data_7HZB
# 
_entry.id   7HZB 
# 
_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   7HZB         pdb_00007hzb 10.2210/pdb7hzb/pdb 
WWPDB D_1001408119 ?            ?                   
# 
_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                        7HZB 
_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~-(2-chloro-3-methoxyphenyl)piperidine-1,3-dicarboxamide' 311.764   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                         65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                               78.133    1   ?         ? ? ? 
5 water       nat water                                                              18.015    314 ?         ? ? ? 
# 
_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~-(2-chloro-3-methoxyphenyl)piperidine-1,3-dicarboxamide' A1BOV 
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 
A1BOV non-polymer         . '(3S)-N~1~-(2-chloro-3-methoxyphenyl)piperidine-1,3-dicarboxamide' ? 'C14 H18 Cl N3 O3' 311.764 
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 140 146 146 GLU GLU 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 140 146 146 GLU GLU 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        A1BOV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BOV 
_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 A1BOV 1   201 201 A1BOV LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 3 ZN    1   201 1   ZN    ZN  C . 
F 4 DMS   1   202 1   DMS   DMS C . 
G 5 HOH   1   301 177 HOH   HOH A . 
G 5 HOH   2   302 226 HOH   HOH A . 
G 5 HOH   3   303 62  HOH   HOH A . 
G 5 HOH   4   304 314 HOH   HOH A . 
G 5 HOH   5   305 260 HOH   HOH A . 
G 5 HOH   6   306 143 HOH   HOH A . 
G 5 HOH   7   307 286 HOH   HOH A . 
G 5 HOH   8   308 51  HOH   HOH A . 
G 5 HOH   9   309 297 HOH   HOH A . 
G 5 HOH   10  310 118 HOH   HOH A . 
G 5 HOH   11  311 130 HOH   HOH A . 
G 5 HOH   12  312 255 HOH   HOH A . 
G 5 HOH   13  313 212 HOH   HOH A . 
G 5 HOH   14  314 49  HOH   HOH A . 
G 5 HOH   15  315 135 HOH   HOH A . 
G 5 HOH   16  316 124 HOH   HOH A . 
G 5 HOH   17  317 151 HOH   HOH A . 
G 5 HOH   18  318 100 HOH   HOH A . 
G 5 HOH   19  319 126 HOH   HOH A . 
G 5 HOH   20  320 68  HOH   HOH A . 
G 5 HOH   21  321 9   HOH   HOH A . 
G 5 HOH   22  322 198 HOH   HOH A . 
G 5 HOH   23  323 54  HOH   HOH A . 
G 5 HOH   24  324 224 HOH   HOH A . 
G 5 HOH   25  325 120 HOH   HOH A . 
G 5 HOH   26  326 244 HOH   HOH A . 
G 5 HOH   27  327 122 HOH   HOH A . 
G 5 HOH   28  328 247 HOH   HOH A . 
G 5 HOH   29  329 10  HOH   HOH A . 
G 5 HOH   30  330 57  HOH   HOH A . 
G 5 HOH   31  331 142 HOH   HOH A . 
G 5 HOH   32  332 5   HOH   HOH A . 
G 5 HOH   33  333 38  HOH   HOH A . 
G 5 HOH   34  334 99  HOH   HOH A . 
G 5 HOH   35  335 191 HOH   HOH A . 
G 5 HOH   36  336 72  HOH   HOH A . 
G 5 HOH   37  337 121 HOH   HOH A . 
G 5 HOH   38  338 310 HOH   HOH A . 
G 5 HOH   39  339 98  HOH   HOH A . 
G 5 HOH   40  340 25  HOH   HOH A . 
G 5 HOH   41  341 32  HOH   HOH A . 
G 5 HOH   42  342 287 HOH   HOH A . 
G 5 HOH   43  343 167 HOH   HOH A . 
G 5 HOH   44  344 86  HOH   HOH A . 
G 5 HOH   45  345 305 HOH   HOH A . 
G 5 HOH   46  346 95  HOH   HOH A . 
G 5 HOH   47  347 47  HOH   HOH A . 
G 5 HOH   48  348 6   HOH   HOH A . 
G 5 HOH   49  349 254 HOH   HOH A . 
G 5 HOH   50  350 34  HOH   HOH A . 
G 5 HOH   51  351 146 HOH   HOH A . 
G 5 HOH   52  352 123 HOH   HOH A . 
G 5 HOH   53  353 201 HOH   HOH A . 
G 5 HOH   54  354 71  HOH   HOH A . 
G 5 HOH   55  355 271 HOH   HOH A . 
G 5 HOH   56  356 231 HOH   HOH A . 
G 5 HOH   57  357 136 HOH   HOH A . 
G 5 HOH   58  358 21  HOH   HOH A . 
G 5 HOH   59  359 103 HOH   HOH A . 
G 5 HOH   60  360 73  HOH   HOH A . 
G 5 HOH   61  361 2   HOH   HOH A . 
G 5 HOH   62  362 272 HOH   HOH A . 
G 5 HOH   63  363 75  HOH   HOH A . 
G 5 HOH   64  364 267 HOH   HOH A . 
G 5 HOH   65  365 27  HOH   HOH A . 
G 5 HOH   66  366 199 HOH   HOH A . 
G 5 HOH   67  367 203 HOH   HOH A . 
G 5 HOH   68  368 169 HOH   HOH A . 
G 5 HOH   69  369 302 HOH   HOH A . 
G 5 HOH   70  370 309 HOH   HOH A . 
G 5 HOH   71  371 101 HOH   HOH A . 
G 5 HOH   72  372 31  HOH   HOH A . 
G 5 HOH   73  373 285 HOH   HOH A . 
G 5 HOH   74  374 11  HOH   HOH A . 
G 5 HOH   75  375 127 HOH   HOH A . 
G 5 HOH   76  376 274 HOH   HOH A . 
G 5 HOH   77  377 36  HOH   HOH A . 
G 5 HOH   78  378 150 HOH   HOH A . 
G 5 HOH   79  379 28  HOH   HOH A . 
G 5 HOH   80  380 238 HOH   HOH A . 
G 5 HOH   81  381 225 HOH   HOH A . 
G 5 HOH   82  382 182 HOH   HOH A . 
G 5 HOH   83  383 257 HOH   HOH A . 
G 5 HOH   84  384 261 HOH   HOH A . 
G 5 HOH   85  385 163 HOH   HOH A . 
G 5 HOH   86  386 147 HOH   HOH A . 
G 5 HOH   87  387 40  HOH   HOH A . 
G 5 HOH   88  388 113 HOH   HOH A . 
G 5 HOH   89  389 82  HOH   HOH A . 
G 5 HOH   90  390 239 HOH   HOH A . 
G 5 HOH   91  391 35  HOH   HOH A . 
G 5 HOH   92  392 141 HOH   HOH A . 
G 5 HOH   93  393 253 HOH   HOH A . 
G 5 HOH   94  394 109 HOH   HOH A . 
G 5 HOH   95  395 241 HOH   HOH A . 
G 5 HOH   96  396 211 HOH   HOH A . 
G 5 HOH   97  397 70  HOH   HOH A . 
G 5 HOH   98  398 43  HOH   HOH A . 
G 5 HOH   99  399 213 HOH   HOH A . 
G 5 HOH   100 400 129 HOH   HOH A . 
G 5 HOH   101 401 307 HOH   HOH A . 
G 5 HOH   102 402 245 HOH   HOH A . 
G 5 HOH   103 403 115 HOH   HOH A . 
G 5 HOH   104 404 133 HOH   HOH A . 
G 5 HOH   105 405 179 HOH   HOH A . 
G 5 HOH   106 406 256 HOH   HOH A . 
G 5 HOH   107 407 273 HOH   HOH A . 
G 5 HOH   108 408 200 HOH   HOH A . 
G 5 HOH   109 409 308 HOH   HOH A . 
G 5 HOH   110 410 278 HOH   HOH A . 
G 5 HOH   111 411 19  HOH   HOH A . 
G 5 HOH   112 412 4   HOH   HOH A . 
G 5 HOH   113 413 69  HOH   HOH A . 
G 5 HOH   114 414 39  HOH   HOH A . 
G 5 HOH   115 415 313 HOH   HOH A . 
G 5 HOH   116 416 288 HOH   HOH A . 
G 5 HOH   117 417 188 HOH   HOH A . 
G 5 HOH   118 418 173 HOH   HOH A . 
G 5 HOH   119 419 291 HOH   HOH A . 
G 5 HOH   120 420 268 HOH   HOH A . 
G 5 HOH   121 421 222 HOH   HOH A . 
G 5 HOH   122 422 153 HOH   HOH A . 
G 5 HOH   123 423 13  HOH   HOH A . 
G 5 HOH   124 424 171 HOH   HOH A . 
G 5 HOH   125 425 104 HOH   HOH A . 
G 5 HOH   126 426 184 HOH   HOH A . 
G 5 HOH   127 427 165 HOH   HOH A . 
G 5 HOH   128 428 202 HOH   HOH A . 
G 5 HOH   129 429 300 HOH   HOH A . 
G 5 HOH   130 430 164 HOH   HOH A . 
G 5 HOH   131 431 229 HOH   HOH A . 
G 5 HOH   132 432 50  HOH   HOH A . 
G 5 HOH   133 433 292 HOH   HOH A . 
G 5 HOH   134 434 114 HOH   HOH A . 
G 5 HOH   135 435 196 HOH   HOH A . 
G 5 HOH   136 436 58  HOH   HOH A . 
G 5 HOH   137 437 264 HOH   HOH A . 
G 5 HOH   138 438 246 HOH   HOH A . 
G 5 HOH   139 439 311 HOH   HOH A . 
G 5 HOH   140 440 102 HOH   HOH A . 
G 5 HOH   141 441 217 HOH   HOH A . 
G 5 HOH   142 442 236 HOH   HOH A . 
G 5 HOH   143 443 275 HOH   HOH A . 
G 5 HOH   144 444 105 HOH   HOH A . 
G 5 HOH   145 445 282 HOH   HOH A . 
G 5 HOH   146 446 204 HOH   HOH A . 
G 5 HOH   147 447 131 HOH   HOH A . 
G 5 HOH   148 448 280 HOH   HOH A . 
G 5 HOH   149 449 158 HOH   HOH A . 
G 5 HOH   150 450 174 HOH   HOH A . 
G 5 HOH   151 451 227 HOH   HOH A . 
G 5 HOH   152 452 137 HOH   HOH A . 
G 5 HOH   153 453 144 HOH   HOH A . 
G 5 HOH   154 454 281 HOH   HOH A . 
G 5 HOH   155 455 154 HOH   HOH A . 
H 5 HOH   1   301 262 HOH   HOH C . 
H 5 HOH   2   302 91  HOH   HOH C . 
H 5 HOH   3   303 295 HOH   HOH C . 
H 5 HOH   4   304 45  HOH   HOH C . 
H 5 HOH   5   305 157 HOH   HOH C . 
H 5 HOH   6   306 77  HOH   HOH C . 
H 5 HOH   7   307 107 HOH   HOH C . 
H 5 HOH   8   308 209 HOH   HOH C . 
H 5 HOH   9   309 52  HOH   HOH C . 
H 5 HOH   10  310 194 HOH   HOH C . 
H 5 HOH   11  311 140 HOH   HOH C . 
H 5 HOH   12  312 294 HOH   HOH C . 
H 5 HOH   13  313 125 HOH   HOH C . 
H 5 HOH   14  314 93  HOH   HOH C . 
H 5 HOH   15  315 249 HOH   HOH C . 
H 5 HOH   16  316 33  HOH   HOH C . 
H 5 HOH   17  317 186 HOH   HOH C . 
H 5 HOH   18  318 134 HOH   HOH C . 
H 5 HOH   19  319 185 HOH   HOH C . 
H 5 HOH   20  320 132 HOH   HOH C . 
H 5 HOH   21  321 220 HOH   HOH C . 
H 5 HOH   22  322 41  HOH   HOH C . 
H 5 HOH   23  323 219 HOH   HOH C . 
H 5 HOH   24  324 166 HOH   HOH C . 
H 5 HOH   25  325 175 HOH   HOH C . 
H 5 HOH   26  326 26  HOH   HOH C . 
H 5 HOH   27  327 208 HOH   HOH C . 
H 5 HOH   28  328 161 HOH   HOH C . 
H 5 HOH   29  329 12  HOH   HOH C . 
H 5 HOH   30  330 16  HOH   HOH C . 
H 5 HOH   31  331 67  HOH   HOH C . 
H 5 HOH   32  332 111 HOH   HOH C . 
H 5 HOH   33  333 56  HOH   HOH C . 
H 5 HOH   34  334 74  HOH   HOH C . 
H 5 HOH   35  335 79  HOH   HOH C . 
H 5 HOH   36  336 42  HOH   HOH C . 
H 5 HOH   37  337 89  HOH   HOH C . 
H 5 HOH   38  338 3   HOH   HOH C . 
H 5 HOH   39  339 259 HOH   HOH C . 
H 5 HOH   40  340 155 HOH   HOH C . 
H 5 HOH   41  341 306 HOH   HOH C . 
H 5 HOH   42  342 81  HOH   HOH C . 
H 5 HOH   43  343 85  HOH   HOH C . 
H 5 HOH   44  344 180 HOH   HOH C . 
H 5 HOH   45  345 7   HOH   HOH C . 
H 5 HOH   46  346 96  HOH   HOH C . 
H 5 HOH   47  347 178 HOH   HOH C . 
H 5 HOH   48  348 97  HOH   HOH C . 
H 5 HOH   49  349 162 HOH   HOH C . 
H 5 HOH   50  350 30  HOH   HOH C . 
H 5 HOH   51  351 149 HOH   HOH C . 
H 5 HOH   52  352 139 HOH   HOH C . 
H 5 HOH   53  353 14  HOH   HOH C . 
H 5 HOH   54  354 181 HOH   HOH C . 
H 5 HOH   55  355 116 HOH   HOH C . 
H 5 HOH   56  356 44  HOH   HOH C . 
H 5 HOH   57  357 15  HOH   HOH C . 
H 5 HOH   58  358 119 HOH   HOH C . 
H 5 HOH   59  359 80  HOH   HOH C . 
H 5 HOH   60  360 55  HOH   HOH C . 
H 5 HOH   61  361 46  HOH   HOH C . 
H 5 HOH   62  362 24  HOH   HOH C . 
H 5 HOH   63  363 277 HOH   HOH C . 
H 5 HOH   64  364 90  HOH   HOH C . 
H 5 HOH   65  365 23  HOH   HOH C . 
H 5 HOH   66  366 252 HOH   HOH C . 
H 5 HOH   67  367 145 HOH   HOH C . 
H 5 HOH   68  368 266 HOH   HOH C . 
H 5 HOH   69  369 20  HOH   HOH C . 
H 5 HOH   70  370 160 HOH   HOH C . 
H 5 HOH   71  371 53  HOH   HOH C . 
H 5 HOH   72  372 193 HOH   HOH C . 
H 5 HOH   73  373 66  HOH   HOH C . 
H 5 HOH   74  374 61  HOH   HOH C . 
H 5 HOH   75  375 78  HOH   HOH C . 
H 5 HOH   76  376 148 HOH   HOH C . 
H 5 HOH   77  377 18  HOH   HOH C . 
H 5 HOH   78  378 37  HOH   HOH C . 
H 5 HOH   79  379 88  HOH   HOH C . 
H 5 HOH   80  380 242 HOH   HOH C . 
H 5 HOH   81  381 83  HOH   HOH C . 
H 5 HOH   82  382 110 HOH   HOH C . 
H 5 HOH   83  383 48  HOH   HOH C . 
H 5 HOH   84  384 63  HOH   HOH C . 
H 5 HOH   85  385 258 HOH   HOH C . 
H 5 HOH   86  386 84  HOH   HOH C . 
H 5 HOH   87  387 29  HOH   HOH C . 
H 5 HOH   88  388 250 HOH   HOH C . 
H 5 HOH   89  389 168 HOH   HOH C . 
H 5 HOH   90  390 108 HOH   HOH C . 
H 5 HOH   91  391 301 HOH   HOH C . 
H 5 HOH   92  392 276 HOH   HOH C . 
H 5 HOH   93  393 22  HOH   HOH C . 
H 5 HOH   94  394 216 HOH   HOH C . 
H 5 HOH   95  395 214 HOH   HOH C . 
H 5 HOH   96  396 270 HOH   HOH C . 
H 5 HOH   97  397 92  HOH   HOH C . 
H 5 HOH   98  398 159 HOH   HOH C . 
H 5 HOH   99  399 304 HOH   HOH C . 
H 5 HOH   100 400 243 HOH   HOH C . 
H 5 HOH   101 401 8   HOH   HOH C . 
H 5 HOH   102 402 303 HOH   HOH C . 
H 5 HOH   103 403 64  HOH   HOH C . 
H 5 HOH   104 404 112 HOH   HOH C . 
H 5 HOH   105 405 106 HOH   HOH C . 
H 5 HOH   106 406 138 HOH   HOH C . 
H 5 HOH   107 407 17  HOH   HOH C . 
H 5 HOH   108 408 240 HOH   HOH C . 
H 5 HOH   109 409 1   HOH   HOH C . 
H 5 HOH   110 410 65  HOH   HOH C . 
H 5 HOH   111 411 269 HOH   HOH C . 
H 5 HOH   112 412 156 HOH   HOH C . 
H 5 HOH   113 413 251 HOH   HOH C . 
H 5 HOH   114 414 206 HOH   HOH C . 
H 5 HOH   115 415 263 HOH   HOH C . 
H 5 HOH   116 416 176 HOH   HOH C . 
H 5 HOH   117 417 315 HOH   HOH C . 
H 5 HOH   118 418 117 HOH   HOH C . 
H 5 HOH   119 419 195 HOH   HOH C . 
H 5 HOH   120 420 289 HOH   HOH C . 
H 5 HOH   121 421 59  HOH   HOH C . 
H 5 HOH   122 422 190 HOH   HOH C . 
H 5 HOH   123 423 76  HOH   HOH C . 
H 5 HOH   124 424 237 HOH   HOH C . 
H 5 HOH   125 425 283 HOH   HOH C . 
H 5 HOH   126 426 233 HOH   HOH C . 
H 5 HOH   127 427 172 HOH   HOH C . 
H 5 HOH   128 428 60  HOH   HOH C . 
H 5 HOH   129 429 298 HOH   HOH C . 
H 5 HOH   130 430 189 HOH   HOH C . 
H 5 HOH   131 431 170 HOH   HOH C . 
H 5 HOH   132 432 94  HOH   HOH C . 
H 5 HOH   133 433 293 HOH   HOH C . 
H 5 HOH   134 434 265 HOH   HOH C . 
H 5 HOH   135 435 215 HOH   HOH C . 
H 5 HOH   136 436 299 HOH   HOH C . 
H 5 HOH   137 437 230 HOH   HOH C . 
H 5 HOH   138 438 87  HOH   HOH C . 
H 5 HOH   139 439 187 HOH   HOH C . 
H 5 HOH   140 440 296 HOH   HOH C . 
H 5 HOH   141 441 248 HOH   HOH C . 
H 5 HOH   142 442 207 HOH   HOH C . 
H 5 HOH   143 443 223 HOH   HOH C . 
H 5 HOH   144 444 234 HOH   HOH C . 
H 5 HOH   145 445 312 HOH   HOH C . 
H 5 HOH   146 446 205 HOH   HOH C . 
H 5 HOH   147 447 221 HOH   HOH C . 
H 5 HOH   148 448 284 HOH   HOH C . 
H 5 HOH   149 449 152 HOH   HOH C . 
H 5 HOH   150 450 197 HOH   HOH C . 
H 5 HOH   151 451 210 HOH   HOH C . 
H 5 HOH   152 452 218 HOH   HOH C . 
H 5 HOH   153 453 228 HOH   HOH C . 
H 5 HOH   154 454 183 HOH   HOH C . 
H 5 HOH   155 455 290 HOH   HOH C . 
H 5 HOH   156 456 232 HOH   HOH C . 
H 5 HOH   157 457 128 HOH   HOH C . 
H 5 HOH   158 458 279 HOH   HOH C . 
H 5 HOH   159 459 316 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           7HZB 
_cell.length_a           86.814 
_cell.length_b           57.753 
_cell.length_c           65.341 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.87 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HZB 
_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          7HZB 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.57 
_exptl_crystal.density_percent_sol   52.09 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-12-13 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92203 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HZB 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             37.80 
_reflns.d_resolution_high            1.45 
_reflns.number_obs                   55302 
_reflns.percent_possible_obs         97.7 
_reflns.pdbx_Rmerge_I_obs            0.166 
_reflns.pdbx_netI_over_sigmaI        5.6 
_reflns.pdbx_redundancy              6.4 
_reflns.pdbx_Rrim_I_all              0.181 
_reflns.pdbx_Rpim_I_all              0.070 
_reflns.pdbx_CC_half                 0.988 
_reflns.pdbx_number_measured_all     354502 
_reflns.pdbx_chi_squared             0.50 
_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                  1.45 
_reflns_shell.d_res_low                   1.48 
_reflns_shell.number_measured_all         11328 
_reflns_shell.number_unique_obs           2330 
_reflns_shell.Rmerge_I_obs                2.286 
_reflns_shell.pdbx_chi_squared            0.01 
_reflns_shell.pdbx_redundancy             4.9 
_reflns_shell.percent_possible_obs        78.1 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             2.560 
_reflns_shell.pdbx_Rpim_I_all             1.133 
_reflns_shell.pdbx_CC_half                0.325 
_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                                 7HZB 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     43313 
_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                             28.88 
_refine.ls_d_res_high                            1.473 
_refine.ls_percent_reflns_obs                    79.5 
_refine.ls_R_factor_obs                          0.2540 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2529 
_refine.ls_R_factor_R_free                       0.2757 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.990 
_refine.ls_number_reflns_R_free                  2160 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.942 
_refine.correlation_coeff_Fo_to_Fc_free          0.935 
_refine.B_iso_mean                               27.13 
_refine.aniso_B[1][1]                            1.47750 
_refine.aniso_B[2][2]                            -3.13050 
_refine.aniso_B[3][3]                            1.65300 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.30900 
_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             0.110 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.105 
_refine.pdbx_overall_SU_R_Blow_DPI               0.117 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.110 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HZB 
_refine_analyze.Luzzati_coordinate_error_obs    0.30 
_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        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         27 
_refine_hist.number_atoms_solvent             314 
_refine_hist.number_atoms_total               2507 
_refine_hist.d_res_high                       1.473 
_refine_hist.d_res_low                        28.88 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.011 ? 2.00  2265 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.93  ? 2.00  3088 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  760  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  406  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2265 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.49  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.72 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  280  '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  1807 '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                       1.47 
_refine_ls_shell.d_res_low                        1.58 
_refine_ls_shell.number_reflns_R_work             823 
_refine_ls_shell.R_factor_R_work                  0.3968 
_refine_ls_shell.percent_reflns_obs               8.44 
_refine_ls_shell.R_factor_R_free                  0.3589 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.07 
_refine_ls_shell.number_reflns_R_free             44 
_refine_ls_shell.number_reflns_all                867 
_refine_ls_shell.R_factor_all                     0.3950 
# 
_struct.entry_id                  7HZB 
_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-0036304-001 (A71EV2A-x4524)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HZB 
_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 3 ? 
F N N 4 ? 
G N N 5 ? 
H 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 7HZB A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HZB 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,G 
2 1 B,E,F,H 
# 
_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 ? ? ? ? ? ? ? 2.431 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.410 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.412 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.137 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.426 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.393 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 E ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.269 ? ? 
# 
_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_555 110.6 ? 
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_555 103.4 ? 
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_555 116.0 ? 
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_555 106.6 ? 
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_555 105.5 ? 
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_555 114.3 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 112.8 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.4 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.2 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 104.4 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.6 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 111.6 ? 
# 
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 121 ? GLY A 119 GLY A 127 
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 ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
AA3 1 2 N ASP B 29  ? N ASP C 35  O LEU B 34  ? O LEU C 40  
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 ASP B 130 ? O ASP C 136 N HIS B 91  ? N HIS C 97  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7HZB 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    422 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    433 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -99.84  36.67   
2 1 SER A 125 ? ? -131.33 -30.41  
3 1 ASN C 14  ? ? -98.08  36.24   
4 1 SER C 105 ? ? -160.31 114.53  
5 1 CYS C 116 ? ? -125.20 -169.11 
# 
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 14.9152 8.2830   14.5369 0.0423 -0.0954 0.0116 0.0265 0.0066 -0.0029 1.3057 0.7906 0.7057 0.7430  
-0.1082 -0.2982 -0.0463 0.0252  0.1343 0.0140 0.0800 -0.0019 -0.0358 -0.0710 -0.0337 
'X-RAY DIFFRACTION' 2 ? refined 25.7982 -20.4299 17.9409 0.0381 -0.0881 0.0125 0.0227 0.0066 0.0206  0.4681 1.2062 0.5830 -0.0634 
0.0748  -0.1676 0.0025  -0.0066 0.1248 0.0075 0.0747 0.0791  0.0097  0.0100  -0.0772 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BOV N1   N  N N 1   
A1BOV C4   C  Y N 2   
A1BOV C5   C  Y N 3   
A1BOV C6   C  N N 4   
A1BOV C7   C  N N 5   
A1BOV C8   C  N N 6   
A1BOV C10  C  N S 7   
A1BOV C13  C  Y N 8   
A1BOV CL   CL N N 9   
A1BOV C1   C  Y N 10  
A1BOV O    O  N N 11  
A1BOV C    C  N N 12  
A1BOV C3   C  Y N 13  
A1BOV C2   C  Y N 14  
A1BOV N    N  N N 15  
A1BOV O1   O  N N 16  
A1BOV C12  C  N N 17  
A1BOV C11  C  N N 18  
A1BOV O2   O  N N 19  
A1BOV N2   N  N N 20  
A1BOV C9   C  N N 21  
A1BOV H6   H  N N 22  
A1BOV H8   H  N N 23  
A1BOV H9   H  N N 24  
A1BOV H10  H  N N 25  
A1BOV H11  H  N N 26  
A1BOV H    H  N N 27  
A1BOV H1   H  N N 28  
A1BOV H2   H  N N 29  
A1BOV H3   H  N N 30  
A1BOV H5   H  N N 31  
A1BOV H4   H  N N 32  
A1BOV H7   H  N N 33  
A1BOV H16  H  N N 34  
A1BOV H17  H  N N 35  
A1BOV H15  H  N N 36  
A1BOV H14  H  N N 37  
A1BOV H12  H  N N 38  
A1BOV H13  H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
ZN    ZN   ZN N N 440 
# 
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 
A1BOV C   O    sing N N 1   
A1BOV O   C1   sing N N 2   
A1BOV C1  C2   doub Y N 3   
A1BOV C2  C3   sing Y N 4   
A1BOV C3  C4   doub Y N 5   
A1BOV C4  C5   sing Y N 6   
A1BOV N   C5   sing N N 7   
A1BOV C6  N    sing N N 8   
A1BOV O1  C6   doub N N 9   
A1BOV N1  C6   sing N N 10  
A1BOV N1  C7   sing N N 11  
A1BOV C7  C8   sing N N 12  
A1BOV C8  C9   sing N N 13  
A1BOV C9  C10  sing N N 14  
A1BOV C11 C10  sing N N 15  
A1BOV N2  C11  sing N N 16  
A1BOV O2  C11  doub N N 17  
A1BOV C10 C12  sing N N 18  
A1BOV C12 N1   sing N N 19  
A1BOV C5  C13  doub Y N 20  
A1BOV C1  C13  sing Y N 21  
A1BOV C13 CL   sing N N 22  
A1BOV C4  H6   sing N N 23  
A1BOV C7  H8   sing N N 24  
A1BOV C7  H9   sing N N 25  
A1BOV C8  H10  sing N N 26  
A1BOV C8  H11  sing N N 27  
A1BOV C10 H    sing N N 28  
A1BOV C   H1   sing N N 29  
A1BOV C   H2   sing N N 30  
A1BOV C   H3   sing N N 31  
A1BOV C3  H5   sing N N 32  
A1BOV C2  H4   sing N N 33  
A1BOV N   H7   sing N N 34  
A1BOV C12 H16  sing N N 35  
A1BOV C12 H17  sing N N 36  
A1BOV N2  H15  sing N N 37  
A1BOV N2  H14  sing N N 38  
A1BOV C9  H12  sing N N 39  
A1BOV C9  H13  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_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                    7HZB 
_atom_sites.fract_transf_matrix[1][1]   0.011519 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000981 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017315 
_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]   0.015360 
_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  
CL 
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   ? 17.506 8.210   24.963 1.00 23.28 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.766 8.241   24.226 1.00 24.72 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 18.912 7.012   23.300 1.00 24.24 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.247 5.981   23.500 1.00 23.99 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 19.941 8.324   25.190 1.00 27.57 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.080 7.107   25.897 1.00 30.37 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.783 7.138   22.297 1.00 23.43 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.047 6.045   21.360 1.00 23.10 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.515 6.508   19.986 1.00 22.38 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.184 7.610   19.543 1.00 21.78 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.255 5.657   19.290 1.00 21.49 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.772 5.976   17.959 1.00 22.35 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.766 4.727   17.022 1.00 22.51 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.536 3.603   17.492 1.00 21.83 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.194 6.521   18.087 1.00 22.28 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.968 4.940   15.701 1.00 22.64 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.132 3.897   14.690 1.00 22.24 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.593 3.988   14.284 1.00 21.98 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.103 5.098   14.027 1.00 22.55 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.200 4.077   13.445 1.00 22.62 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.746 4.279   13.830 1.00 23.31 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.368 2.913   12.454 1.00 22.68 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.814 4.801   12.638 1.00 23.79 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.300 2.847   14.275 1.00 21.02 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.688 2.831   13.877 1.00 22.03 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.794 1.977   12.592 1.00 22.31 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.727 0.756   12.679 1.00 22.30 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.560 2.237   15.012 1.00 22.01 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.573 3.132   16.236 1.00 22.01 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.344 4.288   16.270 1.00 22.83 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.742 2.873   17.327 1.00 22.45 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.328 5.143   17.374 1.00 23.41 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.721 3.723   18.440 1.00 23.15 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.517 4.860   18.453 1.00 23.93 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.527 5.723   19.535 1.00 25.67 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.872 2.637   11.419 1.00 22.90 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.967 2.004   10.100 1.00 24.12 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.210 2.553   9.407  1.00 24.38 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.427 3.781   9.405  1.00 24.53 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.666 2.180   9.246  1.00 25.01 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.217 3.652   9.144  1.00 25.05 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.818 1.549   7.859  1.00 25.28 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.101 1.652   8.942  1.00 24.22 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.358 2.053   8.318  1.00 24.12 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.164 2.973   9.224  1.00 23.59 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.269 2.713   10.431 1.00 23.15 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.658 4.092   8.678  1.00 23.25 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.329 5.100   9.507  1.00 23.36 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.387 6.292   9.848  1.00 23.59 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.838 7.440   9.992  1.00 23.56 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.634 5.564   8.911  1.00 24.34 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.703 4.510   9.022  1.00 28.13 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.468 4.441   10.005 1.00 30.11 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.768 3.665   8.017  1.00 28.50 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.104 5.985   10.067 1.00 23.23 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.109 7.000   10.441 1.00 23.14 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.440 6.670   11.779 1.00 22.70 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.228 5.484   12.094 1.00 22.60 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.003 7.119   9.372  1.00 23.88 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.479 7.518   7.996  1.00 25.38 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.096 8.747   7.780  1.00 25.83 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.264 6.694   6.898  1.00 26.66 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.503 9.135   6.511  1.00 26.47 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.703 7.055   5.631  1.00 27.62 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.312 8.285   5.439  1.00 27.94 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.747 8.665   4.189  1.00 29.61 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.011 7.745   12.523 1.00 20.79 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.278 7.661   13.773 1.00 19.71 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.019 8.548   13.532 1.00 19.84 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.155 9.736   13.202 1.00 19.01 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.124 8.199   14.972 1.00 20.70 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.310 8.634   16.206 1.00 22.11 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.184 9.013   17.412 1.00 23.79 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.606 10.067  18.257 1.00 25.29 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.968 9.853   19.403 1.00 27.96 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.742 8.614   19.823 1.00 26.98 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.487 10.875  20.101 1.00 27.81 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.805 7.938   13.623 1.00 20.13 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.536 8.645   13.376 1.00 20.27 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.836 8.864   14.704 1.00 21.44 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.487 7.909   15.398 1.00 19.85 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.619 7.883   12.381 1.00 20.73 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.415 8.742   11.981 1.00 21.55 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.399 7.423   11.153 1.00 20.62 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.642 10.140  15.061 1.00 21.64 ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.014 10.536  16.319 0.50 21.47 ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.033 10.525  16.327 0.50 22.29 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.890 11.536  16.085 1.00 21.57 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.814 12.165  15.004 1.00 20.81 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.051 11.158  17.295 0.50 21.42 ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.166 11.125  17.219 0.50 23.92 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 22.897 10.094  17.955 0.50 21.96 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.658 11.656  18.545 0.50 24.87 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.908 12.220  16.607 0.50 20.55 ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.264 10.110  17.460 0.50 24.50 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 18.998 11.701  17.099 1.00 21.08 ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 17.941 12.720  17.084 1.00 20.77 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.719 14.085  17.104 1.00 19.73 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.599 14.255  17.958 1.00 19.12 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.148 12.643  18.389 1.00 21.45 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.242 11.433  18.509 1.00 22.14 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.565 10.445  19.203 1.00 22.14 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.086 11.497  17.855 1.00 21.08 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.418 15.031  16.207 1.00 19.76 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.148 16.333  16.199 1.00 20.34 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.080 17.027  17.589 1.00 21.51 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.070 17.586  18.027 1.00 22.67 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.576 17.272  15.110 1.00 22.81 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.437 18.504  14.778 1.00 23.51 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.621 19.428  13.872 1.00 24.02 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.355 20.612  13.416 1.00 26.12 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.370 21.781  14.060 1.00 28.89 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.738 21.917  15.224 1.00 25.68 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.017 22.827  13.541 1.00 29.24 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 17.940 16.935  18.307 1.00 21.09 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 17.802 17.623  19.606 1.00 22.28 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.640 17.015  20.757 1.00 22.33 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 18.752 17.640  21.825 1.00 22.78 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.329 17.763  20.013 1.00 23.79 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.694 16.491  20.502 1.00 26.36 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.005 15.643  19.640 1.00 27.76 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.600 15.998  21.764 1.00 27.33 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.538 14.662  20.393 1.00 28.28 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.859 14.834  21.683 1.00 28.35 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.238 15.830  20.531 1.00 21.87 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.102 15.142  21.502 1.00 21.75 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.589 15.060  21.033 1.00 22.34 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.413 14.473  21.722 1.00 22.16 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.565 13.746  21.839 1.00 22.60 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.162 13.712  22.431 1.00 24.35 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.677 12.259  22.627 1.00 25.12 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.099 14.500  23.760 1.00 24.72 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 21.924 15.672  19.872 1.00 22.08 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.281 15.681  19.352 1.00 23.52 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.240 16.338  20.369 1.00 24.10 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 23.868 17.311  21.034 1.00 23.64 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.325 16.448  18.027 1.00 23.54 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.433 15.745  20.535 1.00 23.90 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.467 16.257  21.450 1.00 24.23 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.381 17.276  20.720 1.00 24.44 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.285 17.410  19.493 1.00 24.30 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.317 15.060  21.958 1.00 25.80 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.036 14.494  20.849 1.00 26.05 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.474 13.980  22.660 1.00 26.60 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.326 17.940  21.451 1.00 25.17 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.301 18.841  20.825 1.00 26.74 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.156 18.028  19.838 1.00 26.26 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.324 18.454  18.705 1.00 26.16 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.204 19.544  21.861 1.00 28.31 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.390 20.253  21.246 1.00 34.61 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.258 21.495  20.643 1.00 37.44 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.679 19.837  21.110 1.00 37.13 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.469 21.816  20.198 1.00 38.78 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.361 20.852  20.456 1.00 39.20 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.609 16.828  20.237 1.00 25.94 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.387 15.975  19.339 1.00 26.35 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.651 15.683  18.000 1.00 25.48 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.281 15.754  16.944 1.00 25.74 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.815 14.679  20.028 1.00 29.07 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.740 13.854  19.170 1.00 35.34 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 33.898 14.226  18.924 1.00 38.09 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.244 12.740  18.659 1.00 36.18 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.329 15.399  18.049 1.00 24.14 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.509 15.191  16.848 1.00 23.61 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.554 16.442  15.942 1.00 23.84 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.771 16.300  14.740 1.00 23.76 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.041 14.898  17.209 1.00 22.89 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.802 13.535  17.836 1.00 22.98 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.537 12.583  17.486 1.00 22.14 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 25.902 13.431  18.707 1.00 23.72 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.335 17.655  16.514 1.00 23.17 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.397 18.905  15.737 1.00 23.74 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.819 19.181  15.180 1.00 23.78 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 29.955 19.699  14.079 1.00 23.15 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 27.872 20.111  16.552 1.00 24.25 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.380 20.188  16.663 1.00 25.41 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.616 19.811  17.728 1.00 26.46 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.464 20.639  15.647 1.00 26.01 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.283 20.055  17.465 1.00 26.91 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.162 20.536  16.180 1.00 26.69 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.618 21.098  14.334 1.00 26.43 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.031 20.926  15.458 1.00 27.54 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.505 21.470  13.620 1.00 27.28 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.229 21.396  14.180 1.00 27.97 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.864 18.780  15.920 1.00 24.07 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.264 18.950  15.509 1.00 24.63 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.692 17.941  14.409 1.00 24.43 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.739 18.117  13.773 1.00 24.72 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.183 18.846  16.727 1.00 25.32 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.871 16.881  14.180 1.00 23.92 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.131 15.841  13.165 1.00 24.41 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.880 15.627  12.303 1.00 24.04 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.560 14.493  11.926 1.00 23.79 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.580 14.521  13.839 1.00 26.15 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.892 14.664  14.565 1.00 30.34 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 34.979 14.555  13.969 1.00 32.11 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 33.830 14.934  15.873 1.00 30.80 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.171 16.743  12.002 1.00 23.46 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 28.922 16.768  11.269 1.00 23.54 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.007 16.279  9.840  1.00 23.68 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.856 16.737  9.078  1.00 24.48 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.319 18.207  11.286 1.00 23.13 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 26.941 18.336  10.676 1.00 23.86 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 25.913 17.515  11.472 1.00 24.23 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.508 19.791  10.539 1.00 24.55 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.068 15.407  9.446  1.00 23.20 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 27.962 14.937  8.068  1.00 22.59 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.728 15.631  7.431  1.00 22.70 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.832 16.212  6.362  1.00 22.28 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.836 13.382  7.989  1.00 21.50 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.367 12.925  6.604  1.00 21.21 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.154 12.702  8.361  1.00 21.05 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.567 15.565  8.115  1.00 22.20 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.295 16.104  7.633  1.00 23.40 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.329 16.301  8.801  1.00 23.59 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.361 15.536  9.758  1.00 22.00 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.682 15.082  6.628  1.00 24.24 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.281 15.358  6.177  1.00 25.78 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.893 16.209  5.185  1.00 27.42 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.079 14.707  6.641  1.00 25.64 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.525 16.157  5.027  1.00 27.86 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 19.998 15.274  5.938  1.00 26.87 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.808 13.765  7.641  1.00 25.73 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.662 14.877  6.157  1.00 27.26 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.493 13.368  7.851  1.00 26.39 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.435 13.932  7.124  1.00 26.83 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.471 17.337  8.729  1.00 23.59 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.478 17.577  9.757  1.00 23.25 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.243 18.204  9.141  1.00 24.25 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.342 18.968  8.174  1.00 25.22 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.024 18.433  10.925 1.00 23.76 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.633 19.782  10.539 1.00 24.99 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.677 20.954  10.360 1.00 29.69 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.049 21.914  9.650  1.00 32.91 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.548 20.908  10.899 1.00 29.69 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.073 17.880  9.692  1.00 23.45 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.829 18.454  9.218  1.00 24.67 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.869 18.650  10.386 1.00 25.22 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.292 17.673  10.881 1.00 25.61 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.204 17.564  8.123  1.00 26.54 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.055 18.197  7.372  1.00 31.51 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.332 19.016  7.973  1.00 32.33 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.861 17.854  6.185  1.00 34.16 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.677 19.918  10.804 1.00 24.44 ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.765 20.271  11.892 0.50 24.54 ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.772 20.224  11.907 0.50 24.49 ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.320 19.824  11.619 1.00 24.44 ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.646 19.335  12.524 1.00 25.32 ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.818 21.773  12.181 0.50 25.09 ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 15.882 21.688  12.336 0.50 24.83 ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 14.884 22.150  13.180 0.50 26.18 ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.662 22.550  11.236 0.50 25.64 ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.831 19.981  10.373 1.00 23.97 ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.453 19.582  10.039 1.00 23.77 ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.178 18.064  10.246 1.00 23.56 ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.031 17.689  10.440 1.00 25.21 ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.067 20.014  8.623  1.00 24.71 ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.640 19.201  7.613  1.00 27.79 ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.220 17.213  10.179 1.00 21.80 ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.150 15.750  10.367 1.00 21.20 ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.627 15.289  11.773 1.00 21.12 ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.471 14.108  12.100 1.00 20.51 ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.014 15.030  9.309  1.00 20.97 ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.543 15.239  7.872  1.00 22.14 ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.415 14.510  6.874  1.00 24.12 ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.314 13.053  7.026  1.00 24.37 ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.509 12.185  6.031  1.00 25.93 ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.794 12.620  4.802  1.00 23.44 ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.373 10.874  6.245  1.00 24.59 ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.253 16.204  12.567 1.00 20.39 ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.818 15.866  13.878 1.00 20.40 ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 15.970 14.866  13.705 1.00 20.57 ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.189 14.026  14.585 1.00 21.90 ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.761 15.324  14.872 1.00 22.32 ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.316 15.076  16.284 1.00 24.57 ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.176 15.876  16.740 1.00 22.18 ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 13.897 14.070  16.932 1.00 26.38 ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.764 14.993  12.620 1.00 19.37 ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.890 14.072  12.415 1.00 18.96 ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.229 14.809  12.298 1.00 20.03 ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.283 15.912  11.748 1.00 19.96 ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.704 13.226  11.159 1.00 18.85 ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.628 12.126  11.185 1.00 19.97 ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.558 11.399  9.849  1.00 19.68 ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.901 11.124  12.292 1.00 20.01 ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.310 14.118  12.722 1.00 19.97 ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.684 14.581  12.613 1.00 20.51 ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.532 13.327  12.443 1.00 21.28 ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.275 12.292  13.075 1.00 21.65 ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.144 15.356  13.869 1.00 19.23 ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.552 15.998  13.770 1.00 20.47 ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.579 17.360  14.415 1.00 21.16 ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.654 15.066  14.409 1.00 20.26 ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.488 13.399  11.536 1.00 19.81 ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.420 12.299  11.275 1.00 20.01 ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.850 12.809  11.451 1.00 20.94 ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.209 13.817  10.857 1.00 21.66 ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.241 11.666  9.881  1.00 19.98 ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.292 10.570  9.655  1.00 20.85 ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.819 11.130  9.685  1.00 20.15 ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.660 12.112  12.243 1.00 20.54 ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.068 12.479  12.421 1.00 21.25 ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 28.970 11.296  11.972 1.00 21.78 ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.482 10.160  11.824 1.00 20.82 ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.359 12.870  13.867 1.00 21.79 ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.092 11.797  14.750 1.00 23.75 ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.259 11.569  11.719 1.00 23.09 ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.177 10.494  11.296 1.00 24.21 ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.816 9.803   12.508 1.00 24.53 ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 31.984 10.435  13.572 1.00 23.85 ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.255 11.029  10.361 1.00 26.63 ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.047 11.981  11.051 1.00 30.29 ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.186 8.500   12.346 1.00 24.54 ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.789 7.713   13.429 1.00 24.83 ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.085 7.055   12.992 1.00 26.40 ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.275 6.813   11.801 1.00 26.35 ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.807 6.622   13.945 1.00 25.57 ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.505 5.692   12.893 1.00 25.74 ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.534 7.204   14.502 1.00 25.77 ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.954 6.720   13.963 1.00 27.10 ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.213 6.047   13.669 1.00 29.16 ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 35.987 4.535   13.505 1.00 29.22 ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.537 3.941   12.588 1.00 29.66 ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.277 6.392   14.722 1.00 32.72 ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.811 5.989   16.009 1.00 34.66 ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.615 7.875   14.737 1.00 33.55 ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.157 3.935   14.375 1.00 29.51 ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.824 2.512   14.311 1.00 30.53 ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.649 2.238   13.361 1.00 30.47 ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.717 3.045   13.282 1.00 30.26 ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.478 1.996   15.704 1.00 31.27 ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.675 1.076   12.670 1.00 29.85 ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.590 0.669   11.782 1.00 29.23 ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.450 0.066   12.599 1.00 28.43 ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.691 -0.723  13.523 1.00 28.21 ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.074 -0.330  10.731 1.00 31.72 ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.601 0.351   9.473  1.00 37.31 ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 33.899 -0.646  8.398  1.00 43.97 ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 34.515 -1.701  8.649  1.00 45.31 ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.487 -0.327  7.176  1.00 45.60 ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.233 0.495   12.280 1.00 26.87 ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.024 0.049   12.949 1.00 26.91 ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.494 -1.258  12.399 1.00 26.53 ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.913 -1.716  11.331 1.00 26.45 ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.548 -1.862  13.135 1.00 26.71 ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.993 -3.159  12.767 1.00 26.89 ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.554 -3.126  12.277 1.00 25.86 ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 25.075 -4.157  11.784 1.00 26.07 ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.151 -4.147  13.920 1.00 27.61 ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.867 -4.630  14.245 1.00 30.85 ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.835 -1.984  12.452 1.00 24.19 ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.446 -1.905  12.015 1.00 23.29 ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.324 -1.856  10.492 1.00 24.13 ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.189 -1.307  9.819  1.00 24.29 ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.726 -0.692  12.641 1.00 21.69 ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.662 -0.730  14.167 1.00 22.99 ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.278 -1.794  14.722 1.00 23.11 ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.983 0.309   14.812 1.00 23.35 ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.265 -2.455  9.962  1.00 24.21 ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 21.970 -2.419  8.522  1.00 25.44 ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.698 -1.609  8.329  1.00 25.03 ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.747 -1.841  9.074  1.00 26.45 ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.748 -3.838  7.979  1.00 27.82 ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 22.997 -4.542  8.067  1.00 30.48 ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 21.267 -3.838  6.530  1.00 29.20 ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.640 -0.709  7.328  1.00 23.86 ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.428 0.079   7.098  1.00 23.80 ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.470 -0.715  6.219  1.00 24.11 ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.898 -1.305  5.221  1.00 23.87 ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.727 1.475   6.468  1.00 23.81 ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.818 2.236   7.277  1.00 24.59 ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.440 2.338   6.353  1.00 24.13 ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.433 2.524   8.742  1.00 25.47 ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.181 -0.714  6.571  1.00 24.18 ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.160 -1.371  5.757  1.00 24.46 ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.922 -0.533  4.486  1.00 24.95 ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.922 0.705   4.530  1.00 25.00 ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.855 -1.466  6.527  1.00 24.43 ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.669 -1.216  3.367  1.00 24.54 ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.369 -0.541  2.107  1.00 24.80 ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 14.073 -1.244  1.651  1.00 26.06 ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 14.116 -2.286  0.970  1.00 25.80 ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.534 -0.722  1.108  1.00 25.08 ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.871 -0.073  1.542  1.00 27.16 ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.841 1.443   1.841  1.00 26.74 ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.143 1.908   2.362  1.00 24.87 ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.352 3.058   3.001  1.00 25.42 ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.362 3.929   3.160  1.00 23.30 ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.564 3.366   3.450  1.00 24.58 ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.922 -0.712  2.111  1.00 26.34 ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.628 -1.390  1.943  1.00 27.44 ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.434 -0.421  2.205  1.00 27.84 ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.643 0.739   2.542  1.00 28.17 ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.601 -2.508  2.970  1.00 28.73 ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.539 -1.866  4.662  1.00 30.75 ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 9.191  -0.958  2.205  1.00 29.00 ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 8.028  -0.146  2.543  1.00 31.42 ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.174  -0.799  3.647  1.00 32.17 ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.963  -0.559  3.710  1.00 33.56 ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 7.196  0.261   1.305  1.00 35.88 ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.547  -0.884  0.569  1.00 43.24 ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 6.929  -2.054  0.828  1.00 43.41 ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.668  -0.614  -0.290 1.00 47.92 ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.823  -1.576  4.548  1.00 30.94 ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.176  -2.204  5.702  1.00 29.29 ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.386  -1.189  6.547  1.00 27.68 ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.819  -0.058  6.732  1.00 28.48 ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.192  -2.948  6.570  1.00 29.88 ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.815  -4.505  5.870  1.00 30.67 ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.220  -1.608  7.046  1.00 25.60 ? 59  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 53  ? 4.396  -0.843  7.982  1.00 23.98 ? 59  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 53  ? 4.186  -1.603  9.312  1.00 21.94 ? 59  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 53  ? 3.375  -1.190  10.133 1.00 21.80 ? 59  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 53  ? 3.070  -0.401  7.381  1.00 25.80 ? 59  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 53  ? 3.187  0.759   6.432  1.00 30.07 ? 59  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 53  ? 1.802  1.288   6.103  1.00 35.29 ? 59  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 53  ? 1.319  1.179   4.970  1.00 36.43 ? 59  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 53  ? 1.103  1.840   7.099  1.00 35.56 ? 59  GLN   A NE2 1 
