data_7HWL
# 
_entry.id   7HWL 
# 
_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   7HWL         pdb_00007hwl 10.2210/pdb7hwl/pdb 
WWPDB D_1001408021 ?            ?                   
# 
_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                        7HWL 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                      15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[2-(2-methoxyphenyl)ethyl]-5-oxopyrrolidine-3-carboxamide' 262.304   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                         65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                               78.133    2   ?         ? ? ? 
5 water       nat water                                                              18.015    342 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[2-(2-methoxyphenyl)ethyl]-5-oxopyrrolidine-3-carboxamide' A1BQJ 
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 
A1BQJ non-polymer         . '(3S)-1-[2-(2-methoxyphenyl)ethyl]-5-oxopyrrolidine-3-carboxamide' ? 'C14 H18 N2 O3'  262.304 
ALA   'L-peptide linking' y ALANINE                                                            ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                           ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                         ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                    ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                           ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                               ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                          ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                    ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                            ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                          ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                              ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                         ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                            ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                             ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                         ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                      ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                            ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                             ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                          ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                         ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                           ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                             ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                         ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 146 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        A1BQJ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BQJ 
_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 A1BQJ 1   201 201 A1BQJ LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 1   DMS   DMS A . 
F 3 ZN    1   201 1   ZN    ZN  C . 
G 4 DMS   1   202 1   DMS   DMS C . 
H 5 HOH   1   301 295 HOH   HOH A . 
H 5 HOH   2   302 294 HOH   HOH A . 
H 5 HOH   3   303 183 HOH   HOH A . 
H 5 HOH   4   304 82  HOH   HOH A . 
H 5 HOH   5   305 343 HOH   HOH A . 
H 5 HOH   6   306 204 HOH   HOH A . 
H 5 HOH   7   307 288 HOH   HOH A . 
H 5 HOH   8   308 239 HOH   HOH A . 
H 5 HOH   9   309 211 HOH   HOH A . 
H 5 HOH   10  310 203 HOH   HOH A . 
H 5 HOH   11  311 320 HOH   HOH A . 
H 5 HOH   12  312 179 HOH   HOH A . 
H 5 HOH   13  313 192 HOH   HOH A . 
H 5 HOH   14  314 137 HOH   HOH A . 
H 5 HOH   15  315 86  HOH   HOH A . 
H 5 HOH   16  316 142 HOH   HOH A . 
H 5 HOH   17  317 76  HOH   HOH A . 
H 5 HOH   18  318 95  HOH   HOH A . 
H 5 HOH   19  319 98  HOH   HOH A . 
H 5 HOH   20  320 286 HOH   HOH A . 
H 5 HOH   21  321 331 HOH   HOH A . 
H 5 HOH   22  322 21  HOH   HOH A . 
H 5 HOH   23  323 114 HOH   HOH A . 
H 5 HOH   24  324 241 HOH   HOH A . 
H 5 HOH   25  325 197 HOH   HOH A . 
H 5 HOH   26  326 124 HOH   HOH A . 
H 5 HOH   27  327 20  HOH   HOH A . 
H 5 HOH   28  328 248 HOH   HOH A . 
H 5 HOH   29  329 305 HOH   HOH A . 
H 5 HOH   30  330 235 HOH   HOH A . 
H 5 HOH   31  331 143 HOH   HOH A . 
H 5 HOH   32  332 144 HOH   HOH A . 
H 5 HOH   33  333 327 HOH   HOH A . 
H 5 HOH   34  334 209 HOH   HOH A . 
H 5 HOH   35  335 87  HOH   HOH A . 
H 5 HOH   36  336 257 HOH   HOH A . 
H 5 HOH   37  337 309 HOH   HOH A . 
H 5 HOH   38  338 17  HOH   HOH A . 
H 5 HOH   39  339 9   HOH   HOH A . 
H 5 HOH   40  340 94  HOH   HOH A . 
H 5 HOH   41  341 113 HOH   HOH A . 
H 5 HOH   42  342 90  HOH   HOH A . 
H 5 HOH   43  343 3   HOH   HOH A . 
H 5 HOH   44  344 12  HOH   HOH A . 
H 5 HOH   45  345 101 HOH   HOH A . 
H 5 HOH   46  346 57  HOH   HOH A . 
H 5 HOH   47  347 64  HOH   HOH A . 
H 5 HOH   48  348 296 HOH   HOH A . 
H 5 HOH   49  349 264 HOH   HOH A . 
H 5 HOH   50  350 58  HOH   HOH A . 
H 5 HOH   51  351 190 HOH   HOH A . 
H 5 HOH   52  352 70  HOH   HOH A . 
H 5 HOH   53  353 250 HOH   HOH A . 
H 5 HOH   54  354 207 HOH   HOH A . 
H 5 HOH   55  355 230 HOH   HOH A . 
H 5 HOH   56  356 45  HOH   HOH A . 
H 5 HOH   57  357 37  HOH   HOH A . 
H 5 HOH   58  358 321 HOH   HOH A . 
H 5 HOH   59  359 297 HOH   HOH A . 
H 5 HOH   60  360 128 HOH   HOH A . 
H 5 HOH   61  361 283 HOH   HOH A . 
H 5 HOH   62  362 229 HOH   HOH A . 
H 5 HOH   63  363 316 HOH   HOH A . 
H 5 HOH   64  364 314 HOH   HOH A . 
H 5 HOH   65  365 118 HOH   HOH A . 
H 5 HOH   66  366 263 HOH   HOH A . 
H 5 HOH   67  367 18  HOH   HOH A . 
H 5 HOH   68  368 38  HOH   HOH A . 
H 5 HOH   69  369 56  HOH   HOH A . 
H 5 HOH   70  370 153 HOH   HOH A . 
H 5 HOH   71  371 4   HOH   HOH A . 
H 5 HOH   72  372 212 HOH   HOH A . 
H 5 HOH   73  373 122 HOH   HOH A . 
H 5 HOH   74  374 134 HOH   HOH A . 
H 5 HOH   75  375 252 HOH   HOH A . 
H 5 HOH   76  376 244 HOH   HOH A . 
H 5 HOH   77  377 195 HOH   HOH A . 
H 5 HOH   78  378 157 HOH   HOH A . 
H 5 HOH   79  379 302 HOH   HOH A . 
H 5 HOH   80  380 61  HOH   HOH A . 
H 5 HOH   81  381 43  HOH   HOH A . 
H 5 HOH   82  382 161 HOH   HOH A . 
H 5 HOH   83  383 208 HOH   HOH A . 
H 5 HOH   84  384 104 HOH   HOH A . 
H 5 HOH   85  385 28  HOH   HOH A . 
H 5 HOH   86  386 308 HOH   HOH A . 
H 5 HOH   87  387 167 HOH   HOH A . 
H 5 HOH   88  388 39  HOH   HOH A . 
H 5 HOH   89  389 73  HOH   HOH A . 
H 5 HOH   90  390 265 HOH   HOH A . 
H 5 HOH   91  391 59  HOH   HOH A . 
H 5 HOH   92  392 180 HOH   HOH A . 
H 5 HOH   93  393 32  HOH   HOH A . 
H 5 HOH   94  394 254 HOH   HOH A . 
H 5 HOH   95  395 79  HOH   HOH A . 
H 5 HOH   96  396 173 HOH   HOH A . 
H 5 HOH   97  397 335 HOH   HOH A . 
H 5 HOH   98  398 222 HOH   HOH A . 
H 5 HOH   99  399 24  HOH   HOH A . 
H 5 HOH   100 400 158 HOH   HOH A . 
H 5 HOH   101 401 72  HOH   HOH A . 
H 5 HOH   102 402 228 HOH   HOH A . 
H 5 HOH   103 403 216 HOH   HOH A . 
H 5 HOH   104 404 258 HOH   HOH A . 
H 5 HOH   105 405 62  HOH   HOH A . 
H 5 HOH   106 406 7   HOH   HOH A . 
H 5 HOH   107 407 51  HOH   HOH A . 
H 5 HOH   108 408 172 HOH   HOH A . 
H 5 HOH   109 409 120 HOH   HOH A . 
H 5 HOH   110 410 133 HOH   HOH A . 
H 5 HOH   111 411 27  HOH   HOH A . 
H 5 HOH   112 412 121 HOH   HOH A . 
H 5 HOH   113 413 198 HOH   HOH A . 
H 5 HOH   114 414 284 HOH   HOH A . 
H 5 HOH   115 415 319 HOH   HOH A . 
H 5 HOH   116 416 152 HOH   HOH A . 
H 5 HOH   117 417 71  HOH   HOH A . 
H 5 HOH   118 418 200 HOH   HOH A . 
H 5 HOH   119 419 55  HOH   HOH A . 
H 5 HOH   120 420 92  HOH   HOH A . 
H 5 HOH   121 421 109 HOH   HOH A . 
H 5 HOH   122 422 247 HOH   HOH A . 
H 5 HOH   123 423 251 HOH   HOH A . 
H 5 HOH   124 424 199 HOH   HOH A . 
H 5 HOH   125 425 50  HOH   HOH A . 
H 5 HOH   126 426 165 HOH   HOH A . 
H 5 HOH   127 427 96  HOH   HOH A . 
H 5 HOH   128 428 136 HOH   HOH A . 
H 5 HOH   129 429 307 HOH   HOH A . 
H 5 HOH   130 430 300 HOH   HOH A . 
H 5 HOH   131 431 303 HOH   HOH A . 
H 5 HOH   132 432 42  HOH   HOH A . 
H 5 HOH   133 433 317 HOH   HOH A . 
H 5 HOH   134 434 116 HOH   HOH A . 
H 5 HOH   135 435 10  HOH   HOH A . 
H 5 HOH   136 436 84  HOH   HOH A . 
H 5 HOH   137 437 78  HOH   HOH A . 
H 5 HOH   138 438 301 HOH   HOH A . 
H 5 HOH   139 439 324 HOH   HOH A . 
H 5 HOH   140 440 68  HOH   HOH A . 
H 5 HOH   141 441 313 HOH   HOH A . 
H 5 HOH   142 442 219 HOH   HOH A . 
H 5 HOH   143 443 214 HOH   HOH A . 
H 5 HOH   144 444 220 HOH   HOH A . 
H 5 HOH   145 445 315 HOH   HOH A . 
H 5 HOH   146 446 291 HOH   HOH A . 
H 5 HOH   147 447 282 HOH   HOH A . 
H 5 HOH   148 448 75  HOH   HOH A . 
H 5 HOH   149 449 270 HOH   HOH A . 
H 5 HOH   150 450 289 HOH   HOH A . 
H 5 HOH   151 451 205 HOH   HOH A . 
H 5 HOH   152 452 276 HOH   HOH A . 
H 5 HOH   153 453 334 HOH   HOH A . 
H 5 HOH   154 454 274 HOH   HOH A . 
H 5 HOH   155 455 53  HOH   HOH A . 
H 5 HOH   156 456 339 HOH   HOH A . 
H 5 HOH   157 457 236 HOH   HOH A . 
H 5 HOH   158 458 215 HOH   HOH A . 
H 5 HOH   159 459 253 HOH   HOH A . 
H 5 HOH   160 460 338 HOH   HOH A . 
H 5 HOH   161 461 170 HOH   HOH A . 
H 5 HOH   162 462 271 HOH   HOH A . 
H 5 HOH   163 463 246 HOH   HOH A . 
H 5 HOH   164 464 210 HOH   HOH A . 
H 5 HOH   165 465 106 HOH   HOH A . 
H 5 HOH   166 466 163 HOH   HOH A . 
H 5 HOH   167 467 261 HOH   HOH A . 
H 5 HOH   168 468 238 HOH   HOH A . 
H 5 HOH   169 469 123 HOH   HOH A . 
H 5 HOH   170 470 318 HOH   HOH A . 
H 5 HOH   171 471 189 HOH   HOH A . 
H 5 HOH   172 472 340 HOH   HOH A . 
I 5 HOH   1   301 345 HOH   HOH C . 
I 5 HOH   2   302 217 HOH   HOH C . 
I 5 HOH   3   303 255 HOH   HOH C . 
I 5 HOH   4   304 304 HOH   HOH C . 
I 5 HOH   5   305 285 HOH   HOH C . 
I 5 HOH   6   306 213 HOH   HOH C . 
I 5 HOH   7   307 80  HOH   HOH C . 
I 5 HOH   8   308 91  HOH   HOH C . 
I 5 HOH   9   309 131 HOH   HOH C . 
I 5 HOH   10  310 97  HOH   HOH C . 
I 5 HOH   11  311 311 HOH   HOH C . 
I 5 HOH   12  312 166 HOH   HOH C . 
I 5 HOH   13  313 15  HOH   HOH C . 
I 5 HOH   14  314 47  HOH   HOH C . 
I 5 HOH   15  315 41  HOH   HOH C . 
I 5 HOH   16  316 119 HOH   HOH C . 
I 5 HOH   17  317 35  HOH   HOH C . 
I 5 HOH   18  318 60  HOH   HOH C . 
I 5 HOH   19  319 176 HOH   HOH C . 
I 5 HOH   20  320 77  HOH   HOH C . 
I 5 HOH   21  321 262 HOH   HOH C . 
I 5 HOH   22  322 83  HOH   HOH C . 
I 5 HOH   23  323 132 HOH   HOH C . 
I 5 HOH   24  324 231 HOH   HOH C . 
I 5 HOH   25  325 145 HOH   HOH C . 
I 5 HOH   26  326 221 HOH   HOH C . 
I 5 HOH   27  327 226 HOH   HOH C . 
I 5 HOH   28  328 237 HOH   HOH C . 
I 5 HOH   29  329 69  HOH   HOH C . 
I 5 HOH   30  330 88  HOH   HOH C . 
I 5 HOH   31  331 174 HOH   HOH C . 
I 5 HOH   32  332 13  HOH   HOH C . 
I 5 HOH   33  333 234 HOH   HOH C . 
I 5 HOH   34  334 141 HOH   HOH C . 
I 5 HOH   35  335 2   HOH   HOH C . 
I 5 HOH   36  336 177 HOH   HOH C . 
I 5 HOH   37  337 281 HOH   HOH C . 
I 5 HOH   38  338 151 HOH   HOH C . 
I 5 HOH   39  339 249 HOH   HOH C . 
I 5 HOH   40  340 150 HOH   HOH C . 
I 5 HOH   41  341 19  HOH   HOH C . 
I 5 HOH   42  342 156 HOH   HOH C . 
I 5 HOH   43  343 93  HOH   HOH C . 
I 5 HOH   44  344 159 HOH   HOH C . 
I 5 HOH   45  345 31  HOH   HOH C . 
I 5 HOH   46  346 186 HOH   HOH C . 
I 5 HOH   47  347 140 HOH   HOH C . 
I 5 HOH   48  348 5   HOH   HOH C . 
I 5 HOH   49  349 48  HOH   HOH C . 
I 5 HOH   50  350 310 HOH   HOH C . 
I 5 HOH   51  351 225 HOH   HOH C . 
I 5 HOH   52  352 46  HOH   HOH C . 
I 5 HOH   53  353 188 HOH   HOH C . 
I 5 HOH   54  354 49  HOH   HOH C . 
I 5 HOH   55  355 147 HOH   HOH C . 
I 5 HOH   56  356 322 HOH   HOH C . 
I 5 HOH   57  357 26  HOH   HOH C . 
I 5 HOH   58  358 155 HOH   HOH C . 
I 5 HOH   59  359 99  HOH   HOH C . 
I 5 HOH   60  360 149 HOH   HOH C . 
I 5 HOH   61  361 110 HOH   HOH C . 
I 5 HOH   62  362 115 HOH   HOH C . 
I 5 HOH   63  363 227 HOH   HOH C . 
I 5 HOH   64  364 74  HOH   HOH C . 
I 5 HOH   65  365 66  HOH   HOH C . 
I 5 HOH   66  366 30  HOH   HOH C . 
I 5 HOH   67  367 162 HOH   HOH C . 
I 5 HOH   68  368 175 HOH   HOH C . 
I 5 HOH   69  369 290 HOH   HOH C . 
I 5 HOH   70  370 330 HOH   HOH C . 
I 5 HOH   71  371 16  HOH   HOH C . 
I 5 HOH   72  372 154 HOH   HOH C . 
I 5 HOH   73  373 130 HOH   HOH C . 
I 5 HOH   74  374 184 HOH   HOH C . 
I 5 HOH   75  375 14  HOH   HOH C . 
I 5 HOH   76  376 299 HOH   HOH C . 
I 5 HOH   77  377 194 HOH   HOH C . 
I 5 HOH   78  378 243 HOH   HOH C . 
I 5 HOH   79  379 65  HOH   HOH C . 
I 5 HOH   80  380 34  HOH   HOH C . 
I 5 HOH   81  381 103 HOH   HOH C . 
I 5 HOH   82  382 105 HOH   HOH C . 
I 5 HOH   83  383 25  HOH   HOH C . 
I 5 HOH   84  384 325 HOH   HOH C . 
I 5 HOH   85  385 6   HOH   HOH C . 
I 5 HOH   86  386 224 HOH   HOH C . 
I 5 HOH   87  387 292 HOH   HOH C . 
I 5 HOH   88  388 89  HOH   HOH C . 
I 5 HOH   89  389 223 HOH   HOH C . 
I 5 HOH   90  390 117 HOH   HOH C . 
I 5 HOH   91  391 1   HOH   HOH C . 
I 5 HOH   92  392 171 HOH   HOH C . 
I 5 HOH   93  393 139 HOH   HOH C . 
I 5 HOH   94  394 44  HOH   HOH C . 
I 5 HOH   95  395 127 HOH   HOH C . 
I 5 HOH   96  396 81  HOH   HOH C . 
I 5 HOH   97  397 33  HOH   HOH C . 
I 5 HOH   98  398 202 HOH   HOH C . 
I 5 HOH   99  399 85  HOH   HOH C . 
I 5 HOH   100 400 8   HOH   HOH C . 
I 5 HOH   101 401 287 HOH   HOH C . 
I 5 HOH   102 402 193 HOH   HOH C . 
I 5 HOH   103 403 54  HOH   HOH C . 
I 5 HOH   104 404 178 HOH   HOH C . 
I 5 HOH   105 405 100 HOH   HOH C . 
I 5 HOH   106 406 333 HOH   HOH C . 
I 5 HOH   107 407 277 HOH   HOH C . 
I 5 HOH   108 408 168 HOH   HOH C . 
I 5 HOH   109 409 63  HOH   HOH C . 
I 5 HOH   110 410 22  HOH   HOH C . 
I 5 HOH   111 411 312 HOH   HOH C . 
I 5 HOH   112 412 344 HOH   HOH C . 
I 5 HOH   113 413 245 HOH   HOH C . 
I 5 HOH   114 414 298 HOH   HOH C . 
I 5 HOH   115 415 233 HOH   HOH C . 
I 5 HOH   116 416 232 HOH   HOH C . 
I 5 HOH   117 417 336 HOH   HOH C . 
I 5 HOH   118 418 126 HOH   HOH C . 
I 5 HOH   119 419 67  HOH   HOH C . 
I 5 HOH   120 420 306 HOH   HOH C . 
I 5 HOH   121 421 125 HOH   HOH C . 
I 5 HOH   122 422 148 HOH   HOH C . 
I 5 HOH   123 423 196 HOH   HOH C . 
I 5 HOH   124 424 40  HOH   HOH C . 
I 5 HOH   125 425 102 HOH   HOH C . 
I 5 HOH   126 426 323 HOH   HOH C . 
I 5 HOH   127 427 326 HOH   HOH C . 
I 5 HOH   128 428 129 HOH   HOH C . 
I 5 HOH   129 429 293 HOH   HOH C . 
I 5 HOH   130 430 36  HOH   HOH C . 
I 5 HOH   131 431 29  HOH   HOH C . 
I 5 HOH   132 432 52  HOH   HOH C . 
I 5 HOH   133 433 23  HOH   HOH C . 
I 5 HOH   134 434 191 HOH   HOH C . 
I 5 HOH   135 435 164 HOH   HOH C . 
I 5 HOH   136 436 269 HOH   HOH C . 
I 5 HOH   137 437 111 HOH   HOH C . 
I 5 HOH   138 438 146 HOH   HOH C . 
I 5 HOH   139 439 11  HOH   HOH C . 
I 5 HOH   140 440 181 HOH   HOH C . 
I 5 HOH   141 441 160 HOH   HOH C . 
I 5 HOH   142 442 329 HOH   HOH C . 
I 5 HOH   143 443 273 HOH   HOH C . 
I 5 HOH   144 444 242 HOH   HOH C . 
I 5 HOH   145 445 138 HOH   HOH C . 
I 5 HOH   146 446 278 HOH   HOH C . 
I 5 HOH   147 447 256 HOH   HOH C . 
I 5 HOH   148 448 267 HOH   HOH C . 
I 5 HOH   149 449 185 HOH   HOH C . 
I 5 HOH   150 450 341 HOH   HOH C . 
I 5 HOH   151 451 328 HOH   HOH C . 
I 5 HOH   152 452 182 HOH   HOH C . 
I 5 HOH   153 453 112 HOH   HOH C . 
I 5 HOH   154 454 280 HOH   HOH C . 
I 5 HOH   155 455 279 HOH   HOH C . 
I 5 HOH   156 456 272 HOH   HOH C . 
I 5 HOH   157 457 342 HOH   HOH C . 
I 5 HOH   158 458 218 HOH   HOH C . 
I 5 HOH   159 459 260 HOH   HOH C . 
I 5 HOH   160 460 187 HOH   HOH C . 
I 5 HOH   161 461 107 HOH   HOH C . 
I 5 HOH   162 462 337 HOH   HOH C . 
I 5 HOH   163 463 266 HOH   HOH C . 
I 5 HOH   164 464 169 HOH   HOH C . 
I 5 HOH   165 465 240 HOH   HOH C . 
I 5 HOH   166 466 259 HOH   HOH C . 
I 5 HOH   167 467 206 HOH   HOH C . 
I 5 HOH   168 468 201 HOH   HOH C . 
I 5 HOH   169 469 135 HOH   HOH C . 
I 5 HOH   170 470 275 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           7HWL 
_cell.length_a           86.652 
_cell.length_b           57.209 
_cell.length_c           64.740 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.91 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HWL 
_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          7HWL 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.51 
_exptl_crystal.density_percent_sol   51.09 
_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   2024-11-22 
_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                     7HWL 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.69 
_reflns.d_resolution_high            1.31 
_reflns.number_obs                   70008 
_reflns.percent_possible_obs         91.7 
_reflns.pdbx_Rmerge_I_obs            0.059 
_reflns.pdbx_netI_over_sigmaI        13.6 
_reflns.pdbx_redundancy              3.9 
_reflns.pdbx_Rrim_I_all              0.067 
_reflns.pdbx_Rpim_I_all              0.032 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     274115 
_reflns.pdbx_chi_squared             0.89 
_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                  1.31 
_reflns_shell.d_res_low                   1.38 
_reflns_shell.number_measured_all         16748 
_reflns_shell.number_unique_obs           6651 
_reflns_shell.Rmerge_I_obs                0.665 
_reflns_shell.pdbx_chi_squared            0.73 
_reflns_shell.pdbx_redundancy             2.5 
_reflns_shell.percent_possible_obs        60.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   2.1 
_reflns_shell.pdbx_Rrim_I_all             0.838 
_reflns_shell.pdbx_Rpim_I_all             0.498 
_reflns_shell.pdbx_CC_half                0.541 
_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                                 7HWL 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     69693 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             47.69 
_refine.ls_d_res_high                            1.306 
_refine.ls_percent_reflns_obs                    91.1 
_refine.ls_R_factor_obs                          0.1768 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1761 
_refine.ls_R_factor_R_free                       0.1892 
_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                  3477 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.944 
_refine.correlation_coeff_Fo_to_Fc_free          0.957 
_refine.B_iso_mean                               16.85 
_refine.aniso_B[1][1]                            -1.84340 
_refine.aniso_B[2][2]                            0.14170 
_refine.aniso_B[3][3]                            1.70170 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.02770 
_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             0.049 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.049 
_refine.pdbx_overall_SU_R_Blow_DPI               0.052 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.051 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HWL 
_refine_analyze.Luzzati_coordinate_error_obs    0.16 
_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        2157 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             342 
_refine_hist.number_atoms_total               2528 
_refine_hist.d_res_high                       1.306 
_refine_hist.d_res_low                        47.69 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.012 ? 2.00  2256 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.06  ? 2.00  3074 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  755  '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  403  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2256 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.89  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.02 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  279  '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  2039 '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                       1.31 
_refine_ls_shell.d_res_low                        1.32 
_refine_ls_shell.number_reflns_R_work             1316 
_refine_ls_shell.R_factor_R_work                  0.2450 
_refine_ls_shell.percent_reflns_obs               46.51 
_refine_ls_shell.R_factor_R_free                  0.2824 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.60 
_refine_ls_shell.number_reflns_R_free             78 
_refine_ls_shell.number_reflns_all                1394 
_refine_ls_shell.R_factor_all                     0.2469 
# 
_struct.entry_id                  7HWL 
_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-0034398-001 (A71EV2A-x3956)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HWL 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I 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 7HWL A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HWL C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,H 
2 1 B,F,G,I   
# 
_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 ? ? ? ? ? ? ? 2.352 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.233 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
# 
_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_555 110.0 ? 
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_555 104.8 ? 
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_555 106.3 ? 
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_555 101.3 ? 
