711 0.1577 0.2237 -0.0072 0.0117  0.0061  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1761 0.1593 0.2281 -0.0069 0.0164  0.0065  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1801 0.1649 0.2439 -0.0080 0.0192  0.0076  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1794 0.1671 0.2474 -0.0072 0.0200  0.0079  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1784 0.1601 0.2215 -0.0037 0.0200  0.0063  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1811 0.1630 0.2150 -0.0025 0.0170  0.0049  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1963 0.1734 0.2364 -0.0022 0.0255  0.0077  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1959 0.1785 0.2238 0.0005  0.0186  0.0036  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1880 0.1707 0.2583 -0.0098 0.0215  0.0082  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1987 0.1836 0.2826 -0.0110 0.0253  0.0096  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2020 0.1821 0.2837 -0.0096 0.0337  0.0120  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2146 0.1903 0.2965 -0.0110 0.0352  0.0125  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2009 0.1882 0.2981 -0.0147 0.0208  0.0081  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2189 0.2110 0.3174 -0.0149 0.0127  0.0064  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2349 0.2325 0.3428 -0.0143 0.0116  0.0070  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2508 0.2416 0.3402 -0.0147 0.0066  0.0045  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2467 0.2479 0.3545 -0.0135 0.0046  0.0063  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2652 0.2597 0.3536 -0.0138 0.0000  0.0038  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2728 0.2722 0.3703 -0.0132 -0.0011 0.0049  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3102 0.3124 0.4058 -0.0114 -0.0072 0.0051  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2038 0.1838 0.2819 -0.0064 0.0392  0.0134  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2152 0.1901 0.2879 -0.0035 0.0478  0.0163  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2303 0.2075 0.3120 -0.0024 0.0544  0.0182  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2416 0.2226 0.3237 -0.0008 0.0532  0.0168  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2368 0.2085 0.2908 0.0014  0.0480  0.0156  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2349 0.2108 0.2852 0.0031  0.0439  0.0126  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2572 0.2234 0.3029 0.0061  0.0568  0.0189  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2352 0.2103 0.3266 -0.0037 0.0617  0.0215  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2347 0.2124 0.3364 -0.0025 0.0692  0.0238  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2343 0.2202 0.3513 -0.0053 0.0636  0.0213  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2281 0.2173 0.3546 -0.0096 0.0563  0.0193  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2367 0.2256 0.3535 -0.0020 0.0660  0.0210  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2363 0.2324 0.3663 -0.0035 0.0606  0.0190  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2193 0.2158 0.3383 -0.0019 0.0531  0.0159  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2208 0.2209 0.3452 -0.0006 0.0517  0.0149  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2726 0.2723 0.4143 -0.0014 0.0682  0.0208  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3605 0.3617 0.5192 -0.0044 0.0748  0.0238  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3911 0.3974 0.5668 -0.0091 0.0697  0.0228  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3863 0.3828 0.5404 -0.0015 0.0861  0.0275  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1994 0.1922 0.3048 -0.0022 0.0486  0.0146  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1912 0.1841 0.2874 -0.0012 0.0423  0.0120  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1694 0.1629 0.2641 -0.0043 0.0344  0.0111  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1677 0.1589 0.2610 -0.0062 0.0341  0.0116  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2066 0.1949 0.2858 0.0026  0.0447  0.0107  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2249 0.2119 0.3013 0.0071  0.0518  0.0108  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2391 0.2288 0.3230 0.0084  0.0525  0.0097  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2464 0.2287 0.3115 0.0109  0.0581  0.0121  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2596 0.2476 0.3395 0.0132  0.0592  0.0091  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2645 0.2452 0.3245 0.0161  0.0648  0.0119  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2862 0.2698 0.3538 0.0171  0.0654  0.0102  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3213 0.3030 0.3831 0.0228  0.0720  0.0095  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1527 0.1482 0.2464 -0.0043 0.0286  0.0098  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1494 0.1451 0.2388 -0.0061 0.0219  0.0092  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1617 0.1555 0.2405 -0.0043 0.0209  0.0079  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1695 0.1640 0.2506 -0.0029 0.0216  0.0074  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1588 0.1589 0.2586 -0.0072 0.0164  0.0096  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2029 0.2028 0.2960 -0.0074 0.0099  0.0095  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1994 0.2033 0.3009 -0.0074 0.0041  0.0101  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2361 0.2396 0.3321 -0.0056 0.0006  0.0116  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2833 0.2862 0.3717 -0.0051 -0.0042 0.0120  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2977 0.3000 0.3825 -0.0064 -0.0069 0.0100  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2665 0.2683 0.3502 -0.0030 -0.0058 0.0144  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1610 0.1525 0.2295 -0.0043 0.0197  0.0071  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1648 0.1555 0.2256 -0.0031 0.0186  0.0055  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1769 0.1686 0.2363 -0.0045 0.0139  0.0062  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1734 0.1645 0.2294 -0.0054 0.0119  0.0066  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1725 0.1608 0.2230 -0.0012 0.0207  0.0041  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1687 0.1577 0.2143 0.0001  0.0193  0.0014  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1674 0.1536 0.2167 0.0010  0.0262  0.0045  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1656 0.1581 0.2271 -0.0043 0.0127  0.0065  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1731 0.1660 0.2324 -0.0049 0.0095  0.0082  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1624 0.1548 0.2201 -0.0047 0.0105  0.0074  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1644 0.1565 0.2249 -0.0042 0.0125  0.0051  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1796 0.1736 0.2452 -0.0048 0.0070  0.0108  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2081 0.2036 0.2769 -0.0053 0.0046  0.0109  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1804 0.1744 0.2539 -0.0040 0.0090  0.0110  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1558 0.1483 0.2103 -0.0050 0.0093  0.0093  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1499 0.1422 0.2067 -0.0054 0.0109  0.0093  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1583 0.1491 0.2232 -0.0053 0.0117  0.0108  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1649 0.1551 0.2312 -0.0045 0.0102  0.0142  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1513 0.1436 0.2039 -0.0053 0.0107  0.0124  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1830 0.1765 0.2281 -0.0049 0.0103  0.0108  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1933 0.1862 0.2325 -0.0042 0.0083  0.0114  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1891 0.1844 0.2352 -0.0053 0.0119  0.0084  19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1518 0.1418 0.2222 -0.0058 0.0135  0.0080  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1450 0.1325 0.2236 -0.0055 0.0146  0.0090  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1602 0.1456 0.2405 -0.0053 0.0149  0.0149  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1759 0.1597 0.2596 -0.0038 0.0144  0.0179  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1518 0.1383 0.2359 -0.0062 0.0161  0.0041  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1586 0.1416 0.2508 -0.0054 0.0173  0.0037  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1762 0.1576 0.2741 -0.0065 0.0181  -0.0019 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1862 0.1635 0.2920 -0.0056 0.0194  -0.0038 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2022 0.1750 0.3162 -0.0063 0.0211  -0.0006 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1960 0.1681 0.3106 -0.0076 0.0221  0.0054  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1966 0.1650 0.3179 -0.0052 0.0223  -0.0032 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1642 0.1498 0.2410 -0.0060 0.0159  0.0169  21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1773 0.1601 0.2540 -0.0050 0.0174  0.0233  21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1965 0.1796 0.2654 -0.0022 0.0142  0.0273  21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2245 0.2049 0.2920 0.0001  0.0147  0.0329  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1878 0.1707 0.2641 -0.0063 0.0207  0.0247  21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1915 0.1775 0.2580 -0.0057 0.0196  0.0246  21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2013 0.1910 0.2662 -0.0069 0.0183  0.0191  21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2138 0.1993 0.2712 -0.0035 0.0198  0.0292  21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2171 0.2082 0.2731 -0.0057 0.0180  0.0205  21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2257 0.2143 0.2765 -0.0036 0.0187  0.0262  21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1896 0.1759 0.2540 -0.0021 0.0107  0.0244  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1945 0.1819 0.2534 0.0002  0.0064  0.0264  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1961 0.1852 0.2619 0.0006  0.0039  0.0249  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.1931 0.1843 0.2572 0.0021  -0.0005 0.0253  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1960 0.1852 0.2459 -0.0001 0.0045  0.0242  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2118 0.2000 0.2546 0.0002  0.0072  0.0260  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2205 0.2100 0.2546 0.0004  0.0050  0.0233  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2168 0.2023 0.2552 0.0033  0.0082  0.0322  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1876 0.1763 0.2617 -0.0005 0.0064  0.0227  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1818 0.1727 0.2633 0.0002  0.0052  0.0214  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1885 0.1796 0.2735 0.0032  0.0022  0.0255  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.1826 0.1702 0.2666 0.0049  0.0032  0.0294  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1809 0.1705 0.2691 -0.0004 0.0090  0.0184  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1974 0.1925 0.2870 0.0041  -0.0014 0.0248  24  THR   A N   
135  C CA  . THR   A 18  ? 0.2172 0.2140 0.3109 0.0077  -0.0055 0.0280  24  THR   A CA  
136  C C   . THR   A 18  ? 0.2222 0.2189 0.3275 0.0092  -0.0032 0.0285  24  THR   A C   
137  O O   . THR   A 18  ? 0.2080 0.2037 0.3176 0.0073  0.0015  0.0256  24  THR   A O   
138  C CB  . THR   A 18  ? 0.2376 0.2400 0.3331 0.0077  -0.0114 0.0258  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2417 0.2475 0.3476 0.0053  -0.0092 0.0223  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2525 0.2544 0.3367 0.0065  -0.0137 0.0244  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2366 0.2347 0.3467 0.0133  -0.0068 0.0318  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2598 0.2585 0.3819 0.0153  -0.0049 0.0321  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2278 0.2320 0.3596 0.0131  -0.0034 0.0275  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2262 0.2292 0.3645 0.0131  0.0016  0.0258  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3197 0.3205 0.4456 0.0207  -0.0102 0.0363  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4400 0.4347 0.5561 0.0242  -0.0110 0.0421  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4906 0.4773 0.6054 0.0240  -0.0049 0.0448  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4806 0.4760 0.5881 0.0283  -0.0168 0.0458  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.5105 0.4929 0.6164 0.0277  -0.0061 0.0509  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.5102 0.4977 0.6102 0.0309  -0.0133 0.0518  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2264 0.2361 0.3588 0.0114  -0.0072 0.0255  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2148 0.2293 0.3573 0.0092  -0.0047 0.0220  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1931 0.2038 0.3304 0.0062  0.0022  0.0194  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1892 0.2011 0.3337 0.0062  0.0072  0.0177  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2414 0.2618 0.3873 0.0076  -0.0102 0.0202  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3176 0.3448 0.4756 0.0106  -0.0165 0.0209  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3264 0.3565 0.4964 0.0130  -0.0145 0.0218  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3335 0.3636 0.4883 0.0112  -0.0245 0.0202  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1782 0.1845 0.3028 0.0044  0.0026  0.0190  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1629 0.1658 0.2817 0.0026  0.0081  0.0163  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1672 0.1669 0.2894 0.0044  0.0125  0.0155  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1782 0.1775 0.3015 0.0046  0.0172  0.0128  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1519 0.1512 0.2582 0.0011  0.0070  0.0163  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2107 0.2119 0.3118 -0.0007 0.0041  0.0157  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2194 0.2229 0.3248 -0.0020 0.0052  0.0140  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2208 0.2205 0.3135 -0.0008 0.0011  0.0169  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1678 0.1643 0.2909 0.0062  0.0113  0.0179  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1777 0.1701 0.3047 0.0078  0.0152  0.0165  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1989 0.1942 0.3369 0.0105  0.0174  0.0160  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2081 0.2009 0.3479 0.0117  0.0219  0.0128  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1783 0.1657 0.3048 0.0089  0.0140  0.0199  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1972 0.1806 0.3157 0.0063  0.0149  0.0191  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2116 0.1948 0.3228 0.0052  0.0126  0.0220  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1978 0.1772 0.3157 0.0049  0.0181  0.0146  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2137 0.1937 0.3213 0.0028  0.0149  0.0201  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2123 0.1902 0.3244 0.0024  0.0177  0.0152  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2095 0.1869 0.3309 0.0058  0.0211  0.0095  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2194 0.1945 0.3315 0.0005  0.0196  0.0107  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2215 0.1954 0.3413 0.0043  0.0225  0.0048  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2232 0.1965 0.3390 0.0014  0.0214  0.0052  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2014 0.2024 0.3471 0.0117  0.0141  0.0185  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2069 0.2123 0.3655 0.0142  0.0165  0.0182  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2120 0.2202 0.3723 0.0128  0.0217  0.0152  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2178 0.2287 0.3877 0.0151  0.0261  0.0145  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2141 0.2259 0.3819 0.0159  0.0106  0.0212  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1962 0.2042 0.3477 0.0096  0.0216  0.0140  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2020 0.2113 0.3532 0.0086  0.0271  0.0122  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1995 0.2028 0.3359 0.0081  0.0299  0.0095  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1869 0.1899 0.3173 0.0067  0.0322  0.0089  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2204 0.2347 0.3759 0.0056  0.0243  0.0133  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2659 0.2875 0.4381 0.0063  0.0212  0.0148  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2643 0.2898 0.4486 0.0075  0.0261  0.0148  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2726 0.2964 0.4457 0.0062  0.0130  0.0160  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1926 0.1910 0.3240 0.0094  0.0296  0.0078  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1998 0.1934 0.3190 0.0091  0.0307  0.0044  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1991 0.1916 0.3128 0.0114  0.0366  0.0013  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2047 0.1974 0.3236 0.0145  0.0411  0.0005  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2069 0.1960 0.3266 0.0099  0.0294  0.0028  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2142 0.1989 0.3245 0.0095  0.0296  -0.0020 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2232 0.2089 0.3260 0.0064  0.0262  -0.0011 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2115 0.1914 0.3264 0.0101  0.0289  -0.0040 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1948 0.1859 0.2972 0.0106  0.0367  -0.0001 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2131 0.2021 0.3063 0.0138  0.0418  -0.0028 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2268 0.2119 0.3100 0.0151  0.0394  -0.0082 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2441 0.2265 0.3228 0.0190  0.0419  -0.0126 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2251 0.2151 0.3130 0.0127  0.0438  -0.0002 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2422 0.2289 0.3170 0.0170  0.0487  -0.0025 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2251 0.2192 0.3255 0.0113  0.0466  0.0040  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2067 0.1920 0.2873 0.0119  0.0342  -0.0082 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2153 0.1983 0.2893 0.0123  0.0314  -0.0135 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1958 0.1798 0.2728 0.0082  0.0267  -0.0118 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1972 0.1833 0.2745 0.0058  0.0256  -0.0074 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2343 0.2170 0.2950 0.0150  0.0326  -0.0156 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2457 0.2279 0.2997 0.0155  0.0284  -0.0211 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2654 0.2458 0.3161 0.0186  0.0271  -0.0281 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2402 0.2245 0.2906 0.0133  0.0248  -0.0204 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2684 0.2503 0.3154 0.0179  0.0223  -0.0321 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2506 0.2350 0.2975 0.0147  0.0212  -0.0271 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2339 0.2200 0.2846 0.0102  0.0239  -0.0154 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2560 0.2430 0.3000 0.0135  0.0174  -0.0283 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2452 0.2330 0.2916 0.0092  0.0206  -0.0165 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2539 0.2425 0.2976 0.0108  0.0175  -0.0226 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1914 0.1735 0.2707 0.0073  0.0244  -0.0156 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1900 0.1729 0.2718 0.0037  0.0212  -0.0139 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1875 0.1696 0.2691 0.0034  0.0190  -0.0203 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1930 0.1728 0.2758 0.0056  0.0193  -0.0261 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1960 0.1778 0.2872 0.0017  0.0209  -0.0089 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2146 0.1925 0.3141 0.0031  0.0225  -0.0105 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2509 0.2252 0.3551 0.0021  0.0217  -0.0155 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3154 0.2862 0.4233 0.0041  0.0229  -0.0201 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2345 0.2095 0.3396 -0.0008 0.0201  -0.0152 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1823 0.1667 0.2633 0.0009  0.0167  -0.0198 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1839 0.1689 0.2678 0.0001  0.0143  -0.0260 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1876 0.1740 0.2783 -0.0039 0.0138  -0.0224 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1814 0.1709 0.2670 -0.0046 0.0133  -0.0193 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2235 0.2114 0.2968 0.0033  0.0122  -0.0308 35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3167 0.3064 0.3933 0.0035  0.0084  -0.0390 35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3422 0.3322 0.4306 -0.0004 0.0076  -0.0398 35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3279 0.3189 0.3953 0.0077  0.0063  -0.0445 35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2000 0.1833 0.3021 -0.0063 0.0147  -0.0225 36  SER   A N   
241  C CA  A SER   A 30  ? 0.2106 0.1944 0.3199 -0.0097 0.0158  -0.0184 36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2068 0.1907 0.3158 -0.0097 0.0158  -0.0182 36  SER   A CA  
243  C C   . SER   A 30  ? 0.2056 0.1945 0.3155 -0.0110 0.0137  -0.0224 36  SER   A C   
244  O O   . SER   A 30  ? 0.2145 0.2060 0.3245 -0.0126 0.0149  -0.0178 36  SER   A O   
245  C CB  A SER   A 30  ? 0.2330 0.2113 0.3553 -0.0117 0.0179  -0.0183 36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2187 0.1972 0.3406 -0.0118 0.0180  -0.0174 36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2660 0.2442 0.3965 -0.0150 0.0201  -0.0144 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2324 0.2100 0.3624 -0.0125 0.0164  -0.0261 36  SER   A OG  
249  N N   . SER   A 31  ? 0.1975 0.1885 0.3075 -0.0096 0.0104  -0.0312 37  SER   A N   
250  C CA  . SER   A 31  ? 0.2153 0.2124 0.3270 -0.0102 0.0075  -0.0356 37  SER   A CA  
251  C C   . SER   A 31  ? 0.2087 0.2099 0.3077 -0.0080 0.0069  -0.0323 37  SER   A C   
252  O O   . SER   A 31  ? 0.2193 0.2255 0.3204 -0.0086 0.0056  -0.0334 37  SER   A O   
253  C CB  . SER   A 31  ? 0.2559 0.2548 0.3700 -0.0083 0.0029  -0.0464 37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3184 0.3174 0.4172 -0.0030 0.0010  -0.0490 37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1833 0.1821 0.2707 -0.0055 0.0081  -0.0283 38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1729 0.1741 0.2489 -0.0035 0.0079  -0.0251 38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1732 0.1728 0.2474 -0.0053 0.0106  -0.0169 38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1646 0.1655 0.2305 -0.0042 0.0105  -0.0143 38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1848 0.1841 0.2491 0.0007  0.0077  -0.0267 38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1957 0.1965 0.2570 0.0043  0.0045  -0.0349 38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1949 0.1933 0.2430 0.0095  0.0055  -0.0354 38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1903 0.1891 0.2282 0.0113  0.0067  -0.0309 38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2248 0.2221 0.2500 0.0165  0.0074  -0.0314 38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2310 0.2270 0.2505 0.0211  0.0067  -0.0366 38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2011 0.1978 0.2187 0.0177  0.0088  -0.0269 38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1645 0.1608 0.2457 -0.0075 0.0127  -0.0130 39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1563 0.1509 0.2347 -0.0081 0.0143  -0.0058 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1639 0.1577 0.2337 -0.0061 0.0137  -0.0043 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1696 0.1637 0.2341 -0.0060 0.0134  -0.0004 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1755 0.1725 0.2520 -0.0090 0.0150  -0.0024 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1786 0.1734 0.2507 -0.0088 0.0161  0.0044  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1836 0.1752 0.2595 -0.0089 0.0169  0.0075  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1792 0.1754 0.2436 -0.0080 0.0156  0.0064  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1554 0.1480 0.2245 -0.0043 0.0138  -0.0074 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1519 0.1438 0.2154 -0.0027 0.0145  -0.0057 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1569 0.1467 0.2261 -0.0021 0.0160  -0.0047 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1670 0.1552 0.2412 -0.0016 0.0166  -0.0077 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1593 0.1517 0.2149 0.0001  0.0147  -0.0095 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1748 0.1691 0.2231 0.0008  0.0134  -0.0098 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1960 0.1897 0.2353 0.0047  0.0140  -0.0127 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1691 0.1630 0.2148 -0.0006 0.0135  -0.0050 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1435 0.1336 0.2124 -0.0020 0.0164  -0.0012 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1403 0.1297 0.2153 -0.0009 0.0180  -0.0001 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1516 0.1421 0.2243 -0.0003 0.0194  0.0013  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1541 0.1456 0.2235 -0.0016 0.0178  0.0032  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1469 0.1359 0.2290 -0.0018 0.0166  0.0039  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1651 0.1539 0.2552 -0.0002 0.0179  0.0050  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1934 0.1799 0.2900 0.0000  0.0173  0.0073  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1539 0.1460 0.2463 -0.0003 0.0166  0.0080  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1524 0.1427 0.2278 0.0017  0.0228  0.0003  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1572 0.1484 0.2332 0.0021  0.0256  0.0021  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1621 0.1551 0.2494 0.0026  0.0271  0.0038  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1742 0.1661 0.2646 0.0047  0.0289  0.0021  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1779 0.1671 0.2453 0.0051  0.0299  -0.0001 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1778 0.1672 0.2477 0.0055  0.0346  0.0028  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1856 0.1737 0.2423 0.0054  0.0277  -0.0019 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1580 0.1538 0.2521 0.0009  0.0261  0.0066  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1662 0.1653 0.2732 0.0015  0.0270  0.0081  43  SER   A CA  