ATOM   419  N  N   . THR   A 1 54  ? 4.952  -2.692  9.534  1.00 21.58 ? 60  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 54  ? 4.984  -3.409  10.790 1.00 22.14 ? 60  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 54  ? 6.457  -3.673  11.157 1.00 21.37 ? 60  THR   A C   1 
ATOM   422  O  O   . THR   A 1 54  ? 7.318  -3.946  10.303 1.00 21.94 ? 60  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 54  ? 4.156  -4.698  10.755 1.00 25.33 ? 60  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 54  ? 4.789  -5.637  9.884  1.00 28.13 ? 60  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 54  ? 2.712  -4.468  10.349 1.00 26.04 ? 60  THR   A CG2 1 
ATOM   426  N  N   . GLY   A 1 55  ? 6.736  -3.543  12.438 1.00 19.67 ? 61  GLY   A N   1 
ATOM   427  C  CA  . GLY   A 1 55  ? 8.074  -3.767  12.957 1.00 19.51 ? 61  GLY   A CA  1 
ATOM   428  C  C   . GLY   A 1 55  ? 8.069  -3.888  14.468 1.00 18.86 ? 61  GLY   A C   1 
ATOM   429  O  O   . GLY   A 1 55  ? 7.027  -4.127  15.079 1.00 19.24 ? 61  GLY   A O   1 
ATOM   430  N  N   . VAL   A 1 56  ? 9.212  -3.647  15.088 1.00 17.44 ? 62  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 56  ? 9.387  -3.747  16.534 1.00 16.69 ? 62  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 56  ? 10.263 -2.579  16.991 1.00 16.84 ? 62  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 56  ? 11.266 -2.305  16.349 1.00 17.35 ? 62  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 56  ? 10.062 -5.108  16.826 1.00 17.51 ? 62  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 56  ? 10.548 -5.189  18.269 1.00 18.78 ? 62  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 56  ? 9.131  -6.281  16.477 1.00 17.78 ? 62  VAL   A CG2 1 
ATOM   437  N  N   . TYR   A 1 57  ? 9.901  -1.881  18.079 1.00 17.54 ? 63  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 10.729 -0.751  18.572 1.00 17.96 ? 63  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 11.198 -0.936  20.035 1.00 18.44 ? 63  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 10.502 -1.591  20.794 1.00 19.31 ? 63  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 10.010 0.608   18.381 1.00 18.68 ? 63  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 9.025  0.988   19.475 1.00 20.02 ? 63  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 7.764  0.410   19.538 1.00 20.88 ? 63  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 9.365  1.906   20.463 1.00 20.58 ? 63  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 6.847  0.777   20.515 1.00 21.04 ? 63  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 8.455  2.273   21.458 1.00 20.71 ? 63  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 7.211  1.676   21.498 1.00 21.31 ? 63  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 6.277  2.038   22.426 1.00 22.89 ? 63  TYR   A OH  1 
ATOM   449  N  N   . TYR   A 1 58  ? 12.319 -0.302  20.443 1.00 17.68 ? 64  TYR   A N   1 
ATOM   450  C  CA  . TYR   A 1 58  ? 12.795 -0.402  21.826 1.00 17.90 ? 64  TYR   A CA  1 
ATOM   451  C  C   . TYR   A 1 58  ? 12.307 0.774   22.639 1.00 18.77 ? 64  TYR   A C   1 
ATOM   452  O  O   . TYR   A 1 58  ? 12.519 1.924   22.252 1.00 18.89 ? 64  TYR   A O   1 
ATOM   453  C  CB  . TYR   A 1 58  ? 14.324 -0.522  21.937 1.00 18.12 ? 64  TYR   A CB  1 
ATOM   454  C  CG  . TYR   A 1 58  ? 14.784 -0.669  23.369 1.00 18.13 ? 64  TYR   A CG  1 
ATOM   455  C  CD1 . TYR   A 1 58  ? 14.392 -1.759  24.134 1.00 18.83 ? 64  TYR   A CD1 1 
ATOM   456  C  CD2 . TYR   A 1 58  ? 15.577 0.304   23.970 1.00 18.14 ? 64  TYR   A CD2 1 
ATOM   457  C  CE1 . TYR   A 1 58  ? 14.768 -1.876  25.465 1.00 19.71 ? 64  TYR   A CE1 1 
ATOM   458  C  CE2 . TYR   A 1 58  ? 15.962 0.201   25.296 1.00 19.22 ? 64  TYR   A CE2 1 
ATOM   459  C  CZ  . TYR   A 1 58  ? 15.574 -0.902  26.036 1.00 20.66 ? 64  TYR   A CZ  1 
ATOM   460  O  OH  . TYR   A 1 58  ? 15.957 -1.006  27.341 1.00 22.66 ? 64  TYR   A OH  1 
ATOM   461  N  N   . CYS   A 1 59  ? 11.670 0.476   23.789 1.00 18.69 ? 65  CYS   A N   1 
ATOM   462  C  CA  . CYS   A 1 59  ? 11.110 1.474   24.703 1.00 19.15 ? 65  CYS   A CA  1 
ATOM   463  C  C   . CYS   A 1 59  ? 11.940 1.479   26.011 1.00 19.21 ? 65  CYS   A C   1 
ATOM   464  O  O   . CYS   A 1 59  ? 11.743 0.587   26.847 1.00 19.23 ? 65  CYS   A O   1 
ATOM   465  C  CB  . CYS   A 1 59  ? 9.644  1.156   24.985 1.00 20.88 ? 65  CYS   A CB  1 
ATOM   466  S  SG  . CYS   A 1 59  ? 8.877  2.247   26.219 1.00 24.83 ? 65  CYS   A SG  1 
ATOM   467  N  N   . SER   A 1 60  ? 12.878 2.448   26.173 1.00 18.49 ? 66  SER   A N   1 
ATOM   468  C  CA  . SER   A 1 60  ? 13.736 2.484   27.364 1.00 20.05 ? 66  SER   A CA  1 
ATOM   469  C  C   . SER   A 1 60  ? 12.963 2.621   28.700 1.00 20.33 ? 66  SER   A C   1 
ATOM   470  O  O   . SER   A 1 60  ? 13.370 2.023   29.702 1.00 21.80 ? 66  SER   A O   1 
ATOM   471  C  CB  . SER   A 1 60  ? 14.826 3.550   27.237 1.00 23.61 ? 66  SER   A CB  1 
ATOM   472  O  OG  . SER   A 1 60  ? 14.369 4.887   27.349 1.00 28.43 ? 66  SER   A OG  1 
ATOM   473  N  N   . SER   A 1 61  ? 11.831 3.383   28.719 1.00 19.20 ? 67  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 61  ? 10.974 3.611   29.896 1.00 19.22 ? 67  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 61  ? 10.228 2.344   30.390 1.00 20.00 ? 67  SER   A C   1 
ATOM   476  O  O   . SER   A 1 61  ? 9.580  2.395   31.442 1.00 20.52 ? 67  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 61  ? 9.964  4.732   29.640 1.00 19.70 ? 67  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 61  ? 9.131  4.435   28.529 1.00 19.80 ? 67  SER   A OG  1 
ATOM   479  N  N   . ARG   A 1 62  ? 10.348 1.217   29.646 1.00 19.53 ? 68  ARG   A N   1 
ATOM   480  C  CA  . ARG   A 1 62  ? 9.750  -0.075  29.989 1.00 20.16 ? 68  ARG   A CA  1 
ATOM   481  C  C   . ARG   A 1 62  ? 10.761 -1.242  29.854 1.00 21.18 ? 68  ARG   A C   1 
ATOM   482  O  O   . ARG   A 1 62  ? 10.376 -2.402  30.073 1.00 22.35 ? 68  ARG   A O   1 
ATOM   483  C  CB  . ARG   A 1 62  ? 8.573  -0.373  29.047 1.00 22.23 ? 68  ARG   A CB  1 
ATOM   484  C  CG  . ARG   A 1 62  ? 7.407  0.604   29.185 1.00 23.73 ? 68  ARG   A CG  1 
ATOM   485  C  CD  . ARG   A 1 62  ? 6.608  0.312   30.418 1.00 23.96 ? 68  ARG   A CD  1 
ATOM   486  N  NE  . ARG   A 1 62  ? 5.513  1.260   30.584 1.00 24.50 ? 68  ARG   A NE  1 
ATOM   487  C  CZ  . ARG   A 1 62  ? 5.596  2.407   31.245 1.00 23.68 ? 68  ARG   A CZ  1 
ATOM   488  N  NH1 . ARG   A 1 62  ? 6.736  2.770   31.820 1.00 21.83 ? 68  ARG   A NH1 1 
ATOM   489  N  NH2 . ARG   A 1 62  ? 4.532  3.198   31.348 1.00 23.35 ? 68  ARG   A NH2 1 
ATOM   490  N  N   . ARG   A 1 63  ? 12.004 -0.964  29.424 1.00 20.32 ? 69  ARG   A N   1 
ATOM   491  C  CA  . ARG   A 1 63  ? 13.040 -1.996  29.164 1.00 21.41 ? 69  ARG   A CA  1 
ATOM   492  C  C   . ARG   A 1 63  ? 12.464 -3.124  28.259 1.00 22.18 ? 69  ARG   A C   1 
ATOM   493  O  O   . ARG   A 1 63  ? 12.639 -4.307  28.542 1.00 22.26 ? 69  ARG   A O   1 
ATOM   494  C  CB  . ARG   A 1 63  ? 13.582 -2.590  30.472 1.00 22.71 ? 69  ARG   A CB  1 
ATOM   495  C  CG  . ARG   A 1 63  ? 14.947 -2.043  30.810 1.00 26.06 ? 69  ARG   A CG  1 
ATOM   496  C  CD  . ARG   A 1 63  ? 15.484 -2.528  32.146 1.00 26.00 ? 69  ARG   A CD  1 
ATOM   497  N  NE  . ARG   A 1 63  ? 16.232 -1.460  32.810 1.00 26.92 ? 69  ARG   A NE  1 
ATOM   498  C  CZ  . ARG   A 1 63  ? 16.004 -1.043  34.054 1.00 28.10 ? 69  ARG   A CZ  1 
ATOM   499  N  NH1 . ARG   A 1 63  ? 15.059 -1.618  34.793 1.00 27.41 ? 69  ARG   A NH1 1 
ATOM   500  N  NH2 . ARG   A 1 63  ? 16.734 -0.065  34.577 1.00 27.61 ? 69  ARG   A NH2 1 
ATOM   501  N  N   . LYS   A 1 64  ? 11.669 -2.736  27.260 1.00 21.74 ? 70  LYS   A N   1 
ATOM   502  C  CA  . LYS   A 1 64  ? 10.974 -3.705  26.403 1.00 22.85 ? 70  LYS   A CA  1 
ATOM   503  C  C   . LYS   A 1 64  ? 10.920 -3.327  24.945 1.00 22.65 ? 70  LYS   A C   1 
ATOM   504  O  O   . LYS   A 1 64  ? 10.784 -2.149  24.607 1.00 22.33 ? 70  LYS   A O   1 
ATOM   505  C  CB  . LYS   A 1 64  ? 9.524  -3.891  26.887 1.00 26.73 ? 70  LYS   A CB  1 
ATOM   506  C  CG  . LYS   A 1 64  ? 9.376  -4.943  27.976 1.00 34.76 ? 70  LYS   A CG  1 
ATOM   507  C  CD  . LYS   A 1 64  ? 7.925  -5.303  28.209 1.00 43.08 ? 70  LYS   A CD  1 
ATOM   508  C  CE  . LYS   A 1 64  ? 7.748  -5.928  29.577 1.00 48.56 ? 70  LYS   A CE  1 
ATOM   509  N  NZ  . LYS   A 1 64  ? 8.312  -5.057  30.647 1.00 51.99 ? 70  LYS   A NZ  1 
ATOM   510  N  N   . HIS   A 1 65  ? 10.939 -4.360  24.078 1.00 21.68 ? 71  HIS   A N   1 
ATOM   511  C  CA  . HIS   A 1 65  ? 10.787 -4.211  22.630 1.00 21.53 ? 71  HIS   A CA  1 
ATOM   512  C  C   . HIS   A 1 65  ? 9.323  -4.543  22.332 1.00 21.36 ? 71  HIS   A C   1 
ATOM   513  O  O   . HIS   A 1 65  ? 8.821  -5.584  22.781 1.00 21.58 ? 71  HIS   A O   1 
ATOM   514  C  CB  . HIS   A 1 65  ? 11.702 -5.205  21.871 1.00 21.78 ? 71  HIS   A CB  1 
ATOM   515  C  CG  . HIS   A 1 65  ? 13.167 -4.947  22.051 1.00 23.81 ? 71  HIS   A CG  1 
ATOM   516  N  ND1 . HIS   A 1 65  ? 13.890 -4.213  21.133 1.00 26.65 ? 71  HIS   A ND1 1 
ATOM   517  C  CD2 . HIS   A 1 65  ? 13.998 -5.341  23.037 1.00 24.31 ? 71  HIS   A CD2 1 
ATOM   518  C  CE1 . HIS   A 1 65  ? 15.129 -4.178  21.587 1.00 25.72 ? 71  HIS   A CE1 1 
ATOM   519  N  NE2 . HIS   A 1 65  ? 15.247 -4.842  22.720 1.00 25.75 ? 71  HIS   A NE2 1 
ATOM   520  N  N   . TYR   A 1 66  ? 8.610  -3.642  21.644 1.00 20.18 ? 72  TYR   A N   1 
ATOM   521  C  CA  . TYR   A 1 66  ? 7.186  -3.867  21.352 1.00 19.68 ? 72  TYR   A CA  1 
ATOM   522  C  C   . TYR   A 1 66  ? 6.904  -3.999  19.866 1.00 18.58 ? 72  TYR   A C   1 
ATOM   523  O  O   . TYR   A 1 66  ? 7.346  -3.155  19.079 1.00 18.78 ? 72  TYR   A O   1 
ATOM   524  C  CB  . TYR   A 1 66  ? 6.323  -2.697  21.867 1.00 19.42 ? 72  TYR   A CB  1 
ATOM   525  C  CG  . TYR   A 1 66  ? 6.284  -2.529  23.380 1.00 20.48 ? 72  TYR   A CG  1 
ATOM   526  C  CD1 . TYR   A 1 66  ? 5.434  -3.301  24.167 1.00 21.78 ? 72  TYR   A CD1 1 
ATOM   527  C  CD2 . TYR   A 1 66  ? 7.043  -1.551  24.009 1.00 21.46 ? 72  TYR   A CD2 1 
ATOM   528  C  CE1 . TYR   A 1 66  ? 5.341  -3.102  25.548 1.00 23.61 ? 72  TYR   A CE1 1 
ATOM   529  C  CE2 . TYR   A 1 66  ? 6.981  -1.361  25.380 1.00 22.75 ? 72  TYR   A CE2 1 
ATOM   530  C  CZ  . TYR   A 1 66  ? 6.132  -2.143  26.151 1.00 24.51 ? 72  TYR   A CZ  1 
ATOM   531  O  OH  . TYR   A 1 66  ? 6.038  -1.942  27.509 1.00 26.62 ? 72  TYR   A OH  1 
ATOM   532  N  N   . PRO   A 1 67  ? 6.082  -4.993  19.469 1.00 18.30 ? 73  PRO   A N   1 
ATOM   533  C  CA  . PRO   A 1 67  ? 5.674  -5.051  18.052 1.00 18.14 ? 73  PRO   A CA  1 
ATOM   534  C  C   . PRO   A 1 67  ? 4.623  -3.967  17.775 1.00 19.45 ? 73  PRO   A C   1 
ATOM   535  O  O   . PRO   A 1 67  ? 3.695  -3.801  18.576 1.00 20.00 ? 73  PRO   A O   1 
ATOM   536  C  CB  . PRO   A 1 67  ? 5.049  -6.455  17.891 1.00 18.66 ? 73  PRO   A CB  1 
ATOM   537  C  CG  . PRO   A 1 67  ? 4.692  -6.902  19.299 1.00 19.70 ? 73  PRO   A CG  1 
ATOM   538  C  CD  . PRO   A 1 67  ? 5.430  -6.032  20.306 1.00 17.60 ? 73  PRO   A CD  1 
ATOM   539  N  N   . VAL   A 1 68  ? 4.747  -3.252  16.659 1.00 18.37 ? 74  VAL   A N   1 
ATOM   540  C  CA  . VAL   A 1 68  ? 3.781  -2.202  16.317 1.00 19.09 ? 74  VAL   A CA  1 
ATOM   541  C  C   . VAL   A 1 68  ? 3.507  -2.142  14.802 1.00 19.37 ? 74  VAL   A C   1 
ATOM   542  O  O   . VAL   A 1 68  ? 4.335  -2.560  13.993 1.00 18.88 ? 74  VAL   A O   1 
ATOM   543  C  CB  . VAL   A 1 68  ? 4.279  -0.799  16.778 1.00 20.58 ? 74  VAL   A CB  1 
ATOM   544  C  CG1 . VAL   A 1 68  ? 4.325  -0.665  18.281 1.00 20.86 ? 74  VAL   A CG1 1 
ATOM   545  C  CG2 . VAL   A 1 68  ? 5.619  -0.455  16.149 1.00 21.08 ? 74  VAL   A CG2 1 
ATOM   546  N  N   . SER   A 1 69  ? 2.375  -1.552  14.448 1.00 19.88 ? 75  SER   A N   1 
ATOM   547  C  CA  . SER   A 1 69  ? 1.983  -1.179  13.098 1.00 21.74 ? 75  SER   A CA  1 
ATOM   548  C  C   . SER   A 1 69  ? 2.159  0.344   13.082 1.00 21.24 ? 75  SER   A C   1 
ATOM   549  O  O   . SER   A 1 69  ? 1.745  1.030   14.049 1.00 20.46 ? 75  SER   A O   1 
ATOM   550  C  CB  . SER   A 1 69  ? 0.517  -1.512  12.839 1.00 25.38 ? 75  SER   A CB  1 
ATOM   551  O  OG  . SER   A 1 69  ? 0.328  -2.917  12.810 1.00 28.95 ? 75  SER   A OG  1 
ATOM   552  N  N   . PHE   A 1 70  ? 2.804  0.862   12.031 1.00 19.87 ? 76  PHE   A N   1 
ATOM   553  C  CA  . PHE   A 1 70  ? 3.113  2.283   11.897 1.00 20.23 ? 76  PHE   A CA  1 
ATOM   554  C  C   . PHE   A 1 70  ? 2.736  2.864   10.532 1.00 20.72 ? 76  PHE   A C   1 
ATOM   555  O  O   . PHE   A 1 70  ? 2.778  2.165   9.499  1.00 20.85 ? 76  PHE   A O   1 
ATOM   556  C  CB  . PHE   A 1 70  ? 4.599  2.564   12.230 1.00 19.04 ? 76  PHE   A CB  1 
ATOM   557  C  CG  . PHE   A 1 70  ? 5.616  1.765   11.435 1.00 18.92 ? 76  PHE   A CG  1 
ATOM   558  C  CD1 . PHE   A 1 70  ? 6.073  0.541   11.892 1.00 18.59 ? 76  PHE   A CD1 1 
ATOM   559  C  CD2 . PHE   A 1 70  ? 6.168  2.275   10.267 1.00 19.11 ? 76  PHE   A CD2 1 
ATOM   560  C  CE1 . PHE   A 1 70  ? 7.024  -0.188  11.157 1.00 19.57 ? 76  PHE   A CE1 1 
ATOM   561  C  CE2 . PHE   A 1 70  ? 7.133  1.553   9.543  1.00 19.23 ? 76  PHE   A CE2 1 
ATOM   562  C  CZ  . PHE   A 1 70  ? 7.551  0.335   9.984  1.00 18.33 ? 76  PHE   A CZ  1 
ATOM   563  N  N   . SER   A 1 71  ? 2.367  4.151   10.519 1.00 21.77 ? 77  SER   A N   1 
ATOM   564  C  CA  . SER   A 1 71  ? 1.959  4.872   9.305  1.00 22.13 ? 77  SER   A CA  1 
ATOM   565  C  C   . SER   A 1 71  ? 3.144  5.153   8.337  1.00 21.96 ? 77  SER   A C   1 
ATOM   566  O  O   . SER   A 1 71  ? 4.288  4.949   8.705  1.00 22.50 ? 77  SER   A O   1 
ATOM   567  C  CB  . SER   A 1 71  ? 1.241  6.177   9.671  1.00 23.86 ? 77  SER   A CB  1 
ATOM   568  O  OG  . SER   A 1 71  ? 2.099  7.076   10.364 1.00 25.02 ? 77  SER   A OG  1 
ATOM   569  N  N   . LYS   A 1 72  ? 2.863  5.551   7.089  1.00 22.11 ? 78  LYS   A N   1 
ATOM   570  C  CA  . LYS   A 1 72  ? 3.925  5.851   6.119  1.00 23.41 ? 78  LYS   A CA  1 
ATOM   571  C  C   . LYS   A 1 72  ? 4.612  7.186   6.461  1.00 23.82 ? 78  LYS   A C   1 
ATOM   572  O  O   . LYS   A 1 72  ? 3.971  8.053   7.062  1.00 23.36 ? 78  LYS   A O   1 
ATOM   573  C  CB  . LYS   A 1 72  ? 3.343  5.854   4.697  1.00 25.84 ? 78  LYS   A CB  1 
ATOM   574  C  CG  . LYS   A 1 72  ? 2.887  4.460   4.264  1.00 31.35 ? 78  LYS   A CG  1 
ATOM   575  C  CD  . LYS   A 1 72  ? 2.821  4.331   2.743  1.00 38.65 ? 78  LYS   A CD  1 
ATOM   576  C  CE  . LYS   A 1 72  ? 2.414  2.936   2.317  1.00 44.10 ? 78  LYS   A CE  1 
ATOM   577  N  NZ  . LYS   A 1 72  ? 2.794  2.643   0.906  1.00 47.03 ? 78  LYS   A NZ  1 
ATOM   578  N  N   . PRO   A 1 73  ? 5.898  7.403   6.086  1.00 25.23 ? 79  PRO   A N   1 
ATOM   579  C  CA  . PRO   A 1 73  ? 6.548  8.693   6.411  1.00 25.46 ? 79  PRO   A CA  1 
ATOM   580  C  C   . PRO   A 1 73  ? 5.708  9.892   5.891  1.00 26.42 ? 79  PRO   A C   1 
ATOM   581  O  O   . PRO   A 1 73  ? 5.231  9.870   4.749  1.00 26.39 ? 79  PRO   A O   1 
ATOM   582  C  CB  . PRO   A 1 73  ? 7.914  8.600   5.722  1.00 27.35 ? 79  PRO   A CB  1 
ATOM   583  C  CG  . PRO   A 1 73  ? 8.143  7.146   5.469  1.00 28.24 ? 79  PRO   A CG  1 
ATOM   584  C  CD  . PRO   A 1 73  ? 6.811  6.472   5.389  1.00 25.77 ? 79  PRO   A CD  1 
ATOM   585  N  N   . SER   A 1 74  ? 5.435  10.874  6.761  1.00 26.82 ? 80  SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 4.561  12.007  6.422  1.00 28.16 ? 80  SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 4.929  13.311  7.180  1.00 27.76 ? 80  SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 5.744  13.278  8.094  1.00 26.60 ? 80  SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 3.109  11.656  6.761  1.00 31.91 ? 80  SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 2.742  10.346  6.362  1.00 37.90 ? 80  SER   A OG  1 
ATOM   591  N  N   . LEU   A 1 75  ? 4.247  14.436  6.825  1.00 28.39 ? 81  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 75  ? 4.374  15.757  7.444  1.00 29.98 ? 81  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 75  ? 3.305  15.814  8.553  1.00 31.50 ? 81  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 75  ? 2.114  15.843  8.254  1.00 32.73 ? 81  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 75  ? 4.086  16.853  6.378  1.00 30.68 ? 81  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 75  ? 4.550  18.272  6.726  1.00 33.26 ? 81  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 75  ? 6.063  18.341  6.848  1.00 33.42 ? 81  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 75  ? 4.092  19.278  5.668  1.00 34.04 ? 81  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 76  ? 3.714  15.782  9.823  1.00 31.41 ? 82  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 76  ? 2.794  15.743  10.962 1.00 32.13 ? 82  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 76  ? 3.058  16.902  11.929 1.00 33.09 ? 82  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 76  ? 4.210  17.232  12.176 1.00 31.93 ? 82  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 76  ? 2.965  14.379  11.685 1.00 31.91 ? 82  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 76  ? 2.518  13.205  10.796 1.00 33.08 ? 82  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 76  ? 2.276  14.344  13.043 1.00 32.28 ? 82  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 76  ? 2.953  11.864  11.313 1.00 34.13 ? 82  ILE   A CD1 1 
ATOM   607  N  N   . PHE   A 1 77  ? 1.992  17.487  12.511 1.00 34.17 ? 83  PHE   A N   1 
ATOM   608  C  CA  . PHE   A 1 77  ? 2.172  18.569  13.476 1.00 35.30 ? 83  PHE   A CA  1 
ATOM   609  C  C   . PHE   A 1 77  ? 2.548  17.997  14.846 1.00 34.64 ? 83  PHE   A C   1 
ATOM   610  O  O   . PHE   A 1 77  ? 1.885  17.088  15.354 1.00 34.82 ? 83  PHE   A O   1 
ATOM   611  C  CB  . PHE   A 1 77  ? 0.907  19.424  13.583 1.00 36.56 ? 83  PHE   A CB  1 
ATOM   612  C  CG  . PHE   A 1 77  ? 1.108  20.721  14.324 1.00 38.89 ? 83  PHE   A CG  1 
ATOM   613  C  CD1 . PHE   A 1 77  ? 1.819  21.761  13.751 1.00 40.43 ? 83  PHE   A CD1 1 
ATOM   614  C  CD2 . PHE   A 1 77  ? 0.528  20.927  15.564 1.00 40.63 ? 83  PHE   A CD2 1 
ATOM   615  C  CE1 . PHE   A 1 77  ? 1.988  22.962  14.428 1.00 41.76 ? 83  PHE   A CE1 1 
ATOM   616  C  CE2 . PHE   A 1 77  ? 0.682  22.134  16.230 1.00 41.37 ? 83  PHE   A CE2 1 
ATOM   617  C  CZ  . PHE   A 1 77  ? 1.393  23.149  15.650 1.00 41.70 ? 83  PHE   A CZ  1 
ATOM   618  N  N   . VAL   A 1 78  ? 3.634  18.524  15.423 1.00 33.86 ? 84  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 78  ? 4.161  18.138  16.727 1.00 33.87 ? 84  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 78  ? 4.051  19.358  17.639 1.00 34.98 ? 84  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 78  ? 4.485  20.443  17.255 1.00 34.51 ? 84  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 78  ? 5.643  17.674  16.622 1.00 33.51 ? 84  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 78  ? 6.142  17.138  17.966 1.00 33.90 ? 84  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 78  ? 5.831  16.637  15.513 1.00 33.16 ? 84  VAL   A CG2 1 
ATOM   625  N  N   . GLU   A 1 79  ? 3.478  19.173  18.842 1.00 36.39 ? 85  GLU   A N   1 
ATOM   626  C  CA  . GLU   A 1 79  ? 3.290  20.236  19.832 1.00 38.04 ? 85  GLU   A CA  1 
ATOM   627  C  C   . GLU   A 1 79  ? 4.614  20.806  20.305 1.00 38.74 ? 85  GLU   A C   1 
ATOM   628  O  O   . GLU   A 1 79  ? 5.633  20.103  20.264 1.00 38.67 ? 85  GLU   A O   1 
ATOM   629  C  CB  . GLU   A 1 79  ? 2.491  19.709  21.045 1.00 41.46 ? 85  GLU   A CB  1 
ATOM   630  C  CG  . GLU   A 1 79  ? 1.019  19.448  20.758 1.00 48.29 ? 85  GLU   A CG  1 
ATOM   631  C  CD  . GLU   A 1 79  ? 0.279  20.627  20.155 1.00 56.62 ? 85  GLU   A CD  1 
ATOM   632  O  OE1 . GLU   A 1 79  ? 0.257  21.705  20.792 1.00 57.84 ? 85  GLU   A OE1 1 
ATOM   633  O  OE2 . GLU   A 1 79  ? -0.265 20.481  19.037 1.00 59.52 ? 85  GLU   A OE2 1 
ATOM   634  N  N   . ALA   A 1 80  ? 4.598  22.059  20.808 1.00 39.31 ? 86  ALA   A N   1 
ATOM   635  C  CA  . ALA   A 1 80  ? 5.801  22.717  21.321 1.00 40.58 ? 86  ALA   A CA  1 
ATOM   636  C  C   . ALA   A 1 80  ? 6.401  21.917  22.471 1.00 41.44 ? 86  ALA   A C   1 
ATOM   637  O  O   . ALA   A 1 80  ? 5.670  21.416  23.322 1.00 41.69 ? 86  ALA   A O   1 
ATOM   638  C  CB  . ALA   A 1 80  ? 5.477  24.130  21.793 1.00 41.19 ? 86  ALA   A CB  1 
ATOM   639  N  N   . SER   A 1 81  ? 7.715  21.695  22.419 1.00 41.75 ? 87  SER   A N   1 
ATOM   640  C  CA  . SER   A 1 81  ? 8.485  20.998  23.455 1.00 42.28 ? 87  SER   A CA  1 
ATOM   641  C  C   . SER   A 1 81  ? 9.570  21.984  23.975 1.00 42.14 ? 87  SER   A C   1 
ATOM   642  O  O   . SER   A 1 81  ? 9.610  23.134  23.521 1.00 42.76 ? 87  SER   A O   1 
ATOM   643  C  CB  . SER   A 1 81  ? 9.146  19.746  22.871 1.00 43.98 ? 87  SER   A CB  1 
ATOM   644  O  OG  . SER   A 1 81  ? 10.216 20.087  22.002 1.00 46.57 ? 87  SER   A OG  1 
ATOM   645  N  N   . GLU   A 1 82  ? 10.493 21.535  24.854 1.00 41.50 ? 88  GLU   A N   1 
ATOM   646  C  CA  . GLU   A 1 82  ? 11.606 22.401  25.283 1.00 41.28 ? 88  GLU   A CA  1 
ATOM   647  C  C   . GLU   A 1 82  ? 12.717 22.501  24.185 1.00 39.27 ? 88  GLU   A C   1 
ATOM   648  O  O   . GLU   A 1 82  ? 13.563 23.396  24.246 1.00 38.96 ? 88  GLU   A O   1 
ATOM   649  C  CB  . GLU   A 1 82  ? 12.201 21.921  26.624 1.00 44.95 ? 88  GLU   A CB  1 
ATOM   650  C  CG  . GLU   A 1 82  ? 12.563 20.448  26.645 1.00 52.55 ? 88  GLU   A CG  1 
ATOM   651  C  CD  . GLU   A 1 82  ? 13.503 20.013  27.756 1.00 61.79 ? 88  GLU   A CD  1 
ATOM   652  O  OE1 . GLU   A 1 82  ? 13.466 18.816  28.126 1.00 63.48 ? 88  GLU   A OE1 1 
ATOM   653  O  OE2 . GLU   A 1 82  ? 14.286 20.860  28.246 1.00 64.69 ? 88  GLU   A OE2 1 
ATOM   654  N  N   . TYR   A 1 83  ? 12.685 21.596  23.169 1.00 37.59 ? 89  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 83  ? 13.649 21.515  22.068 1.00 36.26 ? 89  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 83  ? 13.157 22.153  20.768 1.00 34.32 ? 89  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 83  ? 13.979 22.550  19.942 1.00 33.61 ? 89  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 83  ? 13.990 20.043  21.775 1.00 36.61 ? 89  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 83  ? 14.495 19.292  22.984 1.00 37.46 ? 89  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 83  ? 15.809 19.428  23.412 1.00 38.26 ? 89  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 83  ? 13.648 18.481  23.728 1.00 38.76 ? 89  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 83  ? 16.277 18.753  24.531 1.00 39.21 ? 89  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 83  ? 14.105 17.797  24.847 1.00 39.83 ? 89  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 83  ? 15.420 17.940  25.250 1.00 40.57 ? 89  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 83  ? 15.876 17.269  26.358 1.00 42.14 ? 89  TYR   A OH  1 
ATOM   666  N  N   . TYR   A 1 84  ? 11.832 22.227  20.558 1.00 33.22 ? 90  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 84  ? 11.300 22.774  19.293 1.00 32.37 ? 90  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 84  ? 10.031 23.568  19.554 1.00 34.47 ? 90  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 84  ? 9.218  23.157  20.392 1.00 34.82 ? 90  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 84  ? 10.908 21.631  18.304 1.00 29.66 ? 90  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 84  ? 12.041 20.778  17.757 1.00 26.60 ? 90  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 84  ? 12.981 21.312  16.885 1.00 25.19 ? 90  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 84  ? 12.163 19.436  18.111 1.00 25.68 ? 90  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 84  ? 13.995 20.522  16.360 1.00 24.73 ? 90  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 84  ? 13.169 18.641  17.590 1.00 24.85 ? 90  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 84  ? 14.100 19.202  16.745 1.00 24.09 ? 90  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 84  ? 15.124 18.487  16.206 1.00 22.49 ? 90  TYR   A OH  1 
ATOM   678  N  N   . PRO   A 1 85  ? 9.768  24.623  18.763 1.00 35.88 ? 91  PRO   A N   1 
ATOM   679  C  CA  . PRO   A 1 85  ? 8.434  25.252  18.830 1.00 37.27 ? 91  PRO   A CA  1 
ATOM   680  C  C   . PRO   A 1 85  ? 7.388  24.344  18.108 1.00 38.33 ? 91  PRO   A C   1 
ATOM   681  O  O   . PRO   A 1 85  ? 7.786  23.428  17.359 1.00 38.40 ? 91  PRO   A O   1 
ATOM   682  C  CB  . PRO   A 1 85  ? 8.645  26.579  18.088 1.00 37.86 ? 91  PRO   A CB  1 
ATOM   683  C  CG  . PRO   A 1 85  ? 9.714  26.272  17.084 1.00 37.62 ? 91  PRO   A CG  1 
ATOM   684  C  CD  . PRO   A 1 85  ? 10.601 25.210  17.685 1.00 35.56 ? 91  PRO   A CD  1 
ATOM   685  N  N   . ALA   A 1 86  ? 6.059  24.582  18.295 1.00 38.52 ? 92  ALA   A N   1 
ATOM   686  C  CA  . ALA   A 1 86  ? 5.022  23.747  17.641 1.00 38.58 ? 92  ALA   A CA  1 
ATOM   687  C  C   . ALA   A 1 86  ? 5.183  23.895  16.119 1.00 37.25 ? 92  ALA   A C   1 
ATOM   688  O  O   . ALA   A 1 86  ? 5.105  25.017  15.609 1.00 37.40 ? 92  ALA   A O   1 
ATOM   689  C  CB  . ALA   A 1 86  ? 3.632  24.202  18.066 1.00 38.90 ? 92  ALA   A CB  1 
ATOM   690  N  N   . ARG   A 1 87  ? 5.538  22.801  15.423 1.00 35.11 ? 93  ARG   A N   1 
ATOM   691  C  CA  . ARG   A 1 87  ? 5.815  22.854  13.987 1.00 33.20 ? 93  ARG   A CA  1 
ATOM   692  C  C   . ARG   A 1 87  ? 5.376  21.535  13.266 1.00 32.09 ? 93  ARG   A C   1 
ATOM   693  O  O   . ARG   A 1 87  ? 4.953  20.579  13.919 1.00 31.98 ? 93  ARG   A O   1 
ATOM   694  C  CB  . ARG   A 1 87  ? 7.340  23.109  13.789 1.00 33.09 ? 93  ARG   A CB  1 
ATOM   695  C  CG  . ARG   A 1 87  ? 8.206  21.816  13.865 1.00 32.38 ? 93  ARG   A CG  1 
ATOM   696  C  CD  . ARG   A 1 87  ? 9.491  21.910  14.658 1.00 31.58 ? 93  ARG   A CD  1 
ATOM   697  N  NE  . ARG   A 1 87  ? 10.452 20.860  14.268 1.00 30.39 ? 93  ARG   A NE  1 
ATOM   698  C  CZ  . ARG   A 1 87  ? 10.466 19.629  14.773 1.00 29.95 ? 93  ARG   A CZ  1 
ATOM   699  N  NH1 . ARG   A 1 87  ? 9.561  19.263  15.679 1.00 28.47 ? 93  ARG   A NH1 1 
ATOM   700  N  NH2 . ARG   A 1 87  ? 11.381 18.750  14.372 1.00 27.65 ? 93  ARG   A NH2 1 
ATOM   701  N  N   . TYR   A 1 88  ? 5.528  21.488  11.926 1.00 31.07 ? 94  TYR   A N   1 
ATOM   702  C  CA  . TYR   A 1 88  ? 5.282  20.304  11.120 1.00 30.30 ? 94  TYR   A CA  1 
ATOM   703  C  C   . TYR   A 1 88  ? 6.604  19.572  10.953 1.00 28.93 ? 94  TYR   A C   1 
ATOM   704  O  O   . TYR   A 1 88  ? 7.559  20.144  10.421 1.00 29.91 ? 94  TYR   A O   1 
ATOM   705  C  CB  . TYR   A 1 88  ? 4.709  20.664  9.735  1.00 31.20 ? 94  TYR   A CB  1 
ATOM   706  C  CG  . TYR   A 1 88  ? 3.226  20.955  9.803  1.00 33.12 ? 94  TYR   A CG  1 
ATOM   707  C  CD1 . TYR   A 1 88  ? 2.299  19.923  9.871  1.00 34.23 ? 94  TYR   A CD1 1 
ATOM   708  C  CD2 . TYR   A 1 88  ? 2.760  22.256  9.926  1.00 34.63 ? 94  TYR   A CD2 1 
ATOM   709  C  CE1 . TYR   A 1 88  ? 0.943  20.179  10.017 1.00 35.56 ? 94  TYR   A CE1 1 
ATOM   710  C  CE2 . TYR   A 1 88  ? 1.404  22.527  10.054 1.00 36.09 ? 94  TYR   A CE2 1 
ATOM   711  C  CZ  . TYR   A 1 88  ? 0.497  21.483  10.109 1.00 37.24 ? 94  TYR   A CZ  1 
ATOM   712  O  OH  . TYR   A 1 88  ? -0.843 21.755  10.236 1.00 40.32 ? 94  TYR   A OH  1 
ATOM   713  N  N   . GLN   A 1 89  ? 6.687  18.336  11.453 1.00 26.57 ? 95  GLN   A N   1 
ATOM   714  C  CA  . GLN   A 1 89  ? 7.891  17.534  11.277 1.00 24.62 ? 95  GLN   A CA  1 
ATOM   715  C  C   . GLN   A 1 89  ? 7.661  16.621  10.071 1.00 24.80 ? 95  GLN   A C   1 
ATOM   716  O  O   . GLN   A 1 89  ? 6.577  16.036  9.923  1.00 25.28 ? 95  GLN   A O   1 
ATOM   717  C  CB  . GLN   A 1 89  ? 8.224  16.723  12.554 1.00 23.53 ? 95  GLN   A CB  1 
ATOM   718  C  CG  . GLN   A 1 89  ? 9.414  15.790  12.402 1.00 21.17 ? 95  GLN   A CG  1 
ATOM   719  C  CD  . GLN   A 1 89  ? 9.987  15.316  13.737 1.00 22.41 ? 95  GLN   A CD  1 
ATOM   720  O  OE1 . GLN   A 1 89  ? 10.036 16.058  14.747 1.00 24.18 ? 95  GLN   A OE1 1 
ATOM   721  N  NE2 . GLN   A 1 89  ? 10.452 14.079  13.758 1.00 21.06 ? 95  GLN   A NE2 1 
ATOM   722  N  N   . SER   A 1 90  ? 8.673  16.504  9.197  1.00 23.93 ? 96  SER   A N   1 
ATOM   723  C  CA  . SER   A 1 90  ? 8.577  15.675  8.010  1.00 23.61 ? 96  SER   A CA  1 
ATOM   724  C  C   . SER   A 1 90  ? 9.216  14.291  8.212  1.00 22.63 ? 96  SER   A C   1 
ATOM   725  O  O   . SER   A 1 90  ? 10.010 14.089  9.137  1.00 22.34 ? 96  SER   A O   1 
ATOM   726  C  CB  . SER   A 1 90  ? 9.242  16.371  6.823  1.00 25.84 ? 96  SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 90  ? 10.634 16.537  7.047  1.00 27.73 ? 96  SER   A OG  1 
ATOM   728  N  N   . HIS   A 1 91  ? 8.854  13.349  7.329  1.00 22.53 ? 97  HIS   A N   1 
ATOM   729  C  CA  . HIS   A 1 91  ? 9.369  11.983  7.334  1.00 23.59 ? 97  HIS   A CA  1 
ATOM   730  C  C   . HIS   A 1 91  ? 9.109  11.272  8.698  1.00 23.02 ? 97  HIS   A C   1 
ATOM   731  O  O   . HIS   A 1 91  ? 9.894  10.411  9.117  1.00 23.19 ? 97  HIS   A O   1 
ATOM   732  C  CB  . HIS   A 1 91  ? 10.843 11.926  6.890  1.00 25.19 ? 97  HIS   A CB  1 
ATOM   733  C  CG  . HIS   A 1 91  ? 11.104 12.540  5.539  1.00 28.68 ? 97  HIS   A CG  1 
ATOM   734  N  ND1 . HIS   A 1 91  ? 11.172 11.770  4.392  1.00 30.87 ? 97  HIS   A ND1 1 
ATOM   735  C  CD2 . HIS   A 1 91  ? 11.304 13.834  5.200  1.00 30.20 ? 97  HIS   A CD2 1 
ATOM   736  C  CE1 . HIS   A 1 91  ? 11.429 12.610  3.401  1.00 31.32 ? 97  HIS   A CE1 1 
ATOM   737  N  NE2 . HIS   A 1 91  ? 11.515 13.861  3.839  1.00 31.13 ? 97  HIS   A NE2 1 
ATOM   738  N  N   . LEU   A 1 92  ? 7.977  11.603  9.338  1.00 21.31 ? 98  LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? 7.548  11.051  10.632 1.00 21.52 ? 98  LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? 6.474  9.954   10.412 1.00 21.87 ? 98  LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? 5.629  10.089  9.541  1.00 23.14 ? 98  LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? 6.984  12.180  11.540 1.00 21.79 ? 98  LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? 6.742  11.826  13.032 1.00 23.43 ? 98  LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? 8.024  11.381  13.716 1.00 23.48 ? 98  LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? 6.116  13.007  13.781 1.00 24.51 ? 98  LEU   A CD2 1 
ATOM   746  N  N   . MET   A 1 93  ? 6.528  8.885   11.202 1.00 21.33 ? 99  MET   A N   1 
ATOM   747  C  CA  . MET   A 1 93  ? 5.594  7.752   11.143 1.00 21.31 ? 99  MET   A CA  1 
ATOM   748  C  C   . MET   A 1 93  ? 5.050  7.568   12.556 1.00 22.01 ? 99  MET   A C   1 
ATOM   749  O  O   . MET   A 1 93  ? 5.843  7.556   13.505 1.00 23.05 ? 99  MET   A O   1 
ATOM   750  C  CB  . MET   A 1 93  ? 6.359  6.474   10.719 1.00 21.12 ? 99  MET   A CB  1 
ATOM   751  C  CG  . MET   A 1 93  ? 7.119  6.608   9.380  1.00 23.29 ? 99  MET   A CG  1 
ATOM   752  S  SD  . MET   A 1 93  ? 8.206  5.176   8.973  1.00 27.72 ? 99  MET   A SD  1 
ATOM   753  C  CE  . MET   A 1 93  ? 9.397  5.320   10.269 1.00 26.22 ? 99  MET   A CE  1 
ATOM   754  N  N   . LEU   A 1 94  ? 3.718  7.396   12.711 1.00 20.98 ? 100 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 94  ? 3.078  7.226   14.010 1.00 20.82 ? 100 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 94  ? 2.597  5.790   14.241 1.00 20.70 ? 100 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 94  ? 2.189  5.094   13.306 1.00 20.98 ? 100 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 94  ? 1.849  8.171   14.156 1.00 20.86 ? 100 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 94  ? 2.135  9.669   14.236 1.00 23.91 ? 100 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 94  ? 0.830  10.460  14.467 1.00 24.90 ? 100 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 94  ? 3.133  10.005  15.392 1.00 24.73 ? 100 LEU   A CD2 1 
ATOM   762  N  N   . ALA   A 1 95  ? 2.602  5.393   15.501 1.00 20.71 ? 101 ALA   A N   1 
ATOM   763  C  CA  . ALA   A 1 95  ? 2.156  4.088   15.975 1.00 21.80 ? 101 ALA   A CA  1 
ATOM   764  C  C   . ALA   A 1 95  ? 1.546  4.259   17.386 1.00 21.43 ? 101 ALA   A C   1 
ATOM   765  O  O   . ALA   A 1 95  ? 1.882  5.199   18.121 1.00 21.67 ? 101 ALA   A O   1 
ATOM   766  C  CB  . ALA   A 1 95  ? 3.357  3.125   16.051 1.00 21.96 ? 101 ALA   A CB  1 
ATOM   767  N  N   . VAL   A 1 96  ? 0.716  3.293   17.789 1.00 20.94 ? 102 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 96  ? 0.162  3.281   19.131 1.00 22.19 ? 102 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 96  ? 1.172  2.587   20.030 1.00 24.16 ? 102 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 96  ? 1.576  1.463   19.746 1.00 25.95 ? 102 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 96  ? -1.235 2.608   19.152 1.00 21.98 ? 102 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 96  ? -1.723 2.363   20.584 1.00 22.19 ? 102 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 96  ? -2.227 3.471   18.387 1.00 22.05 ? 102 VAL   A CG2 1 
ATOM   774  N  N   . GLY   A 1 97  ? 1.621  3.273   21.056 1.00 24.08 ? 103 GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 97  ? 2.586  2.700   21.977 1.00 24.76 ? 103 GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 97  ? 3.096  3.669   23.001 1.00 24.82 ? 103 GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 97  ? 2.870  4.877   22.899 1.00 25.14 ? 103 GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 98  ? 3.786  3.114   24.006 1.00 24.34 ? 104 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 98  ? 4.342  3.907   25.087 1.00 23.56 ? 104 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 98  ? 5.619  4.629   24.680 1.00 23.33 ? 104 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 98  ? 6.561  4.000   24.174 1.00 22.97 ? 104 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 98  ? 4.589  3.047   26.354 1.00 22.85 ? 104 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 98  ? 4.852  3.906   27.556 1.00 23.77 ? 104 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 98  ? 3.862  4.708   28.096 1.00 24.87 ? 104 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 98  ? 6.015  4.158   28.208 1.00 25.13 ? 104 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 98  ? 4.440  5.393   29.074 1.00 25.06 ? 104 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 98  ? 5.736  5.099   29.176 1.00 25.79 ? 104 HIS   A NE2 1 
ATOM   788  N  N   . SER   A 1 99  ? 5.700  5.916   25.028 1.00 24.12 ? 105 SER   A N   1 
ATOM   789  C  CA  . SER   A 1 99  ? 6.857  6.748   24.746 1.00 25.44 ? 105 SER   A CA  1 
ATOM   790  C  C   . SER   A 1 99  ? 6.918  7.951   25.735 1.00 26.42 ? 105 SER   A C   1 
ATOM   791  O  O   . SER   A 1 99  ? 5.938  8.667   25.901 1.00 27.41 ? 105 SER   A O   1 
ATOM   792  C  CB  . SER   A 1 99  ? 6.807  7.232   23.294 1.00 28.52 ? 105 SER   A CB  1 
ATOM   793  O  OG  . SER   A 1 99  ? 7.874  8.106   22.944 1.00 33.78 ? 105 SER   A OG  1 
ATOM   794  N  N   . GLU   A 1 100 ? 8.053  8.152   26.394 1.00 25.45 ? 106 GLU   A N   1 
ATOM   795  C  CA  . GLU   A 1 100 ? 8.322  9.323   27.249 1.00 26.41 ? 106 GLU   A CA  1 
ATOM   796  C  C   . GLU   A 1 100 ? 9.487  10.128  26.573 1.00 26.89 ? 106 GLU   A C   1 
ATOM   797  O  O   . GLU   A 1 100 ? 10.124 9.587   25.653 1.00 27.20 ? 106 GLU   A O   1 
ATOM   798  C  CB  . GLU   A 1 100 ? 8.680  8.898   28.694 1.00 27.19 ? 106 GLU   A CB  1 
ATOM   799  C  CG  . GLU   A 1 100 ? 7.534  8.203   29.407 1.00 27.50 ? 106 GLU   A CG  1 
ATOM   800  C  CD  . GLU   A 1 100 ? 7.847  7.464   30.703 1.00 30.34 ? 106 GLU   A CD  1 
ATOM   801  O  OE1 . GLU   A 1 100 ? 8.778  7.878   31.435 1.00 29.65 ? 106 GLU   A OE1 1 
ATOM   802  O  OE2 . GLU   A 1 100 ? 7.122  6.488   31.004 1.00 28.60 ? 106 GLU   A OE2 1 
ATOM   803  N  N   . PRO   A 1 101 ? 9.792  11.394  26.970 1.00 26.74 ? 107 PRO   A N   1 
ATOM   804  C  CA  . PRO   A 1 101 ? 10.866 12.144  26.257 1.00 26.25 ? 107 PRO   A CA  1 
ATOM   805  C  C   . PRO   A 1 101 ? 12.200 11.396  26.061 1.00 24.41 ? 107 PRO   A C   1 
ATOM   806  O  O   . PRO   A 1 101 ? 12.758 11.379  24.945 1.00 24.63 ? 107 PRO   A O   1 
ATOM   807  C  CB  . PRO   A 1 101 ? 11.042 13.424  27.094 1.00 27.60 ? 107 PRO   A CB  1 
ATOM   808  C  CG  . PRO   A 1 101 ? 9.701  13.630  27.748 1.00 28.09 ? 107 PRO   A CG  1 
ATOM   809  C  CD  . PRO   A 1 101 ? 9.100  12.246  27.965 1.00 26.77 ? 107 PRO   A CD  1 
ATOM   810  N  N   . GLY   A 1 102 ? 12.698 10.788  27.145 1.00 22.30 ? 108 GLY   A N   1 
ATOM   811  C  CA  . GLY   A 1 102 ? 13.936 10.007  27.175 1.00 21.72 ? 108 GLY   A CA  1 
ATOM   812  C  C   . GLY   A 1 102 ? 13.932 8.758   26.307 1.00 20.48 ? 108 GLY   A C   1 
ATOM   813  O  O   . GLY   A 1 102 ? 14.979 8.113   26.173 1.00 21.38 ? 108 GLY   A O   1 
ATOM   814  N  N   . ASP   A 1 103 ? 12.761 8.351   25.755 1.00 19.26 ? 109 ASP   A N   1 
ATOM   815  C  CA  . ASP   A 1 103 ? 12.666 7.201   24.822 1.00 20.07 ? 109 ASP   A CA  1 
ATOM   816  C  C   . ASP   A 1 103 ? 13.206 7.521   23.381 1.00 20.45 ? 109 ASP   A C   1 
ATOM   817  O  O   . ASP   A 1 103 ? 13.453 6.601   22.581 1.00 19.92 ? 109 ASP   A O   1 
ATOM   818  C  CB  . ASP   A 1 103 ? 11.242 6.636   24.781 1.00 19.91 ? 109 ASP   A CB  1 
ATOM   819  C  CG  . ASP   A 1 103 ? 10.875 5.879   26.045 1.00 22.10 ? 109 ASP   A CG  1 
ATOM   820  O  OD1 . ASP   A 1 103 ? 11.746 5.203   26.601 1.00 20.04 ? 109 ASP   A OD1 1 
ATOM   821  O  OD2 . ASP   A 1 103 ? 9.700  5.935   26.445 1.00 25.02 ? 109 ASP   A OD2 1 
ATOM   822  N  N   . CYS   A 1 104 ? 13.466 8.830   23.081 1.00 20.38 ? 110 CYS   A N   1 
ATOM   823  C  CA  . CYS   A 1 104 ? 14.000 9.199   21.755 1.00 20.06 ? 110 CYS   A CA  1 
ATOM   824  C  C   . CYS   A 1 104 ? 15.345 8.503   21.513 1.00 18.80 ? 110 CYS   A C   1 
ATOM   825  O  O   . CYS   A 1 104 ? 16.158 8.379   22.441 1.00 18.87 ? 110 CYS   A O   1 
ATOM   826  C  CB  . CYS   A 1 104 ? 14.112 10.705  21.567 1.00 21.59 ? 110 CYS   A CB  1 
ATOM   827  S  SG  . CYS   A 1 104 ? 12.527 11.577  21.587 1.00 25.35 ? 110 CYS   A SG  1 
ATOM   828  N  N   . GLY   A 1 105 ? 15.549 8.041   20.295 1.00 17.66 ? 111 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 105 ? 16.778 7.306   19.988 1.00 17.32 ? 111 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 105 ? 16.590 5.799   19.953 1.00 18.90 ? 111 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 105 ? 17.441 5.083   19.406 1.00 19.23 ? 111 GLY   A O   1 
ATOM   832  N  N   . GLY   A 1 106 ? 15.475 5.297   20.513 1.00 19.07 ? 112 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 106 ? 15.194 3.872   20.456 1.00 19.65 ? 112 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 106 ? 15.006 3.413   19.011 1.00 18.59 ? 112 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 106 ? 14.390 4.125   18.222 1.00 18.49 ? 112 GLY   A O   1 
ATOM   836  N  N   . ILE   A 1 107 ? 15.596 2.250   18.620 1.00 18.92 ? 113 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 107 ? 15.471 1.785   17.244 1.00 18.06 ? 113 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 107 ? 14.120 1.119   16.912 1.00 18.96 ? 113 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 107 ? 13.611 0.324   17.695 1.00 19.02 ? 113 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 107 ? 16.680 0.832   16.901 1.00 17.70 ? 113 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 107 ? 17.936 1.672   16.665 1.00 17.58 ? 113 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 107 ? 16.373 -0.074  15.665 1.00 18.33 ? 113 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 107 ? 19.189 0.886   16.448 1.00 20.15 ? 113 ILE   A CD1 1 
ATOM   844  N  N   . LEU   A 1 108 ? 13.580 1.408   15.704 1.00 17.89 ? 114 LEU   A N   1 
ATOM   845  C  CA  . LEU   A 1 108 ? 12.427 0.702   15.156 1.00 17.37 ? 114 LEU   A CA  1 
ATOM   846  C  C   . LEU   A 1 108 ? 13.037 -0.179  14.021 1.00 17.86 ? 114 LEU   A C   1 
ATOM   847  O  O   . LEU   A 1 108 ? 13.795 0.347   13.182 1.00 17.75 ? 114 LEU   A O   1 
ATOM   848  C  CB  . LEU   A 1 108 ? 11.393 1.692   14.555 1.00 17.25 ? 114 LEU   A CB  1 
ATOM   849  C  CG  . LEU   A 1 108 ? 10.338 1.084   13.638 1.00 18.15 ? 114 LEU   A CG  1 
ATOM   850  C  CD1 . LEU   A 1 108 ? 9.287  0.336   14.433 1.00 17.32 ? 114 LEU   A CD1 1 
ATOM   851  C  CD2 . LEU   A 1 108 ? 9.633  2.155   12.790 1.00 19.48 ? 114 LEU   A CD2 1 
ATOM   852  N  N   . ARG   A 1 109 ? 12.688 -1.482  13.965 1.00 17.61 ? 115 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 109 ? 13.245 -2.356  12.938 1.00 18.03 ? 115 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 109 ? 12.190 -3.316  12.353 1.00 19.28 ? 115 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 109 ? 11.215 -3.627  13.023 1.00 18.83 ? 115 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 109 ? 14.446 -3.144  13.486 1.00 17.83 ? 115 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 109 ? 14.041 -4.188  14.510 1.00 18.55 ? 115 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 109 ? 15.225 -4.924  15.122 1.00 20.19 ? 115 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 109 ? 15.957 -4.065  16.049 1.00 23.09 ? 115 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 109 ? 17.254 -3.786  15.953 1.00 23.50 ? 115 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 109 ? 17.992 -4.342  14.996 1.00 21.72 ? 115 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 109 ? 17.839 -3.002  16.854 1.00 21.61 ? 115 ARG   A NH2 1 
ATOM   863  N  N   . CYS   A 1 110 ? 12.419 -3.787  11.123 1.00 19.95 ? 116 CYS   A N   1 
ATOM   864  C  CA  . CYS   A 1 110 ? 11.559 -4.757  10.431 1.00 21.46 ? 116 CYS   A CA  1 
ATOM   865  C  C   . CYS   A 1 110 ? 12.484 -5.955  10.003 1.00 24.29 ? 116 CYS   A C   1 
ATOM   866  O  O   . CYS   A 1 110 ? 13.661 -6.011  10.416 1.00 24.56 ? 116 CYS   A O   1 
ATOM   867  C  CB  . CYS   A 1 110 ? 10.941 -4.086  9.212  1.00 22.80 ? 116 CYS   A CB  1 
ATOM   868  S  SG  . CYS   A 1 110 ? 12.184 -3.575  7.995  1.00 25.78 ? 116 CYS   A SG  1 
ATOM   869  N  N   . GLN   A 1 111 ? 11.969 -6.896  9.166  1.00 25.05 ? 117 GLN   A N   1 
ATOM   870  C  CA  . GLN   A 1 111 ? 12.790 -8.016  8.684  1.00 27.13 ? 117 GLN   A CA  1 
ATOM   871  C  C   . GLN   A 1 111 ? 14.019 -7.569  7.834  1.00 28.47 ? 117 GLN   A C   1 
ATOM   872  O  O   . GLN   A 1 111 ? 14.988 -8.332  7.738  1.00 30.16 ? 117 GLN   A O   1 
ATOM   873  C  CB  . GLN   A 1 111 ? 11.930 -9.016  7.870  1.00 29.45 ? 117 GLN   A CB  1 
ATOM   874  C  CG  . GLN   A 1 111 ? 11.326 -8.399  6.615  1.00 34.87 ? 117 GLN   A CG  1 
ATOM   875  C  CD  . GLN   A 1 111 ? 10.534 -9.382  5.783  1.00 42.30 ? 117 GLN   A CD  1 
ATOM   876  O  OE1 . GLN   A 1 111 ? 9.296  -9.326  5.732  1.00 44.40 ? 117 GLN   A OE1 1 
ATOM   877  N  NE2 . GLN   A 1 111 ? 11.229 -10.291 5.097  1.00 42.86 ? 117 GLN   A NE2 1 
ATOM   878  N  N   . HIS   A 1 112 ? 13.971 -6.374  7.202  1.00 27.30 ? 118 HIS   A N   1 
ATOM   879  C  CA  . HIS   A 1 112 ? 15.070 -5.900  6.332  1.00 26.97 ? 118 HIS   A CA  1 
ATOM   880  C  C   . HIS   A 1 112 ? 16.185 -5.124  7.067  1.00 27.05 ? 118 HIS   A C   1 
ATOM   881  O  O   . HIS   A 1 112 ? 17.262 -4.914  6.491  1.00 27.98 ? 118 HIS   A O   1 
ATOM   882  C  CB  . HIS   A 1 112 ? 14.523 -5.066  5.149  1.00 27.90 ? 118 HIS   A CB  1 
ATOM   883  C  CG  . HIS   A 1 112 ? 13.415 -5.759  4.406  1.00 30.87 ? 118 HIS   A CG  1 
ATOM   884  N  ND1 . HIS   A 1 112 ? 12.094 -5.491  4.686  1.00 32.04 ? 118 HIS   A ND1 1 
ATOM   885  C  CD2 . HIS   A 1 112 ? 13.472 -6.721  3.449  1.00 32.23 ? 118 HIS   A CD2 1 
ATOM   886  C  CE1 . HIS   A 1 112 ? 11.380 -6.269  3.887  1.00 32.89 ? 118 HIS   A CE1 1 
ATOM   887  N  NE2 . HIS   A 1 112 ? 12.166 -7.036  3.124  1.00 32.96 ? 118 HIS   A NE2 1 
ATOM   888  N  N   . GLY   A 1 113 ? 15.932 -4.717  8.317  1.00 25.77 ? 119 GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 113 ? 16.915 -3.949  9.073  1.00 24.89 ? 119 GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 113 ? 16.324 -2.760  9.817  1.00 22.77 ? 119 GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 113 ? 15.149 -2.769  10.169 1.00 22.18 ? 119 GLY   A O   1 
ATOM   892  N  N   . VAL   A 1 114 ? 17.143 -1.740  10.097 1.00 21.17 ? 120 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 114 ? 16.700 -0.550  10.847 1.00 19.97 ? 120 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 114 ? 15.824 0.367   9.956  1.00 18.99 ? 120 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 114 ? 16.254 0.775   8.882  1.00 19.03 ? 120 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 114 ? 17.904 0.237   11.455 1.00 20.00 ? 120 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 114 ? 17.442 1.482   12.207 1.00 20.33 ? 120 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 114 ? 18.728 -0.664  12.369 1.00 20.66 ? 120 VAL   A CG2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 14.643 0.729   10.451 1.00 18.67 ? 121 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 13.656 1.589   9.783  1.00 19.70 ? 121 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.785 3.093   10.199 1.00 20.04 ? 121 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 13.586 4.009   9.385  1.00 20.90 ? 121 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 12.224 1.074   10.101 1.00 20.26 ? 121 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 11.146 2.056   9.624  1.00 21.14 ? 121 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 11.984 -0.319  9.512  1.00 20.15 ? 121 VAL   A CG2 1 
ATOM   906  N  N   . GLY   A 1 116 ? 14.019 3.309   11.489 1.00 18.63 ? 122 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 116 ? 14.132 4.644   12.051 1.00 18.59 ? 122 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 116 ? 14.429 4.661   13.538 1.00 18.54 ? 122 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 116 ? 14.854 3.643   14.096 1.00 18.40 ? 122 GLY   A O   1 
ATOM   910  N  N   . ILE   A 1 117 ? 14.182 5.826   14.205 1.00 17.54 ? 123 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 117 ? 14.456 5.984   15.634 1.00 16.00 ? 123 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 117 ? 13.322 6.805   16.246 1.00 16.85 ? 123 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 117 ? 12.800 7.723   15.592 1.00 17.87 ? 123 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 117 ? 15.831 6.662   15.951 1.00 16.59 ? 123 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 117 ? 16.003 7.966   15.164 1.00 16.67 ? 123 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 117 ? 17.041 5.722   15.786 1.00 16.85 ? 123 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 117 ? 17.231 8.819   15.666 1.00 18.17 ? 123 ILE   A CD1 1 
ATOM   918  N  N   . VAL   A 1 118 ? 12.960 6.498   17.513 1.00 16.18 ? 124 VAL   A N   1 
ATOM   919  C  CA  . VAL   A 1 118 ? 11.911 7.238   18.240 1.00 16.30 ? 124 VAL   A CA  1 
ATOM   920  C  C   . VAL   A 1 118 ? 12.248 8.732   18.209 1.00 17.69 ? 124 VAL   A C   1 
ATOM   921  O  O   . VAL   A 1 118 ? 13.411 9.087   18.455 1.00 17.03 ? 124 VAL   A O   1 
ATOM   922  C  CB  . VAL   A 1 118 ? 11.784 6.768   19.720 1.00 17.41 ? 124 VAL   A CB  1 
ATOM   923  C  CG1 . VAL   A 1 118 ? 10.786 7.657   20.467 1.00 18.32 ? 124 VAL   A CG1 1 
ATOM   924  C  CG2 . VAL   A 1 118 ? 11.335 5.299   19.799 1.00 17.08 ? 124 VAL   A CG2 1 
ATOM   925  N  N   . SER   A 1 119 ? 11.260 9.597   17.900 1.00 19.71 ? 125 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 119 ? 11.510 11.037  17.806 1.00 20.91 ? 125 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 119 ? 10.465 11.846  18.598 1.00 21.94 ? 125 SER   A C   1 
ATOM   928  O  O   . SER   A 1 119 ? 10.802 12.893  19.128 1.00 22.72 ? 125 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 119 ? 11.547 11.469  16.341 1.00 22.95 ? 125 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 119 ? 11.729 12.864  16.150 1.00 25.72 ? 125 SER   A OG  1 
ATOM   931  N  N   . THR   A 1 120 ? 9.210  11.321  18.709 1.00 21.61 ? 126 THR   A N   1 
ATOM   932  C  CA  . THR   A 1 120 ? 8.080  11.975  19.391 1.00 21.46 ? 126 THR   A CA  1 
ATOM   933  C  C   . THR   A 1 120 ? 7.257  10.936  20.230 1.00 23.77 ? 126 THR   A C   1 
ATOM   934  O  O   . THR   A 1 120 ? 7.422  9.714   20.080 1.00 24.30 ? 126 THR   A O   1 
ATOM   935  C  CB  . THR   A 1 120 ? 7.138  12.678  18.356 1.00 21.21 ? 126 THR   A CB  1 
ATOM   936  O  OG1 . THR   A 1 120 ? 6.324  11.708  17.682 1.00 21.65 ? 126 THR   A OG1 1 
ATOM   937  C  CG2 . THR   A 1 120 ? 7.857  13.558  17.370 1.00 20.04 ? 126 THR   A CG2 1 
ATOM   938  N  N   . GLY   A 1 121 ? 6.359  11.435  21.070 1.00 24.80 ? 127 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 121 ? 5.514  10.554  21.869 1.00 27.00 ? 127 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 121 ? 4.429  11.315  22.582 1.00 30.05 ? 127 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 121 ? 4.096  12.445  22.198 1.00 29.74 ? 127 GLY   A O   1 
ATOM   942  N  N   . GLY   A 1 122 ? 3.896  10.693  23.635 1.00 32.06 ? 128 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 122 ? 2.857  11.330  24.425 1.00 33.97 ? 128 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 122 ? 1.775  10.428  24.977 1.00 35.95 ? 128 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 122 ? 2.028  9.517   25.777 1.00 37.25 ? 128 GLY   A O   1 
ATOM   946  N  N   . ASN   A 1 123 ? 0.553  10.724  24.563 1.00 35.82 ? 129 ASN   A N   1 
ATOM   947  C  CA  . ASN   A 1 123 ? -0.689 10.130  25.029 1.00 35.98 ? 129 ASN   A CA  1 
ATOM   948  C  C   . ASN   A 1 123 ? -1.035 8.784   24.384 1.00 34.06 ? 129 ASN   A C   1 
ATOM   949  O  O   . ASN   A 1 123 ? -2.042 8.662   23.682 1.00 34.75 ? 129 ASN   A O   1 
ATOM   950  C  CB  . ASN   A 1 123 ? -1.817 11.151  24.845 1.00 39.40 ? 129 ASN   A CB  1 
ATOM   951  C  CG  . ASN   A 1 123 ? -1.568 12.234  23.785 1.00 45.55 ? 129 ASN   A CG  1 
ATOM   952  O  OD1 . ASN   A 1 123 ? -1.371 13.423  24.096 1.00 47.42 ? 129 ASN   A OD1 1 
ATOM   953  N  ND2 . ASN   A 1 123 ? -1.586 11.845  22.513 1.00 46.83 ? 129 ASN   A ND2 1 
ATOM   954  N  N   . GLY   A 1 124 ? -0.219 7.773   24.658 1.00 31.75 ? 130 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 124 ? -0.419 6.458   24.070 1.00 30.87 ? 130 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 124 ? 0.016  6.373   22.609 1.00 28.38 ? 130 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 124 ? -0.328 5.415   21.921 1.00 28.12 ? 130 GLY   A O   1 
ATOM   958  N  N   . LEU   A 1 125 ? 0.813  7.360   22.139 1.00 27.30 ? 131 LEU   A N   1 
ATOM   959  C  CA  . LEU   A 1 125 ? 1.362  7.430   20.782 1.00 26.94 ? 131 LEU   A CA  1 
ATOM   960  C  C   . LEU   A 1 125 ? 2.903  7.489   20.833 1.00 25.42 ? 131 LEU   A C   1 
ATOM   961  O  O   . LEU   A 1 125 ? 3.480  7.889   21.856 1.00 25.84 ? 131 LEU   A O   1 
ATOM   962  C  CB  . LEU   A 1 125 ? 0.809  8.669   20.031 1.00 27.16 ? 131 LEU   A CB  1 
ATOM   963  C  CG  . LEU   A 1 125 ? -0.667 8.623   19.691 1.00 29.36 ? 131 LEU   A CG  1 
ATOM   964  C  CD1 . LEU   A 1 125 ? -1.230 10.037  19.457 1.00 30.12 ? 131 LEU   A CD1 1 
ATOM   965  C  CD2 . LEU   A 1 125 ? -0.933 7.733   18.482 1.00 29.50 ? 131 LEU   A CD2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 3.561  7.030   19.758 1.00 22.87 ? 132 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 5.010  7.040   19.581 1.00 21.29 ? 132 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 5.324  7.366   18.094 1.00 20.25 ? 132 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 4.741  6.773   17.201 1.00 19.57 ? 132 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 5.682  5.705   20.037 1.00 20.95 ? 132 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 5.214  4.524   19.189 1.00 20.91 ? 132 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 7.197  5.817   20.006 1.00 20.72 ? 132 VAL   A CG2 1 
ATOM   973  N  N   . GLY   A 1 127 ? 6.222  8.317   17.867 1.00 20.48 ? 133 GLY   A N   1 
ATOM   974  C  CA  . GLY   A 1 127 ? 6.618  8.764   16.540 1.00 20.50 ? 133 GLY   A CA  1 
ATOM   975  C  C   . GLY   A 1 127 ? 8.047  8.356   16.211 1.00 20.77 ? 133 GLY   A C   1 
ATOM   976  O  O   . GLY   A 1 127 ? 8.920  8.390   17.086 1.00 20.48 ? 133 GLY   A O   1 
ATOM   977  N  N   . PHE   A 1 128 ? 8.291  7.987   14.941 1.00 20.08 ? 134 PHE   A N   1 
ATOM   978  C  CA  . PHE   A 1 128 ? 9.603  7.543   14.473 1.00 20.47 ? 134 PHE   A CA  1 
ATOM   979  C  C   . PHE   A 1 128 ? 10.130 8.389   13.307 1.00 20.62 ? 134 PHE   A C   1 
ATOM   980  O  O   . PHE   A 1 128 ? 9.402  8.612   12.332 1.00 20.99 ? 134 PHE   A O   1 
ATOM   981  C  CB  . PHE   A 1 128 ? 9.524  6.076   14.030 1.00 20.09 ? 134 PHE   A CB  1 
ATOM   982  C  CG  . PHE   A 1 128 ? 8.935  5.149   15.081 1.00 20.25 ? 134 PHE   A CG  1 
ATOM   983  C  CD1 . PHE   A 1 128 ? 9.680  4.768   16.197 1.00 21.05 ? 134 PHE   A CD1 1 
ATOM   984  C  CD2 . PHE   A 1 128 ? 7.659  4.627   14.932 1.00 20.67 ? 134 PHE   A CD2 1 
ATOM   985  C  CE1 . PHE   A 1 128 ? 9.139  3.905   17.153 1.00 21.33 ? 134 PHE   A CE1 1 
ATOM   986  C  CE2 . PHE   A 1 128 ? 7.131  3.752   15.879 1.00 21.13 ? 134 PHE   A CE2 1 
ATOM   987  C  CZ  . PHE   A 1 128 ? 7.868  3.410   16.991 1.00 21.03 ? 134 PHE   A CZ  1 
ATOM   988  N  N   . ALA   A 1 129 ? 11.388 8.847   13.381 1.00 20.62 ? 135 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 129 ? 11.992 9.565   12.244 1.00 21.03 ? 135 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 129 ? 12.488 8.488   11.250 1.00 20.10 ? 135 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 129 ? 13.344 7.676   11.605 1.00 19.40 ? 135 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 129 ? 13.148 10.445  12.706 1.00 21.10 ? 135 ALA   A CB  1 
ATOM   993  N  N   . ASP   A 1 130 ? 11.888 8.421   10.050 1.00 20.19 ? 136 ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 130 ? 12.283 7.446   9.018  1.00 20.28 ? 136 ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 130 ? 13.716 7.732   8.499  1.00 20.28 ? 136 ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 130 ? 14.110 8.893   8.435  1.00 21.40 ? 136 ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 130 ? 11.284 7.487   7.844  1.00 21.96 ? 136 ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 130 ? 11.578 6.472   6.740  1.00 28.95 ? 136 ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 130 ? 11.688 5.258   7.052  1.00 28.56 ? 136 ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 130 ? 11.739 6.889   5.574  1.00 32.38 ? 136 ASP   A OD2 1 
ATOM   1001 N  N   . VAL   A 1 131 ? 14.508 6.676   8.198  1.00 19.03 ? 137 VAL   A N   1 
ATOM   1002 C  CA  . VAL   A 1 131 ? 15.855 6.815   7.616  1.00 19.20 ? 137 VAL   A CA  1 
ATOM   1003 C  C   . VAL   A 1 131 ? 16.014 6.004   6.285  1.00 19.45 ? 137 VAL   A C   1 
ATOM   1004 O  O   . VAL   A 1 131 ? 17.068 6.080   5.641  1.00 20.50 ? 137 VAL   A O   1 