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_555 118.1 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 110.0 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.4 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.1 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 106.4 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.8 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.7 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 26  ? N VAL A 32  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7HWL 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 347 ? ? O A HOH 439 ? ? 1.52 
2 1 O A HOH 364 ? ? O C HOH 464 ? ? 1.86 
3 1 O C HOH 375 ? ? O C HOH 406 ? ? 1.90 
4 1 O A HOH 415 ? ? O A HOH 454 ? ? 1.90 
5 1 O C HOH 322 ? ? O C HOH 414 ? ? 1.98 
6 1 O A HOH 402 ? ? O A HOH 415 ? ? 2.11 
7 1 O C HOH 327 ? ? O C HOH 384 ? ? 2.14 
8 1 O A HOH 429 ? ? O A HOH 471 ? ? 2.17 
# 
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 14.7612 8.2047   14.4530 -0.0164 -0.0192 -0.0047 0.0084 -0.0009 0.0046 1.0710 0.5849 0.5656 0.5009 
-0.4201 -0.1994 -0.0118 0.0417 0.0817 0.0204 0.0477 0.0025 -0.0032 -0.0539 -0.0360 
'X-RAY DIFFRACTION' 2 ? refined 25.8032 -20.2099 17.7371 -0.0195 -0.0170 0.0088  0.0045 -0.0004 0.0100 0.5170 0.8028 0.2423 
-0.0696 -0.1593 -0.0921 0.0128  0.0105 0.0959 0.0155 0.0250 0.0301 0.0290  0.0149  -0.0378 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
6 1 Y 1 C ALA 147 ? B ALA 141 
7 1 Y 1 C MET 148 ? B MET 142 
8 1 Y 1 C GLU 149 ? B GLU 143 
9 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 
A1BQJ N1   N  N N 1   
A1BQJ C4   C  Y N 2   
A1BQJ C5   C  Y N 3   
A1BQJ C6   C  Y N 4   
A1BQJ C7   C  N N 5   
A1BQJ C8   C  N N 6   
A1BQJ C10  C  N S 7   
A1BQJ C13  C  N N 8   
A1BQJ O2   O  N N 9   
A1BQJ C12  C  N N 10  
A1BQJ C11  C  N N 11  
A1BQJ O1   O  N N 12  
A1BQJ C9   C  N N 13  
A1BQJ N    N  N N 14  
A1BQJ C1   C  Y N 15  
A1BQJ O    O  N N 16  
A1BQJ C    C  N N 17  
A1BQJ C3   C  Y N 18  
A1BQJ C2   C  Y N 19  
A1BQJ H15  H  N N 20  
A1BQJ H14  H  N N 21  
A1BQJ H6   H  N N 22  
A1BQJ H7   H  N N 23  
A1BQJ H8   H  N N 24  
A1BQJ H9   H  N N 25  
A1BQJ H11  H  N N 26  
A1BQJ H10  H  N N 27  
A1BQJ H    H  N N 28  
A1BQJ H16  H  N N 29  
A1BQJ H17  H  N N 30  
A1BQJ H13  H  N N 31  
A1BQJ H12  H  N N 32  
A1BQJ H2   H  N N 33  
A1BQJ H1   H  N N 34  
A1BQJ H3   H  N N 35  
A1BQJ H5   H  N N 36  
A1BQJ H4   H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BQJ C   O    sing N N 1   
A1BQJ O   C1   sing N N 2   
A1BQJ C1  C2   doub Y N 3   
A1BQJ C2  C3   sing Y N 4   
A1BQJ C3  C4   doub Y N 5   
A1BQJ C4  C5   sing Y N 6   
A1BQJ C5  C6   doub Y N 7   
A1BQJ C1  C6   sing Y N 8   
A1BQJ C6  C7   sing N N 9   
A1BQJ C7  C8   sing N N 10  
A1BQJ C8  N    sing N N 11  
A1BQJ N   C9   sing N N 12  
A1BQJ C9  C10  sing N N 13  
A1BQJ C11 C10  sing N N 14  
A1BQJ N1  C11  sing N N 15  
A1BQJ O1  C11  doub N N 16  
A1BQJ C10 C12  sing N N 17  
A1BQJ C12 C13  sing N N 18  
A1BQJ N   C13  sing N N 19  
A1BQJ C13 O2   doub N N 20  
A1BQJ N1  H15  sing N N 21  
A1BQJ N1  H14  sing N N 22  
A1BQJ C4  H6   sing N N 23  
A1BQJ C5  H7   sing N N 24  
A1BQJ C7  H8   sing N N 25  
A1BQJ C7  H9   sing N N 26  
A1BQJ C8  H11  sing N N 27  
A1BQJ C8  H10  sing N N 28  
A1BQJ C10 H    sing N N 29  
A1BQJ C12 H16  sing N N 30  
A1BQJ C12 H17  sing N N 31  
A1BQJ C9  H13  sing N N 32  
A1BQJ C9  H12  sing N N 33  
A1BQJ C   H2   sing N N 34  
A1BQJ C   H1   sing N N 35  
A1BQJ C   H3   sing N N 36  
A1BQJ C3  H5   sing N N 37  
A1BQJ C2  H4   sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HWL 
_atom_sites.fract_transf_matrix[1][1]   0.011540 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000991 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017480 
_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]   0.015503 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.471 8.217   24.735 1.00 12.92 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.733 8.290   23.968 1.00 13.43 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 18.876 7.078   23.069 1.00 12.64 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.153 6.078   23.233 1.00 13.82 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 19.920 8.384   24.934 1.00 16.17 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.037 7.190   25.683 1.00 18.49 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.796 7.144   22.117 1.00 11.77 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.063 6.022   21.221 1.00 10.72 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.523 6.480   19.852 1.00 10.74 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.248 7.609   19.443 1.00 12.16 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.213 5.603   19.150 1.00 9.78  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.726 5.937   17.809 1.00 10.09 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.723 4.719   16.916 1.00 9.84  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.611 3.571   17.390 1.00 11.07 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.160 6.472   17.941 1.00 11.05 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.791 4.954   15.595 1.00 9.63  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.027 3.888   14.615 1.00 9.15  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.499 3.988   14.225 1.00 10.08 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 23.999 5.102   13.937 1.00 10.11 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.169 4.091   13.350 1.00 9.81  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.672 4.268   13.662 1.00 11.23 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.398 2.926   12.379 1.00 11.35 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.888 4.796   12.449 1.00 11.12 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.218 2.843   14.201 1.00 9.98  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.636 2.830   13.817 1.00 11.22 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.743 1.998   12.536 1.00 10.92 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.721 0.750   12.599 1.00 11.45 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.499 2.244   14.952 1.00 12.20 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.525 3.148   16.161 1.00 10.99 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.379 4.249   16.218 1.00 11.89 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.679 2.924   17.245 1.00 12.45 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.390 5.100   17.319 1.00 12.58 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.696 3.764   18.359 1.00 13.32 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.535 4.865   18.371 1.00 13.41 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.546 5.730   19.459 1.00 15.50 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.830 2.668   11.384 1.00 11.54 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.912 2.005   10.090 1.00 11.50 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.158 2.494   9.386  1.00 12.80 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.392 3.715   9.330  1.00 11.43 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.630 2.261   9.227  1.00 13.05 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.264 3.758   9.143  1.00 14.45 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.794 1.648   7.843  1.00 15.04 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.035 1.589   8.920  1.00 14.10 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.268 2.026   8.261  1.00 13.42 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.093 2.916   9.177  1.00 13.04 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.181 2.617   10.378 1.00 13.25 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.544 4.075   8.672  1.00 12.28 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.238 5.052   9.514  1.00 12.46 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.320 6.254   9.832  1.00 12.05 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.803 7.391   9.964  1.00 12.44 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.575 5.500   8.912  1.00 13.63 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.648 4.443   9.043  1.00 17.69 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.392 4.369   10.036 1.00 20.05 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.682 3.556   8.090  1.00 16.61 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.017 5.980   10.050 1.00 10.91 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.050 7.008   10.408 1.00 10.52 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.363 6.659   11.732 1.00 10.09 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.102 5.471   12.049 1.00 10.65 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.966 7.067   9.324  1.00 11.97 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.487 7.475   7.963  1.00 12.67 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.147 8.682   7.778  1.00 13.37 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.312 6.656   6.863  1.00 14.99 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.600 9.081   6.517  1.00 14.45 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.744 7.052   5.598  1.00 15.96 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.388 8.263   5.434  1.00 16.66 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.835 8.691   4.194  1.00 20.32 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.037 7.707   12.490 1.00 9.92  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.222 7.653   13.710 1.00 9.87  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 24.997 8.528   13.446 1.00 9.48  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.152 9.741   13.161 1.00 9.92  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.033 8.207   14.909 1.00 9.95  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.225 8.525   16.164 1.00 10.14 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.171 8.905   17.337 1.00 11.48 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.607 9.968   18.179 1.00 12.84 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.928 9.766   19.307 1.00 14.74 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.685 8.531   19.729 1.00 15.44 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.454 10.802  20.004 1.00 13.73 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.797 7.911   13.497 1.00 9.03  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.532 8.644   13.235 1.00 8.81  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.831 8.847   14.558 1.00 9.04  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.514 7.848   15.255 1.00 9.73  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.590 7.853   12.298 1.00 9.48  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.371 8.699   11.920 1.00 10.56 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.297 7.332   11.038 1.00 10.90 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.578 10.111  14.920 1.00 8.33  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 20.930 10.444  16.195 1.00 9.62  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 19.804 11.427  15.979 1.00 9.20  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.677 12.057  14.898 1.00 10.62 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 21.966 11.074  17.189 1.00 11.74 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 22.972 10.028  17.639 1.00 15.00 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.649 12.342  16.624 1.00 11.46 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 18.961 11.618  17.024 1.00 9.55  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 17.968 12.705  16.959 1.00 9.36  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 18.750 14.024  16.967 1.00 10.45 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 19.675 14.189  17.782 1.00 10.37 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.089 12.696  18.224 1.00 9.18  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.225 11.468  18.313 1.00 9.55  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 16.626 10.480  18.949 1.00 11.24 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.065 11.470  17.652 1.00 11.04 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.398 14.961  16.076 1.00 9.63  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.152 16.245  16.053 1.00 10.12 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.085 16.918  17.419 1.00 11.74 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.079 17.462  17.870 1.00 12.24 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.546 17.167  14.982 1.00 10.71 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.345 18.460  14.731 1.00 11.02 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.605 19.329  13.733 1.00 11.57 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.362 20.523  13.284 1.00 13.37 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.358 21.683  13.933 1.00 15.72 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.768 21.786  15.121 1.00 15.42 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.957 22.753  13.402 1.00 16.53 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 17.915 16.820  18.105 1.00 10.65 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 17.778 17.515  19.386 1.00 11.69 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 18.620 16.901  20.516 1.00 12.77 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 18.775 17.547  21.561 1.00 13.86 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.286 17.674  19.782 1.00 13.07 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 15.614 16.425  20.281 1.00 11.46 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 14.970 15.559  19.408 1.00 12.31 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 15.402 15.985  21.547 1.00 12.51 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 14.465 14.574  20.160 1.00 12.21 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 14.659 14.807  21.453 1.00 13.08 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.153 15.680  20.317 1.00 12.07 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.024 15.011  21.294 1.00 11.66 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 21.497 14.951  20.867 1.00 13.30 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 22.325 14.336  21.544 1.00 14.42 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 19.513 13.604  21.603 1.00 12.06 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.096 13.603  22.174 1.00 13.04 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 17.635 12.185  22.438 1.00 12.96 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.012 14.397  23.498 1.00 15.41 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 21.840 15.587  19.716 1.00 12.43 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.234 15.541  19.259 1.00 12.55 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.190 16.175  20.262 1.00 13.92 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 23.888 17.219  20.861 1.00 14.78 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.362 16.245  17.905 1.00 12.22 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.372 15.576  20.410 1.00 13.58 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 26.417 16.096  21.322 1.00 13.95 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.334 17.101  20.600 1.00 14.00 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.282 17.243  19.355 1.00 13.41 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.285 14.921  21.833 1.00 15.95 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.052 14.398  20.732 1.00 15.82 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 26.462 13.810  22.480 1.00 16.62 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.255 17.775  21.346 1.00 14.70 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.236 18.634  20.718 1.00 14.67 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.113 17.834  19.768 1.00 13.87 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.393 18.317  18.666 1.00 14.18 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.144 19.316  21.776 1.00 16.00 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.396 19.976  21.189 1.00 25.12 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 31.341 21.188  20.527 1.00 29.85 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 32.662 19.489  21.082 1.00 29.00 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 32.574 21.463  20.141 1.00 30.75 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 33.410 20.456  20.421 1.00 31.67 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.508 16.592  20.155 1.00 13.25 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.336 15.797  19.257 1.00 13.74 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.582 15.489  17.953 1.00 12.46 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.205 15.501  16.888 1.00 12.71 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 31.794 14.483  19.903 1.00 16.30 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 32.794 13.768  19.025 1.00 24.84 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 33.947 14.233  18.865 1.00 28.34 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.356 12.674  18.369 1.00 27.40 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.244 15.257  18.019 1.00 11.52 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.467 15.058  16.792 1.00 11.45 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.553 16.313  15.874 1.00 10.94 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.804 16.182  14.671 1.00 11.32 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.010 14.787  17.119 1.00 11.64 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 26.745 13.426  17.706 1.00 12.77 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.406 12.452  17.271 1.00 12.44 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 25.888 13.338  18.609 1.00 12.82 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.351 17.517  16.446 1.00 10.70 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.406 18.752  15.664 1.00 11.03 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.811 19.013  15.112 1.00 11.80 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.927 19.575  14.009 1.00 12.83 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.921 19.950  16.522 1.00 11.66 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.419 20.024  16.630 1.00 11.78 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.645 19.685  17.700 1.00 13.51 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.518 20.510  15.625 1.00 12.19 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.317 19.936  17.432 1.00 13.20 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.206 20.401  16.138 1.00 12.56 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.696 20.962  14.308 1.00 13.83 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.082 20.811  15.400 1.00 14.13 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.589 21.284  13.559 1.00 14.24 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.313 21.265  14.110 1.00 14.90 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.864 18.616  15.855 1.00 11.25 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.230 18.836  15.410 1.00 12.44 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.673 17.827  14.329 1.00 13.31 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.737 17.986  13.728 1.00 14.75 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.158 18.775  16.624 1.00 14.64 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.876 16.751  14.115 1.00 12.38 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.176 15.702  13.113 1.00 12.25 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.938 15.525  12.227 1.00 11.88 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.559 14.403  11.880 1.00 11.95 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.544 14.373  13.854 1.00 13.21 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.898 14.551  14.522 1.00 15.89 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.948 14.481  13.863 1.00 18.66 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.912 14.826  15.835 1.00 17.03 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.286 16.616  11.876 1.00 12.10 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.994 16.576  11.207 1.00 11.33 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 29.063 16.124  9.778  1.00 12.24 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.913 16.601  9.016  1.00 13.43 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.394 18.010  11.250 1.00 11.14 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.999 18.166  10.652 1.00 11.90 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.943 17.400  11.472 1.00 12.30 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.584 19.648  10.604 1.00 14.24 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 28.131 15.251  9.371  1.00 11.08 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.996 14.849  7.972  1.00 11.84 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.751 15.552  7.382  1.00 12.22 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.803 16.089  6.276  1.00 13.92 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.870 13.311  7.880  1.00 11.40 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.477 12.895  6.448  1.00 13.39 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 29.176 12.629  8.331  1.00 12.58 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.607 15.505  8.102  1.00 10.79 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 24.354 16.043  7.584  1.00 11.52 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.374 16.277  8.719  1.00 12.07 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.389 15.493  9.672  1.00 11.73 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.738 15.042  6.564  1.00 13.09 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 22.327 15.305  6.093  1.00 14.00 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.928 16.183  5.118  1.00 16.41 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 21.123 14.677  6.585  1.00 13.24 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 20.556 16.119  4.963  1.00 17.46 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 20.042 15.184  5.837  1.00 15.50 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.861 13.726  7.574  1.00 13.93 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.716 14.733  6.029  1.00 16.05 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.562 13.268  7.745  1.00 14.30 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.500 13.793  7.003  1.00 15.21 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.535 17.310  8.635  1.00 13.02 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.513 17.514  9.644  1.00 12.36 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.290 18.142  9.009  1.00 13.58 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 20.407 18.942  8.065  1.00 14.21 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 22.004 18.351  10.821 1.00 13.69 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.615 19.710  10.437 1.00 14.74 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.653 20.884  10.221 1.00 15.26 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.983 21.836  9.466  1.00 17.63 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.555 20.881  10.822 1.00 14.27 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 19.111 17.848  9.548  1.00 12.32 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.863 18.399  9.024  1.00 12.39 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.890 18.562  10.179 1.00 12.58 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.352 17.573  10.714 1.00 12.39 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 17.304 17.479  7.918  1.00 14.50 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 16.053 17.974  7.236  1.00 17.25 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.212 18.549  7.914  1.00 20.79 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.891 17.718  6.028  1.00 20.26 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.662 19.834  10.578 1.00 12.71 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.761 20.150  11.672 0.50 12.68 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.770 20.091  11.697 0.50 13.64 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.320 19.692  11.385 1.00 13.70 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.624 19.189  12.298 1.00 14.12 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.804 21.656  11.925 0.50 13.44 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.876 21.550  12.137 0.50 17.27 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.853 22.055  12.891 0.50 14.74 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.566 22.394  11.046 0.50 22.87 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.862 19.836  10.127 1.00 13.74 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.488 