299  C C   . SER   A 37  ? 0.1897 0.1908 0.3023 0.0010  0.0312  0.0093  43  SER   A C   
300  O O   . SER   A 37  ? 0.1823 0.1818 0.2890 -0.0004 0.0322  0.0095  43  SER   A O   
301  C CB  . SER   A 37  ? 0.1827 0.1844 0.2958 0.0003  0.0209  0.0102  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2054 0.2084 0.3163 -0.0021 0.0170  0.0109  43  SER   A OG  
303  N N   . SER   A 38  ? 0.1946 0.1991 0.3196 0.0021  0.0343  0.0103  44  SER   A N   
304  C CA  . SER   A 38  ? 0.1975 0.2043 0.3310 0.0013  0.0395  0.0118  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2104 0.2224 0.3568 -0.0021 0.0346  0.0128  44  SER   A C   
306  O O   . SER   A 38  ? 0.2155 0.2307 0.3671 -0.0024 0.0278  0.0127  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2161 0.2243 0.3571 0.0047  0.0467  0.0121  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2492 0.2613 0.4009 0.0056  0.0431  0.0121  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2189 0.2313 0.3706 -0.0045 0.0379  0.0137  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2416 0.2588 0.4068 -0.0081 0.0327  0.0134  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2750 0.2965 0.4588 -0.0092 0.0395  0.0147  45  THR   A C   
312  O O   . THR   A 39  ? 0.2905 0.3091 0.4720 -0.0073 0.0492  0.0167  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2545 0.2674 0.4106 -0.0109 0.0295  0.0124  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2775 0.2858 0.4303 -0.0112 0.0380  0.0140  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2510 0.2598 0.3891 -0.0098 0.0246  0.0114  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2893 0.3174 0.4910 -0.0120 0.0345  0.0137  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3109 0.3441 0.5340 -0.0139 0.0408  0.0148  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3324 0.3616 0.5577 -0.0182 0.0436  0.0149  46  THR   A C   
319  O O   . THR   A 40  ? 0.3522 0.3808 0.5875 -0.0192 0.0536  0.0175  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3310 0.3747 0.5754 -0.0144 0.0337  0.0130  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3545 0.3992 0.5956 -0.0161 0.0214  0.0099  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3373 0.3841 0.5823 -0.0096 0.0340  0.0140  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3241 0.3500 0.5399 -0.0204 0.0356  0.0124  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3252 0.3460 0.5422 -0.0242 0.0374  0.0120  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3384 0.3491 0.5335 -0.0222 0.0441  0.0146  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3386 0.3465 0.5153 -0.0185 0.0428  0.0148  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3244 0.3466 0.5419 -0.0269 0.0251  0.0073  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3411 0.3461 0.5389 -0.0244 0.0510  0.0165  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3597 0.3550 0.5372 -0.0217 0.0573  0.0193  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3528 0.3439 0.5160 -0.0225 0.0485  0.0161  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3546 0.3470 0.5270 -0.0264 0.0416  0.0128  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4091 0.3991 0.5955 -0.0235 0.0681  0.0231  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5110 0.4914 0.6763 -0.0187 0.0769  0.0275  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6240 0.6054 0.7837 -0.0134 0.0857  0.0309  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6517 0.6403 0.8263 -0.0136 0.0880  0.0310  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6605 0.6348 0.7983 -0.0078 0.0908  0.0334  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3446 0.3313 0.4862 -0.0185 0.0482  0.0166  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3386 0.3223 0.4666 -0.0186 0.0405  0.0139  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3388 0.3147 0.4624 -0.0198 0.0424  0.0143  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3607 0.3316 0.4871 -0.0196 0.0514  0.0178  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3086 0.2826 0.4235 -0.0204 0.0347  0.0110  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.2960 0.2623 0.4058 -0.0213 0.0349  0.0103  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.2975 0.2574 0.3870 -0.0167 0.0384  0.0126  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.2990 0.2513 0.3844 -0.0164 0.0413  0.0135  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.2996 0.2676 0.4109 -0.0237 0.0245  0.0050  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3278 0.3006 0.4235 -0.0205 0.0163  0.0030  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.2835 0.2464 0.3613 -0.0129 0.0379  0.0131  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.2696 0.2285 0.3293 -0.0083 0.0391  0.0140  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2649 0.2202 0.3168 -0.0037 0.0475  0.0179  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.2754 0.2325 0.3343 -0.0035 0.0528  0.0200  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.2638 0.2283 0.3158 -0.0069 0.0325  0.0113  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.2931 0.2600 0.3475 -0.0096 0.0246  0.0080  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3031 0.2654 0.3538 -0.0100 0.0229  0.0067  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.2452 0.2179 0.3037 -0.0106 0.0201  0.0067  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2596 0.2099 0.2960 0.0008  0.0488  0.0189  52  THR   A N   
356  C CA  . THR   A 46  ? 0.2797 0.2264 0.3035 0.0071  0.0549  0.0220  52  THR   A CA  
357  C C   . THR   A 46  ? 0.2691 0.2188 0.2785 0.0114  0.0494  0.0190  52  THR   A C   
358  O O   . THR   A 46  ? 0.2741 0.2251 0.2818 0.0101  0.0434  0.0163  52  THR   A O   
359  C CB  . THR   A 46  ? 0.3391 0.2762 0.3604 0.0090  0.0629  0.0269  52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3756 0.3081 0.3902 0.0097  0.0595  0.0259  52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3398 0.2747 0.3790 0.0037  0.0682  0.0292  52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2495 0.2010 0.2502 0.0164  0.0511  0.0188  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2336 0.1893 0.2245 0.0198  0.0453  0.0149  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2487 0.2000 0.2246 0.0266  0.0467  0.0161  53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2616 0.2073 0.2304 0.0312  0.0534  0.0200  53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2341 0.1948 0.2255 0.0212  0.0449  0.0124  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2457 0.2103 0.2523 0.0154  0.0444  0.0120  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2319 0.1977 0.2172 0.0235  0.0382  0.0073  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2573 0.2261 0.2717 0.0102  0.0374  0.0097  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2299 0.1837 0.2009 0.0279  0.0409  0.0133  54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2444 0.1954 0.2014 0.0351  0.0407  0.0138  54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2474 0.2015 0.1952 0.0412  0.0401  0.0114  54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2411 0.2016 0.1940 0.0391  0.0363  0.0071  54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2373 0.1924 0.1942 0.0346  0.0341  0.0104  54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2606 0.2096 0.1940 0.0493  0.0433  0.0140  55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.2650 0.2165 0.1867 0.0567  0.0417  0.0110  55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.2841 0.2349 0.1933 0.0641  0.0381  0.0105  55  ARG   A C   
378  O O   . ARG   A 49  ? 0.2949 0.2380 0.1920 0.0707  0.0431  0.0158  55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.2738 0.2189 0.1884 0.0608  0.0506  0.0156  55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.2783 0.2242 0.2074 0.0535  0.0550  0.0167  55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.2910 0.2453 0.2286 0.0498  0.0488  0.0100  55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.2857 0.2404 0.2365 0.0441  0.0534  0.0117  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3088 0.2695 0.2714 0.0388  0.0492  0.0076  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2892 0.2554 0.2524 0.0381  0.0413  0.0018  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.3058 0.2669 0.2803 0.0345  0.0532  0.0096  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2824 0.2410 0.1965 0.0626  0.0298  0.0049  56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2965 0.2560 0.2029 0.0684  0.0258  0.0043  56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3050 0.2759 0.2179 0.0676  0.0164  -0.0036 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3127 0.2895 0.2361 0.0620  0.0138  -0.0079 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.2907 0.2447 0.2019 0.0647  0.0288  0.0089  56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2780 0.2385 0.2079 0.0535  0.0250  0.0056  56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3195 0.2934 0.2279 0.0729  0.0119  -0.0051 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3271 0.3124 0.2448 0.0717  0.0037  -0.0122 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.3254 0.3123 0.2506 0.0686  0.0031  -0.0108 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3318 0.3267 0.2605 0.0712  -0.0025 -0.0149 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3818 0.3726 0.2900 0.0813  -0.0029 -0.0173 57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.4895 0.4754 0.3828 0.0912  -0.0024 -0.0133 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.4863 0.4631 0.3762 0.0905  0.0041  -0.0061 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5773 0.5685 0.4628 0.0998  -0.0089 -0.0177 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3068 0.2865 0.2349 0.0633  0.0088  -0.0055 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2774 0.2579 0.2115 0.0607  0.0084  -0.0048 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2644 0.2559 0.2121 0.0556  0.0038  -0.0100 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2571 0.2522 0.2125 0.0504  0.0031  -0.0123 58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2812 0.2525 0.2175 0.0552  0.0142  0.0001  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2842 0.2412 0.2080 0.0605  0.0209  0.0071  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2343 0.2307 0.1854 0.0574  0.0013  -0.0114 59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2301 0.2363 0.1948 0.0527  -0.0013 -0.0151 59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2212 0.2247 0.1882 0.0502  0.0017  -0.0124 59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2216 0.2326 0.1976 0.0485  0.0005  -0.0145 59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2627 0.2800 0.2323 0.0573  -0.0071 -0.0205 59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3339 0.3560 0.3051 0.0580  -0.0112 -0.0253 59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3942 0.4286 0.3736 0.0618  -0.0180 -0.0318 59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4150 0.4514 0.3864 0.0697  -0.0227 -0.0348 59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3622 0.4052 0.3580 0.0568  -0.0186 -0.0342 59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2145 0.2069 0.1736 0.0503  0.0057  -0.0080 60  THR   A N   
416  C CA  . THR   A 54  ? 0.2120 0.2001 0.1722 0.0476  0.0083  -0.0062 60  THR   A CA  
417  C C   . THR   A 54  ? 0.2133 0.1921 0.1719 0.0425  0.0117  -0.0032 60  THR   A C   
418  O O   . THR   A 54  ? 0.2256 0.1991 0.1799 0.0432  0.0134  -0.0012 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2349 0.2189 0.1883 0.0539  0.0090  -0.0050 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2551 0.2286 0.1985 0.0576  0.0115  -0.0015 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2512 0.2453 0.2072 0.0596  0.0052  -0.0081 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1937 0.1713 0.1564 0.0377  0.0125  -0.0032 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1956 0.1658 0.1589 0.0328  0.0145  -0.0013 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1913 0.1613 0.1574 0.0292  0.0141  -0.0023 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2056 0.1788 0.1709 0.0315  0.0135  -0.0036 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1950 0.1609 0.1637 0.0244  0.0143  -0.0017 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.2036 0.1683 0.1730 0.0217  0.0132  -0.0028 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1964 0.1648 0.1720 0.0168  0.0119  -0.0025 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.2046 0.1714 0.1838 0.0145  0.0124  -0.0014 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2313 0.1856 0.1977 0.0214  0.0139  -0.0031 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2498 0.2028 0.2161 0.0189  0.0115  -0.0055 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2393 0.1888 0.1994 0.0268  0.0155  -0.0030 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1848 0.1577 0.1613 0.0156  0.0106  -0.0031 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1816 0.1573 0.1631 0.0118  0.0093  -0.0023 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1799 0.1528 0.1584 0.0108  0.0073  -0.0031 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1781 0.1489 0.1502 0.0134  0.0072  -0.0044 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1719 0.1555 0.1583 0.0114  0.0100  -0.0015 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1700 0.1573 0.1547 0.0128  0.0110  -0.0012 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1782 0.1677 0.1606 0.0163  0.0125  -0.0022 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1809 0.1699 0.1668 0.0112  0.0110  0.0005  63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1823 0.1761 0.1647 0.0178  0.0146  -0.0015 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1915 0.1835 0.1754 0.0130  0.0134  0.0017  63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1960 0.1907 0.1787 0.0160  0.0155  0.0006  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.2292 0.2271 0.2107 0.0181  0.0189  0.0021  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1821 0.1551 0.1647 0.0078  0.0052  -0.0025 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1962 0.1674 0.1754 0.0075  0.0021  -0.0037 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1945 0.1708 0.1720 0.0085  0.0026  -0.0014 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1856 0.1659 0.1693 0.0068  0.0036  0.0009  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2023 0.1715 0.1876 0.0043  -0.0011 -0.0045 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.2097 0.1777 0.1908 0.0049  -0.0058 -0.0065 64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2155 0.1784 0.1894 0.0068  -0.0078 -0.0101 64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2138 0.1854 0.1971 0.0043  -0.0084 -0.0050 64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2415 0.2032 0.2097 0.0083  -0.0129 -0.0128 64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2237 0.1943 0.2012 0.0061  -0.0134 -0.0069 64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2537 0.2195 0.2232 0.0082  -0.0158 -0.0111 64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.3093 0.2740 0.2715 0.0107  -0.0215 -0.0139 64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1940 0.1693 0.1629 0.0115  0.0024  -0.0020 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1902 0.1692 0.1559 0.0132  0.0043  0.0010  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.2012 0.1774 0.1598 0.0145  0.0001  0.0005  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2179 0.1903 0.1668 0.0176  -0.0017 -0.0023 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.2012 0.1816 0.1618 0.0166  0.0084  0.0012  65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2309 0.2147 0.1868 0.0194  0.0127  0.0056  65  CYS   A SG  
463  N N   . SER   A 60  ? 0.1912 0.1691 0.1543 0.0129  -0.0020 0.0027  66  SER   A N   
464  C CA  . SER   A 60  ? 0.2131 0.1891 0.1698 0.0148  -0.0072 0.0020  66  SER   A CA  
465  C C   . SER   A 60  ? 0.2170 0.1921 0.1601 0.0201  -0.0056 0.0038  66  SER   A C   
466  O O   . SER   A 60  ? 0.2325 0.2045 0.1655 0.0234  -0.0105 0.0008  66  SER   A O   
467  C CB  . SER   A 60  ? 0.2665 0.2450 0.2313 0.0128  -0.0095 0.0045  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3458 0.3272 0.3137 0.0127  -0.0044 0.0098  66  SER   A OG  
469  N N   . SER   A 61  ? 0.1998 0.1775 0.1426 0.0213  0.0012  0.0083  67  SER   A N   
470  C CA  . SER   A 61  ? 0.2197 0.1967 0.1498 0.0267  0.0047  0.0113  67  SER   A CA  
471  C C   . SER   A 61  ? 0.2266 0.2005 0.1457 0.0305  0.0051  0.0072  67  SER   A C   
472  O O   . SER   A 61  ? 0.2458 0.2184 0.1524 0.0358  0.0080  0.0089  67  SER   A O   
473  C CB  . SER   A 61  ? 0.2393 0.2201 0.1752 0.0263  0.0130  0.0174  67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2396 0.2237 0.1843 0.0240  0.0169  0.0160  67  SER   A OG  
475  N N   . ARG   A 62  ? 0.2165 0.1887 0.1400 0.0281  0.0028  0.0020  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.2219 0.1900 0.1359 0.0316  0.0023  -0.0026 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2487 0.2114 0.1628 0.0299  -0.0054 -0.0093 68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2706 0.2283 0.1778 0.0323  -0.0067 -0.0142 68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2336 0.2041 0.1537 0.0310  0.0080  -0.0023 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.2519 0.2281 0.1733 0.0330  0.0157  0.0030  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.2818 0.2557 0.1881 0.0395  0.0189  0.0033  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.2864 0.2658 0.1953 0.0414  0.0276  0.0090  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.2872 0.2684 0.1956 0.0419  0.0312  0.0150  68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.2841 0.2623 0.1881 0.0413  0.0262  0.0160  68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.2649 0.2507 0.1777 0.0432  0.0401  0.0202  68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2509 0.2145 0.1746 0.0255  -0.0101 -0.0096 69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2824 0.2417 0.2111 0.0226  -0.0163 -0.0154 69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2916 0.2469 0.2234 0.0215  -0.0137 -0.0182 69  ARG   A C   
489  O O   . ARG   A 63  ? 0.3107 0.2598 0.2387 0.0224  -0.0171 -0.0238 69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3387 0.2943 0.2575 0.0259  -0.0237 -0.0207 69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.4104 0.3694 0.3264 0.0275  -0.0277 -0.0185 69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4327 0.3887 0.3471 0.0281  -0.0377 -0.0260 69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.4568 0.4157 0.3651 0.0316  -0.0428 -0.0245 69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.4919 0.4490 0.3819 0.0389  -0.0450 -0.0250 69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.4978 0.4503 0.3741 0.0432  -0.0424 -0.0278 69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.4779 0.4378 0.3622 0.0427  -0.0493 -0.0225 69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2710 0.2295 0.2082 0.0205  -0.0077 -0.0143 70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2671 0.2220 0.2054 0.0209  -0.0049 -0.0160 70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2478 0.2063 0.1963 0.0181  -0.0012 -0.0126 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2396 0.2042 0.1929 0.0167  0.0005  -0.0088 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.3101 0.2658 0.2390 0.0261  -0.0005 -0.0155 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.4337 0.3828 0.3506 0.0304  -0.0027 -0.0206 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.5208 0.4717 0.4313 0.0355  0.0032  -0.0194 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.6021 0.5459 0.5001 0.0406  0.0021  -0.0247 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6508 0.5948 0.5360 0.0446  0.0008  -0.0252 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2384 0.1924 0.1892 0.0180  0.0001  -0.0139 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2195 0.1761 0.1767 0.0171  0.0036  -0.0110 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2276 0.1864 0.1806 0.0215  0.0071  -0.0104 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2601 0.2146 0.2060 0.0249  0.0074  -0.0129 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2173 0.1672 0.1791 0.0151  0.0035  -0.0119 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2225 0.1712 0.1917 0.0105  0.0006  -0.0125 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2657 0.2175 0.2430 0.0077  0.0020  -0.0096 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2389 0.1835 0.2092 0.0087  -0.0038 -0.0161 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2590 0.2092 0.2431 0.0042  -0.0009 -0.0111 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2715 0.2178 0.2521 0.0045  -0.0049 -0.0152 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2030 0.1688 0.1609 0.0216  0.0095  -0.0078 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1986 0.1683 0.1552 0.0257  0.0123  -0.0075 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2011 0.1726 0.1622 0.0265  0.0130  -0.0066 72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1982 0.1725 0.1648 0.0237  0.0124  -0.0053 72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.1983 0.1771 0.1581 0.0258  0.0144  -0.0057 72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2138 0.1914 0.1667 0.0271  0.0150  -0.0057 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2487 0.2242 0.1939 0.0317  0.0168  -0.0074 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2198 0.1987 0.1730 0.0246  0.0140  -0.0039 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2699 0.2440 0.2066 0.0340  0.0176  -0.0075 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2354 0.2129 0.1801 0.0269  0.0146  -0.0035 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2712 0.2464 0.2070 0.0317  0.0165  -0.0054 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.3048 0.2783 0.2300 0.0351  0.0174  -0.0050 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2031 0.1735 0.1612 0.0311  0.0143  -0.0073 73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2133 0.1863 0.1740 0.0333  0.0145  -0.0064 73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2271 0.2120 0.1949 0.0338  0.0145  -0.0065 73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2575 0.2478 0.2274 0.0345  0.0159  -0.0069 73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2278 0.1957 0.1826 0.0391  0.0155  -0.0071 73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2349 0.2022 0.1863 0.0403  0.0165  -0.0088 73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2078 0.1743 0.1594 0.0353  0.0154  -0.0091 73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2015 0.1904 0.1735 0.0335  0.0132  -0.0064 74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2009 0.2008 0.1818 0.0332  0.0124  -0.0075 74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2094 0.2126 0.1908 0.0372  0.0101  -0.0089 74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2061 0.2028 0.1810 0.0388  0.0097  -0.0080 74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2175 0.2200 0.2049 0.0274  0.0121  -0.0069 74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2280 0.2312 0.2167 0.0247  0.0143  -0.0055 74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2166 0.2122 0.2007 0.0251  0.0114  -0.0059 74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.2062 0.2201 0.1959 0.0389  0.0087  -0.0113 75  SER   A N   
543  C CA  . SER   A 69  ? 0.2128 0.2324 0.2049 0.0425  0.0050  -0.0140 75  SER   A CA  