ATOM   1005 C  CB  . VAL   A 1 131 ? 17.008 6.481   8.613  1.00 19.75 ? 137 VAL   A CB  1 
ATOM   1006 C  CG1 . VAL   A 1 131 ? 16.978 7.402   9.845  1.00 19.52 ? 137 VAL   A CG1 1 
ATOM   1007 C  CG2 . VAL   A 1 131 ? 17.008 5.001   8.998  1.00 20.59 ? 137 VAL   A CG2 1 
ATOM   1008 N  N   . ARG   A 1 132 ? 14.982 5.222   5.879  1.00 18.91 ? 138 ARG   A N   1 
ATOM   1009 C  CA  . ARG   A 1 132 ? 15.051 4.341   4.694  1.00 18.55 ? 138 ARG   A CA  1 
ATOM   1010 C  C   . ARG   A 1 132 ? 15.281 5.064   3.334  1.00 20.56 ? 138 ARG   A C   1 
ATOM   1011 O  O   . ARG   A 1 132 ? 15.733 4.436   2.367  1.00 20.85 ? 138 ARG   A O   1 
ATOM   1012 C  CB  . ARG   A 1 132 ? 13.813 3.448   4.620  1.00 18.39 ? 138 ARG   A CB  1 
ATOM   1013 C  CG  . ARG   A 1 132 ? 13.645 2.544   5.841  1.00 17.62 ? 138 ARG   A CG  1 
ATOM   1014 C  CD  . ARG   A 1 132 ? 12.365 1.747   5.692  1.00 19.16 ? 138 ARG   A CD  1 
ATOM   1015 N  NE  . ARG   A 1 132 ? 11.193 2.614   5.936  1.00 20.07 ? 138 ARG   A NE  1 
ATOM   1016 C  CZ  . ARG   A 1 132 ? 9.942  2.168   6.013  1.00 20.76 ? 138 ARG   A CZ  1 
ATOM   1017 N  NH1 . ARG   A 1 132 ? 9.667  0.901   5.731  1.00 22.96 ? 138 ARG   A NH1 1 
ATOM   1018 N  NH2 . ARG   A 1 132 ? 8.941  3.014   6.261  1.00 20.44 ? 138 ARG   A NH2 1 
ATOM   1019 N  N   . ASP   A 1 133 ? 14.958 6.360   3.261  1.00 21.01 ? 139 ASP   A N   1 
ATOM   1020 C  CA  . ASP   A 1 133 ? 15.179 7.123   2.022  1.00 22.08 ? 139 ASP   A CA  1 
ATOM   1021 C  C   . ASP   A 1 133 ? 16.637 7.665   1.907  1.00 21.75 ? 139 ASP   A C   1 
ATOM   1022 O  O   . ASP   A 1 133 ? 17.019 8.193   0.859  1.00 22.02 ? 139 ASP   A O   1 
ATOM   1023 C  CB  . ASP   A 1 133 ? 14.160 8.276   1.922  1.00 24.71 ? 139 ASP   A CB  1 
ATOM   1024 C  CG  . ASP   A 1 133 ? 14.369 9.329   3.007  1.00 27.79 ? 139 ASP   A CG  1 
ATOM   1025 O  OD1 . ASP   A 1 133 ? 14.499 8.942   4.209  1.00 28.25 ? 139 ASP   A OD1 1 
ATOM   1026 O  OD2 . ASP   A 1 133 ? 14.427 10.526  2.666  1.00 28.63 ? 139 ASP   A OD2 1 
ATOM   1027 N  N   . LEU   A 1 134 ? 17.433 7.600   3.006  1.00 21.01 ? 140 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 134 ? 18.805 8.120   3.039  1.00 20.82 ? 140 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 134 ? 19.770 7.064   2.505  1.00 21.24 ? 140 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 134 ? 20.496 6.415   3.272  1.00 20.85 ? 140 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 134 ? 19.179 8.533   4.485  1.00 20.61 ? 140 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 134 ? 18.275 9.592   5.124  1.00 21.57 ? 140 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 134 ? 18.713 9.921   6.546  1.00 22.97 ? 140 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 134 ? 18.288 10.862  4.337  1.00 22.33 ? 140 LEU   A CD2 1 
ATOM   1035 N  N   . LEU   A 1 135 ? 19.747 6.869   1.178  1.00 22.72 ? 141 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 20.557 5.830   0.526  1.00 23.53 ? 141 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 22.068 5.974   0.733  1.00 23.59 ? 141 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 22.781 4.962   0.769  1.00 24.00 ? 141 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 20.220 5.732   -0.989 1.00 23.94 ? 141 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 18.709 5.684   -1.348 1.00 24.80 ? 141 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 18.512 5.573   -2.871 1.00 26.13 ? 141 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 17.932 4.604   -0.546 1.00 25.49 ? 141 LEU   A CD2 1 
ATOM   1043 N  N   . TRP   A 1 136 ? 22.561 7.217   0.906  1.00 23.49 ? 142 TRP   A N   1 
ATOM   1044 C  CA  . TRP   A 1 136 ? 23.984 7.453   1.102  1.00 23.42 ? 142 TRP   A CA  1 
ATOM   1045 C  C   . TRP   A 1 136 ? 24.538 6.860   2.414  1.00 23.43 ? 142 TRP   A C   1 
ATOM   1046 O  O   . TRP   A 1 136 ? 25.751 6.699   2.532  1.00 23.45 ? 142 TRP   A O   1 
ATOM   1047 C  CB  . TRP   A 1 136 ? 24.309 8.954   1.016  1.00 23.37 ? 142 TRP   A CB  1 
ATOM   1048 C  CG  . TRP   A 1 136 ? 23.492 9.788   1.949  1.00 22.41 ? 142 TRP   A CG  1 
ATOM   1049 C  CD1 . TRP   A 1 136 ? 22.349 10.469  1.652  1.00 23.00 ? 142 TRP   A CD1 1 
ATOM   1050 C  CD2 . TRP   A 1 136 ? 23.803 10.095  3.314  1.00 22.00 ? 142 TRP   A CD2 1 
ATOM   1051 N  NE1 . TRP   A 1 136 ? 21.917 11.168  2.754  1.00 22.82 ? 142 TRP   A NE1 1 
ATOM   1052 C  CE2 . TRP   A 1 136 ? 22.787 10.943  3.794  1.00 22.56 ? 142 TRP   A CE2 1 
ATOM   1053 C  CE3 . TRP   A 1 136 ? 24.847 9.736   4.179  1.00 22.35 ? 142 TRP   A CE3 1 
ATOM   1054 C  CZ2 . TRP   A 1 136 ? 22.796 11.451  5.093  1.00 22.48 ? 142 TRP   A CZ2 1 
ATOM   1055 C  CZ3 . TRP   A 1 136 ? 24.853 10.242  5.467  1.00 22.42 ? 142 TRP   A CZ3 1 
ATOM   1056 C  CH2 . TRP   A 1 136 ? 23.831 11.084  5.913  1.00 22.13 ? 142 TRP   A CH2 1 
ATOM   1057 N  N   . LEU   A 1 137 ? 23.660 6.484   3.368  1.00 23.15 ? 143 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 137 ? 24.113 5.840   4.609  1.00 24.30 ? 143 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 137 ? 24.841 4.500   4.328  1.00 26.33 ? 143 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 137 ? 25.603 4.053   5.181  1.00 25.77 ? 143 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 137 ? 22.925 5.566   5.535  1.00 23.38 ? 143 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 137 ? 22.296 6.787   6.220  1.00 23.21 ? 143 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 137 ? 21.072 6.367   7.026  1.00 23.70 ? 143 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 137 ? 23.324 7.480   7.160  1.00 23.47 ? 143 LEU   A CD2 1 
ATOM   1065 N  N   . ASP   A 1 138 ? 24.568 3.860   3.160  1.00 28.24 ? 144 ASP   A N   1 
ATOM   1066 C  CA  . ASP   A 1 138 ? 25.139 2.560   2.751  1.00 31.98 ? 144 ASP   A CA  1 
ATOM   1067 C  C   . ASP   A 1 138 ? 26.476 2.637   2.025  1.00 36.00 ? 144 ASP   A C   1 
ATOM   1068 O  O   . ASP   A 1 138 ? 26.947 1.601   1.557  1.00 35.83 ? 144 ASP   A O   1 
ATOM   1069 C  CB  . ASP   A 1 138 ? 24.175 1.835   1.788  1.00 34.17 ? 144 ASP   A CB  1 
ATOM   1070 C  CG  . ASP   A 1 138 ? 22.844 1.459   2.390  1.00 41.02 ? 144 ASP   A CG  1 
ATOM   1071 O  OD1 . ASP   A 1 138 ? 22.759 1.372   3.623  1.00 42.43 ? 144 ASP   A OD1 1 
ATOM   1072 O  OD2 . ASP   A 1 138 ? 21.882 1.257   1.623  1.00 44.29 ? 144 ASP   A OD2 1 
ATOM   1073 N  N   . GLU   A 1 139 ? 27.073 3.831   1.879  1.00 38.70 ? 145 GLU   A N   1 
ATOM   1074 C  CA  . GLU   A 1 139 ? 28.332 3.951   1.121  1.00 41.56 ? 145 GLU   A CA  1 
ATOM   1075 C  C   . GLU   A 1 139 ? 29.247 5.105   1.608  1.00 44.16 ? 145 GLU   A C   1 
ATOM   1076 O  O   . GLU   A 1 139 ? 28.869 5.847   2.517  1.00 43.91 ? 145 GLU   A O   1 
ATOM   1077 C  CB  . GLU   A 1 139 ? 27.995 4.123   -0.370 1.00 44.22 ? 145 GLU   A CB  1 
ATOM   1078 C  CG  . GLU   A 1 139 ? 27.267 5.425   -0.645 1.00 50.15 ? 145 GLU   A CG  1 
ATOM   1079 C  CD  . GLU   A 1 139 ? 26.122 5.318   -1.630 1.00 58.32 ? 145 GLU   A CD  1 
ATOM   1080 O  OE1 . GLU   A 1 139 ? 25.767 6.355   -2.237 1.00 60.41 ? 145 GLU   A OE1 1 
ATOM   1081 O  OE2 . GLU   A 1 139 ? 25.573 4.203   -1.788 1.00 60.92 ? 145 GLU   A OE2 1 
ATOM   1082 N  N   . GLU   A 1 140 ? 30.448 5.245   0.984  1.00 46.31 ? 146 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 140 ? 31.460 6.281   1.252  1.00 48.75 ? 146 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 140 ? 32.115 6.088   2.620  1.00 49.80 ? 146 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 140 ? 32.993 5.235   2.771  1.00 50.29 ? 146 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 140 ? 30.888 7.709   1.049  1.00 52.42 ? 146 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 140 ? 31.605 8.842   1.777  1.00 59.36 ? 146 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 140 ? 32.732 9.500   1.006  1.00 67.57 ? 146 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 140 ? 32.613 10.710  0.700  1.00 69.63 ? 146 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 140 ? 33.734 8.810   0.706  1.00 69.95 ? 146 GLU   A OE2 1 
ATOM   1091 N  N   . SER   B 1 1   ? 21.850 -21.414 7.839  1.00 26.25 ? 7   SER   C N   1 
ATOM   1092 C  CA  . SER   B 1 1   ? 20.669 -21.305 8.704  1.00 27.08 ? 7   SER   C CA  1 
ATOM   1093 C  C   . SER   B 1 1   ? 20.666 -22.416 9.779  1.00 26.52 ? 7   SER   C C   1 
ATOM   1094 O  O   . SER   B 1 1   ? 21.324 -23.456 9.603  1.00 26.92 ? 7   SER   C O   1 
ATOM   1095 C  CB  . SER   B 1 1   ? 19.390 -21.380 7.870  1.00 29.46 ? 7   SER   C CB  1 
ATOM   1096 O  OG  . SER   B 1 1   ? 19.207 -22.688 7.344  1.00 31.72 ? 7   SER   C OG  1 
ATOM   1097 N  N   . GLY   B 1 2   ? 19.965 -22.163 10.888 1.00 25.91 ? 8   GLY   C N   1 
ATOM   1098 C  CA  . GLY   B 1 2   ? 19.848 -23.115 11.990 1.00 24.96 ? 8   GLY   C CA  1 
ATOM   1099 C  C   . GLY   B 1 2   ? 19.513 -22.484 13.336 1.00 23.48 ? 8   GLY   C C   1 
ATOM   1100 O  O   . GLY   B 1 2   ? 19.906 -21.346 13.609 1.00 22.82 ? 8   GLY   C O   1 
ATOM   1101 N  N   . ALA   B 1 3   ? 18.810 -23.240 14.208 1.00 22.73 ? 9   ALA   C N   1 
ATOM   1102 C  CA  . ALA   B 1 3   ? 18.457 -22.784 15.560 1.00 22.53 ? 9   ALA   C CA  1 
ATOM   1103 C  C   . ALA   B 1 3   ? 18.590 -23.922 16.615 1.00 22.17 ? 9   ALA   C C   1 
ATOM   1104 O  O   . ALA   B 1 3   ? 18.745 -25.091 16.241 1.00 22.40 ? 9   ALA   C O   1 
ATOM   1105 C  CB  . ALA   B 1 3   ? 17.039 -22.211 15.574 1.00 22.82 ? 9   ALA   C CB  1 
ATOM   1106 N  N   . ILE   B 1 4   ? 18.575 -23.567 17.923 1.00 21.92 ? 10  ILE   C N   1 
ATOM   1107 C  CA  . ILE   B 1 4   ? 18.553 -24.505 19.050 1.00 22.77 ? 10  ILE   C CA  1 
ATOM   1108 C  C   . ILE   B 1 4   ? 17.157 -24.322 19.678 1.00 23.70 ? 10  ILE   C C   1 
ATOM   1109 O  O   . ILE   B 1 4   ? 16.696 -23.180 19.878 1.00 24.02 ? 10  ILE   C O   1 
ATOM   1110 C  CB  . ILE   B 1 4   ? 19.653 -24.226 20.100 1.00 23.02 ? 10  ILE   C CB  1 
ATOM   1111 C  CG1 . ILE   B 1 4   ? 21.057 -24.095 19.459 1.00 23.70 ? 10  ILE   C CG1 1 
ATOM   1112 C  CG2 . ILE   B 1 4   ? 19.608 -25.280 21.221 1.00 23.52 ? 10  ILE   C CG2 1 
ATOM   1113 C  CD1 . ILE   B 1 4   ? 22.164 -23.488 20.416 1.00 23.88 ? 10  ILE   C CD1 1 
ATOM   1114 N  N   . TYR   B 1 5   ? 16.453 -25.427 19.925 1.00 23.33 ? 11  TYR   C N   1 
ATOM   1115 C  CA  . TYR   B 1 5   ? 15.127 -25.373 20.520 1.00 23.90 ? 11  TYR   C CA  1 
ATOM   1116 C  C   . TYR   B 1 5   ? 15.178 -26.073 21.878 1.00 25.04 ? 11  TYR   C C   1 
ATOM   1117 O  O   . TYR   B 1 5   ? 15.203 -27.298 21.912 1.00 26.43 ? 11  TYR   C O   1 
ATOM   1118 C  CB  . TYR   B 1 5   ? 14.109 -26.052 19.577 1.00 23.49 ? 11  TYR   C CB  1 
ATOM   1119 C  CG  . TYR   B 1 5   ? 13.931 -25.282 18.286 1.00 23.85 ? 11  TYR   C CG  1 
ATOM   1120 C  CD1 . TYR   B 1 5   ? 13.159 -24.130 18.245 1.00 24.93 ? 11  TYR   C CD1 1 
ATOM   1121 C  CD2 . TYR   B 1 5   ? 14.584 -25.672 17.123 1.00 24.12 ? 11  TYR   C CD2 1 
ATOM   1122 C  CE1 . TYR   B 1 5   ? 13.034 -23.389 17.084 1.00 25.76 ? 11  TYR   C CE1 1 
ATOM   1123 C  CE2 . TYR   B 1 5   ? 14.455 -24.946 15.948 1.00 25.58 ? 11  TYR   C CE2 1 
ATOM   1124 C  CZ  . TYR   B 1 5   ? 13.669 -23.806 15.932 1.00 26.93 ? 11  TYR   C CZ  1 
ATOM   1125 O  OH  . TYR   B 1 5   ? 13.510 -23.062 14.788 1.00 28.96 ? 11  TYR   C OH  1 
ATOM   1126 N  N   . VAL   B 1 6   ? 15.278 -25.307 22.981 1.00 24.35 ? 12  VAL   C N   1 
ATOM   1127 C  CA  . VAL   B 1 6   ? 15.349 -25.822 24.350 1.00 24.96 ? 12  VAL   C CA  1 
ATOM   1128 C  C   . VAL   B 1 6   ? 14.214 -25.184 25.185 1.00 25.64 ? 12  VAL   C C   1 
ATOM   1129 O  O   . VAL   B 1 6   ? 14.017 -23.973 25.117 1.00 26.12 ? 12  VAL   C O   1 
ATOM   1130 C  CB  . VAL   B 1 6   ? 16.757 -25.629 24.979 1.00 25.98 ? 12  VAL   C CB  1 
ATOM   1131 C  CG1 . VAL   B 1 6   ? 17.244 -24.175 24.874 1.00 26.22 ? 12  VAL   C CG1 1 
ATOM   1132 C  CG2 . VAL   B 1 6   ? 16.803 -26.152 26.420 1.00 25.90 ? 12  VAL   C CG2 1 
ATOM   1133 N  N   . GLY   B 1 7   ? 13.387 -26.006 25.861 1.00 25.47 ? 13  GLY   C N   1 
ATOM   1134 C  CA  . GLY   B 1 7   ? 12.239 -25.504 26.623 1.00 24.89 ? 13  GLY   C CA  1 
ATOM   1135 C  C   . GLY   B 1 7   ? 11.320 -24.641 25.764 1.00 24.84 ? 13  GLY   C C   1 
ATOM   1136 O  O   . GLY   B 1 7   ? 11.039 -24.990 24.612 1.00 24.98 ? 13  GLY   C O   1 
ATOM   1137 N  N   . ASN   B 1 8   ? 10.919 -23.468 26.276 1.00 24.12 ? 14  ASN   C N   1 
ATOM   1138 C  CA  . ASN   B 1 8   ? 10.146 -22.521 25.463 1.00 24.14 ? 14  ASN   C CA  1 
ATOM   1139 C  C   . ASN   B 1 8   ? 11.058 -21.422 24.865 1.00 23.50 ? 14  ASN   C C   1 
ATOM   1140 O  O   . ASN   B 1 8   ? 10.621 -20.288 24.687 1.00 23.95 ? 14  ASN   C O   1 
ATOM   1141 C  CB  . ASN   B 1 8   ? 8.954  -21.954 26.210 1.00 26.81 ? 14  ASN   C CB  1 
ATOM   1142 C  CG  . ASN   B 1 8   ? 7.863  -22.992 26.371 1.00 32.19 ? 14  ASN   C CG  1 
ATOM   1143 O  OD1 . ASN   B 1 8   ? 6.964  -23.129 25.530 1.00 33.75 ? 14  ASN   C OD1 1 
ATOM   1144 N  ND2 . ASN   B 1 8   ? 7.943  -23.769 27.445 1.00 33.30 ? 14  ASN   C ND2 1 
ATOM   1145 N  N   . TYR   B 1 9   ? 12.297 -21.791 24.484 1.00 22.59 ? 15  TYR   C N   1 
ATOM   1146 C  CA  . TYR   B 1 9   ? 13.247 -20.848 23.866 1.00 23.55 ? 15  TYR   C CA  1 
ATOM   1147 C  C   . TYR   B 1 9   ? 13.709 -21.321 22.469 1.00 23.38 ? 15  TYR   C C   1 
ATOM   1148 O  O   . TYR   B 1 9   ? 13.852 -22.525 22.238 1.00 23.20 ? 15  TYR   C O   1 
ATOM   1149 C  CB  . TYR   B 1 9   ? 14.496 -20.657 24.748 1.00 24.15 ? 15  TYR   C CB  1 
ATOM   1150 C  CG  . TYR   B 1 9   ? 14.220 -20.129 26.143 1.00 26.36 ? 15  TYR   C CG  1 
ATOM   1151 C  CD1 . TYR   B 1 9   ? 13.678 -18.865 26.336 1.00 28.31 ? 15  TYR   C CD1 1 
ATOM   1152 C  CD2 . TYR   B 1 9   ? 14.580 -20.859 27.272 1.00 28.32 ? 15  TYR   C CD2 1 
ATOM   1153 C  CE1 . TYR   B 1 9   ? 13.448 -18.362 27.617 1.00 29.95 ? 15  TYR   C CE1 1 
ATOM   1154 C  CE2 . TYR   B 1 9   ? 14.333 -20.379 28.557 1.00 30.20 ? 15  TYR   C CE2 1 
ATOM   1155 C  CZ  . TYR   B 1 9   ? 13.776 -19.123 28.727 1.00 31.89 ? 15  TYR   C CZ  1 
ATOM   1156 O  OH  . TYR   B 1 9   ? 13.555 -18.643 30.002 1.00 35.27 ? 15  TYR   C OH  1 
ATOM   1157 N  N   . ARG   B 1 10  ? 14.036 -20.354 21.580 1.00 22.55 ? 16  ARG   C N   1 
ATOM   1158 C  CA  . ARG   B 1 10  ? 14.594 -20.565 20.239 1.00 22.20 ? 16  ARG   C CA  1 
ATOM   1159 C  C   . ARG   B 1 10  ? 15.881 -19.704 20.194 1.00 22.21 ? 16  ARG   C C   1 
ATOM   1160 O  O   . ARG   B 1 10  ? 15.812 -18.495 20.432 1.00 22.50 ? 16  ARG   C O   1 
ATOM   1161 C  CB  . ARG   B 1 10  ? 13.585 -20.141 19.135 1.00 24.14 ? 16  ARG   C CB  1 
ATOM   1162 C  CG  . ARG   B 1 10  ? 14.214 -19.846 17.749 1.00 25.70 ? 16  ARG   C CG  1 
ATOM   1163 C  CD  . ARG   B 1 10  ? 13.173 -19.571 16.655 1.00 27.03 ? 16  ARG   C CD  1 
ATOM   1164 N  NE  . ARG   B 1 10  ? 13.636 -18.631 15.625 1.00 27.71 ? 16  ARG   C NE  1 
ATOM   1165 C  CZ  . ARG   B 1 10  ? 14.086 -18.975 14.420 1.00 29.02 ? 16  ARG   C CZ  1 
ATOM   1166 N  NH1 . ARG   B 1 10  ? 14.249 -20.257 14.104 1.00 27.51 ? 16  ARG   C NH1 1 
ATOM   1167 N  NH2 . ARG   B 1 10  ? 14.469 -18.040 13.555 1.00 28.66 ? 16  ARG   C NH2 1 
ATOM   1168 N  N   . VAL   B 1 11  ? 17.062 -20.338 19.975 1.00 21.47 ? 17  VAL   C N   1 
ATOM   1169 C  CA  . VAL   B 1 11  ? 18.354 -19.647 19.952 1.00 21.45 ? 17  VAL   C CA  1 
ATOM   1170 C  C   . VAL   B 1 11  ? 18.863 -19.579 18.511 1.00 21.84 ? 17  VAL   C C   1 
ATOM   1171 O  O   . VAL   B 1 11  ? 19.087 -20.613 17.868 1.00 21.08 ? 17  VAL   C O   1 
ATOM   1172 C  CB  . VAL   B 1 11  ? 19.404 -20.322 20.869 1.00 22.31 ? 17  VAL   C CB  1 
ATOM   1173 C  CG1 . VAL   B 1 11  ? 20.658 -19.465 20.972 1.00 22.96 ? 17  VAL   C CG1 1 
ATOM   1174 C  CG2 . VAL   B 1 11  ? 18.819 -20.652 22.240 1.00 22.70 ? 17  VAL   C CG2 1 
ATOM   1175 N  N   . VAL   B 1 12  ? 19.027 -18.351 18.002 1.00 21.71 ? 18  VAL   C N   1 
ATOM   1176 C  CA  A VAL   B 1 12  ? 19.460 -18.103 16.629 0.50 21.50 ? 18  VAL   C CA  1 
ATOM   1177 C  CA  B VAL   B 1 12  ? 19.440 -18.115 16.625 0.50 21.89 ? 18  VAL   C CA  1 
ATOM   1178 C  C   . VAL   B 1 12  ? 20.599 -17.095 16.581 1.00 21.44 ? 18  VAL   C C   1 
ATOM   1179 O  O   . VAL   B 1 12  ? 20.804 -16.341 17.549 1.00 21.17 ? 18  VAL   C O   1 
ATOM   1180 C  CB  A VAL   B 1 12  ? 18.289 -17.563 15.759 0.50 22.23 ? 18  VAL   C CB  1 
ATOM   1181 C  CB  B VAL   B 1 12  ? 18.186 -17.591 15.854 0.50 23.34 ? 18  VAL   C CB  1 
ATOM   1182 C  CG1 A VAL   B 1 12  ? 17.352 -18.676 15.347 0.50 23.07 ? 18  VAL   C CG1 1 
ATOM   1183 C  CG1 B VAL   B 1 12  ? 18.493 -17.207 14.417 0.50 23.92 ? 18  VAL   C CG1 1 
ATOM   1184 C  CG2 A VAL   B 1 12  ? 17.546 -16.415 16.453 0.50 21.82 ? 18  VAL   C CG2 1 
ATOM   1185 C  CG2 B VAL   B 1 12  ? 17.063 -18.609 15.889 0.50 24.11 ? 18  VAL   C CG2 1 
ATOM   1186 N  N   . ASN   B 1 13  ? 21.353 -17.061 15.443 1.00 20.03 ? 19  ASN   C N   1 
ATOM   1187 C  CA  . ASN   B 1 13  ? 22.391 -16.058 15.185 1.00 18.87 ? 19  ASN   C CA  1 
ATOM   1188 C  C   . ASN   B 1 13  ? 21.610 -14.685 15.132 1.00 18.68 ? 19  ASN   C C   1 
ATOM   1189 O  O   . ASN   B 1 13  ? 20.620 -14.599 14.419 1.00 18.60 ? 19  ASN   C O   1 
ATOM   1190 C  CB  . ASN   B 1 13  ? 22.984 -16.273 13.809 1.00 20.22 ? 19  ASN   C CB  1 
ATOM   1191 C  CG  . ASN   B 1 13  ? 23.868 -17.506 13.693 1.00 20.94 ? 19  ASN   C CG  1 
ATOM   1192 O  OD1 . ASN   B 1 13  ? 23.463 -18.549 13.134 1.00 21.70 ? 19  ASN   C OD1 1 
ATOM   1193 N  ND2 . ASN   B 1 13  ? 25.095 -17.384 14.155 1.00 17.26 ? 19  ASN   C ND2 1 
ATOM   1194 N  N   . ARG   B 1 14  ? 22.049 -13.641 15.858 1.00 18.96 ? 20  ARG   C N   1 
ATOM   1195 C  CA  . ARG   B 1 14  ? 21.329 -12.346 15.850 1.00 18.69 ? 20  ARG   C CA  1 
ATOM   1196 C  C   . ARG   B 1 14  ? 21.190 -11.802 14.401 1.00 20.17 ? 20  ARG   C C   1 
ATOM   1197 O  O   . ARG   B 1 14  ? 20.146 -11.251 14.071 1.00 21.75 ? 20  ARG   C O   1 
ATOM   1198 C  CB  . ARG   B 1 14  ? 22.062 -11.323 16.725 1.00 19.67 ? 20  ARG   C CB  1 
ATOM   1199 C  CG  . ARG   B 1 14  ? 21.240 -10.046 17.063 1.00 21.27 ? 20  ARG   C CG  1 
ATOM   1200 C  CD  . ARG   B 1 14  ? 22.168 -9.052  17.737 1.00 21.47 ? 20  ARG   C CD  1 
ATOM   1201 N  NE  . ARG   B 1 14  ? 21.520 -7.819  18.187 1.00 24.12 ? 20  ARG   C NE  1 
ATOM   1202 C  CZ  . ARG   B 1 14  ? 21.407 -6.714  17.444 1.00 25.70 ? 20  ARG   C CZ  1 
ATOM   1203 N  NH1 . ARG   B 1 14  ? 21.849 -6.701  16.187 1.00 23.95 ? 20  ARG   C NH1 1 
ATOM   1204 N  NH2 . ARG   B 1 14  ? 20.847 -5.613  17.953 1.00 23.52 ? 20  ARG   C NH2 1 
ATOM   1205 N  N   . HIS   B 1 15  ? 22.209 -11.996 13.523 1.00 20.32 ? 21  HIS   C N   1 
ATOM   1206 C  CA  . HIS   B 1 15  ? 22.137 -11.457 12.144 1.00 21.71 ? 21  HIS   C CA  1 
ATOM   1207 C  C   . HIS   B 1 15  ? 21.110 -12.163 11.216 1.00 23.25 ? 21  HIS   C C   1 
ATOM   1208 O  O   . HIS   B 1 15  ? 20.824 -11.661 10.115 1.00 24.34 ? 21  HIS   C O   1 
ATOM   1209 C  CB  . HIS   B 1 15  ? 23.517 -11.414 11.480 1.00 22.36 ? 21  HIS   C CB  1 
ATOM   1210 C  CG  . HIS   B 1 15  ? 24.039 -12.742 11.034 1.00 23.16 ? 21  HIS   C CG  1 
ATOM   1211 N  ND1 . HIS   B 1 15  ? 24.860 -13.508 11.854 1.00 24.19 ? 21  HIS   C ND1 1 
ATOM   1212 C  CD2 . HIS   B 1 15  ? 23.930 -13.355 9.830  1.00 23.79 ? 21  HIS   C CD2 1 
ATOM   1213 C  CE1 . HIS   B 1 15  ? 25.191 -14.575 11.139 1.00 24.70 ? 21  HIS   C CE1 1 
ATOM   1214 N  NE2 . HIS   B 1 15  ? 24.667 -14.519 9.909  1.00 24.87 ? 21  HIS   C NE2 1 
ATOM   1215 N  N   . LEU   B 1 16  ? 20.559 -13.297 11.668 1.00 23.18 ? 22  LEU   C N   1 
ATOM   1216 C  CA  . LEU   B 1 16  ? 19.542 -14.069 10.941 1.00 23.55 ? 22  LEU   C CA  1 
ATOM   1217 C  C   . LEU   B 1 16  ? 18.158 -14.046 11.630 1.00 24.42 ? 22  LEU   C C   1 
ATOM   1218 O  O   . LEU   B 1 16  ? 17.227 -14.680 11.133 1.00 24.68 ? 22  LEU   C O   1 
ATOM   1219 C  CB  . LEU   B 1 16  ? 20.008 -15.519 10.688 1.00 23.72 ? 22  LEU   C CB  1 
ATOM   1220 C  CG  . LEU   B 1 16  ? 21.285 -15.661 9.873  1.00 24.81 ? 22  LEU   C CG  1 
ATOM   1221 C  CD1 . LEU   B 1 16  ? 21.741 -17.123 9.800  1.00 25.34 ? 22  LEU   C CD1 1 
ATOM   1222 C  CD2 . LEU   B 1 16  ? 21.114 -15.064 8.484  1.00 25.82 ? 22  LEU   C CD2 1 
ATOM   1223 N  N   . ALA   B 1 17  ? 18.016 -13.302 12.751 1.00 24.81 ? 23  ALA   C N   1 
ATOM   1224 C  CA  . ALA   B 1 17  ? 16.753 -13.203 13.485 1.00 26.02 ? 23  ALA   C CA  1 
ATOM   1225 C  C   . ALA   B 1 17  ? 15.650 -12.645 12.576 1.00 26.71 ? 23  ALA   C C   1 
ATOM   1226 O  O   . ALA   B 1 17  ? 15.919 -11.769 11.760 1.00 26.56 ? 23  ALA   C O   1 
ATOM   1227 C  CB  . ALA   B 1 17  ? 16.922 -12.313 14.712 1.00 26.16 ? 23  ALA   C CB  1 
ATOM   1228 N  N   . THR   B 1 18  ? 14.439 -13.213 12.670 1.00 26.69 ? 24  THR   C N   1 
ATOM   1229 C  CA  . THR   B 1 18  ? 13.286 -12.790 11.867 1.00 26.95 ? 24  THR   C CA  1 
ATOM   1230 C  C   . THR   B 1 18  ? 12.477 -11.705 12.631 1.00 27.68 ? 24  THR   C C   1 
ATOM   1231 O  O   . THR   B 1 18  ? 12.755 -11.438 13.810 1.00 27.22 ? 24  THR   C O   1 
ATOM   1232 C  CB  . THR   B 1 18  ? 12.374 -14.039 11.604 1.00 27.54 ? 24  THR   C CB  1 
ATOM   1233 O  OG1 . THR   B 1 18  ? 11.829 -14.492 12.843 1.00 28.38 ? 24  THR   C OG1 1 
ATOM   1234 C  CG2 . THR   B 1 18  ? 13.096 -15.175 10.891 1.00 27.39 ? 24  THR   C CG2 1 
ATOM   1235 N  N   . HIS   B 1 19  ? 11.423 -11.121 11.990 1.00 27.57 ? 25  HIS   C N   1 
ATOM   1236 C  CA  . HIS   B 1 19  ? 10.531 -10.170 12.655 1.00 28.43 ? 25  HIS   C CA  1 
ATOM   1237 C  C   . HIS   B 1 19  ? 9.855  -10.882 13.831 1.00 28.74 ? 25  HIS   C C   1 
ATOM   1238 O  O   . HIS   B 1 19  ? 9.859  -10.340 14.928 1.00 29.85 ? 25  HIS   C O   1 
ATOM   1239 C  CB  . HIS   B 1 19  ? 9.465  -9.613  11.681 1.00 29.98 ? 25  HIS   C CB  1 
ATOM   1240 C  CG  . HIS   B 1 19  ? 8.352  -8.866  12.371 1.00 33.28 ? 25  HIS   C CG  1 
ATOM   1241 N  ND1 . HIS   B 1 19  ? 8.522  -7.577  12.824 1.00 35.45 ? 25  HIS   C ND1 1 
ATOM   1242 C  CD2 . HIS   B 1 19  ? 7.107  -9.283  12.711 1.00 35.19 ? 25  HIS   C CD2 1 
ATOM   1243 C  CE1 . HIS   B 1 19  ? 7.372  -7.227  13.379 1.00 35.99 ? 25  HIS   C CE1 1 
ATOM   1244 N  NE2 . HIS   B 1 19  ? 6.489  -8.222  13.337 1.00 36.17 ? 25  HIS   C NE2 1 
ATOM   1245 N  N   . ASN   B 1 20  ? 9.351  -12.120 13.627 1.00 27.99 ? 26  ASN   C N   1 
ATOM   1246 C  CA  . ASN   B 1 20  ? 8.732  -12.878 14.713 1.00 28.46 ? 26  ASN   C CA  1 
ATOM   1247 C  C   . ASN   B 1 20  ? 9.666  -13.029 15.949 1.00 27.90 ? 26  ASN   C C   1 
ATOM   1248 O  O   . ASN   B 1 20  ? 9.203  -12.863 17.078 1.00 27.98 ? 26  ASN   C O   1 
ATOM   1249 C  CB  . ASN   B 1 20  ? 8.218  -14.232 14.219 1.00 30.92 ? 26  ASN   C CB  1 
ATOM   1250 C  CG  . ASN   B 1 20  ? 7.454  -14.970 15.292 1.00 36.81 ? 26  ASN   C CG  1 
ATOM   1251 O  OD1 . ASN   B 1 20  ? 6.347  -14.571 15.681 1.00 39.45 ? 26  ASN   C OD1 1 
ATOM   1252 N  ND2 . ASN   B 1 20  ? 8.041  -16.037 15.832 1.00 38.32 ? 26  ASN   C ND2 1 
ATOM   1253 N  N   . ASP   B 1 21  ? 10.967 -13.316 15.730 1.00 26.92 ? 27  ASP   C N   1 
ATOM   1254 C  CA  . ASP   B 1 21  ? 11.961 -13.404 16.809 1.00 26.38 ? 27  ASP   C CA  1 
ATOM   1255 C  C   . ASP   B 1 21  ? 12.040 -12.069 17.587 1.00 26.41 ? 27  ASP   C C   1 
ATOM   1256 O  O   . ASP   B 1 21  ? 12.004 -12.083 18.821 1.00 26.36 ? 27  ASP   C O   1 
ATOM   1257 C  CB  . ASP   B 1 21  ? 13.360 -13.733 16.253 1.00 25.06 ? 27  ASP   C CB  1 
ATOM   1258 C  CG  . ASP   B 1 21  ? 13.526 -15.148 15.741 1.00 24.66 ? 27  ASP   C CG  1 
ATOM   1259 O  OD1 . ASP   B 1 21  ? 12.855 -16.051 16.277 1.00 23.86 ? 27  ASP   C OD1 1 
ATOM   1260 O  OD2 . ASP   B 1 21  ? 14.299 -15.339 14.771 1.00 23.13 ? 27  ASP   C OD2 1 
ATOM   1261 N  N   . TRP   B 1 22  ? 12.156 -10.927 16.873 1.00 26.17 ? 28  TRP   C N   1 
ATOM   1262 C  CA  . TRP   B 1 22  ? 12.201 -9.612  17.526 1.00 26.34 ? 28  TRP   C CA  1 
ATOM   1263 C  C   . TRP   B 1 22  ? 10.868 -9.282  18.258 1.00 26.83 ? 28  TRP   C C   1 
ATOM   1264 O  O   . TRP   B 1 22  ? 10.891 -8.662  19.325 1.00 26.81 ? 28  TRP   C O   1 
ATOM   1265 C  CB  . TRP   B 1 22  ? 12.593 -8.491  16.538 1.00 25.77 ? 28  TRP   C CB  1 
ATOM   1266 C  CG  . TRP   B 1 22  ? 14.054 -8.437  16.207 1.00 25.76 ? 28  TRP   C CG  1 
ATOM   1267 C  CD1 . TRP   B 1 22  ? 14.657 -8.932  15.085 1.00 26.24 ? 28  TRP   C CD1 1 
ATOM   1268 C  CD2 . TRP   B 1 22  ? 15.111 -7.894  17.021 1.00 25.63 ? 28  TRP   C CD2 1 
ATOM   1269 N  NE1 . TRP   B 1 22  ? 16.011 -8.702  15.135 1.00 26.50 ? 28  TRP   C NE1 1 
ATOM   1270 C  CE2 . TRP   B 1 22  ? 16.321 -8.088  16.320 1.00 26.24 ? 28  TRP   C CE2 1 
ATOM   1271 C  CE3 . TRP   B 1 22  ? 15.154 -7.272  18.274 1.00 25.90 ? 28  TRP   C CE3 1 
ATOM   1272 C  CZ2 . TRP   B 1 22  ? 17.545 -7.631  16.801 1.00 26.81 ? 28  TRP   C CZ2 1 
ATOM   1273 C  CZ3 . TRP   B 1 22  ? 16.377 -6.846  18.761 1.00 26.55 ? 28  TRP   C CZ3 1 
ATOM   1274 C  CH2 . TRP   B 1 22  ? 17.554 -7.022  18.021 1.00 26.87 ? 28  TRP   C CH2 1 
ATOM   1275 N  N   . ALA   B 1 23  ? 9.725  -9.741  17.706 1.00 27.04 ? 29  ALA   C N   1 
ATOM   1276 C  CA  . ALA   B 1 23  ? 8.387  -9.519  18.292 1.00 28.37 ? 29  ALA   C CA  1 
ATOM   1277 C  C   . ALA   B 1 23  ? 8.142  -10.405 19.548 1.00 29.57 ? 29  ALA   C C   1 
ATOM   1278 O  O   . ALA   B 1 23  ? 7.182  -10.173 20.293 1.00 30.59 ? 29  ALA   C O   1 
ATOM   1279 C  CB  . ALA   B 1 23  ? 7.306  -9.771  17.244 1.00 28.53 ? 29  ALA   C CB  1 
ATOM   1280 N  N   . ASN   B 1 24  ? 9.009  -11.428 19.775 1.00 28.43 ? 30  ASN   C N   1 
ATOM   1281 C  CA  . ASN   B 1 24  ? 8.904  -12.321 20.924 1.00 28.72 ? 30  ASN   C CA  1 
ATOM   1282 C  C   . ASN   B 1 24  ? 10.280 -12.435 21.615 1.00 28.82 ? 30  ASN   C C   1 
ATOM   1283 O  O   . ASN   B 1 24  ? 10.671 -13.517 22.062 1.00 29.64 ? 30  ASN   C O   1 
ATOM   1284 C  CB  . ASN   B 1 24  ? 8.382  -13.694 20.464 1.00 30.08 ? 30  ASN   C CB  1 
ATOM   1285 C  CG  . ASN   B 1 24  ? 6.980  -13.672 19.915 1.00 32.63 ? 30  ASN   C CG  1 
ATOM   1286 O  OD1 . ASN   B 1 24  ? 5.987  -13.732 20.664 1.00 35.00 ? 30  ASN   C OD1 1 
ATOM   1287 N  ND2 . ASN   B 1 24  ? 6.861  -13.575 18.605 1.00 32.24 ? 30  ASN   C ND2 1 
ATOM   1288 N  N   . LEU   B 1 25  ? 11.026 -11.306 21.674 1.00 27.64 ? 31  LEU   C N   1 
ATOM   1289 C  CA  . LEU   B 1 25  ? 12.375 -11.226 22.214 1.00 26.78 ? 31  LEU   C CA  1 
ATOM   1290 C  C   . LEU   B 1 25  ? 12.516 -11.578 23.692 1.00 26.29 ? 31  LEU   C C   1 
ATOM   1291 O  O   . LEU   B 1 25  ? 11.770 -11.072 24.524 1.00 26.78 ? 31  LEU   C O   1 
ATOM   1292 C  CB  . LEU   B 1 25  ? 12.970 -9.816  21.954 1.00 26.27 ? 31  LEU   C CB  1 
ATOM   1293 C  CG  . LEU   B 1 25  ? 14.431 -9.662  22.334 1.00 26.57 ? 31  LEU   C CG  1 
ATOM   1294 C  CD1 . LEU   B 1 25  ? 15.326 -10.583 21.472 1.00 27.25 ? 31  LEU   C CD1 1 
ATOM   1295 C  CD2 . LEU   B 1 25  ? 14.889 -8.208  22.258 1.00 26.81 ? 31  LEU   C CD2 1 
ATOM   1296 N  N   . VAL   B 1 26  ? 13.509 -12.406 24.021 1.00 25.27 ? 32  VAL   C N   1 
ATOM   1297 C  CA  . VAL   B 1 26  ? 13.820 -12.741 25.406 1.00 25.00 ? 32  VAL   C CA  1 
ATOM   1298 C  C   . VAL   B 1 26  ? 15.142 -12.010 25.768 1.00 25.68 ? 32  VAL   C C   1 
ATOM   1299 O  O   . VAL   B 1 26  ? 15.219 -11.321 26.779 1.00 26.38 ? 32  VAL   C O   1 
ATOM   1300 C  CB  . VAL   B 1 26  ? 13.951 -14.278 25.619 1.00 25.56 ? 32  VAL   C CB  1 
ATOM   1301 C  CG1 . VAL   B 1 26  ? 14.621 -14.603 26.958 1.00 25.85 ? 32  VAL   C CG1 1 
ATOM   1302 C  CG2 . VAL   B 1 26  ? 12.596 -14.972 25.518 1.00 25.32 ? 32  VAL   C CG2 1 
ATOM   1303 N  N   . TRP   B 1 27  ? 16.183 -12.176 24.923 1.00 25.50 ? 33  TRP   C N   1 
ATOM   1304 C  CA  . TRP   B 1 27  ? 17.517 -11.628 25.146 1.00 25.28 ? 33  TRP   C CA  1 
ATOM   1305 C  C   . TRP   B 1 27  ? 18.297 -11.573 23.815 1.00 24.53 ? 33  TRP   C C   1 
ATOM   1306 O  O   . TRP   B 1 27  ? 18.115 -12.431 22.967 1.00 23.87 ? 33  TRP   C O   1 
ATOM   1307 C  CB  . TRP   B 1 27  ? 18.260 -12.556 26.144 1.00 25.48 ? 33  TRP   C CB  1 
ATOM   1308 C  CG  . TRP   B 1 27  ? 19.716 -12.274 26.348 1.00 25.98 ? 33  TRP   C CG  1 
ATOM   1309 C  CD1 . TRP   B 1 27  ? 20.265 -11.342 27.180 1.00 26.99 ? 33  TRP   C CD1 1 
ATOM   1310 C  CD2 . TRP   B 1 27  ? 20.817 -12.988 25.761 1.00 25.65 ? 33  TRP   C CD2 1 
ATOM   1311 N  NE1 . TRP   B 1 27  ? 21.641 -11.385 27.097 1.00 27.37 ? 33  TRP   C NE1 1 
ATOM   1312 C  CE2 . TRP   B 1 27  ? 22.005 -12.374 26.218 1.00 26.39 ? 33  TRP   C CE2 1 
ATOM   1313 C  CE3 . TRP   B 1 27  ? 20.913 -14.029 24.829 1.00 25.96 ? 33  TRP   C CE3 1 
ATOM   1314 C  CZ2 . TRP   B 1 27  ? 23.267 -12.818 25.834 1.00 26.74 ? 33  TRP   C CZ2 1 
ATOM   1315 C  CZ3 . TRP   B 1 27  ? 22.168 -14.471 24.454 1.00 26.98 ? 33  TRP   C CZ3 1 
ATOM   1316 C  CH2 . TRP   B 1 27  ? 23.323 -13.859 24.947 1.00 27.07 ? 33  TRP   C CH2 1 
ATOM   1317 N  N   . GLU   B 1 28  ? 19.151 -10.552 23.636 1.00 23.62 ? 34  GLU   C N   1 
ATOM   1318 C  CA  . GLU   B 1 28  ? 19.976 -10.439 22.449 1.00 23.72 ? 34  GLU   C CA  1 
ATOM   1319 C  C   . GLU   B 1 28  ? 21.295 -9.778  22.796 1.00 23.96 ? 34  GLU   C C   1 
ATOM   1320 O  O   . GLU   B 1 28  ? 21.344 -8.923  23.690 1.00 23.62 ? 34  GLU   C O   1 
ATOM   1321 C  CB  . GLU   B 1 28  ? 19.265 -9.701  21.300 1.00 24.98 ? 34  GLU   C CB  1 
ATOM   1322 C  CG  . GLU   B 1 28  ? 18.730 -8.308  21.630 1.00 27.64 ? 34  GLU   C CG  1 
ATOM   1323 C  CD  . GLU   B 1 28  ? 19.711 -7.151  21.519 1.00 29.95 ? 34  GLU   C CD  1 
ATOM   1324 O  OE1 . GLU   B 1 28  ? 19.469 -6.117  22.179 1.00 29.98 ? 34  GLU   C OE1 1 
ATOM   1325 O  OE2 . GLU   B 1 28  ? 20.740 -7.288  20.811 1.00 27.08 ? 34  GLU   C OE2 1 
ATOM   1326 N  N   . ASP   B 1 29  ? 22.367 -10.177 22.095 1.00 23.28 ? 35  ASP   C N   1 
ATOM   1327 C  CA  . ASP   B 1 29  ? 23.668 -9.577  22.298 1.00 23.60 ? 35  ASP   C CA  1 
ATOM   1328 C  C   . ASP   B 1 29  ? 24.435 -9.527  20.971 1.00 23.52 ? 35  ASP   C C   1 
ATOM   1329 O  O   . ASP   B 1 29  ? 24.916 -10.563 20.494 1.00 23.47 ? 35  ASP   C O   1 
ATOM   1330 C  CB  . ASP   B 1 29  ? 24.440 -10.356 23.370 1.00 25.09 ? 35  ASP   C CB  1 
ATOM   1331 C  CG  . ASP   B 1 29  ? 25.704 -9.668  23.851 1.00 29.47 ? 35  ASP   C CG  1 
ATOM   1332 O  OD1 . ASP   B 1 29  ? 26.334 -8.963  23.049 1.00 31.12 ? 35  ASP   C OD1 1 
ATOM   1333 O  OD2 . ASP   B 1 29  ? 26.084 -9.874  25.021 1.00 30.47 ? 35  ASP   C OD2 1 
ATOM   1334 N  N   . SER   B 1 30  ? 24.581 -8.309  20.388 1.00 22.44 ? 36  SER   C N   1 
ATOM   1335 C  CA  A SER   B 1 30  ? 25.305 -8.110  19.125 0.50 22.36 ? 36  SER   C CA  1 
ATOM   1336 C  CA  B SER   B 1 30  ? 25.296 -8.161  19.116 0.50 22.45 ? 36  SER   C CA  1 
ATOM   1337 C  C   . SER   B 1 30  ? 26.767 -8.577  19.209 1.00 22.37 ? 36  SER   C C   1 
ATOM   1338 O  O   . SER   B 1 30  ? 27.263 -9.210  18.272 1.00 23.21 ? 36  SER   C O   1 
ATOM   1339 C  CB  A SER   B 1 30  ? 25.237 -6.644  18.694 0.50 22.84 ? 36  SER   C CB  1 
ATOM   1340 C  CB  B SER   B 1 30  ? 25.150 -6.748  18.553 0.50 23.18 ? 36  SER   C CB  1 
ATOM   1341 O  OG  A SER   B 1 30  ? 26.008 -6.408  17.526 0.50 23.27 ? 36  SER   C OG  1 
ATOM   1342 O  OG  B SER   B 1 30  ? 25.556 -5.775  19.500 0.50 23.81 ? 36  SER   C OG  1 
ATOM   1343 N  N   . SER   B 1 31  ? 27.465 -8.286  20.350 1.00 22.14 ? 37  SER   C N   1 
ATOM   1344 C  CA  . SER   B 1 31  ? 28.866 -8.706  20.496 1.00 22.96 ? 37  SER   C CA  1 
ATOM   1345 C  C   . SER   B 1 31  ? 29.069 -10.242 20.409 1.00 21.95 ? 37  SER   C C   1 
ATOM   1346 O  O   . SER   B 1 31  ? 30.147 -10.690 20.024 1.00 22.31 ? 37  SER   C O   1 
ATOM   1347 C  CB  . SER   B 1 31  ? 29.479 -8.155  21.780 1.00 26.28 ? 37  SER   C CB  1 
ATOM   1348 O  OG  . SER   B 1 31  ? 29.060 -8.843  22.949 1.00 28.84 ? 37  SER   C OG  1 
ATOM   1349 N  N   . ARG   B 1 32  ? 28.046 -11.043 20.770 1.00 21.60 ? 38  ARG   C N   1 
ATOM   1350 C  CA  . ARG   B 1 32  ? 28.081 -12.518 20.724 1.00 22.60 ? 38  ARG   C CA  1 
ATOM   1351 C  C   . ARG   B 1 32  ? 27.394 -13.103 19.465 1.00 22.33 ? 38  ARG   C C   1 
ATOM   1352 O  O   . ARG   B 1 32  ? 27.464 -14.315 19.251 1.00 22.11 ? 38  ARG   C O   1 
ATOM   1353 C  CB  . ARG   B 1 32  ? 27.375 -13.110 21.973 1.00 24.15 ? 38  ARG   C CB  1 
ATOM   1354 C  CG  . ARG   B 1 32  ? 28.022 -12.736 23.300 1.00 26.61 ? 38  ARG   C CG  1 
ATOM   1355 C  CD  . ARG   B 1 32  ? 27.281 -13.329 24.491 1.00 27.90 ? 38  ARG   C CD  1 
ATOM   1356 N  NE  . ARG   B 1 32  ? 27.344 -14.796 24.511 1.00 25.79 ? 38  ARG   C NE  1 
ATOM   1357 C  CZ  . ARG   B 1 32  ? 27.285 -15.539 25.618 1.00 25.79 ? 38  ARG   C CZ  1 
ATOM   1358 N  NH1 . ARG   B 1 32  ? 27.144 -14.962 26.810 1.00 23.17 ? 38  ARG   C NH1 1 
ATOM   1359 N  NH2 . ARG   B 1 32  ? 27.391 -16.862 25.545 1.00 23.74 ? 38  ARG   C NH2 1 
ATOM   1360 N  N   . ASP   B 1 33  ? 26.717 -12.250 18.648 1.00 20.64 ? 39  ASP   C N   1 
ATOM   1361 C  CA  . ASP   B 1 33  ? 25.938 -12.691 17.499 1.00 20.01 ? 39  ASP   C CA  1 
ATOM   1362 C  C   . ASP   B 1 33  ? 24.836 -13.656 17.945 1.00 19.55 ? 39  ASP   C C   1 
ATOM   1363 O  O   . ASP   B 1 33  ? 24.554 -14.617 17.212 1.00 19.52 ? 39  ASP   C O   1 
ATOM   1364 C  CB  . ASP   B 1 33  ? 26.802 -13.303 16.364 1.00 21.22 ? 39  ASP   C CB  1 
ATOM   1365 C  CG  . ASP   B 1 33  ? 25.993 -13.592 15.096 1.00 22.68 ? 39  ASP   C CG  1 
ATOM   1366 O  OD1 . ASP   B 1 33  ? 25.068 -12.787 14.782 1.00 22.09 ? 39  ASP   C OD1 1 
ATOM   1367 O  OD2 . ASP   B 1 33  ? 26.257 -14.646 14.432 1.00 19.15 ? 39  ASP   C OD2 1 
ATOM   1368 N  N   . LEU   B 1 34  ? 24.180 -13.390 19.122 1.00 18.09 ? 40  LEU   C N   1 
ATOM   1369 C  CA  . LEU   B 1 34  ? 23.092 -14.266 19.610 1.00 17.60 ? 40  LEU   C CA  1 
ATOM   1370 C  C   . LEU   B 1 34  ? 21.799 -13.489 19.872 1.00 18.37 ? 40  LEU   C C   1 
ATOM   1371 O  O   . LEU   B 1 34  ? 21.842 -12.346 20.322 1.00 19.07 ? 40  LEU   C O   1 
ATOM   1372 C  CB  . LEU   B 1 34  ? 23.467 -14.984 20.911 1.00 17.45 ? 40  LEU   C CB  1 
ATOM   1373 C  CG  . LEU   B 1 34  ? 24.514 -16.102 20.844 1.00 19.61 ? 40  LEU   C CG  1 
ATOM   1374 C  CD1 . LEU   B 1 34  ? 24.740 -16.702 22.238 1.00 20.11 ? 40  LEU   C CD1 1 
ATOM   1375 C  CD2 . LEU   B 1 34  ? 24.100 -17.213 19.877 1.00 21.71 ? 40  LEU   C CD2 1 
ATOM   1376 N  N   . LEU   B 1 35  ? 20.670 -14.179 19.689 1.00 18.95 ? 41  LEU   C N   1 
ATOM   1377 C  CA  . LEU   B 1 35  ? 19.328 -13.680 19.957 1.00 20.46 ? 41  LEU   C CA  1 
ATOM   1378 C  C   . LEU   B 1 35  ? 18.508 -14.908 20.390 1.00 21.63 ? 41  LEU   C C   1 
ATOM   1379 O  O   . LEU   B 1 35  ? 18.667 -16.001 19.831 1.00 22.97 ? 41  LEU   C O   1 
ATOM   1380 C  CB  . LEU   B 1 35  ? 18.682 -13.022 18.709 1.00 20.19 ? 41  LEU   C CB  1 
ATOM   1381 C  CG  . LEU   B 1 35  ? 17.317 -12.360 18.979 1.00 21.98 ? 41  LEU   C CG  1 
ATOM   1382 C  CD1 . LEU   B 1 35  ? 17.193 -11.057 18.245 1.00 24.23 ? 41  LEU   C CD1 1 
ATOM   1383 C  CD2 . LEU   B 1 35  ? 16.135 -13.330 18.640 1.00 21.84 ? 41  LEU   C CD2 1 
ATOM   1384 N  N   . VAL   B 1 36  ? 17.717 -14.745 21.440 1.00 21.51 ? 42  VAL   C N   1 
ATOM   1385 C  CA  . VAL   B 1 36  ? 16.826 -15.771 21.951 1.00 21.95 ? 42  VAL   C CA  1 
ATOM   1386 C  C   . VAL   B 1 36  ? 15.395 -15.237 21.952 1.00 22.93 ? 42  VAL   C C   1 
ATOM   1387 O  O   . VAL   B 1 36  ? 15.138 -14.168 22.502 1.00 23.65 ? 42  VAL   C O   1 
ATOM   1388 C  CB  . VAL   B 1 36  ? 17.209 -16.259 23.364 1.00 23.11 ? 42  VAL   C CB  1 
ATOM   1389 C  CG1 . VAL   B 1 36  ? 16.206 -17.302 23.870 1.00 23.25 ? 42  VAL   C CG1 1 
ATOM   1390 C  CG2 . VAL   B 1 36  ? 18.636 -16.812 23.386 1.00 23.56 ? 42  VAL   C CG2 1 
ATOM   1391 N  N   . SER   B 1 37  ? 14.463 -15.994 21.373 1.00 22.46 ? 43  SER   C N   1 
ATOM   1392 C  CA  . SER   B 1 37  ? 13.059 -15.615 21.381 1.00 22.75 ? 43  SER   C CA  1 
ATOM   1393 C  C   . SER   B 1 37  ? 12.227 -16.724 22.075 1.00 23.30 ? 43  SER   C C   1 
ATOM   1394 O  O   . SER   B 1 37  ? 12.721 -17.850 22.262 1.00 22.16 ? 43  SER   C O   1 
ATOM   1395 C  CB  . SER   B 1 37  ? 12.562 -15.372 19.962 1.00 23.70 ? 43  SER   C CB  1 
ATOM   1396 O  OG  . SER   B 1 37  ? 12.699 -16.533 19.161 1.00 25.86 ? 43  SER   C OG  1 
ATOM   1397 N  N   . SER   B 1 38  ? 10.993 -16.392 22.505 1.00 23.70 ? 44  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 38  ? 10.133 -17.389 23.168 1.00 24.74 ? 44  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 38  ? 9.307  -18.168 22.143 1.00 26.41 ? 44  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 38  ? 9.025  -17.663 21.049 1.00 26.88 ? 44  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 38  ? 9.228  -16.728 24.207 1.00 26.57 ? 44  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 38  ? 8.332  -15.848 23.555 1.00 29.57 ? 44  SER   C OG  1 
ATOM   1403 N  N   . THR   B 1 39  ? 8.931  -19.416 22.477 1.00 27.35 ? 45  THR   C N   1 
ATOM   1404 C  CA  . THR   B 1 39  ? 8.158  -20.273 21.571 1.00 28.89 ? 45  THR   C CA  1 
ATOM   1405 C  C   . THR   B 1 39  ? 6.914  -20.831 22.265 1.00 30.70 ? 45  THR   C C   1 
ATOM   1406 O  O   . THR   B 1 39  ? 6.887  -20.941 23.490 1.00 31.30 ? 45  THR   C O   1 
ATOM   1407 C  CB  . THR   B 1 39  ? 9.027  -21.446 21.023 1.00 30.41 ? 45  THR   C CB  1 
ATOM   1408 O  OG1 . THR   B 1 39  ? 9.455  -22.255 22.110 1.00 31.25 ? 45  THR   C OG1 1 
ATOM   1409 C  CG2 . THR   B 1 39  ? 10.228 -20.981 20.209 1.00 31.23 ? 45  THR   C CG2 1 
ATOM   1410 N  N   . THR   B 1 40  ? 5.911  -21.235 21.479 1.00 32.03 ? 46  THR   C N   1 
ATOM   1411 C  CA  . THR   B 1 40  ? 4.688  -21.820 22.035 1.00 34.03 ? 46  THR   C CA  1 
ATOM   1412 C  C   . THR   B 1 40  ? 4.896  -23.310 22.322 1.00 34.38 ? 46  THR   C C   1 
ATOM   1413 O  O   . THR   B 1 40  ? 4.470  -23.801 23.369 1.00 35.15 ? 46  THR   C O   1 
ATOM   1414 C  CB  . THR   B 1 40  ? 3.482  -21.532 21.131 1.00 36.72 ? 46  THR   C CB  1 
ATOM   1415 O  OG1 . THR   B 1 40  ? 3.735  -22.100 19.844 1.00 39.01 ? 46  THR   C OG1 1 
ATOM   1416 C  CG2 . THR   B 1 40  ? 3.222  -20.034 20.967 1.00 37.25 ? 46  THR   C CG2 1 
ATOM   1417 N  N   . ALA   B 1 41  ? 5.559  -24.024 21.398 1.00 34.06 ? 47  ALA   C N   1 
ATOM   1418 C  CA  . ALA   B 1 41  ? 5.863  -25.448 21.549 1.00 34.05 ? 47  ALA   C CA  1 
ATOM   1419 C  C   . ALA   B 1 41  ? 7.184  -25.661 22.313 1.00 34.02 ? 47  ALA   C C   1 
ATOM   1420 O  O   . ALA   B 1 41  ? 8.119  -24.871 22.173 1.00 33.87 ? 47  ALA   C O   1 
ATOM   1421 C  CB  . ALA   B 1 41  ? 5.957  -26.103 20.175 1.00 33.78 ? 47  ALA   C CB  1 
ATOM   1422 N  N   . GLN   B 1 42  ? 7.276  -26.748 23.079 1.00 34.38 ? 48  GLN   C N   1 
ATOM   1423 C  CA  . GLN   B 1 42  ? 8.497  -27.069 23.806 1.00 35.15 ? 48  GLN   C CA  1 
ATOM   1424 C  C   . GLN   B 1 42  ? 9.499  -27.730 22.859 1.00 34.79 ? 48  GLN   C C   1 
ATOM   1425 O  O   . GLN   B 1 42  ? 9.120  -28.591 22.063 1.00 35.71 ? 48  GLN   C O   1 
ATOM   1426 C  CB  . GLN   B 1 42  ? 8.195  -27.980 25.014 1.00 38.32 ? 48  GLN   C CB  1 
ATOM   1427 C  CG  . GLN   B 1 42  ? 7.862  -27.198 26.280 1.00 43.93 ? 48  GLN   C CG  1 
ATOM   1428 C  CD  . GLN   B 1 42  ? 7.835  -28.118 27.469 1.00 50.47 ? 48  GLN   C CD  1 
ATOM   1429 O  OE1 . GLN   B 1 42  ? 7.396  -29.274 27.389 1.00 52.38 ? 48  GLN   C OE1 1 
ATOM   1430 N  NE2 . GLN   B 1 42  ? 8.323  -27.634 28.601 1.00 51.95 ? 48  GLN   C NE2 1 
ATOM   1431 N  N   . GLY   B 1 43  ? 10.760 -27.325 22.964 1.00 33.21 ? 49  GLY   C N   1 
ATOM   1432 C  CA  . GLY   B 1 43  ? 11.850 -27.874 22.173 1.00 32.36 ? 49  GLY   C CA  1 
ATOM   1433 C  C   . GLY   B 1 43  ? 12.433 -29.132 22.792 1.00 31.51 ? 49  GLY   C C   1 
ATOM   1434 O  O   . GLY   B 1 43  ? 12.156 -29.447 23.956 1.00 31.37 ? 49  GLY   C O   1 
ATOM   1435 N  N   . CYS   B 1 44  ? 13.262 -29.842 22.032 1.00 30.79 ? 50  CYS   C N   1 
ATOM   1436 C  CA  . CYS   B 1 44  ? 13.818 -31.097 22.499 1.00 31.87 ? 50  CYS   C CA  1 
ATOM   1437 C  C   . CYS   B 1 44  ? 15.322 -31.095 22.710 1.00 30.86 ? 50  CYS   C C   1 
ATOM   1438 O  O   . CYS   B 1 44  ? 15.827 -32.076 23.254 1.00 32.12 ? 50  CYS   C O   1 
ATOM   1439 C  CB  . CYS   B 1 44  ? 13.386 -32.218 21.561 1.00 34.47 ? 50  CYS   C CB  1 
ATOM   1440 S  SG  . CYS   B 1 44  ? 11.623 -32.615 21.701 1.00 42.66 ? 50  CYS   C SG  1 
ATOM   1441 N  N   . ASP   B 1 45  ? 16.041 -30.038 22.288 1.00 28.52 ? 51  ASP   C N   1 
ATOM   1442 C  CA  . ASP   B 1 45  ? 17.489 -29.986 22.453 1.00 28.06 ? 51  ASP   C CA  1 
ATOM   1443 C  C   . ASP   B 1 45  ? 17.873 -29.803 23.925 1.00 27.02 ? 51  ASP   C C   1 
ATOM   1444 O  O   . ASP   B 1 45  ? 17.133 -29.172 24.709 1.00 27.68 ? 51  ASP   C O   1 
ATOM   1445 C  CB  . ASP   B 1 45  ? 18.126 -28.856 21.611 1.00 29.31 ? 51  ASP   C CB  1 
ATOM   1446 C  CG  . ASP   B 1 45  ? 17.979 -29.035 20.119 1.00 32.37 ? 51  ASP   C CG  1 
ATOM   1447 O  OD1 . ASP   B 1 45  ? 18.224 -30.160 19.630 1.00 33.29 ? 51  ASP   C OD1 1 
ATOM   1448 O  OD2 . ASP   B 1 45  ? 17.630 -28.041 19.433 1.00 32.29 ? 51  ASP   C OD2 1 
ATOM   1449 N  N   . THR   B 1 46  ? 19.007 -30.384 24.294 1.00 24.42 ? 52  THR   C N   1 
ATOM   1450 C  CA  . THR   B 1 46  ? 19.547 -30.235 25.637 1.00 23.92 ? 52  THR   C CA  1 
ATOM   1451 C  C   . THR   B 1 46  ? 20.829 -29.408 25.512 1.00 23.09 ? 52  THR   C C   1 
ATOM   1452 O  O   . THR   B 1 46  ? 21.649 -29.720 24.654 1.00 22.36 ? 52  THR   C O   1 
ATOM   1453 C  CB  . THR   B 1 46  ? 19.899 -31.599 26.251 1.00 25.52 ? 52  THR   C CB  1 
ATOM   1454 O  OG1 . THR   B 1 46  ? 18.748 -32.465 26.285 1.00 25.73 ? 52  THR   C OG1 1 
ATOM   1455 C  CG2 . THR   B 1 46  ? 20.531 -31.452 27.641 1.00 26.52 ? 52  THR   C CG2 1 
ATOM   1456 N  N   . ILE   B 1 47  ? 21.015 -28.391 26.360 1.00 22.55 ? 53  ILE   C N   1 
ATOM   1457 C  CA  . ILE   B 1 47  ? 22.233 -27.583 26.324 1.00 22.57 ? 53  ILE   C CA  1 
ATOM   1458 C  C   . ILE   B 1 47  ? 23.299 -28.298 27.138 1.00 22.22 ? 53  ILE   C C   1 
ATOM   1459 O  O   . ILE   B 1 47  ? 23.000 -28.781 28.242 1.00 22.52 ? 53  ILE   C O   1 
ATOM   1460 C  CB  . ILE   B 1 47  ? 22.018 -26.155 26.903 1.00 23.12 ? 53  ILE   C CB  1 
ATOM   1461 C  CG1 . ILE   B 1 47  ? 20.828 -25.452 26.222 1.00 23.65 ? 53  ILE   C CG1 1 
ATOM   1462 C  CG2 . ILE   B 1 47  ? 23.294 -25.312 26.754 1.00 23.78 ? 53  ILE   C CG2 1 
ATOM   1463 C  CD1 . ILE   B 1 47  ? 21.001 -25.306 24.670 1.00 24.70 ? 53  ILE   C CD1 1 
ATOM   1464 N  N   . ALA   B 1 48  ? 24.529 -28.350 26.620 1.00 21.00 ? 54  ALA   C N   1 
ATOM   1465 C  CA  . ALA   B 1 48  ? 25.623 -28.958 27.371 1.00 21.68 ? 54  ALA   C CA  1 
ATOM   1466 C  C   . ALA   B 1 48  ? 26.018 -28.036 28.526 1.00 22.32 ? 54  ALA   C C   1 
ATOM   1467 O  O   . ALA   B 1 48  ? 26.040 -26.815 28.357 1.00 23.28 ? 54  ALA   C O   1 
ATOM   1468 C  CB  . ALA   B 1 48  ? 26.836 -29.155 26.465 1.00 20.98 ? 54  ALA   C CB  1 
ATOM   1469 N  N   . ARG   B 1 49  ? 26.394 -28.619 29.658 1.00 21.09 ? 55  ARG   C N   1 
ATOM   1470 C  CA  . ARG   B 1 49  ? 26.856 -27.857 30.818 1.00 21.73 ? 55  ARG   C CA  1 
ATOM   1471 C  C   . ARG   B 1 49  ? 28.172 -28.516 31.181 1.00 22.34 ? 55  ARG   C C   1 
ATOM   1472 O  O   . ARG   B 1 49  ? 28.186 -29.512 31.923 1.00 22.71 ? 55  ARG   C O   1 
ATOM   1473 C  CB  . ARG   B 1 49  ? 25.825 -27.949 31.962 1.00 22.29 ? 55  ARG   C CB  1 
ATOM   1474 C  CG  . ARG   B 1 49  ? 24.482 -27.315 31.637 1.00 24.37 ? 55  ARG   C CG  1 
ATOM   1475 C  CD  . ARG   B 1 49  ? 24.508 -25.835 31.215 1.00 25.92 ? 55  ARG   C CD  1 
ATOM   1476 N  NE  . ARG   B 1 49  ? 23.162 -25.393 30.837 1.00 26.45 ? 55  ARG   C NE  1 
ATOM   1477 C  CZ  . ARG   B 1 49  ? 22.885 -24.294 30.139 1.00 26.91 ? 55  ARG   C CZ  1 
ATOM   1478 N  NH1 . ARG   B 1 49  ? 23.855 -23.462 29.777 1.00 24.49 ? 55  ARG   C NH1 1 
ATOM   1479 N  NH2 . ARG   B 1 49  ? 21.636 -23.998 29.834 1.00 26.76 ? 55  ARG   C NH2 1 
ATOM   1480 N  N   . CYS   B 1 50  ? 29.268 -28.022 30.558 1.00 21.97 ? 56  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 50  ? 30.559 -28.690 30.644 1.00 21.35 ? 56  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 50  ? 31.701 -27.745 30.152 1.00 20.72 ? 56  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 50  ? 31.439 -26.621 29.725 1.00 20.24 ? 56  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 50  ? 30.462 -29.889 29.709 1.00 21.91 ? 56  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 50  ? 30.325 -29.379 27.980 1.00 23.45 ? 56  CYS   C SG  1 
ATOM   1486 N  N   . ASP   B 1 51  ? 32.942 -28.276 30.079 1.00 19.88 ? 57  ASP   C N   1 
ATOM   1487 C  CA  . ASP   B 1 51  ? 34.053 -27.510 29.526 1.00 21.00 ? 57  ASP   C CA  1 
ATOM   1488 C  C   . ASP   B 1 51  ? 34.752 -28.308 28.389 1.00 20.77 ? 57  ASP   C C   1 
ATOM   1489 O  O   . ASP   B 1 51  ? 35.936 -28.118 28.167 1.00 21.23 ? 57  ASP   C O   1 
ATOM   1490 C  CB  . ASP   B 1 51  ? 35.036 -27.048 30.608 1.00 24.85 ? 57  ASP   C CB  1 
ATOM   1491 C  CG  . ASP   B 1 51  ? 35.739 -28.166 31.371 1.00 31.17 ? 57  ASP   C CG  1 
ATOM   1492 O  OD1 . ASP   B 1 51  ? 35.304 -29.339 31.251 1.00 31.52 ? 57  ASP   C OD1 1 
ATOM   1493 O  OD2 . ASP   B 1 51  ? 36.716 -27.867 32.093 1.00 35.60 ? 57  ASP   C OD2 1 
ATOM   1494 N  N   . CYS   B 1 52  ? 33.991 -29.177 27.654 1.00 20.43 ? 58  CYS   C N   1 
ATOM   1495 C  CA  . CYS   B 1 52  ? 34.498 -29.954 26.510 1.00 20.15 ? 58  CYS   C CA  1 
ATOM   1496 C  C   . CYS   B 1 52  ? 35.192 -29.070 25.483 1.00 19.92 ? 58  CYS   C C   1 
ATOM   1497 O  O   . CYS   B 1 52  ? 34.750 -27.940 25.226 1.00 20.12 ? 58  CYS   C O   1 
ATOM   1498 C  CB  . CYS   B 1 52  ? 33.380 -30.751 25.838 1.00 20.81 ? 58  CYS   C CB  1 
ATOM   1499 S  SG  . CYS   B 1 52  ? 32.817 -32.209 26.757 1.00 23.86 ? 58  CYS   C SG  1 
ATOM   1500 N  N   . GLN   B 1 53  ? 36.279 -29.595 24.904 1.00 19.03 ? 59  GLN   C N   1 
ATOM   1501 C  CA  . GLN   B 1 53  ? 36.982 -28.956 23.789 1.00 20.15 ? 59  GLN   C CA  1 
ATOM   1502 C  C   . GLN   B 1 53  ? 37.028 -29.852 22.535 1.00 19.76 ? 59  GLN   C C   1 
ATOM   1503 O  O   . GLN   B 1 53  ? 37.741 -29.552 21.588 1.00 18.62 ? 59  GLN   C O   1 
ATOM   1504 C  CB  . GLN   B 1 53  ? 38.375 -28.460 24.167 1.00 22.55 ? 59  GLN   C CB  1 
ATOM   1505 C  CG  . GLN   B 1 53  ? 38.365 -27.193 25.026 1.00 25.26 ? 59  GLN   C CG  1 
ATOM   1506 C  CD  . GLN   B 1 53  ? 39.754 -26.650 25.161 1.00 28.32 ? 59  GLN   C CD  1 
ATOM   1507 O  OE1 . GLN   B 1 53  ? 40.319 -26.647 26.256 1.00 30.26 ? 59  GLN   C OE1 1 
ATOM   1508 N  NE2 . GLN   B 1 53  ? 40.335 -26.219 24.044 1.00 27.08 ? 59  GLN   C NE2 1 
ATOM   1509 N  N   . THR   B 1 54  ? 36.237 -30.932 22.516 1.00 19.98 ? 60  THR   C N   1 
ATOM   1510 C  CA  . THR   B 1 54  ? 36.070 -31.787 21.359 1.00 20.47 ? 60  THR   C CA  1 
ATOM   1511 C  C   . THR   B 1 54  ? 34.570 -32.061 21.176 1.00 20.62 ? 60  THR   C C   1 
ATOM   1512 O  O   . THR   B 1 54  ? 33.806 -32.230 22.140 1.00 21.28 ? 60  THR   C O   1 
ATOM   1513 C  CB  . THR   B 1 54  ? 36.896 -33.062 21.445 1.00 22.58 ? 60  THR   C CB  1 
ATOM   1514 O  OG1 . THR   B 1 54  ? 36.355 -33.885 22.466 1.00 24.82 ? 60  THR   C OG1 1 
ATOM   1515 C  CG2 . THR   B 1 54  ? 38.384 -32.802 21.671 1.00 23.02 ? 60  THR   C CG2 1 
ATOM   1516 N  N   . GLY   B 1 55  ? 34.166 -32.108 19.919 1.00 19.31 ? 61  GLY   C N   1 
ATOM   1517 C  CA  . GLY   B 1 55  ? 32.770 -32.318 19.564 1.00 19.15 ? 61  GLY   C CA  1 
ATOM   1518 C  C   . GLY   B 1 55  ? 32.615 -32.582 18.083 1.00 19.05 ? 61  GLY   C C   1 
ATOM   1519 O  O   . GLY   B 1 55  ? 33.587 -32.890 17.391 1.00 21.08 ? 61  GLY   C O   1 
ATOM   1520 N  N   . VAL   B 1 56  ? 31.411 -32.409 17.577 1.00 17.37 ? 62  VAL   C N   1 
ATOM   1521 C  CA  . VAL   B 1 56  ? 31.094 -32.614 16.165 1.00 16.19 ? 62  VAL   C CA  1 
ATOM   1522 C  C   . VAL   B 1 56  ? 30.169 -31.472 15.724 1.00 16.25 ? 62  VAL   C C   1 
ATOM   1523 O  O   . VAL   B 1 56  ? 29.225 -31.158 16.442 1.00 16.47 ? 62  VAL   C O   1 
ATOM   1524 C  CB  . VAL   B 1 56  ? 30.373 -33.984 16.041 1.00 16.85 ? 62  VAL   C CB  1 
ATOM   1525 C  CG1 . VAL   B 1 56  ? 29.746 -34.155 14.668 1.00 16.75 ? 62  VAL   C CG1 1 
ATOM   1526 C  CG2 . VAL   B 1 56  ? 31.326 -35.146 16.365 1.00 17.69 ? 62  VAL   C CG2 1 
ATOM   1527 N  N   . TYR   B 1 57  ? 30.400 -30.885 14.532 1.00 17.03 ? 63  TYR   C N   1 
ATOM   1528 C  CA  . TYR   B 1 57  ? 29.538 -29.784 14.045 1.00 17.73 ? 63  TYR   C CA  1 
ATOM   1529 C  C   . TYR   B 1 57  ? 28.946 -30.075 12.651 1.00 18.95 ? 63  TYR   C C   1 
ATOM   1530 O  O   . TYR   B 1 57  ? 29.587 -30.760 11.877 1.00 19.84 ? 63  TYR   C O   1 
ATOM   1531 C  CB  . TYR   B 1 57  ? 30.281 -28.427 14.062 1.00 18.83 ? 63  TYR   C CB  1 
ATOM   1532 C  CG  . TYR   B 1 57  ? 31.144 -28.114 12.857 1.00 19.43 ? 63  TYR   C CG  1 
ATOM   1533 C  CD1 . TYR   B 1 57  ? 32.411 -28.666 12.719 1.00 19.97 ? 63  TYR   C CD1 1 
ATOM   1534 C  CD2 . TYR   B 1 57  ? 30.697 -27.255 11.854 1.00 19.83 ? 63  TYR   C CD2 1 
ATOM   1535 C  CE1 . TYR   B 1 57  ? 33.240 -28.319 11.651 1.00 20.51 ? 63  TYR   C CE1 1 
ATOM   1536 C  CE2 . TYR   B 1 57  ? 31.510 -26.915 10.773 1.00 19.89 ? 63  TYR   C CE2 1 
ATOM   1537 C  CZ  . TYR   B 1 57  ? 32.768 -27.486 10.648 1.00 21.26 ? 63  TYR   C CZ  1 
ATOM   1538 O  OH  . TYR   B 1 57  ? 33.606 -27.150 9.594  1.00 22.92 ? 63  TYR   C OH  1 
ATOM   1539 N  N   . TYR   B 1 58  ? 27.767 -29.500 12.314 1.00 19.22 ? 64  TYR   C N   1 
ATOM   1540 C  CA  . TYR   B 1 58  ? 27.179 -29.709 10.992 1.00 20.67 ? 64  TYR   C CA  1 
ATOM   1541 C  C   . TYR   B 1 58  ? 27.580 -28.570 10.055 1.00 21.28 ? 64  TYR   C C   1 
ATOM   1542 O  O   . TYR   B 1 58  ? 27.372 -27.396 10.384 1.00 20.74 ? 64  TYR   C O   1 
ATOM   1543 C  CB  . TYR   B 1 58  ? 25.651 -29.854 11.023 1.00 21.27 ? 64  TYR   C CB  1 
ATOM   1544 C  CG  . TYR   B 1 58  ? 25.077 -30.122 9.637  1.00 22.72 ? 64  TYR   C CG  1 
ATOM   1545 C  CD1 . TYR   B 1 58  ? 25.444 -31.259 8.913  1.00 24.03 ? 64  TYR   C CD1 1 
ATOM   1546 C  CD2 . TYR   B 1 58  ? 24.203 -29.228 9.040  1.00 23.42 ? 64  TYR   C CD2 1 
ATOM   1547 C  CE1 . TYR   B 1 58  ? 24.964 -31.485 7.622  1.00 24.24 ? 64  TYR   C CE1 1 
ATOM   1548 C  CE2 . TYR   B 1 58  ? 23.692 -29.459 7.764  1.00 24.62 ? 64  TYR   C CE2 1 
ATOM   1549 C  CZ  . TYR   B 1 58  ? 24.070 -30.593 7.058  1.00 25.30 ? 64  TYR   C CZ  1 
ATOM   1550 O  OH  . TYR   B 1 58  ? 23.570 -30.827 5.795  1.00 27.78 ? 64  TYR   C OH  1 
ATOM   1551 N  N   . CYS   B 1 59  ? 28.132 -28.943 8.878  1.00 21.80 ? 65  CYS   C N   1 
ATOM   1552 C  CA  . CYS   B 1 59  ? 28.575 -28.001 7.847  1.00 22.87 ? 65  CYS   C CA  1 
ATOM   1553 C  C   . CYS   B 1 59  ? 27.632 -28.129 6.636  1.00 23.96 ? 65  CYS   C C   1 
ATOM   1554 O  O   . CYS   B 1 59  ? 27.792 -29.070 5.848  1.00 24.11 ? 65  CYS   C O   1 
ATOM   1555 C  CB  . CYS   B 1 59  ? 30.023 -28.283 7.461  1.00 23.29 ? 65  CYS   C CB  1 
ATOM   1556 S  SG  . CYS   B 1 59  ? 30.656 -27.247 6.103  1.00 23.70 ? 65  CYS   C SG  1 
ATOM   1557 N  N   . SER   B 1 60  ? 26.635 -27.220 6.499  1.00 23.31 ? 66  SER   C N   1 
ATOM   1558 C  CA  A SER   B 1 60  ? 25.674 -27.343 5.406  0.50 24.27 ? 66  SER   C CA  1 
ATOM   1559 C  CA  B SER   B 1 60  ? 25.675 -27.348 5.405  0.50 23.86 ? 66  SER   C CA  1 
ATOM   1560 C  C   . SER   B 1 60  ? 26.298 -27.249 3.999  1.00 24.23 ? 66  SER   C C   1 
ATOM   1561 O  O   . SER   B 1 60  ? 25.828 -27.932 3.088  1.00 25.15 ? 66  SER   C O   1 
ATOM   1562 C  CB  A SER   B 1 60  ? 24.533 -26.345 5.567  0.50 26.58 ? 66  SER   C CB  1 
ATOM   1563 C  CB  B SER   B 1 60  ? 24.531 -26.355 5.562  0.50 25.01 ? 66  SER   C CB  1 
ATOM   1564 O  OG  A SER   B 1 60  ? 25.009 -25.034 5.823  0.50 30.02 ? 66  SER   C OG  1 
ATOM   1565 O  OG  B SER   B 1 60  ? 23.496 -26.634 4.634  0.50 26.44 ? 66  SER   C OG  1 
ATOM   1566 N  N   . SER   B 1 61  ? 27.364 -26.431 3.821  1.00 23.53 ? 67  SER   C N   1 
ATOM   1567 C  CA  . SER   B 1 61  ? 28.066 -26.246 2.534  1.00 23.70 ? 67  SER   C CA  1 
ATOM   1568 C  C   . SER   B 1 61  ? 28.840 -27.510 2.047  1.00 23.97 ? 67  SER   C C   1 
ATOM   1569 O  O   . SER   B 1 61  ? 29.372 -27.533 0.921  1.00 23.88 ? 67  SER   C O   1 
ATOM   1570 C  CB  . SER   B 1 61  ? 29.018 -25.054 2.611  1.00 23.59 ? 67  SER   C CB  1 
ATOM   1571 O  OG  . SER   B 1 61  ? 29.971 -25.222 3.648  1.00 26.00 ? 67  SER   C OG  1 
ATOM   1572 N  N   . ARG   B 1 62  ? 28.910 -28.555 2.905  1.00 22.89 ? 68  ARG   C N   1 
ATOM   1573 C  CA  . ARG   B 1 62  ? 29.538 -29.838 2.566  1.00 22.25 ? 68  ARG   C CA  1 
ATOM   1574 C  C   . ARG   B 1 62  ? 28.583 -31.045 2.841  1.00 22.15 ? 68  ARG   C C   1 
ATOM   1575 O  O   . ARG   B 1 62  ? 29.003 -32.189 2.652  1.00 22.50 ? 68  ARG   C O   1 
ATOM   1576 C  CB  . ARG   B 1 62  ? 30.796 -30.034 3.401  1.00 24.18 ? 68  ARG   C CB  1 
ATOM   1577 C  CG  . ARG   B 1 62  ? 31.871 -28.994 3.128  1.00 27.83 ? 68  ARG   C CG  1 
ATOM   1578 C  CD  . ARG   B 1 62  ? 32.615 -29.249 1.839  1.00 28.55 ? 68  ARG   C CD  1 
ATOM   1579 N  NE  . ARG   B 1 62  ? 33.623 -28.203 1.618  1.00 31.33 ? 68  ARG   C NE  1 
ATOM   1580 C  CZ  . ARG   B 1 62  ? 33.397 -27.063 0.974  1.00 32.39 ? 68  ARG   C CZ  1 
ATOM   1581 N  NH1 . ARG   B 1 62  ? 32.210 -26.823 0.434  1.00 33.25 ? 68  ARG   C NH1 1 
ATOM   1582 N  NH2 . ARG   B 1 62  ? 34.370 -26.171 0.824  1.00 30.22 ? 68  ARG   C NH2 1 
ATOM   1583 N  N   . ARG   B 1 63  ? 27.368 -30.793 3.389  1.00 22.14 ? 69  ARG   C N   1 
ATOM   1584 C  CA  . ARG   B 1 63  ? 26.395 -31.832 3.788  1.00 23.80 ? 69  ARG   C CA  1 
ATOM   1585 C  C   . ARG   B 1 63  ? 27.080 -32.861 4.698  1.00 24.41 ? 69  ARG   C C   1 
ATOM   1586 O  O   . ARG   B 1 63  ? 26.924 -34.056 4.500  1.00 24.96 ? 69  ARG   C O   1 
ATOM   1587 C  CB  . ARG   B 1 63  ? 25.791 -32.510 2.536  1.00 26.69 ? 69  ARG   C CB  1 
ATOM   1588 C  CG  . ARG   B 1 63  ? 24.344 -32.181 2.306  1.00 31.93 ? 69  ARG   C CG  1 
ATOM   1589 C  CD  . ARG   B 1 63  ? 24.135 -30.771 1.971  1.00 36.24 ? 69  ARG   C CD  1 
ATOM   1590 N  NE  . ARG   B 1 63  ? 22.910 -30.617 1.206  1.00 41.63 ? 69  ARG   C NE  1 
ATOM   1591 C  CZ  . ARG   B 1 63  ? 22.348 -29.447 0.937  1.00 44.69 ? 69  ARG   C CZ  1 
ATOM   1592 N  NH1 . ARG   B 1 63  ? 22.893 -28.318 1.388  1.00 44.90 ? 69  ARG   C NH1 1 
ATOM   1593 N  NH2 . ARG   B 1 63  ? 21.232 -29.392 0.225  1.00 44.58 ? 69  ARG   C NH2 1 
ATOM   1594 N  N   . LYS   B 1 64  ? 27.940 -32.376 5.609  1.00 23.89 ? 70  LYS   C N   1 
ATOM   1595 C  CA  . LYS   B 1 64  ? 28.725 -33.273 6.454  1.00 24.39 ? 70  LYS   C CA  1 
ATOM   1596 C  C   . LYS   B 1 64  ? 28.864 -32.803 7.885  1.00 23.78 ? 70  LYS   C C   1 
ATOM   1597 O  O   . LYS   B 1 64  ? 28.997 -31.603 8.138  1.00 23.67 ? 70  LYS   C O   1 
ATOM   1598 C  CB  . LYS   B 1 64  ? 30.148 -33.434 5.874  1.00 28.00 ? 70  LYS   C CB  1 
ATOM   1599 C  CG  . LYS   B 1 64  ? 30.267 -34.528 4.836  1.00 36.08 ? 70  LYS   C CG  1 
ATOM   1600 C  CD  . LYS   B 1 64  ? 31.717 -34.851 4.529  1.00 42.85 ? 70  LYS   C CD  1 
ATOM   1601 C  CE  . LYS   B 1 64  ? 31.822 -35.550 3.193  1.00 48.22 ? 70  LYS   C CE  1 
ATOM   1602 N  NZ  . LYS   B 1 64  ? 31.140 -34.776 2.119  1.00 51.90 ? 70  LYS   C NZ  1 
ATOM   1603 N  N   . HIS   B 1 65  ? 28.928 -33.782 8.815  1.00 23.10 ? 71  HIS   C N   1 
ATOM   1604 C  CA  . HIS   B 1 65  ? 29.183 -33.524 10.232 1.00 22.97 ? 71  HIS   C CA  1 
ATOM   1605 C  C   . HIS   B 1 65  ? 30.668 -33.800 10.412 1.00 23.91 ? 71  HIS   C C   1 
ATOM   1606 O  O   . HIS   B 1 65  ? 31.150 -34.863 9.983  1.00 25.50 ? 71  HIS   C O   1 
ATOM   1607 C  CB  . HIS   B 1 65  ? 28.362 -34.493 11.131 1.00 22.22 ? 71  HIS   C CB  1 
ATOM   1608 C  CG  . HIS   B 1 65  ? 26.890 -34.270 11.070 1.00 23.62 ? 71  HIS   C CG  1 
ATOM   1609 N  ND1 . HIS   B 1 65  ? 26.237 -33.474 12.002 1.00 25.66 ? 71  HIS   C ND1 1 
ATOM   1610 C  CD2 . HIS   B 1 65  ? 25.981 -34.734 10.179 1.00 23.95 ? 71  HIS   C CD2 1 
ATOM   1611 C  CE1 . HIS   B 1 65  ? 24.959 -33.494 11.658 1.00 25.76 ? 71  HIS   C CE1 1 
ATOM   1612 N  NE2 . HIS   B 1 65  ? 24.755 -34.247 10.574 1.00 25.15 ? 71  HIS   C NE2 1 
ATOM   1613 N  N   . TYR   B 1 66  ? 31.416 -32.851 10.995 1.00 22.71 ? 72  TYR   C N   1 
ATOM   1614 C  CA  . TYR   B 1 66  ? 32.852 -33.063 11.158 1.00 22.36 ? 72  TYR   C CA  1 
ATOM   1615 C  C   . TYR   B 1 66  ? 33.251 -33.123 12.620 1.00 20.90 ? 72  TYR   C C   1 
ATOM   1616 O  O   . TYR   B 1 66  ? 32.894 -32.225 13.396 1.00 20.43 ? 72  TYR   C O   1 
ATOM   1617 C  CB  . TYR   B 1 66  ? 33.662 -31.909 10.521 1.00 22.86 ? 72  TYR   C CB  1 
ATOM   1618 C  CG  . TYR   B 1 66  ? 33.587 -31.808 9.013  1.00 24.66 ? 72  TYR   C CG  1 
ATOM   1619 C  CD1 . TYR   B 1 66  ? 34.441 -32.542 8.207  1.00 26.13 ? 72  TYR   C CD1 1 
ATOM   1620 C  CD2 . TYR   B 1 66  ? 32.750 -30.885 8.399  1.00 26.45 ? 72  TYR   C CD2 1 
ATOM   1621 C  CE1 . TYR   B 1 66  ? 34.414 -32.410 6.821  1.00 27.41 ? 72  TYR   C CE1 1 
ATOM   1622 C  CE2 . TYR   B 1 66  ? 32.699 -30.758 7.019  1.00 27.63 ? 72  TYR   C CE2 1 
ATOM   1623 C  CZ  . TYR   B 1 66  ? 33.545 -31.508 6.230  1.00 28.91 ? 72  TYR   C CZ  1 