19.425  9.795  1.00 14.25 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.249 17.928  9.961  1.00 13.50 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.108 17.524  10.117 1.00 14.48 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 12.104 19.847  8.377  1.00 15.92 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.697 19.041  7.371  1.00 21.45 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.305 17.107  9.955  1.00 11.82 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.199 15.657  10.160 1.00 11.81 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.648 15.211  11.584 1.00 11.03 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.561 14.013  11.914 1.00 10.68 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.092 14.930  9.130  1.00 12.35 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.582 15.086  7.688  1.00 13.48 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.470 14.398  6.668  1.00 13.11 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.371 12.940  6.824  1.00 11.58 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.499 12.068  5.836  1.00 13.08 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.742 12.489  4.588  1.00 14.79 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.385 10.758  6.077  1.00 12.85 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.208 16.145  12.407 1.00 10.45 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.819 15.805  13.697 1.00 9.75  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 15.965 14.792  13.564 1.00 9.82  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.176 13.960  14.453 1.00 10.29 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.790 15.307  14.749 1.00 11.09 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.370 15.086  16.139 1.00 10.98 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.199 15.919  16.595 1.00 12.20 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.017 14.064  16.787 1.00 12.15 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.761 14.908  12.468 1.00 9.81  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.878 13.966  12.303 1.00 9.24  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.233 14.677  12.188 1.00 9.16  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.314 15.799  11.623 1.00 10.19 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.677 13.158  11.027 1.00 9.35  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.594 12.027  11.056 1.00 10.97 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.543 11.301  9.721  1.00 12.43 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.863 11.025  12.192 1.00 11.81 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.286 14.015  12.671 1.00 8.99  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.658 14.471  12.500 1.00 9.21  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.520 13.239  12.356 1.00 9.59  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.325 12.215  13.062 1.00 10.16 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.095 15.333  13.692 1.00 10.01 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.547 15.896  13.642 1.00 10.19 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.646 17.264  14.330 1.00 11.35 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.570 14.962  14.280 1.00 11.58 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.501 13.318  11.447 1.00 9.96  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.444 12.230  11.188 1.00 8.90  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.853 12.739  11.354 1.00 9.36  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.192 13.798  10.791 1.00 10.19 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.233 11.624  9.776  1.00 9.13  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.262 10.521  9.508  1.00 11.39 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.786 11.093  9.635  1.00 10.90 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.663 12.043  12.164 1.00 9.25  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.074 12.391  12.368 1.00 9.41  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.951 11.224  11.909 1.00 10.52 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.478 10.083  11.698 1.00 11.02 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.350 12.751  13.832 1.00 11.13 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.005 11.689  14.711 1.00 11.62 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.246 11.499  11.730 1.00 11.18 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.195 10.466  11.305 1.00 12.50 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.823 9.742   12.514 1.00 14.20 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.987 10.345  13.589 1.00 15.91 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.276 11.088  10.427 1.00 14.77 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.969 12.068  11.181 1.00 17.49 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.163 8.446   12.334 1.00 14.14 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.729 7.631   13.411 1.00 15.32 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.074 7.040   12.978 1.00 17.60 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.308 6.820   11.775 1.00 17.28 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 31.805 6.443   13.783 1.00 16.47 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.685 5.538   12.678 1.00 17.52 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.400 6.899   14.198 1.00 16.69 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 34.934 6.744   13.954 1.00 18.67 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.216 6.120   13.646 1.00 20.49 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.011 4.606   13.421 1.00 20.43 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.535 4.044   12.448 1.00 22.67 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.222 6.421   14.763 1.00 24.99 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 36.681 5.957   15.986 1.00 29.52 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.486 7.906   14.900 1.00 25.52 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.194 3.978   14.263 1.00 20.13 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 34.918 2.541   14.132 1.00 21.42 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 33.694 2.258   13.258 1.00 20.50 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 32.750 3.054   13.240 1.00 19.48 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 34.688 1.930   15.507 1.00 23.78 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 33.679 1.118   12.571 1.00 19.10 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 32.565 0.688   11.737 1.00 18.87 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.457 0.110   12.590 1.00 18.53 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 31.722 -0.609  13.563 1.00 20.27 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.022 -0.346  10.696 1.00 21.20 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.826 0.274   9.544  1.00 26.52 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 34.243 -0.767  8.538  1.00 32.89 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 35.101 -1.613  8.809  1.00 32.74 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 33.634 -0.732  7.357  1.00 35.71 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.216 0.449   12.243 1.00 15.22 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.036 -0.037  12.951 1.00 14.06 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.465 -1.306  12.364 1.00 13.48 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 28.791 -1.685  11.235 1.00 14.89 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 27.529 -1.920  13.129 1.00 13.44 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 26.924 -3.209  12.750 1.00 14.09 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 25.480 -3.151  12.317 1.00 13.93 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 24.935 -4.202  11.932 1.00 14.91 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 27.085 -4.201  13.899 1.00 14.97 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 28.796 -4.665  14.227 1.00 19.15 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 24.824 -1.999  12.419 1.00 11.78 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.434 -1.906  11.985 1.00 11.78 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.354 -1.853  10.457 1.00 13.65 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.229 -1.279  9.803  1.00 15.25 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 22.780 -0.656  12.589 1.00 11.40 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 22.663 -0.699  14.109 1.00 12.87 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 22.321 -1.798  14.654 1.00 13.33 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 22.851 0.366   14.758 1.00 13.23 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.315 -2.433  9.900  1.00 14.41 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.038 -2.361  8.449  1.00 14.93 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.708 -1.621  8.290  1.00 14.05 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.787 -1.792  9.100  1.00 15.64 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.924 -3.747  7.840  1.00 19.19 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 20.894 -4.418  8.535  1.00 23.89 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 23.247 -4.542  7.993  1.00 20.63 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.601 -0.779  7.246  1.00 13.69 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.387 -0.024  7.026  1.00 12.83 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.436 -0.817  6.128  1.00 12.79 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.835 -1.340  5.044  1.00 13.40 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.724 1.343   6.381  1.00 12.74 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.815 2.106   7.163  1.00 13.89 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.457 2.206   6.224  1.00 13.19 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.399 2.445   8.639  1.00 14.48 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.173 -0.849  6.507  1.00 11.36 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.116 -1.466  5.704  1.00 11.85 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.881 -0.619  4.430  1.00 13.13 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.880 0.635   4.471  1.00 12.89 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.819 -1.491  6.505  1.00 11.75 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.642 -1.303  3.301  1.00 14.74 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 15.332 -0.624  2.048  1.00 14.80 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 14.061 -1.342  1.559  1.00 17.31 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 14.130 -2.283  0.759  1.00 18.40 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 16.529 -0.735  1.048  1.00 15.05 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.863 -0.156  1.552  1.00 14.90 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.835 1.359   1.832  1.00 14.15 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 19.155 1.840   2.304  1.00 13.20 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 19.342 2.989   2.941  1.00 14.55 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.343 3.857   3.071  1.00 14.64 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.550 3.320   3.395  1.00 17.35 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.922 -0.863  2.019  1.00 16.82 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.625 -1.536  1.882  1.00 17.94 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.457 -0.579  2.123  1.00 19.23 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.625 0.578   2.487  1.00 20.86 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.580 -2.671  2.903  1.00 17.34 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.510 -2.070  4.609  1.00 16.11 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 9.199  -1.149  2.031  1.00 21.76 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 8.010  -0.376  2.349  1.00 23.95 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 7.219  -1.072  3.489  1.00 22.13 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.987  -0.996  3.531  1.00 23.00 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 7.097  -0.180  1.118  1.00 31.28 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 6.540  -1.458  0.527  1.00 40.51 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.960  -2.558  0.968  1.00 41.77 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 5.682  -1.366  -0.386 1.00 45.91 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.922  -1.719  4.430  1.00 18.87 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.241  -2.324  5.595  1.00 16.75 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.467  -1.262  6.381  1.00 16.99 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.904  -0.108  6.526  1.00 17.52 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.249  -3.039  6.501  1.00 16.54 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.947  -4.596  5.851  1.00 17.96 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.306  -1.644  6.894  1.00 14.93 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.512  -0.847  7.824  1.00 14.55 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.262  -1.596  9.143  1.00 12.89 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.392  -1.212  9.922  1.00 13.87 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.175  -0.372  7.245  1.00 17.49 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.261  0.753   6.243  1.00 21.25 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.848  1.222   5.876  1.00 26.03 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.360  1.014   4.755  1.00 28.16 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.135  1.921   6.768  1.00 21.86 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 4.994  -2.704  9.374  1.00 11.48 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 4.990  -3.411  10.643 1.00 11.94 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.460  -3.661  11.057 1.00 11.42 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.339  -3.860  10.197 1.00 13.22 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.213  -4.707  10.632 1.00 15.35 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 4.846  -5.590  9.728  1.00 21.14 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 2.792  -4.518  10.210 1.00 15.40 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 6.705  -3.578  12.342 1.00 9.96  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.062  -3.781  12.842 1.00 10.35 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.079  -3.811  14.349 1.00 9.80  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.045  -4.046  14.968 1.00 10.57 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 9.261  -3.606  14.961 1.00 9.18  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 9.417  -3.681  16.406 1.00 8.41  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 10.247 -2.484  16.825 1.00 9.11  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 11.247 -2.184  16.161 1.00 9.98  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 10.147 -5.017  16.734 1.00 10.04 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 10.541 -5.085  18.202 1.00 12.20 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 9.231  -6.205  16.394 1.00 10.53 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 9.874  -1.807  17.924 1.00 8.86  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 10.714 -0.706  18.423 1.00 7.81  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 11.145 -0.928  19.858 1.00 8.78  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 10.448 -1.580  20.634 1.00 9.58  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 10.046 0.694   18.280 1.00 8.68  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 9.024  1.050   19.344 1.00 8.72  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 7.750  0.493   19.327 1.00 9.79  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 9.327  1.949   20.365 1.00 8.95  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 6.807  0.802   20.308 1.00 11.16 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 8.379  2.267   21.348 1.00 9.73  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 7.130  1.685   21.308 1.00 11.00 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 6.165  1.960   22.274 1.00 13.31 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 12.290 -0.307  20.227 1.00 8.58  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 12.761 -0.337  21.611 1.00 8.75  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 12.255 0.861   22.395 1.00 8.24  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 12.465 2.015   22.012 1.00 8.67  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 14.313 -0.393  21.669 1.00 9.40  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 14.770 -0.535  23.099 1.00 9.80  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 14.433 -1.645  23.838 1.00 9.69  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 15.502 0.477   23.728 1.00 10.36 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 14.794 -1.752  25.175 1.00 11.94 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 15.868 0.384   25.063 1.00 10.77 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 15.565 -0.762  25.760 1.00 11.58 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 15.899 -0.893  27.104 1.00 14.85 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 11.647 0.553   23.536 1.00 8.32  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 11.083 1.544   24.480 1.00 8.82  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 11.894 1.543   25.782 1.00 9.28  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 11.704 0.642   26.636 1.00 9.55  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 9.622  1.216   24.736 1.00 9.65  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 8.833  2.304   25.956 1.00 10.92 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 12.820 2.510   25.939 1.00 9.74  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 13.681 2.529   27.139 1.00 10.53 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 12.928 2.707   28.468 1.00 10.50 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 13.314 2.135   29.476 1.00 11.65 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 14.780 3.583   27.014 1.00 12.32 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 14.297 4.914   27.108 1.00 13.62 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 11.777 3.417   28.427 1.00 9.55  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 10.969 3.644   29.609 1.00 9.26  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 10.164 2.416   30.064 1.00 9.84  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 9.503  2.446   31.103 1.00 10.44 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 10.037 4.844   29.397 1.00 9.67  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 9.027  4.616   28.436 1.00 10.92 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 10.262 1.302   29.299 1.00 9.98  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 9.704  0.001   29.683 1.00 10.30 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 10.765 -1.109  29.635 1.00 11.94 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 10.439 -2.279  29.918 1.00 12.21 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 8.524  -0.362  28.759 1.00 10.63 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 7.347  0.593   28.895 1.00 11.48 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 6.588  0.276   30.163 1.00 11.18 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 5.431  1.164   30.304 1.00 13.33 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 5.442  2.316   30.967 1.00 12.54 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 6.568  2.767   31.522 1.00 13.56 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 4.325  3.039   31.082 1.00 13.55 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 11.997 -0.815  29.203 1.00 12.15 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 13.015 -1.857  28.945 1.00 13.56 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 12.442 -2.997  28.068 1.00 15.69 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 12.661 -4.196  28.355 1.00 17.02 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 13.548 -2.439  30.246 1.00 17.28 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 14.598 -1.610  30.762 1.00 18.84 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 15.374 -2.481  31.751 1.00 19.96 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.124 -1.543  32.550 1.00 19.16 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 15.772 -1.134  33.760 1.00 15.45 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 14.711 -1.664  34.370 1.00 16.20 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.492 -0.221  34.386 1.00 17.58 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 11.693 -2.647  27.033 1.00 13.17 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 11.020 -3.653  26.236 1.00 13.76 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 10.950 -3.271  24.782 1.00 12.32 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 10.880 -2.078  24.429 1.00 12.01 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 9.564  -3.771  26.739 1.00 17.58 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 9.406  -4.768  27.902 1.00 26.36 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 7.941  -5.037  28.236 1.00 35.28 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 7.801  -5.931  29.450 1.00 41.07 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 8.438  -5.335  30.665 1.00 45.11 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 10.946 -4.278  23.916 1.00 11.33 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 10.724 -4.140  22.479 1.00 10.77 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 9.274  -4.483  22.185 1.00 12.07 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 8.772  -5.532  22.621 1.00 14.92 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 11.649 -5.099  21.700 1.00 9.62  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 13.117 -4.771  21.819 1.00 10.88 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 13.820 -4.063  20.841 1.00 14.60 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 13.967 -5.082  22.822 1.00 11.53 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 15.092 -4.012  21.265 1.00 12.83 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 15.216 -4.590  22.444 1.00 14.70 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 8.582  -3.623  21.450 1.00 10.27 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 7.148  -3.830  21.159 1.00 10.79 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 6.905  -3.944  19.681 1.00 10.01 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 7.394  -3.102  18.929 1.00 10.04 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 6.309  -2.607  21.661 1.00 11.72 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 6.244  -2.466  23.169 1.00 12.27 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 5.456  -3.323  23.934 1.00 13.25 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 6.939  -1.459  23.821 1.00 11.76 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 5.326  -3.160  25.314 1.00 14.24 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 6.828  -1.283  25.205 1.00 13.11 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 6.014  -2.137  25.944 1.00 14.27 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 5.926  -1.946  27.310 1.00 16.98 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 6.079  -4.906  19.255 1.00 10.56 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 5.676  -4.929  17.832 1.00 10.53 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 4.653  -3.829  17.562 1.00 12.19 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 3.730  -3.620  18.384 1.00 16.00 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.019  -6.317  17.653 1.00 12.21 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 4.635  -6.763  19.042 1.00 13.94 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 5.487  -6.005  20.051 1.00 10.86 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 4.779  -3.191  16.428 1.00 9.78  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 3.845  -2.103  16.069 1.00 12.40 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 3.528  -2.113  14.602 1.00 11.25 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.335  -2.491  13.766 1.00 11.44 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 4.391  -0.725  16.443 1.00 15.37 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 4.307  -0.512  17.951 1.00 16.59 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 5.808  -0.507  