544  C C   . SER   A 69  ? 0.1824 0.2086 0.1854 0.0373  0.0039  -0.0159 75  SER   A C   
545  O O   . SER   A 69  ? 0.1799 0.2114 0.1924 0.0337  0.0058  -0.0159 75  SER   A O   
546  C CB  . SER   A 69  ? 0.2555 0.2836 0.2523 0.0479  0.0035  -0.0164 75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3335 0.3545 0.3198 0.0533  0.0046  -0.0145 75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1653 0.1902 0.1665 0.0370  0.0015  -0.0172 76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1673 0.1964 0.1784 0.0320  0.0006  -0.0192 76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1794 0.2146 0.1939 0.0348  -0.0043 -0.0243 76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1983 0.2315 0.2030 0.0409  -0.0068 -0.0252 76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1774 0.1982 0.1844 0.0274  0.0031  -0.0160 76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1766 0.1885 0.1717 0.0297  0.0036  -0.0141 76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1887 0.1928 0.1754 0.0309  0.0061  -0.0106 76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1799 0.1911 0.1728 0.0310  0.0021  -0.0158 76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2003 0.1959 0.1784 0.0326  0.0076  -0.0084 76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1948 0.1978 0.1771 0.0334  0.0040  -0.0132 76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2021 0.1974 0.1780 0.0339  0.0070  -0.0092 76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1698 0.2123 0.1984 0.0308  -0.0057 -0.0279 77  SER   A N   
560  C CA  . SER   A 71  ? 0.1754 0.2243 0.2091 0.0331  -0.0114 -0.0343 77  SER   A CA  
561  C C   . SER   A 71  ? 0.1898 0.2319 0.2139 0.0339  -0.0125 -0.0350 77  SER   A C   
562  O O   . SER   A 71  ? 0.2039 0.2379 0.2224 0.0308  -0.0084 -0.0306 77  SER   A O   
563  C CB  . SER   A 71  ? 0.1886 0.2466 0.2422 0.0280  -0.0122 -0.0382 77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2236 0.2768 0.2816 0.0215  -0.0083 -0.0355 77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1967 0.2423 0.2185 0.0386  -0.0180 -0.0409 78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2247 0.2643 0.2369 0.0403  -0.0186 -0.0420 78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2293 0.2682 0.2524 0.0331  -0.0171 -0.0433 78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2305 0.2757 0.2698 0.0284  -0.0179 -0.0459 78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2715 0.3159 0.2784 0.0479  -0.0258 -0.0490 78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.3536 0.3965 0.3462 0.0564  -0.0268 -0.0466 78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.4160 0.4616 0.3986 0.0653  -0.0336 -0.0525 78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4820 0.5245 0.4489 0.0744  -0.0338 -0.0488 78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.5339 0.5795 0.4895 0.0845  -0.0412 -0.0546 78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2322 0.2635 0.2476 0.0326  -0.0146 -0.0414 79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2297 0.2598 0.2555 0.0265  -0.0131 -0.0425 79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2215 0.2589 0.2604 0.0256  -0.0185 -0.0510 79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2304 0.2706 0.2641 0.0312  -0.0239 -0.0574 79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2531 0.2752 0.2671 0.0286  -0.0105 -0.0405 79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2724 0.2900 0.2707 0.0341  -0.0086 -0.0360 79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2416 0.2649 0.2394 0.0378  -0.0122 -0.0378 79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2039 0.2442 0.2598 0.0188  -0.0170 -0.0512 80  SER   A N   
582  C CA  . SER   A 74  ? 0.2168 0.2640 0.2886 0.0170  -0.0218 -0.0596 80  SER   A CA  
583  C C   . SER   A 74  ? 0.2047 0.2501 0.2925 0.0094  -0.0181 -0.0584 80  SER   A C   
584  O O   . SER   A 74  ? 0.1922 0.2313 0.2770 0.0063  -0.0123 -0.0509 80  SER   A O   
585  C CB  . SER   A 74  ? 0.2674 0.3246 0.3475 0.0187  -0.0254 -0.0627 80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3338 0.3924 0.4219 0.0143  -0.0199 -0.0563 80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1990 0.2493 0.3035 0.0069  -0.0220 -0.0664 81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2092 0.2572 0.3307 -0.0001 -0.0184 -0.0658 81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2170 0.2709 0.3539 -0.0044 -0.0148 -0.0622 81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2168 0.2799 0.3658 -0.0041 -0.0187 -0.0680 81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2284 0.2788 0.3624 -0.0007 -0.0244 -0.0771 81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2909 0.3334 0.4195 -0.0001 -0.0250 -0.0802 81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.3055 0.3514 0.4482 -0.0006 -0.0319 -0.0930 81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.3024 0.3366 0.4352 -0.0053 -0.0173 -0.0722 81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2175 0.2664 0.3541 -0.0079 -0.0073 -0.0527 82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2267 0.2800 0.3745 -0.0111 -0.0023 -0.0477 82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2270 0.2754 0.3876 -0.0170 0.0042  -0.0428 82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2327 0.2724 0.3850 -0.0175 0.0068  -0.0383 82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2503 0.3017 0.3809 -0.0078 0.0007  -0.0401 82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2779 0.3344 0.3984 -0.0018 -0.0050 -0.0446 82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2675 0.3212 0.4058 -0.0104 0.0075  -0.0335 82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3104 0.3638 0.4141 0.0017  -0.0028 -0.0384 82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2185 0.2723 0.3997 -0.0211 0.0074  -0.0433 83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2310 0.2794 0.4245 -0.0262 0.0147  -0.0375 83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2471 0.2897 0.4272 -0.0253 0.0219  -0.0258 83  PHE   A C   
606  O O   . PHE   A 77  ? 0.2549 0.3016 0.4279 -0.0229 0.0236  -0.0223 83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2330 0.2888 0.4534 -0.0309 0.0174  -0.0404 83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2636 0.3127 0.4980 -0.0361 0.0257  -0.0342 83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.2815 0.3295 0.5178 -0.0372 0.0354  -0.0238 83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.2943 0.3367 0.5372 -0.0390 0.0245  -0.0379 83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.2998 0.3407 0.5477 -0.0412 0.0438  -0.0171 83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.3132 0.3481 0.5682 -0.0433 0.0327  -0.0314 83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3067 0.3409 0.5644 -0.0443 0.0424  -0.0207 83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.2529 0.2860 0.4287 -0.0265 0.0254  -0.0202 84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.2577 0.2850 0.4208 -0.0252 0.0313  -0.0096 84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.2727 0.2946 0.4485 -0.0288 0.0387  -0.0035 84  VAL   A C   
617  O O   . VAL   A 78  ? 0.2781 0.2947 0.4622 -0.0311 0.0383  -0.0056 84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.2677 0.2887 0.4113 -0.0220 0.0279  -0.0080 84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.2901 0.3056 0.4215 -0.0204 0.0328  0.0019  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.2671 0.2921 0.3983 -0.0183 0.0216  -0.0133 84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.2798 0.3022 0.4565 -0.0288 0.0461  0.0043  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.2882 0.3051 0.4763 -0.0315 0.0550  0.0119  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.2956 0.3015 0.4725 -0.0299 0.0559  0.0179  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.2918 0.2957 0.4504 -0.0264 0.0510  0.0181  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.3386 0.3580 0.5240 -0.0299 0.0631  0.0199  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.4530 0.4699 0.6564 -0.0332 0.0737  0.0266  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.5838 0.6023 0.7815 -0.0304 0.0829  0.0356  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.6122 0.6262 0.8195 -0.0318 0.0932  0.0438  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.6253 0.6487 0.8085 -0.0265 0.0803  0.0346  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.2959 0.2950 0.4853 -0.0325 0.0621  0.0227  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.3080 0.2968 0.4883 -0.0305 0.0631  0.0288  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.3284 0.3147 0.4867 -0.0251 0.0649  0.0377  86  ALA   A C   
633  O O   . ALA   A 80  ? 0.3398 0.3292 0.4935 -0.0236 0.0697  0.0423  86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.3104 0.2917 0.5079 -0.0337 0.0711  0.0340  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.3230 0.3042 0.4678 -0.0220 0.0606  0.0392  87  SER   A N   
636  C CA  . SER   A 81  ? 0.3223 0.3004 0.4467 -0.0166 0.0606  0.0466  87  SER   A CA  
637  C C   . SER   A 81  ? 0.3411 0.3103 0.4638 -0.0147 0.0613  0.0520  87  SER   A C   
638  O O   . SER   A 81  ? 0.3487 0.3141 0.4857 -0.0177 0.0621  0.0497  87  SER   A O   
639  C CB  . SER   A 81  ? 0.3225 0.3056 0.4326 -0.0144 0.0523  0.0409  87  SER   A CB  
640  O OG  . SER   A 81  ? 0.3098 0.2918 0.4215 -0.0152 0.0462  0.0352  87  SER   A OG  
641  N N   . GLU   A 82  ? 0.3521 0.3180 0.4576 -0.0093 0.0603  0.0585  88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.3681 0.3266 0.4709 -0.0064 0.0595  0.0633  88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.3571 0.3168 0.4640 -0.0078 0.0521  0.0554  88  GLU   A C   
644  O O   . GLU   A 82  ? 0.3647 0.3187 0.4755 -0.0067 0.0518  0.0574  88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.4418 0.3987 0.5240 0.0003  0.0577  0.0701  88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.5760 0.5241 0.6545 0.0048  0.0630  0.0809  88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.7418 0.6868 0.8078 0.0096  0.0699  0.0905  88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.7757 0.7234 0.8234 0.0144  0.0660  0.0911  88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.7946 0.7341 0.8694 0.0088  0.0796  0.0974  88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.3391 0.3058 0.4441 -0.0097 0.0465  0.0469  89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.3294 0.2978 0.4356 -0.0102 0.0402  0.0398  89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.3144 0.2834 0.4355 -0.0144 0.0400  0.0319  89  TYR   A C   
653  O O   . TYR   A 83  ? 0.3245 0.2917 0.4487 -0.0141 0.0370  0.0279  89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.3275 0.3021 0.4214 -0.0089 0.0347  0.0358  89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.3385 0.3127 0.4174 -0.0047 0.0335  0.0417  89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.3582 0.3348 0.4290 -0.0037 0.0354  0.0439  89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.3435 0.3157 0.4167 -0.0014 0.0297  0.0441  89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.3748 0.3510 0.4305 0.0006  0.0332  0.0477  89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.3582 0.3307 0.4177 0.0027  0.0271  0.0480  89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.3892 0.3633 0.4394 0.0038  0.0287  0.0496  89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.4305 0.4043 0.4661 0.0084  0.0255  0.0525  89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.2981 0.2700 0.4289 -0.0178 0.0428  0.0291  90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.2789 0.2522 0.4241 -0.0215 0.0414  0.0202  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.2896 0.2625 0.4514 -0.0255 0.0470  0.0209  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.2859 0.2611 0.4467 -0.0256 0.0516  0.0262  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.2591 0.2406 0.3994 -0.0217 0.0358  0.0118  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.2468 0.2295 0.3729 -0.0184 0.0306  0.0099  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.2478 0.2278 0.3749 -0.0176 0.0278  0.0057  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.2508 0.2375 0.3635 -0.0163 0.0288  0.0118  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.2351 0.2166 0.3511 -0.0148 0.0242  0.0042  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.2399 0.2275 0.3419 -0.0139 0.0246  0.0100  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.2344 0.2196 0.3385 -0.0133 0.0227  0.0065  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.2083 0.1945 0.3036 -0.0111 0.0198  0.0053  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.3016 0.2722 0.4797 -0.0289 0.0467  0.0144  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.3130 0.2848 0.5105 -0.0336 0.0514  0.0130  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.3232 0.3060 0.5224 -0.0349 0.0475  0.0057  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.3394 0.3272 0.5255 -0.0322 0.0410  0.0008  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.3203 0.2867 0.5334 -0.0363 0.0499  0.0059  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.3311 0.2986 0.5318 -0.0331 0.0421  -0.0010 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.3008 0.2685 0.4811 -0.0285 0.0419  0.0070  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.3114 0.2983 0.5285 -0.0389 0.0514  0.0043  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.3115 0.3095 0.5333 -0.0400 0.0474  -0.0033 92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2952 0.2963 0.5176 -0.0396 0.0378  -0.0160 92  ALA   A C   
684  O O   . ALA   A 86  ? 0.2964 0.2923 0.5298 -0.0417 0.0365  -0.0211 92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.3181 0.3196 0.5643 -0.0450 0.0533  -0.0034 92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2780 0.2858 0.4857 -0.0360 0.0314  -0.0204 93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2574 0.2671 0.4618 -0.0342 0.0229  -0.0315 93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2460 0.2649 0.4397 -0.0308 0.0171  -0.0362 93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2577 0.2808 0.4461 -0.0298 0.0197  -0.0308 93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.2521 0.2534 0.4417 -0.0312 0.0219  -0.0291 93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.2623 0.2648 0.4293 -0.0266 0.0209  -0.0238 93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.2643 0.2591 0.4211 -0.0249 0.0237  -0.0160 93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.2654 0.2613 0.4040 -0.0208 0.0204  -0.0155 93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.2682 0.2669 0.3951 -0.0190 0.0207  -0.0108 93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2457 0.2443 0.3585 -0.0159 0.0182  -0.0105 93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.2580 0.2597 0.3878 -0.0203 0.0239  -0.0068 93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2325 0.2538 0.4221 -0.0282 0.0095  -0.0460 94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2341 0.2622 0.4101 -0.0236 0.0042  -0.0494 94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2220 0.2445 0.3759 -0.0193 0.0041  -0.0451 94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2304 0.2470 0.3806 -0.0183 0.0030  -0.0474 94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2462 0.2801 0.4278 -0.0219 -0.0040 -0.0621 94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2634 0.3054 0.4683 -0.0259 -0.0049 -0.0673 94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2835 0.3355 0.4904 -0.0245 -0.0066 -0.0680 94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2757 0.3151 0.5024 -0.0314 -0.0034 -0.0710 94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2981 0.3586 0.5291 -0.0284 -0.0070 -0.0726 94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2923 0.3394 0.5435 -0.0358 -0.0035 -0.0755 94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3117 0.3699 0.5654 -0.0343 -0.0053 -0.0763 94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3491 0.4158 0.6300 -0.0389 -0.0052 -0.0812 94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1935 0.2176 0.3342 -0.0169 0.0055  -0.0390 95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1807 0.2002 0.3024 -0.0132 0.0053  -0.0354 95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1864 0.2100 0.2979 -0.0084 -0.0003 -0.0418 95  GLN   A C   
712  O O   . GLN   A 89  ? 0.2029 0.2334 0.3159 -0.0071 -0.0026 -0.0442 95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1831 0.2010 0.2959 -0.0131 0.0095  -0.0260 95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1861 0.2001 0.2818 -0.0097 0.0089  -0.0230 95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2036 0.2143 0.2930 -0.0102 0.0125  -0.0145 95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2295 0.2379 0.3254 -0.0126 0.0160  -0.0098 95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1576 0.1674 0.2338 -0.0076 0.0117  -0.0123 95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1788 0.1983 0.2799 -0.0052 -0.0022 -0.0444 96  SER   A N   
719  C CA  . SER   A 90  ? 0.1769 0.1989 0.2659 0.0005  -0.0069 -0.0497 96  SER   A CA  
720  C C   . SER   A 90  ? 0.1934 0.2129 0.2657 0.0038  -0.0047 -0.0433 96  SER   A C   
721  O O   . SER   A 90  ? 0.2008 0.2163 0.2709 0.0016  -0.0004 -0.0359 96  SER   A O   
722  C CB  . SER   A 90  ? 0.2030 0.2215 0.2892 0.0031  -0.0094 -0.0563 96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2252 0.2366 0.3063 0.0028  -0.0051 -0.0513 96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1816 0.2036 0.2426 0.0093  -0.0079 -0.0462 97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1769 0.1956 0.2225 0.0128  -0.0057 -0.0406 97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1786 0.1978 0.2257 0.0098  -0.0026 -0.0338 97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1913 0.2059 0.2299 0.0102  0.0005  -0.0281 97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1982 0.2098 0.2357 0.0139  -0.0024 -0.0379 97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2340 0.2446 0.2670 0.0181  -0.0049 -0.0446 97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2749 0.2842 0.2926 0.0251  -0.0058 -0.0459 97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2443 0.2543 0.2852 0.0168  -0.0063 -0.0500 97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2661 0.2744 0.2817 0.0282  -0.0079 -0.0524 97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2656 0.2744 0.2955 0.0232  -0.0086 -0.0556 97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1717 0.1965 0.2301 0.0071  -0.0032 -0.0347 98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1666 0.1918 0.2258 0.0050  0.0001  -0.0287 98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1613 0.1912 0.2158 0.0089  -0.0018 -0.0298 98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1543 0.1904 0.2134 0.0112  -0.0060 -0.0358 98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1670 0.1951 0.2421 0.0000  0.0022  -0.0280 98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1833 0.2111 0.2589 -0.0020 0.0067  -0.0212 98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1995 0.2200 0.2646 -0.0023 0.0092  -0.0151 98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2020 0.2323 0.2941 -0.0065 0.0099  -0.0202 98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1640 0.1911 0.2103 0.0097  0.0008  -0.0245 99  MET   A N   
743  C CA  . MET   A 93  ? 0.1679 0.1983 0.2091 0.0138  -0.0004 -0.0248 99  MET   A CA  
744  C C   . MET   A 93  ? 0.1740 0.2059 0.2193 0.0116  0.0031  -0.0209 99  MET   A C   
745  O O   . MET   A 93  ? 0.1954 0.2219 0.2371 0.0092  0.0063  -0.0161 99  MET   A O   
746  C CB  . MET   A 93  ? 0.1874 0.2108 0.2128 0.0177  0.0001  -0.0222 99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2065 0.2274 0.2255 0.0209  -0.0020 -0.0251 99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2382 0.2498 0.2406 0.0249  0.0007  -0.0206 99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2578 0.2637 0.2631 0.0188  0.0050  -0.0153 99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1607 0.2003 0.2139 0.0127  0.0026  -0.0230 100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1636 0.2046 0.2200 0.0113  0.0070  -0.0190 100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1647 0.2052 0.2115 0.0160  0.0072  -0.0178 100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1684 0.2115 0.2119 0.0206  0.0036  -0.0211 100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1777 0.2280 0.2523 0.0089  0.0081  -0.0213 100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2293 0.2801 0.3168 0.0039  0.0088  -0.0224 100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2460 0.3059 0.3537 0.0012  0.0111  -0.0241 100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2501 0.2926 0.3324 0.0008  0.0131  -0.0162 100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1611 0.1990 0.2044 0.0153  0.0115  -0.0134 101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1676 0.2045 0.2026 0.0197  0.0124  -0.0124 101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1618 0.2005 0.1997 0.0188  0.0176  -0.0092 101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1684 0.2061 0.2106 0.0150  0.0206  -0.0064 101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1974 0.2239 0.2172 0.0210  0.0118  -0.0104 101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1501 0.1906 0.1848 0.0230  0.0191  -0.0092 102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1627 0.2036 0.1966 0.0234  0.0247  -0.0059 102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1939 0.2237 0.2112 0.0242  0.0249  -0.0035 102 VAL   A C   
766  O O   . VAL   A 96  ? 0.2162 0.2403 0.2236 0.0269  0.0222  -0.0048 102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1729 0.2206 0.2105 0.0283  0.0260  -0.0076 102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1876 0.2347 0.2216 0.0301  0.0326  -0.0042 102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1838 0.2434 0.2399 0.0274  0.0246  -0.0110 102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.2050 0.2317 0.2196 0.0220  0.0282  0.0001  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.2168 0.2342 0.2172 0.0226  0.0275  0.0016  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.2159 0.2316 0.2154 0.0204  0.0304  0.0056  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2144 0.2349 0.2250 0.0176  0.0330  0.0076  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2076 0.2163 0.1940 0.0220  0.0299  0.0068  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.2064 0.2126 0.1889 0.0213  0.0319  0.0108  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.2119 0.2153 0.1970 0.0174  0.0281  0.0116  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2072 0.2066 0.1890 0.0164  0.0230  0.0090  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2210 0.2212 0.1873 0.0257  0.0319  0.0109  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2370 0.2347 0.1969 0.0265  0.0339  0.0154  104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2639 0.2651 0.2267 0.0278  0.0413  0.0204  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2569 0.2492 0.2089 0.0263  0.0293  0.0157  104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.2863 0.2833 0.2411 0.0289  0.0413  0.0243  104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2757 0.2677 0.2234 0.0284  0.0335  0.0212  104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.2195 0.2246 0.2106 0.0156  0.0312  0.0157  105 SER   A N   
785  C CA  . SER   A 99  ? 0.2214 0.2235 0.2142 0.0128  0.0282  0.0171  105 SER   A CA  
786  C C   . SER   A 99  ? 0.2478 0.2492 0.2409 0.0132  0.0328  0.0231  105 SER   A C   
787  O O   . SER   A 99  ? 0.2671 0.2720 0.2658 0.0137  0.0392  0.0260  105 SER   A O   
788  C CB  . SER   A 99  ? 0.2211 0.2261 0.2264 0.0089  0.0260  0.0145  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.2791 0.2899 0.2971 0.0073  0.0301  0.0152  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.2345 0.2313 0.2215 0.0136  0.0298  0.0251  106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.2547 0.2492 0.2401 0.0147  0.0328  0.0313  106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.2673 0.2604 0.2604 0.0114  0.0290  0.0313  106 GLU   A C   
793  O O   . GLU   A 100 ? 0.2616 0.2549 0.2573 0.0092  0.0237  0.0266  106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.2898 0.2796 0.2571 0.0201  0.0313  0.0331  106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.3131 0.3038 0.2725 0.0240  0.0365  0.0336  106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.3316 0.3175 0.2711 0.0304  0.0347  0.0342  106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.3357 0.3180 0.2673 0.0330  0.0330  0.0379  106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.3036 0.2892 0.2351 0.0332  0.0347  0.0306  106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.2764 0.2679 0.2743 0.0110  0.0324  0.0367  107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.2791 0.2694 0.2856 0.0081  0.0293  0.0365  107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.2804 0.2691 0.2815 0.0086  0.0214  0.0331  107 PRO   A C   