ATOM   1624 O  OH  . TYR   B 1 66  ? 33.509 -31.340 4.869  1.00 30.67 ? 72  TYR   C OH  1 
ATOM   1625 N  N   . PRO   B 1 67  ? 34.083 -34.116 12.995 1.00 20.56 ? 73  PRO   C N   1 
ATOM   1626 C  CA  . PRO   B 1 67  ? 34.625 -34.097 14.367 1.00 19.78 ? 73  PRO   C CA  1 
ATOM   1627 C  C   . PRO   B 1 67  ? 35.717 -33.027 14.463 1.00 19.92 ? 73  PRO   C C   1 
ATOM   1628 O  O   . PRO   B 1 67  ? 36.564 -32.948 13.564 1.00 20.35 ? 73  PRO   C O   1 
ATOM   1629 C  CB  . PRO   B 1 67  ? 35.213 -35.510 14.554 1.00 21.07 ? 73  PRO   C CB  1 
ATOM   1630 C  CG  . PRO   B 1 67  ? 35.425 -36.067 13.178 1.00 21.66 ? 73  PRO   C CG  1 
ATOM   1631 C  CD  . PRO   B 1 67  ? 34.629 -35.231 12.175 1.00 20.53 ? 73  PRO   C CD  1 
ATOM   1632 N  N   . VAL   B 1 68  ? 35.700 -32.193 15.518 1.00 18.78 ? 74  VAL   C N   1 
ATOM   1633 C  CA  . VAL   B 1 68  ? 36.712 -31.134 15.644 1.00 19.35 ? 74  VAL   C CA  1 
ATOM   1634 C  C   . VAL   B 1 68  ? 37.130 -30.936 17.111 1.00 19.37 ? 74  VAL   C C   1 
ATOM   1635 O  O   . VAL   B 1 68  ? 36.395 -31.279 18.032 1.00 19.73 ? 74  VAL   C O   1 
ATOM   1636 C  CB  . VAL   B 1 68  ? 36.180 -29.773 15.094 1.00 20.48 ? 74  VAL   C CB  1 
ATOM   1637 C  CG1 . VAL   B 1 68  ? 36.032 -29.741 13.580 1.00 21.97 ? 74  VAL   C CG1 1 
ATOM   1638 C  CG2 . VAL   B 1 68  ? 34.897 -29.349 15.834 1.00 20.27 ? 74  VAL   C CG2 1 
ATOM   1639 N  N   . SER   B 1 69  ? 38.285 -30.320 17.296 1.00 20.09 ? 75  SER   C N   1 
ATOM   1640 C  CA  . SER   B 1 69  ? 38.806 -29.791 18.545 1.00 21.44 ? 75  SER   C CA  1 
ATOM   1641 C  C   . SER   B 1 69  ? 38.585 -28.270 18.426 1.00 21.24 ? 75  SER   C C   1 
ATOM   1642 O  O   . SER   B 1 69  ? 38.842 -27.673 17.355 1.00 20.36 ? 75  SER   C O   1 
ATOM   1643 C  CB  . SER   B 1 69  ? 40.293 -30.085 18.679 1.00 24.52 ? 75  SER   C CB  1 
ATOM   1644 O  OG  . SER   B 1 69  ? 40.500 -31.475 18.872 1.00 30.06 ? 75  SER   C OG  1 
ATOM   1645 N  N   . PHE   B 1 70  ? 38.050 -27.653 19.488 1.00 20.64 ? 76  PHE   C N   1 
ATOM   1646 C  CA  . PHE   B 1 70  ? 37.737 -26.220 19.494 1.00 20.30 ? 76  PHE   C CA  1 
ATOM   1647 C  C   . PHE   B 1 70  ? 38.261 -25.503 20.753 1.00 20.34 ? 76  PHE   C C   1 
ATOM   1648 O  O   . PHE   B 1 70  ? 38.355 -26.115 21.838 1.00 20.69 ? 76  PHE   C O   1 
ATOM   1649 C  CB  . PHE   B 1 70  ? 36.232 -25.951 19.304 1.00 19.89 ? 76  PHE   C CB  1 
ATOM   1650 C  CG  . PHE   B 1 70  ? 35.326 -26.663 20.287 1.00 18.73 ? 76  PHE   C CG  1 
ATOM   1651 C  CD1 . PHE   B 1 70  ? 34.827 -27.935 20.007 1.00 18.47 ? 76  PHE   C CD1 1 
ATOM   1652 C  CD2 . PHE   B 1 70  ? 34.922 -26.036 21.458 1.00 19.08 ? 76  PHE   C CD2 1 
ATOM   1653 C  CE1 . PHE   B 1 70  ? 33.994 -28.590 20.911 1.00 20.03 ? 76  PHE   C CE1 1 
ATOM   1654 C  CE2 . PHE   B 1 70  ? 34.061 -26.663 22.342 1.00 19.57 ? 76  PHE   C CE2 1 
ATOM   1655 C  CZ  . PHE   B 1 70  ? 33.599 -27.936 22.081 1.00 18.94 ? 76  PHE   C CZ  1 
ATOM   1656 N  N   . SER   B 1 71  ? 38.608 -24.210 20.604 1.00 19.80 ? 77  SER   C N   1 
ATOM   1657 C  CA  . SER   B 1 71  ? 39.187 -23.402 21.688 1.00 20.31 ? 77  SER   C CA  1 
ATOM   1658 C  C   . SER   B 1 71  ? 38.158 -23.001 22.770 1.00 21.47 ? 77  SER   C C   1 
ATOM   1659 O  O   . SER   B 1 71  ? 36.966 -23.240 22.601 1.00 22.84 ? 77  SER   C O   1 
ATOM   1660 C  CB  . SER   B 1 71  ? 39.884 -22.174 21.103 1.00 21.01 ? 77  SER   C CB  1 
ATOM   1661 O  OG  . SER   B 1 71  ? 38.935 -21.334 20.455 1.00 23.15 ? 77  SER   C OG  1 
ATOM   1662 N  N   . LYS   B 1 72  ? 38.614 -22.430 23.907 1.00 21.30 ? 78  LYS   C N   1 
ATOM   1663 C  CA  . LYS   B 1 72  ? 37.682 -22.029 24.972 1.00 21.65 ? 78  LYS   C CA  1 
ATOM   1664 C  C   . LYS   B 1 72  ? 36.969 -20.702 24.599 1.00 22.18 ? 78  LYS   C C   1 
ATOM   1665 O  O   . LYS   B 1 72  ? 37.524 -19.897 23.844 1.00 22.22 ? 78  LYS   C O   1 
ATOM   1666 C  CB  . LYS   B 1 72  ? 38.446 -21.895 26.295 1.00 24.10 ? 78  LYS   C CB  1 
ATOM   1667 C  CG  . LYS   B 1 72  ? 39.074 -23.205 26.772 1.00 30.83 ? 78  LYS   C CG  1 
ATOM   1668 C  CD  . LYS   B 1 72  ? 39.192 -23.257 28.299 1.00 38.54 ? 78  LYS   C CD  1 
ATOM   1669 C  CE  . LYS   B 1 72  ? 39.651 -24.613 28.803 1.00 44.02 ? 78  LYS   C CE  1 
ATOM   1670 N  NZ  . LYS   B 1 72  ? 39.448 -24.766 30.275 1.00 46.60 ? 78  LYS   C NZ  1 
ATOM   1671 N  N   . PRO   B 1 73  ? 35.742 -20.435 25.110 1.00 22.74 ? 79  PRO   C N   1 
ATOM   1672 C  CA  . PRO   B 1 73  ? 35.045 -19.172 24.726 1.00 22.88 ? 79  PRO   C CA  1 
ATOM   1673 C  C   . PRO   B 1 73  ? 35.909 -17.934 25.039 1.00 22.95 ? 79  PRO   C C   1 
ATOM   1674 O  O   . PRO   B 1 73  ? 36.491 -17.850 26.117 1.00 23.55 ? 79  PRO   C O   1 
ATOM   1675 C  CB  . PRO   B 1 73  ? 33.765 -19.176 25.565 1.00 24.14 ? 79  PRO   C CB  1 
ATOM   1676 C  CG  . PRO   B 1 73  ? 33.576 -20.597 25.988 1.00 24.45 ? 79  PRO   C CG  1 
ATOM   1677 C  CD  . PRO   B 1 73  ? 34.922 -21.287 25.996 1.00 22.48 ? 79  PRO   C CD  1 
ATOM   1678 N  N   . SER   B 1 74  ? 36.082 -17.036 24.059 1.00 22.12 ? 80  SER   C N   1 
ATOM   1679 C  CA  . SER   B 1 74  ? 36.985 -15.881 24.225 1.00 22.40 ? 80  SER   C CA  1 
ATOM   1680 C  C   . SER   B 1 74  ? 36.555 -14.647 23.367 1.00 22.48 ? 80  SER   C C   1 
ATOM   1681 O  O   . SER   B 1 74  ? 35.678 -14.770 22.517 1.00 21.65 ? 80  SER   C O   1 
ATOM   1682 C  CB  . SER   B 1 74  ? 38.397 -16.276 23.800 1.00 25.44 ? 80  SER   C CB  1 
ATOM   1683 O  OG  . SER   B 1 74  ? 38.801 -17.533 24.312 1.00 29.46 ? 80  SER   C OG  1 
ATOM   1684 N  N   . LEU   B 1 75  ? 37.258 -13.490 23.552 1.00 23.37 ? 81  LEU   C N   1 
ATOM   1685 C  CA  . LEU   B 1 75  ? 37.085 -12.257 22.766 1.00 24.74 ? 81  LEU   C CA  1 
ATOM   1686 C  C   . LEU   B 1 75  ? 38.096 -12.363 21.601 1.00 25.72 ? 81  LEU   C C   1 
ATOM   1687 O  O   . LEU   B 1 75  ? 39.308 -12.330 21.835 1.00 26.36 ? 81  LEU   C O   1 
ATOM   1688 C  CB  . LEU   B 1 75  ? 37.451 -11.041 23.648 1.00 26.13 ? 81  LEU   C CB  1 
ATOM   1689 C  CG  . LEU   B 1 75  ? 37.067 -9.643  23.131 1.00 28.21 ? 81  LEU   C CG  1 
ATOM   1690 C  CD1 . LEU   B 1 75  ? 35.591 -9.488  23.011 1.00 28.31 ? 81  LEU   C CD1 1 
ATOM   1691 C  CD2 . LEU   B 1 75  ? 37.607 -8.553  24.077 1.00 29.36 ? 81  LEU   C CD2 1 
ATOM   1692 N  N   . ILE   B 1 76  ? 37.612 -12.573 20.369 1.00 25.34 ? 82  ILE   C N   1 
ATOM   1693 C  CA  . ILE   B 1 76  ? 38.501 -12.777 19.225 1.00 25.61 ? 82  ILE   C CA  1 
ATOM   1694 C  C   . ILE   B 1 76  ? 38.219 -11.732 18.139 1.00 25.53 ? 82  ILE   C C   1 
ATOM   1695 O  O   . ILE   B 1 76  ? 37.060 -11.366 17.947 1.00 24.90 ? 82  ILE   C O   1 
ATOM   1696 C  CB  . ILE   B 1 76  ? 38.292 -14.228 18.674 1.00 26.30 ? 82  ILE   C CB  1 
ATOM   1697 C  CG1 . ILE   B 1 76  ? 38.911 -15.298 19.613 1.00 27.12 ? 82  ILE   C CG1 1 
ATOM   1698 C  CG2 . ILE   B 1 76  ? 38.833 -14.405 17.242 1.00 26.77 ? 82  ILE   C CG2 1 
ATOM   1699 C  CD1 . ILE   B 1 76  ? 38.393 -16.586 19.397 1.00 27.95 ? 82  ILE   C CD1 1 
ATOM   1700 N  N   . PHE   B 1 77  ? 39.278 -11.242 17.449 1.00 26.01 ? 83  PHE   C N   1 
ATOM   1701 C  CA  . PHE   B 1 77  ? 39.063 -10.317 16.343 1.00 27.32 ? 83  PHE   C CA  1 
ATOM   1702 C  C   . PHE   B 1 77  ? 38.641 -11.141 15.106 1.00 27.34 ? 83  PHE   C C   1 
ATOM   1703 O  O   . PHE   B 1 77  ? 39.347 -12.078 14.698 1.00 28.08 ? 83  PHE   C O   1 
ATOM   1704 C  CB  . PHE   B 1 77  ? 40.318 -9.484  16.034 1.00 28.13 ? 83  PHE   C CB  1 
ATOM   1705 C  CG  . PHE   B 1 77  ? 40.027 -8.347  15.077 1.00 29.90 ? 83  PHE   C CG  1 
ATOM   1706 C  CD1 . PHE   B 1 77  ? 39.311 -7.237  15.493 1.00 30.94 ? 83  PHE   C CD1 1 
ATOM   1707 C  CD2 . PHE   B 1 77  ? 40.474 -8.389  13.764 1.00 31.30 ? 83  PHE   C CD2 1 
ATOM   1708 C  CE1 . PHE   B 1 77  ? 39.048 -6.190  14.611 1.00 32.29 ? 83  PHE   C CE1 1 
ATOM   1709 C  CE2 . PHE   B 1 77  ? 40.189 -7.353  12.876 1.00 32.35 ? 83  PHE   C CE2 1 
ATOM   1710 C  CZ  . PHE   B 1 77  ? 39.476 -6.264  13.301 1.00 32.27 ? 83  PHE   C CZ  1 
ATOM   1711 N  N   . VAL   B 1 78  ? 37.509 -10.764 14.500 1.00 26.24 ? 84  VAL   C N   1 
ATOM   1712 C  CA  . VAL   B 1 78  ? 36.950 -11.408 13.320 1.00 25.47 ? 84  VAL   C CA  1 
ATOM   1713 C  C   . VAL   B 1 78  ? 37.027 -10.490 12.072 1.00 25.20 ? 84  VAL   C C   1 
ATOM   1714 O  O   . VAL   B 1 78  ? 36.614 -9.332  12.134 1.00 24.68 ? 84  VAL   C O   1 
ATOM   1715 C  CB  . VAL   B 1 78  ? 35.501 -11.853 13.588 1.00 25.40 ? 84  VAL   C CB  1 
ATOM   1716 C  CG1 . VAL   B 1 78  ? 34.928 -12.593 12.388 1.00 25.70 ? 84  VAL   C CG1 1 
ATOM   1717 C  CG2 . VAL   B 1 78  ? 35.406 -12.716 14.852 1.00 25.19 ? 84  VAL   C CG2 1 
ATOM   1718 N  N   . GLU   B 1 79  ? 37.559 -11.015 10.952 1.00 24.61 ? 85  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 79  ? 37.620 -10.271 9.685  1.00 25.26 ? 85  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 79  ? 36.218 -9.942  9.182  1.00 23.69 ? 85  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 79  ? 35.247 -10.625 9.554  1.00 23.13 ? 85  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 79  ? 38.391 -11.066 8.607  1.00 28.88 ? 85  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 79  ? 39.888 -11.123 8.857  1.00 35.13 ? 85  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 79  ? 40.558 -9.774  9.052  1.00 45.73 ? 85  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 79  ? 40.447 -8.912  8.149  1.00 47.73 ? 85  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 79  ? 41.174 -9.569  10.124 1.00 49.29 ? 85  GLU   C OE2 1 
ATOM   1727 N  N   . ALA   B 1 80  ? 36.100 -8.910  8.337  1.00 23.89 ? 86  ALA   C N   1 
ATOM   1728 C  CA  . ALA   B 1 80  ? 34.810 -8.499  7.773  1.00 24.36 ? 86  ALA   C CA  1 
ATOM   1729 C  C   . ALA   B 1 80  ? 34.158 -9.668  7.002  1.00 24.30 ? 86  ALA   C C   1 
ATOM   1730 O  O   . ALA   B 1 80  ? 34.850 -10.399 6.278  1.00 24.17 ? 86  ALA   C O   1 
ATOM   1731 C  CB  . ALA   B 1 80  ? 34.994 -7.302  6.837  1.00 25.14 ? 86  ALA   C CB  1 
ATOM   1732 N  N   . SER   B 1 81  ? 32.866 -9.901  7.272  1.00 23.53 ? 87  SER   C N   1 
ATOM   1733 C  CA  . SER   B 1 81  ? 32.077 -10.911 6.586  1.00 24.46 ? 87  SER   C CA  1 
ATOM   1734 C  C   . SER   B 1 81  ? 30.976 -10.199 5.759  1.00 25.57 ? 87  SER   C C   1 
ATOM   1735 O  O   . SER   B 1 81  ? 30.872 -8.964  5.813  1.00 25.96 ? 87  SER   C O   1 
ATOM   1736 C  CB  . SER   B 1 81  ? 31.467 -11.884 7.599  1.00 25.44 ? 87  SER   C CB  1 
ATOM   1737 O  OG  . SER   B 1 81  ? 30.433 -11.263 8.344  1.00 26.75 ? 87  SER   C OG  1 
ATOM   1738 N  N   . GLU   B 1 82  ? 30.123 -10.958 5.029  1.00 26.32 ? 88  GLU   C N   1 
ATOM   1739 C  CA  . GLU   B 1 82  ? 29.027 -10.310 4.286  1.00 27.57 ? 88  GLU   C CA  1 
ATOM   1740 C  C   . GLU   B 1 82  ? 27.904 -9.775  5.250  1.00 27.31 ? 88  GLU   C C   1 
ATOM   1741 O  O   . GLU   B 1 82  ? 27.055 -8.983  4.821  1.00 27.68 ? 88  GLU   C O   1 
ATOM   1742 C  CB  . GLU   B 1 82  ? 28.482 -11.208 3.148  1.00 31.21 ? 88  GLU   C CB  1 
ATOM   1743 C  CG  . GLU   B 1 82  ? 27.377 -12.164 3.539  1.00 38.07 ? 88  GLU   C CG  1 
ATOM   1744 C  CD  . GLU   B 1 82  ? 27.058 -13.271 2.545  1.00 45.11 ? 88  GLU   C CD  1 
ATOM   1745 O  OE1 . GLU   B 1 82  ? 27.820 -13.441 1.563  1.00 45.17 ? 88  GLU   C OE1 1 
ATOM   1746 O  OE2 . GLU   B 1 82  ? 26.044 -13.978 2.760  1.00 47.56 ? 88  GLU   C OE2 1 
ATOM   1747 N  N   . TYR   B 1 83  ? 27.943 -10.146 6.554  1.00 25.66 ? 89  TYR   C N   1 
ATOM   1748 C  CA  . TYR   B 1 83  ? 26.911 -9.683  7.499  1.00 24.83 ? 89  TYR   C CA  1 
ATOM   1749 C  C   . TYR   B 1 83  ? 27.453 -8.801  8.686  1.00 24.93 ? 89  TYR   C C   1 
ATOM   1750 O  O   . TYR   B 1 83  ? 26.650 -8.169  9.369  1.00 25.81 ? 89  TYR   C O   1 
ATOM   1751 C  CB  . TYR   B 1 83  ? 26.054 -10.863 8.006  1.00 23.86 ? 89  TYR   C CB  1 
ATOM   1752 C  CG  . TYR   B 1 83  ? 26.869 -12.075 8.409  1.00 23.62 ? 89  TYR   C CG  1 
ATOM   1753 C  CD1 . TYR   B 1 83  ? 27.188 -13.069 7.483  1.00 23.40 ? 89  TYR   C CD1 1 
ATOM   1754 C  CD2 . TYR   B 1 83  ? 27.331 -12.223 9.706  1.00 24.35 ? 89  TYR   C CD2 1 
ATOM   1755 C  CE1 . TYR   B 1 83  ? 27.983 -14.154 7.836  1.00 23.65 ? 89  TYR   C CE1 1 
ATOM   1756 C  CE2 . TYR   B 1 83  ? 28.092 -13.323 10.082 1.00 25.18 ? 89  TYR   C CE2 1 
ATOM   1757 C  CZ  . TYR   B 1 83  ? 28.391 -14.301 9.152  1.00 25.41 ? 89  TYR   C CZ  1 
ATOM   1758 O  OH  . TYR   B 1 83  ? 29.121 -15.383 9.550  1.00 26.59 ? 89  TYR   C OH  1 
ATOM   1759 N  N   . TYR   B 1 84  ? 28.776 -8.741  8.933  1.00 23.85 ? 90  TYR   C N   1 
ATOM   1760 C  CA  . TYR   B 1 84  ? 29.336 -7.845  9.968  1.00 22.87 ? 90  TYR   C CA  1 
ATOM   1761 C  C   . TYR   B 1 84  ? 30.641 -7.212  9.476  1.00 23.81 ? 90  TYR   C C   1 
ATOM   1762 O  O   . TYR   B 1 84  ? 31.420 -7.881  8.763  1.00 24.13 ? 90  TYR   C O   1 
ATOM   1763 C  CB  . TYR   B 1 84  ? 29.638 -8.595  11.286 1.00 21.16 ? 90  TYR   C CB  1 
ATOM   1764 C  CG  . TYR   B 1 84  ? 28.447 -8.971  12.152 1.00 20.93 ? 90  TYR   C CG  1 
ATOM   1765 C  CD1 . TYR   B 1 84  ? 27.634 -7.991  12.736 1.00 21.07 ? 90  TYR   C CD1 1 
ATOM   1766 C  CD2 . TYR   B 1 84  ? 28.233 -10.282 12.529 1.00 21.36 ? 90  TYR   C CD2 1 
ATOM   1767 C  CE1 . TYR   B 1 84  ? 26.579 -8.335  13.605 1.00 21.91 ? 90  TYR   C CE1 1 
ATOM   1768 C  CE2 . TYR   B 1 84  ? 27.160 -10.640 13.347 1.00 21.60 ? 90  TYR   C CE2 1 
ATOM   1769 C  CZ  . TYR   B 1 84  ? 26.373 -9.668  13.955 1.00 22.66 ? 90  TYR   C CZ  1 
ATOM   1770 O  OH  . TYR   B 1 84  ? 25.345 -10.129 14.785 1.00 22.89 ? 90  TYR   C OH  1 
ATOM   1771 N  N   . PRO   B 1 85  ? 30.984 -5.990  9.937  1.00 24.54 ? 91  PRO   C N   1 
ATOM   1772 C  CA  . PRO   B 1 85  ? 32.317 -5.443  9.596  1.00 24.82 ? 91  PRO   C CA  1 
ATOM   1773 C  C   . PRO   B 1 85  ? 33.424 -6.205  10.385 1.00 24.66 ? 91  PRO   C C   1 
ATOM   1774 O  O   . PRO   B 1 85  ? 33.133 -7.079  11.222 1.00 24.42 ? 91  PRO   C O   1 
ATOM   1775 C  CB  . PRO   B 1 85  ? 32.225 -3.986  10.081 1.00 25.97 ? 91  PRO   C CB  1 
ATOM   1776 C  CG  . PRO   B 1 85  ? 31.283 -4.062  11.268 1.00 26.30 ? 91  PRO   C CG  1 
ATOM   1777 C  CD  . PRO   B 1 85  ? 30.236 -5.085  10.849 1.00 24.67 ? 91  PRO   C CD  1 
ATOM   1778 N  N   . ALA   B 1 86  ? 34.687 -5.841  10.159 1.00 24.65 ? 92  ALA   C N   1 
ATOM   1779 C  CA  . ALA   B 1 86  ? 35.805 -6.425  10.915 1.00 25.00 ? 92  ALA   C CA  1 
ATOM   1780 C  C   . ALA   B 1 86  ? 35.686 -5.912  12.377 1.00 25.39 ? 92  ALA   C C   1 
ATOM   1781 O  O   . ALA   B 1 86  ? 35.633 -4.701  12.592 1.00 24.39 ? 92  ALA   C O   1 
ATOM   1782 C  CB  . ALA   B 1 86  ? 37.125 -5.989  10.299 1.00 24.85 ? 92  ALA   C CB  1 
ATOM   1783 N  N   . ARG   B 1 87  ? 35.534 -6.833  13.365 1.00 25.37 ? 93  ARG   C N   1 
ATOM   1784 C  CA  . ARG   B 1 87  ? 35.295 -6.398  14.749 1.00 25.40 ? 93  ARG   C CA  1 
ATOM   1785 C  C   . ARG   B 1 87  ? 35.669 -7.485  15.782 1.00 26.30 ? 93  ARG   C C   1 
ATOM   1786 O  O   . ARG   B 1 87  ? 35.934 -8.638  15.410 1.00 26.80 ? 93  ARG   C O   1 
ATOM   1787 C  CB  . ARG   B 1 87  ? 33.787 -6.046  14.901 1.00 25.11 ? 93  ARG   C CB  1 
ATOM   1788 C  CG  . ARG   B 1 87  ? 32.905 -7.310  14.748 1.00 25.77 ? 93  ARG   C CG  1 
ATOM   1789 C  CD  . ARG   B 1 87  ? 31.409 -7.092  14.882 1.00 26.20 ? 93  ARG   C CD  1 
ATOM   1790 N  NE  . ARG   B 1 87  ? 30.739 -8.374  15.079 1.00 25.87 ? 93  ARG   C NE  1 
ATOM   1791 C  CZ  . ARG   B 1 87  ? 29.666 -8.568  15.837 1.00 27.64 ? 93  ARG   C CZ  1 
ATOM   1792 N  NH1 . ARG   B 1 87  ? 29.087 -7.543  16.458 1.00 27.63 ? 93  ARG   C NH1 1 
ATOM   1793 N  NH2 . ARG   B 1 87  ? 29.169 -9.792  15.993 1.00 27.18 ? 93  ARG   C NH2 1 
ATOM   1794 N  N   . TYR   B 1 88  ? 35.607 -7.143  17.083 1.00 25.11 ? 94  TYR   C N   1 
ATOM   1795 C  CA  . TYR   B 1 88  ? 35.800 -8.136  18.133 1.00 25.29 ? 94  TYR   C CA  1 
ATOM   1796 C  C   . TYR   B 1 88  ? 34.466 -8.801  18.421 1.00 23.60 ? 94  TYR   C C   1 
ATOM   1797 O  O   . TYR   B 1 88  ? 33.467 -8.101  18.635 1.00 22.93 ? 94  TYR   C O   1 
ATOM   1798 C  CB  . TYR   B 1 88  ? 36.240 -7.474  19.445 1.00 26.77 ? 94  TYR   C CB  1 
ATOM   1799 C  CG  . TYR   B 1 88  ? 37.679 -7.051  19.423 1.00 29.29 ? 94  TYR   C CG  1 
ATOM   1800 C  CD1 . TYR   B 1 88  ? 38.698 -7.981  19.595 1.00 30.44 ? 94  TYR   C CD1 1 
ATOM   1801 C  CD2 . TYR   B 1 88  ? 38.032 -5.735  19.159 1.00 31.13 ? 94  TYR   C CD2 1 
ATOM   1802 C  CE1 . TYR   B 1 88  ? 40.030 -7.602  19.543 1.00 32.05 ? 94  TYR   C CE1 1 
ATOM   1803 C  CE2 . TYR   B 1 88  ? 39.360 -5.344  19.110 1.00 32.51 ? 94  TYR   C CE2 1 
ATOM   1804 C  CZ  . TYR   B 1 88  ? 40.358 -6.280  19.305 1.00 33.93 ? 94  TYR   C CZ  1 
ATOM   1805 O  OH  . TYR   B 1 88  ? 41.674 -5.877  19.277 1.00 37.18 ? 94  TYR   C OH  1 
ATOM   1806 N  N   . GLN   B 1 89  ? 34.452 -10.134 18.486 1.00 22.44 ? 95  GLN   C N   1 
ATOM   1807 C  CA  . GLN   B 1 89  ? 33.254 -10.889 18.879 1.00 20.88 ? 95  GLN   C CA  1 
ATOM   1808 C  C   . GLN   B 1 89  ? 33.588 -11.663 20.181 1.00 20.59 ? 95  GLN   C C   1 
ATOM   1809 O  O   . GLN   B 1 89  ? 34.638 -12.322 20.259 1.00 20.60 ? 95  GLN   C O   1 
ATOM   1810 C  CB  . GLN   B 1 89  ? 32.832 -11.849 17.758 1.00 21.56 ? 95  GLN   C CB  1 
ATOM   1811 C  CG  . GLN   B 1 89  ? 31.483 -12.499 17.996 1.00 22.26 ? 95  GLN   C CG  1 
ATOM   1812 C  CD  . GLN   B 1 89  ? 30.877 -13.143 16.763 1.00 22.47 ? 95  GLN   C CD  1 
ATOM   1813 O  OE1 . GLN   B 1 89  ? 30.938 -12.624 15.625 1.00 22.75 ? 95  GLN   C OE1 1 
ATOM   1814 N  NE2 . GLN   B 1 89  ? 30.240 -14.284 16.993 1.00 20.80 ? 95  GLN   C NE2 1 
ATOM   1815 N  N   . SER   B 1 90  ? 32.675 -11.634 21.167 1.00 19.53 ? 96  SER   C N   1 
ATOM   1816 C  CA  . SER   B 1 90  ? 32.895 -12.276 22.467 1.00 19.74 ? 96  SER   C CA  1 
ATOM   1817 C  C   . SER   B 1 90  ? 32.192 -13.672 22.600 1.00 18.86 ? 96  SER   C C   1 
ATOM   1818 O  O   . SER   B 1 90  ? 31.297 -13.957 21.823 1.00 18.76 ? 96  SER   C O   1 
ATOM   1819 C  CB  . SER   B 1 90  ? 32.436 -11.345 23.586 1.00 21.79 ? 96  SER   C CB  1 
ATOM   1820 O  OG  . SER   B 1 90  ? 31.025 -11.216 23.569 1.00 23.33 ? 96  SER   C OG  1 
ATOM   1821 N  N   . HIS   B 1 91  ? 32.676 -14.538 23.522 1.00 18.95 ? 97  HIS   C N   1 
ATOM   1822 C  CA  . HIS   B 1 91  ? 32.170 -15.904 23.748 1.00 20.45 ? 97  HIS   C CA  1 
ATOM   1823 C  C   . HIS   B 1 91  ? 32.258 -16.773 22.465 1.00 19.54 ? 97  HIS   C C   1 
ATOM   1824 O  O   . HIS   B 1 91  ? 31.419 -17.646 22.225 1.00 20.85 ? 97  HIS   C O   1 
ATOM   1825 C  CB  . HIS   B 1 91  ? 30.772 -15.892 24.371 1.00 22.21 ? 97  HIS   C CB  1 
ATOM   1826 C  CG  . HIS   B 1 91  ? 30.692 -15.122 25.668 1.00 25.46 ? 97  HIS   C CG  1 
ATOM   1827 N  ND1 . HIS   B 1 91  ? 30.782 -15.764 26.894 1.00 27.89 ? 97  HIS   C ND1 1 
ATOM   1828 C  CD2 . HIS   B 1 91  ? 30.525 -13.791 25.884 1.00 26.79 ? 97  HIS   C CD2 1 
ATOM   1829 C  CE1 . HIS   B 1 91  ? 30.639 -14.817 27.812 1.00 28.22 ? 97  HIS   C CE1 1 
ATOM   1830 N  NE2 . HIS   B 1 91  ? 30.475 -13.612 27.252 1.00 27.91 ? 97  HIS   C NE2 1 
ATOM   1831 N  N   . LEU   B 1 92  ? 33.316 -16.534 21.667 1.00 18.26 ? 98  LEU   C N   1 
ATOM   1832 C  CA  . LEU   B 1 92  ? 33.610 -17.235 20.412 1.00 18.87 ? 98  LEU   C CA  1 
ATOM   1833 C  C   . LEU   B 1 92  ? 34.680 -18.321 20.642 1.00 19.45 ? 98  LEU   C C   1 
ATOM   1834 O  O   . LEU   B 1 92  ? 35.624 -18.121 21.405 1.00 20.37 ? 98  LEU   C O   1 
ATOM   1835 C  CB  . LEU   B 1 92  ? 34.114 -16.237 19.330 1.00 19.29 ? 98  LEU   C CB  1 
ATOM   1836 C  CG  . LEU   B 1 92  ? 34.137 -16.726 17.874 1.00 21.69 ? 98  LEU   C CG  1 
ATOM   1837 C  CD1 . LEU   B 1 92  ? 32.751 -17.205 17.400 1.00 22.98 ? 98  LEU   C CD1 1 
ATOM   1838 C  CD2 . LEU   B 1 92  ? 34.750 -15.675 16.932 1.00 22.76 ? 98  LEU   C CD2 1 
ATOM   1839 N  N   . MET   B 1 93  ? 34.520 -19.458 19.968 1.00 18.32 ? 99  MET   C N   1 
ATOM   1840 C  CA  . MET   B 1 93  ? 35.436 -20.608 20.024 1.00 17.84 ? 99  MET   C CA  1 
ATOM   1841 C  C   . MET   B 1 93  ? 35.793 -20.952 18.570 1.00 18.90 ? 99  MET   C C   1 
ATOM   1842 O  O   . MET   B 1 93  ? 34.892 -21.054 17.741 1.00 19.35 ? 99  MET   C O   1 
ATOM   1843 C  CB  . MET   B 1 93  ? 34.710 -21.827 20.660 1.00 18.89 ? 99  MET   C CB  1 
ATOM   1844 C  CG  . MET   B 1 93  ? 34.140 -21.538 22.052 1.00 21.67 ? 99  MET   C CG  1 
ATOM   1845 S  SD  . MET   B 1 93  ? 33.109 -22.921 22.671 1.00 24.79 ? 99  MET   C SD  1 
ATOM   1846 C  CE  . MET   B 1 93  ? 31.764 -22.879 21.501 1.00 24.71 ? 99  MET   C CE  1 
ATOM   1847 N  N   . LEU   B 1 94  ? 37.084 -21.189 18.267 1.00 18.26 ? 100 LEU   C N   1 
ATOM   1848 C  CA  . LEU   B 1 94  ? 37.552 -21.487 16.926 1.00 18.90 ? 100 LEU   C CA  1 
ATOM   1849 C  C   . LEU   B 1 94  ? 37.989 -22.956 16.792 1.00 19.22 ? 100 LEU   C C   1 
ATOM   1850 O  O   . LEU   B 1 94  ? 38.471 -23.563 17.749 1.00 19.25 ? 100 LEU   C O   1 
ATOM   1851 C  CB  . LEU   B 1 94  ? 38.793 -20.610 16.584 1.00 19.83 ? 100 LEU   C CB  1 
ATOM   1852 C  CG  . LEU   B 1 94  ? 38.596 -19.105 16.429 1.00 21.24 ? 100 LEU   C CG  1 
ATOM   1853 C  CD1 . LEU   B 1 94  ? 39.905 -18.434 16.001 1.00 22.05 ? 100 LEU   C CD1 1 
ATOM   1854 C  CD2 . LEU   B 1 94  ? 37.508 -18.803 15.391 1.00 22.80 ? 100 LEU   C CD2 1 
ATOM   1855 N  N   . ALA   B 1 95  ? 37.870 -23.472 15.582 1.00 18.97 ? 101 ALA   C N   1 
ATOM   1856 C  CA  . ALA   B 1 95  ? 38.325 -24.813 15.196 1.00 19.75 ? 101 ALA   C CA  1 
ATOM   1857 C  C   . ALA   B 1 95  ? 38.828 -24.743 13.735 1.00 19.45 ? 101 ALA   C C   1 
ATOM   1858 O  O   . ALA   B 1 95  ? 38.454 -23.831 12.990 1.00 20.39 ? 101 ALA   C O   1 
ATOM   1859 C  CB  . ALA   B 1 95  ? 37.162 -25.816 15.303 1.00 19.52 ? 101 ALA   C CB  1 
ATOM   1860 N  N   . VAL   B 1 96  ? 39.654 -25.699 13.321 1.00 19.42 ? 102 VAL   C N   1 
ATOM   1861 C  CA  . VAL   B 1 96  ? 40.114 -25.764 11.941 1.00 21.11 ? 102 VAL   C CA  1 
ATOM   1862 C  C   . VAL   B 1 96  ? 39.026 -26.516 11.172 1.00 22.05 ? 102 VAL   C C   1 
ATOM   1863 O  O   . VAL   B 1 96  ? 38.686 -27.659 11.513 1.00 22.52 ? 102 VAL   C O   1 
ATOM   1864 C  CB  . VAL   B 1 96  ? 41.513 -26.446 11.830 1.00 22.57 ? 102 VAL   C CB  1 
ATOM   1865 C  CG1 . VAL   B 1 96  ? 41.907 -26.653 10.365 1.00 24.08 ? 102 VAL   C CG1 1 
ATOM   1866 C  CG2 . VAL   B 1 96  ? 42.562 -25.601 12.557 1.00 23.16 ? 102 VAL   C CG2 1 
ATOM   1867 N  N   . GLY   B 1 97  ? 38.449 -25.849 10.176 1.00 22.12 ? 103 GLY   C N   1 
ATOM   1868 C  CA  . GLY   B 1 97  ? 37.357 -26.446 9.412  1.00 22.25 ? 103 GLY   C CA  1 
ATOM   1869 C  C   . GLY   B 1 97  ? 36.704 -25.463 8.460  1.00 23.01 ? 103 GLY   C C   1 
ATOM   1870 O  O   . GLY   B 1 97  ? 37.005 -24.262 8.483  1.00 23.65 ? 103 GLY   C O   1 
ATOM   1871 N  N   . HIS   B 1 98  ? 35.864 -25.970 7.566  1.00 22.26 ? 104 HIS   C N   1 
ATOM   1872 C  CA  . HIS   B 1 98  ? 35.212 -25.122 6.572  1.00 22.23 ? 104 HIS   C CA  1 
ATOM   1873 C  C   . HIS   B 1 98  ? 33.985 -24.389 7.150  1.00 22.17 ? 104 HIS   C C   1 
ATOM   1874 O  O   . HIS   B 1 98  ? 33.196 -24.976 7.914  1.00 21.09 ? 104 HIS   C O   1 
ATOM   1875 C  CB  . HIS   B 1 98  ? 34.826 -25.939 5.343  1.00 23.62 ? 104 HIS   C CB  1 
ATOM   1876 C  CG  . HIS   B 1 98  ? 34.238 -25.108 4.251  1.00 27.65 ? 104 HIS   C CG  1 
ATOM   1877 N  ND1 . HIS   B 1 98  ? 34.950 -24.053 3.668  1.00 30.15 ? 104 HIS   C ND1 1 
ATOM   1878 C  CD2 . HIS   B 1 98  ? 33.024 -25.198 3.661  1.00 29.44 ? 104 HIS   C CD2 1 
ATOM   1879 C  CE1 . HIS   B 1 98  ? 34.122 -23.517 2.778  1.00 30.76 ? 104 HIS   C CE1 1 
ATOM   1880 N  NE2 . HIS   B 1 98  ? 32.955 -24.186 2.731  1.00 30.47 ? 104 HIS   C NE2 1 
ATOM   1881 N  N   . SER   B 1 99  ? 33.786 -23.136 6.706  1.00 22.00 ? 105 SER   C N   1 
ATOM   1882 C  CA  . SER   B 1 99  ? 32.629 -22.358 7.135  1.00 22.06 ? 105 SER   C CA  1 
ATOM   1883 C  C   . SER   B 1 99  ? 32.355 -21.201 6.159  1.00 23.01 ? 105 SER   C C   1 
ATOM   1884 O  O   . SER   B 1 99  ? 33.170 -20.295 6.018  1.00 22.95 ? 105 SER   C O   1 
ATOM   1885 C  CB  . SER   B 1 99  ? 32.817 -21.845 8.556  1.00 23.29 ? 105 SER   C CB  1 
ATOM   1886 O  OG  . SER   B 1 99  ? 31.690 -21.101 8.985  1.00 25.55 ? 105 SER   C OG  1 
ATOM   1887 N  N   . GLU   B 1 100 ? 31.205 -21.271 5.479  1.00 23.35 ? 106 GLU   C N   1 
ATOM   1888 C  CA  . GLU   B 1 100 ? 30.686 -20.242 4.570  1.00 24.01 ? 106 GLU   C CA  1 
ATOM   1889 C  C   . GLU   B 1 100 ? 29.544 -19.479 5.304  1.00 23.88 ? 106 GLU   C C   1 
ATOM   1890 O  O   . GLU   B 1 100 ? 28.954 -20.015 6.272  1.00 24.35 ? 106 GLU   C O   1 
ATOM   1891 C  CB  . GLU   B 1 100 ? 30.150 -20.907 3.281  1.00 26.77 ? 106 GLU   C CB  1 
ATOM   1892 C  CG  . GLU   B 1 100 ? 30.919 -20.522 2.026  1.00 34.46 ? 106 GLU   C CG  1 
ATOM   1893 C  CD  . GLU   B 1 100 ? 31.447 -21.708 1.242  1.00 37.12 ? 106 GLU   C CD  1 
ATOM   1894 O  OE1 . GLU   B 1 100 ? 30.808 -22.780 1.282  1.00 36.67 ? 106 GLU   C OE1 1 
ATOM   1895 O  OE2 . GLU   B 1 100 ? 32.510 -21.572 0.601  1.00 38.88 ? 106 GLU   C OE2 1 
ATOM   1896 N  N   . PRO   B 1 101 ? 29.168 -18.261 4.838  1.00 23.39 ? 107 PRO   C N   1 
ATOM   1897 C  CA  . PRO   B 1 101 ? 28.072 -17.523 5.524  1.00 22.45 ? 107 PRO   C CA  1 
ATOM   1898 C  C   . PRO   B 1 101 ? 26.791 -18.356 5.769  1.00 21.72 ? 107 PRO   C C   1 
ATOM   1899 O  O   . PRO   B 1 101 ? 26.200 -18.280 6.845  1.00 22.12 ? 107 PRO   C O   1 
ATOM   1900 C  CB  . PRO   B 1 101 ? 27.786 -16.313 4.591  1.00 23.97 ? 107 PRO   C CB  1 
ATOM   1901 C  CG  . PRO   B 1 101 ? 28.771 -16.384 3.446  1.00 24.49 ? 107 PRO   C CG  1 
ATOM   1902 C  CD  . PRO   B 1 101 ? 29.768 -17.486 3.721  1.00 23.26 ? 107 PRO   C CD  1 
ATOM   1903 N  N   . GLY   B 1 102 ? 26.393 -19.155 4.772  1.00 20.93 ? 108 GLY   C N   1 
ATOM   1904 C  CA  . GLY   B 1 102 ? 25.216 -20.026 4.830  1.00 21.26 ? 108 GLY   C CA  1 
ATOM   1905 C  C   . GLY   B 1 102 ? 25.298 -21.147 5.857  1.00 20.83 ? 108 GLY   C C   1 
ATOM   1906 O  O   . GLY   B 1 102 ? 24.295 -21.802 6.156  1.00 21.44 ? 108 GLY   C O   1 
ATOM   1907 N  N   . ASP   B 1 103 ? 26.492 -21.420 6.367  1.00 20.72 ? 109 ASP   C N   1 
ATOM   1908 C  CA  . ASP   B 1 103 ? 26.753 -22.423 7.433  1.00 20.36 ? 109 ASP   C CA  1 
ATOM   1909 C  C   . ASP   B 1 103 ? 26.382 -21.949 8.841  1.00 20.26 ? 109 ASP   C C   1 
ATOM   1910 O  O   . ASP   B 1 103 ? 26.247 -22.778 9.783  1.00 20.28 ? 109 ASP   C O   1 
ATOM   1911 C  CB  . ASP   B 1 103 ? 28.203 -22.893 7.422  1.00 21.08 ? 109 ASP   C CB  1 
ATOM   1912 C  CG  . ASP   B 1 103 ? 28.524 -23.731 6.207  1.00 23.32 ? 109 ASP   C CG  1 
ATOM   1913 O  OD1 . ASP   B 1 103 ? 27.642 -24.462 5.750  1.00 22.70 ? 109 ASP   C OD1 1 
ATOM   1914 O  OD2 . ASP   B 1 103 ? 29.660 -23.644 5.705  1.00 25.48 ? 109 ASP   C OD2 1 
ATOM   1915 N  N   . CYS   B 1 104 ? 26.174 -20.605 9.002  1.00 18.94 ? 110 CYS   C N   1 
ATOM   1916 C  CA  . CYS   B 1 104 ? 25.757 -20.023 10.287 1.00 18.83 ? 110 CYS   C CA  1 
ATOM   1917 C  C   . CYS   B 1 104 ? 24.517 -20.733 10.820 1.00 17.95 ? 110 CYS   C C   1 
ATOM   1918 O  O   . CYS   B 1 104 ? 23.628 -21.020 10.027 1.00 18.76 ? 110 CYS   C O   1 
ATOM   1919 C  CB  . CYS   B 1 104 ? 25.510 -18.532 10.126 1.00 19.86 ? 110 CYS   C CB  1 
ATOM   1920 S  SG  . CYS   B 1 104 ? 27.015 -17.549 10.179 1.00 22.73 ? 110 CYS   C SG  1 
ATOM   1921 N  N   . GLY   B 1 105 ? 24.508 -21.076 12.092 1.00 16.33 ? 111 GLY   C N   1 
ATOM   1922 C  CA  . GLY   B 1 105 ? 23.367 -21.768 12.685 1.00 17.08 ? 111 GLY   C CA  1 
ATOM   1923 C  C   . GLY   B 1 105 ? 23.537 -23.280 12.833 1.00 17.99 ? 111 GLY   C C   1 
ATOM   1924 O  O   . GLY   B 1 105 ? 22.762 -23.915 13.549 1.00 18.94 ? 111 GLY   C O   1 
ATOM   1925 N  N   . GLY   B 1 106 ? 24.529 -23.872 12.152 1.00 17.92 ? 112 GLY   C N   1 
ATOM   1926 C  CA  . GLY   B 1 106 ? 24.846 -25.304 12.274 1.00 18.74 ? 112 GLY   C CA  1 
ATOM   1927 C  C   . GLY   B 1 106 ? 25.223 -25.635 13.718 1.00 17.72 ? 112 GLY   C C   1 
ATOM   1928 O  O   . GLY   B 1 106 ? 25.921 -24.834 14.369 1.00 17.62 ? 112 GLY   C O   1 
ATOM   1929 N  N   . ILE   B 1 107 ? 24.684 -26.735 14.270 1.00 17.74 ? 113 ILE   C N   1 
ATOM   1930 C  CA  . ILE   B 1 107 ? 24.946 -27.071 15.669 1.00 18.20 ? 113 ILE   C CA  1 
ATOM   1931 C  C   . ILE   B 1 107 ? 26.319 -27.737 15.895 1.00 19.66 ? 113 ILE   C C   1 
ATOM   1932 O  O   . ILE   B 1 107 ? 26.749 -28.616 15.137 1.00 19.58 ? 113 ILE   C O   1 
ATOM   1933 C  CB  . ILE   B 1 107 ? 23.761 -27.936 16.268 1.00 20.63 ? 113 ILE   C CB  1 
ATOM   1934 C  CG1 . ILE   B 1 107 ? 22.530 -27.024 16.611 1.00 23.13 ? 113 ILE   C CG1 1 
ATOM   1935 C  CG2 . ILE   B 1 107 ? 24.205 -28.760 17.500 1.00 21.84 ? 113 ILE   C CG2 1 
ATOM   1936 C  CD1 . ILE   B 1 107 ? 21.263 -27.763 17.155 1.00 25.34 ? 113 ILE   C CD1 1 
ATOM   1937 N  N   . LEU   B 1 108 ? 26.980 -27.346 17.008 1.00 18.98 ? 114 LEU   C N   1 
ATOM   1938 C  CA  . LEU   B 1 108 ? 28.193 -27.998 17.484 1.00 18.11 ? 114 LEU   C CA  1 
ATOM   1939 C  C   . LEU   B 1 108 ? 27.726 -28.756 18.760 1.00 18.74 ? 114 LEU   C C   1 
ATOM   1940 O  O   . LEU   B 1 108 ? 27.070 -28.143 19.620 1.00 18.05 ? 114 LEU   C O   1 
ATOM   1941 C  CB  . LEU   B 1 108 ? 29.281 -26.948 17.839 1.00 17.83 ? 114 LEU   C CB  1 
ATOM   1942 C  CG  . LEU   B 1 108 ? 30.435 -27.482 18.706 1.00 18.72 ? 114 LEU   C CG  1 
ATOM   1943 C  CD1 . LEU   B 1 108 ? 31.400 -28.360 17.892 1.00 18.59 ? 114 LEU   C CD1 1 
ATOM   1944 C  CD2 . LEU   B 1 108 ? 31.229 -26.338 19.328 1.00 19.83 ? 114 LEU   C CD2 1 
ATOM   1945 N  N   . ARG   B 1 109 ? 28.078 -30.056 18.885 1.00 19.33 ? 115 ARG   C N   1 
ATOM   1946 C  CA  . ARG   B 1 109 ? 27.646 -30.820 20.046 1.00 20.59 ? 115 ARG   C CA  1 
ATOM   1947 C  C   . ARG   B 1 109 ? 28.746 -31.746 20.583 1.00 20.66 ? 115 ARG   C C   1 
ATOM   1948 O  O   . ARG   B 1 109 ? 29.623 -32.188 19.826 1.00 20.22 ? 115 ARG   C O   1 
ATOM   1949 C  CB  . ARG   B 1 109 ? 26.376 -31.628 19.719 1.00 23.33 ? 115 ARG   C CB  1 
ATOM   1950 C  CG  . ARG   B 1 109 ? 26.651 -32.784 18.753 1.00 29.58 ? 115 ARG   C CG  1 
ATOM   1951 C  CD  . ARG   B 1 109 ? 25.386 -33.553 18.371 1.00 37.34 ? 115 ARG   C CD  1 
ATOM   1952 N  NE  . ARG   B 1 109 ? 24.534 -32.791 17.451 1.00 43.79 ? 115 ARG   C NE  1 
ATOM   1953 C  CZ  . ARG   B 1 109 ? 23.269 -32.447 17.703 1.00 49.51 ? 115 ARG   C CZ  1 
ATOM   1954 N  NH1 . ARG   B 1 109 ? 22.687 -32.810 18.845 1.00 50.23 ? 115 ARG   C NH1 1 
ATOM   1955 N  NH2 . ARG   B 1 109 ? 22.576 -31.743 16.815 1.00 50.02 ? 115 ARG   C NH2 1 
ATOM   1956 N  N   . CYS   B 1 110 ? 28.664 -32.055 21.877 1.00 20.43 ? 116 CYS   C N   1 
ATOM   1957 C  CA  . CYS   B 1 110 ? 29.599 -32.968 22.574 1.00 20.07 ? 116 CYS   C CA  1 
ATOM   1958 C  C   . CYS   B 1 110 ? 28.714 -34.072 23.247 1.00 21.86 ? 116 CYS   C C   1 
ATOM   1959 O  O   . CYS   B 1 110 ? 27.496 -34.136 22.983 1.00 23.54 ? 116 CYS   C O   1 
ATOM   1960 C  CB  . CYS   B 1 110 ? 30.373 -32.173 23.621 1.00 20.85 ? 116 CYS   C CB  1 
ATOM   1961 S  SG  . CYS   B 1 110 ? 29.291 -31.490 24.888 1.00 21.58 ? 116 CYS   C SG  1 
ATOM   1962 N  N   . GLN   B 1 111 ? 29.294 -34.911 24.136 1.00 22.14 ? 117 GLN   C N   1 
ATOM   1963 C  CA  . GLN   B 1 111 ? 28.505 -35.953 24.835 1.00 23.41 ? 117 GLN   C CA  1 
ATOM   1964 C  C   . GLN   B 1 111 ? 27.414 -35.367 25.769 1.00 23.53 ? 117 GLN   C C   1 
ATOM   1965 O  O   . GLN   B 1 111 ? 26.451 -36.074 26.101 1.00 24.57 ? 117 GLN   C O   1 
ATOM   1966 C  CB  . GLN   B 1 111 ? 29.430 -36.890 25.649 1.00 26.89 ? 117 GLN   C CB  1 
ATOM   1967 C  CG  . GLN   B 1 111 ? 30.200 -36.159 26.743 1.00 32.16 ? 117 GLN   C CG  1 
ATOM   1968 C  CD  . GLN   B 1 111 ? 31.090 -37.064 27.566 1.00 41.15 ? 117 GLN   C CD  1 
ATOM   1969 O  OE1 . GLN   B 1 111 ? 32.323 -37.043 27.432 1.00 44.21 ? 117 GLN   C OE1 1 
ATOM   1970 N  NE2 . GLN   B 1 111 ? 30.484 -37.857 28.457 1.00 41.64 ? 117 GLN   C NE2 1 
ATOM   1971 N  N   . HIS   B 1 112 ? 27.574 -34.101 26.236 1.00 21.65 ? 118 HIS   C N   1 
ATOM   1972 C  CA  . HIS   B 1 112 ? 26.599 -33.508 27.164 1.00 22.30 ? 118 HIS   C CA  1 
ATOM   1973 C  C   . HIS   B 1 112 ? 25.431 -32.781 26.480 1.00 22.99 ? 118 HIS   C C   1 
ATOM   1974 O  O   . HIS   B 1 112 ? 24.437 -32.493 27.145 1.00 24.67 ? 118 HIS   C O   1 
ATOM   1975 C  CB  . HIS   B 1 112 ? 27.284 -32.588 28.198 1.00 22.99 ? 118 HIS   C CB  1 
ATOM   1976 C  CG  . HIS   B 1 112 ? 28.473 -33.223 28.872 1.00 24.03 ? 118 HIS   C CG  1 
ATOM   1977 N  ND1 . HIS   B 1 112 ? 29.755 -33.022 28.398 1.00 24.96 ? 118 HIS   C ND1 1 
ATOM   1978 C  CD2 . HIS   B 1 112 ? 28.529 -34.068 29.929 1.00 25.12 ? 118 HIS   C CD2 1 
ATOM   1979 C  CE1 . HIS   B 1 112 ? 30.557 -33.717 29.184 1.00 25.89 ? 118 HIS   C CE1 1 
ATOM   1980 N  NE2 . HIS   B 1 112 ? 29.867 -34.376 30.122 1.00 26.14 ? 118 HIS   C NE2 1 
ATOM   1981 N  N   . GLY   B 1 113 ? 25.520 -32.538 25.172 1.00 21.78 ? 119 GLY   C N   1 
ATOM   1982 C  CA  . GLY   B 1 113 ? 24.455 -31.852 24.454 1.00 21.61 ? 119 GLY   C CA  1 
ATOM   1983 C  C   . GLY   B 1 113 ? 24.948 -30.767 23.512 1.00 20.45 ? 119 GLY   C C   1 
ATOM   1984 O  O   . GLY   B 1 113 ? 26.069 -30.837 23.022 1.00 19.37 ? 119 GLY   C O   1 
ATOM   1985 N  N   . VAL   B 1 114 ? 24.098 -29.759 23.240 1.00 19.33 ? 120 VAL   C N   1 
ATOM   1986 C  CA  . VAL   B 1 114 ? 24.452 -28.667 22.342 1.00 19.45 ? 120 VAL   C CA  1 
ATOM   1987 C  C   . VAL   B 1 114 ? 25.422 -27.669 23.007 1.00 19.43 ? 120 VAL   C C   1 
ATOM   1988 O  O   . VAL   B 1 114 ? 25.121 -27.134 24.074 1.00 20.00 ? 120 VAL   C O   1 
ATOM   1989 C  CB  . VAL   B 1 114 ? 23.173 -27.935 21.837 1.00 20.55 ? 120 VAL   C CB  1 
ATOM   1990 C  CG1 . VAL   B 1 114 ? 23.548 -26.771 20.924 1.00 20.76 ? 120 VAL   C CG1 1 
ATOM   1991 C  CG2 . VAL   B 1 114 ? 22.203 -28.913 21.149 1.00 21.05 ? 120 VAL   C CG2 1 
ATOM   1992 N  N   . VAL   B 1 115 ? 26.571 -27.427 22.368 1.00 19.24 ? 121 VAL   C N   1 
ATOM   1993 C  CA  . VAL   B 1 115 ? 27.631 -26.508 22.828 1.00 20.49 ? 121 VAL   C CA  1 
ATOM   1994 C  C   . VAL   B 1 115 ? 27.458 -25.049 22.303 1.00 20.16 ? 121 VAL   C C   1 
ATOM   1995 O  O   . VAL   B 1 115 ? 27.757 -24.049 23.012 1.00 20.58 ? 121 VAL   C O   1 
ATOM   1996 C  CB  . VAL   B 1 115 ? 29.001 -27.077 22.402 1.00 21.02 ? 121 VAL   C CB  1 
ATOM   1997 C  CG1 . VAL   B 1 115 ? 30.127 -26.056 22.644 1.00 20.49 ? 121 VAL   C CG1 1 
ATOM   1998 C  CG2 . VAL   B 1 115 ? 29.290 -28.422 23.084 1.00 21.84 ? 121 VAL   C CG2 1 
ATOM   1999 N  N   . GLY   B 1 116 ? 27.074 -24.961 21.037 1.00 18.74 ? 122 GLY   C N   1 
ATOM   2000 C  CA  . GLY   B 1 116 ? 26.890 -23.684 20.366 1.00 19.67 ? 122 GLY   C CA  1 
ATOM   2001 C  C   . GLY   B 1 116 ? 26.413 -23.820 18.929 1.00 19.14 ? 122 GLY   C C   1 
ATOM   2002 O  O   . GLY   B 1 116 ? 25.921 -24.884 18.527 1.00 18.56 ? 122 GLY   C O   1 
ATOM   2003 N  N   . ILE   B 1 117 ? 26.562 -22.727 18.144 1.00 17.89 ? 123 ILE   C N   1 
ATOM   2004 C  CA  . ILE   B 1 117 ? 26.127 -22.712 16.739 1.00 16.48 ? 123 ILE   C CA  1 
ATOM   2005 C  C   . ILE   B 1 117 ? 27.175 -21.914 15.924 1.00 16.95 ? 123 ILE   C C   1 
ATOM   2006 O  O   . ILE   B 1 117 ? 27.709 -20.904 16.418 1.00 17.24 ? 123 ILE   C O   1 
ATOM   2007 C  CB  . ILE   B 1 117 ? 24.693 -22.057 16.526 1.00 17.85 ? 123 ILE   C CB  1 
ATOM   2008 C  CG1 . ILE   B 1 117 ? 24.594 -20.690 17.232 1.00 19.10 ? 123 ILE   C CG1 1 
ATOM   2009 C  CG2 . ILE   B 1 117 ? 23.510 -22.985 16.944 1.00 18.23 ? 123 ILE   C CG2 1 
ATOM   2010 C  CD1 . ILE   B 1 117 ? 23.294 -19.865 16.827 1.00 19.78 ? 123 ILE   C CD1 1 
ATOM   2011 N  N   . VAL   B 1 118 ? 27.428 -22.332 14.662 1.00 16.67 ? 124 VAL   C N   1 
ATOM   2012 C  CA  . VAL   B 1 118 ? 28.359 -21.643 13.738 1.00 17.61 ? 124 VAL   C CA  1 
ATOM   2013 C  C   . VAL   B 1 118 ? 28.001 -20.153 13.624 1.00 18.54 ? 124 VAL   C C   1 
ATOM   2014 O  O   . VAL   B 1 118 ? 26.822 -19.826 13.512 1.00 19.31 ? 124 VAL   C O   1 
ATOM   2015 C  CB  . VAL   B 1 118 ? 28.387 -22.317 12.323 1.00 17.98 ? 124 VAL   C CB  1 
ATOM   2016 C  CG1 . VAL   B 1 118 ? 29.164 -21.464 11.307 1.00 17.81 ? 124 VAL   C CG1 1 
ATOM   2017 C  CG2 . VAL   B 1 118 ? 28.990 -23.717 12.414 1.00 18.52 ? 124 VAL   C CG2 1 
ATOM   2018 N  N   . SER   B 1 119 ? 29.010 -19.257 13.688 1.00 18.71 ? 125 SER   C N   1 
ATOM   2019 C  CA  . SER   B 1 119 ? 28.820 -17.800 13.647 1.00 19.61 ? 125 SER   C CA  1 
ATOM   2020 C  C   . SER   B 1 119 ? 29.851 -17.099 12.752 1.00 19.03 ? 125 SER   C C   1 
ATOM   2021 O  O   . SER   B 1 119 ? 29.567 -16.026 12.237 1.00 20.00 ? 125 SER   C O   1 
ATOM   2022 C  CB  . SER   B 1 119 ? 28.894 -17.203 15.060 1.00 21.74 ? 125 SER   C CB  1 
ATOM   2023 O  OG  . SER   B 1 119 ? 28.797 -15.782 15.070 1.00 23.98 ? 125 SER   C OG  1 
ATOM   2024 N  N   . THR   B 1 120 ? 31.057 -17.691 12.580 1.00 18.15 ? 126 THR   C N   1 
ATOM   2025 C  CA  . THR   B 1 120 ? 32.101 -17.052 11.777 1.00 17.89 ? 126 THR   C CA  1 
ATOM   2026 C  C   . THR   B 1 120 ? 32.824 -18.101 10.862 1.00 20.19 ? 126 THR   C C   1 
ATOM   2027 O  O   . THR   B 1 120 ? 32.790 -19.312 11.108 1.00 19.54 ? 126 THR   C O   1 
ATOM   2028 C  CB  . THR   B 1 120 ? 33.170 -16.333 12.697 1.00 16.96 ? 126 THR   C CB  1 
ATOM   2029 O  OG1 . THR   B 1 120 ? 34.071 -17.303 13.283 1.00 17.79 ? 126 THR   C OG1 1 
ATOM   2030 C  CG2 . THR   B 1 120 ? 32.570 -15.417 13.762 1.00 16.93 ? 126 THR   C CG2 1 
ATOM   2031 N  N   . GLY   B 1 121 ? 33.500 -17.588 9.848  1.00 21.98 ? 127 GLY   C N   1 
ATOM   2032 C  CA  . GLY   B 1 121 ? 34.243 -18.412 8.902  1.00 24.32 ? 127 GLY   C CA  1 
ATOM   2033 C  C   . GLY   B 1 121 ? 35.232 -17.585 8.104  1.00 27.06 ? 127 GLY   C C   1 
ATOM   2034 O  O   . GLY   B 1 121 ? 35.025 -16.384 7.902  1.00 27.32 ? 127 GLY   C O   1 
ATOM   2035 N  N   . GLY   B 1 122 ? 36.258 -18.252 7.584  1.00 28.58 ? 128 GLY   C N   1 
ATOM   2036 C  CA  . GLY   B 1 122 ? 37.318 -17.628 6.799  1.00 29.91 ? 128 GLY   C CA  1 
ATOM   2037 C  C   . GLY   B 1 122 ? 38.702 -18.062 7.262  1.00 30.29 ? 128 GLY   C C   1 
ATOM   2038 O  O   . GLY   B 1 122 ? 38.860 -18.485 8.410  1.00 29.93 ? 128 GLY   C O   1 
ATOM   2039 N  N   . ASN   B 1 123 ? 39.718 -17.958 6.377  1.00 30.36 ? 129 ASN   C N   1 
ATOM   2040 C  CA  . ASN   B 1 123 ? 41.114 -18.344 6.662  1.00 31.08 ? 129 ASN   C CA  1 
ATOM   2041 C  C   . ASN   B 1 123 ? 41.299 -19.791 7.098  1.00 30.42 ? 129 ASN   C C   1 
ATOM   2042 O  O   . ASN   B 1 123 ? 42.324 -20.117 7.713  1.00 31.35 ? 129 ASN   C O   1 
ATOM   2043 C  CB  . ASN   B 1 123 ? 41.790 -17.403 7.685  1.00 33.64 ? 129 ASN   C CB  1 
ATOM   2044 C  CG  . ASN   B 1 123 ? 42.652 -16.346 7.041  1.00 39.37 ? 129 ASN   C CG  1 
ATOM   2045 O  OD1 . ASN   B 1 123 ? 42.839 -16.314 5.818  1.00 41.08 ? 129 ASN   C OD1 1 
ATOM   2046 N  ND2 . ASN   B 1 123 ? 43.176 -15.429 7.844  1.00 40.77 ? 129 ASN   C ND2 1 
ATOM   2047 N  N   . GLY   B 1 124 ? 40.350 -20.656 6.738  1.00 29.17 ? 130 GLY   C N   1 
ATOM   2048 C  CA  . GLY   B 1 124 ? 40.423 -22.068 7.094  1.00 28.59 ? 130 GLY   C CA  1 
ATOM   2049 C  C   . GLY   B 1 124 ? 40.013 -22.372 8.524  1.00 27.36 ? 130 GLY   C C   1 
ATOM   2050 O  O   . GLY   B 1 124 ? 40.347 -23.436 9.047  1.00 27.33 ? 130 GLY   C O   1 
ATOM   2051 N  N   . LEU   B 1 125 ? 39.296 -21.428 9.182  1.00 25.85 ? 131 LEU   C N   1 
ATOM   2052 C  CA  . LEU   B 1 125 ? 38.818 -21.616 10.549 1.00 25.75 ? 131 LEU   C CA  1 
ATOM   2053 C  C   . LEU   B 1 125 ? 37.298 -21.428 10.598 1.00 24.36 ? 131 LEU   C C   1 
ATOM   2054 O  O   . LEU   B 1 125 ? 36.736 -20.648 9.805  1.00 25.49 ? 131 LEU   C O   1 
ATOM   2055 C  CB  . LEU   B 1 125 ? 39.481 -20.604 11.506 1.00 27.04 ? 131 LEU   C CB  1 
ATOM   2056 C  CG  . LEU   B 1 125 ? 41.007 -20.542 11.452 1.00 29.60 ? 131 LEU   C CG  1 
ATOM   2057 C  CD1 . LEU   B 1 125 ? 41.526 -19.261 12.026 1.00 30.82 ? 131 LEU   C CD1 1 
ATOM   2058 C  CD2 . LEU   B 1 125 ? 41.627 -21.757 12.111 1.00 30.28 ? 131 LEU   C CD2 1 
ATOM   2059 N  N   . VAL   B 1 126 ? 36.628 -22.132 11.520 1.00 20.99 ? 132 VAL   C N   1 
ATOM   2060 C  CA  . VAL   B 1 126 ? 35.195 -21.989 11.777 1.00 20.00 ? 132 VAL   C CA  1 
ATOM   2061 C  C   . VAL   B 1 126 ? 35.040 -21.493 13.246 1.00 19.33 ? 132 VAL   C C   1 
ATOM   2062 O  O   . VAL   B 1 126 ? 35.697 -22.008 14.152 1.00 18.37 ? 132 VAL   C O   1 
ATOM   2063 C  CB  . VAL   B 1 126 ? 34.449 -23.335 11.576 1.00 19.46 ? 132 VAL   C CB  1 
ATOM   2064 C  CG1 . VAL   B 1 126 ? 35.100 -24.444 12.403 1.00 20.03 ? 132 VAL   C CG1 1 
ATOM   2065 C  CG2 . VAL   B 1 126 ? 32.966 -23.211 11.921 1.00 19.60 ? 132 VAL   C CG2 1 
ATOM   2066 N  N   . GLY   B 1 127 ? 34.147 -20.522 13.469 1.00 20.17 ? 133 GLY   C N   1 
ATOM   2067 C  CA  . GLY   B 1 127 ? 33.884 -19.970 14.790 1.00 20.44 ? 133 GLY   C CA  1 
ATOM   2068 C  C   . GLY   B 1 127 ? 32.467 -20.276 15.265 1.00 20.71 ? 133 GLY   C C   1 
ATOM   2069 O  O   . GLY   B 1 127 ? 31.514 -20.175 14.485 1.00 20.61 ? 133 GLY   C O   1 
ATOM   2070 N  N   . PHE   B 1 128 ? 32.336 -20.667 16.548 1.00 18.68 ? 134 PHE   C N   1 
ATOM   2071 C  CA  . PHE   B 1 128 ? 31.063 -21.050 17.181 1.00 19.18 ? 134 PHE   C CA  1 
ATOM   2072 C  C   . PHE   B 1 128 ? 30.683 -20.114 18.344 1.00 19.21 ? 134 PHE   C C   1 
ATOM   2073 O  O   . PHE   B 1 128 ? 31.493 -19.896 19.259 1.00 20.06 ? 134 PHE   C O   1 
ATOM   2074 C  CB  . PHE   B 1 128 ? 31.138 -22.510 17.715 1.00 18.11 ? 134 PHE   C CB  1 
ATOM   2075 C  CG  . PHE   B 1 128 ? 31.649 -23.533 16.700 1.00 17.89 ? 134 PHE   C CG  1 
ATOM   2076 C  CD1 . PHE   B 1 128 ? 30.781 -24.140 15.804 1.00 18.89 ? 134 PHE   C CD1 1 
ATOM   2077 C  CD2 . PHE   B 1 128 ? 32.969 -23.969 16.734 1.00 19.47 ? 134 PHE   C CD2 1 
ATOM   2078 C  CE1 . PHE   B 1 128 ? 31.247 -25.078 14.883 1.00 19.72 ? 134 PHE   C CE1 1 
ATOM   2079 C  CE2 . PHE   B 1 128 ? 33.429 -24.942 15.842 1.00 20.24 ? 134 PHE   C CE2 1 
ATOM   2080 C  CZ  . PHE   B 1 128 ? 32.570 -25.468 14.898 1.00 20.21 ? 134 PHE   C CZ  1 
ATOM   2081 N  N   . ALA   B 1 129 ? 29.439 -19.635 18.357 1.00 18.88 ? 135 ALA   C N   1 
ATOM   2082 C  CA  . ALA   B 1 129 ? 28.965 -18.816 19.478 1.00 18.68 ? 135 ALA   C CA  1 
ATOM   2083 C  C   . ALA   B 1 129 ? 28.587 -19.775 20.611 1.00 18.08 ? 135 ALA   C C   1 
ATOM   2084 O  O   . ALA   B 1 129 ? 27.686 -20.610 20.451 1.00 16.60 ? 135 ALA   C O   1 
ATOM   2085 C  CB  . ALA   B 1 129 ? 27.758 -17.980 19.060 1.00 18.51 ? 135 ALA   C CB  1 
ATOM   2086 N  N   . ASP   B 1 130 ? 29.318 -19.699 21.725 1.00 19.15 ? 136 ASP   C N   1 
ATOM   2087 C  CA  . ASP   B 1 130 ? 29.060 -20.584 22.883 1.00 20.25 ? 136 ASP   C CA  1 
ATOM   2088 C  C   . ASP   B 1 130 ? 27.708 -20.243 23.540 1.00 20.49 ? 136 ASP   C C   1 
ATOM   2089 O  O   . ASP   B 1 130 ? 27.325 -19.063 23.563 1.00 20.77 ? 136 ASP   C O   1 
ATOM   2090 C  CB  . ASP   B 1 130 ? 30.195 -20.429 23.916 1.00 23.10 ? 136 ASP   C CB  1 
ATOM   2091 C  CG  . ASP   B 1 130 ? 30.053 -21.342 25.127 1.00 27.01 ? 136 ASP   C CG  1 
ATOM   2092 O  OD1 . ASP   B 1 130 ? 29.912 -22.572 24.938 1.00 27.39 ? 136 ASP   C OD1 1 
ATOM   2093 O  OD2 . ASP   B 1 130 ? 30.039 -20.819 26.258 1.00 29.35 ? 136 ASP   C OD2 1 
ATOM   2094 N  N   . VAL   B 1 131 ? 26.970 -21.265 24.052 1.00 19.48 ? 137 VAL   C N   1 
ATOM   2095 C  CA  . VAL   B 1 131 ? 25.714 -21.060 24.790 1.00 19.31 ? 137 VAL   C CA  1 
ATOM   2096 C  C   . VAL   B 1 131 ? 25.740 -21.729 26.204 1.00 19.33 ? 137 VAL   C C   1 
ATOM   2097 O  O   . VAL   B 1 131 ? 24.789 -21.588 26.982 1.00 20.44 ? 137 VAL   C O   1 
ATOM   2098 C  CB  . VAL   B 1 131 ? 24.439 -21.477 23.992 1.00 20.81 ? 137 VAL   C CB  1 
ATOM   2099 C  CG1 . VAL   B 1 131 ? 24.314 -20.690 22.683 1.00 21.20 ? 137 VAL   C CG1 1 
ATOM   2100 C  CG2 . VAL   B 1 131 ? 24.416 -22.974 23.727 1.00 21.67 ? 137 VAL   C CG2 1 
ATOM   2101 N  N   . ARG   B 1 132 ? 26.804 -22.486 26.530 1.00 18.36 ? 138 ARG   C N   1 
ATOM   2102 C  CA  . ARG   B 1 132 ? 26.897 -23.241 27.796 1.00 18.11 ? 138 ARG   C CA  1 
ATOM   2103 C  C   . ARG   B 1 132 ? 26.884 -22.395 29.100 1.00 20.62 ? 138 ARG   C C   1 
ATOM   2104 O  O   . ARG   B 1 132 ? 26.569 -22.925 30.173 1.00 22.32 ? 138 ARG   C O   1 
ATOM   2105 C  CB  . ARG   B 1 132 ? 28.130 -24.153 27.790 1.00 16.61 ? 138 ARG   C CB  1 
ATOM   2106 C  CG  . ARG   B 1 132 ? 28.133 -25.141 26.637 1.00 15.60 ? 138 ARG   C CG  1 
ATOM   2107 C  CD  . ARG   B 1 132 ? 29.412 -25.948 26.704 1.00 16.10 ? 138 ARG   C CD  1 
ATOM   2108 N  NE  . ARG   B 1 132 ? 30.535 -25.108 26.255 1.00 16.77 ? 138 ARG   C NE  1 
ATOM   2109 C  CZ  . ARG   B 1 132 ? 31.765 -25.567 26.071 1.00 19.93 ? 138 ARG   C CZ  1 
ATOM   2110 N  NH1 . ARG   B 1 132 ? 32.085 -26.798 26.460 1.00 19.43 ? 138 ARG   C NH1 1 
ATOM   2111 N  NH2 . ARG   B 1 132 ? 32.721 -24.758 25.629 1.00 20.05 ? 138 ARG   C NH2 1 
ATOM   2112 N  N   . ASP   B 1 133 ? 27.231 -21.097 29.005 1.00 20.60 ? 139 ASP   C N   1 
ATOM   2113 C  CA  . ASP   B 1 133 ? 27.220 -20.222 30.170 1.00 20.29 ? 139 ASP   C CA  1 
ATOM   2114 C  C   . ASP   B 1 133 ? 25.795 -19.641 30.452 1.00 21.32 ? 139 ASP   C C   1 
ATOM   2115 O  O   . ASP   B 1 133 ? 25.585 -19.039 31.508 1.00 22.35 ? 139 ASP   C O   1 
ATOM   2116 C  CB  . ASP   B 1 133 ? 28.239 -19.065 29.977 1.00 21.89 ? 139 ASP   C CB  1 
ATOM   2117 C  CG  . ASP   B 1 133 ? 27.837 -18.103 28.861 1.00 25.38 ? 139 ASP   C CG  1 
ATOM   2118 O  OD1 . ASP   B 1 133 ? 27.504 -18.590 27.742 1.00 24.33 ? 139 ASP   C OD1 1 
ATOM   2119 O  OD2 . ASP   B 1 133 ? 27.841 -16.863 29.104 1.00 27.27 ? 139 ASP   C OD2 1 
ATOM   2120 N  N   . LEU   B 1 134 ? 24.832 -19.805 29.499 1.00 21.01 ? 140 LEU   C N   1 
ATOM   2121 C  CA  . LEU   B 1 134 ? 23.474 -19.264 29.619 1.00 21.10 ? 140 LEU   C CA  1 
ATOM   2122 C  C   . LEU   B 1 134 ? 22.606 -20.248 30.392 1.00 21.11 ? 140 LEU   C C   1 
ATOM   2123 O  O   . LEU   B 1 134 ? 21.766 -20.938 29.803 1.00 20.75 ? 140 LEU   C O   1 
ATOM   2124 C  CB  . LEU   B 1 134 ? 22.897 -18.995 28.208 1.00 20.79 ? 140 LEU   C CB  1 
ATOM   2125 C  CG  . LEU   B 1 134 ? 23.699 -18.000 27.342 1.00 21.59 ? 140 LEU   C CG  1 
ATOM   2126 C  CD1 . LEU   B 1 134 ? 23.073 -17.792 25.987 1.00 21.89 ? 140 LEU   C CD1 1 
ATOM   2127 C  CD2 . LEU   B 1 134 ? 23.814 -16.637 28.028 1.00 22.63 ? 140 LEU   C CD2 1 
ATOM   2128 N  N   . LEU   B 1 135 ? 22.844 -20.349 31.713 1.00 22.31 ? 141 LEU   C N   1 
ATOM   2129 C  CA  . LEU   B 1 135 ? 22.148 -21.329 32.565 1.00 24.14 ? 141 LEU   C CA  1 
ATOM   2130 C  C   . LEU   B 1 135 ? 20.623 -21.168 32.595 1.00 24.91 ? 141 LEU   C C   1 
ATOM   2131 O  O   . LEU   B 1 135 ? 19.906 -22.164 32.779 1.00 25.44 ? 141 LEU   C O   1 
ATOM   2132 C  CB  . LEU   B 1 135 ? 22.732 -21.351 34.006 1.00 24.81 ? 141 LEU   C CB  1 
ATOM   2133 C  CG  . LEU   B 1 135 ? 24.267 -21.398 34.127 1.00 26.28 ? 141 LEU   C CG  1 
ATOM   2134 C  CD1 . LEU   B 1 135 ? 24.717 -21.460 35.588 1.00 27.22 ? 141 LEU   C CD1 1 
ATOM   2135 C  CD2 . LEU   B 1 135 ? 24.881 -22.541 33.306 1.00 26.29 ? 141 LEU   C CD2 1 
ATOM   2136 N  N   . TRP   B 1 136 ? 20.126 -19.930 32.396 1.00 24.95 ? 142 TRP   C N   1 
ATOM   2137 C  CA  . TRP   B 1 136 ? 18.687 -19.671 32.419 1.00 25.54 ? 142 TRP   C CA  1 
ATOM   2138 C  C   . TRP   B 1 136 ? 17.934 -20.373 31.269 1.00 25.61 ? 142 TRP   C C   1 
ATOM   2139 O  O   . TRP   B 1 136 ? 16.725 -20.522 31.357 1.00 26.42 ? 142 TRP   C O   1 
ATOM   2140 C  CB  . TRP   B 1 136 ? 18.406 -18.168 32.412 1.00 25.84 ? 142 TRP   C CB  1 
ATOM   2141 C  CG  . TRP   B 1 136 ? 19.072 -17.431 31.295 1.00 25.76 ? 142 TRP   C CG  1 
ATOM   2142 C  CD1 . TRP   B 1 136 ? 20.245 -16.741 31.356 1.00 26.59 ? 142 TRP   C CD1 1 
ATOM   2143 C  CD2 . TRP   B 1 136 ? 18.558 -17.231 29.962 1.00 25.80 ? 142 TRP   C CD2 1 
ATOM   2144 N  NE1 . TRP   B 1 136 ? 20.505 -16.136 30.140 1.00 26.83 ? 142 TRP   C NE1 1 
ATOM   2145 C  CE2 . TRP   B 1 136 ? 19.491 -16.432 29.264 1.00 26.53 ? 142 TRP   C CE2 1 
ATOM   2146 C  CE3 . TRP   B 1 136 ? 17.405 -17.648 29.290 1.00 26.50 ? 142 TRP   C CE3 1 
ATOM   2147 C  CZ2 . TRP   B 1 136 ? 19.295 -16.030 27.935 1.00 26.88 ? 142 TRP   C CZ2 1 
ATOM   2148 C  CZ3 . TRP   B 1 136 ? 17.214 -17.246 27.976 1.00 26.91 ? 142 TRP   C CZ3 1 
ATOM   2149 C  CH2 . TRP   B 1 136 ? 18.161 -16.468 27.308 1.00 26.96 ? 142 TRP   C CH2 1 
ATOM   2150 N  N   . LEU   B 1 137 ? 18.642 -20.842 30.221 1.00 24.92 ? 143 LEU   C N   1 
ATOM   2151 C  CA  . LEU   B 1 137 ? 17.995 -21.587 29.127 1.00 25.98 ? 143 LEU   C CA  1 
ATOM   2152 C  C   . LEU   B 1 137 ? 17.320 -22.890 29.636 1.00 27.65 ? 143 LEU   C C   1 
ATOM   2153 O  O   . LEU   B 1 137 ? 16.419 -23.401 28.973 1.00 28.48 ? 143 LEU   C O   1 
ATOM   2154 C  CB  . LEU   B 1 137 ? 19.020 -21.960 28.040 1.00 26.30 ? 143 LEU   C CB  1 
ATOM   2155 C  CG  . LEU   B 1 137 ? 19.550 -20.813 27.163 1.00 27.46 ? 143 LEU   C CG  1 
ATOM   2156 C  CD1 . LEU   B 1 137 ? 20.628 -21.307 26.200 1.00 28.01 ? 143 LEU   C CD1 1 
ATOM   2157 C  CD2 . LEU   B 1 137 ? 18.432 -20.188 26.350 1.00 28.34 ? 143 LEU   C CD2 1 
ATOM   2158 N  N   . ASP   B 1 138 ? 17.775 -23.432 30.795 1.00 28.19 ? 144 ASP   C N   1 
ATOM   2159 C  CA  . ASP   B 1 138 ? 17.269 -24.680 31.395 1.00 30.42 ? 144 ASP   C CA  1 
ATOM   2160 C  C   . ASP   B 1 138 ? 16.047 -24.526 32.296 1.00 33.93 ? 144 ASP   C C   1 
ATOM   2161 O  O   . ASP   B 1 138 ? 15.643 -25.521 32.903 1.00 34.05 ? 144 ASP   C O   1 
ATOM   2162 C  CB  . ASP   B 1 138 ? 18.357 -25.338 32.253 1.00 30.14 ? 144 ASP   C CB  1 
ATOM   2163 C  CG  . ASP   B 1 138 ? 19.569 -25.794 31.478 1.00 31.38 ? 144 ASP   C CG  1 
ATOM   2164 O  OD1 . ASP   B 1 138 ? 19.455 -25.982 30.241 1.00 30.88 ? 144 ASP   C OD1 1 
ATOM   2165 O  OD2 . ASP   B 1 138 ? 20.634 -25.976 32.107 1.00 32.95 ? 144 ASP   C OD2 1 
ATOM   2166 N  N   . GLU   B 1 139 ? 15.497 -23.314 32.441 1.00 36.53 ? 145 GLU   C N   1 
ATOM   2167 C  CA  . GLU   B 1 139 ? 14.375 -23.109 33.363 1.00 40.28 ? 145 GLU   C CA  1 
ATOM   2168 C  C   . GLU   B 1 139 ? 13.401 -21.991 32.919 1.00 43.27 ? 145 GLU   C C   1 
ATOM   2169 O  O   . GLU   B 1 139 ? 13.636 -21.343 31.895 1.00 43.40 ? 145 GLU   C O   1 
ATOM   2170 C  CB  . GLU   B 1 139 ? 14.940 -22.812 34.765 1.00 44.48 ? 145 GLU   C CB  1 
ATOM   2171 C  CG  . GLU   B 1 139 ? 15.698 -21.499 34.812 1.00 52.57 ? 145 GLU   C CG  1 
ATOM   2172 C  CD  . GLU   B 1 139 ? 16.976 -21.541 35.622 1.00 63.71 ? 145 GLU   C CD  1 
ATOM   2173 O  OE1 . GLU   B 1 139 ? 17.424 -20.464 36.081 1.00 66.37 ? 145 GLU   C OE1 1 
ATOM   2174 O  OE2 . GLU   B 1 139 ? 17.535 -22.650 35.793 1.00 67.20 ? 145 GLU   C OE2 1 
ATOM   2175 N  N   . GLU   B 1 140 ? 12.313 -21.768 33.712 1.00 45.45 ? 146 GLU   C N   1 
ATOM   2176 C  CA  . GLU   B 1 140 ? 11.280 -20.746 33.498 1.00 47.60 ? 146 GLU   C CA  1 
ATOM   2177 C  C   . GLU   B 1 140 ? 10.430 -21.068 32.272 1.00 49.82 ? 146 GLU   C C   1 
ATOM   2178 O  O   . GLU   B 1 140 ? 9.548  -21.932 32.352 1.00 51.24 ? 146 GLU   C O   1 
ATOM   2179 C  CB  . GLU   B 1 140 ? 11.878 -19.317 33.471 1.00 49.74 ? 146 GLU   C CB  1 
ATOM   2180 C  CG  . GLU   B 1 140 ? 11.050 -18.253 32.758 1.00 54.94 ? 146 GLU   C CG  1 
ATOM   2181 C  CD  . GLU   B 1 140 ? 10.029 -17.519 33.606 1.00 60.07 ? 146 GLU   C CD  1 
ATOM   2182 O  OE1 . GLU   B 1 140 ? 10.151 -16.279 33.726 1.00 62.52 ? 146 GLU   C OE1 1 
ATOM   2183 O  OE2 . GLU   B 1 140 ? 9.105  -18.174 34.140 1.00 60.70 ? 146 GLU   C OE2 1 
HETATM 2184 N  N1  . A1BOV C 2 .   ? 9.005  15.396  21.900 1.00 47.34 ? 201 A1BOV A N1  1 
HETATM 2185 C  C4  . A1BOV C 2 .   ? 5.500  15.532  24.759 1.00 54.15 ? 201 A1BOV A C4  1 
HETATM 2186 C  C5  . A1BOV C 2 .   ? 6.461  14.572  24.447 1.00 53.69 ? 201 A1BOV A C5  1 
HETATM 2187 C  C6  . A1BOV C 2 .   ? 7.850  14.824  22.363 1.00 49.07 ? 201 A1BOV A C6  1 
HETATM 2188 C  C7  . A1BOV C 2 .   ? 10.013 16.050  22.757 1.00 46.54 ? 201 A1BOV A C7  1 
HETATM 2189 C  C8  . A1BOV C 2 .   ? 11.382 16.126  22.071 1.00 45.81 ? 201 A1BOV A C8  1 
HETATM 2190 C  C10 . A1BOV C 2 .   ? 10.212 15.930  19.830 1.00 45.01 ? 201 A1BOV A C10 1 
HETATM 2191 C  C13 . A1BOV C 2 .   ? 6.393  13.317  25.067 1.00 55.23 ? 201 A1BOV A C13 1 
HETATM 2192 CL CL  . A1BOV C 2 .   ? 7.424  12.040  24.537 1.00 56.54 ? 201 A1BOV A CL  1 
HETATM 2193 C  C1  . A1BOV C 2 .   ? 5.429  13.073  26.054 1.00 55.35 ? 201 A1BOV A C1  1 
HETATM 2194 O  O   . A1BOV C 2 .   ? 5.473  11.836  26.632 1.00 55.52 ? 201 A1BOV A O   1 
HETATM 2195 C  C   . A1BOV C 2 .   ? 5.406  11.773  28.058 1.00 55.57 ? 201 A1BOV A C   1 
HETATM 2196 C  C3  . A1BOV C 2 .   ? 4.536  15.274  25.720 1.00 54.76 ? 201 A1BOV A C3  1 
HETATM 2197 C  C2  . A1BOV C 2 .   ? 4.506  14.057  26.381 1.00 55.09 ? 201 A1BOV A C2  1 
HETATM 2198 N  N   . A1BOV C 2 .   ? 7.618  14.932  23.705 1.00 51.46 ? 201 A1BOV A N   1 
HETATM 2199 O  O1  . A1BOV C 2 .   ? 7.088  14.234  21.612 1.00 48.59 ? 201 A1BOV A O1  1 
HETATM 2200 C  C12 . A1BOV C 2 .   ? 8.882  16.029  20.582 1.00 46.11 ? 201 A1BOV A C12 1 
HETATM 2201 C  C11 . A1BOV C 2 .   ? 10.157 16.402  18.387 1.00 43.70 ? 201 A1BOV A C11 1 
HETATM 2202 O  O2  . A1BOV C 2 .   ? 9.612  17.466  18.084 1.00 43.45 ? 201 A1BOV A O2  1 
HETATM 2203 N  N2  . A1BOV C 2 .   ? 10.702 15.593  17.491 1.00 42.77 ? 201 A1BOV A N2  1 
HETATM 2204 C  C9  . A1BOV C 2 .   ? 11.266 16.690  20.650 1.00 45.42 ? 201 A1BOV A C9  1 
HETATM 2205 ZN ZN  . ZN    D 3 .   ? 11.162 -3.956  5.844  1.00 26.60 2 202 ZN    A ZN  1 
HETATM 2206 ZN ZN  . ZN    E 3 .   ? 30.587 -31.535 26.899 1.00 22.97 2 201 ZN    C ZN  1 
HETATM 2207 S  S   . DMS   F 4 .   ? 20.815 -32.661 10.361 1.00 87.38 ? 202 DMS   C S   1 
HETATM 2208 O  O   . DMS   F 4 .   ? 21.358 -32.950 8.991  1.00 87.33 ? 202 DMS   C O   1 
HETATM 2209 C  C1  . DMS   F 4 .   ? 22.203 -32.303 11.474 1.00 87.37 ? 202 DMS   C C1  1 
HETATM 2210 C  C2  . DMS   F 4 .   ? 20.164 -30.970 10.319 1.00 87.29 ? 202 DMS   C C2  1 
HETATM 2211 O  O   . HOH   G 5 .   ? 35.432 -3.926  8.115  1.00 29.01 ? 301 HOH   A O   1 