15.900 1.00 15.42 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.346  -1.538  14.267 1.00 11.49 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 1.960  -1.134  12.913 1.00 11.40 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.171  0.394   12.862 1.00 10.85 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 1.766  1.111   13.816 1.00 12.08 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.473  -1.394  12.699 1.00 15.49 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.230  -2.788  12.698 1.00 23.51 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 2.787  0.896   11.795 1.00 10.78 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.102  2.310   11.705 1.00 11.51 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.694  2.892   10.348 1.00 12.12 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.631  2.173   9.338  1.00 13.53 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.601  2.573   12.058 1.00 12.06 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.619  1.771   11.269 1.00 10.96 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.044  0.525   11.712 1.00 10.39 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.208  2.297   10.135 1.00 11.91 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 6.997  -0.202  10.998 1.00 11.39 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.173  1.557   9.416  1.00 12.55 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.528  0.291   9.839  1.00 11.37 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.387  4.185   10.331 1.00 12.48 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 1.977  4.861   9.111  1.00 12.94 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.150  5.088   8.148  1.00 12.64 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.319  5.007   8.560  1.00 12.97 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.267  6.181   9.439  1.00 14.88 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.107  7.095   10.131 1.00 16.31 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.868  5.415   6.902  1.00 13.00 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.930  5.729   5.944  1.00 13.60 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.554  7.086   6.286  1.00 14.68 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.854  7.957   6.819  1.00 15.49 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.337  5.728   4.520  1.00 16.07 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.966  4.336   4.082  1.00 18.89 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.556  4.324   2.596  1.00 26.48 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.273  2.920   2.133  1.00 32.62 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 2.283  2.827   0.647  1.00 37.76 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.822  7.329   5.937  1.00 14.26 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.445  8.617   6.266  1.00 14.51 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.664  9.789   5.685  1.00 15.05 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.282  9.760   4.507  1.00 16.97 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.870  8.499   5.660  1.00 16.56 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 8.040  7.074   5.247  1.00 19.22 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.734  6.402   5.223  1.00 15.28 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.375  10.762  6.537  1.00 14.22 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.592  11.898  6.078  1.00 16.16 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.880  13.157  6.890  1.00 15.04 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.689  13.160  7.822  1.00 14.28 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 3.115  11.545  6.053  1.00 21.84 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.729  11.459  7.401  1.00 26.02 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 4.188  14.252  6.509  1.00 16.58 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.341  15.549  7.154  1.00 17.47 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.255  15.624  8.241  1.00 18.83 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 2.045  15.661  7.929  1.00 20.81 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 4.142  16.638  6.087  1.00 18.76 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.430  18.049  6.519  1.00 21.23 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 5.909  18.251  6.772  1.00 21.72 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 3.978  19.045  5.429  1.00 22.96 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.677  15.585  9.508  1.00 18.02 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.789  15.516  10.684 1.00 19.53 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.026  16.698  11.634 1.00 20.04 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.180  17.086  11.890 1.00 19.15 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.097  14.208  11.440 1.00 21.51 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.839  12.928  10.563 1.00 24.64 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.390  14.132  12.821 1.00 23.21 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 1.385  12.493  10.402 1.00 28.10 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 1.944  17.247  12.207 1.00 20.80 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.068  18.353  13.151 1.00 21.64 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.498  17.782  14.503 1.00 21.83 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 1.960  16.774  14.988 1.00 23.74 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 0.725  19.111  13.289 1.00 23.32 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 0.915  20.449  13.952 1.00 26.54 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.588  21.471  13.305 1.00 29.17 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.486  20.660  15.240 1.00 29.07 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.790  22.695  13.923 1.00 31.29 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 0.707  21.881  15.864 1.00 29.66 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.319  22.899  15.190 1.00 30.91 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.572  18.339  15.051 1.00 19.15 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.112  17.895  16.321 1.00 18.14 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 3.998  19.081  17.311 1.00 17.23 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 4.441  20.194  16.991 1.00 17.22 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 5.588  17.473  16.136 1.00 16.73 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 6.208  17.075  17.479 1.00 18.16 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 5.691  16.336  15.092 1.00 17.39 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 3.451  18.810  18.495 1.00 16.96 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 3.261  19.856  19.500 1.00 18.25 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 4.592  20.424  19.963 1.00 18.16 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 5.624  19.748  19.922 1.00 18.34 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 2.510  19.276  20.707 1.00 21.35 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 1.057  18.920  20.417 1.00 28.95 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 0.270  20.103  19.889 1.00 40.58 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 0.286  21.172  20.542 1.00 43.62 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? -0.319 19.982  18.792 1.00 46.41 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 4.539  21.656  20.514 1.00 19.38 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 5.711  22.337  21.094 1.00 20.34 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 6.287  21.481  22.182 1.00 20.29 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 5.551  20.853  22.957 1.00 22.20 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 5.297  23.662  21.699 1.00 21.41 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 7.611  21.416  22.227 1.00 19.77 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 8.303  20.639  23.246 1.00 19.29 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 9.443  21.505  23.811 1.00 19.88 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 9.587  22.673  23.442 1.00 21.18 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 8.925  19.397  22.605 1.00 19.56 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 9.922  19.793  21.665 1.00 18.93 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 10.302 20.891  24.625 1.00 20.29 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 11.476 21.581  25.145 1.00 20.21 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 12.489 21.886  24.008 1.00 18.33 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 13.299 22.813  24.124 1.00 18.61 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 12.143 20.612  26.130 1.00 24.96 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.368 21.135  26.827 1.00 32.51 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 14.051 20.115  27.717 1.00 39.37 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 13.392 19.127  28.126 1.00 38.67 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 15.253 20.314  28.011 1.00 42.07 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 12.413 21.145  22.889 1.00 17.50 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 13.423 21.285  21.824 1.00 16.76 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 12.999 21.949  20.552 1.00 16.73 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 13.859 22.413  19.804 1.00 16.82 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 13.982 19.906  21.489 1.00 17.28 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 14.747 19.346  22.664 1.00 17.38 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 16.032 19.782  22.952 1.00 20.48 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.162 18.449  23.531 1.00 19.59 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 16.748 19.257  24.023 1.00 22.84 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 14.861 17.929  24.621 1.00 21.76 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.148 18.355  24.873 1.00 24.81 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.834 17.864  25.969 1.00 29.26 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 11.668 22.011  20.271 1.00 16.33 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 11.174 22.685  19.066 1.00 16.52 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 9.824  23.361  19.378 1.00 16.85 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 9.052  22.788  20.161 1.00 17.71 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 10.893 21.660  17.932 1.00 16.59 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.070 20.827  17.436 1.00 13.94 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 12.978 21.345  16.532 1.00 14.29 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 12.256 19.522  17.874 1.00 13.85 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.046 20.575  16.075 1.00 13.37 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 13.276 18.732  17.386 1.00 13.77 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.182 19.276  16.515 1.00 13.17 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.227 18.513  16.058 1.00 12.58 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 9.517  24.474  18.699 1.00 18.56 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 8.141  25.027  18.783 1.00 19.20 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.174  24.082  18.037 1.00 20.88 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 7.623  23.165  17.311 1.00 19.99 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 8.264  26.383  18.047 1.00 20.67 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 9.314  26.160  17.078 1.00 20.62 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 10.333 25.219  17.714 1.00 19.02 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 5.858  24.304  18.140 1.00 21.58 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 4.885  23.455  17.429 1.00 21.57 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.124  23.700  15.932 1.00 21.02 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.355  24.821  15.499 1.00 22.31 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 3.453  23.845  17.837 1.00 22.74 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.250  22.629  15.168 1.00 19.21 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.643  22.724  13.776 1.00 18.60 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.249  21.429  13.086 1.00 18.14 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 4.883  20.458  13.756 1.00 19.21 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.187  22.902  13.708 1.00 18.54 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 7.989  21.582  13.900 1.00 18.69 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.386  21.824  14.365 1.00 18.41 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.312 20.731  14.003 1.00 16.96 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.316 19.496  14.498 1.00 17.05 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 9.410  19.130  15.423 1.00 17.61 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 11.238 18.618  14.098 1.00 14.82 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.434  21.382  11.766 1.00 18.39 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.287  20.182  10.988 1.00 19.07 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.667  19.540  10.845 1.00 17.32 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.646  20.173  10.425 1.00 17.39 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.763  20.526  9.598  1.00 20.03 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.285  20.825  9.609  1.00 20.80 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.350  19.803  9.546  1.00 20.73 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.817  22.124  9.745  1.00 22.76 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.986  20.064  9.623  1.00 22.91 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.460  22.397  9.786  1.00 24.32 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.549  21.362  9.746  1.00 25.07 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.802 21.606  9.800  1.00 28.58 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.729  18.227  11.156 1.00 15.53 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.946  17.419  10.997 1.00 14.29 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.728  16.515  9.799  1.00 13.42 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.666  15.889  9.678  1.00 13.98 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.212  16.609  12.267 1.00 14.29 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.444  15.737  12.148 1.00 12.90 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 9.988  15.229  13.483 1.00 13.35 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.047 15.967  14.473 1.00 13.76 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.428 13.956  13.522 1.00 12.34 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.723  16.407  8.920  1.00 12.74 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.607  15.580  7.741  1.00 12.98 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 9.215  14.195  7.968  1.00 12.73 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.978  13.976  8.935  1.00 13.51 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 9.288  16.272  6.566  1.00 14.91 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.674 16.419  6.854  1.00 18.51 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.829  13.255  7.079  1.00 12.90 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.333  11.889  7.066  1.00 12.47 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 9.067  11.203  8.422  1.00 11.97 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.883  10.357  8.853  1.00 12.37 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.856 11.864  6.701  1.00 13.86 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 11.164 12.419  5.327  1.00 14.91 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 11.300 11.590  4.235  1.00 17.86 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 11.303 13.699  4.913  1.00 16.60 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 11.561 12.382  3.193  1.00 17.94 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 11.560 13.652  3.545  1.00 17.98 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.946  11.495  9.050  1.00 11.28 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.595  10.961  10.365 1.00 11.56 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.517  9.889   10.182 1.00 11.12 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.580  10.065  9.385  1.00 12.16 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.079  12.121  11.244 1.00 12.46 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.723  11.740  12.704 1.00 14.21 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 7.933  11.356  13.440 1.00 14.63 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.095  12.941  13.454 1.00 17.01 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.643  8.798   10.966 1.00 11.31 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.678  7.671   10.940 1.00 11.22 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.091  7.513   12.343 1.00 11.56 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 5.849  7.519   13.318 1.00 12.56 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.449  6.400   10.575 1.00 12.24 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.094  6.514   9.184  1.00 13.31 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.185  5.131   8.701  1.00 15.34 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.433  5.292   9.947  1.00 19.27 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 3.785  7.356   12.466 1.00 10.95 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.151  7.213   13.768 1.00 11.76 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 2.650  5.805   14.054 1.00 11.63 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.225  5.099   13.113 1.00 13.13 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 1.956  8.162   13.939 1.00 14.45 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.209  9.645   13.863 1.00 17.61 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 0.930  10.453  14.270 1.00 19.78 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.346  10.088  14.779 1.00 19.57 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 2.677  5.418   15.337 1.00 11.70 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.156  4.128   15.776 1.00 10.62 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 1.533  4.324   17.157 1.00 10.31 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 1.801  5.321   17.851 1.00 11.21 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 3.310  3.087   15.897 1.00 12.01 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 0.732  3.340   17.563 1.00 10.56 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.213  3.294   18.906 1.00 11.02 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.235  2.491   19.732 1.00 12.89 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 1.538  1.348   19.428 1.00 14.71 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -1.150 2.593   18.904 1.00 10.71 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -1.637 2.394   20.339 1.00 12.04 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -2.131 3.426   18.078 1.00 11.14 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 1.776  3.152   20.721 1.00 13.68 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 2.787  2.532   21.581 1.00 13.79 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 3.191  3.494   22.670 1.00 13.55 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.016  4.717   22.551 1.00 14.01 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 3.680  2.942   23.796 1.00 14.13 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 4.120  3.798   24.865 1.00 14.52 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 5.399  4.549   24.504 1.00 13.69 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 6.355  3.956   23.965 1.00 13.35 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 4.357  2.982   26.157 1.00 14.12 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 4.752  3.871   27.294 1.00 14.87 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 3.841  4.741   27.871 1.00 15.30 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 5.968  4.074   27.878 1.00 15.25 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 4.535  5.466   28.758 1.00 15.70 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 5.813  5.063   28.821 1.00 15.03 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 5.451  5.799   24.835 1.00 14.00 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 6.637  6.589   24.738 1.00 12.41 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 6.628  7.751   25.724 1.00 14.17 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 5.553  8.296   26.021 1.00 16.24 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 6.970  7.011   23.299 1.00 13.87 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 6.005  7.934   22.821 1.00 15.21 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 7.859  8.140   26.194 1.00 13.15 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 8.220  9.280   27.055 1.00 14.01 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 9.385  10.022  26.380 1.00 14.57 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 10.065 9.485   25.491 1.00 13.63 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 8.634  8.793   28.463 1.00 15.03 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 7.473  8.063   29.110 1.00 16.07 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 7.678  7.502   30.508 1.00 17.09 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 8.434  8.095   31.308 1.00 21.06 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 7.098  6.435   30.790 1.00 16.36 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 9.632  11.287  26.737 1.00 14.58 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 10.646 12.077  25.991 1.00 15.16 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 12.010 11.396  25.814 1.00 14.91 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 12.569 11.368  24.687 1.00 14.29 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 10.693 13.413  26.790 1.00 16.57 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 9.263  13.547  27.303 1.00 17.22 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 8.878  12.133  27.700 1.00 15.05 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 12.523 10.784  26.880 1.00 13.39 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 13.818 10.106  26.853 1.00 12.77 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 13.846 8.804   26.051 1.00 11.05 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 14.909 8.201   25.915 1.00 12.32 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 12.698 8.348   25.526 1.00 10.72 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 12.665 7.194   24.624 1.00 10.44 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 13.199 7.554   23.229 1.00 10.04 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 13.466 6.647   22.417 1.00 9.79  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 11.242 6.612   24.502 1.00 10.17 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 10.858 5.907   25.787 1.00 10.85 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 11.729 5.253   26.379 1.00 10.99 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 9.669  5.966   26.164 1.00 11.40 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 13.348 8.872   22.915 1.00 10.14 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 13.911 9.239   21.591 1.00 10.36 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 15.275 8.562   21.383 1.00 10.16 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 16.103 8.481   22.312 1.00 10.95 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 14.020 10.756  21.488 1.00 11.80 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 12.419 11.585  21.221 1.00 12.53 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 15.473 8.015   20.192 1.00 9.68  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 16.707 7.328   19.859 1.00 9.83  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 16.545 5.822   19.793 1.00 10.01 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 17.414 5.139   19.232 1.00 10.40 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 15.463 5.278   20.373 1.00 9.29  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 15.230 3.839   20.281 1.00 9.00  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.011 3.417   18.830 1.00 8.46  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 14.332 4.125   