802  O O   . PRO   A 101 ? 0.2943 0.2841 0.3038 0.0054  0.0185  0.0296  107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.2907 0.2776 0.2979 0.0098  0.0342  0.0440  107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.2895 0.2779 0.2973 0.0108  0.0423  0.0474  107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.2747 0.2651 0.2713 0.0133  0.0403  0.0436  107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.2606 0.2470 0.2483 0.0125  0.0182  0.0336  108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2498 0.2352 0.2336 0.0130  0.0105  0.0301  108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.2319 0.2187 0.2181 0.0104  0.0074  0.0236  108 GLY   A C   
809  O O   . GLY   A 102 ? 0.2377 0.2239 0.2246 0.0097  0.0019  0.0204  108 GLY   A O   
810  N N   . ASP   A 103 ? 0.2124 0.2011 0.2008 0.0093  0.0111  0.0219  109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.1951 0.1843 0.1851 0.0075  0.0089  0.0166  109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1893 0.1800 0.1905 0.0040  0.0084  0.0149  109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1855 0.1757 0.1876 0.0029  0.0066  0.0113  109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.2049 0.1958 0.1927 0.0086  0.0127  0.0155  109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.2330 0.2214 0.2077 0.0127  0.0124  0.0153  109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.2292 0.2142 0.1969 0.0139  0.0074  0.0133  109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.2162 0.2064 0.1883 0.0148  0.0173  0.0170  109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1919 0.1837 0.2012 0.0025  0.0103  0.0173  110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1823 0.1753 0.2012 -0.0002 0.0099  0.0152  110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1745 0.1659 0.1934 -0.0007 0.0060  0.0133  110 CYS   A C   
821  O O   . CYS   A 104 ? 0.1934 0.1835 0.2091 0.0004  0.0029  0.0145  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1900 0.1831 0.2171 -0.0013 0.0122  0.0180  110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.2235 0.2192 0.2570 -0.0022 0.0176  0.0190  110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1694 0.1612 0.1915 -0.0019 0.0062  0.0103  111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1737 0.1641 0.1977 -0.0027 0.0039  0.0088  111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.1813 0.1695 0.1996 -0.0023 0.0029  0.0066  111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1821 0.1686 0.2033 -0.0033 0.0025  0.0053  111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1745 0.1621 0.1853 -0.0006 0.0033  0.0062  112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1666 0.1512 0.1719 0.0002  0.0028  0.0039  112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1650 0.1490 0.1722 0.0002  0.0053  0.0027  112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1744 0.1614 0.1835 0.0007  0.0073  0.0028  112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1658 0.1458 0.1727 -0.0002 0.0053  0.0016  113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1688 0.1473 0.1759 0.0007  0.0082  0.0015  113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1695 0.1469 0.1693 0.0038  0.0094  0.0006  113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1935 0.1681 0.1885 0.0048  0.0084  -0.0003 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1944 0.1687 0.2059 -0.0010 0.0091  0.0017  113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2031 0.1803 0.2234 -0.0031 0.0091  0.0028  113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2191 0.1892 0.2272 0.0011  0.0131  0.0024  113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2294 0.2037 0.2575 -0.0054 0.0100  0.0030  113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1603 0.1397 0.1593 0.0059  0.0112  0.0005  114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1609 0.1396 0.1536 0.0098  0.0121  -0.0003 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1761 0.1491 0.1659 0.0116  0.0147  0.0009  114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1716 0.1451 0.1640 0.0112  0.0162  0.0015  114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1635 0.1490 0.1579 0.0115  0.0115  -0.0018 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1839 0.1703 0.1728 0.0165  0.0115  -0.0031 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1800 0.1653 0.1650 0.0183  0.0114  -0.0032 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1973 0.1914 0.1906 0.0176  0.0098  -0.0058 114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1889 0.1561 0.1735 0.0136  0.0158  0.0014  115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2097 0.1701 0.1912 0.0157  0.0195  0.0036  115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2258 0.1839 0.1987 0.0214  0.0203  0.0039  115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2341 0.1932 0.2045 0.0228  0.0184  0.0024  115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2331 0.1864 0.2186 0.0123  0.0207  0.0044  115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.2842 0.2387 0.2794 0.0074  0.0205  0.0046  115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3261 0.2741 0.3276 0.0040  0.0211  0.0045  115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.3249 0.2743 0.3376 0.0001  0.0224  0.0054  115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.3268 0.2723 0.3435 0.0000  0.0281  0.0085  115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.2922 0.2315 0.3014 0.0039  0.0331  0.0113  115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.3519 0.2998 0.3803 -0.0035 0.0294  0.0092  115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2228 0.1769 0.1904 0.0253  0.0236  0.0062  116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2294 0.1792 0.1878 0.0317  0.0248  0.0075  116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2474 0.1858 0.2043 0.0319  0.0305  0.0117  116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2568 0.1924 0.2214 0.0267  0.0326  0.0127  116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2518 0.2066 0.2039 0.0375  0.0237  0.0069  116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2353 0.1873 0.1848 0.0386  0.0280  0.0095  116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.2496 0.1814 0.1974 0.0382  0.0332  0.0145  117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.2627 0.1824 0.2095 0.0387  0.0398  0.0193  117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.2679 0.1860 0.2162 0.0379  0.0451  0.0228  117 GLN   A C   
868  O O   . GLN   A 111 ? 0.2851 0.1942 0.2370 0.0363  0.0515  0.0269  117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.3034 0.2159 0.2387 0.0468  0.0421  0.0224  117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.3829 0.2991 0.3068 0.0549  0.0419  0.0239  117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.4982 0.4097 0.4106 0.0638  0.0421  0.0260  117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.5447 0.4639 0.4542 0.0678  0.0362  0.0224  117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.4890 0.3877 0.3956 0.0675  0.0490  0.0321  117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.2567 0.1832 0.2034 0.0390  0.0430  0.0211  118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.2583 0.1837 0.2046 0.0397  0.0482  0.0241  118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.2507 0.1807 0.2103 0.0321  0.0479  0.0224  118 HIS   A C   
877  O O   . HIS   A 112 ? 0.2632 0.1914 0.2250 0.0320  0.0535  0.0253  118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.2716 0.2017 0.2059 0.0470  0.0465  0.0230  118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.3204 0.2473 0.2408 0.0559  0.0458  0.0244  118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.3335 0.2683 0.2509 0.0589  0.0382  0.0196  118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.3431 0.2596 0.2528 0.0625  0.0520  0.0304  118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.3502 0.2801 0.2553 0.0674  0.0391  0.0222  118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.3571 0.2754 0.2562 0.0701  0.0474  0.0291  118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2331 0.1691 0.2010 0.0267  0.0418  0.0181  119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2183 0.1590 0.1986 0.0202  0.0407  0.0165  119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2021 0.1521 0.1850 0.0181  0.0337  0.0120  119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2181 0.1706 0.1961 0.0200  0.0297  0.0097  119 GLY   A O   
888  N N   . VAL   A 114 ? 0.1950 0.1498 0.1864 0.0142  0.0328  0.0109  120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1871 0.1495 0.1820 0.0120  0.0273  0.0076  120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1936 0.1607 0.1823 0.0161  0.0258  0.0055  120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2023 0.1688 0.1879 0.0190  0.0286  0.0060  120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.1937 0.1592 0.1998 0.0074  0.0271  0.0076  120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2002 0.1725 0.2092 0.0059  0.0225  0.0050  120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2077 0.1701 0.2217 0.0032  0.0268  0.0083  120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1934 0.1651 0.1811 0.0164  0.0214  0.0028  121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1992 0.1765 0.1841 0.0196  0.0188  -0.0003 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1984 0.1815 0.1920 0.0158  0.0164  -0.0026 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1869 0.1730 0.1810 0.0174  0.0155  -0.0053 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2129 0.1923 0.1937 0.0222  0.0161  -0.0017 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2258 0.2129 0.2079 0.0243  0.0124  -0.0059 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2210 0.1940 0.1922 0.0271  0.0185  0.0006  121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1812 0.1654 0.1811 0.0115  0.0152  -0.0018 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1876 0.1762 0.1955 0.0084  0.0135  -0.0029 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1881 0.1767 0.2000 0.0048  0.0124  -0.0011 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1903 0.1756 0.1995 0.0044  0.0125  0.0003  122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1768 0.1689 0.1948 0.0027  0.0113  -0.0012 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1724 0.1643 0.1922 0.0005  0.0103  0.0009  123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1637 0.1593 0.1856 0.0003  0.0102  0.0010  123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1619 0.1606 0.1888 0.0002  0.0106  -0.0008 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1708 0.1621 0.1967 -0.0016 0.0100  0.0026  123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1808 0.1738 0.2128 -0.0018 0.0110  0.0015  123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1916 0.1796 0.2176 -0.0020 0.0102  0.0032  123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2045 0.1971 0.2432 -0.0035 0.0106  0.0036  123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1495 0.1446 0.1682 0.0002  0.0099  0.0029  124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1419 0.1403 0.1630 0.0001  0.0113  0.0041  124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1520 0.1513 0.1815 -0.0019 0.0122  0.0055  124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1521 0.1490 0.1827 -0.0028 0.0113  0.0071  124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1542 0.1507 0.1684 0.0012  0.0113  0.0065  124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1671 0.1664 0.1839 0.0014  0.0144  0.0089  124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1590 0.1538 0.1654 0.0034  0.0107  0.0046  124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1544 0.1572 0.1910 -0.0026 0.0139  0.0044  125 SER   A N   
922  C CA  . SER   A 119 ? 0.1652 0.1680 0.2112 -0.0047 0.0152  0.0053  125 SER   A CA  
923  C C   . SER   A 119 ? 0.1800 0.1852 0.2324 -0.0057 0.0187  0.0075  125 SER   A C   
924  O O   . SER   A 119 ? 0.1885 0.1918 0.2466 -0.0070 0.0209  0.0107  125 SER   A O   
925  C CB  . SER   A 119 ? 0.1764 0.1806 0.2282 -0.0052 0.0139  0.0005  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1851 0.1886 0.2468 -0.0072 0.0149  0.0002  125 SER   A OG  
927  N N   . THR   A 120 ? 0.1697 0.1790 0.2221 -0.0048 0.0198  0.0062  126 THR   A N   
928  C CA  . THR   A 120 ? 0.1797 0.1919 0.2401 -0.0058 0.0243  0.0086  126 THR   A CA  
929  C C   . THR   A 120 ? 0.1914 0.2054 0.2438 -0.0031 0.0262  0.0103  126 THR   A C   
930  O O   . THR   A 120 ? 0.1798 0.1929 0.2224 -0.0008 0.0234  0.0085  126 THR   A O   
931  C CB  . THR   A 120 ? 0.2115 0.2292 0.2869 -0.0079 0.0242  0.0036  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.2303 0.2532 0.3040 -0.0059 0.0217  -0.0010 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.2228 0.2386 0.3046 -0.0098 0.0216  0.0001  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.2022 0.2184 0.2600 -0.0033 0.0315  0.0137  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.2420 0.2605 0.2935 -0.0003 0.0341  0.0149  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.2874 0.3089 0.3478 -0.0009 0.0414  0.0191  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.2849 0.3076 0.3595 -0.0042 0.0441  0.0199  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.3293 0.3512 0.3810 0.0026  0.0449  0.0217  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.3539 0.3782 0.4108 0.0035  0.0533  0.0267  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.3601 0.3926 0.4250 0.0045  0.0552  0.0233  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.3806 0.4176 0.4510 0.0037  0.0496  0.0170  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.3459 0.3810 0.4124 0.0066  0.0633  0.0278  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.3345 0.3786 0.4116 0.0077  0.0664  0.0253  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.2849 0.3310 0.3526 0.0116  0.0607  0.0198  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.2683 0.3232 0.3483 0.0119  0.0602  0.0157  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.3761 0.4282 0.4787 0.0025  0.0662  0.0217  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.4502 0.5000 0.5656 -0.0017 0.0728  0.0270  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.4857 0.5328 0.5983 -0.0001 0.0820  0.0347  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.4444 0.4951 0.5744 -0.0067 0.0687  0.0231  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.2487 0.2872 0.2964 0.0146  0.0563  0.0194  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.2306 0.2694 0.2701 0.0180  0.0511  0.0143  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.2180 0.2582 0.2630 0.0156  0.0433  0.0088  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2250 0.2670 0.2675 0.0183  0.0394  0.0047  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1931 0.2314 0.2439 0.0112  0.0410  0.0089  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1935 0.2322 0.2476 0.0095  0.0342  0.0041  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1909 0.2206 0.2338 0.0082  0.0310  0.0054  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.2092 0.2342 0.2469 0.0076  0.0337  0.0100  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1935 0.2386 0.2669 0.0054  0.0342  0.0018  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.2264 0.2825 0.3153 0.0062  0.0356  -0.0015 131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2417 0.3036 0.3522 0.0013  0.0368  -0.0032 131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.2254 0.2850 0.3107 0.0100  0.0289  -0.0074 131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1628 0.1907 0.2024 0.0083  0.0254  0.0017  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1544 0.1754 0.1873 0.0068  0.0225  0.0023  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1550 0.1778 0.1940 0.0055  0.0186  -0.0019 132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1626 0.1892 0.2026 0.0079  0.0164  -0.0056 132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1623 0.1765 0.1803 0.0092  0.0207  0.0030  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1862 0.2009 0.1993 0.0127  0.0190  -0.0001 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1631 0.1717 0.1778 0.0071  0.0178  0.0035  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1454 0.1660 0.1888 0.0025  0.0180  -0.0014 133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1498 0.1714 0.1981 0.0017  0.0147  -0.0056 133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1492 0.1644 0.1893 0.0017  0.0129  -0.0048 133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1532 0.1640 0.1902 0.0004  0.0141  -0.0010 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1489 0.1635 0.1849 0.0039  0.0103  -0.0081 134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1552 0.1640 0.1844 0.0041  0.0096  -0.0072 134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1592 0.1684 0.1924 0.0040  0.0083  -0.0104 134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1556 0.1685 0.1905 0.0061  0.0063  -0.0148 134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1513 0.1571 0.1702 0.0076  0.0090  -0.0073 134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1520 0.1571 0.1661 0.0087  0.0099  -0.0055 134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1578 0.1581 0.1676 0.0074  0.0106  -0.0026 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1577 0.1672 0.1719 0.0115  0.0096  -0.0072 134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1686 0.1674 0.1727 0.0090  0.0112  -0.0018 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1631 0.1715 0.1723 0.0131  0.0109  -0.0057 134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1652 0.1679 0.1689 0.0118  0.0118  -0.0031 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1502 0.1556 0.1843 0.0023  0.0092  -0.0087 135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1528 0.1574 0.1890 0.0028  0.0086  -0.0117 135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1572 0.1589 0.1833 0.0065  0.0087  -0.0120 135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1694 0.1672 0.1913 0.0062  0.0105  -0.0085 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1540 0.1557 0.1952 0.0001  0.0100  -0.0090 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1587 0.1621 0.1813 0.0101  0.0071  -0.0163 136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1800 0.1798 0.1915 0.0146  0.0081  -0.0159 136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1804 0.1761 0.1910 0.0146  0.0110  -0.0146 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1830 0.1796 0.2001 0.0131  0.0107  -0.0168 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2064 0.2097 0.2135 0.0196  0.0048  -0.0211 136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2781 0.2774 0.2715 0.0258  0.0061  -0.0201 136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2692 0.2645 0.2572 0.0263  0.0087  -0.0156 136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3461 0.3454 0.3337 0.0303  0.0049  -0.0238 136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1681 0.1589 0.1715 0.0165  0.0144  -0.0109 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1779 0.1652 0.1810 0.0171  0.0183  -0.0094 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2013 0.1848 0.1923 0.0232  0.0213  -0.0088 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2170 0.1973 0.2065 0.0245  0.0257  -0.0070 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1946 0.1796 0.2044 0.0128  0.0210  -0.0048 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1874 0.1754 0.2071 0.0080  0.0182  -0.0048 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2029 0.1844 0.2085 0.0128  0.0225  -0.0014 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.2044 0.1881 0.1864 0.0275  0.0193  -0.0099 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.1987 0.1777 0.1672 0.0343  0.0226  -0.0080 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.2231 0.2019 0.1842 0.0397  0.0231  -0.0113 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2366 0.2101 0.1868 0.0451  0.0282  -0.0082 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.2077 0.1870 0.1681 0.0384  0.0199  -0.0082 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2196 0.1973 0.1847 0.0343  0.0205  -0.0046 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2287 0.2074 0.1866 0.0389  0.0175  -0.0055 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2114 0.1988 0.1758 0.0379  0.0113  -0.0110 138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2385 0.2298 0.2011 0.0410  0.0077  -0.0129 138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2274 0.2141 0.1802 0.0461  0.0092  -0.0099 138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2342 0.2339 0.2060 0.0391  0.0029  -0.0177 138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2278 0.2116 0.1946 0.0386  0.0184  -0.0175 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2377 0.2209 0.1971 0.0441  0.0182  -0.0221 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2414 0.2213 0.2047 0.0425  0.0240  -0.0200 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2636 0.2418 0.2189 0.0480  0.0254  -0.0230 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2484 0.2379 0.2139 0.0435  0.0106  -0.0306 139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.3064 0.2986 0.2891 0.0354  0.0095  -0.0315 139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.3047 0.2972 0.2949 0.0300  0.0109  -0.0266 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3455 0.3391 0.3338 0.0349  0.0072  -0.0372 139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2214 0.2009 0.1968 0.0358  0.0269  -0.0156 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.2099 0.1877 0.1920 0.0339  0.0319  -0.0136 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.2217 0.1943 0.1970 0.0372  0.0401  -0.0076 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.2179 0.1891 0.2010 0.0330  0.0439  -0.0022 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.2065 0.1868 0.2045 0.0260  0.0305  -0.0115 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2226 0.2073 0.2283 0.0225  0.0239  -0.0161 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2132 0.1994 0.2317 0.0159  0.0232  -0.0127 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2422 0.2276 0.2485 0.0248  0.0220  -0.0225 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2325 0.2020 0.1931 0.0452  0.0429  -0.0088 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.2585 0.2221 0.2109 0.0493  0.0519  -0.0021 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.2621 0.2247 0.2254 0.0463  0.0596  0.0020  141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.2795 0.2381 0.2442 0.0460  0.0671  0.0088  141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.2710 0.2311 0.2031 0.0597  0.0536  -0.0038 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.2956 0.2581 0.2170 0.0640  0.0449  -0.0092 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.3128 0.2709 0.2120 0.0756  0.0475  -0.0094 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.3000 0.2633 0.2252 0.0603  0.0419  -0.0062 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.2505 0.2164 0.2228 0.0442  0.0579  -0.0020 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.2547 0.2208 0.2389 0.0418  0.0645  0.0013  142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.2658 0.2339 0.2669 0.0338  0.0648  0.0060  142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.2820 0.2507 0.2941 0.0320  0.0709  0.0096  142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.2495 0.2183 0.2389 0.0420  0.0618  -0.0045 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2419 0.2147 0.2392 0.0369  0.0522  -0.0093 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2464 0.2203 0.2371 0.0387  0.0452  -0.0159 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2379 0.2142 0.2518 0.0296  0.0492  -0.0078 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2488 0.2261 0.2518 0.0325  0.0391  -0.0179 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2428 0.2212 0.2587 0.0273  0.0414  -0.0127 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2375 0.2154 0.2651 0.0252  0.0522  -0.0029 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2391 0.2203 0.2682 0.0213  0.0375  -0.0119 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2422 0.2235 0.2823 0.0195  0.0469  -0.0029 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2388 0.2212 0.2786 0.0180  0.0402  -0.0070 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.2676 0.2373 0.2712 0.0294  0.0583  0.0056  143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.2806 0.2519 0.2984 0.0226  0.0575  0.0090  143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.3315 0.2986 0.3509 0.0228  0.0657  0.0149  143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.3220 0.2908 0.3563 0.0176  0.0669  0.0173  143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2643 0.2368 0.2809 0.0193  0.0499  0.0074  143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2484 0.2255 0.2696 0.0167  0.0425  0.0029  143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2535 0.2316 0.2722 0.0144  0.0366  0.0020  143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2446 0.2250 0.2812 0.0122  0.0417  0.0039  143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.3836 0.3451 0.3880 0.0288  0.0709  0.0172  144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.4467 0.4023 0.4502 0.0302  0.0799  0.0237  144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.4968 0.4511 0.5046 0.0326  0.0904  0.0275  144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.5084 0.4573 0.5161 0.0339  0.0993  0.0335  144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.4945 0.4440 0.4772 0.0375  0.0815  0.0251  144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.5920 0.5412 0.5693 0.0364  0.0737  0.0231  144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.6055 0.5575 0.5951 0.0294  0.0687  0.0220  144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.6444 0.5908 0.6048 0.0431  0.0725  0.0224  144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.5257 0.4840 0.5362 0.0341  0.0905  0.0244  145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.5669 0.5245 0.5816 0.0372  0.1012  0.0279  145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.5868 0.5515 0.6208 0.0325  0.0992  0.0255  145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.6056 0.5713 0.6470 0.0343  0.1076  0.0279  145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.6095 0.5633 0.6029 0.0471  0.1051  0.0263  145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.6864 0.6440 0.6744 0.0486  0.0957  0.0180  145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.7891 0.7429 0.7532 0.0577  0.0939  0.0142  145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.8007 0.7563 0.7604 0.0610  0.0907  0.0078  145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.8273 0.7764 0.7774 0.0618  0.0953  0.0171  145 GLU   A OE2 