HETATM 2212 O  O   . HOH   G 5 .   ? 8.925  -3.518  0.822  1.00 34.19 ? 302 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 5 .   ? 11.191 8.980   4.357  1.00 24.53 ? 303 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 5 .   ? 2.066  23.472  21.073 1.00 45.57 ? 304 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 5 .   ? 5.122  19.052  24.129 1.00 44.11 ? 305 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 5 .   ? 26.392 -5.709  10.228 1.00 28.81 ? 306 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 5 .   ? 17.174 0.978   28.431 1.00 30.34 ? 307 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 5 .   ? 19.296 10.027  19.710 1.00 21.65 ? 308 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 5 .   ? 3.619  8.722   27.667 1.00 47.80 ? 309 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 5 .   ? 10.468 9.859   31.486 1.00 32.01 ? 310 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 5 .   ? 27.626 8.341   1.738  1.00 41.61 ? 311 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 5 .   ? 6.948  -6.812  24.139 1.00 45.00 ? 312 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 5 .   ? 1.198  8.219   6.292  1.00 43.96 ? 313 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 5 .   ? -0.139 1.305   15.865 1.00 18.67 ? 314 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 5 .   ? 23.242 21.951  7.278  1.00 29.33 ? 315 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 5 .   ? 30.322 10.414  15.646 1.00 29.78 ? 316 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 5 .   ? 31.498 -2.615  15.394 1.00 32.28 ? 317 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 5 .   ? 8.259  -2.769  32.029 1.00 29.31 ? 318 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 5 .   ? 8.533  19.471  19.486 1.00 29.21 ? 319 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 5 .   ? 30.574 3.033   14.885 1.00 35.87 ? 320 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 5 .   ? 11.210 12.828  11.189 1.00 23.36 ? 321 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 5 .   ? 12.253 22.175  12.606 1.00 40.41 ? 322 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 5 .   ? 16.608 3.861   23.834 1.00 21.85 ? 323 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 5 .   ? 17.371 24.562  10.667 1.00 41.18 ? 324 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 5 .   ? 2.617  9.365   9.025  1.00 43.68 ? 325 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 5 .   ? 33.343 14.302  9.682  1.00 36.61 ? 326 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 5 .   ? 28.237 3.445   4.967  1.00 32.68 ? 327 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 5 .   ? 17.018 -3.360  28.194 1.00 41.20 ? 328 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 5 .   ? 22.858 -0.671  5.418  1.00 28.00 ? 329 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 5 .   ? 13.198 11.310  9.298  1.00 23.45 ? 330 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 5 .   ? 2.611  -3.035  20.964 1.00 30.32 ? 331 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 5 .   ? 29.786 11.574  18.939 1.00 39.57 ? 332 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 5 .   ? 6.104  2.467   5.949  1.00 33.63 ? 333 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 5 .   ? 31.505 20.138  11.862 1.00 35.81 ? 334 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 5 .   ? 3.916  -8.229  10.143 1.00 34.86 ? 335 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 5 .   ? 11.916 11.127  29.775 1.00 22.46 ? 336 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 5 .   ? 28.911 15.982  4.549  1.00 36.95 ? 337 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 5 .   ? 20.230 18.184  24.102 1.00 38.98 ? 338 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 5 .   ? 3.178  7.289   24.585 1.00 30.14 ? 339 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 5 .   ? 21.009 -4.240  14.370 1.00 26.12 ? 340 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 5 .   ? 29.031 3.428   12.813 1.00 26.35 ? 341 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 5 .   ? 20.720 -0.894  2.975  1.00 28.08 ? 342 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 5 .   ? 7.384  20.665  17.469 1.00 29.21 ? 343 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 5 .   ? 20.156 19.866  5.534  1.00 42.73 ? 344 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 5 .   ? 11.799 16.275  2.454  1.00 42.04 ? 345 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 5 .   ? 24.900 5.107   21.727 1.00 33.37 ? 346 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 5 .   ? 20.952 -2.622  17.045 1.00 22.64 ? 347 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 5 .   ? 9.529  4.089   33.673 1.00 18.13 ? 348 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 5 .   ? 23.748 11.896  22.050 1.00 40.85 ? 349 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 5 .   ? 13.475 4.074   23.801 1.00 20.05 ? 350 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 5 .   ? 5.400  5.440   32.965 1.00 26.53 ? 351 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 5 .   ? 18.658 17.242  26.834 1.00 42.12 ? 352 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 5 .   ? 9.627  10.811  23.157 1.00 31.27 ? 353 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 5 .   ? 18.307 22.074  9.627  1.00 28.11 ? 354 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 5 .   ? 32.269 2.204   6.111  1.00 39.26 ? 355 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 5 .   ? 0.369  -1.110  19.818 1.00 29.03 ? 356 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 5 .   ? -1.207 -4.432  10.957 1.00 41.96 ? 357 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 5 .   ? 13.927 13.889  24.277 1.00 23.93 ? 358 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 5 .   ? 19.414 3.035   19.592 1.00 28.05 ? 359 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 5 .   ? 26.924 -1.412  8.987  1.00 28.19 ? 360 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 5 .   ? 4.026  -3.985  5.977  1.00 29.59 ? 361 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 5 .   ? 14.388 22.475  8.663  1.00 50.93 ? 362 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 5 .   ? 16.889 6.274   27.278 1.00 42.25 ? 363 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 5 .   ? 14.319 14.887  26.821 1.00 41.88 ? 364 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 5 .   ? 22.502 0.846   17.608 1.00 24.87 ? 365 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 5 .   ? 30.135 -1.353  8.733  1.00 34.64 ? 366 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 5 .   ? 36.662 2.550   9.993  1.00 40.66 ? 367 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 5 .   ? 9.095  3.166   2.944  1.00 29.49 ? 368 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 5 .   ? -1.855 21.686  22.794 1.00 40.40 ? 369 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 5 .   ? 27.756 -1.257  15.977 1.00 36.77 ? 370 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 5 .   ? 10.639 5.306   3.387  1.00 28.99 ? 371 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 5 .   ? 17.400 20.118  17.106 1.00 26.57 ? 372 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 5 .   ? 9.253  19.368  26.384 1.00 48.79 ? 373 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 5 .   ? 14.551 -2.557  18.130 1.00 20.90 ? 374 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 5 .   ? 2.603  16.455  19.540 1.00 32.71 ? 375 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 5 .   ? 5.184  8.347   2.232  1.00 36.26 ? 376 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 5 .   ? 16.025 21.769  7.197  1.00 37.15 ? 377 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 5 .   ? 8.502  -6.437  9.267  1.00 31.47 ? 378 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 5 .   ? 8.109  6.573   33.997 1.00 20.45 ? 379 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 5 .   ? 34.367 18.797  10.966 1.00 28.10 ? 380 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 5 .   ? 30.656 15.864  23.033 1.00 34.66 ? 381 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 5 .   ? 21.517 4.718   24.887 1.00 41.76 ? 382 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 5 .   ? 5.752  -3.964  31.683 1.00 41.65 ? 383 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 5 .   ? 5.330  27.064  19.762 1.00 38.41 ? 384 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 5 .   ? 32.145 8.728   7.632  1.00 33.93 ? 385 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 5 .   ? 28.005 10.982  2.451  1.00 57.80 ? 386 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 5 .   ? 30.604 4.760   5.756  1.00 31.17 ? 387 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 5 .   ? 17.729 10.994  26.057 1.00 29.68 ? 388 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 5 .   ? 22.485 3.468   20.941 1.00 24.15 ? 389 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 5 .   ? 29.291 11.844  21.511 1.00 36.02 ? 390 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 5 .   ? 3.880  0.125   24.314 1.00 22.48 ? 391 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 5 .   ? 15.315 -4.967  0.325  1.00 39.94 ? 392 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 5 .   ? 0.124  5.819   5.876  1.00 34.95 ? 393 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 5 .   ? 34.245 11.133  15.450 1.00 49.12 ? 394 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 5 .   ? 24.201 -3.398  16.417 1.00 36.57 ? 395 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 5 .   ? 13.917 12.446  0.375  1.00 49.25 ? 396 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 5 .   ? 7.290  13.606  4.740  1.00 24.44 ? 397 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 5 .   ? 17.211 -2.552  19.791 1.00 26.53 ? 398 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 5 .   ? 4.713  -4.102  29.185 1.00 38.35 ? 399 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 5 .   ? 0.452  -1.672  9.405  1.00 41.94 ? 400 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 5 .   ? 3.062  -0.793  2.779  1.00 38.98 ? 401 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 5 .   ? 19.598 -0.220  33.505 1.00 42.03 ? 402 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 5 .   ? 16.749 21.435  19.252 1.00 34.16 ? 403 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 5 .   ? 19.779 13.331  2.258  1.00 37.29 ? 404 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 5 .   ? 25.042 17.979  4.574  1.00 37.53 ? 405 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 5 .   ? 1.018  7.140   27.469 1.00 53.92 ? 406 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 5 .   ? 15.562 15.406  3.714  1.00 49.19 ? 407 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 5 .   ? 18.263 18.100  4.209  1.00 42.94 ? 408 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 5 .   ? 10.740 -8.591  0.848  1.00 41.50 ? 409 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 5 .   ? 19.754 21.743  6.912  1.00 47.44 ? 410 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 5 .   ? 23.276 19.347  6.487  1.00 26.43 ? 411 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 5 .   ? 0.406  -1.349  16.856 1.00 24.35 ? 412 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 5 .   ? 23.477 8.268   21.953 1.00 33.05 ? 413 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 5 .   ? 20.900 10.072  22.031 1.00 23.41 ? 414 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 5 .   ? 5.783  17.417  21.909 1.00 38.71 ? 415 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 5 .   ? 27.474 17.833  24.488 1.00 28.15 ? 416 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 5 .   ? 33.724 5.209   16.894 1.00 45.32 ? 417 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 5 .   ? 20.172 -4.479  11.221 1.00 34.92 ? 418 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 5 .   ? 19.758 9.371   -0.780 1.00 29.71 ? 419 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 5 .   ? 16.543 22.170  26.409 1.00 41.87 ? 420 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 5 .   ? 8.268  21.330  7.534  1.00 52.22 ? 421 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 5 .   ? 23.515 -6.949  11.965 1.00 35.31 ? 422 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 5 .   ? 17.846 0.829   20.411 1.00 27.50 ? 423 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 5 .   ? 36.190 -0.535  13.863 1.00 38.51 ? 424 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 5 .   ? 30.938 19.766  8.832  1.00 38.13 ? 425 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 5 .   ? 8.369  16.848  26.190 1.00 43.54 ? 426 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 5 .   ? 17.315 -3.988  3.066  1.00 28.73 ? 427 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 5 .   ? 34.632 17.050  20.336 1.00 44.03 ? 428 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 5 .   ? 35.935 10.845  12.076 1.00 45.22 ? 429 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 5 .   ? 30.386 11.468  3.760  1.00 60.42 ? 430 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 5 .   ? 12.127 -7.172  25.280 1.00 31.96 ? 431 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 5 .   ? 21.780 20.019  19.597 1.00 42.58 ? 432 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 5 .   ? 22.020 -5.397  12.281 1.00 31.85 ? 433 HOH   A O   1 
HETATM 2344 O  O   . HOH   G 5 .   ? -1.545 -3.073  15.652 1.00 29.55 ? 434 HOH   A O   1 
HETATM 2345 O  O   . HOH   G 5 .   ? 36.098 4.121   18.773 1.00 43.81 ? 435 HOH   A O   1 
HETATM 2346 O  O   . HOH   G 5 .   ? 0.879  3.936   26.598 1.00 36.37 ? 436 HOH   A O   1 
HETATM 2347 O  O   . HOH   G 5 .   ? 18.938 -3.295  34.049 1.00 40.49 ? 437 HOH   A O   1 
HETATM 2348 O  O   . HOH   G 5 .   ? 25.574 -1.453  16.422 1.00 30.89 ? 438 HOH   A O   1 
HETATM 2349 O  O   . HOH   G 5 .   ? 2.767  -5.716  14.634 1.00 41.87 ? 439 HOH   A O   1 
HETATM 2350 O  O   . HOH   G 5 .   ? 31.941 7.055   5.712  1.00 32.95 ? 440 HOH   A O   1 
HETATM 2351 O  O   . HOH   G 5 .   ? 6.468  3.162   3.211  1.00 42.24 ? 441 HOH   A O   1 
HETATM 2352 O  O   . HOH   G 5 .   ? 30.629 13.153  23.433 1.00 40.88 ? 442 HOH   A O   1 
HETATM 2353 O  O   . HOH   G 5 .   ? 17.039 -5.025  34.643 1.00 36.21 ? 443 HOH   A O   1 
HETATM 2354 O  O   . HOH   G 5 .   ? 29.720 0.643   16.731 1.00 35.08 ? 444 HOH   A O   1 
HETATM 2355 O  O   . HOH   G 5 .   ? 16.370 13.156  26.645 1.00 30.67 ? 445 HOH   A O   1 
HETATM 2356 O  O   . HOH   G 5 .   ? -0.385 13.831  16.917 1.00 46.73 ? 446 HOH   A O   1 
HETATM 2357 O  O   . HOH   G 5 .   ? 30.787 4.660   17.022 1.00 30.24 ? 447 HOH   A O   1 
HETATM 2358 O  O   . HOH   G 5 .   ? 8.822  12.206  31.757 1.00 40.71 ? 448 HOH   A O   1 
HETATM 2359 O  O   . HOH   G 5 .   ? 23.702 0.914   20.162 1.00 42.04 ? 449 HOH   A O   1 
HETATM 2360 O  O   . HOH   G 5 .   ? 18.742 2.720   26.417 1.00 49.90 ? 450 HOH   A O   1 
HETATM 2361 O  O   . HOH   G 5 .   ? 25.893 13.225  3.004  1.00 41.10 ? 451 HOH   A O   1 
HETATM 2362 O  O   . HOH   G 5 .   ? 12.492 -5.059  33.423 1.00 32.32 ? 452 HOH   A O   1 
HETATM 2363 O  O   . HOH   G 5 .   ? 21.474 -1.064  19.227 1.00 39.76 ? 453 HOH   A O   1 
HETATM 2364 O  O   . HOH   G 5 .   ? 2.257  8.204   1.585  1.00 40.24 ? 454 HOH   A O   1 
HETATM 2365 O  O   . HOH   G 5 .   ? 28.764 1.127   19.434 1.00 42.80 ? 455 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 17.506 -33.667 24.165 1.00 40.71 ? 301 HOH   C O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? 30.678 -18.534 27.232 1.00 21.95 ? 302 HOH   C O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? 38.450 -7.409  7.503  1.00 28.80 ? 303 HOH   C O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? 20.845 -19.024 12.976 1.00 22.83 ? 304 HOH   C O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? 19.809 -4.148  20.507 1.00 28.95 ? 305 HOH   C O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? 29.542 -26.226 -1.329 1.00 22.53 ? 306 HOH   C O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? 24.057 -8.379  9.686  1.00 33.40 ? 307 HOH   C O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? 24.706 -9.506  27.220 1.00 43.48 ? 308 HOH   C O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 37.151 -32.397 11.063 1.00 27.16 ? 309 HOH   C O   1 
HETATM 2375 O  O   . HOH   H 5 .   ? 17.809 -24.595 8.516  1.00 38.01 ? 310 HOH   C O   1 
HETATM 2376 O  O   . HOH   H 5 .   ? 42.586 -11.553 11.189 1.00 30.20 ? 311 HOH   C O   1 
HETATM 2377 O  O   . HOH   H 5 .   ? 17.969 -5.994  24.372 1.00 29.45 ? 312 HOH   C O   1 
HETATM 2378 O  O   . HOH   H 5 .   ? 39.023 -18.958 21.662 1.00 28.42 ? 313 HOH   C O   1 
HETATM 2379 O  O   . HOH   H 5 .   ? 10.141 -8.975  24.268 1.00 33.52 ? 314 HOH   C O   1 
HETATM 2380 O  O   . HOH   H 5 .   ? 23.540 -33.611 29.402 1.00 32.20 ? 315 HOH   C O   1 
HETATM 2381 O  O   . HOH   H 5 .   ? 26.553 -6.354  22.501 1.00 30.02 ? 316 HOH   C O   1 
HETATM 2382 O  O   . HOH   H 5 .   ? 10.873 -6.467  13.477 1.00 38.46 ? 317 HOH   C O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? 14.835 -23.883 12.607 1.00 31.43 ? 318 HOH   C O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? 42.190 -32.181 20.834 1.00 46.51 ? 319 HOH   C O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? 37.045 -18.838 28.556 1.00 33.11 ? 320 HOH   C O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? 22.388 -23.699 6.094  1.00 40.78 ? 321 HOH   C O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? 24.903 -16.020 7.543  1.00 24.93 ? 322 HOH   C O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? 10.589 -31.291 25.156 1.00 37.90 ? 323 HOH   C O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? 21.901 -28.815 4.899  1.00 31.89 ? 324 HOH   C O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 21.273 -25.249 3.913  1.00 45.17 ? 325 HOH   C O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 26.131 -25.434 8.970  1.00 22.95 ? 326 HOH   C O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 14.798 -29.101 26.103 1.00 40.07 ? 327 HOH   C O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? 27.783 -4.415  18.056 1.00 44.70 ? 328 HOH   C O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 33.096 -30.794 31.898 1.00 23.58 ? 329 HOH   C O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 31.009 -21.802 28.620 1.00 19.43 ? 330 HOH   C O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 21.637 -26.713 34.545 1.00 33.07 ? 331 HOH   C O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 40.059 -30.019 11.711 1.00 24.25 ? 332 HOH   C O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 23.061 -5.997  21.482 1.00 28.21 ? 333 HOH   C O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 19.018 -27.992 28.431 1.00 29.95 ? 334 HOH   C O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 32.038 -10.580 14.058 1.00 22.85 ? 335 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? 23.080 -25.521 9.095  1.00 22.63 ? 336 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 10.196 -17.690 18.548 1.00 37.30 ? 337 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 40.581 -27.565 15.205 1.00 18.45 ? 338 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 33.121 -36.562 9.040  1.00 33.38 ? 339 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? 36.625 -31.361 29.884 1.00 37.22 ? 340 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? 13.879 -24.344 29.580 1.00 47.04 ? 341 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? 31.198 -24.139 -1.124 1.00 24.77 ? 342 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? 26.834 -35.910 20.927 1.00 27.53 ? 343 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? 6.364  -9.381  22.851 1.00 35.09 ? 344 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? 30.040 -15.436 19.802 1.00 20.10 ? 345 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? 36.668 -16.784 12.360 1.00 33.20 ? 346 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? 20.069 -23.801 35.442 1.00 33.42 ? 347 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? 25.306 -38.036 24.453 1.00 40.25 ? 348 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? 20.894 -26.005 13.717 1.00 35.58 ? 349 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 5 .   ? 35.179 -13.372 8.956  1.00 23.91 ? 350 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 5 .   ? 16.200 -17.298 11.315 1.00 34.49 ? 351 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 5 .   ? 31.675 -35.557 31.933 1.00 35.38 ? 352 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 5 .   ? 28.192 -16.669 22.339 1.00 20.81 ? 353 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 5 .   ? 22.417 -7.276  25.720 1.00 50.26 ? 354 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 5 .   ? 23.968 -3.436  19.490 1.00 39.67 ? 355 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 5 .   ? 11.826 -24.492 21.942 1.00 24.51 ? 356 HOH   C O   1 
HETATM 2422 O  O   . HOH   H 5 .   ? 23.047 -8.549  14.297 1.00 19.56 ? 357 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 5 .   ? 40.409 -25.660 7.282  1.00 37.68 ? 358 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 5 .   ? 29.776 -13.299 13.118 1.00 24.76 ? 359 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 5 .   ? 17.884 -27.804 16.606 1.00 25.76 ? 360 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 5 .   ? 31.409 -12.322 10.820 1.00 24.43 ? 361 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 5 .   ? 22.805 -28.329 12.806 1.00 25.80 ? 362 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 5 .   ? 20.964 -26.188 1.337  1.00 60.14 ? 363 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 5 .   ? 38.527 -13.730 10.885 1.00 32.43 ? 364 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 5 .   ? 10.793 -17.170 13.108 1.00 45.20 ? 365 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 5 .   ? 36.093 -28.981 2.889  1.00 44.12 ? 366 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 5 .   ? 43.196 -25.817 24.158 1.00 40.29 ? 367 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 5 .   ? 9.686  -8.363  21.949 1.00 37.19 ? 368 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 5 .   ? 32.914 -9.970  11.369 1.00 22.85 ? 369 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 5 .   ? 21.496 -19.133 6.075  1.00 31.82 ? 370 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 5 .   ? 10.015 -24.945 19.973 1.00 23.63 ? 371 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 5 .   ? 5.890  -19.067 25.477 1.00 55.64 ? 372 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 5 .   ? 32.692 -24.016 29.368 1.00 21.91 ? 373 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 5 .   ? 37.979 -31.760 25.874 1.00 32.87 ? 374 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 5 .   ? 18.894 -8.643  13.666 1.00 33.68 ? 375 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 5 .   ? 36.346 -26.558 34.678 1.00 32.04 ? 376 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 5 .   ? 34.326 -13.790 25.821 1.00 27.77 ? 377 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 5 .   ? 17.216 -25.445 13.128 1.00 29.40 ? 378 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 5 .   ? 22.638 -33.575 5.395  1.00 38.77 ? 379 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 5 .   ? 34.697 -2.581  14.386 1.00 34.54 ? 380 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 5 .   ? 41.836 -12.642 17.855 1.00 28.57 ? 381 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 5 .   ? 11.494 -22.618 29.044 1.00 34.66 ? 382 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 5 .   ? 6.459  -22.715 18.876 1.00 33.56 ? 383 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 5 .   ? 34.974 -13.971 6.190  1.00 35.15 ? 384 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 5 .   ? 30.196 -16.265 30.803 1.00 32.86 ? 385 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 5 .   ? 35.310 -35.184 18.160 1.00 42.87 ? 386 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 5 .   ? 26.065 -31.413 31.077 1.00 21.34 ? 387 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 5 .   ? 10.917 -11.968 9.184  1.00 36.52 ? 388 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 5 .   ? 34.960 -4.309  17.717 1.00 34.83 ? 389 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 5 .   ? 36.441 -21.708 7.005  1.00 33.57 ? 390 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 5 .   ? 3.958  -8.404  14.947 1.00 38.55 ? 391 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 5 .   ? 30.054 -6.119  6.348  1.00 36.33 ? 392 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 5 .   ? 26.621 -12.226 27.972 1.00 24.86 ? 393 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 5 .   ? 34.892 -30.537 33.997 1.00 37.17 ? 394 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 5 .   ? 20.288 -32.308 22.343 1.00 38.29 ? 395 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 5 .   ? 9.868  -18.623 27.101 1.00 37.04 ? 396 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 5 .   ? 26.324 -31.614 15.078 1.00 27.70 ? 397 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 5 .   ? 9.728  -24.555 29.776 1.00 35.29 ? 398 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 5 .   ? 18.821 -11.834 7.835  1.00 35.94 ? 399 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 5 .   ? 8.881  -13.405 10.912 1.00 27.02 ? 400 HOH   C O   1 
HETATM 2466 O  O   . HOH   H 5 .   ? 39.851 -30.288 14.686 1.00 19.29 ? 401 HOH   C O   1 
HETATM 2467 O  O   . HOH   H 5 .   ? 30.375 -10.724 28.222 1.00 40.50 ? 402 HOH   C O   1 
HETATM 2468 O  O   . HOH   H 5 .   ? 18.759 -8.296  25.667 1.00 25.70 ? 403 HOH   C O   1 
HETATM 2469 O  O   . HOH   H 5 .   ? 35.734 -29.021 7.880  1.00 25.51 ? 404 HOH   C O   1 
HETATM 2470 O  O   . HOH   H 5 .   ? 4.112  -10.243 20.413 1.00 38.41 ? 405 HOH   C O   1 
HETATM 2471 O  O   . HOH   H 5 .   ? 34.798 -23.666 -0.908 1.00 26.77 ? 406 HOH   C O   1 
HETATM 2472 O  O   . HOH   H 5 .   ? 35.714 -25.000 24.954 1.00 26.71 ? 407 HOH   C O   1 
HETATM 2473 O  O   . HOH   H 5 .   ? 27.262 -19.372 1.827  1.00 28.45 ? 408 HOH   C O   1 
HETATM 2474 O  O   . HOH   H 5 .   ? 28.888 -36.736 7.924  1.00 25.57 ? 409 HOH   C O   1 
HETATM 2475 O  O   . HOH   H 5 .   ? 38.816 -14.781 13.299 1.00 40.63 ? 410 HOH   C O   1 
HETATM 2476 O  O   . HOH   H 5 .   ? 37.055 -14.977 9.774  1.00 28.85 ? 411 HOH   C O   1 
HETATM 2477 O  O   . HOH   H 5 .   ? 12.994 -11.413 28.935 1.00 36.16 ? 412 HOH   C O   1 
HETATM 2478 O  O   . HOH   H 5 .   ? 18.702 -30.696 -1.015 1.00 43.40 ? 413 HOH   C O   1 
HETATM 2479 O  O   . HOH   H 5 .   ? 26.170 -15.651 31.459 1.00 34.50 ? 414 HOH   C O   1 
HETATM 2480 O  O   . HOH   H 5 .   ? 5.403  -16.796 22.936 1.00 49.50 ? 415 HOH   C O   1 
HETATM 2481 O  O   . HOH   H 5 .   ? 39.023 -13.435 26.156 1.00 28.50 ? 416 HOH   C O   1 
HETATM 2482 O  O   . HOH   H 5 .   ? 16.339 -20.972 11.863 1.00 31.88 ? 417 HOH   C O   1 
HETATM 2483 O  O   . HOH   H 5 .   ? 36.855 -29.779 10.064 1.00 31.79 ? 418 HOH   C O   1 
HETATM 2484 O  O   . HOH   H 5 .   ? 14.121 -29.981 18.975 1.00 44.06 ? 419 HOH   C O   1 
HETATM 2485 O  O   . HOH   H 5 .   ? 34.046 -20.784 -2.068 1.00 35.04 ? 420 HOH   C O   1 
HETATM 2486 O  O   . HOH   H 5 .   ? 32.990 -34.498 24.225 1.00 33.27 ? 421 HOH   C O   1 
HETATM 2487 O  O   . HOH   H 5 .   ? 6.189  -17.439 19.594 1.00 41.52 ? 422 HOH   C O   1 
HETATM 2488 O  O   . HOH   H 5 .   ? 30.462 -18.158 8.418  1.00 29.17 ? 423 HOH   C O   1 
HETATM 2489 O  O   . HOH   H 5 .   ? 24.158 -16.573 2.980  1.00 46.42 ? 424 HOH   C O   1 
HETATM 2490 O  O   . HOH   H 5 .   ? 42.302 -12.426 20.666 1.00 37.92 ? 425 HOH   C O   1 
HETATM 2491 O  O   . HOH   H 5 .   ? 22.790 -13.867 30.092 1.00 50.11 ? 426 HOH   C O   1 
HETATM 2492 O  O   . HOH   H 5 .   ? 38.590 -16.918 3.544  1.00 56.15 ? 427 HOH   C O   1 
HETATM 2493 O  O   . HOH   H 5 .   ? 32.788 -14.456 9.538  1.00 25.96 ? 428 HOH   C O   1 
HETATM 2494 O  O   . HOH   H 5 .   ? 20.520 -19.760 36.703 1.00 39.20 ? 429 HOH   C O   1 
HETATM 2495 O  O   . HOH   H 5 .   ? 37.850 -20.895 4.657  1.00 34.22 ? 430 HOH   C O   1 
HETATM 2496 O  O   . HOH   H 5 .   ? 24.365 -14.058 5.572  1.00 36.15 ? 431 HOH   C O   1 
HETATM 2497 O  O   . HOH   H 5 .   ? 31.658 -13.847 4.694  1.00 31.00 ? 432 HOH   C O   1 
HETATM 2498 O  O   . HOH   H 5 .   ? 23.280 -17.853 33.818 1.00 27.38 ? 433 HOH   C O   1 
HETATM 2499 O  O   . HOH   H 5 .   ? 9.676  -13.596 31.872 1.00 43.57 ? 434 HOH   C O   1 
HETATM 2500 O  O   . HOH   H 5 .   ? 38.477 -30.209 28.400 1.00 58.59 ? 435 HOH   C O   1 
HETATM 2501 O  O   . HOH   H 5 .   ? 20.883 -17.863 34.954 1.00 37.66 ? 436 HOH   C O   1 
HETATM 2502 O  O   . HOH   H 5 .   ? 18.273 -19.135 11.188 1.00 26.87 ? 437 HOH   C O   1 
HETATM 2503 O  O   . HOH   H 5 .   ? 33.974 -32.194 29.730 1.00 25.54 ? 438 HOH   C O   1 
HETATM 2504 O  O   . HOH   H 5 .   ? 6.975  -20.327 18.188 1.00 28.31 ? 439 HOH   C O   1 
HETATM 2505 O  O   . HOH   H 5 .   ? 23.685 -16.030 31.915 1.00 31.47 ? 440 HOH   C O   1 
HETATM 2506 O  O   . HOH   H 5 .   ? 10.342 -20.121 29.353 1.00 30.07 ? 441 HOH   C O   1 
HETATM 2507 O  O   . HOH   H 5 .   ? 21.335 -21.163 4.053  1.00 44.47 ? 442 HOH   C O   1 
HETATM 2508 O  O   . HOH   H 5 .   ? 22.933 -16.932 5.644  1.00 37.83 ? 443 HOH   C O   1 
HETATM 2509 O  O   . HOH   H 5 .   ? 17.425 -17.099 8.185  1.00 59.01 ? 444 HOH   C O   1 
HETATM 2510 O  O   . HOH   H 5 .   ? 14.349 -27.121 29.621 1.00 50.71 ? 445 HOH   C O   1 
HETATM 2511 O  O   . HOH   H 5 .   ? 16.291 -23.115 10.044 1.00 51.89 ? 446 HOH   C O   1 
HETATM 2512 O  O   . HOH   H 5 .   ? 35.401 -23.911 28.480 1.00 39.66 ? 447 HOH   C O   1 
HETATM 2513 O  O   . HOH   H 5 .   ? 27.685 -4.594  7.849  1.00 59.24 ? 448 HOH   C O   1 
HETATM 2514 O  O   . HOH   H 5 .   ? 32.502 -19.624 29.203 1.00 36.88 ? 449 HOH   C O   1 
HETATM 2515 O  O   . HOH   H 5 .   ? 23.095 -8.934  7.445  1.00 41.64 ? 450 HOH   C O   1 
HETATM 2516 O  O   . HOH   H 5 .   ? 5.449  -10.533 10.038 1.00 47.73 ? 451 HOH   C O   1 
HETATM 2517 O  O   . HOH   H 5 .   ? 39.026 -25.510 4.799  1.00 36.95 ? 452 HOH   C O   1 
HETATM 2518 O  O   . HOH   H 5 .   ? 41.521 -15.602 13.632 1.00 34.86 ? 453 HOH   C O   1 
HETATM 2519 O  O   . HOH   H 5 .   ? 10.546 -27.310 18.097 1.00 38.99 ? 454 HOH   C O   1 
HETATM 2520 O  O   . HOH   H 5 .   ? 39.206 -2.825  10.776 1.00 36.07 ? 455 HOH   C O   1 
HETATM 2521 O  O   . HOH   H 5 .   ? 22.854 -11.875 6.073  1.00 37.25 ? 456 HOH   C O   1 
HETATM 2522 O  O   . HOH   H 5 .   ? 3.398  -8.473  22.562 1.00 42.55 ? 457 HOH   C O   1 
HETATM 2523 O  O   . HOH   H 5 .   ? 35.799 -36.457 8.765  1.00 48.07 ? 458 HOH   C O   1 
HETATM 2524 O  O   . HOH   H 5 .   ? 19.280 -15.338 35.251 1.00 38.60 ? 459 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   ? 0.3609 0.2229 0.3007 0.0208  -0.0010 -0.0254 7   SER   A N   
2    C  CA  . SER   A 1   ? 0.3778 0.2378 0.3236 0.0209  -0.0037 -0.0233 7   SER   A CA  
3    C  C   . SER   A 1   ? 0.3696 0.2310 0.3205 0.0227  -0.0048 -0.0179 7   SER   A C   
4    O  O   . SER   A 1   ? 0.3662 0.2303 0.3149 0.0228  -0.0050 -0.0152 7   SER   A O   
5    C  CB  . SER   A 1   ? 0.4142 0.2760 0.3573 0.0163  -0.0078 -0.0235 7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.4486 0.3159 0.3894 0.0141  -0.0114 -0.0190 7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.3578 0.2172 0.3153 0.0236  -0.0052 -0.0168 8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.3517 0.2117 0.3143 0.0249  -0.0051 -0.0132 8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.3415 0.1992 0.3097 0.0258  -0.0031 -0.0136 8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.3348 0.1901 0.3026 0.0263  -0.0015 -0.0154 8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.3282 0.1865 0.3019 0.0259  -0.0029 -0.0117 9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.3379 0.1951 0.3161 0.0258  -0.0005 -0.0123 9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.3389 0.1963 0.3200 0.0259  0.0022  -0.0114 9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.3303 0.1878 0.3115 0.0265  0.0016  -0.0101 9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.3348 0.1930 0.3186 0.0248  -0.0022 -0.0125 9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.3402 0.1973 0.3229 0.0247  0.0052  -0.0124 10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.3343 0.1912 0.3194 0.0237  0.0089  -0.0132 10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.3279 0.1862 0.3212 0.0234  0.0102  -0.0142 10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.3344 0.1939 0.3286 0.0223  0.0096  -0.0144 10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.3410 0.1980 0.3204 0.0209  0.0117  -0.0136 10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.3519 0.2091 0.3248 0.0212  0.0101  -0.0117 10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.3417 0.1980 0.3219 0.0186  0.0161  -0.0157 10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.3588 0.2178 0.3272 0.0181  0.0114  -0.0102 10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.3132 0.1715 0.3140 0.0245  0.0120  -0.0147 11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.3219 0.1826 0.3327 0.0246  0.0140  -0.0157 11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.3251 0.1847 0.3380 0.0230  0.0208  -0.0193 11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.3244 0.1814 0.3414 0.0244  0.0229  -0.0201 11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.3177 0.1802 0.3384 0.0275  0.0107  -0.0127 11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.3183 0.1826 0.3355 0.0274  0.0044  -0.0100 11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.3273 0.1943 0.3460 0.0259  0.0027  -0.0101 11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.3263 0.1895 0.3373 0.0278  0.0006  -0.0078 11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.3359 0.2036 0.3500 0.0248  -0.0025 -0.0087 11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.3362 0.2010 0.3424 0.0266  -0.0042 -0.0066 11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.3450 0.2117 0.3526 0.0251  -0.0056 -0.0074 11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.3685 0.2360 0.3708 0.0230  -0.0098 -0.0073 11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.3331 0.1945 0.3424 0.0194  0.0242  -0.0216 12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.3487 0.2101 0.3575 0.0161  0.0311  -0.0260 12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.3483 0.2143 0.3638 0.0144  0.0343  -0.0277 12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.3499 0.2188 0.3634 0.0131  0.0312  -0.0253 12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.3647 0.2252 0.3603 0.0113  0.0321  -0.0264 12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.3665 0.2296 0.3558 0.0095  0.0279  -0.0227 12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.3688 0.2299 0.3620 0.0060  0.0395  -0.0316 12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.3428 0.2095 0.3681 0.0149  0.0406  -0.0316 13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.3369 0.2092 0.3704 0.0135  0.0445  -0.0335 13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.3266 0.2028 0.3671 0.0162  0.0384  -0.0288 13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.3195 0.1946 0.3655 0.0205  0.0334  -0.0253 13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.3213 0.2021 0.3601 0.0126  0.0382  -0.0282 14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.3202 0.2039 0.3634 0.0137  0.0320  -0.0239 14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.3283 0.2087 0.3594 0.0120  0.0259  -0.0208 14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.3273 0.2094 0.3585 0.0102  0.0226  -0.0186 14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.3272 0.2182 0.3795 0.0114  0.0351  -0.0246 14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.3683 0.2633 0.4372 0.0150  0.0396  -0.0262 14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.3885 0.2866 0.4688 0.0185  0.0354  -0.0225 14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.3723 0.2674 0.4433 0.0139  0.0482  -0.0317 14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.3284 0.2037 0.3504 0.0129  0.0245  -0.0206 15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.3315 0.2035 0.3442 0.0122  0.0196  -0.0180 15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.3278 0.1961 0.3385 0.0162  0.0152  -0.0166 15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.3263 0.1935 0.3388 0.0185  0.0165  -0.0174 15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.3445 0.2154 0.3474 0.0086  0.0218  -0.0180 15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.3624 0.2376 0.3643 0.0030  0.0257  -0.0187 15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.3668 0.2442 0.3705 0.0005  0.0237  -0.0163 15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.3793 0.2563 0.3774 -0.0008 0.0315  -0.0218 15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.3737 0.2559 0.3759 -0.0055 0.0270  -0.0162 15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.3904 0.2725 0.3864 -0.0072 0.0354  -0.0227 15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.3929 0.2779 0.3908 -0.0096 0.0330  -0.0194 15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.4130 0.3039 0.4082 -0.0167 0.0366  -0.0195 15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.3059 0.1718 0.3122 0.0165  0.0105  -0.0148 16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.2945 0.1575 0.2969 0.0191  0.0068  -0.0141 16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.2998 0.1596 0.2944 0.0185  0.0062  -0.0134 16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.2898 0.1485 0.2842 0.0167  0.0054  -0.0127 16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.3056 0.1695 0.3115 0.0195  0.0024  -0.0134 16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.3267 0.1875 0.3259 0.0203  -0.0011 -0.0135 16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.3468 0.2092 0.3479 0.0190  -0.0055 -0.0131 16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.3695 0.2280 0.3634 0.0179  -0.0075 -0.0151 16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.4055 0.2634 0.3935 0.0181  -0.0093 -0.0158 16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.3920 0.2528 0.3802 0.0195  -0.0100 -0.0138 16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.4069 0.2608 0.3888 0.0167  -0.0099 -0.0189 16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.3058 0.1642 0.2951 0.0197  0.0068  -0.0132 17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.3098 0.1664 0.2939 0.0196  0.0065  -0.0118 17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.3263 0.1807 0.3077 0.0223  0.0042  -0.0123 17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.3066 0.1616 0.2860 0.0237  0.0038  -0.0127 17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.3164 0.1748 0.2966 0.0179  0.0090  -0.0107 17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.3277 0.1861 0.3050 0.0173  0.0081  -0.0076 17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.3137 0.1746 0.2954 0.0143  0.0124  -0.0118 17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.3297 0.1813 0.3112 0.0227  0.0029  -0.0125 18  VAL   A N   
86   C  CA  A VAL   A 12  ? 0.3293 0.1785 0.3080 0.0247  0.0018  -0.0144 18  VAL   A CA  
87   C  CA  B VAL   A 12  ? 0.3396 0.1889 0.3183 0.0246  0.0017  -0.0144 18  VAL   A CA  
88   C  C   . VAL   A 12  ? 0.3313 0.1780 0.3104 0.0260  0.0028  -0.0135 18  VAL   A C   
89   O  O   . VAL   A 12  ? 0.3207 0.1671 0.3030 0.0249  0.0032  -0.0106 18  VAL   A O   
90   C  CB  A VAL   A 12  ? 0.3290 0.1764 0.3085 0.0236  -0.0004 -0.0170 18  VAL   A CB  
91   C  CB  B VAL   A 12  ? 0.3605 0.2081 0.3404 0.0234  -0.0005 -0.0168 18  VAL   A CB  
92   C  CG1 A VAL   A 12  ? 0.3345 0.1855 0.3143 0.0229  -0.0022 -0.0169 18  VAL   A CG1 
93   C  CG1 B VAL   A 12  ? 0.3747 0.2197 0.3505 0.0239  -0.0011 -0.0200 18  VAL   A CG1 
94   C  CG2 A VAL   A 12  ? 0.3171 0.1625 0.3009 0.0215  -0.0008 -0.0166 18  VAL   A CG2 
95   C  CG2 B VAL   A 12  ? 0.3658 0.2173 0.3479 0.0224  -0.0019 -0.0162 18  VAL   A CG2 
96   N  N   . ASN   A 13  ? 0.3263 0.1718 0.3030 0.0282  0.0033  -0.0155 19  ASN   A N   
97   C  CA  . ASN   A 13  ? 0.3221 0.1651 0.3018 0.0303  0.0049  -0.0152 19  ASN   A CA  
98   C  C   . ASN   A 13  ? 0.3097 0.1466 0.2932 0.0294  0.0044  -0.0170 19  ASN   A C   
99   O  O   . ASN   A 13  ? 0.3036 0.1383 0.2847 0.0278  0.0034  -0.0210 19  ASN   A O   
100  C  CB  . ASN   A 13  ? 0.3320 0.1748 0.3082 0.0323  0.0064  -0.0190 19  ASN   A CB  
101  C  CG  . ASN   A 13  ? 0.3401 0.1885 0.3127 0.0330  0.0069  -0.0172 19  ASN   A CG  
102  O  OD1 . ASN   A 13  ? 0.3410 0.1918 0.3084 0.0317  0.0058  -0.0182 19  ASN   A OD1 
103  N  ND2 . ASN   A 13  ? 0.3247 0.1756 0.3005 0.0347  0.0083  -0.0137 19  ASN   A ND2 
104  N  N   . ARG   A 14  ? 0.3088 0.1433 0.2986 0.0298  0.0047  -0.0136 20  ARG   A N   
105  C  CA  . ARG   A 14  ? 0.3170 0.1448 0.3111 0.0285  0.0041  -0.0148 20  ARG   A CA  
106  C  C   . ARG   A 14  ? 0.3343 0.1559 0.3270 0.0295  0.0057  -0.0218 20  ARG   A C   
107  O  O   . ARG   A 14  ? 0.3508 0.1682 0.3424 0.0268  0.0047  -0.0252 20  ARG   A O   
108  C  CB  . ARG   A 14  ? 0.3462 0.1721 0.3485 0.0292  0.0040  -0.0090 20  ARG   A CB  
109  C  CG  . ARG   A 14  ? 0.3555 0.1750 0.3628 0.0268  0.0028  -0.0083 20  ARG   A CG  
110  C  CD  . ARG   A 14  ? 0.3594 0.1770 0.3762 0.0281  0.0025  -0.0015 20  ARG   A CD  
111  N  NE  . ARG   A 14  ? 0.3863 0.1976 0.4087 0.0254  0.0009  0.0007  20  ARG   A NE  
112  C  CZ  . ARG   A 14  ? 0.4228 0.2239 0.4510 0.0269  0.0021  -0.0027 20  ARG   A CZ  
113  N  NH1 . ARG   A 14  ? 0.3837 0.1803 0.4119 0.0307  0.0055  -0.0096 20  ARG   A NH1 
114  N  NH2 . ARG   A 14  ? 0.4273 0.2227 0.4612 0.0239  0.0003  0.0003  20  ARG   A NH2 
115  N  N   . HIS   A 15  ? 0.3291 0.1509 0.3212 0.0327  0.0085  -0.0243 21  HIS   A N   
116  C  CA  . HIS   A 15  ? 0.3468 0.1628 0.3369 0.0330  0.0113  -0.0320 21  HIS   A CA  
117  C  C   . HIS   A 15  ? 0.3501 0.1681 0.3300 0.0291  0.0098  -0.0371 21  HIS   A C   
118  O  O   . HIS   A 15  ? 0.3587 0.1719 0.3350 0.0273  0.0117  -0.0441 21  HIS   A O   
119  C  CB  . HIS   A 15  ? 0.3646 0.1809 0.3582 0.0374  0.0156  -0.0335 21  HIS   A CB  
120  C  CG  . HIS   A 15  ? 0.3968 0.2213 0.3836 0.0379  0.0160  -0.0333 21  HIS   A CG  
121  N  ND1 . HIS   A 15  ? 0.4115 0.2430 0.4001 0.0395  0.0149  -0.0266 21  HIS   A ND1 
122  C  CD2 . HIS   A 15  ? 0.4112 0.2379 0.3894 0.0364  0.0174  -0.0389 21  HIS   A CD2 
123  C  CE1 . HIS   A 15  ? 0.4185 0.2555 0.4004 0.0393  0.0156  -0.0283 21  HIS   A CE1 
124  N  NE2 . HIS   A 15  ? 0.4223 0.2570 0.3978 0.0375  0.0171  -0.0353 21  HIS   A NE2 
125  N  N   . LEU   A 16  ? 0.3435 0.1683 0.3193 0.0274  0.0066  -0.0337 22  LEU   A N   
126  C  CA  . LEU   A 16  ? 0.3433 0.1716 0.3117 0.0237  0.0040  -0.0360 22  LEU   A CA  
127  C  C   . LEU   A 16  ? 0.3496 0.1792 0.3199 0.0204  0.0002  -0.0335 22  LEU   A C   
128  O  O   . LEU   A 16  ? 0.3472 0.1808 0.3138 0.0173  -0.0027 -0.0338 22  LEU   A O   
129  C  CB  . LEU   A 16  ? 0.3531 0.1886 0.3170 0.0246  0.0035  -0.0338 22  LEU   A CB  
130  C  CG  . LEU   A 16  ? 0.3758 0.2121 0.3373 0.0270  0.0072  -0.0363 22  LEU   A CG  
131  C  CD1 . LEU   A 16  ? 0.3845 0.2280 0.3419 0.0273  0.0062  -0.0329 22  LEU   A CD1 
132  C  CD2 . LEU   A 16  ? 0.3835 0.2162 0.3395 0.0245  0.0095  -0.0439 22  LEU   A CD2 
133  N  N   . ALA   A 17  ? 0.3451 0.1720 0.3220 0.0208  0.0001  -0.0305 23  ALA   A N   
134  C  CA  . ALA   A 17  ? 0.3618 0.1905 0.3415 0.0177  -0.0027 -0.0282 23  ALA   A CA  
135  C  C   . ALA   A 17  ? 0.3708 0.1971 0.3476 0.0132  -0.0048 -0.0325 23  ALA   A C   
136  O  O   . ALA   A 17  ? 0.3681 0.1874 0.3426 0.0123  -0.0032 -0.0375 23  ALA   A O   
137  C  CB  . ALA   A 17  ? 0.3607 0.1867 0.3469 0.0180  -0.0020 -0.0247 23  ALA   A CB  
138  N  N   . THR   A 18  ? 0.3663 0.1984 0.3435 0.0102  -0.0082 -0.0306 24  THR   A N   
139  C  CA  . THR   A 18  ? 0.3713 0.2033 0.3459 0.0047  -0.0112 -0.0333 24  THR   A CA  
140  C  C   . THR   A 18  ? 0.3732 0.2019 0.3534 0.0019  -0.0121 -0.0324 24  THR   A C   
141  O  O   . THR   A 18  ? 0.3698 0.1979 0.3557 0.0042  -0.0106 -0.0289 24  THR   A O   
142  C  CB  . THR   A 18  ? 0.3880 0.2296 0.3627 0.0030  -0.0151 -0.0299 24  THR   A CB  
143  O  OG1 . THR   A 18  ? 0.3866 0.2332 0.3699 0.0046  -0.0154 -0.0249 24  THR   A OG1 
144  C  CG2 . THR   A 18  ? 0.3987 0.2439 0.3683 0.0052  -0.0148 -0.0295 24  THR   A CG2 
145  N  N   . HIS   A 19  ? 0.3836 0.2112 0.3617 -0.0039 -0.0150 -0.0349 25  HIS   A N   
146  C  CA  . HIS   A 19  ? 0.4024 0.2278 0.3857 -0.0075 -0.0163 -0.0336 25  HIS   A CA  
147  C  C   . HIS   A 19  ? 0.3905 0.2254 0.3816 -0.0065 -0.0176 -0.0273 25  HIS   A C   
148  O  O   . HIS   A 19  ? 0.3879 0.2216 0.3844 -0.0062 -0.0163 -0.0246 25  HIS   A O   
149  C  CB  . HIS   A 19  ? 0.4241 0.2482 0.4032 -0.0149 -0.0196 -0.0373 25  HIS   A CB  
150  C  CG  . HIS   A 19  ? 0.5018 0.3263 0.4869 -0.0194 -0.0219 -0.0348 25  HIS   A CG  
151  N  ND1 . HIS   A 19  ? 0.5401 0.3546 0.5278 -0.0204 -0.0201 -0.0361 25  HIS   A ND1 
152  C  CD2 . HIS   A 19  ? 0.5286 0.3632 0.5189 -0.0228 -0.0257 -0.0303 25  HIS   A CD2 
153  C  CE1 . HIS   A 19  ? 0.5541 0.3726 0.5468 -0.0250 -0.0230 -0.0328 25  HIS   A CE1 
154  N  NE2 . HIS   A 19  ? 0.5546 0.3856 0.5493 -0.0265 -0.0262 -0.0294 25  HIS   A NE2 
155  N  N   . ASN   A 20  ? 0.3830 0.2272 0.3752 -0.0060 -0.0196 -0.0248 26  ASN   A N   
156  C  CA  . ASN   A 20  ? 0.3824 0.2354 0.3835 -0.0045 -0.0195 -0.0197 26  ASN   A CA  
157  C  C   . ASN   A 20  ? 0.3711 0.2226 0.3745 0.0000  -0.0151 -0.0181 26  ASN   A C   
158  O  O   . ASN   A 20  ? 0.3712 0.2260 0.3807 -0.0009 -0.0138 -0.0156 26  ASN   A O   
159  C  CB  . ASN   A 20  ? 0.4131 0.2750 0.4165 -0.0036 -0.0220 -0.0170 26  ASN   A CB  
160  C  CG  . ASN   A 20  ? 0.4858 0.3563 0.5005 -0.0020 -0.0212 -0.0126 26  ASN   A CG  
161  O  OD1 . ASN   A 20  ? 0.5167 0.3922 0.5384 -0.0053 -0.0227 -0.0107 26  ASN   A OD1 
162  N  ND2 . ASN   A 20  ? 0.4950 0.3674 0.5123 0.0028  -0.0181 -0.0114 26  ASN   A ND2 
163  N  N   . ASP   A 21  ? 0.3571 0.2045 0.3555 0.0038  -0.0128 -0.0196 27  ASP   A N   
164  C  CA  . ASP   A 21  ? 0.3505 0.1967 0.3498 0.0069  -0.0092 -0.0178 27  ASP   A CA  
165  C  C   . ASP   A 21  ? 0.3543 0.1957 0.3558 0.0048  -0.0085 -0.0166 27  ASP   A C   
166  O  O   . ASP   A 21  ? 0.3509 0.1958 0.3559 0.0041  -0.0068 -0.0135 27  ASP   A O   
167  C  CB  . ASP   A 21  ? 0.3446 0.1870 0.3382 0.0107  -0.0076 -0.0193 27  ASP   A CB  
168  C  CG  . ASP   A 21  ? 0.3448 0.1921 0.3364 0.0129  -0.0079 -0.0191 27  ASP   A CG  
169  O  OD1 . ASP   A 21  ? 0.3306 0.1839 0.3268 0.0131  -0.0079 -0.0169 27  ASP   A OD1 
170  O  OD2 . ASP   A 21  ? 0.3568 0.2018 0.3427 0.0143  -0.0078 -0.0212 27  ASP   A OD2 
171  N  N   . TRP   A 22  ? 0.3491 0.1825 0.3487 0.0032  -0.0095 -0.0191 28  TRP   A N   
172  C  CA  . TRP   A 22  ? 0.3571 0.1848 0.3601 0.0009  -0.0094 -0.0174 28  TRP   A CA  
173  C  C   . TRP   A 22  ? 0.3544 0.1869 0.3622 -0.0039 -0.0110 -0.0149 28  TRP   A C   
174  O  O   . TRP   A 22  ? 0.3453 0.1777 0.3565 -0.0059 -0.0104 -0.0112 28  TRP   A O   
175  C  CB  . TRP   A 22  ? 0.3678 0.1845 0.3689 0.0005  -0.0095 -0.0215 28  TRP   A CB  
176  C  CG  . TRP   A 22  ? 0.3846 0.1962 0.3846 0.0054  -0.0068 -0.0225 28  TRP   A CG  
177  C  CD1 . TRP   A 22  ? 0.4001 0.2103 0.3951 0.0081  -0.0054 -0.0271 28  TRP   A CD1 
178  C  CD2 . TRP   A 22  ? 0.3916 0.2003 0.3964 0.0079  -0.0053 -0.0180 28  TRP   A CD2 
179  N  NE1 . TRP   A 22  ? 0.4064 0.2127 0.4035 0.0125  -0.0026 -0.0263 28  TRP   A NE1 
180  C  CE2 . TRP   A 22  ? 0.4016 0.2073 0.4053 0.0126  -0.0029 -0.0202 28  TRP   A CE2 
181  C  CE3 . TRP   A 22  ? 0.3948 0.2044 0.4049 0.0061  -0.0060 -0.0116 28  TRP   A CE3 
182  C  CZ2 . TRP   A 22  ? 0.4112 0.2147 0.4204 0.0159  -0.0014 -0.0159 28  TRP   A CZ2 
183  C  CZ3 . TRP   A 22  ? 0.4049 0.2123 0.4193 0.0087  -0.0050 -0.0069 28  TRP   A CZ3 
184  C  CH2 . TRP   A 22  ? 0.4146 0.2190 0.4293 0.0138  -0.0029 -0.0089 28  TRP   A CH2 
185  N  N   . ALA   A 23  ? 0.3562 0.1940 0.3644 -0.0063 -0.0133 -0.0163 29  ALA   A N   
186  C  CA  . ALA   A 23  ? 0.3592 0.2034 0.3732 -0.0108 -0.0148 -0.0139 29  ALA   A CA  
187  C  C   . ALA   A 23  ? 0.3516 0.2058 0.3709 -0.0095 -0.0121 -0.0106 29  ALA   A C   
188  O  O   . ALA   A 23  ? 0.3513 0.2115 0.3764 -0.0131 -0.0120 -0.0083 29  ALA   A O   
189  C  CB  . ALA   A 23  ? 0.3668 0.2145 0.3806 -0.0139 -0.0185 -0.0158 29  ALA   A CB  
190  N  N   . ASN   A 24  ? 0.3451 0.2012 0.3626 -0.0049 -0.0095 -0.0107 30  ASN   A N   
191  C  CA  . ASN   A 24  ? 0.3474 0.2114 0.3688 -0.0038 -0.0058 -0.0091 30  ASN   A CA  
192  C  C   . ASN   A 24  ? 0.3452 0.2063 0.3618 -0.0018 -0.0029 -0.0083 30  ASN   A C   
193  O  O   . ASN   A 24  ? 0.3410 0.2059 0.3572 0.0005  0.0001  -0.0088 30  ASN   A O   
194  C  CB  . ASN   A 24  ? 0.3660 0.2364 0.3913 -0.0008 -0.0058 -0.0099 30  ASN   A CB  
195  C  CG  . ASN   A 24  ? 0.4151 0.2909 0.4469 -0.0034 -0.0092 -0.0090 30  ASN   A CG  
196  O  OD1 . ASN   A 24  ? 0.4321 0.3156 0.4723 -0.0054 -0.0078 -0.0073 30  ASN   A OD1 
197  N  ND2 . ASN   A 24  ? 0.4231 0.2961 0.4512 -0.0041 -0.0136 -0.0101 30  ASN   A ND2 
198  N  N   . LEU   A 25  ? 0.3411 0.1954 0.3548 -0.0031 -0.0038 -0.0068 31  LEU   A N   
199  C  CA  . LEU   A 25  ? 0.3441 0.1959 0.3542 -0.0018 -0.0023 -0.0047 31  LEU   A CA  
200  C  C   . LEU   A 25  ? 0.3437 0.2023 0.3537 -0.0047 0.0009  -0.0020 31  LEU   A C   
201  O  O   . LEU   A 25  ? 0.3517 0.2141 0.3645 -0.0093 0.0013  0.0000  31  LEU   A O   
202  C  CB  . LEU   A 25  ? 0.3418 0.1850 0.3521 -0.0027 -0.0044 -0.0026 31  LEU   A CB  
203  C  CG  . LEU   A 25  ? 0.3524 0.1933 0.3610 -0.0009 -0.0037 0.0008  31  LEU   A CG  
204  C  CD1 . LEU   A 25  ? 0.3587 0.1984 0.3636 0.0044  -0.0027 -0.0022 31  LEU   A CD1 
205  C  CD2 . LEU   A 25  ? 0.3626 0.1954 0.3749 -0.0018 -0.0057 0.0042  31  LEU   A CD2 
206  N  N   . VAL   A 26  ? 0.3384 0.1986 0.3444 -0.0028 0.0031  -0.0020 32  VAL   A N   
207  C  CA  . VAL   A 26  ? 0.3294 0.1958 0.3331 -0.0067 0.0063  -0.0001 32  VAL   A CA  
208  C  C   . VAL   A 26  ? 0.3328 0.1966 0.3331 -0.0081 0.0046  0.0052  32  VAL   A C   
209  O  O   . VAL   A 26  ? 0.3266 0.1934 0.3265 -0.0135 0.0045  0.0096  32  VAL   A O   
210  C  CB  . VAL   A 26  ? 0.3149 0.1853 0.3167 -0.0047 0.0102  -0.0038 32  VAL   A CB  
211  C  CG1 . VAL   A 26  ? 0.3114 0.1866 0.3080 -0.0094 0.0137  -0.0025 32  VAL   A CG1 
212  C  CG2 . VAL   A 26  ? 0.3058 0.1802 0.3139 -0.0038 0.0123  -0.0074 32  VAL   A CG2 
213  N  N   . TRP   A 27  ? 0.3287 0.1877 0.3273 -0.0035 0.0032  0.0051  33  TRP   A N   
214  C  CA  . TRP   A 27  ? 0.3447 0.2021 0.3423 -0.0037 0.0015  0.0105  33  TRP   A CA  
215  C  C   . TRP   A 27  ? 0.3488 0.1998 0.3477 0.0025  0.0002  0.0090  33  TRP   A C   
216  O  O   . TRP   A 27  ? 0.3296 0.1797 0.3266 0.0062  0.0011  0.0039  33  TRP   A O   
217  C  CB  . TRP   A 27  ? 0.3550 0.2194 0.3468 -0.0068 0.0039  0.0120  33  TRP   A CB  
218  C  CG  . TRP   A 27  ? 0.3746 0.2397 0.3653 -0.0072 0.0019  0.0180  33  TRP   A CG  
219  C  CD1 . TRP   A 27  ? 0.3940 0.2617 0.3861 -0.0119 -0.0006 0.0260  33  TRP   A CD1 
220  C  CD2 . TRP   A 27  ? 0.3736 0.2385 0.3622 -0.0033 0.0019  0.0175  33  TRP   A CD2 
221  N  NE1 . TRP   A 27  ? 0.3990 0.2683 0.3911 -0.0108 -0.0023 0.0309  33  TRP   A NE1 
222  C  CE2 . TRP   A 27  ? 0.3879 0.2553 0.3779 -0.0054 -0.0006 0.0255  33  TRP   A CE2 
223  C  CE3 . TRP   A 27  ? 0.3761 0.2390 0.3626 0.0017  0.0035  0.0119  33  TRP   A CE3 
224  C  CZ2 . TRP   A 27  ? 0.3924 0.2613 0.3820 -0.0026 -0.0013 0.0276  33  TRP   A CZ2 
225  C  CZ3 . TRP   A 27  ? 0.3846 0.2484 0.3696 0.0040  0.0030  0.0137  33  TRP   A CZ3 
226  C  CH2 . TRP   A 27  ? 0.3886 0.2555 0.3753 0.0020  0.0008  0.0212  33  TRP   A CH2 
227  N  N   . GLU   A 28  ? 0.3489 0.1956 0.3518 0.0036  -0.0019 0.0136  34  GLU   A N   
228  C  CA  . GLU   A 28  ? 0.3457 0.1869 0.3509 0.0095  -0.0021 0.0119  34  GLU   A CA  
229  C  C   . GLU   A 28  ? 0.3567 0.1981 0.3667 0.0100  -0.0035 0.0192  34  GLU   A C   
230  O  O   . GLU   A 28  ? 0.3674 0.2098 0.3812 0.0061  -0.0055 0.0260  34  GLU   A O   
231  C  CB  . GLU   A 28  ? 0.3540 0.1866 0.3623 0.0118  -0.0025 0.0069  34  GLU   A CB  
232  C  CG  . GLU   A 28  ? 0.3693 0.1968 0.3835 0.0088  -0.0044 0.0100  34  GLU   A CG  
233  C  CD  . GLU   A 28  ? 0.4281 0.2493 0.4505 0.0108  -0.0054 0.0151  34  GLU   A CD  
234  O  OE1 . GLU   A 28  ? 0.4680 0.2868 0.4956 0.0073  -0.0074 0.0205  34  GLU   A OE1 
235  O  OE2 . GLU   A 28  ? 0.4281 0.2472 0.4527 0.0157  -0.0041 0.0142  34  GLU   A OE2 
236  N  N   . ASP   A 29  ? 0.3463 0.1877 0.3570 0.0146  -0.0026 0.0187  35  ASP   A N   
237  C  CA  . ASP   A 29  ? 0.3591 0.2015 0.3767 0.0160  -0.0040 0.0261  35  ASP   A CA  
238  C  C   . ASP   A 29  ? 0.3661 0.2040 0.3883 0.0229  -0.0021 0.0225  35  ASP   A C   
239  O  O   . ASP   A 29  ? 0.3714 0.2130 0.3886 0.0250  -0.0005 0.0194  35  ASP   A O   
240  C  CB  . ASP   A 29  ? 0.3809 0.2336 0.3937 0.0119  -0.0048 0.0318  35  ASP   A CB  
241  C  CG  . ASP   A 29  ? 0.4400 0.2965 0.4607 0.0113  -0.0075 0.0422  35  ASP   A CG  
242  O  OD1 . ASP   A 29  ? 0.4487 0.3002 0.4796 0.0170  -0.0076 0.0437  35  ASP   A OD1 
243  O  OD2 . ASP   A 29  ? 0.4720 0.3368 0.4890 0.0050  -0.0095 0.0489  35  ASP   A OD2 
244  N  N   . SER   A 30  ? 0.3557 0.1853 0.3876 0.0261  -0.0019 0.0229  36  SER   A N   
245  C  CA  A SER   A 30  ? 0.3567 0.1814 0.3944 0.0325  0.0010  0.0188  36  SER   A CA  
246  C  CA  B SER   A 30  ? 0.3561 0.1810 0.3934 0.0325  0.0010  0.0186  36  SER   A CA  
247  C  C   . SER   A 30  ? 0.3514 0.1837 0.3933 0.0353  0.0013  0.0243  36  SER   A C   
248  O  O   . SER   A 30  ? 0.3628 0.1961 0.4031 0.0392  0.0042  0.0193  36  SER   A O   
249  C  CB  A SER   A 30  ? 0.3633 0.1773 0.4126 0.0349  0.0017  0.0187  36  SER   A CB  
250  C  CB  B SER   A 30  ? 0.3606 0.1743 0.4085 0.0350  0.0020  0.0172  36  SER   A CB  
251  O  OG  A SER   A 30  ? 0.3765 0.1858 0.4325 0.0410  0.0057  0.0140  36  SER   A OG  
252  O  OG  B SER   A 30  ? 0.3674 0.1809 0.4258 0.0335  -0.0010 0.0275  36  SER   A OG  
253  N  N   . SER   A 31  ? 0.3416 0.1804 0.3888 0.0325  -0.0020 0.0351  37  SER   A N   
254  C  CA  . SER   A 31  ? 0.3346 0.1820 0.3865 0.0342  -0.0026 0.0417  37  SER   A CA  
255  C  C   . SER   A 31  ? 0.3336 0.1886 0.3730 0.0328  -0.0015 0.0378  37  SER   A C   
256  O  O   . SER   A 31  ? 0.3515 0.2122 0.3941 0.0354  -0.0007 0.0401  37  SER   A O   
257  C  CB  . SER   A 31  ? 0.3420 0.1961 0.4007 0.0298  -0.0073 0.0551  37  SER   A CB  
258  O  OG  . SER   A 31  ? 0.3826 0.2441 0.4291 0.0218  -0.0098 0.0576  37  SER   A OG  
259  N  N   . ARG   A 32  ? 0.3155 0.1708 0.3421 0.0286  -0.0014 0.0325  38  ARG   A N   
260  C  CA  . ARG   A 32  ? 0.3098 0.1704 0.3251 0.0270  -0.0003 0.0285  38  ARG   A CA  
261  C  C   . ARG   A 32  ? 0.3125 0.1677 0.3222 0.0305  0.0026  0.0182  38  ARG   A C   
262  O  O   . ARG   A 32  ? 0.3061 0.1649 0.3081 0.0299  0.0036  0.0152  38  ARG   A O   
263  C  CB  . ARG   A 32  ? 0.3087 0.1733 0.3148 0.0198  -0.0016 0.0295  38  ARG   A CB  
264  C  CG  . ARG   A 32  ? 0.3205 0.1926 0.3282 0.0140  -0.0046 0.0395  38  ARG   A CG  
265  C  CD  . ARG   A 32  ? 0.3476 0.2237 0.3451 0.0063  -0.0046 0.0388  38  ARG   A CD  
266  N  NE  . ARG   A 32  ? 0.3531 0.2320 0.3408 0.0049  -0.0023 0.0334  38  ARG   A NE  
267  C  CZ  . ARG   A 32  ? 0.3740 0.2584 0.3530 -0.0024 -0.0016 0.0336  38  ARG   A CZ  
268  N  NH1 . ARG   A 32  ? 0.3413 0.2304 0.3188 -0.0095 -0.0032 0.0392  38  ARG   A NH1 
269  N  NH2 . ARG   A 32  ? 0.3591 0.2444 0.3306 -0.0032 0.0008  0.0284  38  ARG   A NH2 
270  N  N   . ASP   A 33  ? 0.3049 0.1517 0.3182 0.0331  0.0038  0.0133  39  ASP   A N   
271  C  CA  . ASP   A 33  ? 0.3084 0.1510 0.3158 0.0348  0.0058  0.0042  39  ASP   A CA  
272  C  C   . ASP   A 33  ? 0.3129 0.1574 0.3112 0.0308  0.0047  0.0017  39  ASP   A C   
273  O  O   . ASP   A 33  ? 0.3316 0.1767 0.3237 0.0314  0.0055  -0.0032 39  ASP   A O   
274  C  CB  . ASP   A 33  ? 0.3324 0.1774 0.3382 0.0384  0.0083  0.0011  39  ASP   A CB  
275  C  CG  . ASP   A 33  ? 0.3643 0.2056 0.3635 0.0391  0.0100  -0.0076 39  ASP   A CG  
276  O  OD1 . ASP   A 33  ? 0.3362 0.1707 0.3360 0.0385  0.0101  -0.0118 39  ASP   A OD1 
277  O  OD2 . ASP   A 33  ? 0.3879 0.2334 0.3810 0.0394  0.0109  -0.0097 39  ASP   A OD2 
278  N  N   . LEU   A 34  ? 0.2973 0.1430 0.2956 0.0267  0.0030  0.0051  40  LEU   A N   
279  C  CA  . LEU   A 34  ? 0.2935 0.1413 0.2855 0.0234  0.0029  0.0025  40  LEU   A CA  
280  C  C   . LEU   A 34  ? 0.3076 0.1517 0.3017 0.0212  0.0020  0.0011  40  LEU   A C   
281  O  O   . LEU   A 34  ? 0.3058 0.1474 0.3051 0.0200  0.0009  0.0047  40  LEU   A O   
282  C  CB  . LEU   A 34  ? 0.2911 0.1455 0.2796 0.0193  0.0030  0.0065  40  LEU   A CB  
283  C  CG  . LEU   A 34  ? 0.3052 0.1642 0.2895 0.0198  0.0038  0.0072  40  LEU   A CG  
284  C  CD1 . LEU   A 34  ? 0.3010 0.1658 0.2809 0.0141  0.0041  0.0104  40  LEU   A CD1 
285  C  CD2 . LEU   A 34  ? 0.3075 0.1651 0.2876 0.0221  0.0049  0.0014  40  LEU   A CD2 
286  N  N   . LEU   A 35  ? 0.3078 0.1526 0.2985 0.0201  0.0023  -0.0031 41  LEU   A N   
287  C  CA  . LEU   A 35  ? 0.3144 0.1579 0.3070 0.0175  0.0014  -0.0044 41  LEU   A CA  
288  C  C   . LEU   A 35  ? 0.3232 0.1717 0.3135 0.0160  0.0025  -0.0063 41  LEU   A C   
289  O  O   . LEU   A 35  ? 0.3284 0.1783 0.3159 0.0180  0.0031  -0.0084 41  LEU   A O   
290  C  CB  . LEU   A 35  ? 0.2998 0.1373 0.2935 0.0188  0.0004  -0.0087 41  LEU   A CB  
291  C  CG  . LEU   A 35  ? 0.3151 0.1513 0.3114 0.0154  -0.0010 -0.0094 41  LEU   A CG  
292  C  CD1 . LEU   A 35  ? 0.3257 0.1539 0.3246 0.0153  -0.0019 -0.0114 41  LEU   A CD1 
293  C  CD2 . LEU   A 35  ? 0.3115 0.1519 0.3063 0.0145  -0.0017 -0.0124 41  LEU   A CD2 
294  N  N   . VAL   A 36  ? 0.3030 0.1544 0.2952 0.0123  0.0031  -0.0051 42  VAL   A N   
295  C  CA  . VAL   A 36  ? 0.3039 0.1600 0.2965 0.0110  0.0051  -0.0072 42  VAL   A CA  
296  C  C   . VAL   A 36  ? 0.3138 0.1706 0.3112 0.0092  0.0042  -0.0082 42  VAL   A C   
297  O  O   . VAL   A 36  ? 0.3224 0.1787 0.3217 0.0062  0.0035  -0.0060 42  VAL   A O   
298  C  CB  . VAL   A 36  ? 0.3027 0.1636 0.2929 0.0074  0.0081  -0.0057 42  VAL   A CB  
299  C  CG1 . VAL   A 36  ? 0.3116 0.1764 0.3043 0.0066  0.0114  -0.0090 42  VAL   A CG1 
300  C  CG2 . VAL   A 36  ? 0.3064 0.1675 0.2915 0.0082  0.0085  -0.0042 42  VAL   A CG2 
301  N  N   . SER   A 37  ? 0.3072 0.1658 0.3074 0.0108  0.0039  -0.0107 43  SER   A N   
302  C  CA  . SER   A 37  ? 0.3134 0.1746 0.3195 0.0088  0.0028  -0.0110 43  SER   A CA  
303  C  C   . SER   A 37  ? 0.3161 0.1838 0.3278 0.0088  0.0060  -0.0120 43  SER   A C   
304  O  O   . SER   A 37  ? 0.3040 0.1725 0.3146 0.0108  0.0085  -0.0130 43  SER   A O   
305  C  CB  . SER   A 37  ? 0.3210 0.1795 0.3272 0.0099  -0.0011 -0.0124 43  SER   A CB  
306  O  OG  . SER   A 37  ? 0.3459 0.2055 0.3510 0.0129  -0.0017 -0.0134 43  SER   A OG  
307  N  N   . SER   A 38  ? 0.3289 0.2012 0.3474 0.0064  0.0063  -0.0116 44  SER   A N   
308  C  CA  . SER   A 38  ? 0.3382 0.2171 0.3648 0.0069  0.0102  -0.0128 44  SER   A CA  
309  C  C   . SER   A 38  ? 0.3390 0.2201 0.3728 0.0101  0.0075  -0.0124 44  SER   A C   
310  O  O   . SER   A 38  ? 0.3313 0.2109 0.3640 0.0099  0.0023  -0.0112 44  SER   A O   
311  C  CB  . SER   A 38  ? 0.3650 0.2496 0.3970 0.0027  0.0127  -0.0124 44  SER   A CB  
312  O  OG  . SER   A 38  ? 0.4100 0.2953 0.4457 0.0011  0.0081  -0.0106 44  SER   A OG  
313  N  N   . THR   A 39  ? 0.3355 0.2201 0.3768 0.0127  0.0111  -0.0133 45  THR   A N   
314  C  CA  . THR   A 39  ? 0.3353 0.2228 0.3855 0.0159  0.0082  -0.0114 45  THR   A CA  
315  C  C   . THR   A 39  ? 0.3475 0.2426 0.4130 0.0168  0.0120  -0.0111 45  THR   A C   
316  O  O   . THR   A 39  ? 0.3455 0.2424 0.4134 0.0157  0.0186  -0.0141 45  THR   A O   