18.068 1.00 8.82  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 15.553 2.249   18.446 1.00 8.92  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 15.410 1.812   17.052 1.00 8.71  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.069 1.165   16.763 1.00 8.50  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 13.600 0.353   17.552 1.00 8.92  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 16.590 0.854   16.729 1.00 9.09  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 17.852 1.705   16.440 1.00 10.57 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 16.329 -0.069  15.520 1.00 9.87  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.126 0.851   16.352 1.00 13.46 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 13.507 1.486   15.589 1.00 7.98  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 12.410 0.751   14.969 1.00 7.98  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.036 -0.103  13.855 1.00 8.45  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 13.820 0.427   13.032 1.00 8.89  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 11.406 1.760   14.329 1.00 8.66  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.323 1.119   13.442 1.00 9.30  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 9.330  0.314   14.296 1.00 11.13 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.535  2.208   12.652 1.00 11.72 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 12.714 -1.393  13.820 1.00 8.67  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.293 -2.293  12.812 1.00 8.84  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.233 -3.201  12.269 1.00 9.68  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.233 -3.515  12.901 1.00 10.02 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.451 -3.121  13.426 1.00 9.86  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 13.987 -4.074  14.548 1.00 10.43 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 15.208 -4.823  15.092 1.00 11.50 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 16.003 -3.950  15.941 1.00 13.22 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 17.316 -3.735  15.840 1.00 13.14 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 17.998 -4.185  14.788 1.00 14.83 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 17.940 -2.991  16.739 1.00 14.20 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.491 -3.703  11.056 1.00 11.15 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.632 -4.689  10.381 1.00 13.95 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.485 -5.883  9.981  1.00 17.00 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.671 -5.965  10.331 1.00 15.88 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 10.950 -4.037  9.188  1.00 14.68 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.108 -3.657  7.822  1.00 13.82 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 11.876 -6.843  9.208  1.00 19.58 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 12.661 -7.989  8.772  1.00 21.64 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 13.893 -7.626  7.902  1.00 21.57 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 14.842 -8.399  7.826  1.00 24.08 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 11.803 -9.043  8.026  1.00 25.54 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.300 -8.538  6.686  1.00 30.81 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.358 -9.493  5.986  1.00 37.47 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.128  -9.387  6.097  1.00 39.73 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.911 -10.404 5.212  1.00 37.58 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.908 -6.429  7.306  1.00 18.08 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.991 -5.994  6.398  1.00 17.54 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.130 -5.207  7.063  1.00 16.79 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.166 -4.927  6.434  1.00 19.82 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.393 -5.152  5.265  1.00 16.87 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.292 -5.899  4.547  1.00 17.56 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.950 -5.563  4.692  1.00 19.85 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.384 -6.932  3.661  1.00 20.76 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.278 -6.395  3.905  1.00 22.16 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 12.105 -7.226  3.266  1.00 22.44 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.911 -4.761  8.312  1.00 15.23 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 16.917 -3.958  8.989  1.00 14.46 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.285 -2.786  9.740  1.00 12.08 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.090 -2.796  10.084 1.00 11.83 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.126 -1.769  10.015 1.00 10.68 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.674 -0.582  10.755 1.00 10.35 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.829 0.331   9.868  1.00 8.95  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.266 0.702   8.755  1.00 9.74  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 17.906 0.191   11.331 1.00 10.60 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.477 1.496   12.015 1.00 11.68 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 18.668 -0.696  12.328 1.00 12.24 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.676 0.747   10.382 1.00 8.83  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.738 1.571   9.642  1.00 9.38  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.880 3.035   10.065 1.00 9.50  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.740 3.951   9.240  1.00 10.41 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.283 1.081   9.925  1.00 10.63 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.218 2.025   9.339  1.00 12.91 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.067 -0.347  9.404  1.00 11.97 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.087 3.294   11.362 1.00 9.38  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.180 4.664   11.866 1.00 9.73  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.379 4.691   13.367 1.00 8.88  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 14.696 3.638   13.960 1.00 9.12  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.237 5.874   13.976 1.00 8.73  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.429 6.015   15.433 1.00 8.49  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.264 6.771   16.038 1.00 8.37  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 12.662 7.636   15.381 1.00 9.27  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 15.770 6.730   15.818 1.00 9.43  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 15.902 8.058   15.068 1.00 10.89 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 16.950 5.777   15.613 1.00 10.95 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.172 8.865   15.574 1.00 12.50 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 12.957 6.499   17.299 1.00 8.67  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 11.899 7.226   18.016 1.00 8.64  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.252 8.724   17.996 1.00 8.74  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 13.417 9.083   18.304 1.00 9.23  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 11.779 6.732   19.472 1.00 8.93  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 10.764 7.579   20.247 1.00 10.29 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 11.343 5.256   19.519 1.00 9.85  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.280 9.582   17.670 1.00 9.48  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 11.481 11.032  17.596 1.00 9.69  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 10.349 11.797  18.294 1.00 11.04 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 10.604 12.930  18.697 1.00 12.13 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 11.639 11.430  16.132 1.00 10.71 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 11.743 12.835  15.923 1.00 11.07 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.110  11.262  18.372 1.00 10.99 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.000  12.046  18.982 1.00 12.51 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.116  11.084  19.781 1.00 14.26 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 7.294  9.847   19.717 1.00 12.54 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.119  12.737  17.880 1.00 13.17 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.341  11.760  17.197 1.00 14.22 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 7.906  13.594  16.903 1.00 14.04 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 6.096  11.612  20.457 1.00 14.61 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 5.130  10.757  21.141 1.00 15.42 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 4.249  11.526  22.104 1.00 16.54 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 4.340  12.738  22.216 1.00 17.00 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 3.491  10.740  22.857 1.00 17.34 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 2.594  11.212  23.906 1.00 17.72 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 1.243  10.538  23.785 1.00 17.66 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 0.835  10.160  22.678 1.00 17.77 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 0.544  10.376  24.917 1.00 16.38 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? -0.813 9.847   24.987 1.00 16.50 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -1.016 8.553   24.248 1.00 15.90 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -2.100 8.330   23.688 1.00 17.09 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -1.770 10.924  24.498 1.00 18.44 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -1.796 12.116  25.422 1.00 23.11 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -2.082 11.970  26.614 1.00 26.31 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -1.466 13.280  24.872 1.00 25.05 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? -0.073 7.651   24.402 1.00 13.95 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? -0.193 6.339   23.820 1.00 14.28 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 0.167  6.313   22.351 1.00 12.80 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.011  5.255   21.748 1.00 13.98 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 0.805  7.376   21.828 1.00 12.21 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 1.364  7.359   20.458 1.00 11.88 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 2.890  7.405   20.536 1.00 12.51 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 3.467  7.932   21.521 1.00 13.59 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 0.888  8.586   19.665 1.00 12.37 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? -0.621 8.598   19.405 1.00 13.54 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -1.092 9.986   19.000 1.00 16.01 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -1.024 7.517   18.362 1.00 13.96 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 3.536  6.891   19.493 1.00 10.56 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 4.986  7.020   19.364 1.00 10.73 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.235  7.381   17.857 1.00 10.83 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 4.610  6.790   16.976 1.00 11.58 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 5.721  5.732   19.817 1.00 10.71 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 5.217  4.502   19.076 1.00 10.92 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 7.240  5.898   19.682 1.00 11.47 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.158  8.287   17.582 1.00 10.66 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 6.489  8.647   16.201 1.00 10.49 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 7.948  8.351   15.930 1.00 9.86  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 8.807  8.530   16.799 1.00 11.47 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.211  7.911   14.716 1.00 9.27  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.580  7.516   14.308 1.00 9.12  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.036 8.311   13.101 1.00 10.40 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.282  8.463   12.125 1.00 11.17 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.561  6.016   13.901 1.00 9.67  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 8.929  5.094   14.932 1.00 9.51  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 9.665  4.626   16.022 1.00 9.59  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 7.605  4.698   14.801 1.00 10.99 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.084  3.759   16.957 1.00 9.69  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.039  3.834   15.725 1.00 10.70 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 7.784  3.374   16.805 1.00 9.77  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.285 8.806   13.181 1.00 9.36  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 11.911 9.497   12.042 1.00 10.48 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.426 8.419   11.095 1.00 9.97  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.311 7.618   11.480 1.00 10.17 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.055 10.371  12.555 1.00 10.50 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.887 8.332   9.861  1.00 10.08 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.302 7.345   8.884  1.00 10.60 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.724 7.656   8.407  1.00 10.76 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.088 8.841   8.236  1.00 11.81 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.355 7.412   7.655  1.00 12.84 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.632 6.389   6.597  1.00 19.49 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.775 5.201   6.945  1.00 15.61 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.789 6.792   5.406  1.00 28.10 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.502 6.601   8.117  1.00 9.95  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.829 6.756   7.496  1.00 9.83  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.951 5.940   6.197  1.00 10.69 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.028 5.950   5.584  1.00 10.35 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.999 6.409   8.462  1.00 9.77  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.025 7.335   9.686  1.00 10.75 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.020 4.934   8.867  1.00 10.56 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.886 5.231   5.772  1.00 10.78 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.994 4.313   4.636  1.00 11.31 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 15.275 5.003   3.312  1.00 11.91 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.742 4.344   2.349  1.00 12.67 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.742 3.437   4.548  1.00 11.74 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.603 2.484   5.738  1.00 11.51 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.304 1.687   5.587  1.00 12.67 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.153 2.573   5.817  1.00 12.52 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.889  2.169   5.894  1.00 14.90 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.572  0.900   5.624  1.00 14.55 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.927  3.050   6.184  1.00 15.69 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.947 6.309   3.187  1.00 11.57 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 15.217 7.024   1.939  1.00 12.43 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 16.651 7.557   1.834  1.00 11.99 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 17.040 8.057   0.777  1.00 13.60 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 14.229 8.195   1.789  1.00 14.40 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 14.425 9.251   2.877  1.00 17.11 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.515 8.882   4.072  1.00 15.58 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 14.473 10.447  2.545  1.00 18.76 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.444 7.494   2.936  1.00 11.13 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.816 8.039   3.009  1.00 11.55 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.799 7.020   2.469  1.00 11.79 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 20.472 6.299   3.209  1.00 11.74 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 19.158 8.463   4.457  1.00 12.04 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 18.168 9.481   5.069  1.00 13.16 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.545 9.741   6.534  1.00 13.01 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 18.164 10.784  4.299  1.00 14.52 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 19.808 6.890   1.144  1.00 11.78 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 20.562 5.805   0.498  1.00 11.96 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 22.050 5.914   0.728  1.00 12.21 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 22.746 4.886   0.768  1.00 13.27 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 20.233 5.690   -1.027 1.00 13.32 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 18.729 5.672   -1.357 1.00 15.32 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 18.529 5.417   -2.836 1.00 17.11 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.937 4.618   -0.558 1.00 16.44 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 22.549 7.147   0.901  1.00 11.46 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.968 7.410   1.093  1.00 11.86 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 24.507 6.815   2.400  1.00 13.29 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.728 6.676   2.547  1.00 14.62 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 24.254 8.920   0.959  1.00 12.92 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 23.429 9.765   1.880  1.00 12.51 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 22.260 10.400  1.578  1.00 13.04 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 23.727 10.090  3.251  1.00 12.97 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 21.808 11.100  2.678  1.00 13.63 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 22.700 10.937  3.710  1.00 13.24 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.784 9.772   4.116  1.00 13.97 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.680 11.433  5.022  1.00 14.40 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.790 10.327  5.395  1.00 14.76 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.749 11.139  5.824  1.00 14.73 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.623 6.447   3.359  1.00 11.75 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 24.100 5.803   4.592  1.00 13.28 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.802 4.469   4.269  1.00 15.37 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.625 4.021   5.083  1.00 16.05 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.948 5.544   5.561  1.00 12.67 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.399 6.774   6.232  1.00 12.61 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.129 6.402   7.019  1.00 14.06 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.483 7.436   7.171  1.00 13.80 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.498 3.846   3.094  1.00 17.44 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 25.074 2.544   2.713  1.00 20.59 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 26.415 2.630   1.997  1.00 24.27 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.951 1.581   1.622  1.00 25.42 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 24.098 1.789   1.769  1.00 21.20 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.750 1.423   2.332  1.00 25.44 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 22.577 1.525   3.560  1.00 26.78 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.851 1.032   1.542  1.00 31.27 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.959 3.835   1.768  1.00 25.46 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 28.226 3.967   1.038  1.00 28.19 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 29.204 4.928   1.720  1.00 29.06 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.798 5.722   2.570  1.00 29.54 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 27.924 4.420   -0.394 1.00 33.23 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 27.223 5.765   -0.427 1.00 40.15 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 26.399 6.078   -1.660 1.00 47.63 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 26.163 7.280   -1.926 1.00 46.74 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 25.988 5.124   -2.360 1.00 51.83 ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 21.808 -21.319 7.625  1.00 15.84 ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 20.682 -21.108 8.553  1.00 15.63 ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 20.654 -22.208 9.630  1.00 14.68 ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 21.322 -23.255 9.475  1.00 16.15 ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 19.367 -21.133 7.764  1.00 18.71 ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 19.160 -22.420 7.203  1.00 23.05 ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 19.895 -21.980 10.708 1.00 14.57 ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 19.753 -22.996 11.747 1.00 14.23 ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 19.461 -22.373 13.093 1.00 12.76 ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 19.819 -21.222 13.336 1.00 13.07 ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 18.802 -23.115 13.976 1.00 11.44 ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 18.473 -22.617 15.323 1.00 11.26 ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 18.587 -23.740 16.350 1.00 10.82 ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 18.620 -24.934 15.980 1.00 12.67 ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 17.029 -22.054 15.340 1.00 14.19 ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 18.651 -23.352 17.634 1.00 10.33 ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 18.545 -24.292 18.752 1.00 10.33 ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 17.148 -24.100 19.354 1.00 10.51 ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 16.711 -22.949 19.549 1.00 11.45 ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 19.597 -23.977 19.820 1.00 10.80 ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 21.039 -23.853 19.233 1.00 11.27 ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 19.512 -25.035 20.947 1.00 12.86 ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 22.018 -23.224 20.229 1.00 12.74 ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 16.439 -25.198 19.647 1.00 10.85 ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 15.095 -25.147 20.248 1.00 11.44 ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 15.165 -25.833 21.610 1.00 11.58 ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 15.249 -27.061 21.677 1.00 13.20 ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 14.058 -25.843 19.320 1.00 12.30 ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 13.871 -25.073 18.025 1.00 12.21 ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 13.038 -23.949 17.969 1.00 13.28 ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 14.576 -25.419 16.876 1.00 13.36 ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 12.879 -23.232 16.798 1.00 14.03 ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 14.436 -24.699 15.696 1.00 14.71 ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 13.595 -23.597 15.664 1.00 15.21 ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 13.500 -22.848 14.508 1.00 17.71 ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 15.200 -25.083 22.699 1.00 12.49 ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 15.292 -25.642 24.058 1.00 13.10 ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 14.152 -25.032 24.901 1.00 13.44 ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 13.970 -23.817 24.895 1.00 11.72 ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 16.695 -25.373 24.672 1.00 14.10 ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 17.088 -23.875 24.573 1.00 14.36 ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 16.743 -25.869 26.112 1.00 16.21 ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 13.332 -25.854 25.584 1.00 14.73 ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 12.216 -25.291 26.365 1.00 14.79 ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 11.287 -24.460 25.496 1.00 14.78 ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 11.014 -24.847 24.353 1.00 15.67 ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 10.959 -23.257 25.936 1.00 14.50 ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 10.181 -22.346 25.117 1.00 15.16 ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 11.064 -21.231 24.532 1.00 14.16 ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 10.614 -20.104 24.372 1.00 14.27 ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 8.958  -21.781 25.884 1.00 16.97 ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 7.857  -22.831 26.030 1.00 23.86 ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 6.974  -22.974 25.176 1.00 26.12 ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 7.965  -23.637 27.063 1.00 26.22 ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 12.290 -21.592 24.140 1.00 12.29 ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 13.239 -20.637 23.553 1.00 11.59 ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 13.715 -21.131 22.180 1.00 11.28 ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 13.900 -22.341 21.958 1.00 11.89 ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 14.480 -20.504 24.456 1.00 12.61 ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 14.167 -19.985 25.851 1.00 13.59 ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 13.595 -18.729 26.033 1.00 15.73 ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 14.476 -20.739 26.984 1.00 16.32 ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 13.337 -18.235 27.311 1.00 17.80 ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 14.230 -20.244 28.267 1.00 18.66 ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 13.669 -18.992 28.417 1.00 21.17 ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 13.438 -18.471 29.679 1.00 26.29 ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 13.938 -20.190 21.281 1.00 10.62 ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 14.554 -20.399 19.957 1.00 10.80 ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 15.811 -19.525 19.960 1.00 10.43 ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 15.722 -18.306 20.180 1.00 11.25 ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 13.578 -19.946 18.842 1.00 12.47 ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 14.211 -19.774 17.442 1.00 12.84 ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 13.135 -19.474 16.392 1.00 13.23 ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 13.583 -18.514 15.372 1.00 14.29 ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 14.078 -18.827 14.172 1.00 14.64 ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 14.304 -20.104 13.844 1.00 16.26 ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 14.426 -17.867 13.322 1.00 16.23 ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 16.996 -20.139 19.717 1.00 10.29 ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 18.287 -19.412 19.685 1.00 9.70  ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 18.759 -19.363 18.252 1.00 9.99  ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 18.934 -20.431 17.623 1.00 10.58 ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 19.372 -20.132 20.541 1.00 10.30 ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 20.645 -19.288 20.611 1.00 12.08 ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 18.849 -20.518 21.938 1.00 11.71 ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 19.006 -18.156 17.724 1.00 9.75  ? 18  VAL   C N   1 