1078 N N   . SER   B 1   ? 0.3435 0.3181 0.3383 0.0030  -0.0177 -0.0123 7   SER   C N   
1079 C CA  . SER   B 1   ? 0.3403 0.3192 0.3471 0.0044  -0.0193 -0.0128 7   SER   C CA  
1080 C C   . SER   B 1   ? 0.3187 0.3010 0.3326 0.0058  -0.0181 -0.0117 7   SER   C C   
1081 O O   . SER   B 1   ? 0.3130 0.2933 0.3225 0.0056  -0.0182 -0.0101 7   SER   C O   
1082 C CB  . SER   B 1   ? 0.3708 0.3474 0.3797 0.0036  -0.0259 -0.0127 7   SER   C CB  
1083 O OG  . SER   B 1   ? 0.4255 0.3984 0.4307 0.0030  -0.0307 -0.0104 7   SER   C OG  
1084 N N   . GLY   B 2   ? 0.2936 0.2807 0.3177 0.0067  -0.0166 -0.0128 8   GLY   C N   
1085 C CA  . GLY   B 2   ? 0.2706 0.2606 0.3013 0.0077  -0.0148 -0.0129 8   GLY   C CA  
1086 C C   . GLY   B 2   ? 0.2536 0.2487 0.2912 0.0075  -0.0104 -0.0145 8   GLY   C C   
1087 O O   . GLY   B 2   ? 0.2679 0.2638 0.3035 0.0066  -0.0081 -0.0146 8   GLY   C O   
1088 N N   . ALA   B 3   ? 0.2246 0.2225 0.2700 0.0081  -0.0090 -0.0158 9   ALA   C N   
1089 C CA  . ALA   B 3   ? 0.2102 0.2125 0.2608 0.0069  -0.0042 -0.0175 9   ALA   C CA  
1090 C C   . ALA   B 3   ? 0.2145 0.2179 0.2677 0.0070  -0.0010 -0.0189 9   ALA   C C   
1091 O O   . ALA   B 3   ? 0.2298 0.2309 0.2847 0.0087  -0.0033 -0.0190 9   ALA   C O   
1092 C CB  . ALA   B 3   ? 0.2073 0.2131 0.2681 0.0067  -0.0053 -0.0192 9   ALA   C CB  
1093 N N   . ILE   B 4   ? 0.1996 0.2055 0.2525 0.0048  0.0040  -0.0201 10  ILE   C N   
1094 C CA  . ILE   B 4   ? 0.1880 0.1947 0.2428 0.0041  0.0080  -0.0224 10  ILE   C CA  
1095 C C   . ILE   B 4   ? 0.1946 0.2061 0.2598 0.0033  0.0113  -0.0259 10  ILE   C C   
1096 O O   . ILE   B 4   ? 0.2007 0.2148 0.2666 0.0012  0.0126  -0.0257 10  ILE   C O   
1097 C CB  . ILE   B 4   ? 0.1885 0.1944 0.2338 0.0010  0.0113  -0.0212 10  ILE   C CB  
1098 C CG1 . ILE   B 4   ? 0.2063 0.2089 0.2435 0.0016  0.0085  -0.0178 10  ILE   C CG1 
1099 C CG2 . ILE   B 4   ? 0.1904 0.1962 0.2355 -0.0007 0.0157  -0.0241 10  ILE   C CG2 
1100 C CD1 . ILE   B 4   ? 0.2272 0.2298 0.2571 -0.0014 0.0103  -0.0156 10  ILE   C CD1 
1101 N N   . TYR   B 5   ? 0.2028 0.2154 0.2768 0.0049  0.0129  -0.0293 11  TYR   C N   
1102 C CA  . TYR   B 5   ? 0.2050 0.2229 0.2910 0.0043  0.0169  -0.0333 11  TYR   C CA  
1103 C C   . TYR   B 5   ? 0.2340 0.2520 0.3184 0.0022  0.0240  -0.0373 11  TYR   C C   
1104 O O   . TYR   B 5   ? 0.2448 0.2601 0.3315 0.0044  0.0241  -0.0392 11  TYR   C O   
1105 C CB  . TYR   B 5   ? 0.2059 0.2252 0.3065 0.0084  0.0125  -0.0346 11  TYR   C CB  
1106 C CG  . TYR   B 5   ? 0.2058 0.2247 0.3070 0.0094  0.0054  -0.0311 11  TYR   C CG  
1107 C CD1 . TYR   B 5   ? 0.2117 0.2352 0.3194 0.0079  0.0056  -0.0315 11  TYR   C CD1 
1108 C CD2 . TYR   B 5   ? 0.2239 0.2372 0.3176 0.0111  -0.0010 -0.0275 11  TYR   C CD2 
1109 C CE1 . TYR   B 5   ? 0.2369 0.2592 0.3438 0.0083  -0.0009 -0.0286 11  TYR   C CE1 
1110 C CE2 . TYR   B 5   ? 0.2374 0.2493 0.3292 0.0112  -0.0069 -0.0248 11  TYR   C CE2 
1111 C CZ  . TYR   B 5   ? 0.2527 0.2689 0.3511 0.0099  -0.0071 -0.0255 11  TYR   C CZ  
1112 O OH  . TYR   B 5   ? 0.2782 0.2922 0.3736 0.0096  -0.0131 -0.0232 11  TYR   C OH  
1113 N N   . VAL   B 6   ? 0.2390 0.2592 0.3184 -0.0024 0.0297  -0.0383 12  VAL   C N   
1114 C CA  . VAL   B 6   ? 0.2453 0.2648 0.3200 -0.0057 0.0368  -0.0422 12  VAL   C CA  
1115 C C   . VAL   B 6   ? 0.2532 0.2783 0.3339 -0.0094 0.0439  -0.0460 12  VAL   C C   
1116 O O   . VAL   B 6   ? 0.2367 0.2638 0.3144 -0.0124 0.0437  -0.0434 12  VAL   C O   
1117 C CB  . VAL   B 6   ? 0.2655 0.2800 0.3226 -0.0093 0.0364  -0.0387 12  VAL   C CB  
1118 C CG1 . VAL   B 6   ? 0.2690 0.2839 0.3194 -0.0117 0.0337  -0.0337 12  VAL   C CG1 
1119 C CG2 . VAL   B 6   ? 0.2810 0.2940 0.3308 -0.0141 0.0434  -0.0424 12  VAL   C CG2 
1120 N N   . GLY   B 7   ? 0.2664 0.2941 0.3570 -0.0089 0.0500  -0.0523 13  GLY   C N   
1121 C CA  . GLY   B 7   ? 0.2785 0.3125 0.3760 -0.0128 0.0580  -0.0567 13  GLY   C CA  
1122 C C   . GLY   B 7   ? 0.2837 0.3236 0.3936 -0.0114 0.0547  -0.0548 13  GLY   C C   
1123 O O   . GLY   B 7   ? 0.2962 0.3369 0.4172 -0.0059 0.0481  -0.0535 13  GLY   C O   
1124 N N   . ASN   B 8   ? 0.2717 0.3145 0.3776 -0.0168 0.0579  -0.0536 14  ASN   C N   
1125 C CA  . ASN   B 8   ? 0.2662 0.3140 0.3828 -0.0161 0.0541  -0.0514 14  ASN   C CA  
1126 C C   . ASN   B 8   ? 0.2428 0.2859 0.3472 -0.0169 0.0469  -0.0445 14  ASN   C C   
1127 O O   . ASN   B 8   ? 0.2406 0.2860 0.3466 -0.0196 0.0460  -0.0424 14  ASN   C O   
1128 C CB  . ASN   B 8   ? 0.3025 0.3573 0.4267 -0.0212 0.0622  -0.0550 14  ASN   C CB  
1129 C CG  . ASN   B 8   ? 0.3965 0.4575 0.5385 -0.0190 0.0688  -0.0624 14  ASN   C CG  
1130 O OD1 . ASN   B 8   ? 0.4259 0.4909 0.5865 -0.0133 0.0647  -0.0637 14  ASN   C OD1 
1131 N ND2 . ASN   B 8   ? 0.4166 0.4777 0.5530 -0.0233 0.0788  -0.0674 14  ASN   C ND2 
1132 N N   . TYR   B 9   ? 0.2284 0.2649 0.3218 -0.0144 0.0418  -0.0412 15  TYR   C N   
1133 C CA  . TYR   B 9   ? 0.2221 0.2541 0.3051 -0.0145 0.0355  -0.0354 15  TYR   C CA  
1134 C C   . TYR   B 9   ? 0.2054 0.2343 0.2897 -0.0087 0.0279  -0.0333 15  TYR   C C   
1135 O O   . TYR   B 9   ? 0.2036 0.2311 0.2902 -0.0054 0.0272  -0.0349 15  TYR   C O   
1136 C CB  . TYR   B 9   ? 0.2364 0.2632 0.3025 -0.0182 0.0370  -0.0329 15  TYR   C CB  
1137 C CG  . TYR   B 9   ? 0.2620 0.2899 0.3220 -0.0253 0.0435  -0.0338 15  TYR   C CG  
1138 C CD1 . TYR   B 9   ? 0.2835 0.3141 0.3463 -0.0289 0.0445  -0.0326 15  TYR   C CD1 
1139 C CD2 . TYR   B 9   ? 0.2888 0.3144 0.3393 -0.0290 0.0486  -0.0358 15  TYR   C CD2 
1140 C CE1 . TYR   B 9   ? 0.3081 0.3390 0.3637 -0.0363 0.0505  -0.0329 15  TYR   C CE1 
1141 C CE2 . TYR   B 9   ? 0.3140 0.3397 0.3565 -0.0365 0.0547  -0.0365 15  TYR   C CE2 
1142 C CZ  . TYR   B 9   ? 0.3334 0.3618 0.3783 -0.0403 0.0556  -0.0348 15  TYR   C CZ  
1143 O OH  . TYR   B 9   ? 0.3740 0.4019 0.4096 -0.0487 0.0615  -0.0349 15  TYR   C OH  
1144 N N   . ARG   B 10  ? 0.1740 0.2008 0.2553 -0.0081 0.0224  -0.0295 16  ARG   C N   
1145 C CA  . ARG   B 10  ? 0.1726 0.1955 0.2517 -0.0039 0.0156  -0.0271 16  ARG   C CA  
1146 C C   . ARG   B 10  ? 0.1740 0.1923 0.2402 -0.0052 0.0139  -0.0232 16  ARG   C C   
1147 O O   . ARG   B 10  ? 0.1811 0.1994 0.2454 -0.0079 0.0141  -0.0218 16  ARG   C O   
1148 C CB  . ARG   B 10  ? 0.1825 0.2073 0.2712 -0.0021 0.0106  -0.0271 16  ARG   C CB  
1149 C CG  . ARG   B 10  ? 0.1978 0.2175 0.2804 0.0004  0.0038  -0.0242 16  ARG   C CG  
1150 C CD  . ARG   B 10  ? 0.2095 0.2304 0.3010 0.0016  -0.0019 -0.0244 16  ARG   C CD  
1151 N NE  . ARG   B 10  ? 0.2351 0.2515 0.3189 0.0011  -0.0063 -0.0222 16  ARG   C NE  
1152 C CZ  . ARG   B 10  ? 0.2714 0.2829 0.3489 0.0029  -0.0116 -0.0208 16  ARG   C CZ  
1153 N NH1 . ARG   B 10  ? 0.2704 0.2803 0.3478 0.0053  -0.0136 -0.0205 16  ARG   C NH1 
1154 N NH2 . ARG   B 10  ? 0.2640 0.2713 0.3344 0.0020  -0.0144 -0.0197 16  ARG   C NH2 
1155 N N   . VAL   B 11  ? 0.1727 0.1872 0.2312 -0.0036 0.0125  -0.0217 17  VAL   C N   
1156 C CA  . VAL   B 11  ? 0.1723 0.1832 0.2209 -0.0043 0.0111  -0.0183 17  VAL   C CA  
1157 C C   . VAL   B 11  ? 0.1732 0.1813 0.2205 -0.0010 0.0063  -0.0170 17  VAL   C C   
1158 O O   . VAL   B 11  ? 0.1846 0.1915 0.2320 0.0014  0.0045  -0.0174 17  VAL   C O   
1159 C CB  . VAL   B 11  ? 0.1880 0.1971 0.2292 -0.0054 0.0130  -0.0174 17  VAL   C CB  
1160 C CG1 . VAL   B 11  ? 0.1976 0.2041 0.2316 -0.0064 0.0114  -0.0136 17  VAL   C CG1 
1161 C CG2 . VAL   B 11  ? 0.1780 0.1891 0.2192 -0.0090 0.0182  -0.0197 17  VAL   C CG2 
1162 N N   . VAL   B 12  ? 0.1603 0.1665 0.2054 -0.0013 0.0043  -0.0155 18  VAL   C N   
1163 C CA  . VAL   B 12  ? 0.1745 0.1774 0.2167 0.0011  0.0007  -0.0150 18  VAL   C CA  
1164 C C   . VAL   B 12  ? 0.1682 0.1683 0.2049 0.0010  0.0008  -0.0131 18  VAL   C C   
1165 O O   . VAL   B 12  ? 0.1706 0.1710 0.2071 -0.0010 0.0023  -0.0117 18  VAL   C O   
1166 C CB  . VAL   B 12  ? 0.2026 0.2055 0.2497 0.0013  -0.0024 -0.0162 18  VAL   C CB  
1167 C CG1 . VAL   B 12  ? 0.2423 0.2480 0.2969 0.0022  -0.0038 -0.0179 18  VAL   C CG1 
1168 C CG2 . VAL   B 12  ? 0.1870 0.1909 0.2371 -0.0013 -0.0013 -0.0161 18  VAL   C CG2 
1169 N N   . ASN   B 13  ? 0.1595 0.1566 0.1921 0.0030  -0.0008 -0.0131 19  ASN   C N   
1170 C CA  . ASN   B 13  ? 0.1610 0.1556 0.1910 0.0034  -0.0004 -0.0122 19  ASN   C CA  
1171 C C   . ASN   B 13  ? 0.1672 0.1602 0.2001 0.0022  -0.0016 -0.0128 19  ASN   C C   
1172 O O   . ASN   B 13  ? 0.1814 0.1738 0.2159 0.0019  -0.0036 -0.0145 19  ASN   C O   
1173 C CB  . ASN   B 13  ? 0.1769 0.1685 0.2022 0.0052  -0.0011 -0.0133 19  ASN   C CB  
1174 C CG  . ASN   B 13  ? 0.2019 0.1944 0.2238 0.0059  0.0000  -0.0124 19  ASN   C CG  
1175 O OD1 . ASN   B 13  ? 0.2008 0.1930 0.2210 0.0060  -0.0014 -0.0127 19  ASN   C OD1 
1176 N ND2 . ASN   B 13  ? 0.1873 0.1808 0.2091 0.0062  0.0021  -0.0111 19  ASN   C ND2 
1177 N N   . ARG   B 14  ? 0.1719 0.1641 0.2059 0.0011  -0.0009 -0.0111 20  ARG   C N   
1178 C CA  . ARG   B 14  ? 0.1680 0.1580 0.2047 -0.0005 -0.0021 -0.0112 20  ARG   C CA  
1179 C C   . ARG   B 14  ? 0.1729 0.1586 0.2083 0.0010  -0.0040 -0.0138 20  ARG   C C   
1180 O O   . ARG   B 14  ? 0.1822 0.1670 0.2197 -0.0005 -0.0059 -0.0149 20  ARG   C O   
1181 C CB  . ARG   B 14  ? 0.1750 0.1632 0.2124 -0.0018 -0.0020 -0.0083 20  ARG   C CB  
1182 C CG  . ARG   B 14  ? 0.1952 0.1809 0.2352 -0.0045 -0.0034 -0.0076 20  ARG   C CG  
1183 C CD  . ARG   B 14  ? 0.2079 0.1901 0.2483 -0.0051 -0.0045 -0.0042 20  ARG   C CD  
1184 N NE  . ARG   B 14  ? 0.1883 0.1670 0.2305 -0.0084 -0.0062 -0.0025 20  ARG   C NE  
1185 C CZ  . ARG   B 14  ? 0.2266 0.2001 0.2710 -0.0075 -0.0082 -0.0037 20  ARG   C CZ  
1186 N NH1 . ARG   B 14  ? 0.2241 0.1955 0.2685 -0.0037 -0.0081 -0.0073 20  ARG   C NH1 
1187 N NH2 . ARG   B 14  ? 0.2281 0.1978 0.2739 -0.0109 -0.0101 -0.0014 20  ARG   C NH2 
1188 N N   . HIS   B 15  ? 0.1794 0.1629 0.2111 0.0034  -0.0033 -0.0149 21  HIS   C N   
1189 C CA  . HIS   B 15  ? 0.1881 0.1667 0.2164 0.0042  -0.0044 -0.0180 21  HIS   C CA  
1190 C C   . HIS   B 15  ? 0.2042 0.1826 0.2294 0.0034  -0.0070 -0.0196 21  HIS   C C   
1191 O O   . HIS   B 15  ? 0.2322 0.2060 0.2539 0.0028  -0.0089 -0.0220 21  HIS   C O   
1192 C CB  . HIS   B 15  ? 0.1857 0.1620 0.2109 0.0066  -0.0018 -0.0194 21  HIS   C CB  
1193 C CG  . HIS   B 15  ? 0.2006 0.1790 0.2211 0.0073  -0.0003 -0.0194 21  HIS   C CG  
1194 N ND1 . HIS   B 15  ? 0.1997 0.1826 0.2221 0.0078  0.0011  -0.0168 21  HIS   C ND1 
1195 C CD2 . HIS   B 15  ? 0.2201 0.1959 0.2332 0.0072  -0.0003 -0.0217 21  HIS   C CD2 
1196 C CE1 . HIS   B 15  ? 0.2206 0.2037 0.2377 0.0080  0.0021  -0.0175 21  HIS   C CE1 
1197 N NE2 . HIS   B 15  ? 0.2357 0.2146 0.2467 0.0075  0.0012  -0.0202 21  HIS   C NE2 
1198 N N   . LEU   B 16  ? 0.1912 0.1740 0.2180 0.0031  -0.0075 -0.0183 22  LEU   C N   
1199 C CA  . LEU   B 16  ? 0.2009 0.1836 0.2268 0.0025  -0.0111 -0.0192 22  LEU   C CA  
1200 C C   . LEU   B 16  ? 0.2106 0.1974 0.2453 0.0010  -0.0128 -0.0188 22  LEU   C C   
1201 O O   . LEU   B 16  ? 0.2263 0.2143 0.2636 0.0007  -0.0162 -0.0191 22  LEU   C O   
1202 C CB  . LEU   B 16  ? 0.2013 0.1852 0.2238 0.0036  -0.0109 -0.0182 22  LEU   C CB  
1203 C CG  . LEU   B 16  ? 0.2209 0.2014 0.2347 0.0045  -0.0088 -0.0188 22  LEU   C CG  
1204 C CD1 . LEU   B 16  ? 0.2159 0.1973 0.2263 0.0048  -0.0090 -0.0173 22  LEU   C CD1 
1205 C CD2 . LEU   B 16  ? 0.2460 0.2203 0.2523 0.0035  -0.0104 -0.0214 22  LEU   C CD2 
1206 N N   . ALA   B 17  ? 0.1881 0.1773 0.2278 -0.0003 -0.0105 -0.0179 23  ALA   C N   
1207 C CA  . ALA   B 17  ? 0.1907 0.1846 0.2390 -0.0024 -0.0108 -0.0179 23  ALA   C CA  
1208 C C   . ALA   B 17  ? 0.2002 0.1924 0.2512 -0.0038 -0.0152 -0.0192 23  ALA   C C   
1209 O O   . ALA   B 17  ? 0.2037 0.1903 0.2498 -0.0042 -0.0168 -0.0200 23  ALA   C O   
1210 C CB  . ALA   B 17  ? 0.1844 0.1795 0.2348 -0.0047 -0.0077 -0.0164 23  ALA   C CB  
1211 N N   . THR   B 18  ? 0.1962 0.1932 0.2558 -0.0046 -0.0171 -0.0197 24  THR   C N   
1212 C CA  . THR   B 18  ? 0.2052 0.2016 0.2693 -0.0063 -0.0221 -0.0206 24  THR   C CA  
1213 C C   . THR   B 18  ? 0.2045 0.2033 0.2758 -0.0097 -0.0210 -0.0206 24  THR   C C   
1214 O O   . THR   B 18  ? 0.1941 0.1955 0.2669 -0.0109 -0.0161 -0.0197 24  THR   C O   
1215 C CB  . THR   B 18  ? 0.2190 0.2201 0.2915 -0.0053 -0.0254 -0.0208 24  THR   C CB  
1216 O OG1 . THR   B 18  ? 0.2312 0.2400 0.3148 -0.0057 -0.0211 -0.0211 24  THR   C OG1 
1217 C CG2 . THR   B 18  ? 0.2243 0.2224 0.2895 -0.0026 -0.0270 -0.0202 24  THR   C CG2 
1218 N N   . HIS   B 19  ? 0.2072 0.2055 0.2831 -0.0119 -0.0257 -0.0214 25  HIS   C N   
1219 C CA  . HIS   B 19  ? 0.2314 0.2326 0.3153 -0.0158 -0.0247 -0.0212 25  HIS   C CA  
1220 C C   . HIS   B 19  ? 0.2221 0.2329 0.3175 -0.0167 -0.0200 -0.0211 25  HIS   C C   
1221 O O   . HIS   B 19  ? 0.2311 0.2442 0.3287 -0.0197 -0.0155 -0.0204 25  HIS   C O   
1222 C CB  . HIS   B 19  ? 0.2718 0.2720 0.3604 -0.0181 -0.0314 -0.0221 25  HIS   C CB  
1223 C CG  . HIS   B 19  ? 0.3621 0.3522 0.4389 -0.0183 -0.0354 -0.0230 25  HIS   C CG  
1224 N ND1 . HIS   B 19  ? 0.4121 0.3956 0.4817 -0.0191 -0.0331 -0.0231 25  HIS   C ND1 
1225 C CD2 . HIS   B 19  ? 0.4036 0.3889 0.4749 -0.0183 -0.0417 -0.0240 25  HIS   C CD2 
1226 C CE1 . HIS   B 19  ? 0.4280 0.4032 0.4885 -0.0192 -0.0370 -0.0250 25  HIS   C CE1 
1227 N NE2 . HIS   B 19  ? 0.4295 0.4052 0.4894 -0.0191 -0.0422 -0.0255 25  HIS   C NE2 
1228 N N   . ASN   B 20  ? 0.2057 0.2216 0.3079 -0.0141 -0.0207 -0.0219 26  ASN   C N   
1229 C CA  . ASN   B 20  ? 0.2038 0.2286 0.3176 -0.0146 -0.0155 -0.0229 26  ASN   C CA  
1230 C C   . ASN   B 20  ? 0.1987 0.2231 0.3051 -0.0146 -0.0085 -0.0224 26  ASN   C C   
1231 O O   . ASN   B 20  ? 0.1931 0.2227 0.3047 -0.0175 -0.0027 -0.0231 26  ASN   C O   
1232 C CB  . ASN   B 20  ? 0.2336 0.2625 0.3570 -0.0113 -0.0186 -0.0240 26  ASN   C CB  
1233 C CG  . ASN   B 20  ? 0.3013 0.3396 0.4395 -0.0115 -0.0131 -0.0261 26  ASN   C CG  
1234 O OD1 . ASN   B 20  ? 0.3329 0.3777 0.4834 -0.0145 -0.0115 -0.0272 26  ASN   C OD1 
1235 N ND2 . ASN   B 20  ? 0.3220 0.3612 0.4596 -0.0085 -0.0098 -0.0271 26  ASN   C ND2 
1236 N N   . ASP   B 21  ? 0.1961 0.2146 0.2903 -0.0119 -0.0088 -0.0213 27  ASP   C N   
1237 C CA  . ASP   B 21  ? 0.1987 0.2165 0.2857 -0.0123 -0.0033 -0.0204 27  ASP   C CA  
1238 C C   . ASP   B 21  ? 0.2078 0.2237 0.2913 -0.0166 -0.0009 -0.0187 27  ASP   C C   
1239 O O   . ASP   B 21  ? 0.2178 0.2365 0.3010 -0.0196 0.0043  -0.0183 27  ASP   C O   
1240 C CB  . ASP   B 21  ? 0.1876 0.1993 0.2632 -0.0089 -0.0049 -0.0192 27  ASP   C CB  
1241 C CG  . ASP   B 21  ? 0.2015 0.2143 0.2781 -0.0054 -0.0062 -0.0201 27  ASP   C CG  
1242 O OD1 . ASP   B 21  ? 0.1989 0.2168 0.2829 -0.0052 -0.0035 -0.0215 27  ASP   C OD1 
1243 O OD2 . ASP   B 21  ? 0.2072 0.2151 0.2768 -0.0031 -0.0098 -0.0196 27  ASP   C OD2 
1244 N N   . TRP   B 22  ? 0.2147 0.2254 0.2952 -0.0174 -0.0048 -0.0177 28  TRP   C N   
1245 C CA  . TRP   B 22  ? 0.2173 0.2248 0.2947 -0.0214 -0.0036 -0.0157 28  TRP   C CA  
1246 C C   . TRP   B 22  ? 0.2134 0.2269 0.3000 -0.0265 -0.0009 -0.0160 28  TRP   C C   
1247 O O   . TRP   B 22  ? 0.2205 0.2334 0.3043 -0.0309 0.0024  -0.0141 28  TRP   C O   
1248 C CB  . TRP   B 22  ? 0.2196 0.2191 0.2924 -0.0206 -0.0085 -0.0152 28  TRP   C CB  
1249 C CG  . TRP   B 22  ? 0.2098 0.2032 0.2733 -0.0173 -0.0088 -0.0143 28  TRP   C CG  
1250 C CD1 . TRP   B 22  ? 0.2208 0.2113 0.2798 -0.0132 -0.0108 -0.0158 28  TRP   C CD1 
1251 C CD2 . TRP   B 22  ? 0.2051 0.1949 0.2636 -0.0182 -0.0071 -0.0115 28  TRP   C CD2 
1252 N NE1 . TRP   B 22  ? 0.2256 0.2119 0.2783 -0.0112 -0.0097 -0.0145 28  TRP   C NE1 
1253 C CE2 . TRP   B 22  ? 0.2166 0.2023 0.2695 -0.0140 -0.0080 -0.0117 28  TRP   C CE2 
1254 C CE3 . TRP   B 22  ? 0.2093 0.1988 0.2673 -0.0226 -0.0052 -0.0086 28  TRP   C CE3 
1255 C CZ2 . TRP   B 22  ? 0.2230 0.2048 0.2722 -0.0135 -0.0075 -0.0092 28  TRP   C CZ2 
1256 C CZ3 . TRP   B 22  ? 0.2256 0.2102 0.2781 -0.0225 -0.0055 -0.0055 28  TRP   C CZ3 
1257 C CH2 . TRP   B 22  ? 0.2227 0.2041 0.2720 -0.0176 -0.0067 -0.0059 28  TRP   C CH2 
1258 N N   . ALA   B 23  ? 0.2040 0.2231 0.3016 -0.0263 -0.0024 -0.0183 29  ALA   C N   
1259 C CA  . ALA   B 23  ? 0.2131 0.2393 0.3218 -0.0311 0.0006  -0.0191 29  ALA   C CA  
1260 C C   . ALA   B 23  ? 0.2307 0.2641 0.3430 -0.0326 0.0084  -0.0206 29  ALA   C C   
1261 O O   . ALA   B 23  ? 0.2393 0.2784 0.3586 -0.0377 0.0131  -0.0213 29  ALA   C O   
1262 C CB  . ALA   B 23  ? 0.1951 0.2259 0.3166 -0.0301 -0.0040 -0.0211 29  ALA   C CB  
1263 N N   . ASN   B 24  ? 0.2195 0.2527 0.3275 -0.0286 0.0100  -0.0215 30  ASN   C N   
1264 C CA  . ASN   B 24  ? 0.2162 0.2546 0.3258 -0.0298 0.0174  -0.0235 30  ASN   C CA  
1265 C C   . ASN   B 24  ? 0.2232 0.2555 0.3174 -0.0299 0.0192  -0.0213 30  ASN   C C   
1266 O O   . ASN   B 24  ? 0.2202 0.2538 0.3123 -0.0282 0.0224  -0.0229 30  ASN   C O   
1267 C CB  . ASN   B 24  ? 0.2294 0.2731 0.3500 -0.0249 0.0170  -0.0269 30  ASN   C CB  
1268 C CG  . ASN   B 24  ? 0.2829 0.3337 0.4210 -0.0252 0.0152  -0.0290 30  ASN   C CG  
1269 O OD1 . ASN   B 24  ? 0.2956 0.3540 0.4442 -0.0289 0.0212  -0.0313 30  ASN   C OD1 
1270 N ND2 . ASN   B 24  ? 0.2854 0.3341 0.4271 -0.0220 0.0070  -0.0281 30  ASN   C ND2 
1271 N N   . LEU   B 25  ? 0.2259 0.2515 0.3104 -0.0320 0.0166  -0.0175 31  LEU   C N   
1272 C CA  . LEU   B 25  ? 0.2269 0.2465 0.2984 -0.0320 0.0166  -0.0147 31  LEU   C CA  
1273 C C   . LEU   B 25  ? 0.2369 0.2581 0.3025 -0.0370 0.0229  -0.0145 31  LEU   C C   
1274 O O   . LEU   B 25  ? 0.2513 0.2749 0.3181 -0.0430 0.0269  -0.0144 31  LEU   C O   
1275 C CB  . LEU   B 25  ? 0.2272 0.2395 0.2929 -0.0334 0.0121  -0.0108 31  LEU   C CB  
1276 C CG  . LEU   B 25  ? 0.2376 0.2433 0.2921 -0.0334 0.0107  -0.0071 31  LEU   C CG  
1277 C CD1 . LEU   B 25  ? 0.2401 0.2446 0.2921 -0.0270 0.0086  -0.0079 31  LEU   C CD1 
1278 C CD2 . LEU   B 25  ? 0.2520 0.2507 0.3041 -0.0347 0.0063  -0.0038 31  LEU   C CD2 
1279 N N   . VAL   B 26  ? 0.2175 0.2369 0.2758 -0.0351 0.0239  -0.0143 32  VAL   C N   
1280 C CA  . VAL   B 26  ? 0.2237 0.2426 0.2730 -0.0401 0.0289  -0.0139 32  VAL   C CA  
1281 C C   . VAL   B 26  ? 0.2425 0.2538 0.2797 -0.0416 0.0248  -0.0084 32  VAL   C C   
1282 O O   . VAL   B 26  ? 0.2561 0.2644 0.2850 -0.0481 0.0260  -0.0053 32  VAL   C O   
1283 C CB  . VAL   B 26  ? 0.2323 0.2545 0.2828 -0.0374 0.0327  -0.0179 32  VAL   C CB  
1284 C CG1 . VAL   B 26  ? 0.2477 0.2676 0.2861 -0.0428 0.0371  -0.0174 32  VAL   C CG1 
1285 C CG2 . VAL   B 26  ? 0.2303 0.2602 0.2950 -0.0362 0.0369  -0.0233 32  VAL   C CG2 
1286 N N   . TRP   B 27  ? 0.2289 0.2371 0.2654 -0.0357 0.0197  -0.0072 33  TRP   C N   
1287 C CA  . TRP   B 27  ? 0.2327 0.2346 0.2609 -0.0359 0.0155  -0.0024 33  TRP   C CA  
1288 C C   . TRP   B 27  ? 0.2166 0.2165 0.2483 -0.0290 0.0108  -0.0023 33  TRP   C C   
1289 O O   . TRP   B 27  ? 0.2185 0.2213 0.2547 -0.0245 0.0111  -0.0056 33  TRP   C O   
1290 C CB  . TRP   B 27  ? 0.2378 0.2394 0.2576 -0.0379 0.0177  -0.0020 33  TRP   C CB  
1291 C CG  . TRP   B 27  ? 0.2469 0.2435 0.2601 -0.0373 0.0129  0.0026  33  TRP   C CG  
1292 C CD1 . TRP   B 27  ? 0.2704 0.2619 0.2765 -0.0421 0.0099  0.0079  33  TRP   C CD1 
1293 C CD2 . TRP   B 27  ? 0.2393 0.2357 0.2533 -0.0319 0.0105  0.0025  33  TRP   C CD2 
1294 N NE1 . TRP   B 27  ? 0.2667 0.2554 0.2708 -0.0395 0.0053  0.0111  33  TRP   C NE1 
1295 C CE2 . TRP   B 27  ? 0.2538 0.2459 0.2629 -0.0332 0.0060  0.0076  33  TRP   C CE2 
1296 C CE3 . TRP   B 27  ? 0.2431 0.2425 0.2619 -0.0262 0.0112  -0.0011 33  TRP   C CE3 
1297 C CZ2 . TRP   B 27  ? 0.2532 0.2449 0.2628 -0.0293 0.0033  0.0087  33  TRP   C CZ2 
1298 C CZ3 . TRP   B 27  ? 0.2441 0.2424 0.2616 -0.0228 0.0086  0.0002  33  TRP   C CZ3 
1299 C CH2 . TRP   B 27  ? 0.2458 0.2408 0.2594 -0.0242 0.0050  0.0048  33  TRP   C CH2 
1300 N N   . GLU   B 28  ? 0.2194 0.2140 0.2490 -0.0284 0.0064  0.0014  34  GLU   C N   
1301 C CA  . GLU   B 28  ? 0.2134 0.2059 0.2456 -0.0223 0.0030  0.0011  34  GLU   C CA  
1302 C C   . GLU   B 28  ? 0.2122 0.1998 0.2412 -0.0224 -0.0006 0.0056  34  GLU   C C   
1303 O O   . GLU   B 28  ? 0.2130 0.1973 0.2389 -0.0271 -0.0022 0.0095  34  GLU   C O   
1304 C CB  . GLU   B 28  ? 0.2156 0.2068 0.2536 -0.0197 0.0011  -0.0011 34  GLU   C CB  
1305 C CG  . GLU   B 28  ? 0.2308 0.2185 0.2700 -0.0236 -0.0005 0.0009  34  GLU   C CG  
1306 C CD  . GLU   B 28  ? 0.2740 0.2548 0.3117 -0.0235 -0.0044 0.0047  34  GLU   C CD  
1307 O OE1 . GLU   B 28  ? 0.3290 0.3064 0.3653 -0.0284 -0.0056 0.0080  34  GLU   C OE1 
1308 O OE2 . GLU   B 28  ? 0.2365 0.2152 0.2751 -0.0188 -0.0062 0.0045  34  GLU   C OE2 
1309 N N   . ASP   B 29  ? 0.1988 0.1862 0.2291 -0.0176 -0.0020 0.0053  35  ASP   C N   
1310 C CA  . ASP   B 29  ? 0.2022 0.1860 0.2327 -0.0168 -0.0056 0.0092  35  ASP   C CA  
1311 C C   . ASP   B 29  ? 0.1965 0.1797 0.2323 -0.0106 -0.0064 0.0070  35  ASP   C C   
1312 O O   . ASP   B 29  ? 0.1910 0.1774 0.2267 -0.0076 -0.0047 0.0048  35  ASP   C O   
1313 C CB  . ASP   B 29  ? 0.2174 0.2029 0.2428 -0.0192 -0.0056 0.0118  35  ASP   C CB  
1314 C CG  . ASP   B 29  ? 0.2888 0.2710 0.3152 -0.0194 -0.0103 0.0168  35  ASP   C CG  
1315 O OD1 . ASP   B 29  ? 0.3018 0.2819 0.3352 -0.0153 -0.0126 0.0171  35  ASP   C OD1 
1316 O OD2 . ASP   B 29  ? 0.3087 0.2906 0.3294 -0.0236 -0.0116 0.0202  35  ASP   C OD2 
1317 N N   . SER   B 30  ? 0.1964 0.1750 0.2366 -0.0090 -0.0087 0.0073  36  SER   C N   
1318 C CA  A SER   B 30  ? 0.1991 0.1763 0.2439 -0.0037 -0.0086 0.0044  36  SER   C CA  
1319 C CA  B SER   B 30  ? 0.1998 0.1771 0.2445 -0.0037 -0.0085 0.0043  36  SER   C CA  
1320 C C   . SER   B 30  ? 0.2038 0.1830 0.2514 -0.0010 -0.0089 0.0058  36  SER   C C   
1321 O O   . SER   B 30  ? 0.2195 0.2006 0.2685 0.0027  -0.0066 0.0026  36  SER   C O   
1322 C CB  A SER   B 30  ? 0.2251 0.1960 0.2743 -0.0031 -0.0111 0.0045  36  SER   C CB  
1323 C CB  B SER   B 30  ? 0.2277 0.1989 0.2768 -0.0028 -0.0108 0.0040  36  SER   C CB  
1324 O OG  A SER   B 30  ? 0.2660 0.2348 0.3198 0.0018  -0.0104 0.0013  36  SER   C OG  
1325 O OG  B SER   B 30  ? 0.2731 0.2407 0.3255 -0.0040 -0.0144 0.0088  36  SER   C OG  
1326 N N   . SER   B 31  ? 0.1967 0.1755 0.2446 -0.0035 -0.0118 0.0109  37  SER   C N   
1327 C CA  . SER   B 31  ? 0.1982 0.1795 0.2504 -0.0012 -0.0128 0.0127  37  SER   C CA  
1328 C C   . SER   B 31  ? 0.1968 0.1836 0.2446 -0.0011 -0.0097 0.0109  37  SER   C C   
1329 O O   . SER   B 31  ? 0.2132 0.2028 0.2653 0.0015  -0.0093 0.0109  37  SER   C O   
1330 C CB  . SER   B 31  ? 0.2374 0.2166 0.2909 -0.0044 -0.0180 0.0191  37  SER   C CB  
1331 O OG  . SER   B 31  ? 0.2871 0.2677 0.3313 -0.0099 -0.0182 0.0215  37  SER   C OG  
1332 N N   . ARG   B 32  ? 0.1772 0.1655 0.2179 -0.0037 -0.0075 0.0093  38  ARG   C N   
1333 C CA  . ARG   B 32  ? 0.1684 0.1609 0.2052 -0.0035 -0.0048 0.0075  38  ARG   C CA  
1334 C C   . ARG   B 32  ? 0.1780 0.1714 0.2140 -0.0006 -0.0019 0.0027  38  ARG   C C   
1335 O O   . ARG   B 32  ? 0.1782 0.1742 0.2114 -0.0001 -0.0001 0.0012  38  ARG   C O   
1336 C CB  . ARG   B 32  ? 0.1658 0.1590 0.1956 -0.0085 -0.0043 0.0087  38  ARG   C CB  
1337 C CG  . ARG   B 32  ? 0.1782 0.1697 0.2057 -0.0126 -0.0077 0.0139  38  ARG   C CG  
1338 C CD  . ARG   B 32  ? 0.1849 0.1765 0.2035 -0.0182 -0.0062 0.0143  38  ARG   C CD  
1339 N NE  . ARG   B 32  ? 0.1810 0.1756 0.1965 -0.0178 -0.0032 0.0114  38  ARG   C NE  
1340 C CZ  . ARG   B 32  ? 0.2090 0.2034 0.2170 -0.0223 -0.0022 0.0117  38  ARG   C CZ  
1341 N NH1 . ARG   B 32  ? 0.2240 0.2156 0.2256 -0.0282 -0.0039 0.0151  38  ARG   C NH1 
1342 N NH2 . ARG   B 32  ? 0.2212 0.2176 0.2274 -0.0213 0.0002  0.0089  38  ARG   C NH2 
1343 N N   . ASP   B 33  ? 0.1785 0.1693 0.2163 0.0006  -0.0019 0.0005  39  ASP   C N   
1344 C CA  . ASP   B 33  ? 0.1685 0.1593 0.2045 0.0023  -0.0003 -0.0036 39  ASP   C CA  
1345 C C   . ASP   B 33  ? 0.1662 0.1596 0.1991 0.0002  0.0006  -0.0044 39  ASP   C C   