317  C  CB  . THR   A 39  ? 0.3472 0.2304 0.3938 0.0194  0.0081  -0.0115 45  THR   A CB  
318  O  OG1 . THR   A 39  ? 0.3493 0.2315 0.3971 0.0203  0.0148  -0.0145 45  THR   A OG1 
319  C  CG2 . THR   A 39  ? 0.3562 0.2333 0.3894 0.0190  0.0047  -0.0117 45  THR   A CG2 
320  N  N   . THR   A 40  ? 0.3510 0.2512 0.4276 0.0185  0.0080  -0.0074 46  THR   A N   
321  C  CA  . THR   A 40  ? 0.3684 0.2768 0.4630 0.0202  0.0113  -0.0063 46  THR   A CA  
322  C  C   . THR   A 40  ? 0.3671 0.2736 0.4696 0.0250  0.0161  -0.0074 46  THR   A C   
323  O  O   . THR   A 40  ? 0.3683 0.2777 0.4811 0.0262  0.0236  -0.0105 46  THR   A O   
324  C  CB  . THR   A 40  ? 0.4076 0.3236 0.5120 0.0194  0.0044  -0.0006 46  THR   A CB  
325  O  OG1 . THR   A 40  ? 0.4339 0.3477 0.5354 0.0208  -0.0021 0.0031  46  THR   A OG1 
326  C  CG2 . THR   A 40  ? 0.4200 0.3372 0.5175 0.0139  0.0008  -0.0004 46  THR   A CG2 
327  N  N   . ALA   A 41  ? 0.3741 0.2754 0.4716 0.0273  0.0122  -0.0055 47  ALA   A N   
328  C  CA  . ALA   A 41  ? 0.3859 0.2839 0.4902 0.0315  0.0160  -0.0061 47  ALA   A CA  
329  C  C   . ALA   A 41  ? 0.3922 0.2822 0.4834 0.0306  0.0218  -0.0121 47  ALA   A C   
330  O  O   . ALA   A 41  ? 0.3962 0.2824 0.4713 0.0277  0.0197  -0.0134 47  ALA   A O   
331  C  CB  . ALA   A 41  ? 0.3955 0.2924 0.5001 0.0334  0.0085  -0.0003 47  ALA   A CB  
332  N  N   . GLN   A 42  ? 0.3826 0.2701 0.4814 0.0328  0.0292  -0.0158 48  GLN   A N   
333  C  CA  . GLN   A 42  ? 0.3812 0.2617 0.4679 0.0309  0.0347  -0.0214 48  GLN   A CA  
334  C  C   . GLN   A 42  ? 0.3758 0.2498 0.4547 0.0325  0.0304  -0.0191 48  GLN   A C   
335  O  O   . GLN   A 42  ? 0.3697 0.2434 0.4587 0.0361  0.0271  -0.0147 48  GLN   A O   
336  C  CB  . GLN   A 42  ? 0.4094 0.2893 0.5064 0.0316  0.0449  -0.0274 48  GLN   A CB  
337  C  CG  . GLN   A 42  ? 0.4793 0.3641 0.5743 0.0272  0.0514  -0.0324 48  GLN   A CG  
338  C  CD  . GLN   A 42  ? 0.5618 0.4451 0.6637 0.0268  0.0627  -0.0400 48  GLN   A CD  
339  O  OE1 . GLN   A 42  ? 0.5732 0.4557 0.6926 0.0317  0.0664  -0.0405 48  GLN   A OE1 
340  N  NE2 . GLN   A 42  ? 0.5868 0.4701 0.6758 0.0205  0.0685  -0.0458 48  GLN   A NE2 
341  N  N   . GLY   A 43  ? 0.3631 0.2329 0.4248 0.0294  0.0298  -0.0210 49  GLY   A N   
342  C  CA  . GLY   A 43  ? 0.3684 0.2329 0.4210 0.0300  0.0262  -0.0191 49  GLY   A CA  
343  C  C   . GLY   A 43  ? 0.3654 0.2240 0.4187 0.0303  0.0319  -0.0227 49  GLY   A C   
344  O  O   . GLY   A 43  ? 0.3631 0.2210 0.4210 0.0291  0.0396  -0.0280 49  GLY   A O   
345  N  N   . CYS   A 44  ? 0.3708 0.2250 0.4189 0.0312  0.0283  -0.0201 50  CYS   A N   
346  C  CA  . CYS   A 44  ? 0.3751 0.2228 0.4239 0.0312  0.0328  -0.0228 50  CYS   A CA  
347  C  C   . CYS   A 44  ? 0.3688 0.2129 0.4007 0.0270  0.0335  -0.0251 50  CYS   A C   
348  O  O   . CYS   A 44  ? 0.3738 0.2122 0.4046 0.0256  0.0380  -0.0285 50  CYS   A O   
349  C  CB  . CYS   A 44  ? 0.3814 0.2269 0.4408 0.0352  0.0288  -0.0173 50  CYS   A CB  
350  S  SG  . CYS   A 44  ? 0.4129 0.2622 0.4971 0.0401  0.0297  -0.0143 50  CYS   A SG  
351  N  N   . ASP   A 45  ? 0.3507 0.1979 0.3705 0.0251  0.0290  -0.0231 51  ASP   A N   
352  C  CA  . ASP   A 45  ? 0.3445 0.1901 0.3503 0.0214  0.0291  -0.0240 51  ASP   A CA  
353  C  C   . ASP   A 45  ? 0.3571 0.2027 0.3571 0.0162  0.0355  -0.0293 51  ASP   A C   
354  O  O   . ASP   A 45  ? 0.3569 0.2057 0.3603 0.0150  0.0385  -0.0316 51  ASP   A O   
355  C  CB  . ASP   A 45  ? 0.3260 0.1749 0.3230 0.0214  0.0232  -0.0201 51  ASP   A CB  
356  C  CG  . ASP   A 45  ? 0.3415 0.1910 0.3408 0.0248  0.0172  -0.0155 51  ASP   A CG  
357  O  OD1 . ASP   A 45  ? 0.3436 0.1902 0.3442 0.0257  0.0163  -0.0139 51  ASP   A OD1 
358  O  OD2 . ASP   A 45  ? 0.3452 0.1979 0.3443 0.0259  0.0133  -0.0136 51  ASP   A OD2 
359  N  N   . THR   A 46  ? 0.3621 0.2048 0.3531 0.0122  0.0375  -0.0311 52  THR   A N   
360  C  CA  . THR   A 46  ? 0.3801 0.2237 0.3627 0.0054  0.0428  -0.0357 52  THR   A CA  
361  C  C   . THR   A 46  ? 0.3778 0.2252 0.3479 0.0018  0.0385  -0.0318 52  THR   A C   
362  O  O   . THR   A 46  ? 0.3973 0.2436 0.3640 0.0033  0.0345  -0.0283 52  THR   A O   
363  C  CB  . THR   A 46  ? 0.4126 0.2498 0.3947 0.0023  0.0490  -0.0412 52  THR   A CB  
364  O  OG1 . THR   A 46  ? 0.4425 0.2764 0.4390 0.0062  0.0539  -0.0449 52  THR   A OG1 
365  C  CG2 . THR   A 46  ? 0.4334 0.2722 0.4038 -0.0066 0.0541  -0.0460 52  THR   A CG2 
366  N  N   . ILE   A 47  ? 0.3634 0.2159 0.3273 -0.0032 0.0394  -0.0317 53  ILE   A N   
367  C  CA  . ILE   A 47  ? 0.3643 0.2211 0.3189 -0.0064 0.0350  -0.0268 53  ILE   A CA  
368  C  C   . ILE   A 47  ? 0.3716 0.2283 0.3163 -0.0138 0.0376  -0.0287 53  ILE   A C   
369  O  O   . ILE   A 47  ? 0.3697 0.2255 0.3117 -0.0194 0.0437  -0.0344 53  ILE   A O   
370  C  CB  . ILE   A 47  ? 0.3629 0.2255 0.3163 -0.0087 0.0335  -0.0240 53  ILE   A CB  
371  C  CG1 . ILE   A 47  ? 0.3697 0.2319 0.3327 -0.0025 0.0314  -0.0230 53  ILE   A CG1 
372  C  CG2 . ILE   A 47  ? 0.3677 0.2347 0.3147 -0.0107 0.0283  -0.0174 53  ILE   A CG2 
373  C  CD1 . ILE   A 47  ? 0.3804 0.2407 0.3467 0.0042  0.0259  -0.0194 53  ILE   A CD1 
374  N  N   . ALA   A 48  ? 0.3738 0.2320 0.3131 -0.0143 0.0334  -0.0241 54  ALA   A N   
375  C  CA  . ALA   A 48  ? 0.3802 0.2397 0.3096 -0.0222 0.0347  -0.0247 54  ALA   A CA  
376  C  C   . ALA   A 48  ? 0.3863 0.2534 0.3083 -0.0302 0.0345  -0.0224 54  ALA   A C   
377  O  O   . ALA   A 48  ? 0.3844 0.2565 0.3089 -0.0282 0.0305  -0.0169 54  ALA   A O   
378  C  CB  . ALA   A 48  ? 0.3800 0.2410 0.3071 -0.0204 0.0297  -0.0193 54  ALA   A CB  
379  N  N   . ARG   A 49  ? 0.3839 0.2519 0.2965 -0.0398 0.0385  -0.0262 55  ARG   A N   
380  C  CA  . ARG   A 49  ? 0.3873 0.2637 0.2913 -0.0493 0.0380  -0.0233 55  ARG   A CA  
381  C  C   . ARG   A 49  ? 0.4058 0.2848 0.2994 -0.0575 0.0367  -0.0217 55  ARG   A C   
382  O  O   . ARG   A 49  ? 0.4062 0.2820 0.2921 -0.0652 0.0423  -0.0289 55  ARG   A O   
383  C  CB  . ARG   A 49  ? 0.3918 0.2677 0.2934 -0.0549 0.0452  -0.0309 55  ARG   A CB  
384  C  CG  . ARG   A 49  ? 0.4150 0.2893 0.3278 -0.0473 0.0465  -0.0322 55  ARG   A CG  
385  C  CD  . ARG   A 49  ? 0.4063 0.2861 0.3236 -0.0434 0.0398  -0.0234 55  ARG   A CD  
386  N  NE  . ARG   A 49  ? 0.3800 0.2573 0.3077 -0.0365 0.0411  -0.0255 55  ARG   A NE  
387  C  CZ  . ARG   A 49  ? 0.3843 0.2628 0.3188 -0.0306 0.0360  -0.0199 55  ARG   A CZ  
388  N  NH1 . ARG   A 49  ? 0.3567 0.2387 0.2898 -0.0302 0.0297  -0.0120 55  ARG   A NH1 
389  N  NH2 . ARG   A 49  ? 0.3713 0.2478 0.3146 -0.0255 0.0374  -0.0223 55  ARG   A NH2 
390  N  N   . CYS   A 50  ? 0.4072 0.2917 0.3017 -0.0555 0.0298  -0.0128 56  CYS   A N   
391  C  CA  . CYS   A 50  ? 0.4228 0.3102 0.3098 -0.0617 0.0277  -0.0102 56  CYS   A CA  
392  C  C   . CYS   A 50  ? 0.4236 0.3207 0.3136 -0.0600 0.0200  0.0014  56  CYS   A C   
393  O  O   . CYS   A 50  ? 0.4241 0.3240 0.3222 -0.0537 0.0168  0.0066  56  CYS   A O   
394  C  CB  . CYS   A 50  ? 0.4411 0.3191 0.3316 -0.0558 0.0298  -0.0151 56  CYS   A CB  
395  S  SG  . CYS   A 50  ? 0.4629 0.3393 0.3662 -0.0415 0.0249  -0.0099 56  CYS   A SG  
396  N  N   . ASP   A 51  ? 0.4383 0.3397 0.3237 -0.0645 0.0172  0.0052  57  ASP   A N   
397  C  CA  . ASP   A 51  ? 0.4640 0.3748 0.3548 -0.0619 0.0106  0.0161  57  ASP   A CA  
398  C  C   . ASP   A 51  ? 0.4731 0.3821 0.3672 -0.0568 0.0093  0.0169  57  ASP   A C   
399  O  O   . ASP   A 51  ? 0.4871 0.4052 0.3828 -0.0582 0.0048  0.0249  57  ASP   A O   
400  C  CB  . ASP   A 51  ? 0.5185 0.4419 0.4028 -0.0735 0.0066  0.0242  57  ASP   A CB  
401  C  CG  . ASP   A 51  ? 0.6153 0.5409 0.4866 -0.0859 0.0078  0.0218  57  ASP   A CG  
402  O  OD1 . ASP   A 51  ? 0.6225 0.5379 0.4889 -0.0864 0.0130  0.0121  57  ASP   A OD1 
403  O  OD2 . ASP   A 51  ? 0.6724 0.6099 0.5386 -0.0956 0.0033  0.0299  57  ASP   A OD2 
404  N  N   . CYS   A 52  ? 0.4604 0.3586 0.3566 -0.0506 0.0129  0.0094  58  CYS   A N   
405  C  CA  . CYS   A 52  ? 0.4394 0.3351 0.3386 -0.0455 0.0119  0.0100  58  CYS   A CA  
406  C  C   . CYS   A 52  ? 0.4134 0.3167 0.3217 -0.0380 0.0074  0.0179  58  CYS   A C   
407  O  O   . CYS   A 52  ? 0.4208 0.3253 0.3361 -0.0322 0.0063  0.0200  58  CYS   A O   
408  C  CB  . CYS   A 52  ? 0.4497 0.3334 0.3521 -0.0391 0.0156  0.0023  58  CYS   A CB  
409  S  SG  . CYS   A 52  ? 0.4659 0.3390 0.3604 -0.0468 0.0219  -0.0074 58  CYS   A SG  
410  N  N   . GLN   A 53  ? 0.3854 0.2936 0.2938 -0.0386 0.0052  0.0219  59  GLN   A N   
411  C  CA  . GLN   A 53  ? 0.3595 0.2745 0.2772 -0.0313 0.0024  0.0280  59  GLN   A CA  
412  C  C   . GLN   A 53  ? 0.3347 0.2454 0.2534 -0.0263 0.0034  0.0254  59  GLN   A C   
413  O  O   . GLN   A 53  ? 0.3289 0.2458 0.2537 -0.0216 0.0019  0.0296  59  GLN   A O   
414  C  CB  . GLN   A 53  ? 0.3774 0.3060 0.2970 -0.0361 -0.0016 0.0374  59  GLN   A CB  
415  C  CG  . GLN   A 53  ? 0.4281 0.3628 0.3514 -0.0378 -0.0038 0.0429  59  GLN   A CG  
416  C  CD  . GLN   A 53  ? 0.4874 0.4366 0.4169 -0.0403 -0.0084 0.0540  59  GLN   A CD  
417  O  OE1 . GLN   A 53  ? 0.5009 0.4582 0.4252 -0.0504 -0.0113 0.0594  59  GLN   A OE1 
418  N  NE2 . GLN   A 53  ? 0.4856 0.4391 0.4266 -0.0318 -0.0090 0.0577  59  GLN   A NE2 
419  N  N   . THR   A 54  ? 0.3353 0.2355 0.2491 -0.0274 0.0061  0.0186  60  THR   A N   
420  C  CA  . THR   A 54  ? 0.3437 0.2388 0.2588 -0.0230 0.0066  0.0166  60  THR   A CA  
421  C  C   . THR   A 54  ? 0.3372 0.2210 0.2540 -0.0187 0.0092  0.0101  60  THR   A C   
422  O  O   . THR   A 54  ? 0.3471 0.2250 0.2614 -0.0219 0.0118  0.0056  60  THR   A O   
423  C  CB  . THR   A 54  ? 0.3863 0.2812 0.2951 -0.0298 0.0064  0.0172  60  THR   A CB  
424  O  OG1 . THR   A 54  ? 0.4267 0.3129 0.3291 -0.0363 0.0092  0.0115  60  THR   A OG1 
425  C  CG2 . THR   A 54  ? 0.3914 0.2989 0.2993 -0.0347 0.0036  0.0242  60  THR   A CG2 
426  N  N   . GLY   A 55  ? 0.3147 0.1965 0.2361 -0.0118 0.0086  0.0100  61  GLY   A N   
427  C  CA  . GLY   A 55  ? 0.3145 0.1875 0.2392 -0.0075 0.0100  0.0055  61  GLY   A CA  
428  C  C   . GLY   A 55  ? 0.3054 0.1781 0.2330 -0.0024 0.0084  0.0068  61  GLY   A C   
429  O  O   . GLY   A 55  ? 0.3092 0.1870 0.2350 -0.0032 0.0069  0.0102  61  GLY   A O   
430  N  N   . VAL   A 56  ? 0.2876 0.1556 0.2194 0.0023  0.0084  0.0045  62  VAL   A N   
431  C  CA  . VAL   A 56  ? 0.2775 0.1454 0.2112 0.0061  0.0065  0.0058  62  VAL   A CA  
432  C  C   . VAL   A 56  ? 0.2779 0.1462 0.2156 0.0111  0.0061  0.0042  62  VAL   A C   
433  O  O   . VAL   A 56  ? 0.2848 0.1492 0.2255 0.0119  0.0072  0.0015  62  VAL   A O   
434  C  CB  . VAL   A 56  ? 0.2900 0.1501 0.2252 0.0049  0.0064  0.0052  62  VAL   A CB  
435  C  CG1 . VAL   A 56  ? 0.3053 0.1654 0.2430 0.0081  0.0037  0.0072  62  VAL   A CG1 
436  C  CG2 . VAL   A 56  ? 0.2953 0.1541 0.2261 -0.0006 0.0068  0.0066  62  VAL   A CG2 
437  N  N   . TYR   A 57  ? 0.2852 0.1583 0.2229 0.0139  0.0049  0.0052  63  TYR   A N   
438  C  CA  . TYR   A 57  ? 0.2897 0.1623 0.2304 0.0178  0.0046  0.0030  63  TYR   A CA  
439  C  C   . TYR   A 57  ? 0.2960 0.1687 0.2359 0.0189  0.0025  0.0032  63  TYR   A C   
440  O  O   . TYR   A 57  ? 0.3072 0.1829 0.2437 0.0172  0.0016  0.0055  63  TYR   A O   
441  C  CB  . TYR   A 57  ? 0.2967 0.1744 0.2388 0.0198  0.0057  0.0029  63  TYR   A CB  
442  C  CG  . TYR   A 57  ? 0.3121 0.1957 0.2528 0.0211  0.0062  0.0035  63  TYR   A CG  
443  C  CD1 . TYR   A 57  ? 0.3218 0.2112 0.2605 0.0191  0.0065  0.0065  63  TYR   A CD1 
444  C  CD2 . TYR   A 57  ? 0.3189 0.2029 0.2603 0.0238  0.0067  0.0007  63  TYR   A CD2 
445  C  CE1 . TYR   A 57  ? 0.3218 0.2177 0.2600 0.0202  0.0078  0.0067  63  TYR   A CE1 
446  C  CE2 . TYR   A 57  ? 0.3191 0.2087 0.2590 0.0246  0.0083  0.0000  63  TYR   A CE2 
447  C  CZ  . TYR   A 57  ? 0.3251 0.2210 0.2637 0.0230  0.0090  0.0031  63  TYR   A CZ  
448  O  OH  . TYR   A 57  ? 0.3430 0.2455 0.2810 0.0237  0.0115  0.0022  63  TYR   A OH  
449  N  N   . TYR   A 58  ? 0.2862 0.1568 0.2287 0.0209  0.0016  0.0012  64  TYR   A N   
450  C  CA  . TYR   A 58  ? 0.2891 0.1610 0.2300 0.0207  -0.0010 0.0019  64  TYR   A CA  
451  C  C   . TYR   A 58  ? 0.2997 0.1760 0.2374 0.0216  0.0000  -0.0006 64  TYR   A C   
452  O  O   . TYR   A 58  ? 0.3009 0.1761 0.2409 0.0237  0.0016  -0.0036 64  TYR   A O   
453  C  CB  . TYR   A 58  ? 0.2915 0.1597 0.2374 0.0213  -0.0032 0.0019  64  TYR   A CB  
454  C  CG  . TYR   A 58  ? 0.2913 0.1623 0.2352 0.0198  -0.0068 0.0039  64  TYR   A CG  
455  C  CD1 . TYR   A 58  ? 0.3004 0.1734 0.2419 0.0172  -0.0091 0.0083  64  TYR   A CD1 
456  C  CD2 . TYR   A 58  ? 0.2911 0.1632 0.2348 0.0199  -0.0081 0.0018  64  TYR   A CD2 
457  C  CE1 . TYR   A 58  ? 0.3112 0.1881 0.2498 0.0146  -0.0130 0.0111  64  TYR   A CE1 
458  C  CE2 . TYR   A 58  ? 0.3047 0.1806 0.2450 0.0171  -0.0117 0.0038  64  TYR   A CE2 
459  C  CZ  . TYR   A 58  ? 0.3228 0.2015 0.2605 0.0143  -0.0143 0.0088  64  TYR   A CZ  
460  O  OH  . TYR   A 58  ? 0.3479 0.2315 0.2816 0.0103  -0.0184 0.0117  64  TYR   A OH  
461  N  N   . CYS   A 59  ? 0.2989 0.1800 0.2313 0.0196  -0.0006 0.0005  65  CYS   A N   
462  C  CA  . CYS   A 59  ? 0.3045 0.1902 0.2331 0.0197  0.0015  -0.0029 65  CYS   A CA  
463  C  C   . CYS   A 59  ? 0.3063 0.1933 0.2303 0.0168  -0.0013 -0.0034 65  CYS   A C   
464  O  O   . CYS   A 59  ? 0.3068 0.1976 0.2264 0.0132  -0.0036 0.0001  65  CYS   A O   
465  C  CB  . CYS   A 59  ? 0.3253 0.2173 0.2508 0.0187  0.0038  -0.0016 65  CYS   A CB  
466  S  SG  . CYS   A 59  ? 0.3746 0.2729 0.2959 0.0186  0.0079  -0.0067 65  CYS   A SG  
467  N  N   . SER   A 60  ? 0.2978 0.1820 0.2228 0.0174  -0.0016 -0.0070 66  SER   A N   
468  C  CA  . SER   A 60  ? 0.3184 0.2047 0.2387 0.0135  -0.0050 -0.0071 66  SER   A CA  
469  C  C   . SER   A 60  ? 0.3230 0.2159 0.2338 0.0094  -0.0036 -0.0091 66  SER   A C   
470  O  O   . SER   A 60  ? 0.3419 0.2389 0.2474 0.0043  -0.0076 -0.0057 66  SER   A O   
471  C  CB  . SER   A 60  ? 0.3640 0.2463 0.2868 0.0142  -0.0054 -0.0109 66  SER   A CB  
472  O  OG  . SER   A 60  ? 0.4260 0.3072 0.3469 0.0154  -0.0009 -0.0176 66  SER   A OG  
473  N  N   . SER   A 61  ? 0.3085 0.2033 0.2179 0.0112  0.0022  -0.0140 67  SER   A N   
474  C  CA  . SER   A 61  ? 0.3092 0.2107 0.2103 0.0076  0.0055  -0.0174 67  SER   A CA  
475  C  C   . SER   A 61  ? 0.3183 0.2267 0.2149 0.0041  0.0038  -0.0116 67  SER   A C   
476  O  O   . SER   A 61  ? 0.3252 0.2405 0.2139 -0.0001 0.0061  -0.0138 67  SER   A O   
477  C  CB  . SER   A 61  ? 0.3142 0.2157 0.2187 0.0117  0.0128  -0.0239 67  SER   A CB  
478  O  OG  . SER   A 61  ? 0.3129 0.2143 0.2251 0.0163  0.0142  -0.0205 67  SER   A OG  
479  N  N   . ARG   A 62  ? 0.3116 0.2177 0.2129 0.0051  -0.0001 -0.0046 68  ARG   A N   
480  C  CA  . ARG   A 62  ? 0.3190 0.2297 0.2173 0.0017  -0.0024 0.0018  68  ARG   A CA  
481  C  C   . ARG   A 62  ? 0.3321 0.2390 0.2338 0.0001  -0.0091 0.0092  68  ARG   A C   
482  O  O   . ARG   A 62  ? 0.3466 0.2555 0.2472 -0.0028 -0.0117 0.0154  68  ARG   A O   
483  C  CB  . ARG   A 62  ? 0.3436 0.2548 0.2463 0.0048  0.0008  0.0029  68  ARG   A CB  
484  C  CG  . ARG   A 62  ? 0.3608 0.2776 0.2631 0.0067  0.0074  -0.0026 68  ARG   A CG  
485  C  CD  . ARG   A 62  ? 0.3634 0.2896 0.2575 0.0017  0.0091  -0.0025 68  ARG   A CD  
486  N  NE  . ARG   A 62  ? 0.3679 0.2996 0.2635 0.0040  0.0164  -0.0084 68  ARG   A NE  
487  C  CZ  . ARG   A 62  ? 0.3580 0.2904 0.2513 0.0043  0.0211  -0.0162 68  ARG   A CZ  
488  N  NH1 . ARG   A 62  ? 0.3377 0.2661 0.2257 0.0016  0.0186  -0.0191 68  ARG   A NH1 
489  N  NH2 . ARG   A 62  ? 0.3509 0.2882 0.2481 0.0072  0.0285  -0.0214 68  ARG   A NH2 
490  N  N   . ARG   A 63  ? 0.3213 0.2223 0.2284 0.0022  -0.0115 0.0088  69  ARG   A N   
491  C  CA  . ARG   A 63  ? 0.3342 0.2311 0.2481 0.0021  -0.0169 0.0153  69  ARG   A CA  
492  C  C   . ARG   A 63  ? 0.3437 0.2366 0.2625 0.0038  -0.0163 0.0191  69  ARG   A C   
493  O  O   . ARG   A 63  ? 0.3441 0.2364 0.2651 0.0014  -0.0201 0.0257  69  ARG   A O   
494  C  CB  . ARG   A 63  ? 0.3502 0.2525 0.2601 -0.0039 -0.0227 0.0215  69  ARG   A CB  
495  C  CG  . ARG   A 63  ? 0.3920 0.2940 0.3042 -0.0048 -0.0263 0.0213  69  ARG   A CG  
496  C  CD  . ARG   A 63  ? 0.3904 0.2995 0.2981 -0.0119 -0.0328 0.0282  69  ARG   A CD  
497  N  NE  . ARG   A 63  ? 0.4026 0.3150 0.3051 -0.0152 -0.0340 0.0242  69  ARG   A NE  
498  C  CZ  . ARG   A 63  ? 0.4192 0.3395 0.3091 -0.0226 -0.0348 0.0228  69  ARG   A CZ  
499  N  NH1 . ARG   A 63  ? 0.4111 0.3376 0.2927 -0.0273 -0.0346 0.0255  69  ARG   A NH1 
500  N  NH2 . ARG   A 63  ? 0.4139 0.3361 0.2989 -0.0262 -0.0356 0.0185  69  ARG   A NH2 
501  N  N   . LYS   A 64  ? 0.3384 0.2293 0.2583 0.0070  -0.0116 0.0151  70  LYS   A N   
502  C  CA  . LYS   A 64  ? 0.3525 0.2406 0.2751 0.0072  -0.0107 0.0177  70  LYS   A CA  
503  C  C   . LYS   A 64  ? 0.3501 0.2332 0.2775 0.0109  -0.0073 0.0141  70  LYS   A C   
504  O  O   . LYS   A 64  ? 0.3456 0.2299 0.2730 0.0134  -0.0045 0.0096  70  LYS   A O   
505  C  CB  . LYS   A 64  ? 0.4014 0.2966 0.3174 0.0044  -0.0089 0.0187  70  LYS   A CB  
506  C  CG  . LYS   A 64  ? 0.5033 0.4022 0.4152 -0.0008 -0.0127 0.0250  70  LYS   A CG  
507  C  CD  . LYS   A 64  ? 0.6082 0.5137 0.5149 -0.0037 -0.0107 0.0265  70  LYS   A CD  
508  C  CE  . LYS   A 64  ? 0.6777 0.5898 0.5778 -0.0097 -0.0140 0.0317  70  LYS   A CE  
509  N  NZ  . LYS   A 64  ? 0.7212 0.6383 0.6160 -0.0113 -0.0146 0.0291  70  LYS   A NZ  
510  N  N   . HIS   A 65  ? 0.3384 0.2160 0.2695 0.0104  -0.0074 0.0163  71  HIS   A N   
511  C  CA  . HIS   A 65  ? 0.3369 0.2105 0.2709 0.0119  -0.0043 0.0134  71  HIS   A CA  
512  C  C   . HIS   A 65  ? 0.3348 0.2124 0.2644 0.0094  -0.0027 0.0147  71  HIS   A C   
513  O  O   . HIS   A 65  ? 0.3381 0.2163 0.2656 0.0061  -0.0042 0.0185  71  HIS   A O   
514  C  CB  . HIS   A 65  ? 0.3408 0.2058 0.2810 0.0119  -0.0045 0.0139  71  HIS   A CB  
515  C  CG  . HIS   A 65  ? 0.3654 0.2273 0.3121 0.0145  -0.0060 0.0133  71  HIS   A CG  
516  N  ND1 . HIS   A 65  ? 0.4009 0.2603 0.3514 0.0170  -0.0037 0.0092  71  HIS   A ND1 
517  C  CD2 . HIS   A 65  ? 0.3704 0.2325 0.3208 0.0144  -0.0098 0.0170  71  HIS   A CD2 
518  C  CE1 . HIS   A 65  ? 0.3875 0.2456 0.3441 0.0186  -0.0058 0.0101  71  HIS   A CE1 
519  N  NE2 . HIS   A 65  ? 0.3872 0.2470 0.3442 0.0172  -0.0098 0.0150  71  HIS   A NE2 
520  N  N   . TYR   A 66  ? 0.3187 0.2001 0.2479 0.0106  0.0000  0.0124  72  TYR   A N   
521  C  CA  . TYR   A 66  ? 0.3113 0.1986 0.2378 0.0081  0.0012  0.0145  72  TYR   A CA  
522  C  C   . TYR   A 66  ? 0.2978 0.1829 0.2253 0.0065  0.0026  0.0141  72  TYR   A C   
523  O  O   . TYR   A 66  ? 0.2999 0.1836 0.2301 0.0087  0.0038  0.0117  72  TYR   A O   
524  C  CB  . TYR   A 66  ? 0.3052 0.2013 0.2314 0.0104  0.0032  0.0135  72  TYR   A CB  
525  C  CG  . TYR   A 66  ? 0.3182 0.2188 0.2411 0.0104  0.0029  0.0132  72  TYR   A CG  
526  C  CD1 . TYR   A 66  ? 0.3342 0.2406 0.2528 0.0067  0.0023  0.0165  72  TYR   A CD1 
527  C  CD2 . TYR   A 66  ? 0.3308 0.2305 0.2540 0.0130  0.0034  0.0095  72  TYR   A CD2 
528  C  CE1 . TYR   A 66  ? 0.3571 0.2689 0.2712 0.0055  0.0025  0.0160  72  TYR   A CE1 
529  C  CE2 . TYR   A 66  ? 0.3471 0.2516 0.2656 0.0117  0.0035  0.0085  72  TYR   A CE2 
530  C  CZ  . TYR   A 66  ? 0.3689 0.2797 0.2826 0.0078  0.0031  0.0118  72  TYR   A CZ  
531  O  OH  . TYR   A 66  ? 0.3957 0.3123 0.3035 0.0052  0.0035  0.0107  72  TYR   A OH  
532  N  N   . PRO   A 67  ? 0.2950 0.1807 0.2196 0.0019  0.0024  0.0167  73  PRO   A N   
533  C  CA  . PRO   A 67  ? 0.2933 0.1788 0.2173 -0.0013 0.0036  0.0163  73  PRO   A CA  
534  C  C   . PRO   A 67  ? 0.3059 0.2017 0.2314 -0.0002 0.0043  0.0183  73  PRO   A C   
535  O  O   . PRO   A 67  ? 0.3102 0.2140 0.2358 0.0003  0.0042  0.0207  73  PRO   A O   
536  C  CB  . PRO   A 67  ? 0.3019 0.1852 0.2219 -0.0073 0.0029  0.0186  73  PRO   A CB  
537  C  CG  . PRO   A 67  ? 0.3144 0.2008 0.2332 -0.0071 0.0012  0.0217  73  PRO   A CG  
538  C  CD  . PRO   A 67  ? 0.2866 0.1743 0.2079 -0.0016 0.0008  0.0203  73  PRO   A CD  
539  N  N   . VAL   A 68  ? 0.2915 0.1878 0.2189 -0.0002 0.0049  0.0176  74  VAL   A N   
540  C  CA  . VAL   A 68  ? 0.2959 0.2020 0.2273 0.0010  0.0051  0.0208  74  VAL   A CA  
541  C  C   . VAL   A 68  ? 0.2991 0.2073 0.2296 -0.0039 0.0046  0.0229  74  VAL   A C   
542  O  O   . VAL   A 68  ? 0.2964 0.1974 0.2234 -0.0069 0.0050  0.0200  74  VAL   A O   
543  C  CB  . VAL   A 68  ? 0.3127 0.2191 0.2500 0.0078  0.0062  0.0188  74  VAL   A CB  
544  C  CG1 . VAL   A 68  ? 0.3160 0.2231 0.2534 0.0115  0.0070  0.0169  74  VAL   A CG1 
545  C  CG2 . VAL   A 68  ? 0.3217 0.2199 0.2595 0.0088  0.0063  0.0154  74  VAL   A CG2 
546  N  N   . SER   A 69  ? 0.3007 0.2194 0.2350 -0.0047 0.0037  0.0280  75  SER   A N   
547  C  CA  . SER   A 69  ? 0.3224 0.2463 0.2573 -0.0092 0.0023  0.0320  75  SER   A CA  
548  C  C   . SER   A 69  ? 0.3120 0.2387 0.2562 -0.0029 0.0025  0.0334  75  SER   A C   
549  O  O   . SER   A 69  ? 0.2986 0.2290 0.2498 0.0034  0.0037  0.0339  75  SER   A O   
550  C  CB  . SER   A 69  ? 0.3644 0.2999 0.2999 -0.0141 0.0006  0.0385  75  SER   A CB  
551  O  OG  . SER   A 69  ? 0.4137 0.3459 0.3404 -0.0208 0.0003  0.0371  75  SER   A OG  
552  N  N   . PHE   A 70  ? 0.2955 0.2198 0.2396 -0.0047 0.0018  0.0336  76  PHE   A N   
553  C  CA  . PHE   A 70  ? 0.2969 0.2221 0.2496 0.0005  0.0017  0.0352  76  PHE   A CA  
554  C  C   . PHE   A 70  ? 0.2999 0.2320 0.2552 -0.0044 -0.0010 0.0420  76  PHE   A C   
555  O  O   . PHE   A 70  ? 0.3041 0.2371 0.2511 -0.0128 -0.0022 0.0429  76  PHE   A O   
556  C  CB  . PHE   A 70  ? 0.2860 0.2000 0.2373 0.0043  0.0034  0.0284  76  PHE   A CB  
557  C  CG  . PHE   A 70  ? 0.2897 0.1966 0.2326 -0.0011 0.0039  0.0243  76  PHE   A CG  
558  C  CD1 . PHE   A 70  ? 0.2897 0.1901 0.2265 -0.0025 0.0053  0.0195  76  PHE   A CD1 
559  C  CD2 . PHE   A 70  ? 0.2924 0.1991 0.2347 -0.0045 0.0034  0.0253  76  PHE   A CD2 
560  C  CE1 . PHE   A 70  ? 0.3063 0.1997 0.2376 -0.0068 0.0069  0.0151  76  PHE   A CE1 
561  C  CE2 . PHE   A 70  ? 0.2983 0.1988 0.2334 -0.0095 0.0051  0.0205  76  PHE   A CE2 
562  C  CZ  . PHE   A 70  ? 0.2909 0.1846 0.2211 -0.0103 0.0072  0.0151  76  PHE   A CZ  
563  N  N   . SER   A 71  ? 0.3077 0.2448 0.2746 0.0005  -0.0018 0.0471  77  SER   A N   
564  C  CA  . SER   A 71  ? 0.3080 0.2529 0.2800 -0.0036 -0.0052 0.0557  77  SER   A CA  
565  C  C   . SER   A 71  ? 0.3097 0.2485 0.2762 -0.0075 -0.0058 0.0538  77  SER   A C   
566  O  O   . SER   A 71  ? 0.3217 0.2502 0.2831 -0.0054 -0.0033 0.0458  77  SER   A O   
567  C  CB  . SER   A 71  ? 0.3223 0.2732 0.3111 0.0038  -0.0056 0.0618  77  SER   A CB  
568  O  OG  . SER   A 71  ? 0.3383 0.2799 0.3324 0.0116  -0.0030 0.0563  77  SER   A OG  
569  N  N   . LYS   A 72  ? 0.3089 0.2552 0.2761 -0.0142 -0.0094 0.0616  78  LYS   A N   
570  C  CA  . LYS   A 72  ? 0.3286 0.2708 0.2902 -0.0190 -0.0098 0.0605  78  LYS   A CA  
571  C  C   . LYS   A 72  ? 0.3320 0.2688 0.3041 -0.0112 -0.0094 0.0606  78  LYS   A C   
572  O  O   . LYS   A 72  ? 0.3209 0.2604 0.3063 -0.0041 -0.0100 0.0649  78  LYS   A O   
573  C  CB  . LYS   A 72  ? 0.3568 0.3102 0.3148 -0.0300 -0.0141 0.0696  78  LYS   A CB  
574  C  CG  . LYS   A 72  ? 0.4300 0.3865 0.3746 -0.0396 -0.0139 0.0674  78  LYS   A CG  
575  C  CD  . LYS   A 72  ? 0.5230 0.4872 0.4582 -0.0531 -0.0169 0.0726  78  LYS   A CD  
576  C  CE  . LYS   A 72  ? 0.5963 0.5621 0.5172 -0.0634 -0.0159 0.0688  78  LYS   A CE  
577  N  NZ  . LYS   A 72  ? 0.6369 0.6058 0.5442 -0.0772 -0.0163 0.0686  78  LYS   A NZ  
578  N  N   . PRO   A 73  ? 0.3539 0.2834 0.3213 -0.0126 -0.0081 0.0558  79  PRO   A N   
579  C  CA  . PRO   A 73  ? 0.3553 0.2794 0.3326 -0.0059 -0.0080 0.0562  79  PRO   A CA  
580  C  C   . PRO   A 73  ? 0.3604 0.2925 0.3510 -0.0053 -0.0121 0.0681  79  PRO   A C   
581  O  O   . PRO   A 73  ? 0.3576 0.2990 0.3462 -0.0135 -0.0159 0.0766  79  PRO   A O   
582  C  CB  . PRO   A 73  ? 0.3839 0.3025 0.3528 -0.0108 -0.0068 0.0514  79  PRO   A CB  
583  C  CG  . PRO   A 73  ? 0.4000 0.3175 0.3555 -0.0168 -0.0043 0.0450  79  PRO   A CG  
584  C  CD  . PRO   A 73  ? 0.3667 0.2922 0.3203 -0.0202 -0.0061 0.0495  79  PRO   A CD  
585  N  N   . SER   A 74  ? 0.3618 0.2909 0.3663 0.0041  -0.0113 0.0690  80  SER   A N   
586  C  CA  . SER   A 74  ? 0.3711 0.3069 0.3920 0.0065  -0.0146 0.0804  80  SER   A CA  
587  C  C   . SER   A 74  ? 0.3644 0.2913 0.3989 0.0159  -0.0125 0.0785  80  SER   A C   
588  O  O   . SER   A 74  ? 0.3545 0.2711 0.3849 0.0204  -0.0086 0.0680  80  SER   A O   
589  C  CB  . SER   A 74  ? 0.4130 0.3588 0.4408 0.0084  -0.0151 0.0855  80  SER   A CB  
590  O  OG  . SER   A 74  ? 0.4911 0.4433 0.5056 0.0004  -0.0160 0.0850  80  SER   A OG  
591  N  N   . LEU   A 75  ? 0.3651 0.2964 0.4170 0.0186  -0.0153 0.0891  81  LEU   A N   
592  C  CA  . LEU   A 75  ? 0.3827 0.3058 0.4506 0.0272  -0.0133 0.0887  81  LEU   A CA  
593  C  C   . LEU   A 75  ? 0.3975 0.3225 0.4768 0.0358  -0.0092 0.0863  81  LEU   A C   
594  O  O   . LEU   A 75  ? 0.4057 0.3419 0.4961 0.0362  -0.0112 0.0958  81  LEU   A O   
595  C  CB  . LEU   A 75  ? 0.3852 0.3131 0.4675 0.0251  -0.0186 0.1030  81  LEU   A CB  
596  C  CG  . LEU   A 75  ? 0.4166 0.3335 0.5138 0.0319  -0.0173 0.1029  81  LEU   A CG  
597  C  CD1 . LEU   A 75  ? 0.4267 0.3317 0.5113 0.0298  -0.0156 0.0933  81  LEU   A CD1 
598  C  CD2 . LEU   A 75  ? 0.4189 0.3420 0.5325 0.0296  -0.0233 0.1193  81  LEU   A CD2 
599  N  N   . ILE   A 76  ? 0.4006 0.3160 0.4768 0.0418  -0.0034 0.0739  82  ILE   A N   
600  C  CA  . ILE   A 76  ? 0.4065 0.3237 0.4906 0.0490  0.0016  0.0696  82  ILE   A CA  
601  C  C   . ILE   A 76  ? 0.4186 0.3245 0.5141 0.0572  0.0069  0.0626  82  ILE   A C   
602  O  O   . ILE   A 76  ? 0.4099 0.3046 0.4985 0.0568  0.0078  0.0556  82  ILE   A O   
603  C  CB  . ILE   A 76  ? 0.4095 0.3271 0.4758 0.0466  0.0040  0.0602  82  ILE   A CB  
604  C  CG1 . ILE   A 76  ? 0.4240 0.3525 0.4803 0.0385  -0.0003 0.0664  82  ILE   A CG1 
605  C  CG2 . ILE   A 76  ? 0.4126 0.3303 0.4836 0.0532  0.0100  0.0533  82  ILE   A CG2 
606  C  CD1 . ILE   A 76  ? 0.4441 0.3703 0.4824 0.0351  0.0013  0.0578  82  ILE   A CD1 
607  N  N   . PHE   A 77  ? 0.4254 0.3344 0.5384 0.0644  0.0109  0.0640  83  PHE   A N   
608  C  CA  . PHE   A 77  ? 0.4400 0.3376 0.5638 0.0720  0.0171  0.0559  83  PHE   A CA  
609  C  C   . PHE   A 77  ? 0.4382 0.3303 0.5478 0.0730  0.0231  0.0410  83  PHE   A C   
610  O  O   . PHE   A 77  ? 0.4396 0.3399 0.5434 0.0726  0.0250  0.0389  83  PHE   A O   
611  C  CB  . PHE   A 77  ? 0.4456 0.3484 0.5950 0.0795  0.0202  0.0623  83  PHE   A CB  
612  C  CG  . PHE   A 77  ? 0.4748 0.3644 0.6384 0.0868  0.0266  0.0552  83  PHE   A CG  
613  C  CD1 . PHE   A 77  ? 0.4951 0.3745 0.6664 0.0869  0.0240  0.0588  83  PHE   A CD1 
614  C  CD2 . PHE   A 77  ? 0.4953 0.3830 0.6654 0.0932  0.0356  0.0451  83  PHE   A CD2 
615  C  CE1 . PHE   A 77  ? 0.5119 0.3780 0.6967 0.0933  0.0302  0.0519  83  PHE   A CE1 
616  C  CE2 . PHE   A 77  ? 0.5045 0.3794 0.6879 0.0995  0.0423  0.0376  83  PHE   A CE2 
617  C  CZ  . PHE   A 77  ? 0.5099 0.3736 0.7010 0.0996  0.0395  0.0412  83  PHE   A CZ  
618  N  N   . VAL   A 78  ? 0.4347 0.3135 0.5384 0.0735  0.0255  0.0314  84  VAL   A N   
619  C  CA  . VAL   A 78  ? 0.4414 0.3143 0.5313 0.0734  0.0304  0.0178  84  VAL   A CA  
620  C  C   . VAL   A 78  ? 0.4546 0.3178 0.5565 0.0795  0.0376  0.0097  84  VAL   A C   
621  O  O   . VAL   A 78  ? 0.4484 0.3025 0.5603 0.0812  0.0371  0.0113  84  VAL   A O   
622  C  CB  . VAL   A 78  ? 0.4453 0.3113 0.5168 0.0674  0.0266  0.0133  84  VAL   A CB  
623  C  CG1 . VAL   A 78  ? 0.4562 0.3186 0.5133 0.0663  0.0304  0.0011  84  VAL   A CG1 
624  C  CG2 . VAL   A 78  ? 0.4412 0.3151 0.5035 0.0614  0.0201  0.0213  84  VAL   A CG2 
625  N  N   . GLU   A 79  ? 0.4724 0.3373 0.5729 0.0822  0.0445  0.0007  85  GLU   A N   
626  C  CA  . GLU   A 79  ? 0.4930 0.3491 0.6033 0.0873  0.0531  -0.0092 85  GLU   A CA  
627  C  C   . GLU   A 79  ? 0.5101 0.3516 0.6104 0.0844  0.0537  -0.0187 85  GLU   A C   
628  O  O   . GLU   A 79  ? 0.5155 0.3560 0.5978 0.0784  0.0487  -0.0202 85  GLU   A O   
629  C  CB  . GLU   A 79  ? 0.5354 0.3982 0.6415 0.0886  0.0604  -0.0176 85  GLU   A CB  
630  C  CG  . GLU   A 79  ? 0.6123 0.4889 0.7335 0.0929  0.0621  -0.0095 85  GLU   A CG  
631  C  CD  . GLU   A 79  ? 0.7089 0.5845 0.8579 0.1002  0.0642  -0.0024 85  GLU   A CD  
632  O  OE1 . GLU   A 79  ? 0.7238 0.5894 0.8843 0.1051  0.0719  -0.0107 85  GLU   A OE1 
633  O  OE2 . GLU   A 79  ? 0.7390 0.6237 0.8987 0.1007  0.0581  0.0118  85  GLU   A OE2 
634  N  N   . ALA   A 80  ? 0.5170 0.3473 0.6294 0.0886  0.0601  -0.0257 86  ALA   A N   
635  C  CA  . ALA   A 80  ? 0.5408 0.3567 0.6445 0.0853  0.0613  -0.0354 86  ALA   A CA  
636  C  C   . ALA   A 80  ? 0.5589 0.3758 0.6397 0.0795  0.0628  -0.0464 86  ALA   A C   
637  O  O   . ALA   A 80  ? 0.5611 0.3850 0.6381 0.0802  0.0680  -0.0518 86  ALA   A O   
638  C  CB  . ALA   A 80  ? 0.5466 0.3506 0.6677 0.0907  0.0695  -0.0424 86  ALA   A CB  
639  N  N   . SER   A 81  ? 0.5695 0.3813 0.6354 0.0734  0.0574  -0.0481 87  SER   A N   
640  C  CA  . SER   A 81  ? 0.5830 0.3954 0.6280 0.0670  0.0573  -0.0570 87  SER   A CA  
641  C  C   . SER   A 81  ? 0.5873 0.3858 0.6281 0.0636  0.0588  -0.0662 87  SER   A C   
642  O  O   . SER   A 81  ? 0.5938 0.3823 0.6485 0.0667  0.0604  -0.0655 87  SER   A O   
643  C  CB  . SER   A 81  ? 0.6062 0.4263 0.6383 0.0624  0.0487  -0.0496 87  SER   A CB  
644  O  OG  . SER   A 81  ? 0.6410 0.4552 0.6734 0.0602  0.0429  -0.0450 87  SER   A OG  
645  N  N   . GLU   A 82  ? 0.5855 0.3834 0.6079 0.0566  0.0575  -0.0735 88  GLU   A N   
646  C  CA  . GLU   A 82  ? 0.5885 0.3743 0.6057 0.0519  0.0577  -0.0812 88  GLU   A CA  
647  C  C   . GLU   A 82  ? 0.5637 0.3463 0.5819 0.0499  0.0493  -0.0728 88  GLU   A C   
648  O  O   . GLU   A 82  ? 0.5633 0.3353 0.5817 0.0469  0.0490  -0.0768 88  GLU   A O   
649  C  CB  . GLU   A 82  ? 0.6409 0.4287 0.6384 0.0442  0.0586  -0.0909 88  GLU   A CB  
650  C  CG  . GLU   A 82  ? 0.7374 0.5375 0.7218 0.0405  0.0518  -0.0848 88  GLU   A CG  
651  C  CD  . GLU   A 82  ? 0.8599 0.6618 0.8259 0.0317  0.0496  -0.0911 88  GLU   A CD  
652  O  OE1 . GLU   A 82  ? 0.8812 0.6935 0.8372 0.0290  0.0464  -0.0879 88  GLU   A OE1 
653  O  OE2 . GLU   A 82  ? 0.9010 0.6940 0.8628 0.0270  0.0505  -0.0984 88  GLU   A OE2 
654  N  N   . TYR   A 83  ? 0.5392 0.3311 0.5581 0.0510  0.0431  -0.0614 89  TYR   A N   
655  C  CA  . TYR   A 83  ? 0.5224 0.3138 0.5416 0.0487  0.0359  -0.0533 89  TYR   A CA  
656  C  C   . TYR   A 83  ? 0.4929 0.2826 0.5285 0.0532  0.0345  -0.0437 89  TYR   A C   
657  O  O   . TYR   A 83  ? 0.4844 0.2704 0.5224 0.0509  0.0301  -0.0387 89  TYR   A O   
658  C  CB  . TYR   A 83  ? 0.5266 0.3293 0.5351 0.0459  0.0304  -0.0477 89  TYR   A CB  
659  C  CG  . TYR   A 83  ? 0.5414 0.3474 0.5346 0.0412  0.0303  -0.0546 89  TYR   A CG  
660  C  CD1 . TYR   A 83  ? 0.5555 0.3579 0.5403 0.0354  0.0273  -0.0583 89  TYR   A CD1 
661  C  CD2 . TYR   A 83  ? 0.5571 0.3706 0.5448 0.0419  0.0330  -0.0567 89  TYR   A CD2 
662  C  CE1 . TYR   A 83  ? 0.5706 0.3771 0.5421 0.0303  0.0263  -0.0632 89  TYR   A CE1 
663  C  CE2 . TYR   A 83  ? 0.5741 0.3913 0.5478 0.0367  0.0323  -0.0618 89  TYR   A CE2 
664  C  CZ  . TYR   A 83  ? 0.5873 0.4012 0.5531 0.0309  0.0287  -0.0648 89  TYR   A CZ  
665  O  OH  . TYR   A 83  ? 0.6099 0.4286 0.5625 0.0251  0.0272  -0.0684 89  TYR   A OH  
666  N  N   . TYR   A 84  ? 0.4737 0.2674 0.5211 0.0590  0.0379  -0.0400 90  TYR   A N   
667  C  CA  . TYR   A 84  ? 0.4573 0.2515 0.5211 0.0627  0.0355  -0.0289 90  TYR   A CA  
668  C  C   . TYR   A 84  ? 0.4789 0.2706 0.5602 0.0696  0.0420  -0.0296 90  TYR   A C   
669  O  O   . TYR   A 84  ? 0.4822 0.2788 0.5619 0.0720  0.0472  -0.0352 90  TYR   A O   
670  C  CB  . TYR   A 84  ? 0.4194 0.2270 0.4806 0.0619  0.0302  -0.0181 90  TYR   A CB  
671  C  CG  . TYR   A 84  ? 0.3840 0.1953 0.4315 0.0558  0.0242  -0.0154 90  TYR   A CG  
672  C  CD1 . TYR   A 84  ? 0.3671 0.1739 0.4162 0.0526  0.0200  -0.0109 90  TYR   A CD1 
673  C  CD2 . TYR   A 84  ? 0.3742 0.1935 0.4081 0.0533  0.0230  -0.0172 90  TYR   A CD2 
674  C  CE1 . TYR   A 84  ? 0.3635 0.1746 0.4017 0.0474  0.0155  -0.0088 90  TYR   A CE1 
675  C  CE2 . TYR   A 84  ? 0.3659 0.1884 0.3898 0.0485  0.0183  -0.0149 90  TYR   A CE2 
676  C  CZ  . TYR   A 84  ? 0.3569 0.1753 0.3830 0.0457  0.0150  -0.0112 90  TYR   A CZ  
677  O  OH  . TYR   A 84  ? 0.3383 0.1600 0.3562 0.0411  0.0113  -0.0095 90  TYR   A OH  
678  N  N   . PRO   A 85  ? 0.4927 0.2786 0.5921 0.0731  0.0414  -0.0226 91  PRO   A N   
679  C  CA  . PRO   A 85  ? 0.5033 0.2895 0.6233 0.0807  0.0469  -0.0204 91  PRO   A CA  
680  C  C   . PRO   A 85  ? 0.5099 0.3124 0.6341 0.0827  0.0437  -0.0090 91  PRO   A C   
681  O  O   . PRO   A 85  ? 0.5118 0.3228 0.6246 0.0778  0.0368  -0.0021 91  PRO   A O   
682  C  CB  . PRO   A 85  ? 0.5085 0.2838 0.6462 0.0826  0.0455  -0.0142 91  PRO   A CB  
683  C  CG  . PRO   A 85  ? 0.5082 0.2855 0.6359 0.0760  0.0365  -0.0063 91  PRO   A CG  
684  C  CD  . PRO   A 85  ? 0.4889 0.2698 0.5924 0.0701  0.0352  -0.0144 91  PRO   A CD  
685  N  N   . ALA   A 86  ? 0.5050 0.3124 0.6461 0.0894  0.0488  -0.0069 92  ALA   A N   
686  C  CA  . ALA   A 86  ? 0.4989 0.3225 0.6446 0.0906  0.0455  0.0042  92  ALA   A CA  
687  C  C   . ALA   A 86  ? 0.4784 0.3060 0.6310 0.0881  0.0366  0.0199  92  ALA   A C   
688  O  O   . ALA   A 86  ? 0.4765 0.2974 0.6472 0.0912  0.0360  0.0261  92  ALA   A O   
689  C  CB  . ALA   A 86  ? 0.4947 0.3222 0.6613 0.0987  0.0527  0.0044  92  ALA   A CB  
690  N  N   . ARG   A 87  ? 0.4534 0.2904 0.5903 0.0818  0.0299  0.0255  93  ARG   A N   
691  C  CA  . ARG   A 87  ? 0.4270 0.2684 0.5662 0.0773  0.0216  0.0391  93  ARG   A CA  
692  C  C   . ARG   A 87  ? 0.4111 0.2681 0.5399 0.0724  0.0166  0.0468  93  ARG   A C   
693  O  O   . ARG   A 87  ? 0.4108 0.2740 0.5304 0.0726  0.0192  0.0413  93  ARG   A O   
694  C  CB  . ARG   A 87  ? 0.4331 0.2642 0.5600 0.0719  0.0187  0.0351  93  ARG   A CB  
695  C  CG  . ARG   A 87  ? 0.4307 0.2659 0.5334 0.0653  0.0164  0.0298  93  ARG   A CG  
696  C  CD  . ARG   A 87  ? 0.4285 0.2531 0.5184 0.0630  0.0183  0.0179  93  ARG   A CD  
697  N  NE  . ARG   A 87  ? 0.4179 0.2468 0.4900 0.0564  0.0142  0.0174  93  ARG   A NE  
698  C  CZ  . ARG   A 87  ? 0.4149 0.2497 0.4735 0.0548  0.0149  0.0126  93  ARG   A CZ  
699  N  NH1 . ARG   A 87  ? 0.3949 0.2329 0.4540 0.0585  0.0191  0.0081  93  ARG   A NH1 
700  N  NH2 . ARG   A 87  ? 0.3893 0.2269 0.4345 0.0493  0.0116  0.0123  93  ARG   A NH2 
701  N  N   . TYR   A 88  ? 0.3961 0.2591 0.5253 0.0670  0.0093  0.0591  94  TYR   A N   
702  C  CA  . TYR   A 88  ? 0.3859 0.2620 0.5034 0.0605  0.0044  0.0656  94  TYR   A CA  
703  C  C   . TYR   A 88  ? 0.3770 0.2494 0.4730 0.0537  0.0026  0.0592  94  TYR   A C   
704  O  O   . TYR   A 88  ? 0.3918 0.2580 0.4865 0.0506  0.0001  0.0606  94  TYR   A O   
705  C  CB  . TYR   A 88  ? 0.3902 0.2760 0.5193 0.0571  -0.0022 0.0825  94  TYR   A CB  
706  C  CG  . TYR   A 88  ? 0.4047 0.2995 0.5540 0.0628  -0.0013 0.0907  94  TYR   A CG  
707  C  CD1 . TYR   A 88  ? 0.4160 0.3236 0.5609 0.0617  -0.0014 0.0924  94  TYR   A CD1 
708  C  CD2 . TYR   A 88  ? 0.4175 0.3072 0.5910 0.0700  0.0004  0.0955  94  TYR   A CD2 
709  C  CE1 . TYR   A 88  ? 0.4233 0.3401 0.5877 0.0672  0.0000  0.0995  94  TYR   A CE1 
710  C  CE2 . TYR   A 88  ? 0.4261 0.3245 0.6206 0.0762  0.0021  0.1026  94  TYR   A CE2 
711  C  CZ  . TYR   A 88  ? 0.4375 0.3501 0.6274 0.0748  0.0019  0.1046  94  TYR   A CZ  
712  O  OH  . TYR   A 88  ? 0.4659 0.3884 0.6777 0.0809  0.0036  0.1121  94  TYR   A OH  
713  N  N   . GLN   A 89  ? 0.3511 0.2271 0.4315 0.0517  0.0042  0.0521  95  GLN   A N   
714  C  CA  . GLN   A 89  ? 0.3333 0.2067 0.3954 0.0457  0.0027  0.0466  95  GLN   A CA  
715  C  C   . GLN   A 89  ? 0.3345 0.2188 0.3889 0.0383  -0.0018 0.0546  95  GLN   A C   
716  O  O   . GLN   A 89  ? 0.3368 0.2307 0.3928 0.0379  -0.0025 0.0593  95  GLN   A O   
717  C  CB  . GLN   A 89  ? 0.3246 0.1944 0.3749 0.0474  0.0069  0.0343  95  GLN   A CB  
718  C  CG  . GLN   A 89  ? 0.3008 0.1690 0.3347 0.0419  0.0055  0.0295  95  GLN   A CG  
719  C  CD  . GLN   A 89  ? 0.3212 0.1840 0.3462 0.0437  0.0088  0.0184  95  GLN   A CD  
720  O  OE1 . GLN   A 89  ? 0.3445 0.2006 0.3737 0.0479  0.0121  0.0123  95  GLN   A OE1 
721  N  NE2 . GLN   A 89  ? 0.3074 0.1727 0.3200 0.0401  0.0080  0.0156  95  GLN   A NE2 
722  N  N   . SER   A 90  ? 0.3267 0.2100 0.3725 0.0318  -0.0046 0.0559  96  SER   A N   
723  C  CA  . SER   A 90  ? 0.3225 0.2153 0.3594 0.0235  -0.0081 0.0620  96  SER   A CA  
724  C  C   . SER   A 90  ? 0.3159 0.2082 0.3357 0.0199  -0.0061 0.0533  96  SER   A C   
725  O  O   . SER   A 90  ? 0.3164 0.2009 0.3315 0.0230  -0.0031 0.0437  96  SER   A O   
726  C  CB  . SER   A 90  ? 0.3502 0.2434 0.3882 0.0176  -0.0119 0.0692  96  SER   A CB  
727  O  OG  . SER   A 90  ? 0.3793 0.2635 0.4109 0.0170  -0.0102 0.0615  96  SER   A OG  
728  N  N   . HIS   A 91  ? 0.3145 0.2154 0.3259 0.0128  -0.0080 0.0570  97  HIS   A N   
729  C  CA  . HIS   A 91  ? 0.3331 0.2336 0.3298 0.0086  -0.0060 0.0497  97  HIS   A CA  
730  C  C   . HIS   A 91  ? 0.3276 0.2246 0.3222 0.0145  -0.0027 0.0419  97  HIS   A C   
731  O  O   . HIS   A 91  ? 0.3343 0.2268 0.3200 0.0139  -0.0005 0.0341  97  HIS   A O   
732  C  CB  . HIS   A 91  ? 0.3575 0.2527 0.3469 0.0048  -0.0050 0.0448  97  HIS   A CB  
733  C  CG  . HIS   A 91  ? 0.4001 0.2999 0.3898 -0.0023 -0.0080 0.0525  97  HIS   A CG  
734  N  ND1 . HIS   A 91  ? 0.4290 0.3356 0.4082 -0.0119 -0.0085 0.0543  97  HIS   A ND1 
735  C  CD2 . HIS   A 91  ? 0.4166 0.3152 0.4156 -0.0017 -0.0105 0.0587  97  HIS   A CD2 
736  C  CE1 . HIS   A 91  ? 0.4328 0.3430 0.4143 -0.0172 -0.0114 0.0616  97  HIS   A CE1 
737  N  NE2 . HIS   A 91  ? 0.4279 0.3333 0.4217 -0.0112 -0.0130 0.0651  97  HIS   A NE2 
738  N  N   . LEU   A 92  ? 0.3021 0.2022 0.3055 0.0197  -0.0024 0.0447  98  LEU   A N   
739  C  CA  . LEU   A 92  ? 0.3056 0.2043 0.3078 0.0246  0.0006  0.0385  98  LEU   A CA  
740  C  C   . LEU   A 92  ? 0.3086 0.2162 0.3063 0.0210  -0.0001 0.0418  98  LEU   A C   
741  O  O   . LEU   A 92  ? 0.3204 0.2366 0.3223 0.0176  -0.0030 0.0505  98  LEU   A O   
742  C  CB  . LEU   A 92  ? 0.3053 0.2018 0.3208 0.0326  0.0027  0.0384  98  LEU   A CB  
743  C  CG  . LEU   A 92  ? 0.3276 0.2215 0.3412 0.0375  0.0067  0.0303  98  LEU   A CG  
744  C  CD1 . LEU   A 92  ? 0.3344 0.2201 0.3375 0.0369  0.0079  0.0214  98  LEU   A CD1 
745  C  CD2 . LEU   A 92  ? 0.3372 0.2294 0.3646 0.0445  0.0098  0.0298  98  LEU   A CD2 
746  N  N   . MET   A 93  ? 0.3051 0.2110 0.2945 0.0213  0.0019  0.0355  99  MET   A N   
747  C  CA  . MET   A 93  ? 0.3042 0.2170 0.2883 0.0176  0.0014  0.0375  99  MET   A CA  
748  C  C   . MET   A 93  ? 0.3124 0.2252 0.2987 0.0232  0.0042  0.0335  99  MET   A C   
749  O  O   . MET   A 93  ? 0.3291 0.2343 0.3123 0.0265  0.0063  0.0263  99  MET   A O   
750  C  CB  . MET   A 93  ? 0.3074 0.2166 0.2783 0.0114  0.0016  0.0330  99  MET   A CB  
751  C  CG  . MET   A 93  ? 0.3366 0.2450 0.3034 0.0052  0.0002  0.0347  99  MET   A CG  
752  S  SD  . MET   A 93  ? 0.3993 0.3014 0.3527 -0.0008 0.0025  0.0271  99  MET   A SD  
753  C  CE  . MET   A 93  ? 0.3827 0.2750 0.3384 0.0067  0.0047  0.0193  99  MET   A CE  
754  N  N   . LEU   A 94  ? 0.2947 0.2167 0.2859 0.0236  0.0042  0.0383  100 LEU   A N   
755  C  CA  . LEU   A 94  ? 0.2913 0.2151 0.2845 0.0281  0.0073  0.0349  100 LEU   A CA  
756  C  C   . LEU   A 94  ? 0.2918 0.2194 0.2754 0.0235  0.0069  0.0345  100 LEU   A C   
757  O  O   . LEU   A 94  ? 0.2950 0.2277 0.2746 0.0172  0.0042  0.0392  100 LEU   A O   
758  C  CB  . LEU   A 94  ? 0.2838 0.2161 0.2925 0.0329  0.0085  0.0405  100 LEU   A CB  
759  C  CG  . LEU   A 94  ? 0.3200 0.2475 0.3410 0.0390  0.0101  0.0402  100 LEU   A CG  
760  C  CD1 . LEU   A 94  ? 0.3238 0.2599 0.3622 0.0443  0.0121  0.0456  100 LEU   A CD1 
761  C  CD2 . LEU   A 94  ? 0.3355 0.2520 0.3522 0.0430  0.0138  0.0296  100 LEU   A CD2 
762  N  N   . ALA   A 95  ? 0.2936 0.2193 0.2739 0.0261  0.0095  0.0290  101 ALA   A N   
763  C  CA  . ALA   A 95  ? 0.3092 0.2378 0.2813 0.0224  0.0094  0.0285  101 ALA   A CA  
764  C  C   . ALA   A 95  ? 0.3023 0.2346 0.2773 0.0266  0.0129  0.0256  101 ALA   A C   
765  O  O   . ALA   A 95  ? 0.3050 0.2340 0.2845 0.0318  0.0158  0.0212  101 ALA   A O   
766  C  CB  . ALA   A 95  ? 0.3182 0.2371 0.2792 0.0192  0.0084  0.0236  101 ALA   A CB  
767  N  N   . VAL   A 96  ? 0.2953 0.2341 0.2664 0.0235  0.0129  0.0275  102 VAL   A N   
768  C  CA  . VAL   A 96  ? 0.3095 0.2527 0.2811 0.0260  0.0164  0.0246  102 VAL   A CA  
769  C  C   . VAL   A 96  ? 0.3408 0.2758 0.3013 0.0244  0.0161  0.0190  102 VAL   A C   
770  O  O   . VAL   A 96  ? 0.3674 0.2985 0.3200 0.0197  0.0132  0.0200  102 VAL   A O   
771  C  CB  . VAL   A 96  ? 0.3022 0.2576 0.2755 0.0229  0.0164  0.0301  102 VAL   A CB  
772  C  CG1 . VAL   A 96  ? 0.3040 0.2642 0.2751 0.0238  0.0201  0.0267  102 VAL   A CG1 
773  C  CG2 . VAL   A 96  ? 0.2952 0.2602 0.2824 0.0253  0.0167  0.0364  102 VAL   A CG2 
774  N  N   . GLY   A 97  ? 0.3408 0.2728 0.3015 0.0280  0.0190  0.0133  103 GLY   A N   
775  C  CA  . GLY   A 97  ? 0.3546 0.2804 0.3056 0.0261  0.0181  0.0090  103 GLY   A CA  
776  C  C   . GLY   A 97  ? 0.3563 0.2792 0.3075 0.0293  0.0212  0.0025  103 GLY   A C   
777  O  O   . GLY   A 97  ? 0.3575 0.2806 0.3170 0.0337  0.0245  0.0003  103 GLY   A O   
778  N  N   . HIS   A 98  ? 0.3542 0.2744 0.2963 0.0265  0.0201  -0.0003 104 HIS   A N   
779  C  CA  . HIS   A 98  ? 0.3459 0.2638 0.2854 0.0275  0.0226  -0.0068 104 HIS   A CA  
780  C  C   . HIS   A 98  ? 0.3457 0.2541 0.2867 0.0294  0.0210  -0.0097 104 HIS   A C   
781  O  O   . HIS   A 98  ? 0.3437 0.2467 0.2822 0.0277  0.0167  -0.0074 104 HIS   A O   
782  C  CB  . HIS   A 98  ? 0.3397 0.2600 0.2684 0.0225  0.0213  -0.0075 104 HIS   A CB  
783  C  CG  . HIS   A 98  ? 0.3525 0.2733 0.2773 0.0221  0.0249  -0.0146 104 HIS   A CG  
784  N  ND1 . HIS   A 98  ? 0.3633 0.2901 0.2914 0.0241  0.0316  -0.0191 104 HIS   A ND1 
785  C  CD2 . HIS   A 98  ? 0.3735 0.2892 0.2922 0.0199  0.0230  -0.0182 104 HIS   A CD2 
786  C  CE1 . HIS   A 98  ? 0.3683 0.2928 0.2910 0.0225  0.0340  -0.0262 104 HIS   A CE1 
787  N  NE2 . HIS   A 98  ? 0.3818 0.2999 0.2982 0.0196  0.0286  -0.0255 104 HIS   A NE2 
788  N  N   . SER   A 99  ? 0.3551 0.2612 0.3001 0.0325  0.0249  -0.0152 105 SER   A N   
789  C  CA  . SER   A 99  ? 0.3742 0.2716 0.3209 0.0339  0.0238  -0.0184 105 SER   A CA  
790  C  C   . SER   A 99  ? 0.3872 0.2825 0.3341 0.0351  0.0287  -0.0264 105 SER   A C   
791  O  O   . SER   A 99  ? 0.3965 0.2950 0.3501 0.0383  0.0342  -0.0289 105 SER   A O   
792  C  CB  . SER   A 99  ? 0.4110 0.3056 0.3672 0.0372  0.0228  -0.0145 105 SER   A CB  
793  O  OG  . SER   A 99  ? 0.4794 0.3660 0.4381 0.0384  0.0219  -0.0170 105 SER   A OG  
794  N  N   . GLU   A 100 ? 0.3789 0.2692 0.3189 0.0322  0.0271  -0.0306 106 GLU   A N   
795  C  CA  . GLU   A 100 ? 0.3927 0.2792 0.3314 0.0321  0.0314  -0.0392 106 GLU   A CA  
796  C  C   . GLU   A 100 ? 0.4007 0.2776 0.3434 0.0333  0.0289  -0.0401 106 GLU   A C   
797  O  O   . GLU   A 100 ? 0.4046 0.2797 0.3490 0.0334  0.0239  -0.0343 106 GLU   A O   
798  C  CB  . GLU   A 100 ? 0.4059 0.2958 0.3314 0.0256  0.0311  -0.0432 106 GLU   A CB  
799  C  CG  . GLU   A 100 ? 0.4080 0.3077 0.3291 0.0237  0.0341  -0.0426 106 GLU   A CG  
800  C  CD  . GLU   A 100 ? 0.4468 0.3519 0.3539 0.0160  0.0320  -0.0433 106 GLU   A CD  
801  O  OE1 . GLU   A 100 ? 0.4416 0.3437 0.3413 0.0116  0.0308  -0.0479 106 GLU   A OE1 
802  O  OE2 . GLU   A 100 ? 0.4234 0.3365 0.3269 0.0137  0.0314  -0.0390 106 GLU   A OE2 
803  N  N   . PRO   A 101 ? 0.4002 0.2708 0.3448 0.0340  0.0326  -0.0474 107 PRO   A N   
804  C  CA  . PRO   A 101 ? 0.3954 0.2574 0.3445 0.0348  0.0299  -0.0473 107 PRO   A CA  
805  C  C   . PRO   A 101 ? 0.3744 0.2355 0.3175 0.0309  0.0229  -0.0435 107 PRO   A C   
806  O  O   . PRO   A 101 ? 0.3763 0.2344 0.3250 0.0326  0.0197  -0.0389 107 PRO   A O   
807  C  CB  . PRO   A 101 ? 0.4149 0.2705 0.3633 0.0339  0.0350  -0.0570 107 PRO   A CB  
808  C  CG  . PRO   A 101 ? 0.4189 0.2791 0.3695 0.0361  0.0423  -0.0614 107 PRO   A CG  
809  C  CD  . PRO   A 101 ? 0.4007 0.2714 0.3449 0.0341  0.0401  -0.0561 107 PRO   A CD  
810  N  N   . GLY   A 102 ? 0.3501 0.2145 0.2825 0.0255  0.0208  -0.0452 108 GLY   A N   
811  C  CA  . GLY   A 102 ? 0.3441 0.2092 0.2722 0.0218  0.0142  -0.0411 108 GLY   A CA  
812  C  C   . GLY   A 102 ? 0.3263 0.1944 0.2575 0.0233  0.0105  -0.0330 108 GLY   A C   
813  O  O   . GLY   A 102 ? 0.3378 0.2059 0.2686 0.0213  0.0056  -0.0294 108 GLY   A O   
814  N  N   . ASP   A 103 ? 0.3086 0.1798 0.2433 0.0264  0.0127  -0.0302 109 ASP   A N   
815  C  CA  . ASP   A 103 ? 0.3174 0.1904 0.2546 0.0273  0.0099  -0.0234 109 ASP   A CA  
816  C  C   . ASP   A 103 ? 0.3213 0.1897 0.2662 0.0298  0.0089  -0.0211 109 ASP   A C   
817  O  O   . ASP   A 103 ? 0.3140 0.1826 0.2603 0.0294  0.0067  -0.0167 109 ASP   A O   
818  C  CB  . ASP   A 103 ? 0.3136 0.1923 0.2507 0.0283  0.0123  -0.0211 109 ASP   A CB  
819  C  CG  . ASP   A 103 ? 0.3421 0.2267 0.2710 0.0245  0.0120  -0.0212 109 ASP   A CG  
820  O  OD1 . ASP   A 103 ? 0.3176 0.2023 0.2417 0.0210  0.0079  -0.0195 109 ASP   A OD1 
821  O  OD2 . ASP   A 103 ? 0.3777 0.2674 0.3057 0.0250  0.0157  -0.0223 109 ASP   A OD2 
822  N  N   . CYS   A 104 ? 0.3205 0.1841 0.2698 0.0316  0.0107  -0.0242 110 CYS   A N   
823  C  CA  . CYS   A 104 ? 0.3155 0.1755 0.2713 0.0329  0.0096  -0.0216 110 CYS   A CA  
824  C  C   . CYS   A 104 ? 0.3003 0.1592 0.2549 0.0306  0.0058  -0.0199 110 CYS   A C   
825  O  O   . CYS   A 104 ? 0.3024 0.1613 0.2534 0.0282  0.0038  -0.0218 110 CYS   A O   
826  C  CB  . CYS   A 104 ? 0.3347 0.1895 0.2959 0.0347  0.0116  -0.0246 110 CYS   A CB  
827  S  SG  . CYS   A 104 ? 0.3798 0.2356 0.3476 0.0389  0.0166  -0.0255 110 CYS   A SG  
828  N  N   . GLY   A 105 ? 0.2847 0.1436 0.2428 0.0308  0.0051  -0.0163 111 GLY   A N   
829  C  CA  . GLY   A 105 ? 0.2803 0.1385 0.2393 0.0291  0.0027  -0.0150 111 GLY   A CA  
830  C  C   . GLY   A 105 ? 0.3001 0.1608 0.2574 0.0282  0.0019  -0.0122 111 GLY   A C   
831  O  O   . GLY   A 105 ? 0.3035 0.1633 0.2637 0.0275  0.0011  -0.0109 111 GLY   A O   
832  N  N   . GLY   A 106 ? 0.3026 0.1662 0.2559 0.0282  0.0025  -0.0114 112 GLY   A N   
833  C  CA  . GLY   A 106 ? 0.3099 0.1751 0.2616 0.0270  0.0018  -0.0084 112 GLY   A CA  
834  C  C   . GLY   A 106 ? 0.2961 0.1601 0.2501 0.0266  0.0033  -0.0069 112 GLY   A C   
835  O  O   . GLY   A 106 ? 0.2942 0.1591 0.2492 0.0270  0.0049  -0.0067 112 GLY   A O   
836  N  N   . ILE   A 107 ? 0.3004 0.1625 0.2561 0.0253  0.0030  -0.0058 113 ILE   A N   
837  C  CA  . ILE   A 107 ? 0.2897 0.1504 0.2462 0.0237  0.0052  -0.0057 113 ILE   A CA  
838  C  C   . ILE   A 107 ? 0.3018 0.1647 0.2539 0.0216  0.0061  -0.0038 113 ILE   A C   
839  O  O   . ILE   A 107 ? 0.3031 0.1668 0.2529 0.0212  0.0050  -0.0023 113 ILE   A O   
840  C  CB  . ILE   A 107 ? 0.2848 0.1418 0.2461 0.0232  0.0058  -0.0065 113 ILE   A CB  
841  C  CG1 . ILE   A 107 ? 0.2817 0.1380 0.2481 0.0243  0.0058  -0.0082 113 ILE   A CG1 
842  C  CG2 . ILE   A 107 ? 0.2937 0.1487 0.2540 0.0203  0.0089  -0.0074 113 ILE   A CG2 
843  C  CD1 . ILE   A 107 ? 0.3126 0.1668 0.2863 0.0246  0.0066  -0.0089 113 ILE   A CD1 
844  N  N   . LEU   A 108 ? 0.2881 0.1525 0.2392 0.0195  0.0077  -0.0033 114 LEU   A N   
845  C  CA  . LEU   A 108 ? 0.2820 0.1489 0.2290 0.0162  0.0083  -0.0013 114 LEU   A CA  
846  C  C   . LEU   A 108 ? 0.2898 0.1527 0.2360 0.0124  0.0106  -0.0034 114 LEU   A C   
847  O  O   . LEU   A 108 ? 0.2882 0.1502 0.2362 0.0116  0.0120  -0.0051 114 LEU   A O   
848  C  CB  . LEU   A 108 ? 0.2786 0.1512 0.2255 0.0156  0.0082  0.0016  114 LEU   A CB  
849  C  CG  . LEU   A 108 ? 0.2901 0.1666 0.2330 0.0106  0.0085  0.0043  114 LEU   A CG  
850  C  CD1 . LEU   A 108 ? 0.2794 0.1588 0.2198 0.0103  0.0078  0.0063  114 LEU   A CD1 
851  C  CD2 . LEU   A 108 ? 0.3043 0.1868 0.2493 0.0095  0.0078  0.0083  114 LEU   A CD2 
852  N  N   . ARG   A 109 ? 0.2884 0.1489 0.2320 0.0095  0.0114  -0.0036 115 ARG   A N   
853  C  CA  . ARG   A 109 ? 0.2955 0.1512 0.2385 0.0057  0.0147  -0.0070 115 ARG   A CA  
854  C  C   . ARG   A 109 ? 0.3135 0.1692 0.2501 -0.0002 0.0158  -0.0065 115 ARG   A C   
855  O  O   . ARG   A 109 ? 0.3076 0.1659 0.2419 -0.0004 0.0136  -0.0033 115 ARG   A O   
856  C  CB  . ARG   A 109 ? 0.2930 0.1421 0.2425 0.0085  0.0157  -0.0093 115 ARG   A CB  
857  C  CG  . ARG   A 109 ? 0.3027 0.1494 0.2526 0.0092  0.0138  -0.0070 115 ARG   A CG  
858  C  CD  . ARG   A 109 ? 0.3225 0.1637 0.2812 0.0123  0.0138  -0.0074 115 ARG   A CD  
859  N  NE  . ARG   A 109 ? 0.3567 0.2010 0.3196 0.0166  0.0106  -0.0056 115 ARG   A NE  
860  C  CZ  . ARG   A 109 ? 0.3597 0.2028 0.3303 0.0191  0.0113  -0.0072 115 ARG   A CZ  
861  N  NH1 . ARG   A 109 ? 0.3368 0.1756 0.3127 0.0183  0.0158  -0.0108 115 ARG   A NH1 
862  N  NH2 . ARG   A 109 ? 0.3338 0.1802 0.3071 0.0220  0.0079  -0.0053 115 ARG   A NH2 
863  N  N   . CYS   A 110 ? 0.3238 0.1770 0.2573 -0.0056 0.0193  -0.0101 116 CYS   A N   
864  C  CA  . CYS   A 110 ? 0.3456 0.1978 0.2720 -0.0128 0.0209  -0.0109 116 CYS   A CA  
865  C  C   . CYS   A 110 ? 0.3841 0.2263 0.3126 -0.0148 0.0260  -0.0175 116 CYS   A C   
866  O  O   . CYS   A 110 ? 0.3862 0.2238 0.3232 -0.0096 0.0274  -0.0197 116 CYS   A O   
867  C  CB  . CYS   A 110 ? 0.3624 0.2216 0.2822 -0.0191 0.0209  -0.0095 116 CYS   A CB  
868  S  SG  . CYS   A 110 ? 0.4005 0.2585 0.3205 -0.0217 0.0251  -0.0146 116 CYS   A SG  
869  N  N   . GLN   A 111 ? 0.3970 0.2360 0.3187 -0.0225 0.0290  -0.0206 117 GLN   A N   
870  C  CA  . GLN   A 111 ? 0.4260 0.2546 0.3504 -0.0247 0.0351  -0.0280 117 GLN   A CA  
871  C  C   . GLN   A 111 ? 0.4422 0.2699 0.3698 -0.0246 0.0401  -0.0337 117 GLN   A C   
872  O  O   . GLN   A 111 ? 0.4639 0.2834 0.3988 -0.0230 0.0454  -0.0394 117 GLN   A O   
873  C  CB  . GLN   A 111 ? 0.4597 0.2850 0.3744 -0.0345 0.0379  -0.0312 117 GLN   A CB  
874  C  CG  . GLN   A 111 ? 0.5294 0.3629 0.4327 -0.0434 0.0382  -0.0315 117 GLN   A CG  
875  C  CD  . GLN   A 111 ? 0.6280 0.4586 0.5206 -0.0545 0.0409  -0.0351 117 GLN   A CD  
876  O  OE1 . GLN   A 111 ? 0.6547 0.4923 0.5401 -0.0596 0.0365  -0.0297 117 GLN   A OE1 
877  N  NE2 . GLN   A 111 ? 0.6387 0.4594 0.5304 -0.0589 0.0484  -0.0445 117 GLN   A NE2 
878  N  N   . HIS   A 112 ? 0.4259 0.2623 0.3491 -0.0266 0.0388  -0.0318 118 HIS   A N   
879  C  CA  . HIS   A 112 ? 0.4210 0.2579 0.3459 -0.0277 0.0434  -0.0367 118 HIS   A CA  
880  C  C   . HIS   A 112 ? 0.4179 0.2556 0.3542 -0.0188 0.0419  -0.0351 118 HIS   A C   
881  O  O   . HIS   A 112 ? 0.4285 0.2658 0.3688 -0.0188 0.0463  -0.0395 118 HIS   A O   
882  C  CB  . HIS   A 112 ? 0.4334 0.2792 0.3476 -0.0360 0.0428  -0.0351 118 HIS   A CB  
883  C  CG  . HIS   A 112 ? 0.4746 0.3213 0.3769 -0.0461 0.0435  -0.0359 118 HIS   A CG  
884  N  ND1 . HIS   A 112 ? 0.4888 0.3421 0.3864 -0.0478 0.0374  -0.0285 118 HIS   A ND1 
885  C  CD2 . HIS   A 112 ? 0.4959 0.3379 0.3910 -0.0550 0.0499  -0.0437 118 HIS   A CD2 
886  C  CE1 . HIS   A 112 ? 0.5031 0.3562 0.3903 -0.0580 0.0393  -0.0309 118 HIS   A CE1 
887  N  NE2 . HIS   A 112 ? 0.5073 0.3531 0.3918 -0.0630 0.0469  -0.0405 118 HIS   A NE2 
888  N  N   . GLY   A 113 ? 0.3996 0.2390 0.3405 -0.0119 0.0360  -0.0291 119 GLY   A N   
889  C  CA  . GLY   A 113 ? 0.3851 0.2256 0.3352 -0.0046 0.0339  -0.0273 119 GLY   A CA  
890  C  C   . GLY   A 113 ? 0.3565 0.2033 0.3052 -0.0012 0.0277  -0.0210 119 GLY   A C   
891  O  O   . GLY   A 113 ? 0.3499 0.1993 0.2935 -0.0022 0.0246  -0.0173 119 GLY   A O   
892  N  N   . VAL   A 114 ? 0.3337 0.1829 0.2877 0.0027  0.0262  -0.0200 120 VAL   A N   
893  C  CA  . VAL   A 114 ? 0.3171 0.1707 0.2709 0.0062  0.0212  -0.0153 120 VAL   A CA  
894  C  C   . VAL   A 114 ? 0.3049 0.1642 0.2525 0.0020  0.0202  -0.0125 120 VAL   A C   
895  O  O   . VAL   A 114 ? 0.3053 0.1664 0.2515 -0.0019 0.0223  -0.0137 120 VAL   A O   
896  C  CB  . VAL   A 114 ? 0.3150 0.1685 0.2765 0.0109  0.0199  -0.0155 120 VAL   A CB  
897  C  CG1 . VAL   A 114 ? 0.3183 0.1750 0.2791 0.0139  0.0157  -0.0119 120 VAL   A CG1 
898  C  CG2 . VAL   A 114 ? 0.3222 0.1717 0.2910 0.0147  0.0198  -0.0164 120 VAL   A CG2 
899  N  N   . VAL   A 115 ? 0.3005 0.1633 0.2457 0.0030  0.0169  -0.0082 121 VAL   A N   
900  C  CA  . VAL   A 115 ? 0.3124 0.1815 0.2545 0.0000  0.0150  -0.0036 121 VAL   A CA  
901  C  C   . VAL   A 115 ? 0.3143 0.1854 0.2617 0.0045  0.0124  -0.0007 121 VAL   A C   
902  O  O   . VAL   A 115 ? 0.3237 0.1988 0.2716 0.0021  0.0114  0.0027  121 VAL   A O   
903  C  CB  . VAL   A 115 ? 0.3197 0.1921 0.2581 -0.0013 0.0133  -0.0003 121 VAL   A CB  
904  C  CG1 . VAL   A 115 ? 0.3281 0.2084 0.2667 -0.0028 0.0107  0.0059  121 VAL   A CG1 
905  C  CG2 . VAL   A 115 ? 0.3211 0.1913 0.2533 -0.0073 0.0158  -0.0030 121 VAL   A CG2 
906  N  N   . GLY   A 116 ? 0.2960 0.1646 0.2474 0.0104  0.0112  -0.0016 122 GLY   A N   
907  C  CA  . GLY   A 116 ? 0.2937 0.1626 0.2498 0.0146  0.0094  -0.0003 122 GLY   A CA  
908  C  C   . GLY   A 116 ? 0.2935 0.1596 0.2515 0.0194  0.0085  -0.0025 122 GLY   A C   
909  O  O   . GLY   A 116 ? 0.2927 0.1566 0.2497 0.0197  0.0088  -0.0046 122 GLY   A O   
910  N  N   . ILE   A 117 ? 0.2796 0.1459 0.2408 0.0228  0.0075  -0.0020 123 ILE   A N   
911  C  CA  . ILE   A 117 ? 0.2607 0.1250 0.2223 0.0260  0.0068  -0.0047 123 ILE   A CA  
912  C  C   . ILE   A 117 ? 0.2702 0.1367 0.2332 0.0286  0.0072  -0.0038 123 ILE   A C   
913  O  O   . ILE   A 117 ? 0.2813 0.1491 0.2485 0.0292  0.0075  -0.0013 123 ILE   A O   
914  C  CB  . ILE   A 117 ? 0.2686 0.1291 0.2329 0.0269  0.0061  -0.0074 123 ILE   A CB  
915  C  CG1 . ILE   A 117 ? 0.2685 0.1279 0.2368 0.0268  0.0062  -0.0063 123 ILE   A CG1 
916  C  CG2 . ILE   A 117 ? 0.2720 0.1311 0.2370 0.0255  0.0059  -0.0087 123 ILE   A CG2 
917  C  CD1 . ILE   A 117 ? 0.2879 0.1435 0.2589 0.0275  0.0053  -0.0091 123 ILE   A CD1 
918  N  N   . VAL   A 118 ? 0.2624 0.1297 0.2227 0.0301  0.0074  -0.0057 124 VAL   A N   
919  C  CA  . VAL   A 118 ? 0.2625 0.1323 0.2246 0.0326  0.0090  -0.0063 124 VAL   A CA  
920  C  C   . VAL   A 118 ? 0.2795 0.1455 0.2471 0.0349  0.0099  -0.0082 124 VAL   A C   
921  O  O   . VAL   A 118 ? 0.2729 0.1343 0.2399 0.0343  0.0089  -0.0110 124 VAL   A O   
922  C  CB  . VAL   A 118 ? 0.2778 0.1489 0.2348 0.0327  0.0093  -0.0093 124 VAL   A CB  
923  C  CG1 . VAL   A 118 ? 0.2878 0.1612 0.2470 0.0353  0.0124  -0.0114 124 VAL   A CG1 
924  C  CG2 . VAL   A 118 ? 0.2740 0.1485 0.2263 0.0303  0.0083  -0.0066 124 VAL   A CG2 
925  N  N   . SER   A 119 ? 0.3024 0.1701 0.2765 0.0373  0.0115  -0.0061 125 SER   A N   
926  C  CA  . SER   A 119 ? 0.3168 0.1798 0.2980 0.0396  0.0125  -0.0073 125 SER   A CA  
927  C  C   . SER   A 119 ? 0.3277 0.1912 0.3146 0.0435  0.0163  -0.0095 125 SER   A C   
928  O  O   . SER   A 119 ? 0.3384 0.1961 0.3286 0.0453  0.0182  -0.0140 125 SER   A O   
929  C  CB  . SER   A 119 ? 0.3406 0.2041 0.3274 0.0385  0.0107  -0.0013 125 SER   A CB  
930  O  OG  . SER   A 119 ? 0.3745 0.2332 0.3695 0.0405  0.0112  -0.0010 125 SER   A OG  
931  N  N   . THR   A 120 ? 0.3206 0.1914 0.3089 0.0446  0.0177  -0.0069 126 THR   A N   
932  C  CA  . THR   A 120 ? 0.3156 0.1889 0.3110 0.0486  0.0221  -0.0086 126 THR   A CA  
933  C  C   . THR   A 120 ? 0.3445 0.2251 0.3336 0.0477  0.0237  -0.0097 126 THR   A C   
934  O  O   . THR   A 120 ? 0.3529 0.2366 0.3339 0.0441  0.0208  -0.0074 126 THR   A O   
935  C  CB  . THR   A 120 ? 0.3066 0.1836 0.3157 0.0515  0.0221  -0.0012 126 THR   A CB  
936  O  OG1 . THR   A 120 ? 0.3095 0.1956 0.3174 0.0493  0.0198  0.0056  126 THR   A OG1 
937  C  CG2 . THR   A 120 ? 0.2917 0.1630 0.3066 0.0513  0.0196  0.0021  126 THR   A CG2 
938  N  N   . GLY   A 121 ? 0.3550 0.2385 0.3490 0.0507  0.0287  -0.0131 127 GLY   A N   
939  C  CA  . GLY   A 121 ? 0.3819 0.2733 0.3706 0.0495  0.0306  -0.0139 127 GLY   A CA  
940  C  C   . GLY   A 121 ? 0.4163 0.3116 0.4139 0.0536  0.0372  -0.0173 127 GLY   A C   
941  O  O   . GLY   A 121 ? 0.4087 0.3015 0.4196 0.0582  0.0399  -0.0168 127 GLY   A O   
942  N  N   . GLY   A 122 ? 0.4420 0.3434 0.4328 0.0518  0.0401  -0.0208 128 GLY   A N   
943  C  CA  . GLY   A 122 ? 0.4621 0.3682 0.4605 0.0552  0.0477  -0.0253 128 GLY   A CA  
944  C  C   . GLY   A 122 ? 0.4842 0.4022 0.4797 0.0535  0.0498  -0.0237 128 GLY   A C   
945  O  O   . GLY   A 122 ? 0.5044 0.4249 0.4861 0.0484  0.0486  -0.0258 128 GLY   A O   