ATOM   1163 C  CA  A VAL   B 1 12  ? 19.454 -17.973 16.334 0.50 9.29  ? 18  VAL   C CA  1 
ATOM   1164 C  CA  B VAL   B 1 12  ? 19.409 -18.006 16.335 0.50 10.84 ? 18  VAL   C CA  1 
ATOM   1165 C  C   . VAL   B 1 12  ? 20.589 -16.990 16.247 1.00 10.00 ? 18  VAL   C C   1 
ATOM   1166 O  O   . VAL   B 1 12  ? 20.846 -16.219 17.210 1.00 11.32 ? 18  VAL   C O   1 
ATOM   1167 C  CB  A VAL   B 1 12  ? 18.311 -17.434 15.416 0.50 9.67  ? 18  VAL   C CB  1 
ATOM   1168 C  CB  B VAL   B 1 12  ? 18.128 -17.478 15.585 0.50 14.18 ? 18  VAL   C CB  1 
ATOM   1169 C  CG1 A VAL   B 1 12  ? 17.332 -18.544 15.068 0.50 11.74 ? 18  VAL   C CG1 1 
ATOM   1170 C  CG1 B VAL   B 1 12  ? 18.356 -17.314 14.105 0.50 14.33 ? 18  VAL   C CG1 1 
ATOM   1171 C  CG2 A VAL   B 1 12  ? 17.662 -16.140 15.975 0.50 7.06  ? 18  VAL   C CG2 1 
ATOM   1172 C  CG2 B VAL   B 1 12  ? 16.932 -18.396 15.805 0.50 17.07 ? 18  VAL   C CG2 1 
ATOM   1173 N  N   . ASN   B 1 13  ? 21.292 -16.940 15.082 1.00 9.37  ? 19  ASN   C N   1 
ATOM   1174 C  CA  . ASN   B 1 13  ? 22.280 -15.881 14.878 1.00 9.80  ? 19  ASN   C CA  1 
ATOM   1175 C  C   . ASN   B 1 13  ? 21.476 -14.543 14.839 1.00 10.20 ? 19  ASN   C C   1 
ATOM   1176 O  O   . ASN   B 1 13  ? 20.462 -14.454 14.140 1.00 9.94  ? 19  ASN   C O   1 
ATOM   1177 C  CB  . ASN   B 1 13  ? 22.975 -16.034 13.510 1.00 10.62 ? 19  ASN   C CB  1 
ATOM   1178 C  CG  . ASN   B 1 13  ? 23.821 -17.294 13.453 1.00 10.27 ? 19  ASN   C CG  1 
ATOM   1179 O  OD1 . ASN   B 1 13  ? 23.364 -18.341 13.003 1.00 11.33 ? 19  ASN   C OD1 1 
ATOM   1180 N  ND2 . ASN   B 1 13  ? 25.066 -17.204 13.915 1.00 10.40 ? 19  ASN   C ND2 1 
ATOM   1181 N  N   . ARG   B 1 14  ? 21.957 -13.507 15.542 1.00 10.14 ? 20  ARG   C N   1 
ATOM   1182 C  CA  . ARG   B 1 14  ? 21.218 -12.215 15.566 1.00 9.47  ? 20  ARG   C CA  1 
ATOM   1183 C  C   . ARG   B 1 14  ? 21.080 -11.684 14.137 1.00 11.09 ? 20  ARG   C C   1 
ATOM   1184 O  O   . ARG   B 1 14  ? 20.019 -11.152 13.805 1.00 11.99 ? 20  ARG   C O   1 
ATOM   1185 C  CB  . ARG   B 1 14  ? 21.973 -11.208 16.432 1.00 9.96  ? 20  ARG   C CB  1 
ATOM   1186 C  CG  . ARG   B 1 14  ? 21.205 -9.887  16.658 1.00 10.36 ? 20  ARG   C CG  1 
ATOM   1187 C  CD  . ARG   B 1 14  ? 22.055 -8.931  17.459 1.00 11.87 ? 20  ARG   C CD  1 
ATOM   1188 N  NE  . ARG   B 1 14  ? 21.393 -7.670  17.894 1.00 12.05 ? 20  ARG   C NE  1 
ATOM   1189 C  CZ  . ARG   B 1 14  ? 21.283 -6.577  17.151 1.00 12.47 ? 20  ARG   C CZ  1 
ATOM   1190 N  NH1 . ARG   B 1 14  ? 21.676 -6.583  15.881 1.00 13.80 ? 20  ARG   C NH1 1 
ATOM   1191 N  NH2 . ARG   B 1 14  ? 20.797 -5.454  17.679 1.00 12.54 ? 20  ARG   C NH2 1 
ATOM   1192 N  N   . HIS   B 1 15  ? 22.103 -11.886 13.274 1.00 10.45 ? 21  HIS   C N   1 
ATOM   1193 C  CA  . HIS   B 1 15  ? 22.014 -11.336 11.908 1.00 11.17 ? 21  HIS   C CA  1 
ATOM   1194 C  C   . HIS   B 1 15  ? 21.012 -12.066 11.006 1.00 11.66 ? 21  HIS   C C   1 
ATOM   1195 O  O   . HIS   B 1 15  ? 20.687 -11.536 9.940  1.00 14.11 ? 21  HIS   C O   1 
ATOM   1196 C  CB  . HIS   B 1 15  ? 23.412 -11.233 11.235 1.00 12.09 ? 21  HIS   C CB  1 
ATOM   1197 C  CG  . HIS   B 1 15  ? 24.003 -12.555 10.796 1.00 11.15 ? 21  HIS   C CG  1 
ATOM   1198 N  ND1 . HIS   B 1 15  ? 24.744 -13.358 11.660 1.00 11.62 ? 21  HIS   C ND1 1 
ATOM   1199 C  CD2 . HIS   B 1 15  ? 23.988 -13.125 9.564  1.00 11.83 ? 21  HIS   C CD2 1 
ATOM   1200 C  CE1 . HIS   B 1 15  ? 25.148 -14.406 10.934 1.00 12.51 ? 21  HIS   C CE1 1 
ATOM   1201 N  NE2 . HIS   B 1 15  ? 24.708 -14.308 9.669  1.00 12.74 ? 21  HIS   C NE2 1 
ATOM   1202 N  N   . LEU   B 1 16  ? 20.497 -13.229 11.447 1.00 11.53 ? 22  LEU   C N   1 
ATOM   1203 C  CA  . LEU   B 1 16  ? 19.467 -13.976 10.712 1.00 11.98 ? 22  LEU   C CA  1 
ATOM   1204 C  C   . LEU   B 1 16  ? 18.087 -13.910 11.390 1.00 12.69 ? 22  LEU   C C   1 
ATOM   1205 O  O   . LEU   B 1 16  ? 17.149 -14.620 10.959 1.00 14.21 ? 22  LEU   C O   1 
ATOM   1206 C  CB  . LEU   B 1 16  ? 19.930 -15.423 10.518 1.00 12.81 ? 22  LEU   C CB  1 
ATOM   1207 C  CG  . LEU   B 1 16  ? 21.227 -15.563 9.709  1.00 13.46 ? 22  LEU   C CG  1 
ATOM   1208 C  CD1 . LEU   B 1 16  ? 21.659 -17.038 9.619  1.00 13.92 ? 22  LEU   C CD1 1 
ATOM   1209 C  CD2 . LEU   B 1 16  ? 21.093 -14.929 8.306  1.00 13.58 ? 22  LEU   C CD2 1 
ATOM   1210 N  N   . ALA   B 1 17  ? 17.947 -13.135 12.492 1.00 12.76 ? 23  ALA   C N   1 
ATOM   1211 C  CA  . ALA   B 1 17  ? 16.665 -13.078 13.211 1.00 12.81 ? 23  ALA   C CA  1 
ATOM   1212 C  C   . ALA   B 1 17  ? 15.548 -12.530 12.330 1.00 13.35 ? 23  ALA   C C   1 
ATOM   1213 O  O   . ALA   B 1 17  ? 15.765 -11.580 11.544 1.00 14.50 ? 23  ALA   C O   1 
ATOM   1214 C  CB  . ALA   B 1 17  ? 16.784 -12.213 14.462 1.00 13.84 ? 23  ALA   C CB  1 
ATOM   1215 N  N   . THR   B 1 18  ? 14.350 -13.121 12.475 1.00 13.54 ? 24  THR   C N   1 
ATOM   1216 C  CA  . THR   B 1 18  ? 13.178 -12.680 11.705 1.00 14.58 ? 24  THR   C CA  1 
ATOM   1217 C  C   . THR   B 1 18  ? 12.385 -11.593 12.470 1.00 15.21 ? 24  THR   C C   1 
ATOM   1218 O  O   . THR   B 1 18  ? 12.629 -11.310 13.651 1.00 15.45 ? 24  THR   C O   1 
ATOM   1219 C  CB  . THR   B 1 18  ? 12.254 -13.908 11.463 1.00 16.07 ? 24  THR   C CB  1 
ATOM   1220 O  OG1 . THR   B 1 18  ? 11.711 -14.324 12.708 1.00 16.53 ? 24  THR   C OG1 1 
ATOM   1221 C  CG2 . THR   B 1 18  ? 12.964 -15.075 10.774 1.00 17.62 ? 24  THR   C CG2 1 
ATOM   1222 N  N   . HIS   B 1 19  ? 11.331 -11.018 11.806 1.00 16.10 ? 25  HIS   C N   1 
ATOM   1223 C  CA  . HIS   B 1 19  ? 10.445 -10.082 12.512 1.00 16.63 ? 25  HIS   C CA  1 
ATOM   1224 C  C   . HIS   B 1 19  ? 9.752  -10.814 13.651 1.00 14.90 ? 25  HIS   C C   1 
ATOM   1225 O  O   . HIS   B 1 19  ? 9.663  -10.239 14.737 1.00 16.30 ? 25  HIS   C O   1 
ATOM   1226 C  CB  . HIS   B 1 19  ? 9.339  -9.563  11.558 1.00 18.24 ? 25  HIS   C CB  1 
ATOM   1227 C  CG  . HIS   B 1 19  ? 8.190  -8.872  12.265 1.00 20.65 ? 25  HIS   C CG  1 
ATOM   1228 N  ND1 . HIS   B 1 19  ? 8.329  -7.606  12.805 1.00 22.77 ? 25  HIS   C ND1 1 
ATOM   1229 C  CD2 . HIS   B 1 19  ? 6.972  -9.350  12.593 1.00 22.26 ? 25  HIS   C CD2 1 
ATOM   1230 C  CE1 . HIS   B 1 19  ? 7.138  -7.291  13.309 1.00 22.02 ? 25  HIS   C CE1 1 
ATOM   1231 N  NE2 . HIS   B 1 19  ? 6.300  -8.327  13.253 1.00 22.17 ? 25  HIS   C NE2 1 
ATOM   1232 N  N   . ASN   B 1 20  ? 9.310  -12.075 13.447 1.00 15.47 ? 26  ASN   C N   1 
ATOM   1233 C  CA  . ASN   B 1 20  ? 8.682  -12.811 14.540 1.00 16.21 ? 26  ASN   C CA  1 
ATOM   1234 C  C   . ASN   B 1 20  ? 9.620  -12.990 15.720 1.00 15.15 ? 26  ASN   C C   1 
ATOM   1235 O  O   . ASN   B 1 20  ? 9.182  -12.898 16.865 1.00 14.57 ? 26  ASN   C O   1 
ATOM   1236 C  CB  . ASN   B 1 20  ? 8.123  -14.176 14.087 1.00 18.35 ? 26  ASN   C CB  1 
ATOM   1237 C  CG  . ASN   B 1 20  ? 7.304  -14.843 15.182 1.00 24.46 ? 26  ASN   C CG  1 
ATOM   1238 O  OD1 . ASN   B 1 20  ? 6.195  -14.389 15.500 1.00 26.82 ? 26  ASN   C OD1 1 
ATOM   1239 N  ND2 . ASN   B 1 20  ? 7.858  -15.875 15.838 1.00 26.29 ? 26  ASN   C ND2 1 
ATOM   1240 N  N   . ASP   B 1 21  ? 10.938 -13.204 15.456 1.00 14.00 ? 27  ASP   C N   1 
ATOM   1241 C  CA  . ASP   B 1 21  ? 11.895 -13.299 16.547 1.00 14.03 ? 27  ASP   C CA  1 
ATOM   1242 C  C   . ASP   B 1 21  ? 11.936 -11.990 17.366 1.00 13.23 ? 27  ASP   C C   1 
ATOM   1243 O  O   . ASP   B 1 21  ? 11.882 -12.009 18.599 1.00 14.12 ? 27  ASP   C O   1 
ATOM   1244 C  CB  . ASP   B 1 21  ? 13.296 -13.600 16.018 1.00 13.46 ? 27  ASP   C CB  1 
ATOM   1245 C  CG  . ASP   B 1 21  ? 13.491 -15.017 15.541 1.00 14.00 ? 27  ASP   C CG  1 
ATOM   1246 O  OD1 . ASP   B 1 21  ? 12.914 -15.936 16.152 1.00 14.62 ? 27  ASP   C OD1 1 
ATOM   1247 O  OD2 . ASP   B 1 21  ? 14.183 -15.204 14.525 1.00 13.39 ? 27  ASP   C OD2 1 
ATOM   1248 N  N   . TRP   B 1 22  ? 12.034 -10.832 16.668 1.00 14.02 ? 28  TRP   C N   1 
ATOM   1249 C  CA  . TRP   B 1 22  ? 12.085 -9.537  17.350 1.00 14.74 ? 28  TRP   C CA  1 
ATOM   1250 C  C   . TRP   B 1 22  ? 10.751 -9.201  18.063 1.00 14.66 ? 28  TRP   C C   1 
ATOM   1251 O  O   . TRP   B 1 22  ? 10.771 -8.563  19.115 1.00 15.32 ? 28  TRP   C O   1 
ATOM   1252 C  CB  . TRP   B 1 22  ? 12.456 -8.422  16.372 1.00 14.44 ? 28  TRP   C CB  1 
ATOM   1253 C  CG  . TRP   B 1 22  ? 13.938 -8.393  16.098 1.00 13.90 ? 28  TRP   C CG  1 
ATOM   1254 C  CD1 . TRP   B 1 22  ? 14.581 -8.872  14.988 1.00 15.10 ? 28  TRP   C CD1 1 
ATOM   1255 C  CD2 . TRP   B 1 22  ? 14.958 -7.799  16.930 1.00 12.89 ? 28  TRP   C CD2 1 
ATOM   1256 N  NE1 . TRP   B 1 22  ? 15.940 -8.616  15.079 1.00 15.40 ? 28  TRP   C NE1 1 
ATOM   1257 C  CE2 . TRP   B 1 22  ? 16.195 -7.968  16.266 1.00 14.17 ? 28  TRP   C CE2 1 
ATOM   1258 C  CE3 . TRP   B 1 22  ? 14.941 -7.107  18.147 1.00 14.94 ? 28  TRP   C CE3 1 
ATOM   1259 C  CZ2 . TRP   B 1 22  ? 17.373 -7.413  16.741 1.00 14.23 ? 28  TRP   C CZ2 1 
ATOM   1260 C  CZ3 . TRP   B 1 22  ? 16.127 -6.600  18.641 1.00 16.04 ? 28  TRP   C CZ3 1 
ATOM   1261 C  CH2 . TRP   B 1 22  ? 17.328 -6.766  17.935 1.00 15.54 ? 28  TRP   C CH2 1 
ATOM   1262 N  N   . ALA   B 1 23  ? 9.626  -9.668  17.521 1.00 14.51 ? 29  ALA   C N   1 
ATOM   1263 C  CA  . ALA   B 1 23  ? 8.306  -9.429  18.130 1.00 15.91 ? 29  ALA   C CA  1 
ATOM   1264 C  C   . ALA   B 1 23  ? 8.069  -10.309 19.370 1.00 16.94 ? 29  ALA   C C   1 
ATOM   1265 O  O   . ALA   B 1 23  ? 7.100  -10.115 20.110 1.00 17.56 ? 29  ALA   C O   1 
ATOM   1266 C  CB  . ALA   B 1 23  ? 7.210  -9.684  17.107 1.00 16.54 ? 29  ALA   C CB  1 
ATOM   1267 N  N   . ASN   B 1 24  ? 8.934  -11.347 19.574 1.00 16.07 ? 30  ASN   C N   1 
ATOM   1268 C  CA  . ASN   B 1 24  ? 8.817  -12.266 20.709 1.00 15.24 ? 30  ASN   C CA  1 
ATOM   1269 C  C   . ASN   B 1 24  ? 10.191 -12.333 21.401 1.00 14.68 ? 30  ASN   C C   1 
ATOM   1270 O  O   . ASN   B 1 24  ? 10.626 -13.404 21.818 1.00 14.15 ? 30  ASN   C O   1 
ATOM   1271 C  CB  . ASN   B 1 24  ? 8.349  -13.654 20.175 1.00 16.69 ? 30  ASN   C CB  1 
ATOM   1272 C  CG  . ASN   B 1 24  ? 6.903  -13.586 19.712 1.00 18.43 ? 30  ASN   C CG  1 
ATOM   1273 O  OD1 . ASN   B 1 24  ? 5.945  -13.614 20.539 1.00 19.53 ? 30  ASN   C OD1 1 
ATOM   1274 N  ND2 . ASN   B 1 24  ? 6.711  -13.483 18.398 1.00 19.42 ? 30  ASN   C ND2 1 
ATOM   1275 N  N   . LEU   B 1 25  ? 10.885 -11.204 21.504 1.00 14.70 ? 31  LEU   C N   1 
ATOM   1276 C  CA  . LEU   B 1 25  ? 12.270 -11.191 21.981 1.00 14.13 ? 31  LEU   C CA  1 
ATOM   1277 C  C   . LEU   B 1 25  ? 12.405 -11.519 23.449 1.00 15.43 ? 31  LEU   C C   1 
ATOM   1278 O  O   . LEU   B 1 25  ? 11.638 -11.012 24.283 1.00 16.92 ? 31  LEU   C O   1 
ATOM   1279 C  CB  . LEU   B 1 25  ? 12.843 -9.780  21.716 1.00 14.67 ? 31  LEU   C CB  1 
ATOM   1280 C  CG  . LEU   B 1 25  ? 14.312 -9.596  22.075 1.00 14.62 ? 31  LEU   C CG  1 
ATOM   1281 C  CD1 . LEU   B 1 25  ? 15.223 -10.470 21.168 1.00 15.29 ? 31  LEU   C CD1 1 
ATOM   1282 C  CD2 . LEU   B 1 25  ? 14.705 -8.141  21.953 1.00 16.08 ? 31  LEU   C CD2 1 
ATOM   1283 N  N   . VAL   B 1 26  ? 13.397 -12.360 23.777 1.00 14.09 ? 32  VAL   C N   1 
ATOM   1284 C  CA  . VAL   B 1 26  ? 13.743 -12.638 25.164 1.00 14.73 ? 32  VAL   C CA  1 
ATOM   1285 C  C   . VAL   B 1 26  ? 15.070 -11.929 25.486 1.00 15.05 ? 32  VAL   C C   1 
ATOM   1286 O  O   . VAL   B 1 26  ? 15.185 -11.253 26.519 1.00 16.37 ? 32  VAL   C O   1 
ATOM   1287 C  CB  . VAL   B 1 26  ? 13.883 -14.162 25.388 1.00 14.81 ? 32  VAL   C CB  1 
ATOM   1288 C  CG1 . VAL   B 1 26  ? 14.462 -14.464 26.771 1.00 17.24 ? 32  VAL   C CG1 1 
ATOM   1289 C  CG2 . VAL   B 1 26  ? 12.537 -14.860 25.209 1.00 15.34 ? 32  VAL   C CG2 1 
ATOM   1290 N  N   . TRP   B 1 27  ? 16.085 -12.059 24.598 1.00 13.16 ? 33  TRP   C N   1 
ATOM   1291 C  CA  . TRP   B 1 27  ? 17.396 -11.489 24.876 1.00 13.44 ? 33  TRP   C CA  1 
ATOM   1292 C  C   . TRP   B 1 27  ? 18.197 -11.426 23.568 1.00 13.08 ? 33  TRP   C C   1 
ATOM   1293 O  O   . TRP   B 1 27  ? 18.012 -12.314 22.710 1.00 13.06 ? 33  TRP   C O   1 
ATOM   1294 C  CB  . TRP   B 1 27  ? 18.146 -12.387 25.904 1.00 14.84 ? 33  TRP   C CB  1 
ATOM   1295 C  CG  . TRP   B 1 27  ? 19.628 -12.124 26.093 1.00 15.16 ? 33  TRP   C CG  1 
ATOM   1296 C  CD1 . TRP   B 1 27  ? 20.212 -11.149 26.861 1.00 17.28 ? 33  TRP   C CD1 1 
ATOM   1297 C  CD2 . TRP   B 1 27  ? 20.713 -12.832 25.458 1.00 13.84 ? 33  TRP   C CD2 1 
ATOM   1298 N  NE1 . TRP   B 1 27  ? 21.602 -11.240 26.777 1.00 17.62 ? 33  TRP   C NE1 1 
ATOM   1299 C  CE2 . TRP   B 1 27  ? 21.923 -12.274 25.930 1.00 15.30 ? 33  TRP   C CE2 1 
ATOM   1300 C  CE3 . TRP   B 1 27  ? 20.781 -13.892 24.529 1.00 14.14 ? 33  TRP   C CE3 1 
ATOM   1301 C  CZ2 . TRP   B 1 27  ? 23.179 -12.770 25.542 1.00 15.11 ? 33  TRP   C CZ2 1 
ATOM   1302 C  CZ3 . TRP   B 1 27  ? 22.031 -14.379 24.161 1.00 15.70 ? 33  TRP   C CZ3 1 
ATOM   1303 C  CH2 . TRP   B 1 27  ? 23.199 -13.788 24.633 1.00 15.60 ? 33  TRP   C CH2 1 
ATOM   1304 N  N   . GLU   B 1 28  ? 19.062 -10.437 23.401 1.00 12.59 ? 34  GLU   C N   1 
ATOM   1305 C  CA  . GLU   B 1 28  ? 19.911 -10.356 22.215 1.00 12.88 ? 34  GLU   C CA  1 
ATOM   1306 C  C   . GLU   B 1 28  ? 21.198 -9.675  22.560 1.00 12.79 ? 34  GLU   C C   1 
ATOM   1307 O  O   . GLU   B 1 28  ? 21.223 -8.787  23.445 1.00 13.45 ? 34  GLU   C O   1 
ATOM   1308 C  CB  . GLU   B 1 28  ? 19.226 -9.659  21.038 1.00 13.99 ? 34  GLU   C CB  1 
ATOM   1309 C  CG  . GLU   B 1 28  ? 18.656 -8.289  21.340 1.00 14.50 ? 34  GLU   C CG  1 
ATOM   1310 C  CD  . GLU   B 1 28  ? 19.623 -7.123  21.260 1.00 16.44 ? 34  GLU   C CD  1 
ATOM   1311 O  OE1 . GLU   B 1 28  ? 19.369 -6.097  21.934 1.00 18.97 ? 34  GLU   C OE1 1 
ATOM   1312 O  OE2 . GLU   B 1 28  ? 20.622 -7.214  20.506 1.00 15.50 ? 34  GLU   C OE2 1 
ATOM   1313 N  N   . ASP   B 1 29  ? 22.280 -10.028 21.856 1.00 12.36 ? 35  ASP   C N   1 
ATOM   1314 C  CA  . ASP   B 1 29  ? 23.571 -9.391  22.089 1.00 12.29 ? 35  ASP   C CA  1 
ATOM   1315 C  C   . ASP   B 1 29  ? 24.341 -9.359  20.750 1.00 12.08 ? 35  ASP   C C   1 
ATOM   1316 O  O   . ASP   B 1 29  ? 24.784 -10.401 20.258 1.00 12.22 ? 35  ASP   C O   1 
ATOM   1317 C  CB  . ASP   B 1 29  ? 24.326 -10.173 23.183 1.00 13.60 ? 35  ASP   C CB  1 
ATOM   1318 C  CG  . ASP   B 1 29  ? 25.659 -9.597  23.575 1.00 18.28 ? 35  ASP   C CG  1 
ATOM   1319 O  OD1 . ASP   B 1 29  ? 26.385 -9.138  22.692 1.00 19.19 ? 35  ASP   C OD1 1 
ATOM   1320 O  OD2 . ASP   B 1 29  ? 26.035 -9.734  24.746 1.00 19.83 ? 35  ASP   C OD2 1 
ATOM   1321 N  N   . SER   B 1 30  ? 24.501 -8.151  20.166 1.00 12.08 ? 36  SER   C N   1 
ATOM   1322 C  CA  A SER   B 1 30  ? 25.203 -7.974  18.894 0.50 12.32 ? 36  SER   C CA  1 
ATOM   1323 C  CA  B SER   B 1 30  ? 25.185 -8.035  18.884 0.50 12.30 ? 36  SER   C CA  1 
ATOM   1324 C  C   . SER   B 1 30  ? 26.655 -8.433  18.985 1.00 12.74 ? 36  SER   C C   1 
ATOM   1325 O  O   . SER   B 1 30  ? 27.170 -9.044  18.023 1.00 12.64 ? 36  SER   C O   1 
ATOM   1326 C  CB  A SER   B 1 30  ? 25.143 -6.516  18.440 0.50 14.39 ? 36  SER   C CB  1 
ATOM   1327 C  CB  B SER   B 1 30  ? 25.018 -6.643  18.295 0.50 14.22 ? 36  SER   C CB  1 
ATOM   1328 O  OG  A SER   B 1 30  ? 26.017 -6.267  17.344 0.50 14.56 ? 36  SER   C OG  1 
ATOM   1329 O  OG  B SER   B 1 30  ? 25.516 -5.693  19.217 0.50 14.66 ? 36  SER   C OG  1 
ATOM   1330 N  N   . SER   B 1 31  ? 27.329 -8.158  20.135 1.00 12.88 ? 37  SER   C N   1 
ATOM   1331 C  CA  . SER   B 1 31  ? 28.740 -8.566  20.229 1.00 13.13 ? 37  SER   C CA  1 
ATOM   1332 C  C   . SER   B 1 31  ? 28.920 -10.074 20.180 1.00 12.39 ? 37  SER   C C   1 
ATOM   1333 O  O   . SER   B 1 31  ? 30.016 -10.522 19.818 1.00 13.18 ? 37  SER   C O   1 
ATOM   1334 C  CB  . SER   B 1 31  ? 29.375 -8.019  21.494 1.00 15.53 ? 37  SER   C CB  1 
ATOM   1335 O  OG  . SER   B 1 31  ? 28.972 -8.693  22.663 1.00 20.87 ? 37  SER   C OG  1 
ATOM   1336 N  N   . ARG   B 1 32  ? 27.870 -10.864 20.513 1.00 11.19 ? 38  ARG   C N   1 
ATOM   1337 C  CA  . ARG   B 1 32  ? 27.947 -12.333 20.462 1.00 11.08 ? 38  ARG   C CA  1 
ATOM   1338 C  C   . ARG   B 1 32  ? 27.303 -12.903 19.175 1.00 10.57 ? 38  ARG   C C   1 
ATOM   1339 O  O   . ARG   B 1 32  ? 27.339 -14.124 18.952 1.00 10.28 ? 38  ARG   C O   1 
ATOM   1340 C  CB  . ARG   B 1 32  ? 27.201 -12.932 21.684 1.00 12.60 ? 38  ARG   C CB  1 
ATOM   1341 C  CG  . ARG   B 1 32  ? 27.864 -12.593 23.003 1.00 14.01 ? 38  ARG   C CG  1 
ATOM   1342 C  CD  . ARG   B 1 32  ? 27.103 -13.154 24.207 1.00 11.63 ? 38  ARG   C CD  1 
ATOM   1343 N  NE  . ARG   B 1 32  ? 27.161 -14.632 24.234 1.00 11.08 ? 38  ARG   C NE  1 
ATOM   1344 C  CZ  . ARG   B 1 32  ? 27.169 -15.373 25.344 1.00 11.67 ? 38  ARG   C CZ  1 
ATOM   1345 N  NH1 . ARG   B 1 32  ? 27.091 -14.799 26.539 1.00 13.02 ? 38  ARG   C NH1 1 
ATOM   1346 N  NH2 . ARG   B 1 32  ? 27.323 -16.699 25.267 1.00 11.49 ? 38  ARG   C NH2 1 
ATOM   1347 N  N   . ASP   B 1 33  ? 26.632 -12.048 18.362 1.00 9.83  ? 39  ASP   C N   1 
ATOM   1348 C  CA  . ASP   B 1 33  ? 25.850 -12.511 17.216 1.00 9.97  ? 39  ASP   C CA  1 
ATOM   1349 C  C   . ASP   B 1 33  ? 24.748 -13.475 17.647 1.00 9.87  ? 39  ASP   C C   1 
ATOM   1350 O  O   . ASP   B 1 33  ? 24.436 -14.413 16.907 1.00 10.18 ? 39  ASP   C O   1 
ATOM   1351 C  CB  . ASP   B 1 33  ? 26.685 -13.131 16.091 1.00 10.46 ? 39  ASP   C CB  1 
ATOM   1352 C  CG  . ASP   B 1 33  ? 25.907 -13.464 14.824 1.00 11.28 ? 39  ASP   C CG  1 
ATOM   1353 O  OD1 . ASP   B 1 33  ? 25.011 -12.665 14.440 1.00 12.06 ? 39  ASP   C OD1 1 
ATOM   1354 O  OD2 . ASP   B 1 33  ? 26.205 -14.498 14.203 1.00 10.22 ? 39  ASP   C OD2 1 
ATOM   1355 N  N   . LEU   B 1 34  ? 24.104 -13.248 18.834 1.00 9.85  ? 40  LEU   C N   1 
ATOM   1356 C  CA  . LEU   B 1 34  ? 23.021 -14.139 19.288 1.00 10.36 ? 40  LEU   C CA  1 
ATOM   1357 C  C   . LEU   B 1 34  ? 21.726 -13.390 19.545 1.00 10.38 ? 40  LEU   C C   1 
ATOM   1358 O  O   . LEU   B 1 34  ? 21.738 -12.229 20.023 1.00 11.42 ? 40  LEU   C O   1 
ATOM   1359 C  CB  . LEU   B 1 34  ? 23.391 -14.860 20.589 1.00 10.82 ? 40  LEU   C CB  1 
ATOM   1360 C  CG  . LEU   B 1 34  ? 24.469 -15.965 20.492 1.00 11.01 ? 40  LEU   C CG  1 
ATOM   1361 C  CD1 . LEU   B 1 34  ? 24.712 -16.573 21.895 1.00 12.05 ? 40  LEU   C CD1 1 
ATOM   1362 C  CD2 . LEU   B 1 34  ? 24.038 -17.092 19.512 1.00 11.88 ? 40  LEU   C CD2 1 
ATOM   1363 N  N   . LEU   B 1 35  ? 20.616 -14.085 19.312 1.00 9.80  ? 41  LEU   C N   1 
ATOM   1364 C  CA  . LEU   B 1 35  ? 19.281 -13.586 19.667 1.00 10.71 ? 41  LEU   C CA  1 
ATOM   1365 C  C   . LEU   B 1 35  ? 18.440 -14.795 20.095 1.00 10.49 ? 41  LEU   C C   1 
ATOM   1366 O  O   . LEU   B 1 35  ? 18.527 -15.866 19.477 1.00 11.48 ? 41  LEU   C O   1 
ATOM   1367 C  CB  . LEU   B 1 35  ? 18.638 -12.825 18.483 1.00 10.83 ? 41  LEU   C CB  1 
ATOM   1368 C  CG  . LEU   B 1 35  ? 17.238 -12.242 18.756 1.00 10.82 ? 41  LEU   C CG  1 
ATOM   1369 C  CD1 . LEU   B 1 35  ? 17.034 -10.924 17.994 1.00 13.09 ? 41  LEU   C CD1 1 
ATOM   1370 C  CD2 . LEU   B 1 35  ? 16.144 -13.257 18.398 1.00 11.06 ? 41  LEU   C CD2 1 
ATOM   1371 N  N   . VAL   B 1 36  ? 17.668 -14.622 21.175 1.00 11.00 ? 42  VAL   C N   1 
ATOM   1372 C  CA  . VAL   B 1 36  ? 16.756 -15.631 21.697 1.00 10.75 ? 42  VAL   C CA  1 
ATOM   1373 C  C   . VAL   B 1 36  ? 15.330 -15.096 21.699 1.00 10.88 ? 42  VAL   C C   1 
ATOM   1374 O  O   . VAL   B 1 36  ? 15.103 -13.968 22.192 1.00 12.32 ? 42  VAL   C O   1 
ATOM   1375 C  CB  . VAL   B 1 36  ? 17.191 -16.096 23.107 1.00 11.82 ? 42  VAL   C CB  1 
ATOM   1376 C  CG1 . VAL   B 1 36  ? 16.221 -17.141 23.655 1.00 12.67 ? 42  VAL   C CG1 1 
ATOM   1377 C  CG2 . VAL   B 1 36  ? 18.619 -16.662 23.069 1.00 12.64 ? 42  VAL   C CG2 1 
ATOM   1378 N  N   . SER   B 1 37  ? 14.406 -15.852 21.123 1.00 11.60 ? 43  SER   C N   1 
ATOM   1379 C  CA  . SER   B 1 37  ? 13.004 -15.488 21.103 1.00 11.97 ? 43  SER   C CA  1 
ATOM   1380 C  C   . SER   B 1 37  ? 12.189 -16.584 21.807 1.00 12.27 ? 43  SER   C C   1 
ATOM   1381 O  O   . SER   B 1 37  ? 12.682 -17.718 22.032 1.00 12.35 ? 43  SER   C O   1 
ATOM   1382 C  CB  . SER   B 1 37  ? 12.508 -15.270 19.669 1.00 12.73 ? 43  SER   C CB  1 
ATOM   1383 O  OG  . SER   B 1 37  ? 12.687 -16.437 18.877 1.00 13.73 ? 43  SER   C OG  1 
ATOM   1384 N  N   . SER   B 1 38  ? 10.930 -16.262 22.167 1.00 13.15 ? 44  SER   C N   1 
ATOM   1385 C  CA  . SER   B 1 38  ? 10.058 -17.226 22.822 1.00 14.57 ? 44  SER   C CA  1 
ATOM   1386 C  C   . SER   B 1 38  ? 9.227  -18.016 21.802 1.00 16.43 ? 44  SER   C C   1 
ATOM   1387 O  O   . SER   B 1 38  ? 8.920  -17.521 20.716 1.00 16.98 ? 44  SER   C O   1 
ATOM   1388 C  CB  . SER   B 1 38  ? 9.173  -16.499 23.834 1.00 17.12 ? 44  SER   C CB  1 
ATOM   1389 O  OG  . SER   B 1 38  ? 8.342  -15.574 23.158 1.00 21.08 ? 44  SER   C OG  1 
ATOM   1390 N  N   . THR   B 1 39  ? 8.888  -19.260 22.150 1.00 15.98 ? 45  THR   C N   1 
ATOM   1391 C  CA  . THR   B 1 39  ? 8.122  -20.141 21.265 1.00 16.59 ? 45  THR   C CA  1 
ATOM   1392 C  C   . THR   B 1 39  ? 6.830  -20.607 21.966 1.00 19.11 ? 45  THR   C C   1 
ATOM   1393 O  O   . THR   B 1 39  ? 6.777  -20.674 23.180 1.00 19.10 ? 45  THR   C O   1 
ATOM   1394 C  CB  . THR   B 1 39  ? 8.955  -21.399 20.880 1.00 17.47 ? 45  THR   C CB  1 
ATOM   1395 O  OG1 . THR   B 1 39  ? 9.222  -22.172 22.053 1.00 17.67 ? 45  THR   C OG1 1 
ATOM   1396 C  CG2 . THR   B 1 39  ? 10.303 -21.047 20.190 1.00 17.94 ? 45  THR   C CG2 1 
ATOM   1397 N  N   . THR   B 1 40  ? 5.833  -20.985 21.175 1.00 21.16 ? 46  THR   C N   1 
ATOM   1398 C  CA  . THR   B 1 40  ? 4.590  -21.531 21.721 1.00 22.96 ? 46  THR   C CA  1 