1346 O O   . ASP   B 33  ? 0.1703 0.1648 0.2016 0.0016  0.0014  -0.0067 39  ASP   C O   
1347 C CB  . ASP   B 33  ? 0.1743 0.1657 0.2097 0.0055  0.0013  -0.0057 39  ASP   C CB  
1348 C CG  . ASP   B 33  ? 0.1806 0.1706 0.2124 0.0065  0.0019  -0.0094 39  ASP   C CG  
1349 O OD1 . ASP   B 33  ? 0.1872 0.1745 0.2193 0.0060  0.0007  -0.0109 39  ASP   C OD1 
1350 O OD2 . ASP   B 33  ? 0.1769 0.1681 0.2052 0.0072  0.0030  -0.0104 39  ASP   C OD2 
1351 N N   . LEU   B 34  ? 0.1591 0.1531 0.1915 -0.0034 0.0006  -0.0027 40  LEU   C N   
1352 C CA  . LEU   B 34  ? 0.1619 0.1587 0.1932 -0.0054 0.0025  -0.0044 40  LEU   C CA  
1353 C C   . LEU   B 34  ? 0.1621 0.1589 0.1958 -0.0080 0.0028  -0.0051 40  LEU   C C   
1354 O O   . LEU   B 34  ? 0.1729 0.1674 0.2065 -0.0104 0.0017  -0.0028 40  LEU   C O   
1355 C CB  . LEU   B 34  ? 0.1686 0.1669 0.1961 -0.0084 0.0039  -0.0026 40  LEU   C CB  
1356 C CG  . LEU   B 34  ? 0.1804 0.1796 0.2057 -0.0067 0.0040  -0.0023 40  LEU   C CG  
1357 C CD1 . LEU   B 34  ? 0.1886 0.1884 0.2091 -0.0106 0.0052  -0.0009 40  LEU   C CD1 
1358 C CD2 . LEU   B 34  ? 0.1915 0.1919 0.2178 -0.0038 0.0049  -0.0054 40  LEU   C CD2 
1359 N N   . LEU   B 35  ? 0.1531 0.1528 0.1895 -0.0080 0.0042  -0.0079 41  LEU   C N   
1360 C CA  . LEU   B 35  ? 0.1615 0.1629 0.2018 -0.0109 0.0051  -0.0089 41  LEU   C CA  
1361 C C   . LEU   B 35  ? 0.1697 0.1757 0.2129 -0.0116 0.0083  -0.0116 41  LEU   C C   
1362 O O   . LEU   B 35  ? 0.1746 0.1816 0.2189 -0.0085 0.0080  -0.0132 41  LEU   C O   
1363 C CB  . LEU   B 35  ? 0.1630 0.1628 0.2072 -0.0093 0.0024  -0.0103 41  LEU   C CB  
1364 C CG  . LEU   B 35  ? 0.1727 0.1746 0.2224 -0.0126 0.0029  -0.0112 41  LEU   C CG  
1365 C CD1 . LEU   B 35  ? 0.1857 0.1832 0.2362 -0.0127 -0.0004 -0.0108 41  LEU   C CD1 
1366 C CD2 . LEU   B 35  ? 0.1806 0.1876 0.2374 -0.0117 0.0036  -0.0143 41  LEU   C CD2 
1367 N N   . VAL   B 36  ? 0.1566 0.1652 0.2014 -0.0158 0.0116  -0.0121 42  VAL   C N   
1368 C CA  . VAL   B 36  ? 0.1603 0.1736 0.2096 -0.0167 0.0158  -0.0155 42  VAL   C CA  
1369 C C   . VAL   B 36  ? 0.1700 0.1870 0.2277 -0.0189 0.0172  -0.0172 42  VAL   C C   
1370 O O   . VAL   B 36  ? 0.1780 0.1940 0.2339 -0.0231 0.0177  -0.0153 42  VAL   C O   
1371 C CB  . VAL   B 36  ? 0.1693 0.1825 0.2114 -0.0208 0.0202  -0.0152 42  VAL   C CB  
1372 C CG1 . VAL   B 36  ? 0.1850 0.2029 0.2327 -0.0218 0.0257  -0.0198 42  VAL   C CG1 
1373 C CG2 . VAL   B 36  ? 0.1636 0.1734 0.1982 -0.0189 0.0182  -0.0131 42  VAL   C CG2 
1374 N N   . SER   B 37  ? 0.1709 0.1922 0.2386 -0.0163 0.0173  -0.0205 43  SER   C N   
1375 C CA  . SER   B 37  ? 0.1738 0.2001 0.2523 -0.0183 0.0186  -0.0225 43  SER   C CA  
1376 C C   . SER   B 37  ? 0.1825 0.2149 0.2698 -0.0185 0.0241  -0.0268 43  SER   C C   
1377 O O   . SER   B 37  ? 0.1948 0.2266 0.2803 -0.0161 0.0255  -0.0283 43  SER   C O   
1378 C CB  . SER   B 37  ? 0.1869 0.2128 0.2719 -0.0149 0.0124  -0.0225 43  SER   C CB  
1379 O OG  . SER   B 37  ? 0.2331 0.2589 0.3209 -0.0101 0.0095  -0.0237 43  SER   C OG  
1380 N N   . SER   B 38  ? 0.1835 0.2219 0.2812 -0.0216 0.0277  -0.0290 44  SER   C N   
1381 C CA  . SER   B 38  ? 0.2101 0.2550 0.3182 -0.0218 0.0340  -0.0338 44  SER   C CA  
1382 C C   . SER   B 38  ? 0.2352 0.2843 0.3597 -0.0165 0.0302  -0.0363 44  SER   C C   
1383 O O   . SER   B 38  ? 0.2409 0.2899 0.3705 -0.0148 0.0236  -0.0345 44  SER   C O   
1384 C CB  . SER   B 38  ? 0.2322 0.2821 0.3437 -0.0284 0.0410  -0.0354 44  SER   C CB  
1385 O OG  . SER   B 38  ? 0.2637 0.3158 0.3827 -0.0297 0.0375  -0.0339 44  SER   C OG  
1386 N N   . THR   B 39  ? 0.2510 0.3032 0.3835 -0.0140 0.0339  -0.0404 45  THR   C N   
1387 C CA  . THR   B 39  ? 0.2840 0.3398 0.4334 -0.0088 0.0298  -0.0425 45  THR   C CA  
1388 C C   . THR   B 39  ? 0.3169 0.3816 0.4841 -0.0097 0.0376  -0.0483 45  THR   C C   
1389 O O   . THR   B 39  ? 0.3253 0.3918 0.4882 -0.0140 0.0468  -0.0513 45  THR   C O   
1390 C CB  . THR   B 39  ? 0.3040 0.3543 0.4486 -0.0038 0.0262  -0.0421 45  THR   C CB  
1391 O OG1 . THR   B 39  ? 0.3262 0.3765 0.4681 -0.0048 0.0340  -0.0458 45  THR   C OG1 
1392 C CG2 . THR   B 39  ? 0.3061 0.3482 0.4332 -0.0033 0.0206  -0.0372 45  THR   C CG2 
1393 N N   . THR   B 40  ? 0.3301 0.4002 0.5172 -0.0060 0.0338  -0.0500 46  THR   C N   
1394 C CA  . THR   B 40  ? 0.3523 0.4316 0.5601 -0.0058 0.0409  -0.0561 46  THR   C CA  
1395 C C   . THR   B 40  ? 0.3671 0.4446 0.5798 -0.0010 0.0429  -0.0599 46  THR   C C   
1396 O O   . THR   B 40  ? 0.3768 0.4589 0.5977 -0.0020 0.0526  -0.0660 46  THR   C O   
1397 C CB  . THR   B 40  ? 0.3759 0.4628 0.6053 -0.0045 0.0355  -0.0558 46  THR   C CB  
1398 O OG1 . THR   B 40  ? 0.4104 0.4920 0.6401 0.0004  0.0233  -0.0517 46  THR   C OG1 
1399 C CG2 . THR   B 40  ? 0.3818 0.4713 0.6079 -0.0104 0.0360  -0.0535 46  THR   C CG2 
1400 N N   . ALA   B 41  ? 0.3642 0.4343 0.5710 0.0038  0.0342  -0.0565 47  ALA   C N   
1401 C CA  . ALA   B 41  ? 0.3701 0.4367 0.5806 0.0084  0.0345  -0.0592 47  ALA   C CA  
1402 C C   . ALA   B 41  ? 0.3861 0.4455 0.5752 0.0062  0.0394  -0.0594 47  ALA   C C   
1403 O O   . ALA   B 41  ? 0.3941 0.4490 0.5641 0.0029  0.0382  -0.0552 47  ALA   C O   
1404 C CB  . ALA   B 41  ? 0.3749 0.4367 0.5889 0.0136  0.0222  -0.0549 47  ALA   C CB  
1405 N N   . GLN   B 42  ? 0.3840 0.4419 0.5770 0.0082  0.0444  -0.0643 48  GLN   C N   
1406 C CA  . GLN   B 42  ? 0.3968 0.4479 0.5709 0.0060  0.0489  -0.0650 48  GLN   C CA  
1407 C C   . GLN   B 42  ? 0.3857 0.4280 0.5482 0.0091  0.0397  -0.0596 48  GLN   C C   
1408 O O   . GLN   B 42  ? 0.3930 0.4337 0.5661 0.0142  0.0327  -0.0585 48  GLN   C O   
1409 C CB  . GLN   B 42  ? 0.4388 0.4909 0.6220 0.0069  0.0577  -0.0729 48  GLN   C CB  
1410 C CG  . GLN   B 42  ? 0.5215 0.5674 0.6840 0.0023  0.0644  -0.0747 48  GLN   C CG  
1411 C CD  . GLN   B 42  ? 0.6139 0.6636 0.7672 -0.0053 0.0737  -0.0766 48  GLN   C CD  
1412 O OE1 . GLN   B 42  ? 0.6292 0.6870 0.7942 -0.0072 0.0775  -0.0784 48  GLN   C OE1 
1413 N NE2 . GLN   B 42  ? 0.6453 0.6889 0.7772 -0.0104 0.0771  -0.0761 48  GLN   C NE2 
1414 N N   . GLY   B 43  ? 0.3613 0.3983 0.5027 0.0057  0.0396  -0.0559 49  GLY   C N   
1415 C CA  . GLY   B 43  ? 0.3437 0.3730 0.4724 0.0075  0.0325  -0.0510 49  GLY   C CA  
1416 C C   . GLY   B 43  ? 0.3288 0.3528 0.4506 0.0074  0.0363  -0.0539 49  GLY   C C   
1417 O O   . GLY   B 43  ? 0.3316 0.3564 0.4489 0.0036  0.0447  -0.0581 49  GLY   C O   
1418 N N   . CYS   B 44  ? 0.3122 0.3302 0.4321 0.0108  0.0301  -0.0515 50  CYS   C N   
1419 C CA  . CYS   B 44  ? 0.3106 0.3229 0.4254 0.0109  0.0329  -0.0543 50  CYS   C CA  
1420 C C   . CYS   B 44  ? 0.2958 0.3016 0.3921 0.0090  0.0296  -0.0496 50  CYS   C C   
1421 O O   . CYS   B 44  ? 0.3050 0.3050 0.3977 0.0095  0.0297  -0.0509 50  CYS   C O   
1422 C CB  . CYS   B 44  ? 0.3413 0.3516 0.4721 0.0164  0.0297  -0.0568 50  CYS   C CB  
1423 S SG  . CYS   B 44  ? 0.4151 0.4339 0.5717 0.0189  0.0350  -0.0638 50  CYS   C SG  
1424 N N   . ASP   B 45  ? 0.2580 0.2644 0.3437 0.0068  0.0266  -0.0442 51  ASP   C N   
1425 C CA  . ASP   B 45  ? 0.2573 0.2586 0.3275 0.0050  0.0240  -0.0400 51  ASP   C CA  
1426 C C   . ASP   B 45  ? 0.2628 0.2630 0.3223 0.0000  0.0303  -0.0423 51  ASP   C C   
1427 O O   . ASP   B 45  ? 0.2637 0.2677 0.3236 -0.0032 0.0358  -0.0449 51  ASP   C O   
1428 C CB  . ASP   B 45  ? 0.2781 0.2806 0.3417 0.0044  0.0194  -0.0344 51  ASP   C CB  
1429 C CG  . ASP   B 45  ? 0.3573 0.3588 0.4265 0.0082  0.0124  -0.0315 51  ASP   C CG  
1430 O OD1 . ASP   B 45  ? 0.3881 0.3869 0.4643 0.0112  0.0096  -0.0324 51  ASP   C OD1 
1431 O OD2 . ASP   B 45  ? 0.3484 0.3513 0.4147 0.0080  0.0095  -0.0283 51  ASP   C OD2 
1432 N N   . THR   B 46  ? 0.2527 0.2476 0.3026 -0.0014 0.0294  -0.0413 52  THR   C N   
1433 C CA  . THR   B 46  ? 0.2706 0.2634 0.3082 -0.0069 0.0338  -0.0424 52  THR   C CA  
1434 C C   . THR   B 46  ? 0.2527 0.2452 0.2790 -0.0093 0.0298  -0.0360 52  THR   C C   
1435 O O   . THR   B 46  ? 0.2593 0.2499 0.2844 -0.0071 0.0246  -0.0321 52  THR   C O   
1436 C CB  . THR   B 46  ? 0.3324 0.3190 0.3672 -0.0070 0.0346  -0.0453 52  THR   C CB  
1437 O OG1 . THR   B 46  ? 0.3670 0.3539 0.4134 -0.0047 0.0393  -0.0522 52  THR   C OG1 
1438 C CG2 . THR   B 46  ? 0.3544 0.3376 0.3740 -0.0132 0.0371  -0.0454 52  THR   C CG2 
1439 N N   . ILE   B 47  ? 0.2375 0.2316 0.2560 -0.0141 0.0322  -0.0349 53  ILE   C N   
1440 C CA  . ILE   B 47  ? 0.2341 0.2278 0.2438 -0.0163 0.0281  -0.0289 53  ILE   C CA  
1441 C C   . ILE   B 47  ? 0.2368 0.2261 0.2358 -0.0203 0.0278  -0.0282 53  ILE   C C   
1442 O O   . ILE   B 47  ? 0.2443 0.2312 0.2376 -0.0244 0.0322  -0.0321 53  ILE   C O   
1443 C CB  . ILE   B 47  ? 0.2435 0.2402 0.2502 -0.0198 0.0295  -0.0272 53  ILE   C CB  
1444 C CG1 . ILE   B 47  ? 0.2658 0.2669 0.2833 -0.0169 0.0305  -0.0285 53  ILE   C CG1 
1445 C CG2 . ILE   B 47  ? 0.2455 0.2416 0.2459 -0.0212 0.0245  -0.0208 53  ILE   C CG2 
1446 C CD1 . ILE   B 47  ? 0.2960 0.2981 0.3202 -0.0114 0.0250  -0.0257 53  ILE   C CD1 
1447 N N   . ALA   B 48  ? 0.2184 0.2066 0.2145 -0.0195 0.0227  -0.0235 54  ALA   C N   
1448 C CA  . ALA   B 48  ? 0.2163 0.2009 0.2031 -0.0235 0.0212  -0.0219 54  ALA   C CA  
1449 C C   . ALA   B 48  ? 0.2103 0.1950 0.1881 -0.0295 0.0213  -0.0195 54  ALA   C C   
1450 O O   . ALA   B 48  ? 0.2159 0.2037 0.1954 -0.0292 0.0197  -0.0162 54  ALA   C O   
1451 C CB  . ALA   B 48  ? 0.2103 0.1953 0.1985 -0.0213 0.0160  -0.0171 54  ALA   C CB  
1452 N N   . ARG   B 49  ? 0.2026 0.1830 0.1700 -0.0352 0.0223  -0.0208 55  ARG   C N   
1453 C CA  . ARG   B 49  ? 0.2062 0.1854 0.1628 -0.0420 0.0211  -0.0177 55  ARG   C CA  
1454 C C   . ARG   B 49  ? 0.2198 0.1958 0.1700 -0.0450 0.0164  -0.0148 55  ARG   C C   
1455 O O   . ARG   B 49  ? 0.2357 0.2067 0.1779 -0.0490 0.0183  -0.0182 55  ARG   C O   
1456 C CB  . ARG   B 49  ? 0.2192 0.1958 0.1682 -0.0471 0.0277  -0.0232 55  ARG   C CB  
1457 C CG  . ARG   B 49  ? 0.2227 0.2034 0.1805 -0.0440 0.0329  -0.0267 55  ARG   C CG  
1458 C CD  . ARG   B 49  ? 0.2278 0.2126 0.1894 -0.0431 0.0299  -0.0215 55  ARG   C CD  
1459 N NE  . ARG   B 49  ? 0.2493 0.2379 0.2190 -0.0411 0.0348  -0.0252 55  ARG   C NE  
1460 C CZ  . ARG   B 49  ? 0.2722 0.2646 0.2491 -0.0383 0.0329  -0.0223 55  ARG   C CZ  
1461 N NH1 . ARG   B 49  ? 0.2564 0.2490 0.2333 -0.0371 0.0266  -0.0162 55  ARG   C NH1 
1462 N NH2 . ARG   B 49  ? 0.2826 0.2786 0.2675 -0.0369 0.0373  -0.0259 55  ARG   C NH2 
1463 N N   . CYS   B 50  ? 0.2112 0.1901 0.1660 -0.0430 0.0106  -0.0088 56  CYS   C N   
1464 C CA  . CYS   B 50  ? 0.2134 0.1910 0.1661 -0.0447 0.0060  -0.0057 56  CYS   C CA  
1465 C C   . CYS   B 50  ? 0.2269 0.2091 0.1858 -0.0433 0.0002  0.0012  56  CYS   C C   
1466 O O   . CYS   B 50  ? 0.2247 0.2103 0.1892 -0.0405 0.0000  0.0030  56  CYS   C O   
1467 C CB  . CYS   B 50  ? 0.2125 0.1892 0.1709 -0.0403 0.0075  -0.0088 56  CYS   C CB  
1468 S SG  . CYS   B 50  ? 0.2111 0.1933 0.1829 -0.0321 0.0069  -0.0071 56  CYS   C SG  
1469 N N   . ASP   B 51  ? 0.2256 0.2080 0.1847 -0.0450 -0.0043 0.0045  57  ASP   C N   
1470 C CA  . ASP   B 51  ? 0.2359 0.2236 0.2038 -0.0430 -0.0091 0.0102  57  ASP   C CA  
1471 C C   . ASP   B 51  ? 0.2351 0.2254 0.2107 -0.0391 -0.0089 0.0102  57  ASP   C C   
1472 O O   . ASP   B 51  ? 0.2380 0.2320 0.2193 -0.0395 -0.0127 0.0144  57  ASP   C O   
1473 C CB  . ASP   B 51  ? 0.2604 0.2475 0.2242 -0.0490 -0.0154 0.0155  57  ASP   C CB  
1474 C CG  . ASP   B 51  ? 0.3473 0.3308 0.3039 -0.0543 -0.0178 0.0154  57  ASP   C CG  
1475 O OD1 . ASP   B 51  ? 0.3643 0.3448 0.3183 -0.0535 -0.0140 0.0108  57  ASP   C OD1 
1476 O OD2 . ASP   B 51  ? 0.4035 0.3866 0.3573 -0.0595 -0.0239 0.0201  57  ASP   C OD2 
1477 N N   . CYS   B 52  ? 0.2112 0.1997 0.1875 -0.0357 -0.0048 0.0058  58  CYS   C N   
1478 C CA  . CYS   B 52  ? 0.1935 0.1833 0.1753 -0.0326 -0.0046 0.0060  58  CYS   C CA  
1479 C C   . CYS   B 52  ? 0.1815 0.1776 0.1727 -0.0290 -0.0056 0.0094  58  CYS   C C   
1480 O O   . CYS   B 52  ? 0.1793 0.1778 0.1739 -0.0266 -0.0050 0.0098  58  CYS   C O   
1481 C CB  . CYS   B 52  ? 0.2019 0.1885 0.1839 -0.0290 -0.0008 0.0014  58  CYS   C CB  
1482 S SG  . CYS   B 52  ? 0.2350 0.2136 0.2089 -0.0323 0.0008  -0.0033 58  CYS   C SG  
1483 N N   . GLN   B 53  ? 0.1689 0.1675 0.1643 -0.0291 -0.0068 0.0116  59  GLN   C N   
1484 C CA  . GLN   B 53  ? 0.1746 0.1791 0.1791 -0.0258 -0.0063 0.0137  59  GLN   C CA  
1485 C C   . GLN   B 53  ? 0.1878 0.1916 0.1929 -0.0240 -0.0039 0.0126  59  GLN   C C   
1486 O O   . GLN   B 53  ? 0.1872 0.1957 0.1984 -0.0227 -0.0029 0.0143  59  GLN   C O   
1487 C CB  . GLN   B 53  ? 0.1777 0.1876 0.1891 -0.0280 -0.0097 0.0182  59  GLN   C CB  
1488 C CG  . GLN   B 53  ? 0.1933 0.2045 0.2066 -0.0287 -0.0127 0.0204  59  GLN   C CG  
1489 C CD  . GLN   B 53  ? 0.2253 0.2422 0.2481 -0.0303 -0.0170 0.0251  59  GLN   C CD  
1490 O OE1 . GLN   B 53  ? 0.2408 0.2565 0.2606 -0.0353 -0.0220 0.0279  59  GLN   C OE1 
1491 N NE2 . GLN   B 53  ? 0.2254 0.2484 0.2597 -0.0265 -0.0150 0.0257  59  GLN   C NE2 
1492 N N   . THR   B 54  ? 0.1826 0.1804 0.1814 -0.0241 -0.0029 0.0098  60  THR   C N   
1493 C CA  . THR   B 54  ? 0.2054 0.2009 0.2037 -0.0225 -0.0015 0.0091  60  THR   C CA  
1494 C C   . THR   B 54  ? 0.2027 0.1932 0.1980 -0.0196 -0.0002 0.0054  60  THR   C C   
1495 O O   . THR   B 54  ? 0.2156 0.2032 0.2082 -0.0203 0.0000  0.0029  60  THR   C O   
1496 C CB  . THR   B 54  ? 0.2637 0.2560 0.2590 -0.0262 -0.0029 0.0102  60  THR   C CB  
1497 O OG1 . THR   B 54  ? 0.2945 0.2805 0.2841 -0.0283 -0.0039 0.0077  60  THR   C OG1 
1498 C CG2 . THR   B 54  ? 0.2770 0.2749 0.2767 -0.0296 -0.0045 0.0139  60  THR   C CG2 
1499 N N   . GLY   B 55  ? 0.1770 0.1668 0.1732 -0.0168 0.0006  0.0052  61  GLY   C N   
1500 C CA  . GLY   B 55  ? 0.1807 0.1664 0.1762 -0.0138 0.0009  0.0022  61  GLY   C CA  
1501 C C   . GLY   B 55  ? 0.1744 0.1587 0.1694 -0.0119 0.0005  0.0031  61  GLY   C C   
1502 O O   . GLY   B 55  ? 0.1916 0.1768 0.1852 -0.0136 0.0006  0.0056  61  GLY   C O   
1503 N N   . VAL   B 56  ? 0.1632 0.1449 0.1591 -0.0091 -0.0001 0.0011  62  VAL   C N   
1504 C CA  . VAL   B 56  ? 0.1730 0.1519 0.1670 -0.0078 -0.0016 0.0021  62  VAL   C CA  
1505 C C   . VAL   B 56  ? 0.1823 0.1635 0.1789 -0.0048 -0.0013 0.0005  62  VAL   C C   
1506 O O   . VAL   B 56  ? 0.1739 0.1554 0.1743 -0.0031 -0.0011 -0.0020 62  VAL   C O   
1507 C CB  . VAL   B 56  ? 0.1861 0.1577 0.1794 -0.0074 -0.0046 0.0016  62  VAL   C CB  
1508 C CG1 . VAL   B 56  ? 0.2053 0.1731 0.1959 -0.0066 -0.0075 0.0033  62  VAL   C CG1 
1509 C CG2 . VAL   B 56  ? 0.1974 0.1658 0.1880 -0.0107 -0.0051 0.0030  62  VAL   C CG2 
1510 N N   . TYR   B 57  ? 0.1833 0.1654 0.1772 -0.0046 -0.0010 0.0017  63  TYR   C N   
1511 C CA  . TYR   B 57  ? 0.1882 0.1714 0.1838 -0.0022 -0.0013 0.0001  63  TYR   C CA  
1512 C C   . TYR   B 57  ? 0.1885 0.1668 0.1796 -0.0020 -0.0043 0.0009  63  TYR   C C   
1513 O O   . TYR   B 57  ? 0.1795 0.1546 0.1646 -0.0043 -0.0051 0.0031  63  TYR   C O   
1514 C CB  . TYR   B 57  ? 0.1839 0.1723 0.1807 -0.0019 0.0018  -0.0002 63  TYR   C CB  
1515 C CG  . TYR   B 57  ? 0.1914 0.1802 0.1838 -0.0032 0.0037  0.0009  63  TYR   C CG  
1516 C CD1 . TYR   B 57  ? 0.2182 0.2088 0.2096 -0.0056 0.0056  0.0028  63  TYR   C CD1 
1517 C CD2 . TYR   B 57  ? 0.2099 0.1977 0.1995 -0.0024 0.0040  -0.0003 63  TYR   C CD2 
1518 C CE1 . TYR   B 57  ? 0.2357 0.2278 0.2240 -0.0071 0.0086  0.0032  63  TYR   C CE1 
1519 C CE2 . TYR   B 57  ? 0.2257 0.2138 0.2104 -0.0040 0.0069  -0.0001 63  TYR   C CE2 
1520 C CZ  . TYR   B 57  ? 0.2468 0.2373 0.2312 -0.0063 0.0096  0.0015  63  TYR   C CZ  
1521 O OH  . TYR   B 57  ? 0.2733 0.2649 0.2537 -0.0084 0.0137  0.0012  63  TYR   C OH  
1522 N N   . TYR   B 58  ? 0.1866 0.1644 0.1804 0.0001  -0.0063 -0.0007 64  TYR   C N   
1523 C CA  . TYR   B 58  ? 0.1958 0.1689 0.1852 -0.0002 -0.0103 0.0003  64  TYR   C CA  
1524 C C   . TYR   B 58  ? 0.2086 0.1826 0.1922 -0.0011 -0.0084 0.0000  64  TYR   C C   
1525 O O   . TYR   B 58  ? 0.2004 0.1783 0.1878 0.0004  -0.0062 -0.0021 64  TYR   C O   
1526 C CB  . TYR   B 58  ? 0.2005 0.1723 0.1969 0.0023  -0.0143 -0.0011 64  TYR   C CB  
1527 C CG  . TYR   B 58  ? 0.2216 0.1878 0.2130 0.0015  -0.0199 0.0007  64  TYR   C CG  
1528 C CD1 . TYR   B 58  ? 0.2382 0.1980 0.2238 -0.0004 -0.0239 0.0038  64  TYR   C CD1 
1529 C CD2 . TYR   B 58  ? 0.2459 0.2126 0.2371 0.0020  -0.0217 -0.0003 64  TYR   C CD2 
1530 C CE1 . TYR   B 58  ? 0.2594 0.2132 0.2387 -0.0020 -0.0299 0.0062  64  TYR   C CE1 
1531 C CE2 . TYR   B 58  ? 0.2630 0.2239 0.2481 0.0004  -0.0277 0.0016  64  TYR   C CE2 
1532 C CZ  . TYR   B 58  ? 0.2840 0.2384 0.2629 -0.0017 -0.0319 0.0051  64  TYR   C CZ  
1533 O OH  . TYR   B 58  ? 0.3255 0.2734 0.2970 -0.0039 -0.0386 0.0076  64  TYR   C OH  
1534 N N   . CYS   B 59  ? 0.2113 0.1812 0.1853 -0.0039 -0.0091 0.0018  65  CYS   C N   
1535 C CA  . CYS   B 59  ? 0.2130 0.1829 0.1798 -0.0055 -0.0065 0.0009  65  CYS   C CA  
1536 C C   . CYS   B 59  ? 0.2394 0.2026 0.1985 -0.0069 -0.0119 0.0016  65  CYS   C C   
1537 O O   . CYS   B 59  ? 0.2605 0.2178 0.2110 -0.0100 -0.0151 0.0045  65  CYS   C O   
1538 C CB  . CYS   B 59  ? 0.2122 0.1829 0.1729 -0.0086 -0.0020 0.0021  65  CYS   C CB  
1539 S SG  . CYS   B 59  ? 0.2533 0.2233 0.2044 -0.0112 0.0028  0.0000  65  CYS   C SG  
1540 N N   . SER   B 60  ? 0.2303 0.1941 0.1926 -0.0051 -0.0138 -0.0005 66  SER   C N   
1541 C CA  . SER   B 60  ? 0.2662 0.2237 0.2221 -0.0067 -0.0202 0.0005  66  SER   C CA  
1542 C C   . SER   B 60  ? 0.2801 0.2320 0.2201 -0.0114 -0.0194 0.0011  66  SER   C C   
1543 O O   . SER   B 60  ? 0.2986 0.2434 0.2300 -0.0143 -0.0256 0.0040  66  SER   C O   
1544 C CB  . SER   B 60  ? 0.3216 0.2809 0.2843 -0.0044 -0.0223 -0.0019 66  SER   C CB  
1545 O OG  . SER   B 60  ? 0.4023 0.3649 0.3645 -0.0040 -0.0167 -0.0051 66  SER   C OG  
1546 N N   . SER   B 61  ? 0.2726 0.2275 0.2088 -0.0123 -0.0119 -0.0013 67  SER   C N   
1547 C CA  . SER   B 61  ? 0.2814 0.2313 0.2019 -0.0172 -0.0094 -0.0018 67  SER   C CA  
1548 C C   . SER   B 61  ? 0.2950 0.2412 0.2062 -0.0215 -0.0096 0.0020  67  SER   C C   
1549 O O   . SER   B 61  ? 0.3185 0.2597 0.2148 -0.0267 -0.0077 0.0021  67  SER   C O   
1550 C CB  . SER   B 61  ? 0.2770 0.2316 0.1983 -0.0166 -0.0005 -0.0062 67  SER   C CB  
1551 O OG  . SER   B 61  ? 0.2814 0.2430 0.2118 -0.0148 0.0050  -0.0061 67  SER   C OG  
1552 N N   . ARG   B 62  ? 0.2708 0.2187 0.1898 -0.0200 -0.0115 0.0049  68  ARG   C N   
1553 C CA  . ARG   B 62  ? 0.2787 0.2222 0.1903 -0.0240 -0.0130 0.0090  68  ARG   C CA  
1554 C C   . ARG   B 62  ? 0.2960 0.2341 0.2115 -0.0228 -0.0225 0.0129  68  ARG   C C   
1555 O O   . ARG   B 62  ? 0.3168 0.2497 0.2267 -0.0259 -0.0254 0.0169  68  ARG   C O   
1556 C CB  . ARG   B 62  ? 0.2877 0.2379 0.2056 -0.0236 -0.0062 0.0088  68  ARG   C CB  
1557 C CG  . ARG   B 62  ? 0.3169 0.2723 0.2323 -0.0250 0.0030  0.0054  68  ARG   C CG  
1558 C CD  . ARG   B 62  ? 0.3537 0.3034 0.2521 -0.0318 0.0054  0.0066  68  ARG   C CD  
1559 N NE  . ARG   B 62  ? 0.3950 0.3501 0.2923 -0.0332 0.0153  0.0025  68  ARG   C NE  
1560 C CZ  . ARG   B 62  ? 0.4534 0.4081 0.3464 -0.0330 0.0189  -0.0020 68  ARG   C CZ  
1561 N NH1 . ARG   B 62  ? 0.4538 0.4028 0.3423 -0.0320 0.0128  -0.0026 68  ARG   C NH1 
1562 N NH2 . ARG   B 62  ? 0.4566 0.4163 0.3506 -0.0339 0.0285  -0.0061 68  ARG   C NH2 
1563 N N   . ARG   B 63  ? 0.2889 0.2285 0.2154 -0.0182 -0.0270 0.0116  69  ARG   C N   
1564 C CA  . ARG   B 63  ? 0.3156 0.2520 0.2508 -0.0158 -0.0349 0.0140  69  ARG   C CA  
1565 C C   . ARG   B 63  ? 0.3212 0.2582 0.2614 -0.0153 -0.0334 0.0155  69  ARG   C C   
1566 O O   . ARG   B 63  ? 0.3376 0.2677 0.2756 -0.0168 -0.0392 0.0193  69  ARG   C O   
1567 C CB  . ARG   B 63  ? 0.3641 0.2908 0.2903 -0.0190 -0.0445 0.0181  69  ARG   C CB  
1568 C CG  . ARG   B 63  ? 0.4438 0.3686 0.3636 -0.0204 -0.0472 0.0168  69  ARG   C CG  
1569 C CD  . ARG   B 63  ? 0.5277 0.4542 0.4603 -0.0164 -0.0535 0.0157  69  ARG   C CD  
1570 N NE  . ARG   B 63  ? 0.6047 0.5302 0.5297 -0.0184 -0.0540 0.0136  69  ARG   C NE  
1571 C CZ  . ARG   B 63  ? 0.6513 0.5833 0.5803 -0.0162 -0.0474 0.0089  69  ARG   C CZ  
1572 N NH1 . ARG   B 63  ? 0.6425 0.5825 0.5836 -0.0120 -0.0408 0.0062  69  ARG   C NH1 
1573 N NH2 . ARG   B 63  ? 0.6799 0.6096 0.6009 -0.0185 -0.0483 0.0069  69  ARG   C NH2 
1574 N N   . LYS   B 64  ? 0.3000 0.2444 0.2453 -0.0139 -0.0257 0.0130  70  LYS   C N   
1575 C CA  . LYS   B 64  ? 0.2932 0.2382 0.2417 -0.0143 -0.0239 0.0143  70  LYS   C CA  
1576 C C   . LYS   B 64  ? 0.2602 0.2133 0.2199 -0.0108 -0.0187 0.0110  70  LYS   C C   
1577 O O   . LYS   B 64  ? 0.2456 0.2046 0.2081 -0.0092 -0.0147 0.0082  70  LYS   C O   
1578 C CB  . LYS   B 64  ? 0.3471 0.2917 0.2846 -0.0195 -0.0192 0.0162  70  LYS   C CB  
1579 C CG  . LYS   B 64  ? 0.4878 0.4232 0.4136 -0.0245 -0.0238 0.0209  70  LYS   C CG  
1580 C CD  . LYS   B 64  ? 0.5805 0.5180 0.4987 -0.0295 -0.0173 0.0220  70  LYS   C CD  
1581 C CE  . LYS   B 64  ? 0.6619 0.5901 0.5675 -0.0356 -0.0212 0.0272  70  LYS   C CE  
1582 N NZ  . LYS   B 64  ? 0.6998 0.6225 0.5898 -0.0403 -0.0223 0.0285  70  LYS   C NZ  
1583 N N   . HIS   B 65  ? 0.2401 0.1929 0.2049 -0.0104 -0.0189 0.0115  71  HIS   C N   
1584 C CA  . HIS   B 65  ? 0.2222 0.1816 0.1950 -0.0085 -0.0143 0.0090  71  HIS   C CA  
1585 C C   . HIS   B 65  ? 0.2427 0.2044 0.2113 -0.0120 -0.0101 0.0106  71  HIS   C C   
1586 O O   . HIS   B 65  ? 0.2730 0.2299 0.2352 -0.0155 -0.0116 0.0136  71  HIS   C O   
1587 C CB  . HIS   B 65  ? 0.2200 0.1769 0.2007 -0.0063 -0.0168 0.0079  71  HIS   C CB  
1588 C CG  . HIS   B 65  ? 0.2478 0.2038 0.2358 -0.0027 -0.0202 0.0058  71  HIS   C CG  
1589 N ND1 . HIS   B 65  ? 0.2663 0.2280 0.2626 0.0001  -0.0174 0.0022  71  HIS   C ND1 
1590 C CD2 . HIS   B 65  ? 0.2505 0.2007 0.2396 -0.0017 -0.0264 0.0073  71  HIS   C CD2 
1591 C CE1 . HIS   B 65  ? 0.2483 0.2083 0.2512 0.0027  -0.0212 0.0011  71  HIS   C CE1 
1592 N NE2 . HIS   B 65  ? 0.2685 0.2218 0.2681 0.0019  -0.0271 0.0041  71  HIS   C NE2 
1593 N N   . TYR   B 66  ? 0.2140 0.1832 0.1871 -0.0113 -0.0052 0.0088  72  TYR   C N   
1594 C CA  . TYR   B 66  ? 0.2103 0.1833 0.1825 -0.0143 -0.0014 0.0102  72  TYR   C CA  
1595 C C   . TYR   B 66  ? 0.1946 0.1718 0.1740 -0.0136 -0.0003 0.0093  72  TYR   C C   
1596 O O   . TYR   B 66  ? 0.1899 0.1706 0.1747 -0.0109 0.0004  0.0071  72  TYR   C O   
1597 C CB  . TYR   B 66  ? 0.2213 0.1999 0.1925 -0.0148 0.0035  0.0093  72  TYR   C CB  
1598 C CG  . TYR   B 66  ? 0.2557 0.2302 0.2170 -0.0171 0.0037  0.0100  72  TYR   C CG  
1599 C CD1 . TYR   B 66  ? 0.2751 0.2466 0.2287 -0.0219 0.0045  0.0128  72  TYR   C CD1 
1600 C CD2 . TYR   B 66  ? 0.2751 0.2483 0.2337 -0.0154 0.0032  0.0080  72  TYR   C CD2 
1601 C CE1 . TYR   B 66  ? 0.2981 0.2653 0.2404 -0.0252 0.0050  0.0136  72  TYR   C CE1 
1602 C CE2 . TYR   B 66  ? 0.3004 0.2690 0.2480 -0.0184 0.0032  0.0086  72  TYR   C CE2 
1603 C CZ  . TYR   B 66  ? 0.3263 0.2918 0.2651 -0.0235 0.0043  0.0113  72  TYR   C CZ  
1604 O OH  . TYR   B 66  ? 0.3652 0.3252 0.2906 -0.0275 0.0045  0.0120  72  TYR   C OH  
1605 N N   . PRO   B 67  ? 0.1988 0.1751 0.1775 -0.0167 -0.0004 0.0112  73  PRO   C N   
1606 C CA  . PRO   B 67  ? 0.1962 0.1763 0.1803 -0.0171 0.0003  0.0106  73  PRO   C CA  
1607 C C   . PRO   B 67  ? 0.2093 0.1979 0.1978 -0.0177 0.0041  0.0111  73  PRO   C C   
1608 O O   . PRO   B 67  ? 0.2216 0.2126 0.2086 -0.0198 0.0066  0.0126  73  PRO   C O   
1609 C CB  . PRO   B 67  ? 0.2135 0.1887 0.1945 -0.0208 -0.0016 0.0128  73  PRO   C CB  
1610 C CG  . PRO   B 67  ? 0.2277 0.2001 0.2025 -0.0232 -0.0015 0.0154  73  PRO   C CG  
1611 C CD  . PRO   B 67  ? 0.2064 0.1778 0.1785 -0.0207 -0.0015 0.0143  73  PRO   C CD  
1612 N N   . VAL   B 68  ? 0.1927 0.1859 0.1869 -0.0162 0.0044  0.0099  74  VAL   C N   
1613 C CA  . VAL   B 68  ? 0.2046 0.2055 0.2051 -0.0164 0.0069  0.0107  74  VAL   C CA  
1614 C C   . VAL   B 68  ? 0.2000 0.2038 0.2052 -0.0174 0.0052  0.0114  74  VAL   C C   
1615 O O   . VAL   B 68  ? 0.2104 0.2105 0.2131 -0.0172 0.0031  0.0101  74  VAL   C O   
1616 C CB  . VAL   B 68  ? 0.2240 0.2274 0.2269 -0.0128 0.0089  0.0087  74  VAL   C CB  
1617 C CG1 . VAL   B 68  ? 0.2571 0.2582 0.2545 -0.0127 0.0110  0.0080  74  VAL   C CG1 
1618 C CG2 . VAL   B 68  ? 0.2108 0.2120 0.2139 -0.0102 0.0070  0.0068  74  VAL   C CG2 
1619 N N   . SER   B 69  ? 0.1828 0.1934 0.1949 -0.0186 0.0061  0.0132  75  SER   C N   
1620 C CA  . SER   B 69  ? 0.1839 0.1980 0.2014 -0.0195 0.0037  0.0145  75  SER   C CA  
1621 C C   . SER   B 69  ? 0.1765 0.1936 0.1990 -0.0156 0.0049  0.0133  75  SER   C C   
1622 O O   . SER   B 69  ? 0.1705 0.1897 0.1954 -0.0133 0.0081  0.0121  75  SER   C O   
1623 C CB  . SER   B 69  ? 0.2087 0.2292 0.2338 -0.0224 0.0034  0.0175  75  SER   C CB  
1624 O OG  . SER   B 69  ? 0.2680 0.2856 0.2888 -0.0264 0.0022  0.0187  75  SER   C OG  
1625 N N   . PHE   B 70  ? 0.1594 0.1762 0.1829 -0.0155 0.0022  0.0137  76  PHE   C N   
1626 C CA  . PHE   B 70  ? 0.1606 0.1793 0.1888 -0.0124 0.0026  0.0131  76  PHE   C CA  
1627 C C   . PHE   B 70  ? 0.1582 0.1794 0.1915 -0.0139 -0.0012 0.0159  76  PHE   C C   
1628 O O   . PHE   B 70  ? 0.1763 0.1960 0.2061 -0.0177 -0.0043 0.0177  76  PHE   C O   
1629 C CB  . PHE   B 70  ? 0.1624 0.1762 0.1846 -0.0101 0.0034  0.0102  76  PHE   C CB  
1630 C CG  . PHE   B 70  ? 0.1571 0.1661 0.1722 -0.0121 0.0018  0.0092  76  PHE   C CG  