946  N  N   . ASN   A 123 ? 0.4751 0.4011 0.4848 0.0577  0.0528  -0.0193 129 ASN   A N   
947  C  CA  . ASN   A 123 ? 0.4722 0.4110 0.4839 0.0572  0.0562  -0.0174 129 ASN   A CA  
948  C  C   . ASN   A 123 ? 0.4474 0.3937 0.4532 0.0527  0.0498  -0.0082 129 ASN   A C   
949  O  O   . ASN   A 123 ? 0.4495 0.4049 0.4659 0.0542  0.0491  -0.0007 129 ASN   A O   
950  C  CB  . ASN   A 123 ? 0.5066 0.4510 0.5393 0.0642  0.0626  -0.0164 129 ASN   A CB  
951  C  CG  . ASN   A 123 ? 0.5818 0.5192 0.6295 0.0694  0.0608  -0.0123 129 ASN   A CG  
952  O  OD1 . ASN   A 123 ? 0.6051 0.5347 0.6619 0.0740  0.0661  -0.0185 129 ASN   A OD1 
953  N  ND2 . ASN   A 123 ? 0.5963 0.5363 0.6468 0.0680  0.0535  -0.0016 129 ASN   A ND2 
954  N  N   . GLY   A 124 ? 0.4247 0.3674 0.4143 0.0469  0.0451  -0.0089 130 GLY   A N   
955  C  CA  . GLY   A 124 ? 0.4142 0.3613 0.3974 0.0421  0.0393  -0.0013 130 GLY   A CA  
956  C  C   . GLY   A 124 ? 0.3832 0.3258 0.3694 0.0418  0.0334  0.0051  130 GLY   A C   
957  O  O   . GLY   A 124 ? 0.3794 0.3262 0.3627 0.0380  0.0293  0.0115  130 GLY   A O   
958  N  N   . LEU   A 125 ? 0.3709 0.3047 0.3619 0.0451  0.0331  0.0031  131 LEU   A N   
959  C  CA  . LEU   A 125 ? 0.3671 0.2963 0.3602 0.0443  0.0280  0.0083  131 LEU   A CA  
960  C  C   . LEU   A 125 ? 0.3546 0.2721 0.3393 0.0430  0.0257  0.0035  131 LEU   A C   
961  O  O   . LEU   A 125 ? 0.3628 0.2754 0.3436 0.0440  0.0283  -0.0035 131 LEU   A O   
962  C  CB  . LEU   A 125 ? 0.3636 0.2949 0.3734 0.0492  0.0294  0.0123  131 LEU   A CB  
963  C  CG  . LEU   A 125 ? 0.3834 0.3276 0.4045 0.0504  0.0304  0.0195  131 LEU   A CG  
964  C  CD1 . LEU   A 125 ? 0.3860 0.3318 0.4266 0.0572  0.0338  0.0216  131 LEU   A CD1 
965  C  CD2 . LEU   A 125 ? 0.3846 0.3342 0.4022 0.0448  0.0243  0.0283  131 LEU   A CD2 
966  N  N   . VAL   A 126 ? 0.3246 0.2384 0.3059 0.0400  0.0210  0.0073  132 VAL   A N   
967  C  CA  . VAL   A 126 ? 0.3099 0.2139 0.2851 0.0387  0.0187  0.0041  132 VAL   A CA  
968  C  C   . VAL   A 126 ? 0.2959 0.1981 0.2755 0.0377  0.0157  0.0091  132 VAL   A C   
969  O  O   . VAL   A 126 ? 0.2855 0.1930 0.2650 0.0346  0.0136  0.0148  132 VAL   A O   
970  C  CB  . VAL   A 126 ? 0.3103 0.2120 0.2737 0.0344  0.0163  0.0025  132 VAL   A CB  
971  C  CG1 . VAL   A 126 ? 0.3096 0.2151 0.2698 0.0301  0.0137  0.0079  132 VAL   A CG1 
972  C  CG2 . VAL   A 126 ? 0.3115 0.2044 0.2713 0.0338  0.0144  -0.0009 132 VAL   A CG2 
973  N  N   . GLY   A 127 ? 0.3000 0.1952 0.2828 0.0395  0.0156  0.0069  133 GLY   A N   
974  C  CA  . GLY   A 127 ? 0.2996 0.1932 0.2863 0.0382  0.0130  0.0114  133 GLY   A CA  
975  C  C   . GLY   A 127 ? 0.3078 0.1945 0.2870 0.0351  0.0110  0.0085  133 GLY   A C   
976  O  O   . GLY   A 127 ? 0.3073 0.1884 0.2826 0.0361  0.0118  0.0028  133 GLY   A O   
977  N  N   . PHE   A 128 ? 0.2992 0.1870 0.2766 0.0310  0.0087  0.0126  134 PHE   A N   
978  C  CA  . PHE   A 128 ? 0.3079 0.1903 0.2795 0.0279  0.0076  0.0100  134 PHE   A CA  
979  C  C   . PHE   A 128 ? 0.3090 0.1902 0.2843 0.0262  0.0064  0.0130  134 PHE   A C   
980  O  O   . PHE   A 128 ? 0.3109 0.1976 0.2891 0.0237  0.0050  0.0193  134 PHE   A O   
981  C  CB  . PHE   A 128 ? 0.3051 0.1894 0.2689 0.0232  0.0071  0.0105  134 PHE   A CB  
982  C  CG  . PHE   A 128 ? 0.3078 0.1938 0.2679 0.0238  0.0077  0.0089  134 PHE   A CG  
983  C  CD1 . PHE   A 128 ? 0.3204 0.2019 0.2774 0.0255  0.0081  0.0043  134 PHE   A CD1 
984  C  CD2 . PHE   A 128 ? 0.3111 0.2039 0.2705 0.0220  0.0076  0.0128  134 PHE   A CD2 
985  C  CE1 . PHE   A 128 ? 0.3245 0.2082 0.2776 0.0252  0.0083  0.0039  134 PHE   A CE1 
986  C  CE2 . PHE   A 128 ? 0.3175 0.2122 0.2731 0.0219  0.0081  0.0118  134 PHE   A CE2 
987  C  CZ  . PHE   A 128 ? 0.3189 0.2089 0.2712 0.0235  0.0084  0.0074  134 PHE   A CZ  
988  N  N   . ALA   A 129 ? 0.3111 0.1862 0.2864 0.0267  0.0064  0.0095  135 ALA   A N   
989  C  CA  . ALA   A 129 ? 0.3156 0.1900 0.2936 0.0240  0.0052  0.0125  135 ALA   A CA  
990  C  C   . ALA   A 129 ? 0.3057 0.1818 0.2763 0.0180  0.0052  0.0124  135 ALA   A C   
991  O  O   . ALA   A 129 ? 0.2994 0.1721 0.2658 0.0177  0.0064  0.0074  135 ALA   A O   
992  C  CB  . ALA   A 129 ? 0.3178 0.1854 0.2985 0.0262  0.0054  0.0086  135 ALA   A CB  
993  N  N   . ASP   A 130 ? 0.3053 0.1872 0.2747 0.0130  0.0041  0.0179  136 ASP   A N   
994  C  CA  . ASP   A 130 ? 0.3085 0.1921 0.2700 0.0061  0.0050  0.0169  136 ASP   A CA  
995  C  C   . ASP   A 130 ? 0.3098 0.1899 0.2708 0.0041  0.0062  0.0139  136 ASP   A C   
996  O  O   . ASP   A 130 ? 0.3227 0.2014 0.2891 0.0057  0.0049  0.0160  136 ASP   A O   
997  C  CB  . ASP   A 130 ? 0.3275 0.2193 0.2873 -0.0001 0.0030  0.0242  136 ASP   A CB  
998  C  CG  . ASP   A 130 ? 0.4187 0.3125 0.3686 -0.0087 0.0046  0.0223  136 ASP   A CG  
999  O  OD1 . ASP   A 130 ? 0.4166 0.3074 0.3611 -0.0094 0.0070  0.0168  136 ASP   A OD1 
1000 O  OD2 . ASP   A 130 ? 0.4615 0.3596 0.4093 -0.0151 0.0036  0.0261  136 ASP   A OD2 
1001 N  N   . VAL   A 131 ? 0.2965 0.1746 0.2520 0.0010  0.0090  0.0086  137 VAL   A N   
1002 C  CA  . VAL   A 131 ? 0.2992 0.1754 0.2548 -0.0014 0.0110  0.0055  137 VAL   A CA  
1003 C  C   . VAL   A 131 ? 0.3038 0.1833 0.2519 -0.0098 0.0139  0.0040  137 VAL   A C   
1004 O  O   . VAL   A 131 ? 0.3172 0.1966 0.2650 -0.0129 0.0165  0.0012  137 VAL   A O   
1005 C  CB  . VAL   A 131 ? 0.3069 0.1774 0.2660 0.0036  0.0125  -0.0004 137 VAL   A CB  
1006 C  CG1 . VAL   A 131 ? 0.3032 0.1707 0.2679 0.0100  0.0099  0.0003  137 VAL   A CG1 
1007 C  CG2 . VAL   A 131 ? 0.3194 0.1875 0.2757 0.0039  0.0149  -0.0047 137 VAL   A CG2 
1008 N  N   . ARG   A 132 ? 0.2979 0.1806 0.2398 -0.0141 0.0140  0.0053  138 ARG   A N   
1009 C  CA  . ARG   A 132 ? 0.2955 0.1805 0.2287 -0.0231 0.0174  0.0025  138 ARG   A CA  
1010 C  C   . ARG   A 132 ? 0.3202 0.2116 0.2496 -0.0314 0.0172  0.0060  138 ARG   A C   
1011 O  O   . ARG   A 132 ? 0.3257 0.2185 0.2479 -0.0391 0.0214  0.0016  138 ARG   A O   
1012 C  CB  . ARG   A 132 ? 0.2947 0.1820 0.2219 -0.0266 0.0168  0.0038  138 ARG   A CB  
1013 C  CG  . ARG   A 132 ? 0.2863 0.1676 0.2158 -0.0203 0.0175  0.0001  138 ARG   A CG  
1014 C  CD  . ARG   A 132 ? 0.3067 0.1911 0.2302 -0.0247 0.0165  0.0022  138 ARG   A CD  
1015 N  NE  . ARG   A 132 ? 0.3148 0.2061 0.2416 -0.0229 0.0115  0.0106  138 ARG   A NE  
1016 C  CZ  . ARG   A 132 ? 0.3229 0.2188 0.2470 -0.0253 0.0095  0.0144  138 ARG   A CZ  
1017 N  NH1 . ARG   A 132 ? 0.3539 0.2480 0.2703 -0.0310 0.0117  0.0108  138 ARG   A NH1 
1018 N  NH2 . ARG   A 132 ? 0.3146 0.2174 0.2445 -0.0227 0.0055  0.0221  138 ARG   A NH2 
1019 N  N   . ASP   A 133 ? 0.3230 0.2181 0.2573 -0.0302 0.0125  0.0139  139 ASP   A N   
1020 C  CA  . ASP   A 133 ? 0.3352 0.2369 0.2667 -0.0382 0.0114  0.0189  139 ASP   A CA  
1021 C  C   . ASP   A 133 ? 0.3309 0.2297 0.2658 -0.0373 0.0139  0.0153  139 ASP   A C   
1022 O  O   . ASP   A 133 ? 0.3337 0.2378 0.2653 -0.0448 0.0138  0.0183  139 ASP   A O   
1023 C  CB  . ASP   A 133 ? 0.3648 0.2719 0.3020 -0.0377 0.0049  0.0304  139 ASP   A CB  
1024 C  CG  . ASP   A 133 ? 0.4018 0.3031 0.3510 -0.0274 0.0027  0.0319  139 ASP   A CG  
1025 O  OD1 . ASP   A 133 ? 0.4088 0.3035 0.3611 -0.0194 0.0044  0.0261  139 ASP   A OD1 
1026 O  OD2 . ASP   A 133 ? 0.4099 0.3131 0.3650 -0.0278 -0.0005 0.0388  139 ASP   A OD2 
1027 N  N   . LEU   A 134 ? 0.3217 0.2132 0.2634 -0.0287 0.0155  0.0098  140 LEU   A N   
1028 C  CA  . LEU   A 134 ? 0.3185 0.2077 0.2648 -0.0272 0.0173  0.0068  140 LEU   A CA  
1029 C  C   . LEU   A 134 ? 0.3252 0.2143 0.2676 -0.0312 0.0240  -0.0016 140 LEU   A C   
1030 O  O   . LEU   A 134 ? 0.3203 0.2044 0.2675 -0.0256 0.0270  -0.0078 140 LEU   A O   
1031 C  CB  . LEU   A 134 ? 0.3151 0.1976 0.2705 -0.0171 0.0155  0.0053  140 LEU   A CB  
1032 C  CG  . LEU   A 134 ? 0.3259 0.2072 0.2864 -0.0124 0.0103  0.0117  140 LEU   A CG  
1033 C  CD1 . LEU   A 134 ? 0.3436 0.2183 0.3108 -0.0040 0.0094  0.0085  140 LEU   A CD1 
1034 C  CD2 . LEU   A 134 ? 0.3337 0.2182 0.2968 -0.0163 0.0073  0.0189  140 LEU   A CD2 
1035 N  N   . LEU   A 135 ? 0.3448 0.2400 0.2787 -0.0414 0.0267  -0.0015 141 LEU   A N   
1036 C  CA  . LEU   A 135 ? 0.3564 0.2518 0.2860 -0.0463 0.0345  -0.0105 141 LEU   A CA  
1037 C  C   . LEU   A 135 ? 0.3549 0.2487 0.2926 -0.0429 0.0385  -0.0156 141 LEU   A C   
1038 O  O   . LEU   A 135 ? 0.3603 0.2513 0.3002 -0.0418 0.0450  -0.0239 141 LEU   A O   
1039 C  CB  . LEU   A 135 ? 0.3629 0.2663 0.2802 -0.0596 0.0366  -0.0095 141 LEU   A CB  
1040 C  CG  . LEU   A 135 ? 0.3751 0.2827 0.2844 -0.0649 0.0317  -0.0027 141 LEU   A CG  
1041 C  CD1 . LEU   A 135 ? 0.3934 0.3100 0.2894 -0.0798 0.0337  -0.0018 141 LEU   A CD1 
1042 C  CD2 . LEU   A 135 ? 0.3859 0.2876 0.2950 -0.0600 0.0321  -0.0063 141 LEU   A CD2 
1043 N  N   . TRP   A 136 ? 0.3512 0.2465 0.2946 -0.0409 0.0346  -0.0103 142 TRP   A N   
1044 C  CA  . TRP   A 136 ? 0.3478 0.2428 0.2993 -0.0383 0.0376  -0.0140 142 TRP   A CA  
1045 C  C   . TRP   A 136 ? 0.3469 0.2354 0.3082 -0.0283 0.0383  -0.0186 142 TRP   A C   
1046 O  O   . TRP   A 136 ? 0.3444 0.2335 0.3131 -0.0264 0.0420  -0.0227 142 TRP   A O   
1047 C  CB  . TRP   A 136 ? 0.3452 0.2427 0.3002 -0.0392 0.0326  -0.0069 142 TRP   A CB  
1048 C  CG  . TRP   A 136 ? 0.3333 0.2261 0.2920 -0.0329 0.0252  -0.0004 142 TRP   A CG  
1049 C  CD1 . TRP   A 136 ? 0.3414 0.2358 0.2969 -0.0353 0.0201  0.0076  142 TRP   A CD1 
1050 C  CD2 . TRP   A 136 ? 0.3273 0.2138 0.2946 -0.0238 0.0225  -0.0012 142 TRP   A CD2 
1051 N  NE1 . TRP   A 136 ? 0.3387 0.2274 0.3010 -0.0274 0.0152  0.0108  142 TRP   A NE1 
1052 C  CE2 . TRP   A 136 ? 0.3350 0.2187 0.3034 -0.0208 0.0167  0.0050  142 TRP   A CE2 
1053 C  CE3 . TRP   A 136 ? 0.3304 0.2139 0.3049 -0.0182 0.0243  -0.0065 142 TRP   A CE3 
1054 C  CZ2 . TRP   A 136 ? 0.3340 0.2114 0.3088 -0.0131 0.0135  0.0049  142 TRP   A CZ2 
1055 C  CZ3 . TRP   A 136 ? 0.3311 0.2093 0.3113 -0.0113 0.0201  -0.0055 142 TRP   A CZ3 
1056 C  CH2 . TRP   A 136 ? 0.3288 0.2037 0.3083 -0.0090 0.0151  -0.0005 142 TRP   A CH2 
1057 N  N   . LEU   A 137 ? 0.3448 0.2282 0.3064 -0.0224 0.0348  -0.0175 143 LEU   A N   
1058 C  CA  . LEU   A 137 ? 0.3585 0.2365 0.3283 -0.0141 0.0349  -0.0208 143 LEU   A CA  
1059 C  C   . LEU   A 137 ? 0.3834 0.2605 0.3566 -0.0144 0.0424  -0.0284 143 LEU   A C   
1060 O  O   . LEU   A 137 ? 0.3739 0.2483 0.3569 -0.0083 0.0430  -0.0305 143 LEU   A O   
1061 C  CB  . LEU   A 137 ? 0.3489 0.2228 0.3165 -0.0096 0.0306  -0.0183 143 LEU   A CB  
1062 C  CG  . LEU   A 137 ? 0.3469 0.2199 0.3152 -0.0064 0.0241  -0.0122 143 LEU   A CG  
1063 C  CD1 . LEU   A 137 ? 0.3548 0.2250 0.3205 -0.0027 0.0213  -0.0107 143 LEU   A CD1 
1064 C  CD2 . LEU   A 137 ? 0.3480 0.2189 0.3247 -0.0014 0.0219  -0.0124 143 LEU   A CD2 
1065 N  N   . ASP   A 138 ? 0.4094 0.2886 0.3748 -0.0219 0.0480  -0.0323 144 ASP   A N   
1066 C  CA  . ASP   A 138 ? 0.4566 0.3338 0.4246 -0.0231 0.0564  -0.0407 144 ASP   A CA  
1067 C  C   . ASP   A 138 ? 0.5041 0.3859 0.4779 -0.0259 0.0632  -0.0455 144 ASP   A C   
1068 O  O   . ASP   A 138 ? 0.5014 0.3818 0.4780 -0.0274 0.0716  -0.0533 144 ASP   A O   
1069 C  CB  . ASP   A 138 ? 0.4886 0.3657 0.4438 -0.0313 0.0600  -0.0438 144 ASP   A CB  
1070 C  CG  . ASP   A 138 ? 0.5785 0.4515 0.5284 -0.0294 0.0550  -0.0404 144 ASP   A CG  
1071 O  OD1 . ASP   A 138 ? 0.5955 0.4642 0.5525 -0.0210 0.0507  -0.0379 144 ASP   A OD1 
1072 O  OD2 . ASP   A 138 ? 0.6232 0.4982 0.5614 -0.0370 0.0551  -0.0400 144 ASP   A OD2 
1073 N  N   . GLU   A 139 ? 0.5357 0.4230 0.5116 -0.0270 0.0604  -0.0413 145 GLU   A N   
1074 C  CA  . GLU   A 139 ? 0.5682 0.4615 0.5493 -0.0306 0.0671  -0.0456 145 GLU   A CA  
1075 C  C   . GLU   A 139 ? 0.5970 0.4940 0.5868 -0.0275 0.0626  -0.0405 145 GLU   A C   
1076 O  O   . GLU   A 139 ? 0.5946 0.4886 0.5854 -0.0229 0.0544  -0.0342 145 GLU   A O   
1077 C  CB  . GLU   A 139 ? 0.6045 0.5038 0.5719 -0.0426 0.0713  -0.0472 145 GLU   A CB  
1078 C  CG  . GLU   A 139 ? 0.6814 0.5844 0.6399 -0.0472 0.0632  -0.0377 145 GLU   A CG  
1079 C  CD  . GLU   A 139 ? 0.7891 0.6949 0.7321 -0.0569 0.0628  -0.0361 145 GLU   A CD  
1080 O  OE1 . GLU   A 139 ? 0.8157 0.7273 0.7522 -0.0633 0.0581  -0.0286 145 GLU   A OE1 
1081 O  OE2 . GLU   A 139 ? 0.8248 0.7272 0.7625 -0.0585 0.0669  -0.0417 145 GLU   A OE2 
1082 N  N   . GLU   A 140 ? 0.6201 0.5235 0.6160 -0.0305 0.0685  -0.0438 146 GLU   A N   
1083 C  CA  . GLU   A 140 ? 0.6466 0.5549 0.6509 -0.0293 0.0655  -0.0398 146 GLU   A CA  
1084 C  C   . GLU   A 140 ? 0.6560 0.5612 0.6748 -0.0195 0.0620  -0.0386 146 GLU   A C   
1085 O  O   . GLU   A 140 ? 0.6576 0.5644 0.6888 -0.0158 0.0677  -0.0432 146 GLU   A O   
1086 C  CB  . GLU   A 140 ? 0.6956 0.6052 0.6908 -0.0339 0.0578  -0.0316 146 GLU   A CB  
1087 C  CG  . GLU   A 140 ? 0.7806 0.6909 0.7840 -0.0307 0.0516  -0.0262 146 GLU   A CG  
1088 C  CD  . GLU   A 140 ? 0.8805 0.7994 0.8875 -0.0366 0.0548  -0.0259 146 GLU   A CD  
1089 O  OE1 . GLU   A 140 ? 0.9076 0.8279 0.9102 -0.0412 0.0499  -0.0195 146 GLU   A OE1 
1090 O  OE2 . GLU   A 140 ? 0.9062 0.8303 0.9214 -0.0366 0.0625  -0.0317 146 GLU   A OE2 
1091 N  N   . SER   B 1   ? 0.3991 0.2484 0.3498 0.0089  -0.0232 0.0519  7   SER   C N   
1092 C  CA  . SER   B 1   ? 0.4033 0.2577 0.3678 0.0089  -0.0244 0.0538  7   SER   C CA  
1093 C  C   . SER   B 1   ? 0.3952 0.2522 0.3603 0.0096  -0.0230 0.0507  7   SER   C C   
1094 O  O   . SER   B 1   ? 0.4051 0.2585 0.3592 0.0096  -0.0236 0.0480  7   SER   C O   
1095 C  CB  . SER   B 1   ? 0.4334 0.2854 0.4007 0.0069  -0.0319 0.0593  7   SER   C CB  
1096 O  OG  . SER   B 1   ? 0.4670 0.3139 0.4243 0.0051  -0.0372 0.0592  7   SER   C OG  
1097 N  N   . GLY   B 2   ? 0.3815 0.2441 0.3590 0.0105  -0.0207 0.0511  8   GLY   C N   
1098 C  CA  . GLY   B 2   ? 0.3684 0.2332 0.3469 0.0110  -0.0188 0.0489  8   GLY   C CA  
1099 C  C   . GLY   B 2   ? 0.3441 0.2144 0.3335 0.0130  -0.0133 0.0480  8   GLY   C C   
1100 O  O   . GLY   B 2   ? 0.3340 0.2058 0.3271 0.0146  -0.0096 0.0466  8   GLY   C O   
1101 N  N   . ALA   B 3   ? 0.3325 0.2048 0.3262 0.0130  -0.0125 0.0486  9   ALA   C N   
1102 C  CA  . ALA   B 3   ? 0.3259 0.2023 0.3277 0.0151  -0.0065 0.0476  9   ALA   C CA  
1103 C  C   . ALA   B 3   ? 0.3233 0.1992 0.3200 0.0156  -0.0043 0.0454  9   ALA   C C   
1104 O  O   . ALA   B 3   ? 0.3297 0.2024 0.3190 0.0139  -0.0080 0.0455  9   ALA   C O   
1105 C  CB  . ALA   B 3   ? 0.3231 0.2037 0.3401 0.0149  -0.0065 0.0525  9   ALA   C CB  
1106 N  N   . ILE   B 4   ? 0.3186 0.1963 0.3179 0.0180  0.0018  0.0433  10  ILE   C N   
1107 C  CA  . ILE   B 4   ? 0.3312 0.2079 0.3259 0.0186  0.0046  0.0420  10  ILE   C CA  
1108 C  C   . ILE   B 4   ? 0.3375 0.2181 0.3448 0.0188  0.0083  0.0460  10  ILE   C C   
1109 O  O   . ILE   B 4   ? 0.3375 0.2210 0.3539 0.0205  0.0118  0.0468  10  ILE   C O   
1110 C  CB  . ILE   B 4   ? 0.3379 0.2127 0.3242 0.0215  0.0087  0.0365  10  ILE   C CB  
1111 C  CG1 . ILE   B 4   ? 0.3499 0.2227 0.3279 0.0216  0.0058  0.0328  10  ILE   C CG1 
1112 C  CG2 . ILE   B 4   ? 0.3470 0.2196 0.3269 0.0222  0.0109  0.0358  10  ILE   C CG2 
1113 C  CD1 . ILE   B 4   ? 0.3542 0.2260 0.3270 0.0242  0.0090  0.0274  10  ILE   C CD1 
1114 N  N   . TYR   B 5   ? 0.3323 0.2131 0.3410 0.0170  0.0077  0.0489  11  TYR   C N   
1115 C  CA  . TYR   B 5   ? 0.3337 0.2189 0.3555 0.0169  0.0118  0.0532  11  TYR   C CA  
1116 C  C   . TYR   B 5   ? 0.3510 0.2341 0.3664 0.0181  0.0176  0.0519  11  TYR   C C   
1117 O  O   . TYR   B 5   ? 0.3714 0.2517 0.3811 0.0160  0.0152  0.0529  11  TYR   C O   
1118 C  CB  . TYR   B 5   ? 0.3246 0.2122 0.3560 0.0129  0.0058  0.0588  11  TYR   C CB  
1119 C  CG  . TYR   B 5   ? 0.3265 0.2156 0.3640 0.0119  0.0000  0.0607  11  TYR   C CG  
1120 C  CD1 . TYR   B 5   ? 0.3337 0.2279 0.3856 0.0134  0.0023  0.0633  11  TYR   C CD1 
1121 C  CD2 . TYR   B 5   ? 0.3347 0.2193 0.3625 0.0099  -0.0074 0.0597  11  TYR   C CD2 
1122 C  CE1 . TYR   B 5   ? 0.3425 0.2373 0.3989 0.0128  -0.0032 0.0653  11  TYR   C CE1 
1123 C  CE2 . TYR   B 5   ? 0.3520 0.2367 0.3832 0.0091  -0.0125 0.0616  11  TYR   C CE2 
1124 C  CZ  . TYR   B 5   ? 0.3626 0.2524 0.4082 0.0104  -0.0107 0.0645  11  TYR   C CZ  
1125 O  OH  . TYR   B 5   ? 0.3874 0.2768 0.4362 0.0097  -0.0160 0.0669  11  TYR   C OH  
1126 N  N   . VAL   B 6   ? 0.3427 0.2256 0.3569 0.0216  0.0250  0.0494  12  VAL   C N   
1127 C  CA  . VAL   B 6   ? 0.3543 0.2339 0.3602 0.0233  0.0311  0.0481  12  VAL   C CA  
1128 C  C   . VAL   B 6   ? 0.3580 0.2412 0.3749 0.0254  0.0397  0.0507  12  VAL   C C   
1129 O  O   . VAL   B 6   ? 0.3609 0.2464 0.3851 0.0276  0.0423  0.0499  12  VAL   C O   
1130 C  CB  . VAL   B 6   ? 0.3746 0.2484 0.3641 0.0259  0.0314  0.0415  12  VAL   C CB  
1131 C  CG1 . VAL   B 6   ? 0.3769 0.2512 0.3680 0.0283  0.0325  0.0379  12  VAL   C CG1 
1132 C  CG2 . VAL   B 6   ? 0.3786 0.2478 0.3578 0.0279  0.0372  0.0403  12  VAL   C CG2 
1133 N  N   . GLY   B 7   ? 0.3546 0.2386 0.3746 0.0245  0.0442  0.0545  13  GLY   C N   
1134 C  CA  . GLY   B 7   ? 0.3419 0.2299 0.3737 0.0264  0.0533  0.0577  13  GLY   C CA  
1135 C  C   . GLY   B 7   ? 0.3320 0.2278 0.3841 0.0262  0.0522  0.0614  13  GLY   C C   
1136 O  O   . GLY   B 7   ? 0.3296 0.2291 0.3902 0.0226  0.0443  0.0646  13  GLY   C O   
1137 N  N   . ASN   B 8   ? 0.3201 0.2176 0.3789 0.0303  0.0594  0.0606  14  ASN   C N   
1138 C  CA  . ASN   B 8   ? 0.3117 0.2160 0.3894 0.0308  0.0580  0.0637  14  ASN   C CA  
1139 C  C   . ASN   B 8   ? 0.3066 0.2076 0.3786 0.0325  0.0536  0.0591  14  ASN   C C   
1140 O  O   . ASN   B 8   ? 0.3079 0.2114 0.3907 0.0351  0.0559  0.0597  14  ASN   C O   
1141 C  CB  . ASN   B 8   ? 0.3388 0.2481 0.4317 0.0341  0.0682  0.0670  14  ASN   C CB  
1142 C  CG  . ASN   B 8   ? 0.4007 0.3161 0.5062 0.0311  0.0705  0.0736  14  ASN   C CG  
1143 O  OD1 . ASN   B 8   ? 0.4114 0.3348 0.5361 0.0284  0.0660  0.0793  14  ASN   C OD1 
1144 N  ND2 . ASN   B 8   ? 0.4197 0.3311 0.5143 0.0313  0.0771  0.0731  14  ASN   C ND2 
1145 N  N   . TYR   B 9   ? 0.3021 0.1978 0.3584 0.0307  0.0472  0.0550  15  TYR   C N   
1146 C  CA  . TYR   B 9   ? 0.3170 0.2097 0.3679 0.0316  0.0430  0.0510  15  TYR   C CA  
1147 C  C   . TYR   B 9   ? 0.3153 0.2085 0.3647 0.0277  0.0329  0.0522  15  TYR   C C   
1148 O  O   . TYR   B 9   ? 0.3152 0.2076 0.3589 0.0248  0.0289  0.0533  15  TYR   C O   
1149 C  CB  . TYR   B 9   ? 0.3331 0.2185 0.3659 0.0337  0.0454  0.0441  15  TYR   C CB  
1150 C  CG  . TYR   B 9   ? 0.3631 0.2454 0.3929 0.0378  0.0549  0.0417  15  TYR   C CG  
1151 C  CD1 . TYR   B 9   ? 0.3846 0.2675 0.4235 0.0411  0.0600  0.0414  15  TYR   C CD1 
1152 C  CD2 . TYR   B 9   ? 0.3943 0.2716 0.4100 0.0387  0.0587  0.0392  15  TYR   C CD2 
1153 C  CE1 . TYR   B 9   ? 0.4085 0.2870 0.4426 0.0453  0.0692  0.0387  15  TYR   C CE1 
1154 C  CE2 . TYR   B 9   ? 0.4215 0.2944 0.4317 0.0426  0.0676  0.0369  15  TYR   C CE2 
1155 C  CZ  . TYR   B 9   ? 0.4397 0.3130 0.4588 0.0460  0.0731  0.0364  15  TYR   C CZ  
1156 O  OH  . TYR   B 9   ? 0.4869 0.3544 0.4988 0.0502  0.0823  0.0335  15  TYR   C OH  
1157 N  N   . ARG   B 10  ? 0.3038 0.1969 0.3560 0.0279  0.0291  0.0517  16  ARG   C N   
1158 C  CA  . ARG   B 10  ? 0.3010 0.1931 0.3494 0.0248  0.0205  0.0523  16  ARG   C CA  
1159 C  C   . ARG   B 10  ? 0.3060 0.1936 0.3444 0.0263  0.0206  0.0470  16  ARG   C C   
1160 O  O   . ARG   B 10  ? 0.3081 0.1953 0.3515 0.0287  0.0240  0.0459  16  ARG   C O   
1161 C  CB  . ARG   B 10  ? 0.3191 0.2155 0.3824 0.0235  0.0158  0.0581  16  ARG   C CB  
1162 C  CG  . ARG   B 10  ? 0.3415 0.2351 0.3997 0.0215  0.0082  0.0584  16  ARG   C CG  
1163 C  CD  . ARG   B 10  ? 0.3530 0.2499 0.4243 0.0199  0.0023  0.0645  16  ARG   C CD  
1164 N  NE  . ARG   B 10  ? 0.3633 0.2572 0.4322 0.0198  -0.0017 0.0648  16  ARG   C NE  
1165 C  CZ  . ARG   B 10  ? 0.3842 0.2743 0.4443 0.0170  -0.0089 0.0657  16  ARG   C CZ  
1166 N  NH1 . ARG   B 10  ? 0.3684 0.2567 0.4200 0.0142  -0.0130 0.0656  16  ARG   C NH1 
1167 N  NH2 . ARG   B 10  ? 0.3813 0.2683 0.4393 0.0172  -0.0114 0.0664  16  ARG   C NH2 
1168 N  N   . VAL   B 11  ? 0.3022 0.1863 0.3271 0.0249  0.0173  0.0435  17  VAL   C N   
1169 C  CA  . VAL   B 11  ? 0.3059 0.1866 0.3224 0.0257  0.0172  0.0386  17  VAL   C CA  
1170 C  C   . VAL   B 11  ? 0.3117 0.1918 0.3263 0.0233  0.0113  0.0400  17  VAL   C C   
1171 O  O   . VAL   B 11  ? 0.3043 0.1837 0.3130 0.0212  0.0069  0.0409  17  VAL   C O   
1172 C  CB  . VAL   B 11  ? 0.3222 0.1998 0.3258 0.0265  0.0186  0.0336  17  VAL   C CB  
1173 C  CG1 . VAL   B 11  ? 0.3331 0.2082 0.3312 0.0274  0.0188  0.0286  17  VAL   C CG1 
1174 C  CG2 . VAL   B 11  ? 0.3276 0.2047 0.3304 0.0285  0.0242  0.0330  17  VAL   C CG2 
1175 N  N   . VAL   B 12  ? 0.3088 0.1883 0.3277 0.0238  0.0113  0.0402  18  VAL   C N   
1176 C  CA  A VAL   B 12  ? 0.3074 0.1855 0.3242 0.0217  0.0065  0.0420  18  VAL   C CA  
1177 C  CA  B VAL   B 12  ? 0.3122 0.1903 0.3291 0.0217  0.0065  0.0421  18  VAL   C CA  
1178 C  C   . VAL   B 12  ? 0.3086 0.1842 0.3219 0.0222  0.0082  0.0385  18  VAL   C C   
1179 O  O   . VAL   B 12  ? 0.3047 0.1796 0.3200 0.0241  0.0124  0.0352  18  VAL   C O   
1180 C  CB  A VAL   B 12  ? 0.3125 0.1920 0.3401 0.0211  0.0036  0.0479  18  VAL   C CB  
1181 C  CB  B VAL   B 12  ? 0.3262 0.2061 0.3546 0.0212  0.0039  0.0480  18  VAL   C CB  
1182 C  CG1 A VAL   B 12  ? 0.3217 0.2032 0.3518 0.0192  -0.0007 0.0520  18  VAL   C CG1 
1183 C  CG1 B VAL   B 12  ? 0.3353 0.2126 0.3608 0.0193  -0.0010 0.0506  18  VAL   C CG1 
1184 C  CG2 A VAL   B 12  ? 0.3028 0.1839 0.3422 0.0239  0.0082  0.0486  18  VAL   C CG2 
1185 C  CG2 B VAL   B 12  ? 0.3332 0.2161 0.3668 0.0202  0.0017  0.0517  18  VAL   C CG2 
1186 N  N   . ASN   B 13  ? 0.2931 0.1670 0.3011 0.0202  0.0051  0.0391  19  ASN   C N   
1187 C  CA  . ASN   B 13  ? 0.2795 0.1514 0.2860 0.0199  0.0065  0.0370  19  ASN   C CA  
1188 C  C   . ASN   B 13  ? 0.2740 0.1450 0.2908 0.0209  0.0078  0.0396  19  ASN   C C   
1189 O  O   . ASN   B 13  ? 0.2712 0.1424 0.2932 0.0205  0.0050  0.0446  19  ASN   C O   
1190 C  CB  . ASN   B 13  ? 0.2993 0.1694 0.2995 0.0177  0.0034  0.0390  19  ASN   C CB  
1191 C  CG  . ASN   B 13  ? 0.3118 0.1820 0.3019 0.0171  0.0024  0.0364  19  ASN   C CG  
1192 O  OD1 . ASN   B 13  ? 0.3233 0.1927 0.3084 0.0163  -0.0009 0.0383  19  ASN   C OD1 
1193 N  ND2 . ASN   B 13  ? 0.2658 0.1368 0.2531 0.0175  0.0049  0.0320  19  ASN   C ND2 
1194 N  N   . ARG   B 14  ? 0.2772 0.1464 0.2968 0.0221  0.0114  0.0363  20  ARG   C N   
1195 C  CA  . ARG   B 14  ? 0.2713 0.1385 0.3003 0.0235  0.0128  0.0385  20  ARG   C CA  
1196 C  C   . ARG   B 14  ? 0.2901 0.1554 0.3208 0.0217  0.0093  0.0438  20  ARG   C C   
1197 O  O   . ARG   B 14  ? 0.3074 0.1724 0.3465 0.0228  0.0082  0.0481  20  ARG   C O   
1198 C  CB  . ARG   B 14  ? 0.2847 0.1486 0.3139 0.0245  0.0165  0.0336  20  ARG   C CB  
1199 C  CG  . ARG   B 14  ? 0.3029 0.1637 0.3415 0.0270  0.0191  0.0346  20  ARG   C CG  
1200 C  CD  . ARG   B 14  ? 0.3077 0.1636 0.3445 0.0271  0.0216  0.0294  20  ARG   C CD  
1201 N  NE  . ARG   B 14  ? 0.3404 0.1917 0.3845 0.0298  0.0245  0.0293  20  ARG   C NE  
1202 C  CZ  . ARG   B 14  ? 0.3597 0.2071 0.4095 0.0293  0.0237  0.0323  20  ARG   C CZ  
1203 N  NH1 . ARG   B 14  ? 0.3379 0.1858 0.3865 0.0262  0.0202  0.0362  20  ARG   C NH1 
1204 N  NH2 . ARG   B 14  ? 0.3317 0.1741 0.3878 0.0323  0.0267  0.0316  20  ARG   C NH2 
1205 N  N   . HIS   B 15  ? 0.2951 0.1590 0.3179 0.0191  0.0076  0.0438  21  HIS   C N   
1206 C  CA  . HIS   B 15  ? 0.3141 0.1747 0.3361 0.0174  0.0047  0.0489  21  HIS   C CA  
1207 C  C   . HIS   B 15  ? 0.3338 0.1948 0.3549 0.0168  -0.0006 0.0543  21  HIS   C C   
1208 O  O   . HIS   B 15  ? 0.3489 0.2063 0.3694 0.0158  -0.0038 0.0592  21  HIS   C O   
1209 C  CB  . HIS   B 15  ? 0.3258 0.1844 0.3394 0.0150  0.0055  0.0475  21  HIS   C CB  
1210 C  CG  . HIS   B 15  ? 0.3387 0.1989 0.3423 0.0138  0.0039  0.0466  21  HIS   C CG  
1211 N  ND1 . HIS   B 15  ? 0.3519 0.2152 0.3520 0.0143  0.0060  0.0414  21  HIS   C ND1 
1212 C  CD2 . HIS   B 15  ? 0.3502 0.2081 0.3458 0.0124  0.0006  0.0502  21  HIS   C CD2 
1213 C  CE1 . HIS   B 15  ? 0.3613 0.2245 0.3525 0.0134  0.0041  0.0419  21  HIS   C CE1 
1214 N  NE2 . HIS   B 15  ? 0.3660 0.2256 0.3535 0.0122  0.0011  0.0469  21  HIS   C NE2 
1215 N  N   . LEU   B 16  ? 0.3317 0.1964 0.3527 0.0173  -0.0019 0.0537  22  LEU   C N   
1216 C  CA  . LEU   B 16  ? 0.3360 0.2013 0.3574 0.0165  -0.0075 0.0583  22  LEU   C CA  
1217 C  C   . LEU   B 16  ? 0.3411 0.2107 0.3759 0.0184  -0.0076 0.0606  22  LEU   C C   
1218 O  O   . LEU   B 16  ? 0.3429 0.2140 0.3807 0.0174  -0.0126 0.0646  22  LEU   C O   
1219 C  CB  . LEU   B 16  ? 0.3420 0.2072 0.3521 0.0148  -0.0096 0.0565  22  LEU   C CB  
1220 C  CG  . LEU   B 16  ? 0.3614 0.2227 0.3586 0.0133  -0.0093 0.0550  22  LEU   C CG  
1221 C  CD1 . LEU   B 16  ? 0.3717 0.2327 0.3585 0.0125  -0.0106 0.0525  22  LEU   C CD1 
1222 C  CD2 . LEU   B 16  ? 0.3771 0.2332 0.3705 0.0118  -0.0130 0.0600  22  LEU   C CD2 
1223 N  N   . ALA   B 17  ? 0.3428 0.2140 0.3857 0.0210  -0.0020 0.0581  23  ALA   C N   
1224 C  CA  . ALA   B 17  ? 0.3523 0.2278 0.4085 0.0235  -0.0003 0.0600  23  ALA   C CA  
1225 C  C   . ALA   B 17  ? 0.3574 0.2332 0.4241 0.0237  -0.0052 0.0667  23  ALA   C C   
1226 O  O   . ALA   B 17  ? 0.3574 0.2290 0.4228 0.0233  -0.0073 0.0688  23  ALA   C O   
1227 C  CB  . ALA   B 17  ? 0.3528 0.2277 0.4134 0.0266  0.0068  0.0558  23  ALA   C CB  
1228 N  N   . THR   B 18  ? 0.3519 0.2329 0.4291 0.0240  -0.0074 0.0704  24  THR   C N   
1229 C  CA  . THR   B 18  ? 0.3506 0.2332 0.4400 0.0243  -0.0130 0.0771  24  THR   C CA  
1230 C  C   . THR   B 18  ? 0.3535 0.2388 0.4594 0.0287  -0.0077 0.0782  24  THR   C C   
1231 O  O   . THR   B 18  ? 0.3474 0.2331 0.4538 0.0313  0.0002  0.0734  24  THR   C O   
1232 C  CB  . THR   B 18  ? 0.3550 0.2424 0.4489 0.0220  -0.0185 0.0807  24  THR   C CB  
1233 O  OG1 . THR   B 18  ? 0.3607 0.2541 0.4636 0.0238  -0.0125 0.0791  24  THR   C OG1 
1234 C  CG2 . THR   B 18  ? 0.3599 0.2435 0.4371 0.0181  -0.0235 0.0793  24  THR   C CG2 
1235 N  N   . HIS   B 19  ? 0.3468 0.2340 0.4665 0.0299  -0.0122 0.0844  25  HIS   C N   
1236 C  CA  . HIS   B 19  ? 0.3509 0.2412 0.4882 0.0346  -0.0074 0.0859  25  HIS   C CA  
1237 C  C   . HIS   B 19  ? 0.3493 0.2470 0.4957 0.0363  -0.0013 0.0846  25  HIS   C C   
1238 O  O   . HIS   B 19  ? 0.3622 0.2599 0.5122 0.0400  0.0075  0.0810  25  HIS   C O   
1239 C  CB  . HIS   B 19  ? 0.3652 0.2572 0.5168 0.0355  -0.0147 0.0936  25  HIS   C CB  
1240 C  CG  . HIS   B 19  ? 0.3981 0.2953 0.5710 0.0407  -0.0099 0.0959  25  HIS   C CG  
1241 N  ND1 . HIS   B 19  ? 0.4260 0.3187 0.6022 0.0450  -0.0039 0.0940  25  HIS   C ND1 
1242 C  CD2 . HIS   B 19  ? 0.4130 0.3195 0.6046 0.0422  -0.0096 0.0998  25  HIS   C CD2 
1243 C  CE1 . HIS   B 19  ? 0.4241 0.3230 0.6203 0.0494  -0.0001 0.0967  25  HIS   C CE1 
1244 N  NE2 . HIS   B 19  ? 0.4198 0.3278 0.6267 0.0479  -0.0031 0.1004  25  HIS   C NE2 
1245 N  N   . ASN   B 20  ? 0.3373 0.2403 0.4858 0.0332  -0.0055 0.0871  26  ASN   C N   
1246 C  CA  . ASN   B 20  ? 0.3384 0.2481 0.4949 0.0341  0.0005  0.0864  26  ASN   C CA  
1247 C  C   . ASN   B 20  ? 0.3368 0.2431 0.4801 0.0354  0.0096  0.0789  26  ASN   C C   
1248 O  O   . ASN   B 20  ? 0.3344 0.2436 0.4851 0.0389  0.0181  0.0775  26  ASN   C O   
1249 C  CB  . ASN   B 20  ? 0.3674 0.2816 0.5257 0.0297  -0.0065 0.0899  26  ASN   C CB  
1250 C  CG  . ASN   B 20  ? 0.4361 0.3575 0.6051 0.0304  -0.0001 0.0904  26  ASN   C CG  
1251 O  OD1 . ASN   B 20  ? 0.4605 0.3888 0.6495 0.0333  0.0034  0.0942  26  ASN   C OD1 
1252 N  ND2 . ASN   B 20  ? 0.4600 0.3799 0.6160 0.0281  0.0022  0.0867  26  ASN   C ND2 
1253 N  N   . ASP   B 21  ? 0.3328 0.2330 0.4569 0.0329  0.0079  0.0744  27  ASP   C N   
1254 C  CA  . ASP   B 21  ? 0.3316 0.2280 0.4427 0.0340  0.0149  0.0673  27  ASP   C CA  
1255 C  C   . ASP   B 21  ? 0.3319 0.2249 0.4465 0.0386  0.0221  0.0643  27  ASP   C C   
1256 O  O   . ASP   B 21  ? 0.3318 0.2246 0.4452 0.0412  0.0299  0.0606  27  ASP   C O   
1257 C  CB  . ASP   B 21  ? 0.3229 0.2137 0.4157 0.0308  0.0110  0.0637  27  ASP   C CB  
1258 C  CG  . ASP   B 21  ? 0.3200 0.2120 0.4049 0.0269  0.0056  0.0647  27  ASP   C CG  
1259 O  OD1 . ASP   B 21  ? 0.3070 0.2032 0.3965 0.0265  0.0069  0.0659  27  ASP   C OD1 
1260 O  OD2 . ASP   B 21  ? 0.3054 0.1936 0.3797 0.0242  0.0002  0.0645  27  ASP   C OD2 
1261 N  N   . TRP   B 22  ? 0.3290 0.2184 0.4468 0.0394  0.0196  0.0657  28  TRP   C N   
1262 C  CA  . TRP   B 22  ? 0.3315 0.2164 0.4528 0.0437  0.0258  0.0629  28  TRP   C CA  
1263 C  C   . TRP   B 22  ? 0.3304 0.2200 0.4689 0.0485  0.0319  0.0654  28  TRP   C C   
1264 O  O   . TRP   B 22  ? 0.3314 0.2176 0.4695 0.0525  0.0400  0.0612  28  TRP   C O   
1265 C  CB  . TRP   B 22  ? 0.3263 0.2056 0.4475 0.0433  0.0214  0.0646  28  TRP   C CB  
1266 C  CG  . TRP   B 22  ? 0.3335 0.2068 0.4383 0.0400  0.0193  0.0605  28  TRP   C CG  
1267 C  CD1 . TRP   B 22  ? 0.3427 0.2152 0.4390 0.0357  0.0126  0.0625  28  TRP   C CD1 
1268 C  CD2 . TRP   B 22  ? 0.3372 0.2044 0.4323 0.0406  0.0241  0.0537  28  TRP   C CD2 
1269 N  NE1 . TRP   B 22  ? 0.3520 0.2193 0.4356 0.0338  0.0136  0.0578  28  TRP   C NE1 
1270 C  CE2 . TRP   B 22  ? 0.3498 0.2142 0.4330 0.0364  0.0201  0.0523  28  TRP   C CE2 
1271 C  CE3 . TRP   B 22  ? 0.3418 0.2053 0.4369 0.0441  0.0312  0.0486  28  TRP   C CE3 
1272 C  CZ2 . TRP   B 22  ? 0.3619 0.2209 0.4357 0.0356  0.0224  0.0465  28  TRP   C CZ2 
1273 C  CZ3 . TRP   B 22  ? 0.3560 0.2131 0.4398 0.0431  0.0329  0.0424  28  TRP   C CZ3 
1274 C  CH2 . TRP   B 22  ? 0.3637 0.2192 0.4381 0.0387  0.0283  0.0416  28  TRP   C CH2 
1275 N  N   . ALA   B 23  ? 0.3254 0.2229 0.4789 0.0480  0.0281  0.0721  29  ALA   C N   
1276 C  CA  . ALA   B 23  ? 0.3337 0.2376 0.5067 0.0524  0.0337  0.0755  29  ALA   C CA  
1277 C  C   . ALA   B 23  ? 0.3482 0.2557 0.5196 0.0533  0.0420  0.0729  29  ALA   C C   
1278 O  O   . ALA   B 23  ? 0.3551 0.2669 0.5402 0.0575  0.0496  0.0744  29  ALA   C O   
1279 C  CB  . ALA   B 23  ? 0.3274 0.2389 0.5176 0.0510  0.0258  0.0837  29  ALA   C CB  
1280 N  N   . ASN   B 24  ? 0.3401 0.2456 0.4946 0.0494  0.0408  0.0693  30  ASN   C N   
1281 C  CA  . ASN   B 24  ? 0.3447 0.2521 0.4946 0.0498  0.0478  0.0669  30  ASN   C CA  
1282 C  C   . ASN   B 24  ? 0.3563 0.2552 0.4836 0.0492  0.0501  0.0592  30  ASN   C C   
1283 O  O   . ASN   B 24  ? 0.3701 0.2691 0.4869 0.0468  0.0505  0.0574  30  ASN   C O   
1284 C  CB  . ASN   B 24  ? 0.3579 0.2724 0.5126 0.0453  0.0426  0.0718  30  ASN   C CB  
1285 C  CG  . ASN   B 24  ? 0.3793 0.3029 0.5576 0.0457  0.0401  0.0794  30  ASN   C CG  
1286 O  OD1 . ASN   B 24  ? 0.4025 0.3322 0.5953 0.0485  0.0476  0.0819  30  ASN   C OD1 
1287 N  ND2 . ASN   B 24  ? 0.3724 0.2971 0.5555 0.0429  0.0297  0.0835  30  ASN   C ND2 
1288 N  N   . LEU   B 25  ? 0.3461 0.2375 0.4666 0.0511  0.0510  0.0549  31  LEU   C N   
1289 C  CA  . LEU   B 25  ? 0.3442 0.2277 0.4455 0.0503  0.0518  0.0477  31  LEU   C CA  
1290 C  C   . LEU   B 25  ? 0.3424 0.2227 0.4338 0.0527  0.0599  0.0429  31  LEU   C C   
1291 O  O   . LEU   B 25  ? 0.3469 0.2264 0.4443 0.0572  0.0680  0.0425  31  LEU   C O   
1292 C  CB  . LEU   B 25  ? 0.3407 0.2170 0.4403 0.0518  0.0511  0.0449  31  LEU   C CB  
1293 C  CG  . LEU   B 25  ? 0.3530 0.2217 0.4349 0.0501  0.0502  0.0380  31  LEU   C CG  
1294 C  CD1 . LEU   B 25  ? 0.3637 0.2346 0.4371 0.0449  0.0426  0.0386  31  LEU   C CD1 
1295 C  CD2 . LEU   B 25  ? 0.3586 0.2197 0.4405 0.0518  0.0507  0.0352  31  LEU   C CD2 
1296 N  N   . VAL   B 26  ? 0.3358 0.2133 0.4111 0.0500  0.0579  0.0390  32  VAL   C N   
1297 C  CA  . VAL   B 26  ? 0.3383 0.2109 0.4007 0.0520  0.0643  0.0340  32  VAL   C CA  
1298 C  C   . VAL   B 26  ? 0.3548 0.2184 0.4027 0.0521  0.0629  0.0268  32  VAL   C C   
1299 O  O   . VAL   B 26  ? 0.3681 0.2246 0.4097 0.0556  0.0687  0.0222  32  VAL   C O   
1300 C  CB  . VAL   B 26  ? 0.3468 0.2225 0.4017 0.0491  0.0627  0.0351  32  VAL   C CB  
1301 C  CG1 . VAL   B 26  ? 0.3588 0.2274 0.3959 0.0506  0.0672  0.0293  32  VAL   C CG1 
1302 C  CG2 . VAL   B 26  ? 0.3363 0.2202 0.4057 0.0490  0.0654  0.0418  32  VAL   C CG2 
1303 N  N   . TRP   B 27  ? 0.3543 0.2178 0.3969 0.0482  0.0551  0.0260  33  TRP   C N   
1304 C  CA  . TRP   B 27  ? 0.3577 0.2144 0.3885 0.0472  0.0526  0.0198  33  TRP   C CA  
1305 C  C   . TRP   B 27  ? 0.3468 0.2058 0.3794 0.0431  0.0448  0.0215  33  TRP   C C   
1306 O  O   . TRP   B 27  ? 0.3356 0.2003 0.3711 0.0406  0.0408  0.0258  33  TRP   C O   
1307 C  CB  . TRP   B 27  ? 0.3665 0.2202 0.3816 0.0468  0.0530  0.0154  33  TRP   C CB  
1308 C  CG  . TRP   B 27  ? 0.3784 0.2267 0.3820 0.0452  0.0489  0.0095  33  TRP   C CG  
1309 C  CD1 . TRP   B 27  ? 0.3964 0.2363 0.3927 0.0469  0.0506  0.0035  33  TRP   C CD1 
1310 C  CD2 . TRP   B 27  ? 0.3751 0.2260 0.3734 0.0415  0.0423  0.0088  33  TRP   C CD2 
1311 N  NE1 . TRP   B 27  ? 0.4044 0.2424 0.3930 0.0441  0.0449  -0.0004 33  TRP   C NE1 
1312 C  CE2 . TRP   B 27  ? 0.3891 0.2342 0.3794 0.0409  0.0401  0.0029  33  TRP   C CE2 
1313 C  CE3 . TRP   B 27  ? 0.3763 0.2336 0.3766 0.0386  0.0379  0.0127  33  TRP   C CE3 
1314 C  CZ2 . TRP   B 27  ? 0.3946 0.2414 0.3802 0.0379  0.0343  0.0010  33  TRP   C CZ2 
1315 C  CZ3 . TRP   B 27  ? 0.3911 0.2490 0.3850 0.0360  0.0326  0.0105  33  TRP   C CZ3 
1316 C  CH2 . TRP   B 27  ? 0.3958 0.2492 0.3834 0.0357  0.0311  0.0049  33  TRP   C CH2 
1317 N  N   . GLU   B 28  ? 0.3378 0.1916 0.3681 0.0425  0.0431  0.0182  34  GLU   C N   
1318 C  CA  . GLU   B 28  ? 0.3384 0.1937 0.3692 0.0387  0.0370  0.0196  34  GLU   C CA  
1319 C  C   . GLU   B 28  ? 0.3458 0.1953 0.3691 0.0374  0.0357  0.0137  34  GLU   C C   
1320 O  O   . GLU   B 28  ? 0.3445 0.1874 0.3654 0.0397  0.0389  0.0095  34  GLU   C O   
1321 C  CB  . GLU   B 28  ? 0.3497 0.2067 0.3928 0.0385  0.0354  0.0253  34  GLU   C CB  
1322 C  CG  . GLU   B 28  ? 0.3828 0.2344 0.4330 0.0418  0.0393  0.0247  34  GLU   C CG  
1323 C  CD  . GLU   B 28  ? 0.4153 0.2599 0.4627 0.0406  0.0380  0.0211  34  GLU   C CD  
1324 O  OE1 . GLU   B 28  ? 0.4173 0.2553 0.4665 0.0436  0.0419  0.0184  34  GLU   C OE1 
1325 O  OE2 . GLU   B 28  ? 0.3802 0.2254 0.4234 0.0367  0.0336  0.0210  34  GLU   C OE2 
1326 N  N   . ASP   B 29  ? 0.3377 0.1895 0.3572 0.0338  0.0309  0.0135  35  ASP   C N   
1327 C  CA  . ASP   B 29  ? 0.3446 0.1924 0.3596 0.0319  0.0290  0.0087  35  ASP   C CA  
1328 C  C   . ASP   B 29  ? 0.3417 0.1925 0.3594 0.0281  0.0251  0.0115  35  ASP   C C   
1329 O  O   . ASP   B 29  ? 0.3407 0.1963 0.3547 0.0264  0.0226  0.0126  35  ASP   C O   
1330 C  CB  . ASP   B 29  ? 0.3674 0.2144 0.3716 0.0321  0.0284  0.0034  35  ASP   C CB  
1331 C  CG  . ASP   B 29  ? 0.4257 0.2680 0.4259 0.0305  0.0262  -0.0023 35  ASP   C CG  
1332 O  OD1 . ASP   B 29  ? 0.4448 0.2872 0.4504 0.0278  0.0241  -0.0015 35  ASP   C OD1 
1333 O  OD2 . ASP   B 29  ? 0.4425 0.2810 0.4340 0.0318  0.0262  -0.0074 35  ASP   C OD2 
1334 N  N   . SER   B 30  ? 0.3272 0.1745 0.3509 0.0270  0.0250  0.0127  36  SER   C N   
1335 C  CA  A SER   B 30  ? 0.3250 0.1740 0.3508 0.0234  0.0223  0.0157  36  SER   C CA  
1336 C  CA  B SER   B 30  ? 0.3260 0.1752 0.3517 0.0234  0.0222  0.0158  36  SER   C CA  
1337 C  C   . SER   B 30  ? 0.3260 0.1773 0.3468 0.0206  0.0202  0.0121  36  SER   C C   
1338 O  O   . SER   B 30  ? 0.3356 0.1912 0.3551 0.0185  0.0186  0.0147  36  SER   C O   
1339 C  CB  A SER   B 30  ? 0.3307 0.1740 0.3630 0.0227  0.0229  0.0173  36  SER   C CB  
1340 C  CB  B SER   B 30  ? 0.3347 0.1788 0.3673 0.0227  0.0228  0.0181  36  SER   C CB  
1341 O  OG  A SER   B 30  ? 0.3355 0.1797 0.3690 0.0191  0.0211  0.0203  36  SER   C OG  
1342 O  OG  B SER   B 30  ? 0.3448 0.1824 0.3774 0.0233  0.0242  0.0128  36  SER   C OG  
1343 N  N   . SER   B 31  ? 0.3251 0.1733 0.3428 0.0208  0.0202  0.0059  37  SER   C N   
1344 C  CA  . SER   B 31  ? 0.3355 0.1866 0.3503 0.0184  0.0176  0.0025  37  SER   C CA  
1345 C  C   . SER   B 31  ? 0.3224 0.1798 0.3317 0.0189  0.0163  0.0030  37  SER   C C   
1346 O  O   . SER   B 31  ? 0.3256 0.1872 0.3347 0.0169  0.0144  0.0023  37  SER   C O   
1347 C  CB  . SER   B 31  ? 0.3801 0.2261 0.3922 0.0186  0.0167  -0.0042 37  SER   C CB  
1348 O  OG  . SER   B 31  ? 0.4157 0.2602 0.4197 0.0218  0.0171  -0.0074 37  SER   C OG  
1349 N  N   . ARG   B 32  ? 0.3191 0.1772 0.3245 0.0217  0.0174  0.0043  38  ARG   C N   
1350 C  CA  . ARG   B 32  ? 0.3320 0.1947 0.3318 0.0223  0.0161  0.0050  38  ARG   C CA  
1351 C  C   . ARG   B 32  ? 0.3270 0.1929 0.3285 0.0217  0.0158  0.0110  38  ARG   C C   
1352 O  O   . ARG   B 32  ? 0.3248 0.1938 0.3216 0.0218  0.0144  0.0119  38  ARG   C O   
1353 C  CB  . ARG   B 32  ? 0.3543 0.2150 0.3482 0.0253  0.0175  0.0029  38  ARG   C CB  
1354 C  CG  . ARG   B 32  ? 0.3888 0.2449 0.3774 0.0263  0.0170  -0.0033 38  ARG   C CG  
1355 C  CD  . ARG   B 32  ? 0.4087 0.2618 0.3896 0.0295  0.0192  -0.0049 38  ARG   C CD  
1356 N  NE  . ARG   B 32  ? 0.3826 0.2395 0.3579 0.0298  0.0177  -0.0036 38  ARG   C NE  
1357 C  CZ  . ARG   B 32  ? 0.3865 0.2407 0.3525 0.0319  0.0180  -0.0059 38  ARG   C CZ  
1358 N  NH1 . ARG   B 32  ? 0.3576 0.2052 0.3177 0.0338  0.0199  -0.0098 38  ARG   C NH1 
1359 N  NH2 . ARG   B 32  ? 0.3611 0.2183 0.3225 0.0320  0.0163  -0.0044 38  ARG   C NH2 
1360 N  N   . ASP   B 33  ? 0.3041 0.1685 0.3117 0.0211  0.0166  0.0151  39  ASP   C N   
1361 C  CA  . ASP   B 33  ? 0.2951 0.1613 0.3038 0.0205  0.0155  0.0208  39  ASP   C CA  
1362 C  C   . ASP   B 33  ? 0.2892 0.1570 0.2966 0.0225  0.0155  0.0223  39  ASP   C C   
1363 O  O   . ASP   B 33  ? 0.2891 0.1589 0.2937 0.0217  0.0132  0.0253  39  ASP   C O   
1364 C  CB  . ASP   B 33  ? 0.3110 0.1794 0.3156 0.0182  0.0135  0.0224  39  ASP   C CB  
1365 C  CG  . ASP   B 33  ? 0.3299 0.1980 0.3340 0.0174  0.0117  0.0283  39  ASP   C CG  
1366 O  OD1 . ASP   B 33  ? 0.3211 0.1872 0.3310 0.0178  0.0116  0.0319  39  ASP   C OD1 
1367 O  OD2 . ASP   B 33  ? 0.2868 0.1563 0.2846 0.0167  0.0099  0.0294  39  ASP   C OD2 
1368 N  N   . LEU   B 34  ? 0.2707 0.1368 0.2797 0.0250  0.0183  0.0203  40  LEU   C N   
1369 C  CA  . LEU   B 34  ? 0.2640 0.1319 0.2730 0.0267  0.0193  0.0221  40  LEU   C CA  
1370 C  C   . LEU   B 34  ? 0.2710 0.1381 0.2889 0.0289  0.0224  0.0246  40  LEU   C C   
1371 O  O   . LEU   B 34  ? 0.2802 0.1436 0.3010 0.0303  0.0249  0.0225  40  LEU   C O   
1372 C  CB  . LEU   B 34  ? 0.2649 0.1320 0.2661 0.0282  0.0208  0.0175  40  LEU   C CB  
1373 C  CG  . LEU   B 34  ? 0.2945 0.1632 0.2874 0.0270  0.0178  0.0154  40  LEU   C CG  
1374 C  CD1 . LEU   B 34  ? 0.3042 0.1708 0.2892 0.0289  0.0191  0.0114  40  LEU   C CD1 
1375 C  CD2 . LEU   B 34  ? 0.3205 0.1920 0.3126 0.0256  0.0152  0.0197  40  LEU   C CD2 
1376 N  N   . LEU   B 35  ? 0.2758 0.1462 0.2981 0.0294  0.0223  0.0289  41  LEU   C N   
1377 C  CA  . LEU   B 35  ? 0.2911 0.1625 0.3238 0.0317  0.0254  0.0321  41  LEU   C CA  
1378 C  C   . LEU   B 35  ? 0.3045 0.1796 0.3376 0.0320  0.0263  0.0342  41  LEU   C C   
1379 O  O   . LEU   B 35  ? 0.3222 0.1994 0.3511 0.0296  0.0223  0.0358  41  LEU   C O   
1380 C  CB  . LEU   B 35  ? 0.2841 0.1566 0.3266 0.0309  0.0223  0.0376  41  LEU   C CB  
1381 C  CG  . LEU   B 35  ? 0.3018 0.1758 0.3575 0.0340  0.0255  0.0410  41  LEU   C CG  
1382 C  CD1 . LEU   B 35  ? 0.3288 0.2001 0.3916 0.0345  0.0242  0.0433  41  LEU   C CD1 
1383 C  CD2 . LEU   B 35  ? 0.2954 0.1755 0.3589 0.0333  0.0235  0.0465  41  LEU   C CD2 
1384 N  N   . VAL   B 36  ? 0.3017 0.1768 0.3387 0.0350  0.0321  0.0338  42  VAL   C N   
1385 C  CA  . VAL   B 36  ? 0.3054 0.1840 0.3447 0.0354  0.0344  0.0363  42  VAL   C CA  
1386 C  C   . VAL   B 36  ? 0.3112 0.1935 0.3663 0.0376  0.0379  0.0410  42  VAL   C C   
1387 O  O   . VAL   B 36  ? 0.3198 0.1997 0.3791 0.0409  0.0429  0.0394  42  VAL   C O   
1388 C  CB  . VAL   B 36  ? 0.3249 0.2001 0.3532 0.0372  0.0392  0.0317  42  VAL   C CB  
1389 C  CG1 . VAL   B 36  ? 0.3244 0.2031 0.3559 0.0373  0.0423  0.0352  42  VAL   C CG1 
1390 C  CG2 . VAL   B 36  ? 0.3363 0.2084 0.3504 0.0353  0.0351  0.0273  42  VAL   C CG2 
1391 N  N   . SER   B 37  ? 0.3003 0.1884 0.3646 0.0358  0.0352  0.0467  43  SER   C N   
1392 C  CA  . SER   B 37  ? 0.2965 0.1897 0.3782 0.0377  0.0381  0.0517  43  SER   C CA  
1393 C  C   . SER   B 37  ? 0.3007 0.1983 0.3863 0.0374  0.0419  0.0543  43  SER   C C   
1394 O  O   . SER   B 37  ? 0.2903 0.1867 0.3651 0.0349  0.0400  0.0530  43  SER   C O   
1395 C  CB  . SER   B 37  ? 0.3038 0.2004 0.3963 0.0357  0.0307  0.0572  43  SER   C CB  
1396 O  OG  . SER   B 37  ? 0.3321 0.2302 0.4201 0.0313  0.0235  0.0594  43  SER   C OG  
1397 N  N   . SER   B 38  ? 0.2990 0.2013 0.4001 0.0401  0.0477  0.0580  44  SER   C N   
1398 C  CA  . SER   B 38  ? 0.3086 0.2157 0.4155 0.0396  0.0522  0.0612  44  SER   C CA  
1399 C  C   . SER   B 38  ? 0.3230 0.2372 0.4432 0.0355  0.0449  0.0679  44  SER   C C   
1400 O  O   . SER   B 38  ? 0.3250 0.2416 0.4547 0.0346  0.0382  0.0711  44  SER   C O   
1401 C  CB  . SER   B 38  ? 0.3279 0.2367 0.4449 0.0446  0.0632  0.0618  44  SER   C CB  
1402 O  OG  . SER   B 38  ? 0.3575 0.2717 0.4942 0.0464  0.0622  0.0661  44  SER   C OG  
1403 N  N   . THR   B 39  ? 0.3340 0.2508 0.4543 0.0328  0.0455  0.0703  45  THR   C N   
1404 C  CA  . THR   B 39  ? 0.3477 0.2703 0.4799 0.0283  0.0379  0.0764  45  THR   C CA  
1405 C  C   . THR   B 39  ? 0.3628 0.2927 0.5109 0.0282  0.0442  0.0815  45  THR   C C   
1406 O  O   . THR   B 39  ? 0.3725 0.3009 0.5160 0.0307  0.0542  0.0796  45  THR   C O   
1407 C  CB  . THR   B 39  ? 0.3740 0.2917 0.4899 0.0236  0.0299  0.0747  45  THR   C CB  
1408 O  OG1 . THR   B 39  ? 0.3900 0.3040 0.4933 0.0239  0.0356  0.0718  45  THR   C OG1 
1409 C  CG2 . THR   B 39  ? 0.3910 0.3027 0.4929 0.0234  0.0236  0.0705  45  THR   C CG2 
1410 N  N   . THR   B 40  ? 0.3712 0.3084 0.5374 0.0249  0.0381  0.0880  46  THR   C N   
1411 C  CA  . THR   B 40  ? 0.3878 0.3331 0.5720 0.0239  0.0435  0.0937  46  THR   C CA  
1412 C  C   . THR   B 40  ? 0.3965 0.3391 0.5707 0.0192  0.0421  0.0940  46  THR   C C   
1413 O  O   . THR   B 40  ? 0.4049 0.3491 0.5814 0.0198  0.0512  0.0954  46  THR   C O   
1414 C  CB  . THR   B 40  ? 0.4099 0.3649 0.6204 0.0225  0.0374  0.1008  46  THR   C CB  
1415 O  OG1 . THR   B 40  ? 0.4410 0.3939 0.6473 0.0172  0.0234  0.1021  46  THR   C OG1 
1416 C  CG2 . THR   B 40  ? 0.4123 0.3696 0.6335 0.0279  0.0399  0.1008  46  THR   C CG2 
1417 N  N   . ALA   B 41  ? 0.3981 0.3357 0.5603 0.0148  0.0310  0.0928  47  ALA   C N   
1418 C  CA  . ALA   B 41  ? 0.4031 0.3364 0.5541 0.0105  0.0284  0.0927  47  ALA   C CA  
1419 C  C   . ALA   B 41  ? 0.4145 0.3383 0.5400 0.0127  0.0326  0.0858  47  ALA   C C   
1420 O  O   . ALA   B 41  ? 0.4180 0.3372 0.5317 0.0156  0.0320  0.0806  47  ALA   C O   
1421 C  CB  . ALA   B 41  ? 0.4009 0.3322 0.5502 0.0052  0.0145  0.0943  47  ALA   C CB  
1422 N  N   . GLN   B 42  ? 0.4229 0.3434 0.5401 0.0110  0.0361  0.0859  48  GLN   C N   
1423 C  CA  . GLN   B 42  ? 0.4435 0.3549 0.5370 0.0129  0.0390  0.0799  48  GLN   C CA  
1424 C  C   . GLN   B 42  ? 0.4460 0.3510 0.5248 0.0100  0.0283  0.0769  48  GLN   C C   
1425 O  O   . GLN   B 42  ? 0.4561 0.3614 0.5394 0.0054  0.0206  0.0802  48  GLN   C O   
1426 C  CB  . GLN   B 42  ? 0.4856 0.3952 0.5753 0.0124  0.0469  0.0816  48  GLN   C CB  
1427 C  CG  . GLN   B 42  ? 0.5556 0.4665 0.6470 0.0175  0.0599  0.0809  48  GLN   C CG  
1428 C  CD  . GLN   B 42  ? 0.6433 0.5496 0.7246 0.0173  0.0674  0.0817  48  GLN   C CD  
1429 O  OE1 . GLN   B 42  ? 0.6663 0.5729 0.7510 0.0128  0.0652  0.0861  48  GLN   C OE1 
1430 N  NE2 . GLN   B 42  ? 0.6686 0.5692 0.7359 0.0220  0.0759  0.0776  48  GLN   C NE2 
1431 N  N   . GLY   B 43  ? 0.4336 0.3326 0.4955 0.0128  0.0280  0.0706  49  GLY   C N   
1432 C  CA  . GLY   B 43  ? 0.4300 0.3228 0.4769 0.0112  0.0197  0.0671  49  GLY   C CA  
1433 C  C   . GLY   B 43  ? 0.4263 0.3125 0.4585 0.0102  0.0200  0.0655  49  GLY   C C   
1434 O  O   . GLY   B 43  ? 0.4253 0.3108 0.4559 0.0114  0.0273  0.0663  49  GLY   C O   
1435 N  N   . CYS   B 44  ? 0.4229 0.3036 0.4436 0.0085  0.0124  0.0632  50  CYS   C N   
1436 C  CA  . CYS   B 44  ? 0.4432 0.3171 0.4504 0.0076  0.0116  0.0619  50  CYS   C CA  
1437 C  C   . CYS   B 44  ? 0.4384 0.3064 0.4279 0.0108  0.0108  0.0556  50  CYS   C C   
1438 O  O   . CYS   B 44  ? 0.4602 0.3223 0.4381 0.0110  0.0108  0.0544  50  CYS   C O   
1439 C  CB  . CYS   B 44  ? 0.4764 0.3478 0.4856 0.0028  0.0036  0.0651  50  CYS   C CB  
1440 S  SG  . CYS   B 44  ? 0.5710 0.4488 0.6011 -0.0016 0.0050  0.0732  50  CYS   C SG  
1441 N  N   . ASP   B 45  ? 0.4089 0.2783 0.3966 0.0131  0.0101  0.0519  51  ASP   C N   
1442 C  CA  . ASP   B 45  ? 0.4092 0.2743 0.3826 0.0159  0.0092  0.0461  51  ASP   C CA  
1443 C  C   . ASP   B 45  ? 0.3992 0.2622 0.3653 0.0192  0.0156  0.0435  51  ASP   C C   
1444 O  O   . ASP   B 45  ? 0.4045 0.2702 0.3770 0.0203  0.0221  0.0450  51  ASP   C O   
1445 C  CB  . ASP   B 45  ? 0.4238 0.2911 0.3986 0.0170  0.0070  0.0434  51  ASP   C CB  
1446 C  CG  . ASP   B 45  ? 0.4617 0.3290 0.4393 0.0142  0.0002  0.0453  51  ASP   C CG  
1447 O  OD1 . ASP   B 45  ? 0.4773 0.3400 0.4476 0.0125  -0.0045 0.0453  51  ASP   C OD1 
1448 O  OD2 . ASP   B 45  ? 0.4566 0.3276 0.4426 0.0139  -0.0006 0.0466  51  ASP   C OD2 
1449 N  N   . THR   B 46  ? 0.3725 0.2303 0.3249 0.0208  0.0138  0.0397  52  THR   C N   
1450 C  CA  . THR   B 46  ? 0.3705 0.2249 0.3133 0.0240  0.0183  0.0366  52  THR   C CA  
1451 C  C   . THR   B 46  ? 0.3616 0.2162 0.2994 0.0265  0.0163  0.0310  52  THR   C C   
1452 O  O   . THR   B 46  ? 0.3534 0.2076 0.2885 0.0261  0.0110  0.0293  52  THR   C O   
1453 C  CB  . THR   B 46  ? 0.3969 0.2448 0.3280 0.0241  0.0170  0.0369  52  THR   C CB  
1454 O  OG1 . THR   B 46  ? 0.3980 0.2454 0.3343 0.0211  0.0183  0.0425  52  THR   C OG1 
1455 C  CG2 . THR   B 46  ? 0.4150 0.2583 0.3342 0.0276  0.0205  0.0337  52  THR   C CG2 
1456 N  N   . ILE   B 47  ? 0.3553 0.2099 0.2917 0.0290  0.0205  0.0283  53  ILE   C N   
1457 C  CA  . ILE   B 47  ? 0.3568 0.2114 0.2893 0.0309  0.0184  0.0230  53  ILE   C CA  
1458 C  C   . ILE   B 47  ? 0.3585 0.2080 0.2776 0.0329  0.0162  0.0196  53  ILE   C C   
1459 O  O   . ILE   B 47  ? 0.3666 0.2114 0.2778 0.0341  0.0191  0.0203  53  ILE   C O   
1460 C  CB  . ILE   B 47  ? 0.3622 0.2178 0.2984 0.0326  0.0231  0.0210  53  ILE   C CB  
1461 C  CG1 . ILE   B 47  ? 0.3625 0.2231 0.3130 0.0312  0.0258  0.0249  53  ILE   C CG1 
1462 C  CG2 . ILE   B 47  ? 0.3713 0.2270 0.3051 0.0337  0.0201  0.0158  53  ILE   C CG2 
1463 C  CD1 . ILE   B 47  ? 0.3718 0.2365 0.3300 0.0288  0.0205  0.0262  53  ILE   C CD1 
1464 N  N   . ALA   B 48  ? 0.3437 0.1938 0.2602 0.0334  0.0112  0.0163  54  ALA   C N   
1465 C  CA  . ALA   B 48  ? 0.3575 0.2034 0.2629 0.0357  0.0083  0.0131  54  ALA   C CA  
1466 C  C   . ALA   B 48  ? 0.3681 0.2116 0.2683 0.0379  0.0101  0.0093  54  ALA   C C   
1467 O  O   . ALA   B 48  ? 0.3772 0.2236 0.2836 0.0377  0.0116  0.0074  54  ALA   C O   
1468 C  CB  . ALA   B 48  ? 0.3474 0.1959 0.2540 0.0360  0.0031  0.0106  54  ALA   C CB  
1469 N  N   . ARG   B 49  ? 0.3586 0.1962 0.2467 0.0399  0.0094  0.0079  55  ARG   C N   
1470 C  CA  . ARG   B 49  ? 0.3706 0.2041 0.2508 0.0421  0.0099  0.0039  55  ARG   C CA  
1471 C  C   . ARG   B 49  ? 0.3820 0.2129 0.2539 0.0439  0.0034  0.0009  55  ARG   C C   
1472 O  O   . ARG   B 49  ? 0.3924 0.2173 0.2533 0.0453  0.0024  0.0021  55  ARG   C O   
1473 C  CB  . ARG   B 49  ? 0.3825 0.2098 0.2544 0.0431  0.0162  0.0059  55  ARG   C CB  
1474 C  CG  . ARG   B 49  ? 0.4043 0.2350 0.2865 0.0417  0.0231  0.0092  55  ARG   C CG  
1475 C  CD  . ARG   B 49  ? 0.4196 0.2542 0.3111 0.0415  0.0243  0.0066  55  ARG   C CD  
1476 N  NE  . ARG   B 49  ? 0.4214 0.2597 0.3240 0.0405  0.0304  0.0105  55  ARG   C NE  
1477 C  CZ  . ARG   B 49  ? 0.4217 0.2646 0.3360 0.0398  0.0315  0.0103  55  ARG   C CZ  
1478 N  NH1 . ARG   B 49  ? 0.3902 0.2341 0.3061 0.0398  0.0277  0.0062  55  ARG   C NH1 
1479 N  NH2 . ARG   B 49  ? 0.4152 0.2615 0.3400 0.0392  0.0366  0.0144  55  ARG   C NH2 
1480 N  N   . CYS   B 50  ? 0.3735 0.2094 0.2520 0.0438  -0.0012 -0.0024 56  CYS   C N   
1481 C  CA  . CYS   B 50  ? 0.3669 0.2027 0.2418 0.0455  -0.0077 -0.0047 56  CYS   C CA  
1482 C  C   . CYS   B 50  ? 0.3537 0.1957 0.2378 0.0452  -0.0112 -0.0086 56  CYS   C C   
1483 O  O   . CYS   B 50  ? 0.3439 0.1892 0.2359 0.0434  -0.0085 -0.0093 56  CYS   C O   
1484 C  CB  . CYS   B 50  ? 0.3724 0.2099 0.2500 0.0451  -0.0087 -0.0014 56  CYS   C CB  
1485 S  SG  . CYS   B 50  ? 0.3842 0.2300 0.2767 0.0424  -0.0073 -0.0002 56  CYS   C SG  
1486 N  N   . ASP   B 51  ? 0.3422 0.1862 0.2269 0.0467  -0.0170 -0.0106 57  ASP   C N   
1487 C  CA  . ASP   B 51  ? 0.3505 0.2014 0.2459 0.0461  -0.0200 -0.0137 57  ASP   C CA  
1488 C  C   . ASP   B 51  ? 0.3433 0.2000 0.2460 0.0467  -0.0217 -0.0125 57  ASP   C C   
1489 O  O   . ASP   B 51  ? 0.3449 0.2068 0.2548 0.0474  -0.0252 -0.0150 57  ASP   C O   
1490 C  CB  . ASP   B 51  ? 0.4012 0.2501 0.2928 0.0474  -0.0255 -0.0180 57  ASP   C CB  
1491 C  CG  . ASP   B 51  ? 0.4855 0.3306 0.3682 0.0506  -0.0314 -0.0186 57  ASP   C CG  
1492 O  OD1 . ASP   B 51  ? 0.4928 0.3349 0.3698 0.0519  -0.0303 -0.0154 57  ASP   C OD1 
1493 O  OD2 . ASP   B 51  ? 0.5422 0.3868 0.4236 0.0516  -0.0374 -0.0220 57  ASP   C OD2 
1494 N  N   . CYS   B 52  ? 0.3398 0.1953 0.2411 0.0464  -0.0189 -0.0089 58  CYS   C N   
1495 C  CA  . CYS   B 52  ? 0.3335 0.1926 0.2396 0.0471  -0.0196 -0.0078 58  CYS   C CA  
1496 C  C   . CYS   B 52  ? 0.3238 0.1908 0.2421 0.0457  -0.0185 -0.0091 58  CYS   C C   
1497 O  O   . CYS   B 52  ? 0.3240 0.1930 0.2474 0.0431  -0.0157 -0.0090 58  CYS   C O   
1498 C  CB  . CYS   B 52  ? 0.3442 0.1997 0.2469 0.0459  -0.0167 -0.0039 58  CYS   C CB  
1499 S  SG  . CYS   B 52  ? 0.3903 0.2366 0.2797 0.0477  -0.0181 -0.0016 58  CYS   C SG  
1500 N  N   . GLN   B 53  ? 0.3097 0.1807 0.2327 0.0476  -0.0205 -0.0102 59  GLN   C N   
1501 C  CA  . GLN   B 53  ? 0.3177 0.1960 0.2518 0.0465  -0.0185 -0.0107 59  GLN   C CA  
1502 C  C   . GLN   B 53  ? 0.3130 0.1912 0.2466 0.0476  -0.0163 -0.0089 59  GLN   C C   
1503 O  O   . GLN   B 53  ? 0.2941 0.1778 0.2355 0.0475  -0.0143 -0.0092 59  GLN   C O   
1504 C  CB  . GLN   B 53  ? 0.3430 0.2277 0.2861 0.0476  -0.0217 -0.0140 59  GLN   C CB  
1505 C  CG  . GLN   B 53  ? 0.3763 0.2614 0.3220 0.0453  -0.0231 -0.0161 59  GLN   C CG  
1506 C  CD  . GLN   B 53  ? 0.4089 0.3012 0.3659 0.0455  -0.0265 -0.0189 59  GLN   C CD  
1507 O  OE1 . GLN   B 53  ? 0.4344 0.3256 0.3898 0.0467  -0.0321 -0.0215 59  GLN   C OE1 
1508 N  NE2 . GLN   B 53  ? 0.3869 0.2864 0.3555 0.0442  -0.0233 -0.0183 59  GLN   C NE2 
1509 N  N   . THR   B 54  ? 0.3211 0.1926 0.2453 0.0484  -0.0166 -0.0068 60  THR   C N   
1510 C  CA  . THR   B 54  ? 0.3292 0.1981 0.2503 0.0490  -0.0149 -0.0051 60  THR   C CA  
1511 C  C   . THR   B 54  ? 0.3356 0.1982 0.2498 0.0463  -0.0138 -0.0019 60  THR   C C   
1512 O  O   . THR   B 54  ? 0.3468 0.2055 0.2561 0.0457  -0.0148 -0.0009 60  THR   C O   
1513 C  CB  . THR   B 54  ? 0.3578 0.2245 0.2755 0.0533  -0.0175 -0.0063 60  THR   C CB  
1514 O  OG1 . THR   B 54  ? 0.3915 0.2513 0.3001 0.0543  -0.0205 -0.0054 60  THR   C OG1 
1515 C  CG2 . THR   B 54  ? 0.3579 0.2321 0.2848 0.0561  -0.0190 -0.0092 60  THR   C CG2 
1516 N  N   . GLY   B 55  ? 0.3194 0.1810 0.2334 0.0447  -0.0117 -0.0002 61  GLY   C N   
1517 C  CA  . GLY   B 55  ? 0.3205 0.1770 0.2301 0.0417  -0.0113 0.0031  61  GLY   C CA  
1518 C  C   . GLY   B 55  ? 0.3207 0.1749 0.2280 0.0408  -0.0104 0.0044  61  GLY   C C   
1519 O  O   . GLY   B 55  ? 0.3464 0.2013 0.2532 0.0431  -0.0096 0.0026  61  GLY   C O   
1520 N  N   . VAL   B 56  ? 0.3008 0.1522 0.2070 0.0374  -0.0104 0.0074  62  VAL   C N   
1521 C  CA  . VAL   B 56  ? 0.2883 0.1360 0.1906 0.0360  -0.0105 0.0089  62  VAL   C CA  
1522 C  C   . VAL   B 56  ? 0.2865 0.1368 0.1942 0.0323  -0.0096 0.0117  62  VAL   C C   
1523 O  O   . VAL   B 56  ? 0.2878 0.1389 0.1991 0.0305  -0.0100 0.0136  62  VAL   C O   
1524 C  CB  . VAL   B 56  ? 0.3027 0.1416 0.1962 0.0356  -0.0137 0.0103  62  VAL   C CB  
1525 C  CG1 . VAL   B 56  ? 0.3048 0.1383 0.1932 0.0332  -0.0151 0.0123  62  VAL   C CG1 
1526 C  CG2 . VAL   B 56  ? 0.3164 0.1516 0.2041 0.0397  -0.0147 0.0077  62  VAL   C CG2 
1527 N  N   . TYR   B 57  ? 0.2962 0.1470 0.2039 0.0314  -0.0082 0.0123  63  TYR   C N   
1528 C  CA  . TYR   B 57  ? 0.3028 0.1554 0.2154 0.0281  -0.0078 0.0153  63  TYR   C CA  
1529 C  C   . TYR   B 57  ? 0.3227 0.1690 0.2282 0.0262  -0.0099 0.0178  63  TYR   C C   
1530 O  O   . TYR   B 57  ? 0.3383 0.1801 0.2354 0.0278  -0.0098 0.0163  63  TYR   C O   
1531 C  CB  . TYR   B 57  ? 0.3119 0.1712 0.2325 0.0282  -0.0043 0.0142  63  TYR   C CB  
1532 C  CG  . TYR   B 57  ? 0.3202 0.1795 0.2385 0.0286  -0.0018 0.0139  63  TYR   C CG  
1533 C  CD1 . TYR   B 57  ? 0.3276 0.1878 0.2436 0.0316  0.0002  0.0110  63  TYR   C CD1 
1534 C  CD2 . TYR   B 57  ? 0.3256 0.1837 0.2440 0.0262  -0.0011 0.0168  63  TYR   C CD2 
1535 C  CE1 . TYR   B 57  ? 0.3345 0.1954 0.2493 0.0321  0.0038  0.0108  63  TYR   C CE1 
1536 C  CE2 . TYR   B 57  ? 0.3275 0.1852 0.2430 0.0265  0.0021  0.0168  63  TYR   C CE2 
1537 C  CZ  . TYR   B 57  ? 0.3452 0.2042 0.2585 0.0294  0.0049  0.0139  63  TYR   C CZ  
1538 O  OH  . TYR   B 57  ? 0.3671 0.2259 0.2780 0.0299  0.0093  0.0141  63  TYR   C OH  
1539 N  N   . TYR   B 58  ? 0.3252 0.1710 0.2340 0.0230  -0.0119 0.0214  64  TYR   C N   
1540 C  CA  . TYR   B 58  ? 0.3481 0.1875 0.2498 0.0210  -0.0151 0.0240  64  TYR   C CA  
1541 C  C   . TYR   B 58  ? 0.3552 0.1960 0.2574 0.0204  -0.0126 0.0250  64  TYR   C C   
1542 O  O   . TYR   B 58  ? 0.3433 0.1897 0.2550 0.0195  -0.0109 0.0263  64  TYR   C O   
1543 C  CB  . TYR   B 58  ? 0.3552 0.1928 0.2603 0.0177  -0.0197 0.0279  64  TYR   C CB  
1544 C  CG  . TYR   B 58  ? 0.3788 0.2088 0.2755 0.0154  -0.0245 0.0303  64  TYR   C CG  
1545 C  CD1 . TYR   B 58  ? 0.4030 0.2240 0.2860 0.0161  -0.0268 0.0286  64  TYR   C CD1 
1546 C  CD2 . TYR   B 58  ? 0.3859 0.2167 0.2874 0.0128  -0.0269 0.0343  64  TYR   C CD2 
1547 C  CE1 . TYR   B 58  ? 0.4119 0.2244 0.2849 0.0141  -0.0315 0.0304  64  TYR   C CE1 
1548 C  CE2 . TYR   B 58  ? 0.4066 0.2296 0.2991 0.0107  -0.0322 0.0366  64  TYR   C CE2 
1549 C  CZ  . TYR   B 58  ? 0.4233 0.2368 0.3010 0.0112  -0.0346 0.0345  64  TYR   C CZ  
1550 O  OH  . TYR   B 58  ? 0.4616 0.2658 0.3283 0.0091  -0.0403 0.0364  64  TYR   C OH  
1551 N  N   . CYS   B 59  ? 0.3676 0.2023 0.2585 0.0211  -0.0124 0.0244  65  CYS   C N   
1552 C  CA  . CYS   B 59  ? 0.3821 0.2164 0.2707 0.0206  -0.0096 0.0257  65  CYS   C CA  
1553 C  C   . CYS   B 59  ? 0.4020 0.2276 0.2809 0.0181  -0.0146 0.0291  65  CYS   C C   
1554 O  O   . CYS   B 59  ? 0.4113 0.2283 0.2766 0.0188  -0.0163 0.0281  65  CYS   C O   
1555 C  CB  . CYS   B 59  ? 0.3893 0.2234 0.2723 0.0237  -0.0043 0.0224  65  CYS   C CB  
1556 S  SG  . CYS   B 59  ? 0.3967 0.2291 0.2748 0.0232  0.0004  0.0244  65  CYS   C SG  
1557 N  N   . SER   B 60  ? 0.3910 0.2181 0.2765 0.0154  -0.0174 0.0331  66  SER   C N   
1558 C  CA  A SER   B 60  ? 0.4086 0.2277 0.2859 0.0129  -0.0236 0.0367  66  SER   C CA  
1559 C  CA  B SER   B 60  ? 0.4034 0.2224 0.2807 0.0129  -0.0236 0.0367  66  SER   C CA  
1560 C  C   . SER   B 60  ? 0.4160 0.2268 0.2779 0.0133  -0.0223 0.0370  66  SER   C C   
1561 O  O   . SER   B 60  ? 0.4354 0.2362 0.2840 0.0122  -0.0275 0.0379  66  SER   C O   
1562 C  CB  A SER   B 60  ? 0.4325 0.2557 0.3218 0.0104  -0.0268 0.0411  66  SER   C CB  
1563 C  CB  B SER   B 60  ? 0.4126 0.2358 0.3018 0.0104  -0.0269 0.0411  66  SER   C CB  
1564 O  OG  A SER   B 60  ? 0.4710 0.3006 0.3691 0.0111  -0.0216 0.0416  66  SER   C OG  
1565 O  OG  B SER   B 60  ? 0.4353 0.2511 0.3181 0.0078  -0.0345 0.0447  66  SER   C OG  
1566 N  N   . SER   B 61  ? 0.4056 0.2200 0.2686 0.0148  -0.0152 0.0362  67  SER   C N   
1567 C  CA  . SER   B 61  ? 0.4150 0.2220 0.2637 0.0154  -0.0120 0.0367  67  SER   C CA  
1568 C  C   . SER   B 61  ? 0.4259 0.2255 0.2593 0.0182  -0.0100 0.0329  67  SER   C C   
1569 O  O   . SER   B 61  ? 0.4322 0.2240 0.2510 0.0191  -0.0070 0.0331  67  SER   C O   
1570 C  CB  . SER   B 61  ? 0.4086 0.2226 0.2653 0.0160  -0.0043 0.0371  67  SER   C CB  
1571 O  OG  . SER   B 61  ? 0.4327 0.2556 0.2996 0.0183  0.0008  0.0331  67  SER   C OG  
1572 N  N   . ARG   B 62  ? 0.4107 0.2121 0.2470 0.0197  -0.0112 0.0295  68  ARG   C N   
1573 C  CA  . ARG   B 62  ? 0.4095 0.2033 0.2324 0.0226  -0.0100 0.0257  68  ARG   C CA  
1574 C  C   . ARG   B 62  ? 0.4120 0.1993 0.2304 0.0215  -0.0180 0.0250  68  ARG   C C   
1575 O  O   . ARG   B 62  ? 0.4225 0.2025 0.2301 0.0238  -0.0179 0.0218  68  ARG   C O   