ATOM   1399 C  C   . THR   B 1 40  ? 4.797  -23.003 22.066 1.00 22.98 ? 46  THR   C C   1 
ATOM   1400 O  O   . THR   B 1 40  ? 4.429  -23.446 23.162 1.00 25.19 ? 46  THR   C O   1 
ATOM   1401 C  CB  . THR   B 1 40  ? 3.446  -21.289 20.742 1.00 27.60 ? 46  THR   C CB  1 
ATOM   1402 O  OG1 . THR   B 1 40  ? 3.779  -21.895 19.504 1.00 32.57 ? 46  THR   C OG1 1 
ATOM   1403 C  CG2 . THR   B 1 40  ? 3.215  -19.822 20.484 1.00 26.96 ? 46  THR   C CG2 1 
ATOM   1404 N  N   . ALA   B 1 41  ? 5.470  -23.752 21.162 1.00 20.55 ? 47  ALA   C N   1 
ATOM   1405 C  CA  . ALA   B 1 41  ? 5.721  -25.159 21.407 1.00 20.56 ? 47  ALA   C CA  1 
ATOM   1406 C  C   . ALA   B 1 41  ? 7.051  -25.410 22.104 1.00 18.99 ? 47  ALA   C C   1 
ATOM   1407 O  O   . ALA   B 1 41  ? 7.985  -24.635 21.932 1.00 18.79 ? 47  ALA   C O   1 
ATOM   1408 C  CB  . ALA   B 1 41  ? 5.694  -25.921 20.088 1.00 22.48 ? 47  ALA   C CB  1 
ATOM   1409 N  N   . GLN   B 1 42  ? 7.151  -26.471 22.884 1.00 17.97 ? 48  GLN   C N   1 
ATOM   1410 C  CA  . GLN   B 1 42  ? 8.395  -26.842 23.554 1.00 18.72 ? 48  GLN   C CA  1 
ATOM   1411 C  C   . GLN   B 1 42  ? 9.393  -27.467 22.554 1.00 18.00 ? 48  GLN   C C   1 
ATOM   1412 O  O   . GLN   B 1 42  ? 8.991  -28.230 21.661 1.00 19.50 ? 48  GLN   C O   1 
ATOM   1413 C  CB  . GLN   B 1 42  ? 8.119  -27.798 24.722 1.00 23.09 ? 48  GLN   C CB  1 
ATOM   1414 C  CG  . GLN   B 1 42  ? 7.540  -27.059 25.940 1.00 31.61 ? 48  GLN   C CG  1 
ATOM   1415 C  CD  . GLN   B 1 42  ? 7.348  -28.018 27.089 1.00 41.54 ? 48  GLN   C CD  1 
ATOM   1416 O  OE1 . GLN   B 1 42  ? 6.484  -28.897 27.057 1.00 45.81 ? 48  GLN   C OE1 1 
ATOM   1417 N  NE2 . GLN   B 1 42  ? 8.142  -27.875 28.136 1.00 43.64 ? 48  GLN   C NE2 1 
ATOM   1418 N  N   . GLY   B 1 43  ? 10.665 -27.129 22.714 1.00 15.73 ? 49  GLY   C N   1 
ATOM   1419 C  CA  . GLY   B 1 43  ? 11.761 -27.681 21.912 1.00 15.44 ? 49  GLY   C CA  1 
ATOM   1420 C  C   . GLY   B 1 43  ? 12.417 -28.854 22.624 1.00 15.13 ? 49  GLY   C C   1 
ATOM   1421 O  O   . GLY   B 1 43  ? 12.176 -29.075 23.828 1.00 18.16 ? 49  GLY   C O   1 
ATOM   1422 N  N   . CYS   B 1 44  ? 13.245 -29.579 21.916 1.00 13.48 ? 50  CYS   C N   1 
ATOM   1423 C  CA  . CYS   B 1 44  ? 13.811 -30.802 22.473 1.00 14.27 ? 50  CYS   C CA  1 
ATOM   1424 C  C   . CYS   B 1 44  ? 15.309 -30.858 22.526 1.00 15.47 ? 50  CYS   C C   1 
ATOM   1425 O  O   . CYS   B 1 44  ? 15.860 -31.916 22.873 1.00 17.66 ? 50  CYS   C O   1 
ATOM   1426 C  CB  . CYS   B 1 44  ? 13.256 -31.995 21.698 1.00 14.78 ? 50  CYS   C CB  1 
ATOM   1427 S  SG  . CYS   B 1 44  ? 11.437 -32.022 21.659 1.00 19.25 ? 50  CYS   C SG  1 
ATOM   1428 N  N   . ASP   B 1 45  ? 16.007 -29.774 22.173 1.00 12.87 ? 51  ASP   C N   1 
ATOM   1429 C  CA  . ASP   B 1 45  ? 17.466 -29.781 22.230 1.00 12.48 ? 51  ASP   C CA  1 
ATOM   1430 C  C   . ASP   B 1 45  ? 17.888 -29.604 23.695 1.00 13.43 ? 51  ASP   C C   1 
ATOM   1431 O  O   . ASP   B 1 45  ? 17.188 -28.934 24.489 1.00 15.72 ? 51  ASP   C O   1 
ATOM   1432 C  CB  . ASP   B 1 45  ? 18.042 -28.625 21.387 1.00 13.67 ? 51  ASP   C CB  1 
ATOM   1433 C  CG  . ASP   B 1 45  ? 17.865 -28.785 19.886 1.00 15.56 ? 51  ASP   C CG  1 
ATOM   1434 O  OD1 . ASP   B 1 45  ? 17.877 -29.938 19.399 1.00 16.51 ? 51  ASP   C OD1 1 
ATOM   1435 O  OD2 . ASP   B 1 45  ? 17.696 -27.760 19.191 1.00 13.50 ? 51  ASP   C OD2 1 
ATOM   1436 N  N   . THR   B 1 46  ? 19.014 -30.225 24.055 1.00 12.12 ? 52  THR   C N   1 
ATOM   1437 C  CA  . THR   B 1 46  ? 19.607 -30.040 25.373 1.00 12.27 ? 52  THR   C CA  1 
ATOM   1438 C  C   . THR   B 1 46  ? 20.883 -29.194 25.195 1.00 12.71 ? 52  THR   C C   1 
ATOM   1439 O  O   . THR   B 1 46  ? 21.699 -29.492 24.313 1.00 13.01 ? 52  THR   C O   1 
ATOM   1440 C  CB  . THR   B 1 46  ? 20.018 -31.403 25.943 1.00 14.62 ? 52  THR   C CB  1 
ATOM   1441 O  OG1 . THR   B 1 46  ? 18.844 -32.222 26.126 1.00 17.13 ? 52  THR   C OG1 1 
ATOM   1442 C  CG2 . THR   B 1 46  ? 20.812 -31.293 27.293 1.00 16.66 ? 52  THR   C CG2 1 
ATOM   1443 N  N   . ILE   B 1 47  ? 21.060 -28.169 26.028 1.00 12.20 ? 53  ILE   C N   1 
ATOM   1444 C  CA  . ILE   B 1 47  ? 22.273 -27.353 25.973 1.00 11.82 ? 53  ILE   C CA  1 
ATOM   1445 C  C   . ILE   B 1 47  ? 23.369 -28.035 26.816 1.00 10.76 ? 53  ILE   C C   1 
ATOM   1446 O  O   . ILE   B 1 47  ? 23.140 -28.462 27.958 1.00 12.09 ? 53  ILE   C O   1 
ATOM   1447 C  CB  . ILE   B 1 47  ? 22.005 -25.965 26.575 1.00 12.33 ? 53  ILE   C CB  1 
ATOM   1448 C  CG1 . ILE   B 1 47  ? 20.804 -25.281 25.937 1.00 13.19 ? 53  ILE   C CG1 1 
ATOM   1449 C  CG2 . ILE   B 1 47  ? 23.271 -25.111 26.489 1.00 13.49 ? 53  ILE   C CG2 1 
ATOM   1450 C  CD1 . ILE   B 1 47  ? 21.004 -25.117 24.363 1.00 15.16 ? 53  ILE   C CD1 1 
ATOM   1451 N  N   . ALA   B 1 48  ? 24.568 -28.107 26.268 1.00 10.33 ? 54  ALA   C N   1 
ATOM   1452 C  CA  . ALA   B 1 48  ? 25.710 -28.661 26.997 1.00 10.55 ? 54  ALA   C CA  1 
ATOM   1453 C  C   . ALA   B 1 48  ? 26.069 -27.755 28.171 1.00 10.35 ? 54  ALA   C C   1 
ATOM   1454 O  O   . ALA   B 1 48  ? 26.048 -26.507 28.026 1.00 10.75 ? 54  ALA   C O   1 
ATOM   1455 C  CB  . ALA   B 1 48  ? 26.917 -28.746 26.062 1.00 10.38 ? 54  ALA   C CB  1 
ATOM   1456 N  N   . ARG   B 1 49  ? 26.455 -28.352 29.307 1.00 9.89  ? 55  ARG   C N   1 
ATOM   1457 C  CA  . ARG   B 1 49  ? 26.901 -27.593 30.477 1.00 10.00 ? 55  ARG   C CA  1 
ATOM   1458 C  C   . ARG   B 1 49  ? 28.228 -28.246 30.845 1.00 10.87 ? 55  ARG   C C   1 
ATOM   1459 O  O   . ARG   B 1 49  ? 28.255 -29.286 31.532 1.00 12.40 ? 55  ARG   C O   1 
ATOM   1460 C  CB  . ARG   B 1 49  ? 25.870 -27.613 31.636 1.00 10.79 ? 55  ARG   C CB  1 
ATOM   1461 C  CG  . ARG   B 1 49  ? 24.490 -27.068 31.220 1.00 10.05 ? 55  ARG   C CG  1 
ATOM   1462 C  CD  . ARG   B 1 49  ? 24.513 -25.589 30.846 1.00 11.81 ? 55  ARG   C CD  1 
ATOM   1463 N  NE  . ARG   B 1 49  ? 23.153 -25.150 30.491 1.00 11.85 ? 55  ARG   C NE  1 
ATOM   1464 C  CZ  . ARG   B 1 49  ? 22.900 -24.043 29.782 1.00 12.02 ? 55  ARG   C CZ  1 
ATOM   1465 N  NH1 . ARG   B 1 49  ? 23.884 -23.211 29.454 1.00 12.35 ? 55  ARG   C NH1 1 
ATOM   1466 N  NH2 . ARG   B 1 49  ? 21.646 -23.731 29.444 1.00 13.05 ? 55  ARG   C NH2 1 
ATOM   1467 N  N   . CYS   B 1 50  ? 29.328 -27.658 30.344 1.00 10.89 ? 56  CYS   C N   1 
ATOM   1468 C  CA  . CYS   B 1 50  ? 30.650 -28.296 30.371 1.00 9.61  ? 56  CYS   C CA  1 
ATOM   1469 C  C   . CYS   B 1 50  ? 31.709 -27.334 29.853 1.00 10.20 ? 56  CYS   C C   1 
ATOM   1470 O  O   . CYS   B 1 50  ? 31.393 -26.233 29.385 1.00 11.15 ? 56  CYS   C O   1 
ATOM   1471 C  CB  . CYS   B 1 50  ? 30.599 -29.518 29.436 1.00 9.68  ? 56  CYS   C CB  1 
ATOM   1472 S  SG  . CYS   B 1 50  ? 30.444 -29.078 27.664 1.00 10.70 ? 56  CYS   C SG  1 
ATOM   1473 N  N   . ASP   B 1 51  ? 32.991 -27.811 29.868 1.00 11.53 ? 57  ASP   C N   1 
ATOM   1474 C  CA  . ASP   B 1 51  ? 34.116 -27.084 29.281 1.00 12.20 ? 57  ASP   C CA  1 
ATOM   1475 C  C   . ASP   B 1 51  ? 34.782 -27.936 28.176 1.00 12.72 ? 57  ASP   C C   1 
ATOM   1476 O  O   . ASP   B 1 51  ? 35.968 -27.796 27.925 1.00 13.45 ? 57  ASP   C O   1 
ATOM   1477 C  CB  . ASP   B 1 51  ? 35.139 -26.651 30.339 1.00 14.78 ? 57  ASP   C CB  1 
ATOM   1478 C  CG  . ASP   B 1 51  ? 35.828 -27.776 31.044 1.00 19.46 ? 57  ASP   C CG  1 
ATOM   1479 O  OD1 . ASP   B 1 51  ? 35.477 -28.936 30.792 1.00 18.43 ? 57  ASP   C OD1 1 
ATOM   1480 O  OD2 . ASP   B 1 51  ? 36.756 -27.491 31.845 1.00 26.02 ? 57  ASP   C OD2 1 
ATOM   1481 N  N   . CYS   B 1 52  ? 34.006 -28.787 27.466 1.00 11.35 ? 58  CYS   C N   1 
ATOM   1482 C  CA  . CYS   B 1 52  ? 34.560 -29.566 26.331 1.00 10.75 ? 58  CYS   C CA  1 
ATOM   1483 C  C   . CYS   B 1 52  ? 35.226 -28.663 25.307 1.00 10.26 ? 58  CYS   C C   1 
ATOM   1484 O  O   . CYS   B 1 52  ? 34.784 -27.517 25.083 1.00 10.71 ? 58  CYS   C O   1 
ATOM   1485 C  CB  . CYS   B 1 52  ? 33.469 -30.377 25.631 1.00 11.07 ? 58  CYS   C CB  1 
ATOM   1486 S  SG  . CYS   B 1 52  ? 32.870 -31.793 26.562 1.00 11.59 ? 58  CYS   C SG  1 
ATOM   1487 N  N   . GLN   B 1 53  ? 36.284 -29.175 24.704 1.00 10.07 ? 59  GLN   C N   1 
ATOM   1488 C  CA  . GLN   B 1 53  ? 36.960 -28.572 23.562 1.00 10.67 ? 59  GLN   C CA  1 
ATOM   1489 C  C   . GLN   B 1 53  ? 37.008 -29.503 22.364 1.00 11.26 ? 59  GLN   C C   1 
ATOM   1490 O  O   . GLN   B 1 53  ? 37.772 -29.259 21.419 1.00 11.33 ? 59  GLN   C O   1 
ATOM   1491 C  CB  . GLN   B 1 53  ? 38.387 -28.087 23.900 1.00 11.58 ? 59  GLN   C CB  1 
ATOM   1492 C  CG  . GLN   B 1 53  ? 38.408 -26.834 24.798 1.00 15.99 ? 59  GLN   C CG  1 
ATOM   1493 C  CD  . GLN   B 1 53  ? 39.793 -26.274 24.986 1.00 18.24 ? 59  GLN   C CD  1 
ATOM   1494 O  OE1 . GLN   B 1 53  ? 40.316 -26.311 26.118 1.00 18.71 ? 59  GLN   C OE1 1 
ATOM   1495 N  NE2 . GLN   B 1 53  ? 40.368 -25.729 23.910 1.00 15.86 ? 59  GLN   C NE2 1 
ATOM   1496 N  N   . THR   B 1 54  ? 36.225 -30.594 22.377 1.00 11.10 ? 60  THR   C N   1 
ATOM   1497 C  CA  . THR   B 1 54  ? 36.101 -31.446 21.190 1.00 11.71 ? 60  THR   C CA  1 
ATOM   1498 C  C   . THR   B 1 54  ? 34.610 -31.707 20.975 1.00 11.38 ? 60  THR   C C   1 
ATOM   1499 O  O   . THR   B 1 54  ? 33.825 -31.796 21.937 1.00 11.83 ? 60  THR   C O   1 
ATOM   1500 C  CB  . THR   B 1 54  ? 36.867 -32.758 21.265 1.00 14.29 ? 60  THR   C CB  1 
ATOM   1501 O  OG1 . THR   B 1 54  ? 36.337 -33.503 22.325 1.00 17.38 ? 60  THR   C OG1 1 
ATOM   1502 C  CG2 . THR   B 1 54  ? 38.335 -32.540 21.547 1.00 14.54 ? 60  THR   C CG2 1 
ATOM   1503 N  N   . GLY   B 1 55  ? 34.224 -31.801 19.702 1.00 9.28  ? 61  GLY   C N   1 
ATOM   1504 C  CA  . GLY   B 1 55  ? 32.816 -32.036 19.374 1.00 9.85  ? 61  GLY   C CA  1 
ATOM   1505 C  C   . GLY   B 1 55  ? 32.654 -32.239 17.876 1.00 9.13  ? 61  GLY   C C   1 
ATOM   1506 O  O   . GLY   B 1 55  ? 33.633 -32.560 17.182 1.00 10.38 ? 61  GLY   C O   1 
ATOM   1507 N  N   . VAL   B 1 56  ? 31.425 -32.115 17.394 1.00 8.72  ? 62  VAL   C N   1 
ATOM   1508 C  CA  . VAL   B 1 56  ? 31.127 -32.324 15.975 1.00 8.37  ? 62  VAL   C CA  1 
ATOM   1509 C  C   . VAL   B 1 56  ? 30.233 -31.181 15.545 1.00 8.35  ? 62  VAL   C C   1 
ATOM   1510 O  O   . VAL   B 1 56  ? 29.297 -30.849 16.269 1.00 9.64  ? 62  VAL   C O   1 
ATOM   1511 C  CB  . VAL   B 1 56  ? 30.369 -33.680 15.842 1.00 9.22  ? 62  VAL   C CB  1 
ATOM   1512 C  CG1 . VAL   B 1 56  ? 29.833 -33.866 14.419 1.00 10.92 ? 62  VAL   C CG1 1 
ATOM   1513 C  CG2 . VAL   B 1 56  ? 31.307 -34.847 16.198 1.00 10.71 ? 62  VAL   C CG2 1 
ATOM   1514 N  N   . TYR   B 1 57  ? 30.473 -30.595 14.357 1.00 8.40  ? 63  TYR   C N   1 
ATOM   1515 C  CA  . TYR   B 1 57  ? 29.586 -29.525 13.863 1.00 7.46  ? 63  TYR   C CA  1 
ATOM   1516 C  C   . TYR   B 1 57  ? 29.026 -29.865 12.495 1.00 8.51  ? 63  TYR   C C   1 
ATOM   1517 O  O   . TYR   B 1 57  ? 29.682 -30.569 11.718 1.00 9.76  ? 63  TYR   C O   1 
ATOM   1518 C  CB  . TYR   B 1 57  ? 30.252 -28.105 13.834 1.00 8.62  ? 63  TYR   C CB  1 
ATOM   1519 C  CG  . TYR   B 1 57  ? 31.136 -27.785 12.633 1.00 8.47  ? 63  TYR   C CG  1 
ATOM   1520 C  CD1 . TYR   B 1 57  ? 32.410 -28.308 12.527 1.00 10.21 ? 63  TYR   C CD1 1 
ATOM   1521 C  CD2 . TYR   B 1 57  ? 30.680 -26.968 11.601 1.00 9.18  ? 63  TYR   C CD2 1 
ATOM   1522 C  CE1 . TYR   B 1 57  ? 33.229 -28.015 11.428 1.00 10.75 ? 63  TYR   C CE1 1 
ATOM   1523 C  CE2 . TYR   B 1 57  ? 31.500 -26.645 10.515 1.00 10.04 ? 63  TYR   C CE2 1 
ATOM   1524 C  CZ  . TYR   B 1 57  ? 32.769 -27.175 10.434 1.00 11.34 ? 63  TYR   C CZ  1 
ATOM   1525 O  OH  . TYR   B 1 57  ? 33.611 -26.861 9.372  1.00 12.62 ? 63  TYR   C OH  1 
ATOM   1526 N  N   . TYR   B 1 58  ? 27.843 -29.294 12.204 1.00 8.72  ? 64  TYR   C N   1 
ATOM   1527 C  CA  . TYR   B 1 58  ? 27.225 -29.457 10.890 1.00 9.25  ? 64  TYR   C CA  1 
ATOM   1528 C  C   . TYR   B 1 58  ? 27.619 -28.315 9.965  1.00 8.93  ? 64  TYR   C C   1 
ATOM   1529 O  O   . TYR   B 1 58  ? 27.387 -27.127 10.275 1.00 9.20  ? 64  TYR   C O   1 
ATOM   1530 C  CB  . TYR   B 1 58  ? 25.694 -29.560 10.997 1.00 9.94  ? 64  TYR   C CB  1 
ATOM   1531 C  CG  . TYR   B 1 58  ? 25.086 -29.838 9.628  1.00 10.82 ? 64  TYR   C CG  1 
ATOM   1532 C  CD1 . TYR   B 1 58  ? 25.423 -30.986 8.919  1.00 11.57 ? 64  TYR   C CD1 1 
ATOM   1533 C  CD2 . TYR   B 1 58  ? 24.240 -28.926 9.021  1.00 10.87 ? 64  TYR   C CD2 1 
ATOM   1534 C  CE1 . TYR   B 1 58  ? 24.930 -31.225 7.635  1.00 12.96 ? 64  TYR   C CE1 1 
ATOM   1535 C  CE2 . TYR   B 1 58  ? 23.709 -29.172 7.751  1.00 11.99 ? 64  TYR   C CE2 1 
ATOM   1536 C  CZ  . TYR   B 1 58  ? 24.047 -30.337 7.080  1.00 12.74 ? 64  TYR   C CZ  1 
ATOM   1537 O  OH  . TYR   B 1 58  ? 23.574 -30.589 5.795  1.00 16.20 ? 64  TYR   C OH  1 
ATOM   1538 N  N   . CYS   B 1 59  ? 28.142 -28.695 8.800  1.00 9.03  ? 65  CYS   C N   1 
ATOM   1539 C  CA  . CYS   B 1 59  ? 28.545 -27.757 7.737  1.00 9.56  ? 65  CYS   C CA  1 
ATOM   1540 C  C   . CYS   B 1 59  ? 27.601 -27.939 6.528  1.00 10.66 ? 65  CYS   C C   1 
ATOM   1541 O  O   . CYS   B 1 59  ? 27.769 -28.880 5.735  1.00 11.31 ? 65  CYS   C O   1 
ATOM   1542 C  CB  . CYS   B 1 59  ? 29.997 -28.020 7.363  1.00 9.91  ? 65  CYS   C CB  1 
ATOM   1543 S  SG  . CYS   B 1 59  ? 30.580 -26.976 5.995  1.00 12.12 ? 65  CYS   C SG  1 
ATOM   1544 N  N   . SER   B 1 60  ? 26.601 -27.046 6.398  1.00 11.61 ? 66  SER   C N   1 
ATOM   1545 C  CA  A SER   B 1 60  ? 25.615 -27.230 5.339  0.50 12.67 ? 66  SER   C CA  1 
ATOM   1546 C  CA  B SER   B 1 60  ? 25.616 -27.192 5.336  0.50 11.88 ? 66  SER   C CA  1 
ATOM   1547 C  C   . SER   B 1 60  ? 26.220 -27.129 3.940  1.00 12.38 ? 66  SER   C C   1 
ATOM   1548 O  O   . SER   B 1 60  ? 25.763 -27.851 3.051  1.00 14.09 ? 66  SER   C O   1 
ATOM   1549 C  CB  A SER   B 1 60  ? 24.425 -26.298 5.516  0.50 15.63 ? 66  SER   C CB  1 
ATOM   1550 C  CB  B SER   B 1 60  ? 24.526 -26.140 5.461  0.50 12.47 ? 66  SER   C CB  1 
ATOM   1551 O  OG  A SER   B 1 60  ? 24.807 -24.936 5.483  0.50 18.84 ? 66  SER   C OG  1 
ATOM   1552 O  OG  B SER   B 1 60  ? 23.568 -26.376 4.442  0.50 11.69 ? 66  SER   C OG  1 
ATOM   1553 N  N   . SER   B 1 61  ? 27.229 -26.295 3.759  1.00 11.35 ? 67  SER   C N   1 
ATOM   1554 C  CA  . SER   B 1 61  ? 27.855 -26.164 2.419  1.00 12.24 ? 67  SER   C CA  1 
ATOM   1555 C  C   . SER   B 1 61  ? 28.635 -27.395 1.971  1.00 13.72 ? 67  SER   C C   1 
ATOM   1556 O  O   . SER   B 1 61  ? 29.016 -27.508 0.789  1.00 15.84 ? 67  SER   C O   1 
ATOM   1557 C  CB  . SER   B 1 61  ? 28.714 -24.916 2.348  1.00 13.57 ? 67  SER   C CB  1 
ATOM   1558 O  OG  . SER   B 1 61  ? 29.845 -24.998 3.191  1.00 13.84 ? 67  SER   C OG  1 
ATOM   1559 N  N   . ARG   B 1 62  ? 28.885 -28.346 2.878  1.00 12.30 ? 68  ARG   C N   1 
ATOM   1560 C  CA  . ARG   B 1 62  ? 29.507 -29.621 2.515  1.00 12.68 ? 68  ARG   C CA  1 
ATOM   1561 C  C   . ARG   B 1 62  ? 28.563 -30.796 2.754  1.00 12.54 ? 68  ARG   C C   1 
ATOM   1562 O  O   . ARG   B 1 62  ? 28.962 -31.948 2.558  1.00 14.12 ? 68  ARG   C O   1 
ATOM   1563 C  CB  . ARG   B 1 62  ? 30.793 -29.828 3.317  1.00 13.45 ? 68  ARG   C CB  1 
ATOM   1564 C  CG  . ARG   B 1 62  ? 31.848 -28.739 3.081  1.00 17.61 ? 68  ARG   C CG  1 
ATOM   1565 C  CD  . ARG   B 1 62  ? 32.544 -28.986 1.772  1.00 17.38 ? 68  ARG   C CD  1 
ATOM   1566 N  NE  . ARG   B 1 62  ? 33.562 -27.952 1.479  1.00 20.47 ? 68  ARG   C NE  1 
ATOM   1567 C  CZ  . ARG   B 1 62  ? 33.336 -26.824 0.810  1.00 24.33 ? 68  ARG   C CZ  1 
ATOM   1568 N  NH1 . ARG   B 1 62  ? 32.123 -26.557 0.329  1.00 26.54 ? 68  ARG   C NH1 1 
ATOM   1569 N  NH2 . ARG   B 1 62  ? 34.340 -25.978 0.551  1.00 24.57 ? 68  ARG   C NH2 1 
ATOM   1570 N  N   . ARG   B 1 63  ? 27.349 -30.555 3.276  1.00 13.41 ? 69  ARG   C N   1 
ATOM   1571 C  CA  . ARG   B 1 63  ? 26.397 -31.606 3.703  1.00 14.41 ? 69  ARG   C CA  1 
ATOM   1572 C  C   . ARG   B 1 63  ? 27.091 -32.638 4.597  1.00 15.24 ? 69  ARG   C C   1 
ATOM   1573 O  O   . ARG   B 1 63  ? 26.939 -33.859 4.401  1.00 16.89 ? 69  ARG   C O   1 
ATOM   1574 C  CB  . ARG   B 1 63  ? 25.762 -32.300 2.485  1.00 14.75 ? 69  ARG   C CB  1 
ATOM   1575 C  CG  . ARG   B 1 63  ? 24.878 -31.442 1.632  1.00 17.36 ? 69  ARG   C CG  1 
ATOM   1576 C  CD  . ARG   B 1 63  ? 23.680 -30.963 2.359  1.00 22.78 ? 69  ARG   C CD  1 
ATOM   1577 N  NE  . ARG   B 1 63  ? 22.678 -30.495 1.410  1.00 26.73 ? 69  ARG   C NE  1 
ATOM   1578 C  CZ  . ARG   B 1 63  ? 22.504 -29.228 1.064  1.00 27.17 ? 69  ARG   C CZ  1 
ATOM   1579 N  NH1 . ARG   B 1 63  ? 23.293 -28.278 1.561  1.00 25.22 ? 69  ARG   C NH1 1 
ATOM   1580 N  NH2 . ARG   B 1 63  ? 21.539 -28.895 0.224  1.00 27.93 ? 69  ARG   C NH2 1 
ATOM   1581 N  N   . LYS   B 1 64  ? 27.926 -32.154 5.537  1.00 13.58 ? 70  LYS   C N   1 
ATOM   1582 C  CA  . LYS   B 1 64  ? 28.725 -33.051 6.345  1.00 14.44 ? 70  LYS   C CA  1 
ATOM   1583 C  C   . LYS   B 1 64  ? 28.843 -32.575 7.758  1.00 12.08 ? 70  LYS   C C   1 
ATOM   1584 O  O   . LYS   B 1 64  ? 28.869 -31.375 8.020  1.00 12.22 ? 70  LYS   C O   1 
ATOM   1585 C  CB  . LYS   B 1 64  ? 30.143 -33.083 5.742  1.00 18.31 ? 70  LYS   C CB  1 
ATOM   1586 C  CG  . LYS   B 1 64  ? 30.302 -34.152 4.652  1.00 29.34 ? 70  LYS   C CG  1 
ATOM   1587 C  CD  . LYS   B 1 64  ? 31.759 -34.362 4.265  1.00 37.96 ? 70  LYS   C CD  1 
ATOM   1588 C  CE  . LYS   B 1 64  ? 31.888 -35.352 3.132  1.00 43.44 ? 70  LYS   C CE  1 
ATOM   1589 N  NZ  . LYS   B 1 64  ? 31.164 -34.897 1.917  1.00 47.97 ? 70  LYS   C NZ  1 
ATOM   1590 N  N   . HIS   B 1 65  ? 28.939 -33.536 8.669  1.00 11.19 ? 71  HIS   C N   1 
ATOM   1591 C  CA  . HIS   B 1 65  ? 29.255 -33.285 10.081 1.00 11.52 ? 71  HIS   C CA  1 
ATOM   1592 C  C   . HIS   B 1 65  ? 30.724 -33.545 10.248 1.00 13.18 ? 71  HIS   C C   1 
ATOM   1593 O  O   . HIS   B 1 65  ? 31.206 -34.643 9.927  1.00 16.32 ? 71  HIS   C O   1 
ATOM   1594 C  CB  . HIS   B 1 65  ? 28.420 -34.182 11.019 1.00 11.32 ? 71  HIS   C CB  1 
ATOM   1595 C  CG  . HIS   B 1 65  ? 26.958 -33.906 10.976 1.00 10.27 ? 71  HIS   C CG  1 
ATOM   1596 N  ND1 . HIS   B 1 65  ? 26.312 -33.117 11.922 1.00 13.51 ? 71  HIS   C ND1 1 
ATOM   1597 C  CD2 . HIS   B 1 65  ? 26.039 -34.346 10.084 1.00 11.18 ? 71  HIS   C CD2 1 
ATOM   1598 C  CE1 . HIS   B 1 65  ? 25.017 -33.133 11.597 1.00 11.60 ? 71  HIS   C CE1 1 
ATOM   1599 N  NE2 . HIS   B 1 65  ? 24.803 -33.858 10.512 1.00 13.42 ? 71  HIS   C NE2 1 
ATOM   1600 N  N   . TYR   B 1 66  ? 31.470 -32.591 10.817 1.00 10.27 ? 72  TYR   C N   1 
ATOM   1601 C  CA  . TYR   B 1 66  ? 32.915 -32.779 10.991 1.00 10.47 ? 72  TYR   C CA  1 
ATOM   1602 C  C   . TYR   B 1 66  ? 33.304 -32.844 12.459 1.00 9.57  ? 72  TYR   C C   1 
ATOM   1603 O  O   . TYR   B 1 66  ? 32.894 -31.962 13.217 1.00 9.89  ? 72  TYR   C O   1 
ATOM   1604 C  CB  . TYR   B 1 66  ? 33.669 -31.554 10.399 1.00 11.68 ? 72  TYR   C CB  1 
ATOM   1605 C  CG  . TYR   B 1 66  ? 33.629 -31.452 8.881  1.00 12.13 ? 72  TYR   C CG  1 
ATOM   1606 C  CD1 . TYR   B 1 66  ? 34.468 -32.220 8.099  1.00 14.82 ? 72  TYR   C CD1 1 
ATOM   1607 C  CD2 . TYR   B 1 66  ? 32.859 -30.482 8.246  1.00 12.89 ? 72  TYR   C CD2 1 
ATOM   1608 C  CE1 . TYR   B 1 66  ? 34.481 -32.090 6.708  1.00 15.87 ? 72  TYR   C CE1 1 
ATOM   1609 C  CE2 . TYR   B 1 66  ? 32.846 -30.356 6.854  1.00 14.32 ? 72  TYR   C CE2 1 
ATOM   1610 C  CZ  . TYR   B 1 66  ? 33.686 -31.141 6.096  1.00 16.17 ? 72  TYR   C CZ  1 
ATOM   1611 O  OH  . TYR   B 1 66  ? 33.660 -30.956 4.716  1.00 17.34 ? 72  TYR   C OH  1 
ATOM   1612 N  N   . PRO   B 1 67  ? 34.123 -33.811 12.869 1.00 9.88  ? 73  PRO   C N   1 
ATOM   1613 C  CA  . PRO   B 1 67  ? 34.677 -33.772 14.244 1.00 10.30 ? 73  PRO   C CA  1 
ATOM   1614 C  C   . PRO   B 1 67  ? 35.763 -32.691 14.322 1.00 11.34 ? 73  PRO   C C   1 
ATOM   1615 O  O   . PRO   B 1 67  ? 36.625 -32.595 13.414 1.00 13.46 ? 73  PRO   C O   1 
ATOM   1616 C  CB  . PRO   B 1 67  ? 35.279 -35.173 14.436 1.00 12.50 ? 73  PRO   C CB  1 
ATOM   1617 C  CG  . PRO   B 1 67  ? 35.472 -35.704 13.061 1.00 14.86 ? 73  PRO   C CG  1 
ATOM   1618 C  CD  . PRO   B 1 67  ? 34.604 -34.974 12.081 1.00 10.75 ? 73  PRO   C CD  1 
ATOM   1619 N  N   . VAL   B 1 68  ? 35.734 -31.898 15.387 1.00 9.49  ? 74  VAL   C N   1 
ATOM   1620 C  CA  . VAL   B 1 68  ? 36.700 -30.793 15.508 1.00 9.95  ? 74  VAL   C CA  1 
ATOM   1621 C  C   . VAL   B 1 68  ? 37.098 -30.616 16.950 1.00 10.20 ? 74  VAL   C C   1 
ATOM   1622 O  O   . VAL   B 1 68  ? 36.357 -30.919 17.888 1.00 10.35 ? 74  VAL   C O   1 
ATOM   1623 C  CB  . VAL   B 1 68  ? 36.093 -29.429 15.028 1.00 11.69 ? 74  VAL   C CB  1 
ATOM   1624 C  CG1 . VAL   B 1 68  ? 36.024 -29.355 13.482 1.00 14.87 ? 74  VAL   C CG1 1 
ATOM   1625 C  CG2 . VAL   B 1 68  ? 34.738 -29.128 15.705 1.00 12.85 ? 74  VAL   C CG2 1 
ATOM   1626 N  N   . SER   B 1 69  ? 38.297 -30.042 17.128 1.00 10.63 ? 75  SER   C N   1 
ATOM   1627 C  CA  . SER   B 1 69  ? 38.782 -29.423 18.359 1.00 10.56 ? 75  SER   C CA  1 
ATOM   1628 C  C   . SER   B 1 69  ? 38.508 -27.925 18.240 1.00 9.79  ? 75  SER   C C   1 
ATOM   1629 O  O   . SER   B 1 69  ? 38.618 -27.325 17.155 1.00 10.39 ? 75  SER   C O   1 
ATOM   1630 C  CB  . SER   B 1 69  ? 40.288 -29.607 18.491 1.00 12.40 ? 75  SER   C CB  1 
ATOM   1631 O  OG  . SER   B 1 69  ? 40.601 -30.984 18.619 1.00 16.06 ? 75  SER   C OG  1 
ATOM   1632 N  N   . PHE   B 1 70  ? 38.019 -27.314 19.315 1.00 9.46  ? 76  PHE   C N   1 
ATOM   1633 C  CA  . PHE   B 1 70  ? 37.662 -25.892 19.288 1.00 9.27  ? 76  PHE   C CA  1 
ATOM   1634 C  C   . PHE   B 1 70  ? 38.188 -25.154 20.535 1.00 10.09 ? 76  PHE   C C   1 
ATOM   1635 O  O   . PHE   B 1 70  ? 38.356 -25.779 21.598 1.00 10.28 ? 76  PHE   C O   1 
ATOM   1636 C  CB  . PHE   B 1 70  ? 36.141 -25.677 19.046 1.00 10.28 ? 76  PHE   C CB  1 
ATOM   1637 C  CG  . PHE   B 1 70  ? 35.264 -26.382 20.060 1.00 9.30  ? 76  PHE   C CG  1 
ATOM   1638 C  CD1 . PHE   B 1 70  ? 34.823 -27.688 19.840 1.00 10.21 ? 76  PHE   C CD1 1 
ATOM   1639 C  CD2 . PHE   B 1 70  ? 34.826 -25.718 21.199 1.00 9.73  ? 76  PHE   C CD2 1 
ATOM   1640 C  CE1 . PHE   B 1 70  ? 34.023 -28.329 20.774 1.00 9.46  ? 76  PHE   C CE1 1 
ATOM   1641 C  CE2 . PHE   B 1 70  ? 33.968 -26.355 22.103 1.00 10.23 ? 76  PHE   C CE2 1 
ATOM   1642 C  CZ  . PHE   B 1 70  ? 33.610 -27.663 21.918 1.00 10.09 ? 76  PHE   C CZ  1 
ATOM   1643 N  N   . SER   B 1 71  ? 38.444 -23.871 20.399 1.00 9.68  ? 77  SER   C N   1 
ATOM   1644 C  CA  . SER   B 1 71  ? 39.059 -23.089 21.470 1.00 10.59 ? 77  SER   C CA  1 
ATOM   1645 C  C   . SER   B 1 71  ? 38.083 -22.720 22.577 1.00 10.65 ? 77  SER   C C   1 
ATOM   1646 O  O   . SER   B 1 71  ? 36.874 -22.983 22.499 1.00 11.56 ? 77  SER   C O   1 
ATOM   1647 C  CB  . SER   B 1 71  ? 39.779 -21.880 20.890 1.00 10.56 ? 77  SER   C CB  1 
ATOM   1648 O  OG  . SER   B 1 71  ? 38.877 -20.976 20.271 1.00 12.72 ? 77  SER   C OG  1 
ATOM   1649 N  N   . LYS   B 1 72  ? 38.582 -22.073 23.635 1.00 12.17 ? 78  LYS   C N   1 
ATOM   1650 C  CA  . LYS   B 1 72  ? 37.715 -21.657 24.767 1.00 12.06 ? 78  LYS   C CA  1 
ATOM   1651 C  C   . LYS   B 1 72  ? 36.993 -20.351 24.371 1.00 11.63 ? 78  LYS   C C   1 
ATOM   1652 O  O   . LYS   B 1 72  ? 37.579 -19.529 23.657 1.00 13.22 ? 78  LYS   C O   1 
ATOM   1653 C  CB  . LYS   B 1 72  ? 38.595 -21.422 26.009 1.00 15.00 ? 78  LYS   C CB  1 
ATOM   1654 C  CG  . LYS   B 1 72  ? 39.326 -22.678 26.446 1.00 17.35 ? 78  LYS   C CG  1 
ATOM   1655 C  CD  . LYS   B 1 72  ? 40.318 -22.371 27.573 1.00 27.50 ? 78  LYS   C CD  1 
ATOM   1656 C  CE  . LYS   B 1 72  ? 41.227 -23.528 27.901 1.00 35.68 ? 78  LYS   C CE  1 
ATOM   1657 N  NZ  . LYS   B 1 72  ? 42.430 -23.055 28.640 1.00 40.88 ? 78  LYS   C NZ  1 
ATOM   1658 N  N   . PRO   B 1 73  ? 35.756 -20.123 24.838 1.00 12.04 ? 79  PRO   C N   1 
ATOM   1659 C  CA  . PRO   B 1 73  ? 35.019 -18.882 24.438 1.00 12.37 ? 79  PRO   C CA  1 
ATOM   1660 C  C   . PRO   B 1 73  ? 35.797 -17.640 24.815 1.00 12.55 ? 79  PRO   C C   1 
ATOM   1661 O  O   . PRO   B 1 73  ? 36.258 -17.507 25.973 1.00 14.00 ? 79  PRO   C O   1 
ATOM   1662 C  CB  . PRO   B 1 73  ? 33.705 -18.934 25.220 1.00 14.15 ? 79  PRO   C CB  1 
ATOM   1663 C  CG  . PRO   B 1 73  ? 33.614 -20.314 25.742 1.00 15.92 ? 79  PRO   C CG  1 
ATOM   1664 C  CD  . PRO   B 1 73  ? 34.979 -21.011 25.729 1.00 12.92 ? 79  PRO   C CD  1 
ATOM   1665 N  N   . SER   B 1 74  ? 36.012 -16.741 23.853 1.00 11.55 ? 80  SER   C N   1 
ATOM   1666 C  CA  A SER   B 1 74  ? 36.870 -15.583 24.085 0.50 12.64 ? 80  SER   C CA  1 
ATOM   1667 C  CA  B SER   B 1 74  ? 36.837 -15.565 24.118 0.50 12.41 ? 80  SER   C CA  1 
ATOM   1668 C  C   . SER   B 1 74  ? 36.487 -14.411 23.185 1.00 12.98 ? 80  SER   C C   1 
ATOM   1669 O  O   . SER   B 1 74  ? 35.629 -14.554 22.309 1.00 12.52 ? 80  SER   C O   1 
ATOM   1670 C  CB  A SER   B 1 74  ? 38.318 -15.970 23.791 0.50 15.37 ? 80  SER   C CB  1 
ATOM   1671 C  CB  B SER   B 1 74  ? 38.315 -15.931 23.990 0.50 14.45 ? 80  SER   C CB  1 
ATOM   1672 O  OG  A SER   B 1 74  ? 38.695 -17.125 24.518 0.50 18.00 ? 80  SER   C OG  1 