1631 C CD1 . PHE   B 70  ? 0.1603 0.1651 0.1697 -0.0129 0.0022  0.0078  76  PHE   C CD1 
1632 C CD2 . PHE   B 70  ? 0.1609 0.1691 0.1749 -0.0133 0.0000  0.0095  76  PHE   C CD2 
1633 C CE1 . PHE   B 70  ? 0.1666 0.1669 0.1709 -0.0143 0.0016  0.0059  76  PHE   C CE1 
1634 C CE2 . PHE   B 70  ? 0.1664 0.1702 0.1736 -0.0155 -0.0002 0.0078  76  PHE   C CE2 
1635 C CZ  . PHE   B 70  ? 0.1666 0.1667 0.1697 -0.0156 0.0009  0.0056  76  PHE   C CZ  
1636 N N   . SER   B 71  ? 0.1427 0.1668 0.1837 -0.0113 -0.0014 0.0165  77  SER   C N   
1637 C CA  . SER   B 71  ? 0.1520 0.1782 0.1990 -0.0129 -0.0061 0.0201  77  SER   C CA  
1638 C C   . SER   B 71  ? 0.1773 0.1982 0.2161 -0.0151 -0.0091 0.0207  77  SER   C C   
1639 O O   . SER   B 71  ? 0.1844 0.2008 0.2142 -0.0150 -0.0070 0.0177  77  SER   C O   
1640 C CB  . SER   B 71  ? 0.1523 0.1831 0.2124 -0.0091 -0.0054 0.0206  77  SER   C CB  
1641 O OG  . SER   B 71  ? 0.1799 0.2074 0.2378 -0.0060 -0.0036 0.0181  77  SER   C OG  
1642 N N   . LYS   B 72  ? 0.1704 0.1920 0.2124 -0.0174 -0.0142 0.0246  78  LYS   C N   
1643 C CA  . LYS   B 72  ? 0.1912 0.2076 0.2247 -0.0203 -0.0168 0.0255  78  LYS   C CA  
1644 C C   . LYS   B 72  ? 0.1921 0.2075 0.2290 -0.0167 -0.0157 0.0246  78  LYS   C C   
1645 O O   . LYS   B 72  ? 0.2061 0.2249 0.2541 -0.0127 -0.0152 0.0248  78  LYS   C O   
1646 C CB  . LYS   B 72  ? 0.2251 0.2415 0.2593 -0.0251 -0.0237 0.0308  78  LYS   C CB  
1647 C CG  . LYS   B 72  ? 0.2861 0.3029 0.3164 -0.0293 -0.0253 0.0316  78  LYS   C CG  
1648 C CD  . LYS   B 72  ? 0.4079 0.4223 0.4334 -0.0356 -0.0325 0.0362  78  LYS   C CD  
1649 C CE  . LYS   B 72  ? 0.5014 0.5161 0.5237 -0.0399 -0.0345 0.0370  78  LYS   C CE  
1650 N NZ  . LYS   B 72  ? 0.5634 0.5772 0.5847 -0.0459 -0.0430 0.0427  78  LYS   C NZ  
1651 N N   . PRO   B 73  ? 0.1961 0.2069 0.2242 -0.0183 -0.0151 0.0233  79  PRO   C N   
1652 C CA  . PRO   B 73  ? 0.2093 0.2187 0.2404 -0.0154 -0.0142 0.0225  79  PRO   C CA  
1653 C C   . PRO   B 73  ? 0.2308 0.2411 0.2715 -0.0148 -0.0190 0.0269  79  PRO   C C   
1654 O O   . PRO   B 73  ? 0.2408 0.2502 0.2804 -0.0189 -0.0245 0.0315  79  PRO   C O   
1655 C CB  . PRO   B 73  ? 0.2261 0.2309 0.2460 -0.0191 -0.0134 0.0213  79  PRO   C CB  
1656 C CG  . PRO   B 73  ? 0.2387 0.2424 0.2501 -0.0222 -0.0117 0.0194  79  PRO   C CG  
1657 C CD  . PRO   B 73  ? 0.2069 0.2134 0.2222 -0.0229 -0.0144 0.0219  79  PRO   C CD  
1658 N N   . SER   B 74  ? 0.2234 0.2353 0.2739 -0.0097 -0.0174 0.0255  80  SER   C N   
1659 C CA  . SER   B 74  ? 0.2406 0.2536 0.3031 -0.0082 -0.0219 0.0293  80  SER   C CA  
1660 C C   . SER   B 74  ? 0.2203 0.2318 0.2896 -0.0034 -0.0196 0.0267  80  SER   C C   
1661 O O   . SER   B 74  ? 0.2093 0.2193 0.2731 -0.0017 -0.0148 0.0222  80  SER   C O   
1662 C CB  . SER   B 74  ? 0.2874 0.3063 0.3609 -0.0071 -0.0231 0.0309  80  SER   C CB  
1663 O OG  . SER   B 74  ? 0.3391 0.3620 0.4179 -0.0027 -0.0168 0.0263  80  SER   C OG  
1664 N N   . LEU   B 75  ? 0.2092 0.2204 0.2903 -0.0016 -0.0240 0.0299  81  LEU   C N   
1665 C CA  . LEU   B 75  ? 0.2162 0.2250 0.3050 0.0028  -0.0226 0.0277  81  LEU   C CA  
1666 C C   . LEU   B 75  ? 0.2129 0.2271 0.3135 0.0081  -0.0175 0.0236  81  LEU   C C   
1667 O O   . LEU   B 75  ? 0.2067 0.2258 0.3200 0.0093  -0.0195 0.0258  81  LEU   C O   
1668 C CB  . LEU   B 75  ? 0.2387 0.2444 0.3362 0.0022  -0.0301 0.0334  81  LEU   C CB  
1669 C CG  . LEU   B 75  ? 0.3123 0.3106 0.4009 -0.0014 -0.0339 0.0362  81  LEU   C CG  
1670 C CD1 . LEU   B 75  ? 0.3427 0.3377 0.4412 -0.0022 -0.0426 0.0429  81  LEU   C CD1 
1671 C CD2 . LEU   B 75  ? 0.3188 0.3136 0.4051 0.0014  -0.0290 0.0311  81  LEU   C CD2 
1672 N N   . ILE   B 76  ? 0.1984 0.2117 0.2952 0.0108  -0.0111 0.0177  82  ILE   C N   
1673 C CA  . ILE   B 76  ? 0.2117 0.2292 0.3162 0.0147  -0.0051 0.0131  82  ILE   C CA  
1674 C C   . ILE   B 76  ? 0.2096 0.2233 0.3175 0.0187  -0.0017 0.0083  82  ILE   C C   
1675 O O   . ILE   B 76  ? 0.2011 0.2095 0.2993 0.0179  -0.0014 0.0067  82  ILE   C O   
1676 C CB  . ILE   B 76  ? 0.2432 0.2630 0.3364 0.0129  -0.0004 0.0104  82  ILE   C CB  
1677 C CG1 . ILE   B 76  ? 0.2837 0.3073 0.3757 0.0092  -0.0037 0.0147  82  ILE   C CG1 
1678 C CG2 . ILE   B 76  ? 0.2595 0.2821 0.3561 0.0159  0.0068  0.0050  82  ILE   C CG2 
1679 C CD1 . ILE   B 76  ? 0.3357 0.3602 0.4167 0.0070  -0.0006 0.0131  82  ILE   C CD1 
1680 N N   . PHE   B 77  ? 0.2068 0.2233 0.3290 0.0228  0.0012  0.0058  83  PHE   C N   
1681 C CA  . PHE   B 77  ? 0.2242 0.2362 0.3496 0.0264  0.0049  0.0005  83  PHE   C CA  
1682 C C   . PHE   B 77  ? 0.2374 0.2477 0.3495 0.0260  0.0115  -0.0055 83  PHE   C C   
1683 O O   . PHE   B 77  ? 0.2522 0.2670 0.3606 0.0250  0.0159  -0.0072 83  PHE   C O   
1684 C CB  . PHE   B 77  ? 0.2373 0.2529 0.3825 0.0310  0.0074  -0.0017 83  PHE   C CB  
1685 C CG  . PHE   B 77  ? 0.2638 0.2737 0.4133 0.0348  0.0109  -0.0074 83  PHE   C CG  
1686 C CD1 . PHE   B 77  ? 0.2898 0.3005 0.4379 0.0367  0.0198  -0.0150 83  PHE   C CD1 
1687 C CD2 . PHE   B 77  ? 0.2882 0.2909 0.4405 0.0357  0.0054  -0.0054 83  PHE   C CD2 
1688 C CE1 . PHE   B 77  ? 0.3074 0.3119 0.4583 0.0398  0.0233  -0.0210 83  PHE   C CE1 
1689 C CE2 . PHE   B 77  ? 0.3096 0.3060 0.4653 0.0390  0.0086  -0.0110 83  PHE   C CE2 
1690 C CZ  . PHE   B 77  ? 0.3093 0.3066 0.4642 0.0411  0.0175  -0.0190 83  PHE   C CZ  
1691 N N   . VAL   B 78  ? 0.2411 0.2444 0.3457 0.0261  0.0116  -0.0081 84  VAL   C N   
1692 C CA  . VAL   B 78  ? 0.2481 0.2486 0.3400 0.0254  0.0165  -0.0135 84  VAL   C CA  
1693 C C   . VAL   B 78  ? 0.2628 0.2576 0.3581 0.0283  0.0194  -0.0191 84  VAL   C C   
1694 O O   . VAL   B 78  ? 0.2578 0.2476 0.3572 0.0292  0.0155  -0.0179 84  VAL   C O   
1695 C CB  . VAL   B 78  ? 0.2486 0.2460 0.3265 0.0219  0.0131  -0.0115 84  VAL   C CB  
1696 C CG1 . VAL   B 78  ? 0.2636 0.2577 0.3294 0.0211  0.0168  -0.0165 84  VAL   C CG1 
1697 C CG2 . VAL   B 78  ? 0.2444 0.2464 0.3187 0.0190  0.0106  -0.0068 84  VAL   C CG2 
1698 N N   . GLU   B 79  ? 0.2836 0.2784 0.3759 0.0292  0.0265  -0.0253 85  GLU   C N   
1699 C CA  . GLU   B 79  ? 0.2914 0.2803 0.3853 0.0316  0.0304  -0.0318 85  GLU   C CA  
1700 C C   . GLU   B 79  ? 0.2776 0.2583 0.3602 0.0298  0.0272  -0.0329 85  GLU   C C   
1701 O O   . GLU   B 79  ? 0.2647 0.2452 0.3356 0.0265  0.0243  -0.0303 85  GLU   C O   
1702 C CB  . GLU   B 79  ? 0.3519 0.3421 0.4398 0.0311  0.0390  -0.0382 85  GLU   C CB  
1703 C CG  . GLU   B 79  ? 0.4575 0.4567 0.5550 0.0318  0.0433  -0.0375 85  GLU   C CG  
1704 C CD  . GLU   B 79  ? 0.5661 0.5679 0.6829 0.0363  0.0477  -0.0411 85  GLU   C CD  
1705 O OE1 . GLU   B 79  ? 0.5912 0.6014 0.7188 0.0370  0.0509  -0.0403 85  GLU   C OE1 
1706 O OE2 . GLU   B 79  ? 0.5828 0.5784 0.7050 0.0392  0.0479  -0.0448 85  GLU   C OE2 
1707 N N   . ALA   B 80  ? 0.2786 0.2525 0.3654 0.0320  0.0280  -0.0371 86  ALA   C N   
1708 C CA  . ALA   B 80  ? 0.2800 0.2459 0.3569 0.0300  0.0249  -0.0385 86  ALA   C CA  
1709 C C   . ALA   B 80  ? 0.2796 0.2439 0.3393 0.0266  0.0274  -0.0418 86  ALA   C C   
1710 O O   . ALA   B 80  ? 0.2832 0.2497 0.3381 0.0263  0.0332  -0.0454 86  ALA   C O   
1711 C CB  . ALA   B 80  ? 0.2891 0.2473 0.3730 0.0328  0.0264  -0.0436 86  ALA   C CB  
1712 N N   . SER   B 81  ? 0.2623 0.2231 0.3129 0.0238  0.0226  -0.0400 87  SER   C N   
1713 C CA  . SER   B 81  ? 0.2592 0.2173 0.2944 0.0204  0.0228  -0.0424 87  SER   C CA  
1714 C C   . SER   B 81  ? 0.2839 0.2345 0.3155 0.0189  0.0186  -0.0438 87  SER   C C   
1715 O O   . SER   B 81  ? 0.2935 0.2412 0.3341 0.0204  0.0162  -0.0427 87  SER   C O   
1716 C CB  . SER   B 81  ? 0.2519 0.2157 0.2817 0.0180  0.0199  -0.0372 87  SER   C CB  
1717 O OG  . SER   B 81  ? 0.2397 0.2047 0.2738 0.0173  0.0143  -0.0323 87  SER   C OG  
1718 N N   . GLU   B 82  ? 0.2827 0.2297 0.3015 0.0156  0.0172  -0.0457 88  GLU   C N   
1719 C CA  . GLU   B 82  ? 0.3037 0.2444 0.3192 0.0134  0.0124  -0.0465 88  GLU   C CA  
1720 C C   . GLU   B 82  ? 0.2969 0.2415 0.3194 0.0127  0.0069  -0.0401 88  GLU   C C   
1721 O O   . GLU   B 82  ? 0.2983 0.2385 0.3230 0.0114  0.0034  -0.0399 88  GLU   C O   
1722 C CB  . GLU   B 82  ? 0.3614 0.2993 0.3625 0.0095  0.0104  -0.0482 88  GLU   C CB  
1723 C CG  . GLU   B 82  ? 0.4627 0.3929 0.4526 0.0080  0.0141  -0.0552 88  GLU   C CG  
1724 C CD  . GLU   B 82  ? 0.6007 0.5288 0.5764 0.0035  0.0101  -0.0549 88  GLU   C CD  
1725 O OE1 . GLU   B 82  ? 0.6082 0.5301 0.5786 0.0008  0.0057  -0.0566 88  GLU   C OE1 
1726 O OE2 . GLU   B 82  ? 0.6620 0.5947 0.6329 0.0026  0.0104  -0.0523 88  GLU   C OE2 
1727 N N   . TYR   B 83  ? 0.2859 0.2382 0.3110 0.0129  0.0066  -0.0354 89  TYR   C N   
1728 C CA  . TYR   B 83  ? 0.2821 0.2385 0.3117 0.0115  0.0026  -0.0299 89  TYR   C CA  
1729 C C   . TYR   B 83  ? 0.2777 0.2352 0.3175 0.0129  0.0018  -0.0262 89  TYR   C C   
1730 O O   . TYR   B 83  ? 0.2899 0.2480 0.3324 0.0108  -0.0015 -0.0225 89  TYR   C O   
1731 C CB  . TYR   B 83  ? 0.2916 0.2545 0.3175 0.0105  0.0026  -0.0272 89  TYR   C CB  
1732 C CG  . TYR   B 83  ? 0.3256 0.2871 0.3415 0.0089  0.0021  -0.0297 89  TYR   C CG  
1733 C CD1 . TYR   B 83  ? 0.3500 0.3103 0.3631 0.0064  -0.0021 -0.0295 89  TYR   C CD1 
1734 C CD2 . TYR   B 83  ? 0.3444 0.3063 0.3542 0.0094  0.0055  -0.0315 89  TYR   C CD2 
1735 C CE1 . TYR   B 83  ? 0.3725 0.3310 0.3768 0.0046  -0.0039 -0.0310 89  TYR   C CE1 
1736 C CE2 . TYR   B 83  ? 0.3706 0.3306 0.3701 0.0072  0.0042  -0.0329 89  TYR   C CE2 
1737 C CZ  . TYR   B 83  ? 0.3944 0.3525 0.3912 0.0049  -0.0010 -0.0324 89  TYR   C CZ  
1738 O OH  . TYR   B 83  ? 0.4412 0.3968 0.4283 0.0025  -0.0037 -0.0330 89  TYR   C OH  
1739 N N   . TYR   B 84  ? 0.2628 0.2213 0.3085 0.0160  0.0047  -0.0268 90  TYR   C N   
1740 C CA  . TYR   B 84  ? 0.2574 0.2171 0.3134 0.0173  0.0029  -0.0225 90  TYR   C CA  
1741 C C   . TYR   B 84  ? 0.2732 0.2300 0.3380 0.0212  0.0054  -0.0254 90  TYR   C C   
1742 O O   . TYR   B 84  ? 0.2767 0.2343 0.3404 0.0231  0.0105  -0.0301 90  TYR   C O   
1743 C CB  . TYR   B 84  ? 0.2350 0.2024 0.2924 0.0170  0.0030  -0.0181 90  TYR   C CB  
1744 C CG  . TYR   B 84  ? 0.2290 0.1999 0.2799 0.0135  0.0010  -0.0151 90  TYR   C CG  
1745 C CD1 . TYR   B 84  ? 0.2291 0.2039 0.2733 0.0129  0.0029  -0.0161 90  TYR   C CD1 
1746 C CD2 . TYR   B 84  ? 0.2312 0.2012 0.2829 0.0107  -0.0025 -0.0113 90  TYR   C CD2 
1747 C CE1 . TYR   B 84  ? 0.2186 0.1966 0.2589 0.0103  0.0014  -0.0138 90  TYR   C CE1 
1748 C CE2 . TYR   B 84  ? 0.2333 0.2070 0.2802 0.0076  -0.0032 -0.0093 90  TYR   C CE2 
1749 C CZ  . TYR   B 84  ? 0.2296 0.2074 0.2716 0.0078  -0.0013 -0.0108 90  TYR   C CZ  
1750 O OH  . TYR   B 84  ? 0.2292 0.2103 0.2682 0.0052  -0.0018 -0.0096 90  TYR   C OH  
1751 N N   . PRO   B 85  ? 0.2820 0.2360 0.3569 0.0223  0.0021  -0.0223 91  PRO   C N   
1752 C CA  . PRO   B 85  ? 0.2741 0.2268 0.3610 0.0267  0.0042  -0.0244 91  PRO   C CA  
1753 C C   . PRO   B 85  ? 0.2708 0.2322 0.3633 0.0282  0.0062  -0.0220 91  PRO   C C   
1754 O O   . PRO   B 85  ? 0.2670 0.2338 0.3546 0.0256  0.0044  -0.0175 91  PRO   C O   
1755 C CB  . PRO   B 85  ? 0.2852 0.2329 0.3812 0.0266  -0.0018 -0.0195 91  PRO   C CB  
1756 C CG  . PRO   B 85  ? 0.2977 0.2481 0.3867 0.0218  -0.0063 -0.0131 91  PRO   C CG  
1757 C CD  . PRO   B 85  ? 0.2748 0.2275 0.3510 0.0193  -0.0037 -0.0160 91  PRO   C CD  
1758 N N   . ALA   B 86  ? 0.2640 0.2267 0.3679 0.0324  0.0098  -0.0249 92  ALA   C N   
1759 C CA  . ALA   B 86  ? 0.2697 0.2409 0.3824 0.0339  0.0109  -0.0223 92  ALA   C CA  
1760 C C   . ALA   B 86  ? 0.2675 0.2400 0.3852 0.0321  0.0030  -0.0135 92  ALA   C C   
1761 O O   . ALA   B 86  ? 0.2660 0.2322 0.3876 0.0318  -0.0021 -0.0109 92  ALA   C O   
1762 C CB  . ALA   B 86  ? 0.2717 0.2434 0.4001 0.0389  0.0153  -0.0268 92  ALA   C CB  
1763 N N   . ARG   B 87  ? 0.2586 0.2380 0.3732 0.0298  0.0018  -0.0092 93  ARG   C N   
1764 C CA  . ARG   B 87  ? 0.2495 0.2293 0.3641 0.0266  -0.0055 -0.0013 93  ARG   C CA  
1765 C C   . ARG   B 87  ? 0.2599 0.2474 0.3726 0.0246  -0.0057 0.0022  93  ARG   C C   
1766 O O   . ARG   B 87  ? 0.2718 0.2642 0.3811 0.0252  -0.0004 -0.0013 93  ARG   C O   
1767 C CB  . ARG   B 87  ? 0.2534 0.2285 0.3543 0.0223  -0.0076 -0.0001 93  ARG   C CB  
1768 C CG  . ARG   B 87  ? 0.2204 0.1997 0.3078 0.0196  -0.0043 -0.0018 93  ARG   C CG  
1769 C CD  . ARG   B 87  ? 0.2363 0.2115 0.3133 0.0169  -0.0043 -0.0036 93  ARG   C CD  
1770 N NE  . ARG   B 87  ? 0.2349 0.2136 0.3020 0.0133  -0.0043 -0.0019 93  ARG   C NE  
1771 C CZ  . ARG   B 87  ? 0.2561 0.2388 0.3173 0.0134  -0.0010 -0.0044 93  ARG   C CZ  
1772 N NH1 . ARG   B 87  ? 0.2352 0.2203 0.2891 0.0103  -0.0013 -0.0030 93  ARG   C NH1 
1773 N NH2 . ARG   B 87  ? 0.2510 0.2349 0.3138 0.0163  0.0030  -0.0083 93  ARG   C NH2 
1774 N N   . TYR   B 88  ? 0.2592 0.2471 0.3716 0.0213  -0.0121 0.0092  94  TYR   C N   
1775 C CA  . TYR   B 88  ? 0.2626 0.2566 0.3705 0.0184  -0.0128 0.0123  94  TYR   C CA  
1776 C C   . TYR   B 88  ? 0.2282 0.2208 0.3196 0.0139  -0.0123 0.0124  94  TYR   C C   
1777 O O   . TYR   B 88  ? 0.2355 0.2232 0.3216 0.0110  -0.0156 0.0149  94  TYR   C O   
1778 C CB  . TYR   B 88  ? 0.2905 0.2852 0.4060 0.0166  -0.0202 0.0196  94  TYR   C CB  
1779 C CG  . TYR   B 88  ? 0.3330 0.3313 0.4674 0.0212  -0.0207 0.0196  94  TYR   C CG  
1780 C CD1 . TYR   B 88  ? 0.3553 0.3616 0.4958 0.0221  -0.0182 0.0191  94  TYR   C CD1 
1781 C CD2 . TYR   B 88  ? 0.3657 0.3595 0.5132 0.0248  -0.0232 0.0196  94  TYR   C CD2 
1782 C CE1 . TYR   B 88  ? 0.3764 0.3872 0.5365 0.0265  -0.0180 0.0186  94  TYR   C CE1 
1783 C CE2 . TYR   B 88  ? 0.3797 0.3773 0.5472 0.0297  -0.0231 0.0189  94  TYR   C CE2 
1784 C CZ  . TYR   B 88  ? 0.3940 0.4007 0.5682 0.0305  -0.0201 0.0182  94  TYR   C CZ  
1785 O OH  . TYR   B 88  ? 0.4311 0.4429 0.6269 0.0352  -0.0194 0.0173  94  TYR   C OH  
1786 N N   . GLN   B 89  ? 0.1904 0.1870 0.2745 0.0134  -0.0079 0.0096  95  GLN   C N   
1787 C CA  . GLN   B 89  ? 0.1817 0.1777 0.2526 0.0096  -0.0074 0.0096  95  GLN   C CA  
1788 C C   . GLN   B 89  ? 0.1800 0.1787 0.2478 0.0058  -0.0105 0.0143  95  GLN   C C   
1789 O O   . GLN   B 89  ? 0.1987 0.2019 0.2713 0.0065  -0.0105 0.0154  95  GLN   C O   
1790 C CB  . GLN   B 89  ? 0.1840 0.1817 0.2486 0.0109  -0.0020 0.0045  95  GLN   C CB  
1791 C CG  . GLN   B 89  ? 0.1938 0.1915 0.2473 0.0075  -0.0017 0.0044  95  GLN   C CG  
1792 C CD  . GLN   B 89  ? 0.2088 0.2060 0.2567 0.0087  0.0017  -0.0003 95  GLN   C CD  
1793 O OE1 . GLN   B 89  ? 0.2162 0.2106 0.2653 0.0109  0.0032  -0.0035 95  GLN   C OE1 
1794 N NE2 . GLN   B 89  ? 0.1778 0.1766 0.2191 0.0070  0.0026  -0.0006 95  GLN   C NE2 
1795 N N   . SER   B 90  ? 0.1659 0.1619 0.2256 0.0013  -0.0130 0.0170  96  SER   C N   
1796 C CA  . SER   B 90  ? 0.1658 0.1630 0.2202 -0.0032 -0.0159 0.0211  96  SER   C CA  
1797 C C   . SER   B 90  ? 0.1725 0.1717 0.2172 -0.0051 -0.0122 0.0183  96  SER   C C   
1798 O O   . SER   B 90  ? 0.1857 0.1849 0.2275 -0.0034 -0.0082 0.0139  96  SER   C O   
1799 C CB  . SER   B 90  ? 0.1914 0.1838 0.2411 -0.0080 -0.0204 0.0255  96  SER   C CB  
1800 O OG  . SER   B 90  ? 0.2155 0.2053 0.2581 -0.0097 -0.0177 0.0230  96  SER   C OG  
1801 N N   . HIS   B 91  ? 0.1708 0.1714 0.2110 -0.0088 -0.0140 0.0210  97  HIS   C N   
1802 C CA  . HIS   B 91  ? 0.1699 0.1715 0.2012 -0.0110 -0.0110 0.0185  97  HIS   C CA  
1803 C C   . HIS   B 91  ? 0.1884 0.1929 0.2221 -0.0069 -0.0068 0.0143  97  HIS   C C   
1804 O O   . HIS   B 91  ? 0.1902 0.1944 0.2182 -0.0071 -0.0038 0.0111  97  HIS   C O   
1805 C CB  . HIS   B 91  ? 0.1797 0.1783 0.2026 -0.0142 -0.0091 0.0168  97  HIS   C CB  
1806 C CG  . HIS   B 91  ? 0.2193 0.2145 0.2371 -0.0196 -0.0126 0.0210  97  HIS   C CG  
1807 N ND1 . HIS   B 91  ? 0.2596 0.2536 0.2682 -0.0252 -0.0134 0.0225  97  HIS   C ND1 
1808 C CD2 . HIS   B 91  ? 0.2490 0.2410 0.2689 -0.0207 -0.0157 0.0241  97  HIS   C CD2 
1809 C CE1 . HIS   B 91  ? 0.2767 0.2668 0.2808 -0.0300 -0.0168 0.0265  97  HIS   C CE1 
1810 N NE2 . HIS   B 91  ? 0.2741 0.2629 0.2852 -0.0275 -0.0186 0.0279  97  HIS   C NE2 
1811 N N   . LEU   B 92  ? 0.1857 0.1929 0.2280 -0.0033 -0.0066 0.0144  98  LEU   C N   
1812 C CA  . LEU   B 92  ? 0.1779 0.1873 0.2213 -0.0002 -0.0026 0.0108  98  LEU   C CA  
1813 C C   . LEU   B 92  ? 0.1779 0.1909 0.2223 -0.0015 -0.0026 0.0122  98  LEU   C C   
1814 O O   . LEU   B 92  ? 0.1826 0.1979 0.2330 -0.0026 -0.0058 0.0158  98  LEU   C O   
1815 C CB  . LEU   B 92  ? 0.1807 0.1906 0.2325 0.0039  -0.0010 0.0090  98  LEU   C CB  
1816 C CG  . LEU   B 92  ? 0.2101 0.2210 0.2610 0.0065  0.0037  0.0049  98  LEU   C CG  
1817 C CD1 . LEU   B 92  ? 0.2142 0.2218 0.2560 0.0062  0.0051  0.0020  98  LEU   C CD1 
1818 C CD2 . LEU   B 92  ? 0.2328 0.2436 0.2918 0.0101  0.0058  0.0026  98  LEU   C CD2 
1819 N N   . MET   B 93  ? 0.1615 0.1748 0.2008 -0.0014 0.0003  0.0098  99  MET   C N   
1820 C CA  . MET   B 93  ? 0.1604 0.1765 0.1999 -0.0030 0.0004  0.0110  99  MET   C CA  
1821 C C   . MET   B 93  ? 0.1697 0.1876 0.2110 -0.0006 0.0044  0.0085  99  MET   C C   
1822 O O   . MET   B 93  ? 0.1784 0.1934 0.2145 0.0007  0.0066  0.0056  99  MET   C O   
1823 C CB  . MET   B 93  ? 0.1574 0.1705 0.1874 -0.0060 0.0001  0.0105  99  MET   C CB  
1824 C CG  . MET   B 93  ? 0.1924 0.2033 0.2185 -0.0093 -0.0029 0.0123  99  MET   C CG  
1825 S SD  . MET   B 93  ? 0.2288 0.2358 0.2445 -0.0124 -0.0018 0.0100  99  MET   C SD  
1826 C CE  . MET   B 93  ? 0.2421 0.2473 0.2569 -0.0087 0.0016  0.0056  99  MET   C CE  
1827 N N   . LEU   B 94  ? 0.1511 0.1736 0.1994 -0.0007 0.0054  0.0098  100 LEU   C N   
1828 C CA  . LEU   B 94  ? 0.1548 0.1791 0.2038 0.0007  0.0101  0.0073  100 LEU   C CA  
1829 C C   . LEU   B 94  ? 0.1597 0.1847 0.2039 -0.0022 0.0109  0.0081  100 LEU   C C   
1830 O O   . LEU   B 94  ? 0.1495 0.1760 0.1947 -0.0049 0.0080  0.0109  100 LEU   C O   
1831 C CB  . LEU   B 94  ? 0.1689 0.1986 0.2307 0.0028  0.0124  0.0071  100 LEU   C CB  
1832 C CG  . LEU   B 94  ? 0.1939 0.2226 0.2624 0.0061  0.0119  0.0059  100 LEU   C CG  
1833 C CD1 . LEU   B 94  ? 0.1961 0.2304 0.2797 0.0087  0.0147  0.0052  100 LEU   C CD1 
1834 C CD2 . LEU   B 94  ? 0.2160 0.2392 0.2758 0.0077  0.0144  0.0020  100 LEU   C CD2 
1835 N N   . ALA   B 95  ? 0.1616 0.1847 0.1996 -0.0022 0.0144  0.0058  101 ALA   C N   
1836 C CA  . ALA   B 95  ? 0.1641 0.1873 0.1977 -0.0051 0.0156  0.0067  101 ALA   C CA  
1837 C C   . ALA   B 95  ? 0.1776 0.2027 0.2112 -0.0050 0.0211  0.0047  101 ALA   C C   
1838 O O   . ALA   B 95  ? 0.1861 0.2101 0.2194 -0.0026 0.0236  0.0018  101 ALA   C O   
1839 C CB  . ALA   B 95  ? 0.1653 0.1818 0.1876 -0.0063 0.0135  0.0064  101 ALA   C CB  
1840 N N   . VAL   B 96  ? 0.1851 0.2127 0.2185 -0.0081 0.0231  0.0060  102 VAL   C N   
1841 C CA  . VAL   B 96  ? 0.1999 0.2285 0.2304 -0.0093 0.0289  0.0041  102 VAL   C CA  
1842 C C   . VAL   B 96  ? 0.2336 0.2538 0.2489 -0.0109 0.0276  0.0037  102 VAL   C C   
1843 O O   . VAL   B 96  ? 0.2417 0.2583 0.2514 -0.0132 0.0242  0.0061  102 VAL   C O   
1844 C CB  . VAL   B 96  ? 0.2084 0.2432 0.2448 -0.0128 0.0315  0.0061  102 VAL   C CB  
1845 C CG1 . VAL   B 96  ? 0.2148 0.2503 0.2465 -0.0151 0.0385  0.0039  102 VAL   C CG1 
1846 C CG2 . VAL   B 96  ? 0.2040 0.2473 0.2576 -0.0111 0.0312  0.0071  102 VAL   C CG2 
1847 N N   . GLY   B 97  ? 0.2597 0.2765 0.2690 -0.0097 0.0299  0.0007  103 GLY   C N   
1848 C CA  . GLY   B 97  ? 0.2872 0.2959 0.2828 -0.0113 0.0276  0.0008  103 GLY   C CA  
1849 C C   . GLY   B 97  ? 0.3035 0.3087 0.2930 -0.0101 0.0297  -0.0027 103 GLY   C C   
1850 O O   . GLY   B 97  ? 0.3113 0.3195 0.3076 -0.0074 0.0325  -0.0055 103 GLY   C O   
1851 N N   . HIS   B 98  ? 0.3003 0.2982 0.2768 -0.0125 0.0276  -0.0023 104 HIS   C N   
1852 C CA  . HIS   B 98  ? 0.2992 0.2925 0.2676 -0.0124 0.0286  -0.0053 104 HIS   C CA  
1853 C C   . HIS   B 98  ? 0.2928 0.2833 0.2632 -0.0089 0.0237  -0.0062 104 HIS   C C   
1854 O O   . HIS   B 98  ? 0.2790 0.2680 0.2512 -0.0078 0.0182  -0.0040 104 HIS   C O   
1855 C CB  . HIS   B 98  ? 0.3139 0.3000 0.2666 -0.0173 0.0275  -0.0039 104 HIS   C CB  
1856 C CG  . HIS   B 98  ? 0.3392 0.3191 0.2815 -0.0180 0.0270  -0.0066 104 HIS   C CG  
1857 N ND1 . HIS   B 98  ? 0.3627 0.3436 0.3024 -0.0187 0.0338  -0.0111 104 HIS   C ND1 
1858 C CD2 . HIS   B 98  ? 0.3537 0.3268 0.2894 -0.0178 0.0202  -0.0057 104 HIS   C CD2 
1859 C CE1 . HIS   B 98  ? 0.3722 0.3461 0.3017 -0.0195 0.0308  -0.0127 104 HIS   C CE1 
1860 N NE2 . HIS   B 98  ? 0.3703 0.3396 0.2974 -0.0191 0.0222  -0.0092 104 HIS   C NE2 
1861 N N   . SER   B 99  ? 0.3056 0.2954 0.2758 -0.0073 0.0259  -0.0099 105 SER   C N   
1862 C CA  . SER   B 99  ? 0.3231 0.3096 0.2936 -0.0049 0.0216  -0.0112 105 SER   C CA  
1863 C C   . SER   B 99  ? 0.3349 0.3177 0.2988 -0.0054 0.0245  -0.0155 105 SER   C C   
1864 O O   . SER   B 99  ? 0.3469 0.3316 0.3106 -0.0061 0.0311  -0.0183 105 SER   C O   
1865 C CB  . SER   B 99  ? 0.3532 0.3443 0.3365 -0.0011 0.0201  -0.0108 105 SER   C CB  
1866 O OG  . SER   B 99  ? 0.3986 0.3947 0.3908 0.0006  0.0249  -0.0126 105 SER   C OG  
1867 N N   . GLU   B 100 ? 0.3243 0.3017 0.2829 -0.0053 0.0197  -0.0161 106 GLU   C N   
1868 C CA  . GLU   B 100 ? 0.3329 0.3054 0.2845 -0.0060 0.0207  -0.0201 106 GLU   C CA  
1869 C C   . GLU   B 100 ? 0.3280 0.3008 0.2880 -0.0026 0.0164  -0.0206 106 GLU   C C   
1870 O O   . GLU   B 100 ? 0.3133 0.2887 0.2806 -0.0009 0.0123  -0.0176 106 GLU   C O   
1871 C CB  . GLU   B 100 ? 0.3682 0.3327 0.3036 -0.0105 0.0168  -0.0193 106 GLU   C CB  
1872 C CG  . GLU   B 100 ? 0.4610 0.4235 0.3851 -0.0152 0.0198  -0.0179 106 GLU   C CG  
1873 C CD  . GLU   B 100 ? 0.5519 0.5114 0.4649 -0.0187 0.0268  -0.0224 106 GLU   C CD  
1874 O OE1 . GLU   B 100 ? 0.5791 0.5371 0.4928 -0.0172 0.0291  -0.0271 106 GLU   C OE1 
1875 O OE2 . GLU   B 100 ? 0.5670 0.5252 0.4704 -0.0232 0.0305  -0.0215 106 GLU   C OE2 
1876 N N   . PRO   B 101 ? 0.3381 0.3080 0.2974 -0.0019 0.0175  -0.0245 107 PRO   C N   
1877 C CA  . PRO   B 101 ? 0.3340 0.3043 0.3016 0.0008  0.0135  -0.0246 107 PRO   C CA  
1878 C C   . PRO   B 101 ? 0.3154 0.2847 0.2833 0.0004  0.0062  -0.0215 107 PRO   C C   
1879 O O   . PRO   B 101 ? 0.3300 0.3029 0.3078 0.0025  0.0041  -0.0200 107 PRO   C O   
1880 C CB  . PRO   B 101 ? 0.3623 0.3273 0.3250 0.0003  0.0153  -0.0294 107 PRO   C CB  
1881 C CG  . PRO   B 101 ? 0.3717 0.3368 0.3302 -0.0007 0.0230  -0.0327 107 PRO   C CG  
1882 C CD  . PRO   B 101 ? 0.3507 0.3168 0.3021 -0.0036 0.0231  -0.0294 107 PRO   C CD  
1883 N N   . GLY   B 102 ? 0.2981 0.2625 0.2555 -0.0026 0.0023  -0.0205 108 GLY   C N   
1884 C CA  . GLY   B 102 ? 0.2804 0.2438 0.2397 -0.0028 -0.0050 -0.0176 108 GLY   C CA  
1885 C C   . GLY   B 102 ? 0.2585 0.2264 0.2255 -0.0013 -0.0061 -0.0143 108 GLY   C C   
1886 O O   . GLY   B 102 ? 0.2512 0.2193 0.2230 -0.0006 -0.0113 -0.0125 108 GLY   C O   
1887 N N   . ASP   B 103 ? 0.2331 0.2047 0.2021 -0.0007 -0.0011 -0.0136 109 ASP   C N   
1888 C CA  . ASP   B 103 ? 0.2277 0.2030 0.2032 0.0004  -0.0017 -0.0109 109 ASP   C CA  
1889 C C   . ASP   B 103 ? 0.2145 0.1948 0.2016 0.0030  -0.0013 -0.0111 109 ASP   C C   
1890 O O   . ASP   B 103 ? 0.2133 0.1958 0.2050 0.0035  -0.0020 -0.0094 109 ASP   C O   
1891 C CB  . ASP   B 103 ? 0.2331 0.2104 0.2062 -0.0007 0.0028  -0.0098 109 ASP   C CB  
1892 C CG  . ASP   B 103 ? 0.2786 0.2508 0.2398 -0.0043 0.0019  -0.0085 109 ASP   C CG  
1893 O OD1 . ASP   B 103 ? 0.2849 0.2524 0.2418 -0.0054 -0.0039 -0.0068 109 ASP   C OD1 
1894 O OD2 . ASP   B 103 ? 0.2935 0.2664 0.2499 -0.0062 0.0070  -0.0090 109 ASP   C OD2 
1895 N N   . CYS   B 104 ? 0.2026 0.1839 0.1936 0.0041  0.0000  -0.0132 110 CYS   C N   
1896 C CA  . CYS   B 104 ? 0.2060 0.1912 0.2065 0.0056  0.0002  -0.0129 110 CYS   C CA  
1897 C C   . CYS   B 104 ? 0.1990 0.1848 0.2035 0.0057  -0.0035 -0.0121 110 CYS   C C   
1898 O O   . CYS   B 104 ? 0.2045 0.1874 0.2067 0.0052  -0.0073 -0.0125 110 CYS   C O   
1899 C CB  . CYS   B 104 ? 0.2349 0.2194 0.2379 0.0063  0.0010  -0.0149 110 CYS   C CB  
1900 S SG  . CYS   B 104 ? 0.2669 0.2521 0.2705 0.0073  0.0061  -0.0161 110 CYS   C SG  
1901 N N   . GLY   B 105 ? 0.1910 0.1803 0.2012 0.0061  -0.0024 -0.0112 111 GLY   C N   
1902 C CA  . GLY   B 105 ? 0.1947 0.1851 0.2101 0.0063  -0.0045 -0.0113 111 GLY   C CA  
1903 C C   . GLY   B 105 ? 0.1961 0.1857 0.2106 0.0063  -0.0053 -0.0102 111 GLY   C C   
1904 O O   . GLY   B 105 ? 0.1988 0.1897 0.2189 0.0067  -0.0059 -0.0108 111 GLY   C O   
1905 N N   . GLY   B 106 ? 0.1901 0.1774 0.1978 0.0056  -0.0050 -0.0089 112 GLY   C N   
1906 C CA  . GLY   B 106 ? 0.1837 0.1695 0.1898 0.0051  -0.0058 -0.0074 112 GLY   C CA  
1907 C C   . GLY   B 106 ? 0.1812 0.1701 0.1913 0.0049  -0.0029 -0.0075 112 GLY   C C   
1908 O O   . GLY   B 106 ? 0.1900 0.1818 0.2004 0.0044  -0.0001 -0.0072 112 GLY   C O   
1909 N N   . ILE   B 107 ? 0.1766 0.1645 0.1899 0.0052  -0.0040 -0.0079 113 ILE   C N   
1910 C CA  . ILE   B 107 ? 0.1854 0.1754 0.2011 0.0044  -0.0012 -0.0086 113 ILE   C CA  
1911 C C   . ILE   B 107 ? 0.1845 0.1735 0.1954 0.0027  -0.0003 -0.0067 113 ILE   C C   
1912 O O   . ILE   B 107 ? 0.2004 0.1860 0.2079 0.0024  -0.0022 -0.0053 113 ILE   C O   
1913 C CB  . ILE   B 107 ? 0.2186 0.2081 0.2409 0.0054  -0.0016 -0.0111 113 ILE   C CB  
1914 C CG1 . ILE   B 107 ? 0.2437 0.2365 0.2725 0.0062  -0.0010 -0.0132 113 ILE   C CG1 