1576 C  CB  . ARG   B 62  ? 0.4283 0.2307 0.2598 0.0264  -0.0031 0.0218  68  ARG   C CB  
1577 C  CG  . ARG   B 62  ? 0.4706 0.2794 0.3073 0.0275  0.0051  0.0221  68  ARG   C CG  
1578 C  CD  . ARG   B 62  ? 0.4879 0.2882 0.3085 0.0296  0.0101  0.0215  68  ARG   C CD  
1579 N  NE  . ARG   B 62  ? 0.5184 0.3259 0.3461 0.0302  0.0185  0.0225  68  ARG   C NE  
1580 C  CZ  . ARG   B 62  ? 0.5322 0.3390 0.3594 0.0274  0.0198  0.0265  68  ARG   C CZ  
1581 N  NH1 . ARG   B 62  ? 0.5483 0.3476 0.3676 0.0243  0.0130  0.0299  68  ARG   C NH1 
1582 N  NH2 . ARG   B 62  ? 0.5002 0.3135 0.3347 0.0277  0.0277  0.0273  68  ARG   C NH2 
1583 N  N   . ARG   B 63  ? 0.4073 0.1980 0.2358 0.0180  -0.0242 0.0281  69  ARG   C N   
1584 C  CA  . ARG   B 63  ? 0.4299 0.2163 0.2580 0.0162  -0.0314 0.0282  69  ARG   C CA  
1585 C  C   . ARG   B 63  ? 0.4369 0.2247 0.2661 0.0192  -0.0287 0.0241  69  ARG   C C   
1586 O  O   . ARG   B 63  ? 0.4502 0.2288 0.2692 0.0195  -0.0324 0.0224  69  ARG   C O   
1587 C  CB  . ARG   B 63  ? 0.4773 0.2492 0.2877 0.0142  -0.0384 0.0291  69  ARG   C CB  
1588 C  CG  . ARG   B 63  ? 0.5423 0.3132 0.3577 0.0095  -0.0470 0.0338  69  ARG   C CG  
1589 C  CD  . ARG   B 63  ? 0.5930 0.3692 0.4149 0.0084  -0.0458 0.0375  69  ARG   C CD  
1590 N  NE  . ARG   B 63  ? 0.6640 0.4344 0.4832 0.0045  -0.0552 0.0418  69  ARG   C NE  
1591 C  CZ  . ARG   B 63  ? 0.6989 0.4733 0.5257 0.0028  -0.0569 0.0462  69  ARG   C CZ  
1592 N  NH1 . ARG   B 63  ? 0.6948 0.4788 0.5323 0.0045  -0.0496 0.0467  69  ARG   C NH1 
1593 N  NH2 . ARG   B 63  ? 0.7002 0.4689 0.5247 -0.0006 -0.0664 0.0502  69  ARG   C NH2 
1594 N  N   . LYS   B 64  ? 0.4230 0.2213 0.2633 0.0218  -0.0224 0.0223  70  LYS   C N   
1595 C  CA  . LYS   B 64  ? 0.4285 0.2284 0.2699 0.0253  -0.0198 0.0186  70  LYS   C CA  
1596 C  C   . LYS   B 64  ? 0.4116 0.2231 0.2688 0.0258  -0.0175 0.0183  70  LYS   C C   
1597 O  O   . LYS   B 64  ? 0.4041 0.2238 0.2713 0.0251  -0.0145 0.0195  70  LYS   C O   
1598 C  CB  . LYS   B 64  ? 0.4772 0.2755 0.3110 0.0296  -0.0134 0.0152  70  LYS   C CB  
1599 C  CG  . LYS   B 64  ? 0.5904 0.3749 0.4057 0.0311  -0.0150 0.0133  70  LYS   C CG  
1600 C  CD  . LYS   B 64  ? 0.6778 0.4620 0.4882 0.0364  -0.0076 0.0096  70  LYS   C CD  
1601 C  CE  . LYS   B 64  ? 0.7576 0.5271 0.5474 0.0378  -0.0078 0.0082  70  LYS   C CE  
1602 N  NZ  . LYS   B 64  ? 0.8087 0.5730 0.5904 0.0341  -0.0100 0.0116  70  LYS   C NZ  
1603 N  N   . HIS   B 65  ? 0.4029 0.2138 0.2610 0.0273  -0.0187 0.0165  71  HIS   C N   
1604 C  CA  . HIS   B 65  ? 0.3943 0.2142 0.2642 0.0285  -0.0167 0.0156  71  HIS   C CA  
1605 C  C   . HIS   B 65  ? 0.4057 0.2280 0.2746 0.0332  -0.0122 0.0117  71  HIS   C C   
1606 O  O   . HIS   B 65  ? 0.4315 0.2466 0.2907 0.0358  -0.0125 0.0096  71  HIS   C O   
1607 C  CB  . HIS   B 65  ? 0.3857 0.2025 0.2560 0.0274  -0.0208 0.0165  71  HIS   C CB  
1608 C  CG  . HIS   B 65  ? 0.4024 0.2184 0.2767 0.0228  -0.0249 0.0206  71  HIS   C CG  
1609 N  ND1 . HIS   B 65  ? 0.4215 0.2453 0.3080 0.0211  -0.0239 0.0228  71  HIS   C ND1 
1610 C  CD2 . HIS   B 65  ? 0.4112 0.2194 0.2793 0.0197  -0.0301 0.0228  71  HIS   C CD2 
1611 C  CE1 . HIS   B 65  ? 0.4227 0.2444 0.3116 0.0173  -0.0280 0.0265  71  HIS   C CE1 
1612 N  NE2 . HIS   B 65  ? 0.4216 0.2339 0.2999 0.0161  -0.0325 0.0268  71  HIS   C NE2 
1613 N  N   . TYR   B 66  ? 0.3838 0.2159 0.2632 0.0343  -0.0082 0.0108  72  TYR   C N   
1614 C  CA  . TYR   B 66  ? 0.3776 0.2134 0.2585 0.0387  -0.0044 0.0074  72  TYR   C CA  
1615 C  C   . TYR   B 66  ? 0.3542 0.1963 0.2437 0.0404  -0.0049 0.0057  72  TYR   C C   
1616 O  O   . TYR   B 66  ? 0.3435 0.1915 0.2414 0.0383  -0.0050 0.0067  72  TYR   C O   
1617 C  CB  . TYR   B 66  ? 0.3800 0.2220 0.2664 0.0387  0.0008  0.0074  72  TYR   C CB  
1618 C  CG  . TYR   B 66  ? 0.4083 0.2439 0.2848 0.0379  0.0026  0.0087  72  TYR   C CG  
1619 C  CD1 . TYR   B 66  ? 0.4314 0.2622 0.2990 0.0414  0.0059  0.0066  72  TYR   C CD1 
1620 C  CD2 . TYR   B 66  ? 0.4315 0.2660 0.3076 0.0340  0.0017  0.0121  72  TYR   C CD2 
1621 C  CE1 . TYR   B 66  ? 0.4538 0.2775 0.3102 0.0409  0.0081  0.0077  72  TYR   C CE1 
1622 C  CE2 . TYR   B 66  ? 0.4523 0.2799 0.3176 0.0333  0.0030  0.0135  72  TYR   C CE2 
1623 C  CZ  . TYR   B 66  ? 0.4739 0.2959 0.3287 0.0367  0.0065  0.0112  72  TYR   C CZ  
1624 O  OH  . TYR   B 66  ? 0.5030 0.3172 0.3453 0.0361  0.0083  0.0127  72  TYR   C OH  
1625 N  N   . PRO   B 67  ? 0.3512 0.1918 0.2381 0.0445  -0.0050 0.0031  73  PRO   C N   
1626 C  CA  . PRO   B 67  ? 0.3368 0.1834 0.2313 0.0465  -0.0059 0.0015  73  PRO   C CA  
1627 C  C   . PRO   B 67  ? 0.3316 0.1883 0.2372 0.0474  -0.0024 0.0000  73  PRO   C C   
1628 O  O   . PRO   B 67  ? 0.3361 0.1946 0.2424 0.0491  0.0013  -0.0010 73  PRO   C O   
1629 C  CB  . PRO   B 67  ? 0.3571 0.1982 0.2452 0.0509  -0.0075 -0.0006 73  PRO   C CB  
1630 C  CG  . PRO   B 67  ? 0.3698 0.2042 0.2491 0.0523  -0.0054 -0.0011 73  PRO   C CG  
1631 C  CD  . PRO   B 67  ? 0.3567 0.1898 0.2337 0.0479  -0.0043 0.0013  73  PRO   C CD  
1632 N  N   . VAL   B 68  ? 0.3121 0.1752 0.2262 0.0460  -0.0033 -0.0002 74  VAL   C N   
1633 C  CA  . VAL   B 68  ? 0.3125 0.1848 0.2378 0.0462  -0.0008 -0.0017 74  VAL   C CA  
1634 C  C   . VAL   B 68  ? 0.3092 0.1860 0.2407 0.0472  -0.0037 -0.0036 74  VAL   C C   
1635 O  O   . VAL   B 68  ? 0.3165 0.1894 0.2435 0.0468  -0.0069 -0.0032 74  VAL   C O   
1636 C  CB  . VAL   B 68  ? 0.3246 0.1994 0.2543 0.0420  0.0017  0.0005  74  VAL   C CB  
1637 C  CG1 . VAL   B 68  ? 0.3465 0.2177 0.2707 0.0411  0.0048  0.0023  74  VAL   C CG1 
1638 C  CG2 . VAL   B 68  ? 0.3229 0.1954 0.2518 0.0390  -0.0008 0.0022  74  VAL   C CG2 
1639 N  N   . SER   B 69  ? 0.3122 0.1969 0.2541 0.0482  -0.0027 -0.0055 75  SER   C N   
1640 C  CA  . SER   B 69  ? 0.3253 0.2150 0.2745 0.0484  -0.0058 -0.0076 75  SER   C CA  
1641 C  C   . SER   B 69  ? 0.3189 0.2127 0.2754 0.0442  -0.0038 -0.0069 75  SER   C C   
1642 O  O   . SER   B 69  ? 0.3054 0.2020 0.2664 0.0427  0.0004  -0.0058 75  SER   C O   
1643 C  CB  . SER   B 69  ? 0.3591 0.2555 0.3170 0.0519  -0.0065 -0.0099 75  SER   C CB  
1644 O  OG  . SER   B 69  ? 0.4330 0.3250 0.3842 0.0562  -0.0087 -0.0106 75  SER   C OG  
1645 N  N   . PHE   B 70  ? 0.3117 0.2044 0.2681 0.0425  -0.0063 -0.0075 76  PHE   C N   
1646 C  CA  . PHE   B 70  ? 0.3047 0.1995 0.2671 0.0388  -0.0047 -0.0071 76  PHE   C CA  
1647 C  C   . PHE   B 70  ? 0.3026 0.2000 0.2703 0.0385  -0.0081 -0.0101 76  PHE   C C   
1648 O  O   . PHE   B 70  ? 0.3094 0.2044 0.2722 0.0407  -0.0122 -0.0119 76  PHE   C O   
1649 C  CB  . PHE   B 70  ? 0.3036 0.1927 0.2596 0.0365  -0.0034 -0.0043 76  PHE   C CB  
1650 C  CG  . PHE   B 70  ? 0.2937 0.1770 0.2410 0.0375  -0.0058 -0.0041 76  PHE   C CG  
1651 C  CD1 . PHE   B 70  ? 0.2948 0.1733 0.2338 0.0389  -0.0065 -0.0025 76  PHE   C CD1 
1652 C  CD2 . PHE   B 70  ? 0.2987 0.1806 0.2456 0.0369  -0.0070 -0.0053 76  PHE   C CD2 
1653 C  CE1 . PHE   B 70  ? 0.3187 0.1920 0.2504 0.0395  -0.0083 -0.0017 76  PHE   C CE1 
1654 C  CE2 . PHE   B 70  ? 0.3096 0.1860 0.2481 0.0377  -0.0081 -0.0046 76  PHE   C CE2 
1655 C  CZ  . PHE   B 70  ? 0.3052 0.1776 0.2367 0.0389  -0.0087 -0.0026 76  PHE   C CZ  
1656 N  N   . SER   B 71  ? 0.2913 0.1927 0.2682 0.0356  -0.0068 -0.0106 77  SER   C N   
1657 C  CA  . SER   B 71  ? 0.2953 0.1986 0.2778 0.0347  -0.0105 -0.0138 77  SER   C CA  
1658 C  C   . SER   B 71  ? 0.3150 0.2113 0.2893 0.0341  -0.0121 -0.0147 77  SER   C C   
1659 O  O   . SER   B 71  ? 0.3365 0.2279 0.3034 0.0340  -0.0097 -0.0123 77  SER   C O   
1660 C  CB  . SER   B 71  ? 0.2981 0.2071 0.2933 0.0315  -0.0083 -0.0139 77  SER   C CB  
1661 O  OG  . SER   B 71  ? 0.3265 0.2323 0.3206 0.0287  -0.0044 -0.0113 77  SER   C OG  
1662 N  N   . LYS   B 72  ? 0.3127 0.2083 0.2881 0.0338  -0.0162 -0.0181 78  LYS   C N   
1663 C  CA  . LYS   B 72  ? 0.3228 0.2108 0.2891 0.0336  -0.0170 -0.0192 78  LYS   C CA  
1664 C  C   . LYS   B 72  ? 0.3287 0.2150 0.2988 0.0306  -0.0131 -0.0183 78  LYS   C C   
1665 O  O   . LYS   B 72  ? 0.3242 0.2151 0.3048 0.0281  -0.0118 -0.0180 78  LYS   C O   
1666 C  CB  . LYS   B 72  ? 0.3552 0.2414 0.3192 0.0346  -0.0232 -0.0235 78  LYS   C CB  
1667 C  CG  . LYS   B 72  ? 0.4418 0.3286 0.4011 0.0380  -0.0277 -0.0241 78  LYS   C CG  
1668 C  CD  . LYS   B 72  ? 0.5451 0.4252 0.4942 0.0395  -0.0334 -0.0273 78  LYS   C CD  
1669 C  CE  . LYS   B 72  ? 0.6169 0.4960 0.5595 0.0433  -0.0379 -0.0272 78  LYS   C CE  
1670 N  NZ  . LYS   B 72  ? 0.6574 0.5274 0.5856 0.0449  -0.0424 -0.0294 78  LYS   C NZ  
1671 N  N   . PRO   B 73  ? 0.3406 0.2204 0.3030 0.0308  -0.0110 -0.0177 79  PRO   C N   
1672 C  CA  . PRO   B 73  ? 0.3414 0.2194 0.3084 0.0284  -0.0073 -0.0166 79  PRO   C CA  
1673 C  C   . PRO   B 73  ? 0.3397 0.2182 0.3140 0.0261  -0.0096 -0.0200 79  PRO   C C   
1674 O  O   . PRO   B 73  ? 0.3493 0.2254 0.3202 0.0267  -0.0140 -0.0241 79  PRO   C O   
1675 C  CB  . PRO   B 73  ? 0.3629 0.2338 0.3205 0.0299  -0.0052 -0.0163 79  PRO   C CB  
1676 C  CG  . PRO   B 73  ? 0.3703 0.2400 0.3189 0.0324  -0.0064 -0.0154 79  PRO   C CG  
1677 C  CD  . PRO   B 73  ? 0.3434 0.2173 0.2936 0.0333  -0.0111 -0.0174 79  PRO   C CD  
1678 N  N   . SER   B 74  ? 0.3249 0.2065 0.3091 0.0233  -0.0071 -0.0183 80  SER   C N   
1679 C  CA  . SER   B 74  ? 0.3252 0.2078 0.3182 0.0205  -0.0093 -0.0211 80  SER   C CA  
1680 C  C   . SER   B 74  ? 0.3242 0.2056 0.3243 0.0176  -0.0052 -0.0187 80  SER   C C   
1681 O  O   . SER   B 74  ? 0.3142 0.1954 0.3132 0.0179  -0.0012 -0.0145 80  SER   C O   
1682 C  CB  . SER   B 74  ? 0.3578 0.2488 0.3600 0.0196  -0.0118 -0.0216 80  SER   C CB  
1683 O  OG  . SER   B 74  ? 0.4098 0.3026 0.4067 0.0227  -0.0152 -0.0228 80  SER   C OG  
1684 N  N   . LEU   B 75  ? 0.3331 0.2139 0.3411 0.0146  -0.0070 -0.0211 81  LEU   C N   
1685 C  CA  . LEU   B 75  ? 0.3483 0.2277 0.3641 0.0114  -0.0038 -0.0188 81  LEU   C CA  
1686 C  C   . LEU   B 75  ? 0.3543 0.2422 0.3808 0.0090  -0.0024 -0.0160 81  LEU   C C   
1687 O  O   . LEU   B 75  ? 0.3582 0.2511 0.3925 0.0074  -0.0055 -0.0183 81  LEU   C O   
1688 C  CB  . LEU   B 75  ? 0.3669 0.2404 0.3853 0.0092  -0.0070 -0.0233 81  LEU   C CB  
1689 C  CG  . LEU   B 75  ? 0.3929 0.2617 0.4173 0.0064  -0.0041 -0.0216 81  LEU   C CG  
1690 C  CD1 . LEU   B 75  ? 0.3984 0.2613 0.4160 0.0090  0.0001  -0.0191 81  LEU   C CD1 
1691 C  CD2 . LEU   B 75  ? 0.4090 0.2713 0.4355 0.0041  -0.0083 -0.0269 81  LEU   C CD2 
1692 N  N   . ILE   B 76  ? 0.3488 0.2385 0.3754 0.0090  0.0023  -0.0109 82  ILE   C N   
1693 C  CA  . ILE   B 76  ? 0.3473 0.2442 0.3816 0.0073  0.0049  -0.0080 82  ILE   C CA  
1694 C  C   . ILE   B 76  ? 0.3455 0.2402 0.3844 0.0042  0.0092  -0.0037 82  ILE   C C   
1695 O  O   . ILE   B 76  ? 0.3413 0.2300 0.3749 0.0049  0.0107  -0.0015 82  ILE   C O   
1696 C  CB  . ILE   B 76  ? 0.3573 0.2574 0.3845 0.0105  0.0063  -0.0059 82  ILE   C CB  
1697 C  CG1 . ILE   B 76  ? 0.3674 0.2708 0.3921 0.0133  0.0021  -0.0097 82  ILE   C CG1 
1698 C  CG2 . ILE   B 76  ? 0.3603 0.2651 0.3916 0.0094  0.0109  -0.0019 82  ILE   C CG2 
1699 C  CD1 . ILE   B 76  ? 0.3811 0.2842 0.3967 0.0166  0.0027  -0.0083 82  ILE   C CD1 
1700 N  N   . PHE   B 77  ? 0.3464 0.2460 0.3958 0.0010  0.0112  -0.0022 83  PHE   C N   
1701 C  CA  . PHE   B 77  ? 0.3628 0.2598 0.4155 -0.0019 0.0157  0.0025  83  PHE   C CA  
1702 C  C   . PHE   B 77  ? 0.3652 0.2632 0.4104 -0.0001 0.0198  0.0073  83  PHE   C C   
1703 O  O   . PHE   B 77  ? 0.3725 0.2766 0.4179 0.0012  0.0213  0.0075  83  PHE   C O   
1704 C  CB  . PHE   B 77  ? 0.3670 0.2683 0.4334 -0.0064 0.0171  0.0029  83  PHE   C CB  
1705 C  CG  . PHE   B 77  ? 0.3902 0.2867 0.4592 -0.0097 0.0212  0.0077  83  PHE   C CG  
1706 C  CD1 . PHE   B 77  ? 0.4064 0.2944 0.4750 -0.0110 0.0195  0.0073  83  PHE   C CD1 
1707 C  CD2 . PHE   B 77  ? 0.4061 0.3058 0.4773 -0.0113 0.0269  0.0128  83  PHE   C CD2 
1708 C  CE1 . PHE   B 77  ? 0.4243 0.3071 0.4953 -0.0139 0.0230  0.0120  83  PHE   C CE1 
1709 C  CE2 . PHE   B 77  ? 0.4209 0.3150 0.4930 -0.0143 0.0305  0.0177  83  PHE   C CE2 
1710 C  CZ  . PHE   B 77  ? 0.4227 0.3085 0.4951 -0.0156 0.0283  0.0174  83  PHE   C CZ  
1711 N  N   . VAL   B 78  ? 0.3555 0.2471 0.3944 0.0001  0.0213  0.0111  84  VAL   C N   
1712 C  CA  . VAL   B 78  ? 0.3491 0.2394 0.3794 0.0014  0.0241  0.0157  84  VAL   C CA  
1713 C  C   . VAL   B 78  ? 0.3460 0.2333 0.3781 -0.0017 0.0283  0.0211  84  VAL   C C   
1714 O  O   . VAL   B 78  ? 0.3399 0.2222 0.3756 -0.0037 0.0280  0.0224  84  VAL   C O   
1715 C  CB  . VAL   B 78  ? 0.3529 0.2383 0.3740 0.0042  0.0216  0.0162  84  VAL   C CB  
1716 C  CG1 . VAL   B 78  ? 0.3604 0.2439 0.3722 0.0053  0.0231  0.0207  84  VAL   C CG1 
1717 C  CG2 . VAL   B 78  ? 0.3505 0.2378 0.3690 0.0071  0.0181  0.0114  84  VAL   C CG2 
1718 N  N   . GLU   B 79  ? 0.3389 0.2285 0.3677 -0.0018 0.0323  0.0242  85  GLU   C N   
1719 C  CA  . GLU   B 79  ? 0.3488 0.2346 0.3763 -0.0044 0.0368  0.0298  85  GLU   C CA  
1720 C  C   . GLU   B 79  ? 0.3347 0.2120 0.3534 -0.0038 0.0350  0.0338  85  GLU   C C   
1721 O  O   . GLU   B 79  ? 0.3304 0.2060 0.3425 -0.0009 0.0312  0.0327  85  GLU   C O   
1722 C  CB  . GLU   B 79  ? 0.3953 0.2842 0.4180 -0.0038 0.0420  0.0320  85  GLU   C CB  
1723 C  CG  . GLU   B 79  ? 0.4673 0.3653 0.5022 -0.0051 0.0452  0.0297  85  GLU   C CG  
1724 C  CD  . GLU   B 79  ? 0.5965 0.4958 0.6453 -0.0097 0.0467  0.0304  85  GLU   C CD  
1725 O  OE1 . GLU   B 79  ? 0.6239 0.5181 0.6715 -0.0125 0.0505  0.0355  85  GLU   C OE1 
1726 O  OE2 . GLU   B 79  ? 0.6359 0.5405 0.6963 -0.0107 0.0435  0.0260  85  GLU   C OE2 
1727 N  N   . ALA   B 80  ? 0.3390 0.2109 0.3579 -0.0065 0.0375  0.0387  86  ALA   C N   
1728 C  CA  . ALA   B 80  ? 0.3501 0.2139 0.3618 -0.0059 0.0353  0.0432  86  ALA   C CA  
1729 C  C   . ALA   B 80  ? 0.3545 0.2164 0.3524 -0.0032 0.0341  0.0452  86  ALA   C C   
1730 O  O   . ALA   B 80  ? 0.3544 0.2180 0.3460 -0.0030 0.0374  0.0458  86  ALA   C O   
1731 C  CB  . ALA   B 80  ? 0.3614 0.2194 0.3743 -0.0092 0.0386  0.0488  86  ALA   C CB  
1732 N  N   . SER   B 81  ? 0.3470 0.2057 0.3412 -0.0011 0.0292  0.0457  87  SER   C N   
1733 C  CA  . SER   B 81  ? 0.3639 0.2196 0.3459 0.0008  0.0266  0.0478  87  SER   C CA  
1734 C  C   . SER   B 81  ? 0.3820 0.2299 0.3598 0.0003  0.0239  0.0538  87  SER   C C   
1735 O  O   . SER   B 81  ? 0.3856 0.2306 0.3703 -0.0013 0.0245  0.0559  87  SER   C O   
1736 C  CB  . SER   B 81  ? 0.3749 0.2343 0.3574 0.0036  0.0226  0.0436  87  SER   C CB  
1737 O  OG  . SER   B 81  ? 0.3899 0.2479 0.3788 0.0043  0.0195  0.0437  87  SER   C OG  
1738 N  N   . GLU   B 82  ? 0.3964 0.2403 0.3633 0.0015  0.0202  0.0566  88  GLU   C N   
1739 C  CA  . GLU   B 82  ? 0.4158 0.2524 0.3795 0.0012  0.0163  0.0625  88  GLU   C CA  
1740 C  C   . GLU   B 82  ? 0.4082 0.2462 0.3833 0.0026  0.0124  0.0620  88  GLU   C C   
1741 O  O   . GLU   B 82  ? 0.4140 0.2469 0.3908 0.0026  0.0095  0.0667  88  GLU   C O   
1742 C  CB  . GLU   B 82  ? 0.4688 0.2998 0.4171 0.0016  0.0127  0.0658  88  GLU   C CB  
1743 C  CG  . GLU   B 82  ? 0.5555 0.3880 0.5031 0.0035  0.0065  0.0647  88  GLU   C CG  
1744 C  CD  . GLU   B 82  ? 0.6516 0.4788 0.5835 0.0037  0.0028  0.0664  88  GLU   C CD  
1745 O  OE1 . GLU   B 82  ? 0.6582 0.4805 0.5776 0.0029  0.0060  0.0677  88  GLU   C OE1 
1746 O  OE2 . GLU   B 82  ? 0.6826 0.5101 0.6145 0.0046  -0.0031 0.0663  88  GLU   C OE2 
1747 N  N   . TYR   B 83  ? 0.3826 0.2270 0.3655 0.0041  0.0126  0.0565  89  TYR   C N   
1748 C  CA  . TYR   B 83  ? 0.3684 0.2138 0.3613 0.0059  0.0102  0.0558  89  TYR   C CA  
1749 C  C   . TYR   B 83  ? 0.3655 0.2129 0.3689 0.0058  0.0135  0.0513  89  TYR   C C   
1750 O  O   . TYR   B 83  ? 0.3744 0.2209 0.3855 0.0074  0.0125  0.0510  89  TYR   C O   
1751 C  CB  . TYR   B 83  ? 0.3554 0.2042 0.3470 0.0080  0.0068  0.0542  89  TYR   C CB  
1752 C  CG  . TYR   B 83  ? 0.3526 0.2059 0.3389 0.0083  0.0082  0.0494  89  TYR   C CG  
1753 C  CD1 . TYR   B 83  ? 0.3542 0.2060 0.3290 0.0077  0.0073  0.0505  89  TYR   C CD1 
1754 C  CD2 . TYR   B 83  ? 0.3585 0.2165 0.3503 0.0093  0.0103  0.0439  89  TYR   C CD2 
1755 C  CE1 . TYR   B 83  ? 0.3577 0.2130 0.3280 0.0084  0.0089  0.0462  89  TYR   C CE1 
1756 C  CE2 . TYR   B 83  ? 0.3692 0.2310 0.3565 0.0099  0.0111  0.0398  89  TYR   C CE2 
1757 C  CZ  . TYR   B 83  ? 0.3759 0.2366 0.3531 0.0096  0.0104  0.0410  89  TYR   C CZ  
1758 O  OH  . TYR   B 83  ? 0.3909 0.2550 0.3643 0.0106  0.0113  0.0370  89  TYR   C OH  
1759 N  N   . TYR   B 84  ? 0.3506 0.2008 0.3549 0.0042  0.0171  0.0478  90  TYR   C N   
1760 C  CA  . TYR   B 84  ? 0.3349 0.1858 0.3484 0.0035  0.0191  0.0437  90  TYR   C CA  
1761 C  C   . TYR   B 84  ? 0.3462 0.1967 0.3616 0.0001  0.0227  0.0441  90  TYR   C C   
1762 O  O   . TYR   B 84  ? 0.3513 0.2044 0.3611 -0.0010 0.0247  0.0449  90  TYR   C O   
1763 C  CB  . TYR   B 84  ? 0.3108 0.1672 0.3260 0.0052  0.0188  0.0371  90  TYR   C CB  
1764 C  CG  . TYR   B 84  ? 0.3075 0.1642 0.3235 0.0084  0.0166  0.0357  90  TYR   C CG  
1765 C  CD1 . TYR   B 84  ? 0.3084 0.1612 0.3308 0.0097  0.0166  0.0358  90  TYR   C CD1 
1766 C  CD2 . TYR   B 84  ? 0.3133 0.1740 0.3245 0.0101  0.0153  0.0338  90  TYR   C CD2 
1767 C  CE1 . TYR   B 84  ? 0.3182 0.1719 0.3423 0.0129  0.0158  0.0344  90  TYR   C CE1 
1768 C  CE2 . TYR   B 84  ? 0.3157 0.1769 0.3282 0.0128  0.0141  0.0328  90  TYR   C CE2 
1769 C  CZ  . TYR   B 84  ? 0.3279 0.1861 0.3472 0.0142  0.0148  0.0329  90  TYR   C CZ  
1770 O  OH  . TYR   B 84  ? 0.3299 0.1893 0.3506 0.0170  0.0146  0.0320  90  TYR   C OH  
1771 N  N   . PRO   B 85  ? 0.3536 0.2014 0.3774 -0.0016 0.0239  0.0430  91  PRO   C N   
1772 C  CA  . PRO   B 85  ? 0.3556 0.2043 0.3833 -0.0054 0.0274  0.0431  91  PRO   C CA  
1773 C  C   . PRO   B 85  ? 0.3498 0.2065 0.3804 -0.0057 0.0281  0.0371  91  PRO   C C   
1774 O  O   . PRO   B 85  ? 0.3464 0.2067 0.3749 -0.0029 0.0258  0.0330  91  PRO   C O   
1775 C  CB  . PRO   B 85  ? 0.3693 0.2121 0.4055 -0.0070 0.0274  0.0428  91  PRO   C CB  
1776 C  CG  . PRO   B 85  ? 0.3731 0.2151 0.4110 -0.0034 0.0244  0.0386  91  PRO   C CG  
1777 C  CD  . PRO   B 85  ? 0.3544 0.1981 0.3848 -0.0002 0.0225  0.0412  91  PRO   C CD  
1778 N  N   . ALA   B 86  ? 0.3469 0.2064 0.3833 -0.0091 0.0312  0.0368  92  ALA   C N   
1779 C  CA  . ALA   B 86  ? 0.3470 0.2143 0.3886 -0.0095 0.0312  0.0315  92  ALA   C CA  
1780 C  C   . ALA   B 86  ? 0.3503 0.2164 0.3980 -0.0091 0.0275  0.0257  92  ALA   C C   
1781 O  O   . ALA   B 86  ? 0.3376 0.1982 0.3911 -0.0113 0.0273  0.0259  92  ALA   C O   
1782 C  CB  . ALA   B 86  ? 0.3415 0.2123 0.3905 -0.0136 0.0355  0.0333  92  ALA   C CB  
1783 N  N   . ARG   B 87  ? 0.3499 0.2195 0.3946 -0.0061 0.0246  0.0208  93  ARG   C N   
1784 C  CA  . ARG   B 87  ? 0.3505 0.2171 0.3976 -0.0051 0.0212  0.0154  93  ARG   C CA  
1785 C  C   . ARG   B 87  ? 0.3609 0.2329 0.4054 -0.0028 0.0184  0.0100  93  ARG   C C   
1786 O  O   . ARG   B 87  ? 0.3667 0.2444 0.4073 -0.0013 0.0189  0.0107  93  ARG   C O   
1787 C  CB  . ARG   B 87  ? 0.3507 0.2103 0.3931 -0.0023 0.0206  0.0170  93  ARG   C CB  
1788 C  CG  . ARG   B 87  ? 0.3610 0.2232 0.3949 0.0014  0.0200  0.0184  93  ARG   C CG  
1789 C  CD  . ARG   B 87  ? 0.3690 0.2262 0.4003 0.0043  0.0195  0.0204  93  ARG   C CD  
1790 N  NE  . ARG   B 87  ? 0.3659 0.2264 0.3907 0.0073  0.0183  0.0202  93  ARG   C NE  
1791 C  CZ  . ARG   B 87  ? 0.3894 0.2482 0.4126 0.0104  0.0177  0.0191  93  ARG   C CZ  
1792 N  NH1 . ARG   B 87  ? 0.3897 0.2431 0.4168 0.0114  0.0183  0.0180  93  ARG   C NH1 
1793 N  NH2 . ARG   B 87  ? 0.3842 0.2463 0.4021 0.0125  0.0167  0.0192  93  ARG   C NH2 
1794 N  N   . TYR   B 88  ? 0.3468 0.2156 0.3918 -0.0020 0.0153  0.0046  94  TYR   C N   
1795 C  CA  . TYR   B 88  ? 0.3495 0.2215 0.3899 0.0006  0.0122  -0.0002 94  TYR   C CA  
1796 C  C   . TYR   B 88  ? 0.3321 0.2013 0.3631 0.0047  0.0125  0.0005  94  TYR   C C   
1797 O  O   . TYR   B 88  ? 0.3262 0.1890 0.3560 0.0058  0.0133  0.0012  94  TYR   C O   
1798 C  CB  . TYR   B 88  ? 0.3688 0.2369 0.4114 -0.0003 0.0085  -0.0063 94  TYR   C CB  
1799 C  CG  . TYR   B 88  ? 0.3959 0.2682 0.4488 -0.0044 0.0067  -0.0080 94  TYR   C CG  
1800 C  CD1 . TYR   B 88  ? 0.4067 0.2875 0.4623 -0.0043 0.0046  -0.0098 94  TYR   C CD1 
1801 C  CD2 . TYR   B 88  ? 0.4177 0.2861 0.4790 -0.0085 0.0072  -0.0073 94  TYR   C CD2 
1802 C  CE1 . TYR   B 88  ? 0.4214 0.3075 0.4890 -0.0082 0.0030  -0.0109 94  TYR   C CE1 
1803 C  CE2 . TYR   B 88  ? 0.4299 0.3029 0.5026 -0.0129 0.0056  -0.0084 94  TYR   C CE2 
1804 C  CZ  . TYR   B 88  ? 0.4435 0.3259 0.5199 -0.0127 0.0035  -0.0102 94  TYR   C CZ  
1805 O  OH  . TYR   B 88  ? 0.4782 0.3662 0.5682 -0.0171 0.0018  -0.0111 94  TYR   C OH  
1806 N  N   . GLN   B 89  ? 0.3178 0.1917 0.3431 0.0071  0.0118  0.0003  95  GLN   C N   
1807 C  CA  . GLN   B 89  ? 0.3015 0.1733 0.3186 0.0107  0.0118  0.0008  95  GLN   C CA  
1808 C  C   . GLN   B 89  ? 0.2993 0.1719 0.3112 0.0128  0.0089  -0.0044 95  GLN   C C   
1809 O  O   . GLN   B 89  ? 0.2974 0.1750 0.3101 0.0124  0.0069  -0.0062 95  GLN   C O   
1810 C  CB  . GLN   B 89  ? 0.3103 0.1853 0.3237 0.0114  0.0131  0.0056  95  GLN   C CB  
1811 C  CG  . GLN   B 89  ? 0.3219 0.1949 0.3292 0.0143  0.0131  0.0071  95  GLN   C CG  
1812 C  CD  . GLN   B 89  ? 0.3252 0.1992 0.3295 0.0143  0.0137  0.0124  95  GLN   C CD  
1813 O  OE1 . GLN   B 89  ? 0.3282 0.2016 0.3347 0.0124  0.0149  0.0162  95  GLN   C OE1 
1814 N  NE2 . GLN   B 89  ? 0.3056 0.1804 0.3041 0.0164  0.0127  0.0127  95  GLN   C NE2 
1815 N  N   . SER   B 90  ? 0.2894 0.1569 0.2956 0.0153  0.0089  -0.0063 96  SER   C N   
1816 C  CA  . SER   B 90  ? 0.2950 0.1612 0.2940 0.0175  0.0063  -0.0110 96  SER   C CA  
1817 C  C   . SER   B 90  ? 0.2859 0.1537 0.2770 0.0204  0.0068  -0.0092 96  SER   C C   
1818 O  O   . SER   B 90  ? 0.2841 0.1529 0.2756 0.0208  0.0092  -0.0048 96  SER   C O   
1819 C  CB  . SER   B 90  ? 0.3247 0.1827 0.3206 0.0185  0.0065  -0.0147 96  SER   C CB  
1820 O  OG  . SER   B 90  ? 0.3461 0.2006 0.3398 0.0208  0.0103  -0.0120 96  SER   C OG  
1821 N  N   . HIS   B 91  ? 0.2892 0.1573 0.2737 0.0220  0.0040  -0.0125 97  HIS   C N   
1822 C  CA  . HIS   B 91  ? 0.3104 0.1794 0.2872 0.0245  0.0041  -0.0112 97  HIS   C CA  
1823 C  C   . HIS   B 91  ? 0.2963 0.1708 0.2754 0.0239  0.0046  -0.0070 97  HIS   C C   
1824 O  O   . HIS   B 91  ? 0.3143 0.1886 0.2891 0.0252  0.0056  -0.0041 97  HIS   C O   
1825 C  CB  . HIS   B 91  ? 0.3363 0.2001 0.3076 0.0267  0.0072  -0.0101 97  HIS   C CB  
1826 C  CG  . HIS   B 91  ? 0.3813 0.2382 0.3477 0.0279  0.0074  -0.0146 97  HIS   C CG  
1827 N  ND1 . HIS   B 91  ? 0.4169 0.2700 0.3727 0.0301  0.0059  -0.0177 97  HIS   C ND1 
1828 C  CD2 . HIS   B 91  ? 0.3987 0.2509 0.3684 0.0273  0.0088  -0.0164 97  HIS   C CD2 
1829 C  CE1 . HIS   B 91  ? 0.4248 0.2707 0.3767 0.0308  0.0067  -0.0214 97  HIS   C CE1 
1830 N  NE2 . HIS   B 91  ? 0.4183 0.2634 0.3787 0.0292  0.0084  -0.0209 97  HIS   C NE2 
1831 N  N   . LEU   B 92  ? 0.2763 0.1554 0.2620 0.0219  0.0038  -0.0069 98  LEU   C N   
1832 C  CA  . LEU   B 92  ? 0.2821 0.1656 0.2693 0.0214  0.0047  -0.0036 98  LEU   C CA  
1833 C  C   . LEU   B 92  ? 0.2888 0.1762 0.2741 0.0229  0.0022  -0.0059 98  LEU   C C   
1834 O  O   . LEU   B 92  ? 0.2989 0.1879 0.2870 0.0229  -0.0006 -0.0096 98  LEU   C O   
1835 C  CB  . LEU   B 92  ? 0.2840 0.1696 0.2795 0.0185  0.0068  -0.0016 98  LEU   C CB  
1836 C  CG  . LEU   B 92  ? 0.3138 0.2016 0.3088 0.0179  0.0089  0.0026  98  LEU   C CG  
1837 C  CD1 . LEU   B 92  ? 0.3334 0.2177 0.3222 0.0188  0.0095  0.0063  98  LEU   C CD1 
1838 C  CD2 . LEU   B 92  ? 0.3242 0.2136 0.3269 0.0149  0.0114  0.0045  98  LEU   C CD2 
1839 N  N   . MET   B 93  ? 0.2756 0.1641 0.2565 0.0243  0.0027  -0.0036 99  MET   C N   
1840 C  CA  . MET   B 93  ? 0.2692 0.1608 0.2480 0.0263  0.0007  -0.0051 99  MET   C CA  
1841 C  C   . MET   B 93  ? 0.2811 0.1755 0.2617 0.0259  0.0034  -0.0023 99  MET   C C   
1842 O  O   . MET   B 93  ? 0.2891 0.1805 0.2656 0.0252  0.0052  0.0011  99  MET   C O   
1843 C  CB  . MET   B 93  ? 0.2871 0.1748 0.2559 0.0289  -0.0010 -0.0049 99  MET   C CB  
1844 C  CG  . MET   B 93  ? 0.3251 0.2085 0.2896 0.0296  -0.0024 -0.0070 99  MET   C CG  
1845 S  SD  . MET   B 93  ? 0.3702 0.2485 0.3231 0.0319  -0.0029 -0.0054 99  MET   C SD  
1846 C  CE  . MET   B 93  ? 0.3692 0.2465 0.3232 0.0302  0.0003  -0.0003 99  MET   C CE  
1847 N  N   . LEU   B 94  ? 0.2693 0.1691 0.2553 0.0265  0.0036  -0.0036 100 LEU   C N   
1848 C  CA  . LEU   B 94  ? 0.2764 0.1784 0.2633 0.0264  0.0072  -0.0013 100 LEU   C CA  
1849 C  C   . LEU   B 94  ? 0.2821 0.1846 0.2636 0.0300  0.0065  -0.0021 100 LEU   C C   
1850 O  O   . LEU   B 94  ? 0.2818 0.1858 0.2636 0.0323  0.0030  -0.0049 100 LEU   C O   
1851 C  CB  . LEU   B 94  ? 0.2819 0.1905 0.2811 0.0246  0.0094  -0.0019 100 LEU   C CB  
1852 C  CG  . LEU   B 94  ? 0.2978 0.2058 0.3035 0.0207  0.0109  -0.0007 100 LEU   C CG  
1853 C  CD1 . LEU   B 94  ? 0.3015 0.2164 0.3199 0.0187  0.0134  -0.0009 100 LEU   C CD1 
1854 C  CD2 . LEU   B 94  ? 0.3214 0.2241 0.3208 0.0193  0.0139  0.0036  100 LEU   C CD2 
1855 N  N   . ALA   B 95  ? 0.2813 0.1819 0.2577 0.0305  0.0096  0.0003  101 ALA   C N   
1856 C  CA  . ALA   B 95  ? 0.2933 0.1932 0.2641 0.0340  0.0099  -0.0004 101 ALA   C CA  
1857 C  C   . ALA   B 95  ? 0.2893 0.1898 0.2598 0.0339  0.0154  0.0016  101 ALA   C C   
1858 O  O   . ALA   B 95  ? 0.3015 0.2008 0.2724 0.0309  0.0180  0.0043  101 ALA   C O   
1859 C  CB  . ALA   B 95  ? 0.2971 0.1892 0.2555 0.0351  0.0072  0.0006  101 ALA   C CB  
1860 N  N   . VAL   B 96  ? 0.2891 0.1909 0.2581 0.0373  0.0173  0.0005  102 VAL   C N   
1861 C  CA  . VAL   B 96  ? 0.3116 0.2127 0.2779 0.0378  0.0233  0.0022  102 VAL   C CA  
1862 C  C   . VAL   B 96  ? 0.3324 0.2230 0.2823 0.0381  0.0225  0.0040  102 VAL   C C   
1863 O  O   . VAL   B 96  ? 0.3425 0.2285 0.2848 0.0407  0.0191  0.0026  102 VAL   C O   
1864 C  CB  . VAL   B 96  ? 0.3259 0.2330 0.2986 0.0419  0.0263  0.0001  102 VAL   C CB  
1865 C  CG1 . VAL   B 96  ? 0.3477 0.2524 0.3147 0.0432  0.0336  0.0018  102 VAL   C CG1 
1866 C  CG2 . VAL   B 96  ? 0.3238 0.2418 0.3145 0.0408  0.0262  -0.0013 102 VAL   C CG2 
1867 N  N   . GLY   B 97  ? 0.3364 0.2229 0.2812 0.0353  0.0248  0.0071  103 GLY   C N   
1868 C  CA  . GLY   B 97  ? 0.3465 0.2228 0.2761 0.0349  0.0229  0.0091  103 GLY   C CA  
1869 C  C   . GLY   B 97  ? 0.3586 0.2311 0.2845 0.0313  0.0244  0.0130  103 GLY   C C   
1870 O  O   . GLY   B 97  ? 0.3620 0.2394 0.2973 0.0289  0.0269  0.0143  103 GLY   C O   
1871 N  N   . HIS   B 98  ? 0.3570 0.2200 0.2688 0.0309  0.0227  0.0149  104 HIS   C N   
1872 C  CA  . HIS   B 98  ? 0.3601 0.2181 0.2666 0.0278  0.0232  0.0190  104 HIS   C CA  
1873 C  C   . HIS   B 98  ? 0.3574 0.2157 0.2691 0.0247  0.0181  0.0212  104 HIS   C C   
1874 O  O   . HIS   B 98  ? 0.3441 0.2014 0.2558 0.0248  0.0131  0.0204  104 HIS   C O   
1875 C  CB  . HIS   B 98  ? 0.3873 0.2343 0.2758 0.0286  0.0227  0.0201  104 HIS   C CB  
1876 C  CG  . HIS   B 98  ? 0.4428 0.2838 0.3240 0.0257  0.0229  0.0245  104 HIS   C CG  
1877 N  ND1 . HIS   B 98  ? 0.4724 0.3160 0.3571 0.0246  0.0291  0.0266  104 HIS   C ND1 
1878 C  CD2 . HIS   B 98  ? 0.4718 0.3041 0.3428 0.0236  0.0172  0.0273  104 HIS   C CD2 
1879 C  CE1 . HIS   B 98  ? 0.4856 0.3217 0.3614 0.0220  0.0269  0.0307  104 HIS   C CE1 
1880 N  NE2 . HIS   B 98  ? 0.4870 0.3163 0.3545 0.0215  0.0194  0.0312  104 HIS   C NE2 
1881 N  N   . SER   B 99  ? 0.3539 0.2126 0.2694 0.0219  0.0197  0.0244  105 SER   C N   
1882 C  CA  . SER   B 99  ? 0.3529 0.2114 0.2737 0.0194  0.0155  0.0268  105 SER   C CA  
1883 C  C   . SER   B 99  ? 0.3666 0.2217 0.2860 0.0168  0.0169  0.0313  105 SER   C C   
1884 O  O   . SER   B 99  ? 0.3625 0.2212 0.2883 0.0159  0.0217  0.0318  105 SER   C O   
1885 C  CB  . SER   B 99  ? 0.3612 0.2275 0.2960 0.0194  0.0152  0.0243  105 SER   C CB  
1886 O  OG  . SER   B 99  ? 0.3884 0.2542 0.3283 0.0176  0.0120  0.0265  105 SER   C OG  
1887 N  N   . GLU   B 100 ? 0.3760 0.2240 0.2873 0.0155  0.0123  0.0347  106 GLU   C N   
1888 C  CA  . GLU   B 100 ? 0.3868 0.2300 0.2955 0.0132  0.0118  0.0396  106 GLU   C CA  
1889 C  C   . GLU   B 100 ? 0.3807 0.2263 0.3003 0.0118  0.0075  0.0416  106 GLU   C C   
1890 O  O   . GLU   B 100 ? 0.3839 0.2326 0.3088 0.0126  0.0043  0.0396  106 GLU   C O   
1891 C  CB  . GLU   B 100 ? 0.4311 0.2639 0.3223 0.0130  0.0086  0.0422  106 GLU   C CB  
1892 C  CG  . GLU   B 100 ? 0.5339 0.3612 0.4143 0.0127  0.0138  0.0444  106 GLU   C CG  
1893 C  CD  . GLU   B 100 ? 0.5753 0.3959 0.4392 0.0148  0.0157  0.0424  106 GLU   C CD  
1894 O  OE1 . GLU   B 100 ? 0.5735 0.3897 0.4300 0.0156  0.0101  0.0410  106 GLU   C OE1 
1895 O  OE2 . GLU   B 100 ? 0.5996 0.4194 0.4584 0.0157  0.0230  0.0423  106 GLU   C OE2 
1896 N  N   . PRO   B 101 ? 0.3740 0.2176 0.2969 0.0100  0.0074  0.0457  107 PRO   C N   
1897 C  CA  . PRO   B 101 ? 0.3578 0.2034 0.2917 0.0093  0.0038  0.0474  107 PRO   C CA  
1898 C  C   . PRO   B 101 ? 0.3493 0.1937 0.2823 0.0097  -0.0027 0.0482  107 PRO   C C   
1899 O  O   . PRO   B 101 ? 0.3493 0.1984 0.2927 0.0103  -0.0038 0.0470  107 PRO   C O   
1900 C  CB  . PRO   B 101 ? 0.3791 0.2198 0.3121 0.0076  0.0037  0.0527  107 PRO   C CB  
1901 C  CG  . PRO   B 101 ? 0.3912 0.2272 0.3121 0.0070  0.0078  0.0538  107 PRO   C CG  
1902 C  CD  . PRO   B 101 ? 0.3759 0.2151 0.2927 0.0087  0.0113  0.0489  107 PRO   C CD  
1903 N  N   . GLY   B 102 ? 0.3458 0.1835 0.2661 0.0092  -0.0067 0.0502  108 GLY   C N   
1904 C  CA  . GLY   B 102 ? 0.3511 0.1868 0.2699 0.0088  -0.0135 0.0513  108 GLY   C CA  
1905 C  C   . GLY   B 102 ? 0.3436 0.1833 0.2647 0.0101  -0.0134 0.0470  108 GLY   C C   
1906 O  O   . GLY   B 102 ? 0.3505 0.1901 0.2739 0.0096  -0.0183 0.0480  108 GLY   C O   
1907 N  N   . ASP   B 103 ? 0.3413 0.1843 0.2618 0.0118  -0.0081 0.0427  109 ASP   C N   
1908 C  CA  . ASP   B 103 ? 0.3348 0.1815 0.2573 0.0134  -0.0075 0.0384  109 ASP   C CA  
1909 C  C   . ASP   B 103 ? 0.3266 0.1803 0.2628 0.0139  -0.0064 0.0372  109 ASP   C C   
1910 O  O   . ASP   B 103 ? 0.3257 0.1814 0.2634 0.0150  -0.0071 0.0348  109 ASP   C O   
1911 C  CB  . ASP   B 103 ? 0.3453 0.1930 0.2626 0.0153  -0.0027 0.0344  109 ASP   C CB  
1912 C  CG  . ASP   B 103 ? 0.3814 0.2213 0.2833 0.0157  -0.0033 0.0346  109 ASP   C CG  
1913 O  OD1 . ASP   B 103 ? 0.3781 0.2119 0.2724 0.0148  -0.0087 0.0362  109 ASP   C OD1 
1914 O  OD2 . ASP   B 103 ? 0.4103 0.2500 0.3078 0.0169  0.0018  0.0332  109 ASP   C OD2 
1915 N  N   . CYS   B 104 ? 0.3060 0.1622 0.2514 0.0133  -0.0048 0.0390  110 CYS   C N   
1916 C  CA  . CYS   B 104 ? 0.2990 0.1602 0.2561 0.0140  -0.0034 0.0378  110 CYS   C CA  
1917 C  C   . CYS   B 104 ? 0.2867 0.1484 0.2468 0.0140  -0.0068 0.0392  110 CYS   C C   
1918 O  O   . CYS   B 104 ? 0.2988 0.1573 0.2567 0.0127  -0.0113 0.0430  110 CYS   C O   
1919 C  CB  . CYS   B 104 ? 0.3093 0.1709 0.2743 0.0133  -0.0021 0.0403  110 CYS   C CB  
1920 S  SG  . CYS   B 104 ? 0.3444 0.2078 0.3115 0.0131  0.0033  0.0375  110 CYS   C SG  
1921 N  N   . GLY   B 105 ? 0.2637 0.1288 0.2278 0.0154  -0.0050 0.0363  111 GLY   C N   
1922 C  CA  . GLY   B 105 ? 0.2718 0.1377 0.2394 0.0153  -0.0072 0.0378  111 GLY   C CA  
1923 C  C   . GLY   B 105 ? 0.2867 0.1505 0.2461 0.0155  -0.0091 0.0362  111 GLY   C C   
1924 O  O   . GLY   B 105 ? 0.2976 0.1623 0.2599 0.0154  -0.0099 0.0369  111 GLY   C O   
1925 N  N   . GLY   B 106 ? 0.2903 0.1510 0.2396 0.0157  -0.0095 0.0342  112 GLY   C N   
1926 C  CA  . GLY   B 106 ? 0.3045 0.1622 0.2452 0.0164  -0.0111 0.0322  112 GLY   C CA  
1927 C  C   . GLY   B 106 ? 0.2898 0.1506 0.2329 0.0184  -0.0084 0.0289  112 GLY   C C   
1928 O  O   . GLY   B 106 ? 0.2859 0.1505 0.2332 0.0197  -0.0050 0.0264  112 GLY   C O   
1929 N  N   . ILE   B 107 ? 0.2914 0.1503 0.2322 0.0183  -0.0103 0.0292  113 ILE   C N   
1930 C  CA  . ILE   B 107 ? 0.2963 0.1571 0.2379 0.0202  -0.0079 0.0266  113 ILE   C CA  
1931 C  C   . ILE   B 107 ? 0.3177 0.1774 0.2519 0.0226  -0.0073 0.0224  113 ILE   C C   
1932 O  O   . ILE   B 107 ? 0.3206 0.1762 0.2471 0.0229  -0.0093 0.0218  113 ILE   C O   
1933 C  CB  . ILE   B 107 ? 0.3271 0.1864 0.2702 0.0190  -0.0094 0.0292  113 ILE   C CB  
1934 C  CG1 . ILE   B 107 ? 0.3538 0.2169 0.3083 0.0178  -0.0078 0.0327  113 ILE   C CG1 
1935 C  CG2 . ILE   B 107 ? 0.3445 0.2026 0.2828 0.0210  -0.0079 0.0267  113 ILE   C CG2 
1936 C  CD1 . ILE   B 107 ? 0.3804 0.2433 0.3392 0.0162  -0.0084 0.0361  113 ILE   C CD1 
1937 N  N   . LEU   B 108 ? 0.3074 0.1702 0.2438 0.0246  -0.0048 0.0193  114 LEU   C N   
1938 C  CA  . LEU   B 108 ? 0.2981 0.1607 0.2294 0.0272  -0.0049 0.0155  114 LEU   C CA  
1939 C  C   . LEU   B 108 ? 0.3077 0.1681 0.2362 0.0281  -0.0053 0.0155  114 LEU   C C   
1940 O  O   . LEU   B 108 ? 0.2971 0.1589 0.2297 0.0278  -0.0033 0.0161  114 LEU   C O   
1941 C  CB  . LEU   B 108 ? 0.2913 0.1586 0.2274 0.0284  -0.0027 0.0124  114 LEU   C CB  
1942 C  CG  . LEU   B 108 ? 0.3032 0.1714 0.2367 0.0312  -0.0034 0.0085  114 LEU   C CG  
1943 C  CD1 . LEU   B 108 ? 0.3032 0.1707 0.2325 0.0329  -0.0043 0.0073  114 LEU   C CD1 
1944 C  CD2 . LEU   B 108 ? 0.3137 0.1864 0.2534 0.0315  -0.0021 0.0057  114 LEU   C CD2 
1945 N  N   . ARG   B 109 ? 0.3190 0.1754 0.2400 0.0295  -0.0073 0.0147  115 ARG   C N   
1946 C  CA  . ARG   B 109 ? 0.3373 0.1906 0.2545 0.0303  -0.0076 0.0151  115 ARG   C CA  
1947 C  C   . ARG   B 109 ? 0.3413 0.1921 0.2516 0.0335  -0.0093 0.0122  115 ARG   C C   
1948 O  O   . ARG   B 109 ? 0.3367 0.1869 0.2445 0.0349  -0.0107 0.0105  115 ARG   C O   
1949 C  CB  . ARG   B 109 ? 0.3738 0.2230 0.2898 0.0277  -0.0091 0.0192  115 ARG   C CB  
1950 C  CG  . ARG   B 109 ? 0.4571 0.3008 0.3661 0.0276  -0.0125 0.0192  115 ARG   C CG  
1951 C  CD  . ARG   B 109 ? 0.5570 0.3961 0.4655 0.0244  -0.0150 0.0232  115 ARG   C CD  
1952 N  NE  . ARG   B 109 ? 0.6357 0.4773 0.5507 0.0213  -0.0157 0.0260  115 ARG   C NE  
1953 C  CZ  . ARG   B 109 ? 0.7046 0.5486 0.6278 0.0187  -0.0152 0.0298  115 ARG   C CZ  
1954 N  NH1 . ARG   B 109 ? 0.7131 0.5572 0.6382 0.0185  -0.0131 0.0313  115 ARG   C NH1 
1955 N  NH2 . ARG   B 109 ? 0.7083 0.5545 0.6377 0.0163  -0.0166 0.0324  115 ARG   C NH2 
1956 N  N   . CYS   B 110 ? 0.3401 0.1890 0.2470 0.0347  -0.0091 0.0118  116 CYS   C N   
1957 C  CA  . CYS   B 110 ? 0.3390 0.1847 0.2388 0.0380  -0.0114 0.0095  116 CYS   C CA  
1958 C  C   . CYS   B 110 ? 0.3663 0.2051 0.2593 0.0374  -0.0119 0.0125  116 CYS   C C   
1959 O  O   . CYS   B 110 ? 0.3871 0.2248 0.2824 0.0343  -0.0106 0.0160  116 CYS   C O   
1960 C  CB  . CYS   B 110 ? 0.3475 0.1963 0.2484 0.0400  -0.0111 0.0063  116 CYS   C CB  
1961 S  SG  . CYS   B 110 ? 0.3576 0.2049 0.2574 0.0388  -0.0078 0.0077  116 CYS   C SG  
1962 N  N   . GLN   B 111 ? 0.3738 0.2082 0.2592 0.0402  -0.0138 0.0114  117 GLN   C N   
1963 C  CA  . GLN   B 111 ? 0.3946 0.2218 0.2729 0.0395  -0.0139 0.0145  117 GLN   C CA  
1964 C  C   . GLN   B 111 ? 0.3957 0.2232 0.2751 0.0376  -0.0098 0.0170  117 GLN   C C   
1965 O  O   . GLN   B 111 ? 0.4113 0.2342 0.2881 0.0357  -0.0085 0.0208  117 GLN   C O   
1966 C  CB  . GLN   B 111 ? 0.4435 0.2653 0.3127 0.0433  -0.0170 0.0129  117 GLN   C CB  
1967 C  CG  . GLN   B 111 ? 0.5101 0.3343 0.3776 0.0459  -0.0173 0.0100  117 GLN   C CG  
1968 C  CD  . GLN   B 111 ? 0.6287 0.4475 0.4874 0.0498  -0.0214 0.0088  117 GLN   C CD  
1969 O  OE1 . GLN   B 111 ? 0.6658 0.4875 0.5265 0.0529  -0.0247 0.0056  117 GLN   C OE1 
1970 N  NE2 . GLN   B 111 ? 0.6407 0.4514 0.4899 0.0497  -0.0210 0.0117  117 GLN   C NE2 
1971 N  N   . HIS   B 112 ? 0.3691 0.2014 0.2521 0.0381  -0.0074 0.0149  118 HIS   C N   
1972 C  CA  . HIS   B 112 ? 0.3774 0.2093 0.2607 0.0371  -0.0027 0.0168  118 HIS   C CA  
1973 C  C   . HIS   B 112 ? 0.3810 0.2176 0.2749 0.0339  0.0008  0.0196  118 HIS   C C   
1974 O  O   . HIS   B 112 ? 0.4019 0.2381 0.2974 0.0330  0.0053  0.0221  118 HIS   C O   
1975 C  CB  . HIS   B 112 ? 0.3872 0.2195 0.2666 0.0396  -0.0019 0.0129  118 HIS   C CB  
1976 C  CG  . HIS   B 112 ? 0.4049 0.2332 0.2749 0.0428  -0.0064 0.0101  118 HIS   C CG  
1977 N  ND1 . HIS   B 112 ? 0.4144 0.2466 0.2875 0.0446  -0.0107 0.0064  118 HIS   C ND1 
1978 C  CD2 . HIS   B 112 ? 0.4251 0.2460 0.2834 0.0446  -0.0074 0.0110  118 HIS   C CD2 
1979 C  CE1 . HIS   B 112 ? 0.4306 0.2582 0.2950 0.0475  -0.0145 0.0050  118 HIS   C CE1 
1980 N  NE2 . HIS   B 112 ? 0.4395 0.2598 0.2939 0.0477  -0.0130 0.0077  118 HIS   C NE2 
1981 N  N   . GLY   B 113 ? 0.3619 0.2025 0.2631 0.0324  -0.0013 0.0196  119 GLY   C N   
1982 C  CA  . GLY   B 113 ? 0.3550 0.1998 0.2664 0.0295  0.0008  0.0225  119 GLY   C CA  
1983 C  C   . GLY   B 113 ? 0.3363 0.1863 0.2543 0.0293  0.0000  0.0205  119 GLY   C C   
1984 O  O   . GLY   B 113 ? 0.3234 0.1738 0.2388 0.0307  -0.0027 0.0175  119 GLY   C O   
1985 N  N   . VAL   B 114 ? 0.3177 0.1717 0.2449 0.0278  0.0027  0.0224  120 VAL   C N   
1986 C  CA  . VAL   B 114 ? 0.3157 0.1740 0.2493 0.0273  0.0022  0.0212  120 VAL   C CA  
1987 C  C   . VAL   B 114 ? 0.3152 0.1750 0.2480 0.0295  0.0037  0.0168  120 VAL   C C   
1988 O  O   . VAL   B 114 ? 0.3228 0.1819 0.2551 0.0307  0.0069  0.0159  120 VAL   C O   
1989 C  CB  . VAL   B 114 ? 0.3251 0.1865 0.2691 0.0251  0.0040  0.0251  120 VAL   C CB  
1990 C  CG1 . VAL   B 114 ? 0.3247 0.1895 0.2744 0.0247  0.0034  0.0242  120 VAL   C CG1 
1991 C  CG2 . VAL   B 114 ? 0.3312 0.1912 0.2772 0.0223  0.0013  0.0296  120 VAL   C CG2 
1992 N  N   . VAL   B 115 ? 0.3123 0.1739 0.2448 0.0301  0.0014  0.0140  121 VAL   C N   
1993 C  CA  . VAL   B 115 ? 0.3273 0.1908 0.2605 0.0315  0.0017  0.0098  121 VAL   C CA  
1994 C  C   . VAL   B 115 ? 0.3190 0.1858 0.2610 0.0302  0.0037  0.0100  121 VAL   C C   
1995 O  O   . VAL   B 115 ? 0.3237 0.1908 0.2675 0.0309  0.0051  0.0073  121 VAL   C O   
1996 C  CB  . VAL   B 115 ? 0.3347 0.1990 0.2649 0.0328  -0.0015 0.0072  121 VAL   C CB  
1997 C  CG1 . VAL   B 115 ? 0.3255 0.1932 0.2597 0.0334  -0.0017 0.0033  121 VAL   C CG1 
1998 C  CG2 . VAL   B 115 ? 0.3493 0.2097 0.2708 0.0348  -0.0037 0.0066  121 VAL   C CG2 
1999 N  N   . GLY   B 116 ? 0.2992 0.1675 0.2455 0.0283  0.0031  0.0129  122 GLY   C N   
2000 C  CA  . GLY   B 116 ? 0.3076 0.1782 0.2616 0.0269  0.0044  0.0139  122 GLY   C CA  
2001 C  C   . GLY   B 116 ? 0.3000 0.1710 0.2562 0.0249  0.0029  0.0177  122 GLY   C C   
2002 O  O   . GLY   B 116 ? 0.2946 0.1635 0.2470 0.0243  0.0008  0.0199  122 GLY   C O   
2003 N  N   . ILE   B 117 ? 0.2820 0.1544 0.2434 0.0238  0.0036  0.0185  123 ILE   C N   
2004 C  CA  . ILE   B 117 ? 0.2642 0.1359 0.2263 0.0219  0.0018  0.0222  123 ILE   C CA  
2005 C  C   . ILE   B 117 ? 0.2695 0.1422 0.2324 0.0213  0.0026  0.0212  123 ILE   C C   
2006 O  O   . ILE   B 117 ? 0.2710 0.1455 0.2387 0.0215  0.0047  0.0191  123 ILE   C O   
2007 C  CB  . ILE   B 117 ? 0.2790 0.1508 0.2486 0.0207  0.0018  0.0266  123 ILE   C CB  
2008 C  CG1 . ILE   B 117 ? 0.2918 0.1652 0.2688 0.0215  0.0051  0.0255  123 ILE   C CG1 
2009 C  CG2 . ILE   B 117 ? 0.2837 0.1550 0.2540 0.0204  0.0007  0.0292  123 ILE   C CG2 
2010 C  CD1 . ILE   B 117 ? 0.2972 0.1710 0.2833 0.0209  0.0052  0.0300  123 ILE   C CD1 
2011 N  N   . VAL   B 118 ? 0.2682 0.1391 0.2262 0.0203  0.0012  0.0230  124 VAL   C N   
2012 C  CA  . VAL   B 118 ? 0.2800 0.1513 0.2379 0.0196  0.0028  0.0229  124 VAL   C CA  
2013 C  C   . VAL   B 118 ? 0.2889 0.1609 0.2547 0.0183  0.0043  0.0248  124 VAL   C C   
2014 O  O   . VAL   B 118 ? 0.2980 0.1687 0.2671 0.0176  0.0029  0.0280  124 VAL   C O   
2015 C  CB  . VAL   B 118 ? 0.2888 0.1561 0.2381 0.0188  0.0012  0.0252  124 VAL   C CB  
2016 C  CG1 . VAL   B 118 ? 0.2869 0.1540 0.2360 0.0178  0.0038  0.0262  124 VAL   C CG1 
2017 C  CG2 . VAL   B 118 ? 0.2988 0.1647 0.2403 0.0206  0.0004  0.0226  124 VAL   C CG2 
2018 N  N   . SER   B 119 ? 0.2890 0.1631 0.2589 0.0179  0.0069  0.0228  125 SER   C N   
2019 C  CA  . SER   B 119 ? 0.2980 0.1718 0.2753 0.0167  0.0084  0.0242  125 SER   C CA  
2020 C  C   . SER   B 119 ? 0.2902 0.1643 0.2684 0.0150  0.0107  0.0248  125 SER   C C   
2021 O  O   . SER   B 119 ? 0.3020 0.1741 0.2840 0.0136  0.0115  0.0277  125 SER   C O   
2022 C  CB  . SER   B 119 ? 0.3224 0.1978 0.3056 0.0176  0.0095  0.0205  125 SER   C CB  
2023 O  OG  . SER   B 119 ? 0.3490 0.2232 0.3391 0.0166  0.0110  0.0212  125 SER   C OG  
2024 N  N   . THR   B 120 ? 0.2792 0.1558 0.2547 0.0154  0.0121  0.0224  126 THR   C N   
2025 C  CA  . THR   B 120 ? 0.2748 0.1525 0.2525 0.0138  0.0153  0.0232  126 THR   C CA  
2026 C  C   . THR   B 120 ? 0.3066 0.1843 0.2763 0.0148  0.0168  0.0234  126 THR   C C   
2027 O  O   . THR   B 120 ? 0.3002 0.1779 0.2642 0.0168  0.0151  0.0216  126 THR   C O   
2028 C  CB  . THR   B 120 ? 0.2583 0.1407 0.2456 0.0132  0.0168  0.0193  126 THR   C CB  
2029 O  OG1 . THR   B 120 ? 0.2675 0.1541 0.2543 0.0151  0.0164  0.0154  126 THR   C OG1 
2030 C  CG2 . THR   B 120 ? 0.2563 0.1374 0.2496 0.0130  0.0155  0.0179  126 THR   C CG2 
2031 N  N   . GLY   B 121 ? 0.3295 0.2068 0.2988 0.0133  0.0205  0.0255  127 GLY   C N   
2032 C  CA  . GLY   B 121 ? 0.3620 0.2386 0.3235 0.0144  0.0233  0.0258  127 GLY   C CA  
2033 C  C   . GLY   B 121 ? 0.3950 0.2730 0.3600 0.0126  0.0289  0.0277  127 GLY   C C   
2034 O  O   . GLY   B 121 ? 0.3972 0.2738 0.3669 0.0100  0.0297  0.0304  127 GLY   C O   
2035 N  N   . GLY   B 122 ? 0.4144 0.2946 0.3767 0.0141  0.0330  0.0266  128 GLY   C N   
2036 C  CA  . GLY   B 122 ? 0.4293 0.3117 0.3953 0.0126  0.0396  0.0285  128 GLY   C CA  
2037 C  C   . GLY   B 122 ? 0.4280 0.3193 0.4036 0.0142  0.0429  0.0249  128 GLY   C C   
2038 O  O   . GLY   B 122 ? 0.4196 0.3157 0.4017 0.0157  0.0392  0.0209  128 GLY   C O   
2039 N  N   . ASN   B 123 ? 0.4279 0.3213 0.4045 0.0141  0.0501  0.0265  129 ASN   C N   
2040 C  CA  . ASN   B 123 ? 0.4301 0.3329 0.4179 0.0158  0.0542  0.0238  129 ASN   C CA  
2041 C  C   . ASN   B 123 ? 0.4227 0.3270 0.4063 0.0205  0.0519  0.0198  129 ASN   C C   
2042 O  O   . ASN   B 123 ? 0.4276 0.3406 0.4230 0.0222  0.0527  0.0169  129 ASN   C O   
2043 C  CB  . ASN   B 123 ? 0.4532 0.3647 0.4604 0.0130  0.0528  0.0220  129 ASN   C CB  
2044 C  CG  . ASN   B 123 ? 0.5211 0.4362 0.5383 0.0095  0.0596  0.0252  129 ASN   C CG  
2045 O  OD1 . ASN   B 123 ? 0.5466 0.4581 0.5563 0.0094  0.0663  0.0289  129 ASN   C OD1 
2046 N  ND2 . ASN   B 123 ? 0.5314 0.4527 0.5651 0.0064  0.0579  0.0240  129 ASN   C ND2 
2047 N  N   . GLY   B 124 ? 0.4151 0.3108 0.3825 0.0225  0.0490  0.0200  130 GLY   C N   
2048 C  CA  . GLY   B 124 ? 0.4097 0.3049 0.3715 0.0268  0.0466  0.0166  130 GLY   C CA  
2049 C  C   . GLY   B 124 ? 0.3914 0.2894 0.3586 0.0275  0.0392  0.0133  130 GLY   C C   
2050 O  O   . GLY   B 124 ? 0.3907 0.2904 0.3574 0.0310  0.0373  0.0103  130 GLY   C O   
2051 N  N   . LEU   B 125 ? 0.3707 0.2686 0.3428 0.0242  0.0353  0.0141  131 LEU   C N   
2052 C  CA  . LEU   B 125 ? 0.3679 0.2672 0.3434 0.0247  0.0290  0.0113  131 LEU   C CA  
2053 C  C   . LEU   B 125 ? 0.3554 0.2474 0.3229 0.0231  0.0251  0.0133  131 LEU   C C   
2054 O  O   . LEU   B 125 ? 0.3719 0.2599 0.3366 0.0206  0.0265  0.0169  131 LEU   C O   
2055 C  CB  . LEU   B 125 ? 0.3766 0.2832 0.3675 0.0227  0.0282  0.0094  131 LEU   C CB  
2056 C  CG  . LEU   B 125 ? 0.4021 0.3175 0.4051 0.0233  0.0319  0.0081  131 LEU   C CG  
2057 C  CD1 . LEU   B 125 ? 0.4110 0.3317 0.4285 0.0197  0.0314  0.0075  131 LEU   C CD1 
2058 C  CD2 . LEU   B 125 ? 0.4092 0.3282 0.4130 0.0275  0.0296  0.0046  131 LEU   C CD2 
2059 N  N   . VAL   B 126 ? 0.3144 0.2047 0.2786 0.0246  0.0202  0.0115  132 VAL   C N   
2060 C  CA  . VAL   B 126 ? 0.3051 0.1902 0.2647 0.0233  0.0165  0.0133  132 VAL   C CA  
2061 C  C   . VAL   B 126 ? 0.2929 0.1812 0.2604 0.0230  0.0138  0.0107  132 VAL   C C   
2062 O  O   . VAL   B 126 ? 0.2788 0.1704 0.2488 0.0250  0.0123  0.0073  132 VAL   C O   
2063 C  CB  . VAL   B 126 ? 0.3040 0.1833 0.2520 0.0251  0.0136  0.0136  132 VAL   C CB  
2064 C  CG1 . VAL   B 126 ? 0.3106 0.1922 0.2582 0.0283  0.0122  0.0099  132 VAL   C CG1 
2065 C  CG2 . VAL   B 126 ? 0.3077 0.1831 0.2537 0.0236  0.0099  0.0157  132 VAL   C CG2 
2066 N  N   . GLY   B 127 ? 0.3032 0.1896 0.2735 0.0209  0.0130  0.0125  133 GLY   C N   
2067 C  CA  . GLY   B 127 ? 0.3045 0.1920 0.2802 0.0208  0.0111  0.0101  133 GLY   C CA  
2068 C  C   . GLY   B 127 ? 0.3108 0.1942 0.2820 0.0213  0.0088  0.0115  133 GLY   C C   
2069 O  O   . GLY   B 127 ? 0.3115 0.1916 0.2800 0.0202  0.0087  0.0152  133 GLY   C O   
2070 N  N   . PHE   B 128 ? 0.2852 0.1688 0.2557 0.0229  0.0069  0.0086  134 PHE   C N   
2071 C  CA  . PHE   B 128 ? 0.2938 0.1741 0.2607 0.0235  0.0057  0.0098  134 PHE   C CA  
2072 C  C   . PHE   B 128 ? 0.2931 0.1728 0.2641 0.0236  0.0062  0.0080  134 PHE   C C   
2073 O  O   . PHE   B 128 ? 0.3031 0.1839 0.2752 0.0243  0.0055  0.0041  134 PHE   C O   
2074 C  CB  . PHE   B 128 ? 0.2830 0.1623 0.2428 0.0257  0.0036  0.0084  134 PHE   C CB  
2075 C  CG  . PHE   B 128 ? 0.2822 0.1610 0.2367 0.0264  0.0031  0.0091  134 PHE   C CG  
2076 C  CD1 . PHE   B 128 ? 0.2978 0.1728 0.2470 0.0256  0.0023  0.0124  134 PHE   C CD1 
2077 C  CD2 . PHE   B 128 ? 0.3011 0.1828 0.2559 0.0281  0.0032  0.0063  134 PHE   C CD2 
2078 C  CE1 . PHE   B 128 ? 0.3112 0.1841 0.2538 0.0264  0.0019  0.0126  134 PHE   C CE1 
2079 C  CE2 . PHE   B 128 ? 0.3130 0.1935 0.2625 0.0294  0.0035  0.0066  134 PHE   C CE2 
2080 C  CZ  . PHE   B 128 ? 0.3166 0.1921 0.2591 0.0285  0.0030  0.0097  134 PHE   C CZ  
2081 N  N   . ALA   B 129 ? 0.2890 0.1664 0.2618 0.0231  0.0071  0.0107  135 ALA   C N   
2082 C  CA  . ALA   B 129 ? 0.2862 0.1619 0.2617 0.0238  0.0084  0.0089  135 ALA   C CA  
2083 C  C   . ALA   B 129 ? 0.2813 0.1553 0.2505 0.0259  0.0080  0.0074  135 ALA   C C   
2084 O  O   . ALA   B 129 ? 0.2635 0.1369 0.2302 0.0261  0.0079  0.0103  135 ALA   C O   
2085 C  CB  . ALA   B 129 ? 0.2828 0.1570 0.2636 0.0231  0.0101  0.0126  135 ALA   C CB  
2086 N  N   . ASP   B 130 ? 0.2962 0.1693 0.2623 0.0271  0.0073  0.0030  136 ASP   C N   
2087 C  CA  . ASP   B 130 ? 0.3136 0.1840 0.2719 0.0292  0.0069  0.0016  136 ASP   C CA  
2088 C  C   . ASP   B 130 ? 0.3176 0.1849 0.2758 0.0300  0.0104  0.0032  136 ASP   C C   
2089 O  O   . ASP   B 130 ? 0.3197 0.1861 0.2833 0.0298  0.0126  0.0031  136 ASP   C O   
2090 C  CB  . ASP   B 130 ? 0.3512 0.2205 0.3059 0.0303  0.0047  -0.0036 136 ASP   C CB  
2091 C  CG  . ASP   B 130 ? 0.4054 0.2708 0.3500 0.0326  0.0038  -0.0050 136 ASP   C CG  
2092 O  OD1 . ASP   B 130 ? 0.4115 0.2772 0.3519 0.0333  0.0028  -0.0030 136 ASP   C OD1 
2093 O  OD2 . ASP   B 130 ? 0.4380 0.2992 0.3781 0.0337  0.0042  -0.0080 136 ASP   C OD2 
2094 N  N   . VAL   B 131 ? 0.3073 0.1729 0.2601 0.0311  0.0113  0.0049  137 VAL   C N   
2095 C  CA  . VAL   B 131 ? 0.3059 0.1690 0.2589 0.0322  0.0155  0.0066  137 VAL   C CA  
2096 C  C   . VAL   B 131 ? 0.3112 0.1697 0.2534 0.0344  0.0166  0.0045  137 VAL   C C   
2097 O  O   . VAL   B 131 ? 0.3267 0.1825 0.2675 0.0357  0.0211  0.0055  137 VAL   C O   
2098 C  CB  . VAL   B 131 ? 0.3218 0.1875 0.2813 0.0310  0.0168  0.0123  137 VAL   C CB  
2099 C  CG1 . VAL   B 131 ? 0.3227 0.1915 0.2914 0.0291  0.0156  0.0147  137 VAL   C CG1 
2100 C  CG2 . VAL   B 131 ? 0.3343 0.2001 0.2889 0.0303  0.0142  0.0144  137 VAL   C CG2 
2101 N  N   . ARG   B 132 ? 0.3019 0.1593 0.2364 0.0350  0.0127  0.0018  138 ARG   C N   
2102 C  CA  . ARG   B 132 ? 0.3044 0.1566 0.2271 0.0370  0.0127  0.0003  138 ARG   C CA  
2103 C  C   . ARG   B 132 ? 0.3405 0.1868 0.2564 0.0389  0.0152  -0.0034 138 ARG   C C   
2104 O  O   . ARG   B 132 ? 0.3673 0.2081 0.2727 0.0407  0.0170  -0.0036 138 ARG   C O   
2105 C  CB  . ARG   B 132 ? 0.2872 0.1395 0.2043 0.0375  0.0071  -0.0017 138 ARG   C CB  
2106 C  CG  . ARG   B 132 ? 0.2721 0.1280 0.1928 0.0363  0.0052  0.0015  138 ARG   C CG  
2107 C  CD  . ARG   B 132 ? 0.2800 0.1360 0.1958 0.0376  0.0002  -0.0009 138 ARG   C CD  
2108 N  NE  . ARG   B 132 ? 0.2848 0.1451 0.2072 0.0371  -0.0021 -0.0041 138 ARG   C NE  
2109 C  CZ  . ARG   B 132 ? 0.3239 0.1866 0.2465 0.0381  -0.0061 -0.0062 138 ARG   C CZ  
2110 N  NH1 . ARG   B 132 ? 0.3210 0.1811 0.2362 0.0401  -0.0088 -0.0061 138 ARG   C NH1 
2111 N  NH2 . ARG   B 132 ? 0.3214 0.1888 0.2518 0.0373  -0.0075 -0.0085 138 ARG   C NH2 
2112 N  N   . ASP   B 133 ? 0.3384 0.1849 0.2593 0.0385  0.0152  -0.0064 139 ASP   C N   
2113 C  CA  . ASP   B 133 ? 0.3392 0.1788 0.2530 0.0403  0.0172  -0.0104 139 ASP   C CA  
2114 C  C   . ASP   B 133 ? 0.3522 0.1895 0.2684 0.0415  0.0248  -0.0081 139 ASP   C C   
2115 O  O   . ASP   B 133 ? 0.3703 0.2005 0.2786 0.0437  0.0280  -0.0111 139 ASP   C O   
2116 C  CB  . ASP   B 133 ? 0.3578 0.1977 0.2761 0.0391  0.0135  -0.0147 139 ASP   C CB  
2117 C  CG  . ASP   B 133 ? 0.3961 0.2403 0.3280 0.0373  0.0157  -0.0126 139 ASP   C CG  
2118 O  OD1 . ASP   B 133 ? 0.3781 0.2285 0.3178 0.0359  0.0158  -0.0081 139 ASP   C OD1 
2119 O  OD2 . ASP   B 133 ? 0.4204 0.2611 0.3546 0.0373  0.0170  -0.0152 139 ASP   C OD2 
2120 N  N   . LEU   B 134 ? 0.3426 0.1856 0.2700 0.0404  0.0276  -0.0028 140 LEU   C N   
2121 C  CA  . LEU   B 134 ? 0.3418 0.1846 0.2753 0.0416  0.0345  0.0000  140 LEU   C CA  
2122 C  C   . LEU   B 134 ? 0.3447 0.1855 0.2720 0.0430  0.0391  0.0029  140 LEU   C C   
2123 O  O   . LEU   B 134 ? 0.3359 0.1817 0.2708 0.0417  0.0404  0.0082  140 LEU   C O   
2124 C  CB  . LEU   B 134 ? 0.3302 0.1804 0.2792 0.0395  0.0340  0.0046  140 LEU   C CB  
2125 C  CG  . LEU   B 134 ? 0.3376 0.1896 0.2931 0.0379  0.0302  0.0026  140 LEU   C CG  
2126 C  CD1 . LEU   B 134 ? 0.3352 0.1930 0.3036 0.0360  0.0296  0.0076  140 LEU   C CD1 
2127 C  CD2 . LEU   B 134 ? 0.3531 0.1993 0.3074 0.0396  0.0328  -0.0016 140 LEU   C CD2 
2128 N  N   . LEU   B 135 ? 0.3673 0.2003 0.2800 0.0453  0.0411  -0.0005 141 LEU   C N   
2129 C  CA  . LEU   B 135 ? 0.3944 0.2241 0.2986 0.0466  0.0457  0.0022  141 LEU   C CA  
2130 C  C   . LEU   B 135 ? 0.4003 0.2324 0.3138 0.0475  0.0544  0.0070  141 LEU   C C   
2131 O  O   . LEU   B 135 ? 0.4066 0.2400 0.3200 0.0470  0.0575  0.0115  141 LEU   C O   
2132 C  CB  . LEU   B 135 ? 0.4131 0.2322 0.2976 0.0492  0.0461  -0.0025 141 LEU   C CB  
2133 C  CG  . LEU   B 135 ? 0.4353 0.2517 0.3113 0.0487  0.0371  -0.0076 141 LEU   C CG  
2134 C  CD1 . LEU   B 135 ? 0.4578 0.2630 0.3135 0.0513  0.0370  -0.0118 141 LEU   C CD1 
2135 C  CD2 . LEU   B 135 ? 0.4323 0.2547 0.3121 0.0464  0.0306  -0.0052 141 LEU   C CD2 
2136 N  N   . TRP   B 136 ? 0.3974 0.2306 0.3202 0.0487  0.0582  0.0062  142 TRP   C N   
2137 C  CA  . TRP   B 136 ? 0.4000 0.2363 0.3339 0.0501  0.0665  0.0107  142 TRP   C CA  
2138 C  C   . TRP   B 136 ? 0.3922 0.2385 0.3424 0.0470  0.0647  0.0175  142 TRP   C C   
2139 O  O   . TRP   B 136 ? 0.3981 0.2480 0.3578 0.0476  0.0709  0.0222  142 TRP   C O   
2140 C  CB  . TRP   B 136 ? 0.4021 0.2368 0.3427 0.0525  0.0702  0.0082  142 TRP   C CB  
2141 C  CG  . TRP   B 136 ? 0.3970 0.2354 0.3465 0.0504  0.0632  0.0069  142 TRP   C CG  
2142 C  CD1 . TRP   B 136 ? 0.4114 0.2450 0.3538 0.0500  0.0582  0.0012  142 TRP   C CD1 
2143 C  CD2 . TRP   B 136 ? 0.3887 0.2356 0.3559 0.0483  0.0608  0.0116  142 TRP   C CD2 
2144 N  NE1 . TRP   B 136 ? 0.4087 0.2475 0.3634 0.0478  0.0536  0.0023  142 TRP   C NE1 
2145 C  CE2 . TRP   B 136 ? 0.3975 0.2440 0.3664 0.0468  0.0549  0.0086  142 TRP   C CE2 
2146 C  CE3 . TRP   B 136 ? 0.3901 0.2448 0.3719 0.0473  0.0627  0.0182  142 TRP   C CE3 
2147 C  CZ2 . TRP   B 136 ? 0.3952 0.2480 0.3782 0.0447  0.0515  0.0121  142 TRP   C CZ2 
2148 C  CZ3 . TRP   B 136 ? 0.3886 0.2494 0.3843 0.0452  0.0582  0.0214  142 TRP   C CZ3 
2149 C  CH2 . TRP   B 136 ? 0.3899 0.2493 0.3852 0.0441  0.0528  0.0184  142 TRP   C CH2 
2150 N  N   . LEU   B 137 ? 0.3811 0.2315 0.3341 0.0438  0.0562  0.0180  143 LEU   C N   
2151 C  CA  . LEU   B 137 ? 0.3878 0.2459 0.3534 0.0406  0.0533  0.0239  143 LEU   C CA  
2152 C  C   . LEU   B 137 ? 0.4099 0.2679 0.3728 0.0397  0.0563  0.0281  143 LEU   C C   
2153 O  O   . LEU   B 137 ? 0.4143 0.2782 0.3895 0.0374  0.0560  0.0336  143 LEU   C O   
2154 C  CB  . LEU   B 137 ? 0.3915 0.2516 0.3562 0.0378  0.0442  0.0229  143 LEU   C CB  
2155 C  CG  . LEU   B 137 ? 0.4035 0.2654 0.3745 0.0374  0.0408  0.0208  143 LEU   C CG  
2156 C  CD1 . LEU   B 137 ? 0.4109 0.2743 0.3790 0.0349  0.0331  0.0198  143 LEU   C CD1 
2157 C  CD2 . LEU   B 137 ? 0.4073 0.2747 0.3948 0.0369  0.0424  0.0255  143 LEU   C CD2 
2158 N  N   . ASP   B 138 ? 0.4245 0.2754 0.3711 0.0413  0.0585  0.0256  144 ASP   C N   
2159 C  CA  . ASP   B 138 ? 0.4551 0.3041 0.3964 0.0405  0.0614  0.0293  144 ASP   C CA  
2160 C  C   . ASP   B 138 ? 0.4988 0.3472 0.4433 0.0425  0.0722  0.0325  144 ASP   C C   
2161 O  O   . ASP   B 138 ? 0.5028 0.3490 0.4420 0.0418  0.0756  0.0358  144 ASP   C O   
2162 C  CB  . ASP   B 138 ? 0.4613 0.3018 0.3822 0.0416  0.0586  0.0255  144 ASP   C CB  
2163 C  CG  . ASP   B 138 ? 0.4778 0.3190 0.3953 0.0399  0.0487  0.0230  144 ASP   C CG  
2164 O  OD1 . ASP   B 138 ? 0.4656 0.3130 0.3946 0.0372  0.0442  0.0254  144 ASP   C OD1 
2165 O  OD2 . ASP   B 138 ? 0.5046 0.3397 0.4075 0.0414  0.0454  0.0187  144 ASP   C OD2 
2166 N  N   . GLU   B 139 ? 0.5286 0.3785 0.4809 0.0452  0.0780  0.0316  145 GLU   C N   
2167 C  CA  . GLU   B 139 ? 0.5755 0.4245 0.5305 0.0479  0.0895  0.0343  145 GLU   C CA  
2168 C  C   . GLU   B 139 ? 0.6047 0.4603 0.5791 0.0496  0.0944  0.0362  145 GLU   C C   
2169 O  O   . GLU   B 139 ? 0.6016 0.4616 0.5860 0.0486  0.0883  0.0354  145 GLU   C O   
2170 C  CB  . GLU   B 139 ? 0.6399 0.4772 0.5728 0.0517  0.0944  0.0289  145 GLU   C CB  
2171 C  CG  . GLU   B 139 ? 0.7456 0.5784 0.6735 0.0543  0.0922  0.0221  145 GLU   C CG  
2172 C  CD  . GLU   B 139 ? 0.8978 0.7200 0.8028 0.0555  0.0878  0.0156  145 GLU   C CD  
2173 O  OE1 . GLU   B 139 ? 0.9362 0.7519 0.8337 0.0582  0.0885  0.0099  145 GLU   C OE1 
2174 O  OE2 . GLU   B 139 ? 0.9462 0.7661 0.8409 0.0537  0.0832  0.0163  145 GLU   C OE2 
2175 N  N   . GLU   B 140 ? 0.6306 0.4865 0.6100 0.0525  0.1059  0.0390  146 GLU   C N   
2176 C  CA  . GLU   B 140 ? 0.6496 0.5114 0.6476 0.0552  0.1124  0.0411  146 GLU   C CA  
2177 C  C   . GLU   B 140 ? 0.6653 0.5397 0.6880 0.0515  0.1081  0.0480  146 GLU   C C   
2178 O  O   . GLU   B 140 ? 0.6782 0.5581 0.7107 0.0495  0.1117  0.0541  146 GLU   C O   
2179 C  CB  . GLU   B 140 ? 0.6798 0.5365 0.6737 0.0586  0.1114  0.0347  146 GLU   C CB  
2180 C  CG  . GLU   B 140 ? 0.7361 0.5998 0.7517 0.0604  0.1133  0.0370  146 GLU   C CG  
2181 C  CD  . GLU   B 140 ? 0.7992 0.6620 0.8211 0.0658  0.1264  0.0378  146 GLU   C CD  
2182 O  OE1 . GLU   B 140 ? 0.8319 0.6901 0.8536 0.0697  0.1287  0.0337  146 GLU   C OE1 
2183 O  OE2 . GLU   B 140 ? 0.8043 0.6706 0.8316 0.0662  0.1348  0.0427  146 GLU   C OE2 
2184 N  N1  . A1BOV C .   ? 0.6480 0.4987 0.6519 0.0543  0.0340  -0.0314 201 A1BOV A N1  
2185 C  C4  . A1BOV C .   ? 0.7262 0.5931 0.7381 0.0613  0.0548  -0.0459 201 A1BOV A C4  
2186 C  C5  . A1BOV C .   ? 0.7245 0.5917 0.7236 0.0562  0.0474  -0.0421 201 A1BOV A C5  
2187 C  C6  . A1BOV C .   ? 0.6671 0.5262 0.6713 0.0557  0.0371  -0.0311 201 A1BOV A C6  
2188 C  C7  . A1BOV C .   ? 0.6428 0.4848 0.6406 0.0518  0.0354  -0.0400 201 A1BOV A C7  
2189 C  C8  . A1BOV C .   ? 0.6363 0.4731 0.6310 0.0487  0.0298  -0.0375 201 A1BOV A C8  
2190 C  C10 . A1BOV C .   ? 0.6182 0.4629 0.6291 0.0529  0.0262  -0.0211 201 A1BOV A C10 
2191 C  C13 . A1BOV C .   ? 0.7459 0.6206 0.7320 0.0519  0.0456  -0.0418 201 A1BOV A C13 
2192 CL CL  . A1BOV C .   ? 0.7661 0.6415 0.7408 0.0469  0.0368  -0.0356 201 A1BOV A CL  
2193 C  C1  . A1BOV C .   ? 0.7457 0.6277 0.7297 0.0517  0.0512  -0.0459 201 A1BOV A C1  
2194 O  O   . A1BOV C .   ? 0.7500 0.6387 0.7209 0.0466  0.0484  -0.0447 201 A1BOV A O   
2195 C  C   . A1BOV C .   ? 0.7532 0.6445 0.7137 0.0425  0.0528  -0.0527 201 A1BOV A C   
2196 C  C3  . A1BOV C .   ? 0.7319 0.6062 0.7425 0.0616  0.0611  -0.0506 201 A1BOV A C3  
2197 C  C2  . A1BOV C .   ? 0.7383 0.6205 0.7342 0.0564  0.0592  -0.0507 201 A1BOV A C2  
2198 N  N   . A1BOV C .   ? 0.6991 0.5582 0.6978 0.0550  0.0424  -0.0399 201 A1BOV A N   
2199 O  O1  . A1BOV C .   ? 0.6570 0.5236 0.6655 0.0568  0.0353  -0.0235 201 A1BOV A O1  
2200 C  C12 . A1BOV C .   ? 0.6289 0.4780 0.6451 0.0568  0.0318  -0.0237 201 A1BOV A C12 
2201 C  C11 . A1BOV C .   ? 0.5983 0.4431 0.6191 0.0537  0.0230  -0.0121 201 A1BOV A C11 
2202 O  O2  . A1BOV C .   ? 0.5916 0.4334 0.6257 0.0573  0.0249  -0.0097 201 A1BOV A O2  
2203 N  N2  . A1BOV C .   ? 0.5872 0.4357 0.6019 0.0498  0.0184  -0.0070 201 A1BOV A N2  
2204 C  C9  . A1BOV C .   ? 0.6280 0.4631 0.6346 0.0512  0.0275  -0.0295 201 A1BOV A C9  
# 