1915 C CG2 . ILE   B 107 ? 0.2330 0.2224 0.2552 0.0040  0.0012  -0.0123 113 ILE   C CG2 
1916 C CD1 . ILE   B 107 ? 0.2770 0.2703 0.3150 0.0076  -0.0011 -0.0161 113 ILE   C CD1 
1917 N N   . LEU   B 108 ? 0.1672 0.1589 0.1780 0.0012  0.0022  -0.0064 114 LEU   C N   
1918 C CA  . LEU   B 108 ? 0.1679 0.1594 0.1755 -0.0010 0.0028  -0.0048 114 LEU   C CA  
1919 C C   . LEU   B 108 ? 0.1803 0.1703 0.1886 -0.0022 0.0037  -0.0067 114 LEU   C C   
1920 O O   . LEU   B 108 ? 0.1736 0.1654 0.1837 -0.0027 0.0053  -0.0085 114 LEU   C O   
1921 C CB  . LEU   B 108 ? 0.1653 0.1607 0.1729 -0.0022 0.0041  -0.0029 114 LEU   C CB  
1922 C CG  . LEU   B 108 ? 0.1830 0.1791 0.1889 -0.0049 0.0042  -0.0009 114 LEU   C CG  
1923 C CD1 . LEU   B 108 ? 0.1982 0.1929 0.2017 -0.0057 0.0037  0.0006  114 LEU   C CD1 
1924 C CD2 . LEU   B 108 ? 0.1777 0.1781 0.1863 -0.0057 0.0044  0.0011  114 LEU   C CD2 
1925 N N   . ARG   B 109 ? 0.1854 0.1718 0.1918 -0.0031 0.0028  -0.0068 115 ARG   C N   
1926 C CA  . ARG   B 109 ? 0.1892 0.1732 0.1958 -0.0043 0.0041  -0.0095 115 ARG   C CA  
1927 C C   . ARG   B 109 ? 0.1993 0.1814 0.2011 -0.0076 0.0038  -0.0080 115 ARG   C C   
1928 O O   . ARG   B 109 ? 0.2108 0.1922 0.2106 -0.0081 0.0021  -0.0051 115 ARG   C O   
1929 C CB  . ARG   B 109 ? 0.2273 0.2070 0.2381 -0.0019 0.0027  -0.0118 115 ARG   C CB  
1930 C CG  . ARG   B 109 ? 0.3288 0.3103 0.3466 0.0009  0.0030  -0.0142 115 ARG   C CG  
1931 C CD  . ARG   B 109 ? 0.4336 0.4110 0.4578 0.0036  0.0007  -0.0161 115 ARG   C CD  
1932 N NE  . ARG   B 109 ? 0.5320 0.5122 0.5654 0.0057  0.0021  -0.0196 115 ARG   C NE  
1933 C CZ  . ARG   B 109 ? 0.5771 0.5579 0.6153 0.0056  0.0062  -0.0242 115 ARG   C CZ  
1934 N NH1 . ARG   B 109 ? 0.5529 0.5308 0.5863 0.0032  0.0088  -0.0259 115 ARG   C NH1 
1935 N NH2 . ARG   B 109 ? 0.6102 0.5946 0.6580 0.0073  0.0079  -0.0274 115 ARG   C NH2 
1936 N N   . CYS   B 110 ? 0.2035 0.1844 0.2029 -0.0102 0.0056  -0.0101 116 CYS   C N   
1937 C CA  . CYS   B 110 ? 0.2096 0.1875 0.2041 -0.0137 0.0048  -0.0092 116 CYS   C CA  
1938 C C   . CYS   B 110 ? 0.2321 0.2041 0.2265 -0.0138 0.0062  -0.0138 116 CYS   C C   
1939 O O   . CYS   B 110 ? 0.2285 0.1996 0.2282 -0.0107 0.0075  -0.0171 116 CYS   C O   
1940 C CB  . CYS   B 110 ? 0.2056 0.1863 0.1959 -0.0176 0.0050  -0.0076 116 CYS   C CB  
1941 S SG  . CYS   B 110 ? 0.2161 0.1965 0.2037 -0.0197 0.0084  -0.0115 116 CYS   C SG  
1942 N N   . GLN   B 111 ? 0.2568 0.2247 0.2459 -0.0175 0.0059  -0.0143 117 GLN   C N   
1943 C CA  . GLN   B 111 ? 0.2768 0.2383 0.2657 -0.0178 0.0077  -0.0194 117 GLN   C CA  
1944 C C   . GLN   B 111 ? 0.2859 0.2482 0.2753 -0.0180 0.0125  -0.0247 117 GLN   C C   
1945 O O   . GLN   B 111 ? 0.3001 0.2582 0.2926 -0.0169 0.0152  -0.0300 117 GLN   C O   
1946 C CB  . GLN   B 111 ? 0.3109 0.2673 0.2926 -0.0225 0.0064  -0.0190 117 GLN   C CB  
1947 C CG  . GLN   B 111 ? 0.3659 0.3243 0.3398 -0.0278 0.0073  -0.0185 117 GLN   C CG  
1948 C CD  . GLN   B 111 ? 0.4630 0.4166 0.4301 -0.0329 0.0049  -0.0176 117 GLN   C CD  
1949 O OE1 . GLN   B 111 ? 0.5026 0.4594 0.4684 -0.0353 0.0015  -0.0124 117 GLN   C OE1 
1950 N NE2 . GLN   B 111 ? 0.4758 0.4218 0.4392 -0.0346 0.0069  -0.0228 117 GLN   C NE2 
1951 N N   . HIS   B 112 ? 0.2601 0.2277 0.2473 -0.0196 0.0138  -0.0233 118 HIS   C N   
1952 C CA  . HIS   B 112 ? 0.2564 0.2251 0.2425 -0.0212 0.0187  -0.0278 118 HIS   C CA  
1953 C C   . HIS   B 112 ? 0.2637 0.2371 0.2588 -0.0171 0.0206  -0.0292 118 HIS   C C   
1954 O O   . HIS   B 112 ? 0.2826 0.2570 0.2784 -0.0183 0.0253  -0.0334 118 HIS   C O   
1955 C CB  . HIS   B 112 ? 0.2641 0.2345 0.2407 -0.0269 0.0186  -0.0252 118 HIS   C CB  
1956 C CG  . HIS   B 112 ? 0.2739 0.2402 0.2416 -0.0318 0.0160  -0.0235 118 HIS   C CG  
1957 N ND1 . HIS   B 112 ? 0.2713 0.2402 0.2377 -0.0331 0.0110  -0.0172 118 HIS   C ND1 
1958 C CD2 . HIS   B 112 ? 0.2844 0.2443 0.2447 -0.0359 0.0178  -0.0275 118 HIS   C CD2 
1959 C CE1 . HIS   B 112 ? 0.2816 0.2461 0.2405 -0.0379 0.0093  -0.0171 118 HIS   C CE1 
1960 N NE2 . HIS   B 112 ? 0.2953 0.2537 0.2492 -0.0400 0.0132  -0.0232 118 HIS   C NE2 
1961 N N   . GLY   B 113 ? 0.2525 0.2285 0.2537 -0.0129 0.0170  -0.0257 119 GLY   C N   
1962 C CA  . GLY   B 113 ? 0.2335 0.2137 0.2431 -0.0094 0.0178  -0.0266 119 GLY   C CA  
1963 C C   . GLY   B 113 ? 0.2076 0.1918 0.2174 -0.0081 0.0145  -0.0215 119 GLY   C C   
1964 O O   . GLY   B 113 ? 0.2115 0.1951 0.2175 -0.0086 0.0114  -0.0175 119 GLY   C O   
1965 N N   . VAL   B 114 ? 0.1943 0.1824 0.2090 -0.0067 0.0154  -0.0220 120 VAL   C N   
1966 C CA  . VAL   B 114 ? 0.1875 0.1787 0.2026 -0.0054 0.0128  -0.0182 120 VAL   C CA  
1967 C C   . VAL   B 114 ? 0.1850 0.1778 0.1938 -0.0088 0.0127  -0.0151 120 VAL   C C   
1968 O O   . VAL   B 114 ? 0.1913 0.1845 0.1968 -0.0121 0.0152  -0.0161 120 VAL   C O   
1969 C CB  . VAL   B 114 ? 0.2035 0.1978 0.2260 -0.0033 0.0136  -0.0200 120 VAL   C CB  
1970 C CG1 . VAL   B 114 ? 0.2070 0.2036 0.2289 -0.0025 0.0113  -0.0166 120 VAL   C CG1 
1971 C CG2 . VAL   B 114 ? 0.2037 0.1967 0.2345 0.0005  0.0121  -0.0222 120 VAL   C CG2 
1972 N N   . VAL   B 115 ? 0.1708 0.1643 0.1782 -0.0081 0.0098  -0.0111 121 VAL   C N   
1973 C CA  . VAL   B 115 ? 0.1725 0.1678 0.1766 -0.0105 0.0087  -0.0077 121 VAL   C CA  
1974 C C   . VAL   B 115 ? 0.1704 0.1684 0.1779 -0.0088 0.0081  -0.0062 121 VAL   C C   
1975 O O   . VAL   B 115 ? 0.1651 0.1640 0.1713 -0.0110 0.0078  -0.0044 121 VAL   C O   
1976 C CB  . VAL   B 115 ? 0.1835 0.1786 0.1860 -0.0108 0.0065  -0.0047 121 VAL   C CB  
1977 C CG1 . VAL   B 115 ? 0.1949 0.1928 0.1976 -0.0122 0.0048  -0.0009 121 VAL   C CG1 
1978 C CG2 . VAL   B 115 ? 0.1788 0.1704 0.1770 -0.0134 0.0067  -0.0059 121 VAL   C CG2 
1979 N N   . GLY   B 116 ? 0.1635 0.1618 0.1747 -0.0053 0.0073  -0.0067 122 GLY   C N   
1980 C CA  . GLY   B 116 ? 0.1786 0.1785 0.1926 -0.0037 0.0067  -0.0058 122 GLY   C CA  
1981 C C   . GLY   B 116 ? 0.1738 0.1730 0.1898 -0.0005 0.0056  -0.0067 122 GLY   C C   
1982 O O   . GLY   B 116 ? 0.1809 0.1782 0.1967 0.0004  0.0050  -0.0079 122 GLY   C O   
1983 N N   . ILE   B 117 ? 0.1518 0.1516 0.1692 0.0008  0.0051  -0.0062 123 ILE   C N   
1984 C CA  . ILE   B 117 ? 0.1661 0.1644 0.1835 0.0029  0.0039  -0.0072 123 ILE   C CA  
1985 C C   . ILE   B 117 ? 0.1685 0.1668 0.1845 0.0038  0.0043  -0.0063 123 ILE   C C   
1986 O O   . ILE   B 117 ? 0.1698 0.1696 0.1881 0.0036  0.0050  -0.0053 123 ILE   C O   
1987 C CB  . ILE   B 117 ? 0.1927 0.1909 0.2135 0.0036  0.0031  -0.0091 123 ILE   C CB  
1988 C CG1 . ILE   B 117 ? 0.2072 0.2068 0.2300 0.0025  0.0040  -0.0086 123 ILE   C CG1 
1989 C CG2 . ILE   B 117 ? 0.2092 0.2076 0.2333 0.0036  0.0029  -0.0109 123 ILE   C CG2 
1990 C CD1 . ILE   B 117 ? 0.2258 0.2252 0.2523 0.0029  0.0030  -0.0104 123 ILE   C CD1 
1991 N N   . VAL   B 118 ? 0.1506 0.1468 0.1631 0.0045  0.0038  -0.0068 124 VAL   C N   
1992 C CA  . VAL   B 118 ? 0.1574 0.1536 0.1684 0.0051  0.0055  -0.0069 124 VAL   C CA  
1993 C C   . VAL   B 118 ? 0.1640 0.1599 0.1780 0.0061  0.0056  -0.0083 124 VAL   C C   
1994 O O   . VAL   B 118 ? 0.1631 0.1573 0.1773 0.0063  0.0038  -0.0096 124 VAL   C O   
1995 C CB  . VAL   B 118 ? 0.1676 0.1604 0.1719 0.0047  0.0050  -0.0076 124 VAL   C CB  
1996 C CG1 . VAL   B 118 ? 0.1813 0.1738 0.1834 0.0049  0.0079  -0.0089 124 VAL   C CG1 
1997 C CG2 . VAL   B 118 ? 0.1762 0.1685 0.1774 0.0033  0.0046  -0.0058 124 VAL   C CG2 
1998 N N   . SER   B 119 ? 0.1637 0.1612 0.1811 0.0068  0.0075  -0.0080 125 SER   C N   
1999 C CA  . SER   B 119 ? 0.1676 0.1640 0.1887 0.0079  0.0074  -0.0091 125 SER   C CA  
2000 C C   . SER   B 119 ? 0.1823 0.1780 0.2045 0.0094  0.0102  -0.0110 125 SER   C C   
2001 O O   . SER   B 119 ? 0.1956 0.1883 0.2179 0.0103  0.0104  -0.0133 125 SER   C O   
2002 C CB  . SER   B 119 ? 0.1766 0.1748 0.2030 0.0073  0.0062  -0.0067 125 SER   C CB  
2003 O OG  . SER   B 119 ? 0.1769 0.1732 0.2071 0.0081  0.0056  -0.0072 125 SER   C OG  
2004 N N   . THR   B 120 ? 0.1794 0.1780 0.2029 0.0095  0.0127  -0.0103 126 THR   C N   
2005 C CA  . THR   B 120 ? 0.2031 0.2021 0.2295 0.0109  0.0166  -0.0127 126 THR   C CA  
2006 C C   . THR   B 120 ? 0.2190 0.2197 0.2408 0.0095  0.0199  -0.0131 126 THR   C C   
2007 O O   . THR   B 120 ? 0.1989 0.2008 0.2174 0.0077  0.0185  -0.0106 126 THR   C O   
2008 C CB  . THR   B 120 ? 0.2263 0.2290 0.2646 0.0125  0.0167  -0.0109 126 THR   C CB  
2009 O OG1 . THR   B 120 ? 0.2464 0.2539 0.2878 0.0114  0.0164  -0.0077 126 THR   C OG1 
2010 C CG2 . THR   B 120 ? 0.2339 0.2348 0.2763 0.0129  0.0129  -0.0092 126 THR   C CG2 
2011 N N   . GLY   B 121 ? 0.2386 0.2393 0.2607 0.0101  0.0247  -0.0162 127 GLY   C N   
2012 C CA  . GLY   B 121 ? 0.2636 0.2663 0.2816 0.0081  0.0287  -0.0167 127 GLY   C CA  
2013 C C   . GLY   B 121 ? 0.2811 0.2849 0.3024 0.0090  0.0353  -0.0210 127 GLY   C C   
2014 O O   . GLY   B 121 ? 0.2746 0.2754 0.2981 0.0110  0.0362  -0.0243 127 GLY   C O   
2015 N N   . GLY   B 122 ? 0.3051 0.3130 0.3275 0.0074  0.0400  -0.0211 128 GLY   C N   
2016 C CA  . GLY   B 122 ? 0.3195 0.3298 0.3462 0.0078  0.0478  -0.0257 128 GLY   C CA  
2017 C C   . GLY   B 122 ? 0.3285 0.3469 0.3644 0.0070  0.0515  -0.0240 128 GLY   C C   
2018 O O   . GLY   B 122 ? 0.3229 0.3454 0.3663 0.0073  0.0471  -0.0193 128 GLY   C O   
2019 N N   . ASN   B 123 ? 0.3310 0.3516 0.3659 0.0052  0.0597  -0.0278 129 ASN   C N   
2020 C CA  . ASN   B 123 ? 0.3290 0.3583 0.3742 0.0039  0.0642  -0.0267 129 ASN   C CA  
2021 C C   . ASN   B 123 ? 0.3198 0.3508 0.3598 0.0002  0.0603  -0.0209 129 ASN   C C   
2022 O O   . ASN   B 123 ? 0.3254 0.3641 0.3777 -0.0001 0.0606  -0.0183 129 ASN   C O   
2023 C CB  . ASN   B 123 ? 0.3435 0.3799 0.4110 0.0086  0.0637  -0.0263 129 ASN   C CB  
2024 C CG  . ASN   B 123 ? 0.3946 0.4299 0.4703 0.0124  0.0687  -0.0324 129 ASN   C CG  
2025 O OD1 . ASN   B 123 ? 0.4082 0.4417 0.4777 0.0111  0.0767  -0.0383 129 ASN   C OD1 
2026 N ND2 . ASN   B 123 ? 0.4201 0.4560 0.5095 0.0170  0.0641  -0.0313 129 ASN   C ND2 
2027 N N   . GLY   B 124 ? 0.2946 0.3183 0.3175 -0.0028 0.0563  -0.0191 130 GLY   C N   
2028 C CA  . GLY   B 124 ? 0.2787 0.3025 0.2967 -0.0060 0.0522  -0.0139 130 GLY   C CA  
2029 C C   . GLY   B 124 ? 0.2468 0.2723 0.2729 -0.0037 0.0448  -0.0098 130 GLY   C C   
2030 O O   . GLY   B 124 ? 0.2515 0.2787 0.2777 -0.0061 0.0420  -0.0059 130 GLY   C O   
2031 N N   . LEU   B 125 ? 0.2358 0.2599 0.2672 0.0002  0.0414  -0.0106 131 LEU   C N   
2032 C CA  . LEU   B 125 ? 0.2196 0.2441 0.2562 0.0016  0.0348  -0.0070 131 LEU   C CA  
2033 C C   . LEU   B 125 ? 0.2197 0.2371 0.2473 0.0026  0.0304  -0.0075 131 LEU   C C   
2034 O O   . LEU   B 125 ? 0.2394 0.2531 0.2630 0.0039  0.0321  -0.0109 131 LEU   C O   
2035 C CB  . LEU   B 125 ? 0.2248 0.2546 0.2776 0.0049  0.0343  -0.0067 131 LEU   C CB  
2036 C CG  . LEU   B 125 ? 0.2525 0.2907 0.3181 0.0044  0.0384  -0.0063 131 LEU   C CG  
2037 C CD1 . LEU   B 125 ? 0.2705 0.3128 0.3527 0.0085  0.0393  -0.0077 131 LEU   C CD1 
2038 C CD2 . LEU   B 125 ? 0.2520 0.2937 0.3202 0.0017  0.0341  -0.0014 131 LEU   C CD2 
2039 N N   . VAL   B 126 ? 0.1786 0.1944 0.2036 0.0018  0.0252  -0.0044 132 VAL   C N   
2040 C CA  . VAL   B 126 ? 0.1899 0.2003 0.2090 0.0027  0.0213  -0.0048 132 VAL   C CA  
2041 C C   . VAL   B 126 ? 0.1737 0.1859 0.2002 0.0039  0.0177  -0.0028 132 VAL   C C   
2042 O O   . VAL   B 126 ? 0.1826 0.1980 0.2131 0.0025  0.0162  0.0000  132 VAL   C O   
2043 C CB  . VAL   B 126 ? 0.2129 0.2188 0.2218 0.0004  0.0187  -0.0037 132 VAL   C CB  
2044 C CG1 . VAL   B 126 ? 0.2459 0.2537 0.2558 -0.0018 0.0173  -0.0006 132 VAL   C CG1 
2045 C CG2 . VAL   B 126 ? 0.2154 0.2170 0.2213 0.0016  0.0148  -0.0043 132 VAL   C CG2 
2046 N N   . GLY   B 127 ? 0.1613 0.1710 0.1884 0.0057  0.0162  -0.0041 133 GLY   C N   
2047 C CA  . GLY   B 127 ? 0.1589 0.1694 0.1911 0.0059  0.0128  -0.0020 133 GLY   C CA  
2048 C C   . GLY   B 127 ? 0.1626 0.1696 0.1889 0.0051  0.0101  -0.0020 133 GLY   C C   
2049 O O   . GLY   B 127 ? 0.1711 0.1748 0.1930 0.0057  0.0102  -0.0043 133 GLY   C O   
2050 N N   . PHE   B 128 ? 0.1609 0.1686 0.1874 0.0032  0.0078  0.0002  134 PHE   C N   
2051 C CA  . PHE   B 128 ? 0.1635 0.1687 0.1857 0.0022  0.0063  -0.0004 134 PHE   C CA  
2052 C C   . PHE   B 128 ? 0.1639 0.1691 0.1885 0.0011  0.0047  0.0010  134 PHE   C C   
2053 O O   . PHE   B 128 ? 0.1539 0.1607 0.1811 -0.0004 0.0033  0.0037  134 PHE   C O   
2054 C CB  . PHE   B 128 ? 0.1641 0.1688 0.1824 0.0000  0.0058  0.0004  134 PHE   C CB  
2055 C CG  . PHE   B 128 ? 0.1742 0.1783 0.1896 0.0001  0.0068  0.0001  134 PHE   C CG  
2056 C CD1 . PHE   B 128 ? 0.1669 0.1677 0.1781 0.0009  0.0065  -0.0016 134 PHE   C CD1 
2057 C CD2 . PHE   B 128 ? 0.1849 0.1917 0.2019 -0.0011 0.0076  0.0019  134 PHE   C CD2 
2058 C CE1 . PHE   B 128 ? 0.1738 0.1730 0.1809 0.0001  0.0069  -0.0011 134 PHE   C CE1 
2059 C CE2 . PHE   B 128 ? 0.1961 0.2020 0.2096 -0.0018 0.0088  0.0020  134 PHE   C CE2 
2060 C CZ  . PHE   B 128 ? 0.1844 0.1861 0.1922 -0.0014 0.0084  0.0006  134 PHE   C CZ  
2061 N N   . ALA   B 129 ? 0.1459 0.1491 0.1694 0.0013  0.0045  -0.0006 135 ALA   C N   
2062 C CA  . ALA   B 129 ? 0.1481 0.1509 0.1724 -0.0007 0.0033  0.0007  135 ALA   C CA  
2063 C C   . ALA   B 129 ? 0.1473 0.1500 0.1671 -0.0039 0.0035  0.0009  135 ALA   C C   
2064 O O   . ALA   B 129 ? 0.1474 0.1495 0.1654 -0.0037 0.0049  -0.0016 135 ALA   C O   
2065 C CB  . ALA   B 129 ? 0.1440 0.1450 0.1690 0.0001  0.0035  -0.0013 135 ALA   C CB  
2066 N N   . ASP   B 130 ? 0.1559 0.1587 0.1741 -0.0070 0.0021  0.0038  136 ASP   C N   
2067 C CA  . ASP   B 130 ? 0.1566 0.1585 0.1690 -0.0107 0.0027  0.0034  136 ASP   C CA  
2068 C C   . ASP   B 130 ? 0.1657 0.1664 0.1757 -0.0128 0.0046  0.0015  136 ASP   C C   
2069 O O   . ASP   B 130 ? 0.1696 0.1699 0.1811 -0.0133 0.0039  0.0026  136 ASP   C O   
2070 C CB  . ASP   B 130 ? 0.1764 0.1782 0.1868 -0.0142 -0.0003 0.0075  136 ASP   C CB  
2071 C CG  . ASP   B 130 ? 0.2549 0.2549 0.2576 -0.0188 0.0002  0.0070  136 ASP   C CG  
2072 O OD1 . ASP   B 130 ? 0.2409 0.2405 0.2419 -0.0181 0.0023  0.0042  136 ASP   C OD1 
2073 O OD2 . ASP   B 130 ? 0.2916 0.2898 0.2893 -0.0233 -0.0015 0.0094  136 ASP   C OD2 
2074 N N   . VAL   B 131 ? 0.1625 0.1626 0.1692 -0.0143 0.0073  -0.0016 137 VAL   C N   
2075 C CA  . VAL   B 131 ? 0.1663 0.1661 0.1713 -0.0170 0.0102  -0.0040 137 VAL   C CA  
2076 C C   . VAL   B 131 ? 0.1849 0.1828 0.1821 -0.0221 0.0121  -0.0048 137 VAL   C C   
2077 O O   . VAL   B 131 ? 0.2009 0.1987 0.1959 -0.0251 0.0157  -0.0074 137 VAL   C O   
2078 C CB  . VAL   B 131 ? 0.1738 0.1750 0.1846 -0.0138 0.0127  -0.0083 137 VAL   C CB  
2079 C CG1 . VAL   B 131 ? 0.1736 0.1758 0.1901 -0.0099 0.0105  -0.0076 137 VAL   C CG1 
2080 C CG2 . VAL   B 131 ? 0.1810 0.1815 0.1923 -0.0120 0.0136  -0.0109 137 VAL   C CG2 
2081 N N   . ARG   B 132 ? 0.1800 0.1765 0.1729 -0.0236 0.0101  -0.0030 138 ARG   C N   
2082 C CA  . ARG   B 132 ? 0.1815 0.1752 0.1657 -0.0287 0.0118  -0.0044 138 ARG   C CA  
2083 C C   . ARG   B 132 ? 0.2062 0.1978 0.1820 -0.0352 0.0116  -0.0023 138 ARG   C C   
2084 O O   . ARG   B 132 ? 0.2406 0.2296 0.2081 -0.0401 0.0149  -0.0050 138 ARG   C O   
2085 C CB  . ARG   B 132 ? 0.1726 0.1651 0.1544 -0.0291 0.0088  -0.0026 138 ARG   C CB  
2086 C CG  . ARG   B 132 ? 0.1758 0.1690 0.1635 -0.0240 0.0094  -0.0047 138 ARG   C CG  
2087 C CD  . ARG   B 132 ? 0.1796 0.1720 0.1651 -0.0253 0.0063  -0.0022 138 ARG   C CD  
2088 N NE  . ARG   B 132 ? 0.1838 0.1792 0.1738 -0.0240 0.0024  0.0027  138 ARG   C NE  
2089 C CZ  . ARG   B 132 ? 0.2084 0.2050 0.1999 -0.0243 -0.0004 0.0055  138 ARG   C CZ  
2090 N NH1 . ARG   B 132 ? 0.1953 0.1896 0.1825 -0.0268 -0.0006 0.0047  138 ARG   C NH1 
2091 N NH2 . ARG   B 132 ? 0.1925 0.1927 0.1907 -0.0225 -0.0030 0.0091  138 ARG   C NH2 
2092 N N   . ASP   B 133 ? 0.1994 0.1915 0.1768 -0.0356 0.0080  0.0023  139 ASP   C N   
2093 C CA  . ASP   B 133 ? 0.2054 0.1946 0.1742 -0.0424 0.0068  0.0054  139 ASP   C CA  
2094 C C   . ASP   B 133 ? 0.2239 0.2134 0.1919 -0.0443 0.0117  0.0025  139 ASP   C C   
2095 O O   . ASP   B 133 ? 0.2419 0.2285 0.2007 -0.0511 0.0120  0.0043  139 ASP   C O   
2096 C CB  . ASP   B 133 ? 0.2149 0.2036 0.1867 -0.0421 0.0000  0.0120  139 ASP   C CB  
2097 C CG  . ASP   B 133 ? 0.2811 0.2722 0.2636 -0.0365 -0.0003 0.0123  139 ASP   C CG  
2098 O OD1 . ASP   B 133 ? 0.2682 0.2622 0.2580 -0.0307 0.0020  0.0087  139 ASP   C OD1 
2099 O OD2 . ASP   B 133 ? 0.2969 0.2861 0.2798 -0.0383 -0.0033 0.0161  139 ASP   C OD2 
2100 N N   . LEU   B 134 ? 0.2125 0.2055 0.1898 -0.0391 0.0152  -0.0015 140 LEU   C N   
2101 C CA  . LEU   B 134 ? 0.2170 0.2116 0.1965 -0.0406 0.0197  -0.0043 140 LEU   C CA  
2102 C C   . LEU   B 134 ? 0.2269 0.2217 0.2022 -0.0440 0.0267  -0.0102 140 LEU   C C   
2103 O O   . LEU   B 134 ? 0.2294 0.2272 0.2130 -0.0400 0.0307  -0.0154 140 LEU   C O   
2104 C CB  . LEU   B 134 ? 0.2147 0.2129 0.2068 -0.0337 0.0194  -0.0059 140 LEU   C CB  
2105 C CG  . LEU   B 134 ? 0.2359 0.2335 0.2324 -0.0300 0.0135  -0.0013 140 LEU   C CG  
2106 C CD1 . LEU   B 134 ? 0.2441 0.2444 0.2508 -0.0240 0.0135  -0.0037 140 LEU   C CD1 
2107 C CD2 . LEU   B 134 ? 0.2430 0.2379 0.2354 -0.0344 0.0107  0.0035  140 LEU   C CD2 
2108 N N   . LEU   B 135 ? 0.2354 0.2264 0.1976 -0.0517 0.0281  -0.0094 141 LEU   C N   
2109 C CA  . LEU   B 135 ? 0.2544 0.2447 0.2110 -0.0555 0.0354  -0.0157 141 LEU   C CA  
2110 C C   . LEU   B 135 ? 0.2703 0.2645 0.2331 -0.0560 0.0429  -0.0210 141 LEU   C C   
2111 O O   . LEU   B 135 ? 0.2924 0.2879 0.2581 -0.0555 0.0494  -0.0278 141 LEU   C O   
2112 C CB  . LEU   B 135 ? 0.2623 0.2467 0.2013 -0.0646 0.0351  -0.0137 141 LEU   C CB  
2113 C CG  . LEU   B 135 ? 0.2790 0.2597 0.2119 -0.0655 0.0268  -0.0076 141 LEU   C CG  
2114 C CD1 . LEU   B 135 ? 0.3028 0.2773 0.2174 -0.0753 0.0265  -0.0062 141 LEU   C CD1 
2115 C CD2 . LEU   B 135 ? 0.2668 0.2490 0.2079 -0.0584 0.0245  -0.0089 141 LEU   C CD2 
2116 N N   . TRP   B 136 ? 0.2697 0.2658 0.2360 -0.0569 0.0419  -0.0180 142 TRP   C N   
2117 C CA  . TRP   B 136 ? 0.2786 0.2793 0.2520 -0.0580 0.0488  -0.0225 142 TRP   C CA  
2118 C C   . TRP   B 136 ? 0.2908 0.2972 0.2817 -0.0498 0.0505  -0.0274 142 TRP   C C   
2119 O O   . TRP   B 136 ? 0.2943 0.3053 0.2935 -0.0502 0.0568  -0.0323 142 TRP   C O   
2120 C CB  . TRP   B 136 ? 0.2687 0.2693 0.2414 -0.0613 0.0462  -0.0174 142 TRP   C CB  
2121 C CG  . TRP   B 136 ? 0.2577 0.2578 0.2369 -0.0555 0.0378  -0.0120 142 TRP   C CG  
2122 C CD1 . TRP   B 136 ? 0.2616 0.2571 0.2346 -0.0560 0.0304  -0.0054 142 TRP   C CD1 
2123 C CD2 . TRP   B 136 ? 0.2462 0.2505 0.2399 -0.0485 0.0361  -0.0130 142 TRP   C CD2 
2124 N NE1 . TRP   B 136 ? 0.2621 0.2587 0.2451 -0.0494 0.0252  -0.0031 142 TRP   C NE1 
2125 C CE2 . TRP   B 136 ? 0.2541 0.2556 0.2485 -0.0452 0.0285  -0.0075 142 TRP   C CE2 
2126 C CE3 . TRP   B 136 ? 0.2512 0.2611 0.2577 -0.0450 0.0400  -0.0181 142 TRP   C CE3 
2127 C CZ2 . TRP   B 136 ? 0.2615 0.2650 0.2667 -0.0390 0.0253  -0.0075 142 TRP   C CZ2 
2128 C CZ3 . TRP   B 136 ? 0.2582 0.2701 0.2755 -0.0391 0.0357  -0.0172 142 TRP   C CZ3 
2129 C CH2 . TRP   B 136 ? 0.2575 0.2658 0.2729 -0.0365 0.0288  -0.0121 142 TRP   C CH2 
2130 N N   . LEU   B 137 ? 0.2879 0.2939 0.2845 -0.0427 0.0448  -0.0259 143 LEU   C N   
2131 C CA  . LEU   B 137 ? 0.2885 0.2985 0.3001 -0.0355 0.0451  -0.0297 143 LEU   C CA  
2132 C C   . LEU   B 137 ? 0.3306 0.3420 0.3462 -0.0354 0.0521  -0.0370 143 LEU   C C   
2133 O O   . LEU   B 137 ? 0.3318 0.3477 0.3617 -0.0311 0.0540  -0.0409 143 LEU   C O   
2134 C CB  . LEU   B 137 ? 0.2620 0.2702 0.2757 -0.0293 0.0381  -0.0266 143 LEU   C CB  
2135 C CG  . LEU   B 137 ? 0.2494 0.2574 0.2646 -0.0270 0.0318  -0.0212 143 LEU   C CG  
2136 C CD1 . LEU   B 137 ? 0.2388 0.2449 0.2545 -0.0219 0.0265  -0.0189 143 LEU   C CD1 
2137 C CD2 . LEU   B 137 ? 0.2374 0.2496 0.2644 -0.0244 0.0320  -0.0226 143 LEU   C CD2 
2138 N N   . ASP   B 138 ? 0.3669 0.3740 0.3705 -0.0401 0.0553  -0.0387 144 ASP   C N   
2139 C CA  . ASP   B 138 ? 0.4138 0.4202 0.4184 -0.0407 0.0622  -0.0461 144 ASP   C CA  
2140 C C   . ASP   B 138 ? 0.4602 0.4697 0.4655 -0.0461 0.0720  -0.0519 144 ASP   C C   
2141 O O   . ASP   B 138 ? 0.4709 0.4798 0.4773 -0.0468 0.0789  -0.0589 144 ASP   C O   
2142 C CB  . ASP   B 138 ? 0.4488 0.4483 0.4374 -0.0449 0.0614  -0.0454 144 ASP   C CB  
2143 C CG  . ASP   B 138 ? 0.4984 0.4946 0.4862 -0.0404 0.0537  -0.0415 144 ASP   C CG  
2144 O OD1 . ASP   B 138 ? 0.5017 0.5004 0.5018 -0.0332 0.0500  -0.0408 144 ASP   C OD1 
2145 O OD2 . ASP   B 138 ? 0.5364 0.5275 0.5109 -0.0445 0.0512  -0.0390 144 ASP   C OD2 
2146 N N   . GLU   B 139 ? 0.4805 0.4926 0.4835 -0.0506 0.0732  -0.0492 145 GLU   C N   
2147 C CA  . GLU   B 139 ? 0.5129 0.5284 0.5159 -0.0568 0.0832  -0.0545 145 GLU   C CA  
2148 C C   . GLU   B 139 ? 0.5305 0.5532 0.5477 -0.0552 0.0836  -0.0537 145 GLU   C C   
2149 O O   . GLU   B 139 ? 0.5468 0.5738 0.5669 -0.0602 0.0919  -0.0577 145 GLU   C O   
2150 C CB  . GLU   B 139 ? 0.5658 0.5756 0.5467 -0.0673 0.0853  -0.0518 145 GLU   C CB  
2151 C CG  . GLU   B 139 ? 0.6509 0.6583 0.6243 -0.0696 0.0770  -0.0424 145 GLU   C CG  
2152 C CD  . GLU   B 139 ? 0.7751 0.7745 0.7267 -0.0775 0.0735  -0.0373 145 GLU   C CD  
2153 O OE1 . GLU   B 139 ? 0.7973 0.7944 0.7407 -0.0829 0.0702  -0.0311 145 GLU   C OE1 
2154 O OE2 . GLU   B 139 ? 0.8131 0.8079 0.7560 -0.0782 0.0733  -0.0390 145 GLU   C OE2 
2155 N N1  . A1BN0 C .   ? 0.4977 0.5006 0.5514 -0.0008 0.0512  0.0389  201 A1BN0 A N1  
2156 N N3  . A1BN0 C .   ? 0.3417 0.3403 0.4191 -0.0095 0.0376  0.0272  201 A1BN0 A N3  
2157 C C4  . A1BN0 C .   ? 0.3747 0.3769 0.4438 -0.0075 0.0375  0.0265  201 A1BN0 A C4  
2158 C C5  . A1BN0 C .   ? 0.3304 0.3226 0.4020 -0.0077 0.0380  0.0330  201 A1BN0 A C5  
2159 C C6  . A1BN0 C .   ? 0.3158 0.3066 0.3832 -0.0072 0.0317  0.0297  201 A1BN0 A C6  
2160 C C7  . A1BN0 C .   ? 0.3050 0.2976 0.3836 -0.0103 0.0296  0.0229  201 A1BN0 A C7  
2161 C C8  . A1BN0 C .   ? 0.2913 0.2900 0.3727 -0.0114 0.0288  0.0172  201 A1BN0 A C8  
2162 C C10 . A1BN0 C .   ? 0.3179 0.3189 0.4066 -0.0125 0.0345  0.0201  201 A1BN0 A C10 
2163 C C13 . A1BN0 C .   ? 0.5008 0.5058 0.5258 0.0046  0.0375  0.0275  201 A1BN0 A C13 
2164 O O1  . A1BN0 C .   ? 0.2566 0.2566 0.3605 -0.0159 0.0280  0.0084  201 A1BN0 A O1  
2165 C C9  . A1BN0 C .   ? 0.2620 0.2625 0.3528 -0.0134 0.0261  0.0099  201 A1BN0 A C9  
2166 N N4  . A1BN0 C .   ? 0.2329 0.2353 0.3167 -0.0119 0.0217  0.0053  201 A1BN0 A N4  
2167 O O   . A1BN0 C .   ? 0.3458 0.3535 0.4203 -0.0085 0.0371  0.0218  201 A1BN0 A O   
2168 N N2  . A1BN0 C .   ? 0.4325 0.4317 0.4867 -0.0039 0.0374  0.0306  201 A1BN0 A N2  
2169 C C3  . A1BN0 C .   ? 0.4688 0.4704 0.5134 -0.0014 0.0371  0.0296  201 A1BN0 A C3  
2170 C C11 . A1BN0 C .   ? 0.4861 0.4881 0.5217 -0.0001 0.0315  0.0251  201 A1BN0 A C11 
2171 C C12 . A1BN0 C .   ? 0.4965 0.4999 0.5228 0.0026  0.0316  0.0241  201 A1BN0 A C12 
2172 C C14 . A1BN0 C .   ? 0.5005 0.5056 0.5346 0.0033  0.0437  0.0325  201 A1BN0 A C14 
2173 N N   . A1BN0 C .   ? 0.5114 0.5178 0.5475 0.0048  0.0516  0.0375  201 A1BN0 A N   
2174 C C   . A1BN0 C .   ? 0.5254 0.5328 0.5506 0.0091  0.0550  0.0389  201 A1BN0 A C   
2175 C C2  . A1BN0 C .   ? 0.4875 0.4907 0.5319 0.0001  0.0436  0.0335  201 A1BN0 A C2  
2176 C C1  . A1BN0 C .   ? 0.5039 0.5090 0.5524 0.0019  0.0559  0.0413  201 A1BN0 A C1  
2186 N N1  . A1BN0 G .   ? 0.4100 0.3918 0.4049 0.0079  0.0332  -0.0322 201 A1BN0 C N1  
2187 N N3  . A1BN0 G .   ? 0.2968 0.2784 0.3168 0.0138  0.0189  -0.0260 201 A1BN0 C N3  
2188 C C4  . A1BN0 G .   ? 0.3336 0.3183 0.3494 0.0126  0.0212  -0.0251 201 A1BN0 C C4  
2189 C C5  . A1BN0 G .   ? 0.2885 0.2640 0.3019 0.0126  0.0165  -0.0285 201 A1BN0 C C5  
2190 C C6  . A1BN0 G .   ? 0.2824 0.2584 0.2967 0.0114  0.0110  -0.0252 201 A1BN0 C C6  
2191 C C7  . A1BN0 G .   ? 0.2607 0.2400 0.2852 0.0126  0.0097  -0.0217 201 A1BN0 C C7  
2192 C C8  . A1BN0 G .   ? 0.2499 0.2347 0.2790 0.0135  0.0118  -0.0192 201 A1BN0 C C8  
2193 C C10 . A1BN0 G .   ? 0.2689 0.2535 0.2998 0.0152  0.0166  -0.0225 201 A1BN0 C C10 
2194 C C13 . A1BN0 G .   ? 0.4099 0.3975 0.3992 0.0039  0.0248  -0.0206 201 A1BN0 C C13 
2195 O O1  . A1BN0 G .   ? 0.2097 0.1948 0.2545 0.0155  0.0094  -0.0157 201 A1BN0 C O1  
2196 C C9  . A1BN0 G .   ? 0.2289 0.2159 0.2667 0.0139  0.0096  -0.0154 201 A1BN0 C C9  
2197 N N4  . A1BN0 G .   ? 0.2150 0.2056 0.2521 0.0122  0.0078  -0.0119 201 A1BN0 C N4  
2198 O O   . A1BN0 G .   ? 0.3203 0.3101 0.3428 0.0134  0.0234  -0.0234 201 A1BN0 C O   
2199 N N2  . A1BN0 G .   ? 0.3751 0.3566 0.3791 0.0100  0.0204  -0.0260 201 A1BN0 C N2  
2200 C C3  . A1BN0 G .   ? 0.3967 0.3806 0.3956 0.0082  0.0219  -0.0244 201 A1BN0 C C3  
2201 C C11 . A1BN0 G .   ? 0.4011 0.3872 0.3995 0.0073  0.0183  -0.0203 201 A1BN0 C C11 
2202 C C12 . A1BN0 G .   ? 0.4057 0.3934 0.3997 0.0054  0.0195  -0.0185 201 A1BN0 C C12 
2203 C C14 . A1BN0 G .   ? 0.4078 0.3939 0.3977 0.0049  0.0292  -0.0251 201 A1BN0 C C14 
2204 N N   . A1BN0 G .   ? 0.4077 0.3936 0.3943 0.0037  0.0359  -0.0288 201 A1BN0 C N   
2205 C C   . A1BN0 G .   ? 0.4102 0.3982 0.3913 0.0006  0.0401  -0.0281 201 A1BN0 C C   
2206 C C2  . A1BN0 G .   ? 0.4054 0.3893 0.4002 0.0072  0.0278  -0.0271 201 A1BN0 C C2  
2207 C C1  . A1BN0 G .   ? 0.4119 0.3954 0.4019 0.0058  0.0383  -0.0332 201 A1BN0 C C1  
# 