ATOM   1673 O  OG  B SER   B 1 74  ? 38.652 -16.254 22.652 0.50 15.06 ? 80  SER   C OG  1 
ATOM   1674 N  N   . LEU   B 1 75  ? 37.164 -13.256 23.372 1.00 13.28 ? 81  LEU   C N   1 
ATOM   1675 C  CA  . LEU   B 1 75  ? 36.961 -12.054 22.558 1.00 14.50 ? 81  LEU   C CA  1 
ATOM   1676 C  C   . LEU   B 1 75  ? 37.970 -12.141 21.393 1.00 15.47 ? 81  LEU   C C   1 
ATOM   1677 O  O   . LEU   B 1 75  ? 39.194 -12.086 21.627 1.00 17.43 ? 81  LEU   C O   1 
ATOM   1678 C  CB  . LEU   B 1 75  ? 37.215 -10.790 23.422 1.00 16.14 ? 81  LEU   C CB  1 
ATOM   1679 C  CG  . LEU   B 1 75  ? 36.941 -9.457  22.757 1.00 18.39 ? 81  LEU   C CG  1 
ATOM   1680 C  CD1 . LEU   B 1 75  ? 35.445 -9.261  22.531 1.00 18.02 ? 81  LEU   C CD1 1 
ATOM   1681 C  CD2 . LEU   B 1 75  ? 37.464 -8.317  23.651 1.00 20.62 ? 81  LEU   C CD2 1 
ATOM   1682 N  N   . ILE   B 1 76  ? 37.492 -12.353 20.169 1.00 15.37 ? 82  ILE   C N   1 
ATOM   1683 C  CA  . ILE   B 1 76  ? 38.335 -12.606 18.993 1.00 16.41 ? 82  ILE   C CA  1 
ATOM   1684 C  C   . ILE   B 1 76  ? 38.081 -11.545 17.907 1.00 16.07 ? 82  ILE   C C   1 
ATOM   1685 O  O   . ILE   B 1 76  ? 36.909 -11.210 17.651 1.00 15.39 ? 82  ILE   C O   1 
ATOM   1686 C  CB  . ILE   B 1 76  ? 37.932 -14.013 18.430 1.00 18.94 ? 82  ILE   C CB  1 
ATOM   1687 C  CG1 . ILE   B 1 76  ? 38.200 -15.170 19.423 1.00 21.80 ? 82  ILE   C CG1 1 
ATOM   1688 C  CG2 . ILE   B 1 76  ? 38.564 -14.305 17.055 1.00 21.13 ? 82  ILE   C CG2 1 
ATOM   1689 C  CD1 . ILE   B 1 76  ? 39.643 -15.640 19.517 1.00 24.76 ? 82  ILE   C CD1 1 
ATOM   1690 N  N   . PHE   B 1 77  ? 39.141 -11.057 17.243 1.00 16.62 ? 83  PHE   C N   1 
ATOM   1691 C  CA  . PHE   B 1 77  ? 38.960 -10.109 16.140 1.00 17.13 ? 83  PHE   C CA  1 
ATOM   1692 C  C   . PHE   B 1 77  ? 38.566 -10.940 14.905 1.00 17.77 ? 83  PHE   C C   1 
ATOM   1693 O  O   . PHE   B 1 77  ? 39.237 -11.928 14.569 1.00 19.76 ? 83  PHE   C O   1 
ATOM   1694 C  CB  . PHE   B 1 77  ? 40.267 -9.320  15.844 1.00 17.90 ? 83  PHE   C CB  1 
ATOM   1695 C  CG  . PHE   B 1 77  ? 39.997 -8.141  14.929 1.00 18.71 ? 83  PHE   C CG  1 
ATOM   1696 C  CD1 . PHE   B 1 77  ? 39.281 -7.051  15.382 1.00 19.27 ? 83  PHE   C CD1 1 
ATOM   1697 C  CD2 . PHE   B 1 77  ? 40.357 -8.184  13.575 1.00 20.20 ? 83  PHE   C CD2 1 
ATOM   1698 C  CE1 . PHE   B 1 77  ? 38.998 -5.983  14.534 1.00 20.54 ? 83  PHE   C CE1 1 
ATOM   1699 C  CE2 . PHE   B 1 77  ? 40.042 -7.126  12.722 1.00 20.69 ? 83  PHE   C CE2 1 
ATOM   1700 C  CZ  . PHE   B 1 77  ? 39.392 -6.028  13.213 1.00 21.12 ? 83  PHE   C CZ  1 
ATOM   1701 N  N   . VAL   B 1 78  ? 37.449 -10.580 14.274 1.00 14.77 ? 84  VAL   C N   1 
ATOM   1702 C  CA  . VAL   B 1 78  ? 36.936 -11.324 13.130 1.00 14.27 ? 84  VAL   C CA  1 
ATOM   1703 C  C   . VAL   B 1 78  ? 37.013 -10.396 11.919 1.00 14.22 ? 84  VAL   C C   1 
ATOM   1704 O  O   . VAL   B 1 78  ? 36.561 -9.245  11.999 1.00 14.27 ? 84  VAL   C O   1 
ATOM   1705 C  CB  . VAL   B 1 78  ? 35.454 -11.701 13.413 1.00 14.64 ? 84  VAL   C CB  1 
ATOM   1706 C  CG1 . VAL   B 1 78  ? 34.862 -12.476 12.244 1.00 15.90 ? 84  VAL   C CG1 1 
ATOM   1707 C  CG2 . VAL   B 1 78  ? 35.316 -12.503 14.709 1.00 15.56 ? 84  VAL   C CG2 1 
ATOM   1708 N  N   . GLU   B 1 79  ? 37.517 -10.872 10.779 1.00 13.36 ? 85  GLU   C N   1 
ATOM   1709 C  CA  . GLU   B 1 79  ? 37.545 -10.086 9.551  1.00 14.26 ? 85  GLU   C CA  1 
ATOM   1710 C  C   . GLU   B 1 79  ? 36.124 -9.805  9.027  1.00 13.73 ? 85  GLU   C C   1 
ATOM   1711 O  O   . GLU   B 1 79  ? 35.142 -10.471 9.410  1.00 13.63 ? 85  GLU   C O   1 
ATOM   1712 C  CB  . GLU   B 1 79  ? 38.363 -10.803 8.458  1.00 17.12 ? 85  GLU   C CB  1 
ATOM   1713 C  CG  . GLU   B 1 79  ? 39.851 -10.869 8.788  1.00 21.74 ? 85  GLU   C CG  1 
ATOM   1714 C  CD  . GLU   B 1 79  ? 40.487 -9.511  9.020  1.00 31.04 ? 85  GLU   C CD  1 
ATOM   1715 O  OE1 . GLU   B 1 79  ? 40.301 -8.597  8.181  1.00 34.77 ? 85  GLU   C OE1 1 
ATOM   1716 O  OE2 . GLU   B 1 79  ? 41.134 -9.339  10.076 1.00 34.12 ? 85  GLU   C OE2 1 
ATOM   1717 N  N   . ALA   B 1 80  ? 35.988 -8.786  8.168  1.00 14.52 ? 86  ALA   C N   1 
ATOM   1718 C  CA  . ALA   B 1 80  ? 34.705 -8.425  7.595  1.00 15.46 ? 86  ALA   C CA  1 
ATOM   1719 C  C   . ALA   B 1 80  ? 34.085 -9.614  6.873  1.00 16.42 ? 86  ALA   C C   1 
ATOM   1720 O  O   . ALA   B 1 80  ? 34.790 -10.409 6.236  1.00 18.13 ? 86  ALA   C O   1 
ATOM   1721 C  CB  . ALA   B 1 80  ? 34.926 -7.305  6.581  1.00 16.65 ? 86  ALA   C CB  1 
ATOM   1722 N  N   . SER   B 1 81  ? 32.779 -9.753  7.035  1.00 15.24 ? 87  SER   C N   1 
ATOM   1723 C  CA  . SER   B 1 81  ? 32.047 -10.792 6.354  1.00 16.13 ? 87  SER   C CA  1 
ATOM   1724 C  C   . SER   B 1 81  ? 30.908 -10.137 5.550  1.00 17.56 ? 87  SER   C C   1 
ATOM   1725 O  O   . SER   B 1 81  ? 30.763 -8.893  5.542  1.00 17.36 ? 87  SER   C O   1 
ATOM   1726 C  CB  . SER   B 1 81  ? 31.490 -11.772 7.385  1.00 15.53 ? 87  SER   C CB  1 
ATOM   1727 O  OG  . SER   B 1 81  ? 30.444 -11.109 8.091  1.00 16.36 ? 87  SER   C OG  1 
ATOM   1728 N  N   . GLU   B 1 82  ? 30.077 -10.955 4.902  1.00 18.75 ? 88  GLU   C N   1 
ATOM   1729 C  CA  . GLU   B 1 82  ? 28.976 -10.337 4.164  1.00 19.91 ? 88  GLU   C CA  1 
ATOM   1730 C  C   . GLU   B 1 82  ? 27.931 -9.691  5.107  1.00 19.86 ? 88  GLU   C C   1 
ATOM   1731 O  O   . GLU   B 1 82  ? 27.154 -8.840  4.662  1.00 21.25 ? 88  GLU   C O   1 
ATOM   1732 C  CB  . GLU   B 1 82  ? 28.361 -11.313 3.162  1.00 24.62 ? 88  GLU   C CB  1 
ATOM   1733 C  CG  . GLU   B 1 82  ? 27.520 -12.425 3.740  1.00 32.40 ? 88  GLU   C CG  1 
ATOM   1734 C  CD  . GLU   B 1 82  ? 26.820 -13.210 2.647  1.00 37.91 ? 88  GLU   C CD  1 
ATOM   1735 O  OE1 . GLU   B 1 82  ? 27.442 -13.412 1.578  1.00 39.85 ? 88  GLU   C OE1 1 
ATOM   1736 O  OE2 . GLU   B 1 82  ? 25.653 -13.618 2.854  1.00 39.14 ? 88  GLU   C OE2 1 
ATOM   1737 N  N   . TYR   B 1 83  ? 27.976 -10.000 6.425  1.00 16.75 ? 89  TYR   C N   1 
ATOM   1738 C  CA  . TYR   B 1 83  ? 26.939 -9.520  7.336  1.00 16.81 ? 89  TYR   C CA  1 
ATOM   1739 C  C   . TYR   B 1 83  ? 27.437 -8.666  8.519  1.00 17.45 ? 89  TYR   C C   1 
ATOM   1740 O  O   . TYR   B 1 83  ? 26.603 -8.072  9.191  1.00 19.01 ? 89  TYR   C O   1 
ATOM   1741 C  CB  . TYR   B 1 83  ? 26.076 -10.714 7.832  1.00 15.92 ? 89  TYR   C CB  1 
ATOM   1742 C  CG  . TYR   B 1 83  ? 26.911 -11.920 8.277  1.00 14.87 ? 89  TYR   C CG  1 
ATOM   1743 C  CD1 . TYR   B 1 83  ? 27.280 -12.921 7.371  1.00 15.20 ? 89  TYR   C CD1 1 
ATOM   1744 C  CD2 . TYR   B 1 83  ? 27.355 -12.041 9.588  1.00 15.08 ? 89  TYR   C CD2 1 
ATOM   1745 C  CE1 . TYR   B 1 83  ? 28.058 -14.013 7.769  1.00 13.85 ? 89  TYR   C CE1 1 
ATOM   1746 C  CE2 . TYR   B 1 83  ? 28.102 -13.129 10.000 1.00 14.97 ? 89  TYR   C CE2 1 
ATOM   1747 C  CZ  . TYR   B 1 83  ? 28.439 -14.130 9.096  1.00 13.82 ? 89  TYR   C CZ  1 
ATOM   1748 O  OH  . TYR   B 1 83  ? 29.266 -15.172 9.472  1.00 16.16 ? 89  TYR   C OH  1 
ATOM   1749 N  N   . TYR   B 1 84  ? 28.761 -8.553  8.767  1.00 14.98 ? 90  TYR   C N   1 
ATOM   1750 C  CA  . TYR   B 1 84  ? 29.316 -7.633  9.778  1.00 14.86 ? 90  TYR   C CA  1 
ATOM   1751 C  C   . TYR   B 1 84  ? 30.639 -7.025  9.240  1.00 14.80 ? 90  TYR   C C   1 
ATOM   1752 O  O   . TYR   B 1 84  ? 31.371 -7.679  8.488  1.00 14.95 ? 90  TYR   C O   1 
ATOM   1753 C  CB  . TYR   B 1 84  ? 29.659 -8.359  11.111 1.00 14.38 ? 90  TYR   C CB  1 
ATOM   1754 C  CG  . TYR   B 1 84  ? 28.472 -8.794  11.946 1.00 12.63 ? 90  TYR   C CG  1 
ATOM   1755 C  CD1 . TYR   B 1 84  ? 27.581 -7.861  12.492 1.00 12.88 ? 90  TYR   C CD1 1 
ATOM   1756 C  CD2 . TYR   B 1 84  ? 28.300 -10.108 12.285 1.00 12.03 ? 90  TYR   C CD2 1 
ATOM   1757 C  CE1 . TYR   B 1 84  ? 26.516 -8.258  13.309 1.00 12.86 ? 90  TYR   C CE1 1 
ATOM   1758 C  CE2 . TYR   B 1 84  ? 27.213 -10.523 13.049 1.00 11.49 ? 90  TYR   C CE2 1 
ATOM   1759 C  CZ  . TYR   B 1 84  ? 26.346 -9.595  13.610 1.00 12.32 ? 90  TYR   C CZ  1 
ATOM   1760 O  OH  . TYR   B 1 84  ? 25.274 -10.030 14.391 1.00 12.68 ? 90  TYR   C OH  1 
ATOM   1761 N  N   . PRO   B 1 85  ? 31.002 -5.814  9.694  1.00 15.18 ? 91  PRO   C N   1 
ATOM   1762 C  CA  . PRO   B 1 85  ? 32.350 -5.304  9.396  1.00 14.66 ? 91  PRO   C CA  1 
ATOM   1763 C  C   . PRO   B 1 85  ? 33.393 -6.068  10.238 1.00 14.47 ? 91  PRO   C C   1 
ATOM   1764 O  O   . PRO   B 1 85  ? 33.049 -6.890  11.130 1.00 14.33 ? 91  PRO   C O   1 
ATOM   1765 C  CB  . PRO   B 1 85  ? 32.251 -3.839  9.874  1.00 15.15 ? 91  PRO   C CB  1 
ATOM   1766 C  CG  . PRO   B 1 85  ? 31.325 -3.931  11.085 1.00 15.95 ? 91  PRO   C CG  1 
ATOM   1767 C  CD  . PRO   B 1 85  ? 30.276 -4.955  10.672 1.00 15.53 ? 91  PRO   C CD  1 
ATOM   1768 N  N   . ALA   B 1 86  ? 34.691 -5.803  10.002 1.00 14.03 ? 92  ALA   C N   1 
ATOM   1769 C  CA  . ALA   B 1 86  ? 35.758 -6.363  10.840 1.00 15.85 ? 92  ALA   C CA  1 
ATOM   1770 C  C   . ALA   B 1 86  ? 35.561 -5.814  12.273 1.00 16.06 ? 92  ALA   C C   1 
ATOM   1771 O  O   . ALA   B 1 86  ? 35.330 -4.600  12.447 1.00 17.85 ? 92  ALA   C O   1 
ATOM   1772 C  CB  . ALA   B 1 86  ? 37.125 -5.943  10.307 1.00 16.62 ? 92  ALA   C CB  1 
ATOM   1773 N  N   . ARG   B 1 87  ? 35.575 -6.703  13.263 1.00 14.51 ? 93  ARG   C N   1 
ATOM   1774 C  CA  . ARG   B 1 87  ? 35.303 -6.277  14.636 1.00 14.73 ? 93  ARG   C CA  1 
ATOM   1775 C  C   . ARG   B 1 87  ? 35.677 -7.358  15.641 1.00 14.63 ? 93  ARG   C C   1 
ATOM   1776 O  O   . ARG   B 1 87  ? 35.881 -8.517  15.263 1.00 14.53 ? 93  ARG   C O   1 
ATOM   1777 C  CB  . ARG   B 1 87  ? 33.777 -5.975  14.788 1.00 15.73 ? 93  ARG   C CB  1 
ATOM   1778 C  CG  . ARG   B 1 87  ? 32.948 -7.264  14.714 1.00 14.00 ? 93  ARG   C CG  1 
ATOM   1779 C  CD  . ARG   B 1 87  ? 31.457 -7.000  14.855 1.00 15.43 ? 93  ARG   C CD  1 
ATOM   1780 N  NE  . ARG   B 1 87  ? 30.740 -8.270  15.043 1.00 15.35 ? 93  ARG   C NE  1 
ATOM   1781 C  CZ  . ARG   B 1 87  ? 29.630 -8.429  15.762 1.00 16.38 ? 93  ARG   C CZ  1 
ATOM   1782 N  NH1 . ARG   B 1 87  ? 29.058 -7.383  16.357 1.00 16.39 ? 93  ARG   C NH1 1 
ATOM   1783 N  NH2 . ARG   B 1 87  ? 29.122 -9.640  15.940 1.00 16.74 ? 93  ARG   C NH2 1 
ATOM   1784 N  N   . TYR   B 1 88  ? 35.597 -7.019  16.943 1.00 14.93 ? 94  TYR   C N   1 
ATOM   1785 C  CA  . TYR   B 1 88  ? 35.727 -8.044  17.979 1.00 16.28 ? 94  TYR   C CA  1 
ATOM   1786 C  C   . TYR   B 1 88  ? 34.352 -8.667  18.238 1.00 15.06 ? 94  TYR   C C   1 
ATOM   1787 O  O   . TYR   B 1 88  ? 33.343 -7.963  18.334 1.00 16.10 ? 94  TYR   C O   1 
ATOM   1788 C  CB  . TYR   B 1 88  ? 36.237 -7.444  19.309 1.00 18.34 ? 94  TYR   C CB  1 
ATOM   1789 C  CG  . TYR   B 1 88  ? 37.705 -7.103  19.218 1.00 21.38 ? 94  TYR   C CG  1 
ATOM   1790 C  CD1 . TYR   B 1 88  ? 38.674 -8.073  19.418 1.00 23.05 ? 94  TYR   C CD1 1 
ATOM   1791 C  CD2 . TYR   B 1 88  ? 38.119 -5.821  18.857 1.00 23.63 ? 94  TYR   C CD2 1 
ATOM   1792 C  CE1 . TYR   B 1 88  ? 40.027 -7.775  19.281 1.00 24.79 ? 94  TYR   C CE1 1 
ATOM   1793 C  CE2 . TYR   B 1 88  ? 39.464 -5.505  18.739 1.00 25.06 ? 94  TYR   C CE2 1 
ATOM   1794 C  CZ  . TYR   B 1 88  ? 40.414 -6.485  18.948 1.00 26.58 ? 94  TYR   C CZ  1 
ATOM   1795 O  OH  . TYR   B 1 88  ? 41.742 -6.144  18.831 1.00 29.46 ? 94  TYR   C OH  1 
ATOM   1796 N  N   . GLN   B 1 89  ? 34.317 -9.983  18.327 1.00 14.02 ? 95  GLN   C N   1 
ATOM   1797 C  CA  . GLN   B 1 89  ? 33.111 -10.729 18.674 1.00 12.73 ? 95  GLN   C CA  1 
ATOM   1798 C  C   . GLN   B 1 89  ? 33.444 -11.447 19.981 1.00 12.29 ? 95  GLN   C C   1 
ATOM   1799 O  O   . GLN   B 1 89  ? 34.527 -12.035 20.107 1.00 13.57 ? 95  GLN   C O   1 
ATOM   1800 C  CB  . GLN   B 1 89  ? 32.771 -11.694 17.530 1.00 13.34 ? 95  GLN   C CB  1 
ATOM   1801 C  CG  . GLN   B 1 89  ? 31.490 -12.417 17.793 1.00 13.37 ? 95  GLN   C CG  1 
ATOM   1802 C  CD  . GLN   B 1 89  ? 30.812 -13.020 16.569 1.00 12.36 ? 95  GLN   C CD  1 
ATOM   1803 O  OE1 . GLN   B 1 89  ? 30.756 -12.436 15.475 1.00 13.51 ? 95  GLN   C OE1 1 
ATOM   1804 N  NE2 . GLN   B 1 89  ? 30.251 -14.173 16.760 1.00 12.78 ? 95  GLN   C NE2 1 
ATOM   1805 N  N   . SER   B 1 90  ? 32.535 -11.437 20.938 1.00 11.43 ? 96  SER   C N   1 
ATOM   1806 C  CA  . SER   B 1 90  ? 32.752 -12.062 22.238 1.00 12.02 ? 96  SER   C CA  1 
ATOM   1807 C  C   . SER   B 1 90  ? 32.136 -13.465 22.295 1.00 11.28 ? 96  SER   C C   1 
ATOM   1808 O  O   . SER   B 1 90  ? 31.283 -13.822 21.469 1.00 11.27 ? 96  SER   C O   1 
ATOM   1809 C  CB  . SER   B 1 90  ? 32.188 -11.198 23.385 1.00 13.14 ? 96  SER   C CB  1 
ATOM   1810 O  OG  . SER   B 1 90  ? 30.786 -11.113 23.254 1.00 13.69 ? 96  SER   C OG  1 
ATOM   1811 N  N   . HIS   B 1 91  ? 32.593 -14.262 23.276 1.00 10.98 ? 97  HIS   C N   1 
ATOM   1812 C  CA  . HIS   B 1 91  ? 32.102 -15.614 23.537 1.00 10.27 ? 97  HIS   C CA  1 
ATOM   1813 C  C   . HIS   B 1 91  ? 32.191 -16.484 22.253 1.00 10.46 ? 97  HIS   C C   1 
ATOM   1814 O  O   . HIS   B 1 91  ? 31.301 -17.296 21.992 1.00 11.10 ? 97  HIS   C O   1 
ATOM   1815 C  CB  . HIS   B 1 91  ? 30.648 -15.581 24.089 1.00 11.42 ? 97  HIS   C CB  1 
ATOM   1816 C  CG  . HIS   B 1 91  ? 30.509 -14.826 25.393 1.00 12.97 ? 97  HIS   C CG  1 
ATOM   1817 N  ND1 . HIS   B 1 91  ? 30.491 -15.488 26.609 1.00 14.84 ? 97  HIS   C ND1 1 
ATOM   1818 C  CD2 . HIS   B 1 91  ? 30.414 -13.483 25.629 1.00 14.33 ? 97  HIS   C CD2 1 
ATOM   1819 C  CE1 . HIS   B 1 91  ? 30.351 -14.549 27.546 1.00 14.91 ? 97  HIS   C CE1 1 
ATOM   1820 N  NE2 . HIS   B 1 91  ? 30.309 -13.327 27.012 1.00 15.97 ? 97  HIS   C NE2 1 
ATOM   1821 N  N   . LEU   B 1 92  ? 33.257 -16.308 21.494 1.00 10.07 ? 98  LEU   C N   1 
ATOM   1822 C  CA  . LEU   B 1 92  ? 33.476 -17.006 20.248 1.00 10.19 ? 98  LEU   C CA  1 
ATOM   1823 C  C   . LEU   B 1 92  ? 34.554 -18.072 20.426 1.00 9.64  ? 98  LEU   C C   1 
ATOM   1824 O  O   . LEU   B 1 92  ? 35.531 -17.867 21.149 1.00 10.88 ? 98  LEU   C O   1 
ATOM   1825 C  CB  . LEU   B 1 92  ? 33.940 -15.976 19.164 1.00 11.22 ? 98  LEU   C CB  1 
ATOM   1826 C  CG  . LEU   B 1 92  ? 34.060 -16.540 17.742 1.00 11.65 ? 98  LEU   C CG  1 
ATOM   1827 C  CD1 . LEU   B 1 92  ? 32.705 -16.915 17.167 1.00 12.24 ? 98  LEU   C CD1 1 
ATOM   1828 C  CD2 . LEU   B 1 92  ? 34.702 -15.506 16.787 1.00 13.73 ? 98  LEU   C CD2 1 
ATOM   1829 N  N   . MET   B 1 93  ? 34.361 -19.221 19.763 1.00 9.04  ? 99  MET   C N   1 
ATOM   1830 C  CA  . MET   B 1 93  ? 35.311 -20.351 19.824 1.00 8.59  ? 99  MET   C CA  1 
ATOM   1831 C  C   . MET   B 1 93  ? 35.705 -20.666 18.365 1.00 9.76  ? 99  MET   C C   1 
ATOM   1832 O  O   . MET   B 1 93  ? 34.828 -20.712 17.499 1.00 10.78 ? 99  MET   C O   1 
ATOM   1833 C  CB  . MET   B 1 93  ? 34.603 -21.585 20.414 1.00 9.83  ? 99  MET   C CB  1 
ATOM   1834 C  CG  . MET   B 1 93  ? 34.127 -21.305 21.834 1.00 12.03 ? 99  MET   C CG  1 
ATOM   1835 S  SD  . MET   B 1 93  ? 33.120 -22.631 22.476 1.00 12.38 ? 99  MET   C SD  1 
ATOM   1836 C  CE  . MET   B 1 93  ? 31.706 -22.533 21.426 1.00 13.19 ? 99  MET   C CE  1 
ATOM   1837 N  N   . LEU   B 1 94  ? 36.979 -20.920 18.103 1.00 9.68  ? 100 LEU   C N   1 
ATOM   1838 C  CA  . LEU   B 1 94  ? 37.424 -21.226 16.746 1.00 10.11 ? 100 LEU   C CA  1 
ATOM   1839 C  C   . LEU   B 1 94  ? 37.866 -22.684 16.603 1.00 10.34 ? 100 LEU   C C   1 
ATOM   1840 O  O   . LEU   B 1 94  ? 38.381 -23.278 17.541 1.00 11.56 ? 100 LEU   C O   1 
ATOM   1841 C  CB  . LEU   B 1 94  ? 38.655 -20.364 16.342 1.00 11.43 ? 100 LEU   C CB  1 
ATOM   1842 C  CG  . LEU   B 1 94  ? 38.489 -18.860 16.341 1.00 12.15 ? 100 LEU   C CG  1 
ATOM   1843 C  CD1 . LEU   B 1 94  ? 39.778 -18.170 15.847 1.00 15.31 ? 100 LEU   C CD1 1 
ATOM   1844 C  CD2 . LEU   B 1 94  ? 37.290 -18.411 15.506 1.00 14.59 ? 100 LEU   C CD2 1 
ATOM   1845 N  N   . ALA   B 1 95  ? 37.711 -23.211 15.395 1.00 10.16 ? 101 ALA   C N   1 
ATOM   1846 C  CA  . ALA   B 1 95  ? 38.230 -24.506 14.981 1.00 10.35 ? 101 ALA   C CA  1 
ATOM   1847 C  C   . ALA   B 1 95  ? 38.789 -24.366 13.545 1.00 10.19 ? 101 ALA   C C   1 
ATOM   1848 O  O   . ALA   B 1 95  ? 38.432 -23.427 12.822 1.00 10.18 ? 101 ALA   C O   1 
ATOM   1849 C  CB  . ALA   B 1 95  ? 37.126 -25.581 15.002 1.00 10.77 ? 101 ALA   C CB  1 
ATOM   1850 N  N   . VAL   B 1 96  ? 39.633 -25.304 13.134 1.00 10.42 ? 102 VAL   C N   1 
ATOM   1851 C  CA  . VAL   B 1 96  ? 40.097 -25.362 11.745 1.00 11.65 ? 102 VAL   C CA  1 
ATOM   1852 C  C   . VAL   B 1 96  ? 39.044 -26.118 10.959 1.00 11.76 ? 102 VAL   C C   1 
ATOM   1853 O  O   . VAL   B 1 96  ? 38.739 -27.301 11.257 1.00 13.40 ? 102 VAL   C O   1 
ATOM   1854 C  CB  . VAL   B 1 96  ? 41.455 -26.088 11.704 1.00 12.78 ? 102 VAL   C CB  1 
ATOM   1855 C  CG1 . VAL   B 1 96  ? 41.903 -26.227 10.247 1.00 14.24 ? 102 VAL   C CG1 1 
ATOM   1856 C  CG2 . VAL   B 1 96  ? 42.473 -25.317 12.538 1.00 13.78 ? 102 VAL   C CG2 1 
ATOM   1857 N  N   . GLY   B 1 97  ? 38.426 -25.430 10.009 1.00 12.33 ? 103 GLY   C N   1 
ATOM   1858 C  CA  . GLY   B 1 97  ? 37.361 -26.067 9.243  1.00 13.39 ? 103 GLY   C CA  1 
ATOM   1859 C  C   . GLY   B 1 97  ? 36.692 -25.097 8.320  1.00 13.09 ? 103 GLY   C C   1 
ATOM   1860 O  O   . GLY   B 1 97  ? 36.968 -23.874 8.311  1.00 14.48 ? 103 GLY   C O   1 
ATOM   1861 N  N   . HIS   B 1 98  ? 35.811 -25.652 7.495  1.00 13.18 ? 104 HIS   C N   1 
ATOM   1862 C  CA  . HIS   B 1 98  ? 35.128 -24.861 6.496  1.00 12.99 ? 104 HIS   C CA  1 
ATOM   1863 C  C   . HIS   B 1 98  ? 33.857 -24.161 7.029  1.00 12.54 ? 104 HIS   C C   1 
ATOM   1864 O  O   . HIS   B 1 98  ? 33.055 -24.799 7.736  1.00 13.04 ? 104 HIS   C O   1 
ATOM   1865 C  CB  . HIS   B 1 98  ? 34.768 -25.770 5.329  1.00 15.42 ? 104 HIS   C CB  1 
ATOM   1866 C  CG  . HIS   B 1 98  ? 34.237 -24.989 4.199  1.00 19.02 ? 104 HIS   C CG  1 
ATOM   1867 N  ND1 . HIS   B 1 98  ? 35.028 -24.065 3.523  1.00 21.02 ? 104 HIS   C ND1 1 
ATOM   1868 C  CD2 . HIS   B 1 98  ? 32.984 -24.950 3.709  1.00 20.94 ? 104 HIS   C CD2 1 
ATOM   1869 C  CE1 . HIS   B 1 98  ? 34.229 -23.505 2.635  1.00 23.21 ? 104 HIS   C CE1 1 
ATOM   1870 N  NE2 . HIS   B 1 98  ? 32.992 -24.017 2.699  1.00 23.57 ? 104 HIS   C NE2 1 
ATOM   1871 N  N   . SER   B 1 99  ? 33.616 -22.890 6.616  1.00 12.71 ? 105 SER   C N   1 
ATOM   1872 C  CA  . SER   B 1 99  ? 32.418 -22.122 7.018  1.00 13.08 ? 105 SER   C CA  1 
ATOM   1873 C  C   . SER   B 1 99  ? 32.147 -20.981 6.022  1.00 14.60 ? 105 SER   C C   1 
ATOM   1874 O  O   . SER   B 1 99  ? 32.996 -20.071 5.917  1.00 15.94 ? 105 SER   C O   1 
ATOM   1875 C  CB  . SER   B 1 99  ? 32.638 -21.542 8.420  1.00 14.09 ? 105 SER   C CB  1 
ATOM   1876 O  OG  . SER   B 1 99  ? 31.551 -20.702 8.804  1.00 15.26 ? 105 SER   C OG  1 
ATOM   1877 N  N   . GLU   B 1 100 ? 31.051 -21.080 5.249  1.00 14.63 ? 106 GLU   C N   1 
ATOM   1878 C  CA  . GLU   B 1 100 ? 30.568 -20.049 4.296  1.00 15.12 ? 106 GLU   C CA  1 
ATOM   1879 C  C   . GLU   B 1 100 ? 29.468 -19.296 5.072  1.00 14.07 ? 106 GLU   C C   1 
ATOM   1880 O  O   . GLU   B 1 100 ? 28.916 -19.787 6.062  1.00 12.94 ? 106 GLU   C O   1 
ATOM   1881 C  CB  . GLU   B 1 100 ? 29.845 -20.721 3.064  1.00 18.01 ? 106 GLU   C CB  1 
ATOM   1882 C  CG  . GLU   B 1 100 ? 30.576 -21.770 2.267  1.00 24.45 ? 106 GLU   C CG  1 
ATOM   1883 C  CD  . GLU   B 1 100 ? 31.488 -21.234 1.197  1.00 28.89 ? 106 GLU   C CD  1 
ATOM   1884 O  OE1 . GLU   B 1 100 ? 31.591 -19.989 1.075  1.00 28.27 ? 106 GLU   C OE1 1 
ATOM   1885 O  OE2 . GLU   B 1 100 ? 32.148 -22.059 0.529  1.00 29.95 ? 106 GLU   C OE2 1 
ATOM   1886 N  N   . PRO   B 1 101 ? 29.068 -18.098 4.600  1.00 14.06 ? 107 PRO   C N   1 
ATOM   1887 C  CA  . PRO   B 1 101 ? 27.977 -17.370 5.290  1.00 13.31 ? 107 PRO   C CA  1 
ATOM   1888 C  C   . PRO   B 1 101 ? 26.707 -18.216 5.503  1.00 13.50 ? 107 PRO   C C   1 
ATOM   1889 O  O   . PRO   B 1 101 ? 26.113 -18.142 6.591  1.00 13.58 ? 107 PRO   C O   1 
ATOM   1890 C  CB  . PRO   B 1 101 ? 27.708 -16.146 4.369  1.00 15.76 ? 107 PRO   C CB  1 
ATOM   1891 C  CG  . PRO   B 1 101 ? 28.969 -16.006 3.529  1.00 18.14 ? 107 PRO   C CG  1 
ATOM   1892 C  CD  . PRO   B 1 101 ? 29.692 -17.318 3.494  1.00 15.76 ? 107 PRO   C CD  1 
ATOM   1893 N  N   . GLY   B 1 102 ? 26.322 -19.053 4.526  1.00 12.57 ? 108 GLY   C N   1 
ATOM   1894 C  CA  . GLY   B 1 102 ? 25.095 -19.846 4.677  1.00 12.59 ? 108 GLY   C CA  1 
ATOM   1895 C  C   . GLY   B 1 102 ? 25.208 -20.962 5.706  1.00 12.31 ? 108 GLY   C C   1 
ATOM   1896 O  O   . GLY   B 1 102 ? 24.213 -21.627 6.019  1.00 14.51 ? 108 GLY   C O   1 
ATOM   1897 N  N   . ASP   B 1 103 ? 26.445 -21.256 6.200  1.00 10.84 ? 109 ASP   C N   1 
ATOM   1898 C  CA  . ASP   B 1 103 ? 26.615 -22.284 7.225  1.00 10.24 ? 109 ASP   C CA  1 
ATOM   1899 C  C   . ASP   B 1 103 ? 26.261 -21.780 8.612  1.00 9.85  ? 109 ASP   C C   1 
ATOM   1900 O  O   . ASP   B 1 103 ? 26.155 -22.573 9.552  1.00 10.34 ? 109 ASP   C O   1 
ATOM   1901 C  CB  . ASP   B 1 103 ? 28.078 -22.778 7.246  1.00 11.01 ? 109 ASP   C CB  1 
ATOM   1902 C  CG  . ASP   B 1 103 ? 28.398 -23.574 6.019  1.00 13.22 ? 109 ASP   C CG  1 
ATOM   1903 O  OD1 . ASP   B 1 103 ? 27.540 -24.326 5.579  1.00 13.59 ? 109 ASP   C OD1 1 
ATOM   1904 O  OD2 . ASP   B 1 103 ? 29.523 -23.433 5.492  1.00 13.92 ? 109 ASP   C OD2 1 
ATOM   1905 N  N   . CYS   B 1 104 ? 26.058 -20.445 8.801  1.00 9.62  ? 110 CYS   C N   1 
ATOM   1906 C  CA  . CYS   B 1 104 ? 25.667 -19.890 10.106 1.00 9.47  ? 110 CYS   C CA  1 
ATOM   1907 C  C   . CYS   B 1 104 ? 24.409 -20.595 10.604 1.00 9.96  ? 110 CYS   C C   1 
ATOM   1908 O  O   . CYS   B 1 104 ? 23.465 -20.816 9.830  1.00 11.30 ? 110 CYS   C O   1 
ATOM   1909 C  CB  . CYS   B 1 104 ? 25.445 -18.383 10.031 1.00 9.74  ? 110 CYS   C CB  1 
ATOM   1910 S  SG  . CYS   B 1 104 ? 26.961 -17.426 9.912  1.00 12.01 ? 110 CYS   C SG  1 
ATOM   1911 N  N   . GLY   B 1 105 ? 24.408 -20.966 11.866 1.00 8.32  ? 111 GLY   C N   1 
ATOM   1912 C  CA  . GLY   B 1 105 ? 23.257 -21.641 12.462 1.00 10.53 ? 111 GLY   C CA  1 
ATOM   1913 C  C   . GLY   B 1 105 ? 23.471 -23.135 12.625 1.00 10.12 ? 111 GLY   C C   1 
ATOM   1914 O  O   . GLY   B 1 105 ? 22.709 -23.790 13.354 1.00 10.77 ? 111 GLY   C O   1 
ATOM   1915 N  N   . GLY   B 1 106 ? 24.496 -23.707 11.957 1.00 9.24  ? 112 GLY   C N   1 
ATOM   1916 C  CA  . GLY   B 1 106 ? 24.803 -25.138 12.133 1.00 9.28  ? 112 GLY   C CA  1 
ATOM   1917 C  C   . GLY   B 1 106 ? 25.188 -25.429 13.583 1.00 8.99  ? 112 GLY   C C   1 
ATOM   1918 O  O   . GLY   B 1 106 ? 25.935 -24.647 14.196 1.00 9.07  ? 112 GLY   C O   1 
ATOM   1919 N  N   . ILE   B 1 107 ? 24.739 -26.563 14.119 1.00 8.88  ? 113 ILE   C N   1 
ATOM   1920 C  CA  . ILE   B 1 107 ? 25.024 -26.885 15.512 1.00 9.09  ? 113 ILE   C CA  1 
ATOM   1921 C  C   . ILE   B 1 107 ? 26.385 -27.520 15.704 1.00 8.82  ? 113 ILE   C C   1 
ATOM   1922 O  O   . ILE   B 1 107 ? 26.804 -28.388 14.933 1.00 8.97  ? 113 ILE   C O   1 
ATOM   1923 C  CB  . ILE   B 1 107 ? 23.870 -27.820 16.054 1.00 11.71 ? 113 ILE   C CB  1 
ATOM   1924 C  CG1 . ILE   B 1 107 ? 22.668 -26.850 16.510 1.00 14.34 ? 113 ILE   C CG1 1 
ATOM   1925 C  CG2 . ILE   B 1 107 ? 24.309 -28.691 17.264 1.00 12.12 ? 113 ILE   C CG2 1 
ATOM   1926 C  CD1 . ILE   B 1 107 ? 21.324 -27.562 16.882 1.00 18.85 ? 113 ILE   C CD1 1 
ATOM   1927 N  N   . LEU   B 1 108 ? 27.091 -27.073 16.790 1.00 8.14  ? 114 LEU   C N   1 
ATOM   1928 C  CA  . LEU   B 1 108 ? 28.265 -27.739 17.342 1.00 8.43  ? 114 LEU   C CA  1 
ATOM   1929 C  C   . LEU   B 1 108 ? 27.784 -28.498 18.601 1.00 8.64  ? 114 LEU   C C   1 
ATOM   1930 O  O   . LEU   B 1 108 ? 27.131 -27.905 19.455 1.00 8.41  ? 114 LEU   C O   1 
ATOM   1931 C  CB  . LEU   B 1 108 ? 29.316 -26.691 17.720 1.00 8.01  ? 114 LEU   C CB  1 
ATOM   1932 C  CG  . LEU   B 1 108 ? 30.513 -27.212 18.515 1.00 8.94  ? 114 LEU   C CG  1 
ATOM   1933 C  CD1 . LEU   B 1 108 ? 31.388 -28.133 17.653 1.00 10.33 ? 114 LEU   C CD1 1 
ATOM   1934 C  CD2 . LEU   B 1 108 ? 31.355 -26.032 19.029 1.00 10.43 ? 114 LEU   C CD2 1 
ATOM   1935 N  N   . ARG   B 1 109 ? 28.052 -29.805 18.660 1.00 8.59  ? 115 ARG   C N   1 
ATOM   1936 C  CA  . ARG   B 1 109 ? 27.604 -30.609 19.810 1.00 8.98  ? 115 ARG   C CA  1 
ATOM   1937 C  C   . ARG   B 1 109 ? 28.747 -31.427 20.360 1.00 9.95  ? 115 ARG   C C   1 
ATOM   1938 O  O   . ARG   B 1 109 ? 29.659 -31.846 19.635 1.00 10.52 ? 115 ARG   C O   1 
ATOM   1939 C  CB  . ARG   B 1 109 ? 26.445 -31.539 19.367 1.00 12.21 ? 115 ARG   C CB  1 
ATOM   1940 C  CG  . ARG   B 1 109 ? 26.882 -32.557 18.339 1.00 15.08 ? 115 ARG   C CG  1 
ATOM   1941 C  CD  . ARG   B 1 109 ? 25.781 -33.471 17.853 1.00 19.91 ? 115 ARG   C CD  1 
ATOM   1942 N  NE  . ARG   B 1 109 ? 24.896 -32.727 16.973 1.00 23.50 ? 115 ARG   C NE  1 
ATOM   1943 C  CZ  . ARG   B 1 109 ? 23.579 -32.827 16.988 1.00 29.34 ? 115 ARG   C CZ  1 
ATOM   1944 N  NH1 . ARG   B 1 109 ? 22.982 -33.700 17.793 1.00 29.66 ? 115 ARG   C NH1 1 
ATOM   1945 N  NH2 . ARG   B 1 109 ? 22.845 -32.093 16.164 1.00 30.92 ? 115 ARG   C NH2 1 
ATOM   1946 N  N   . CYS   B 1 110 ? 28.654 -31.703 21.648 1.00 10.19 ? 116 CYS   C N   1 
ATOM   1947 C  CA  . CYS   B 1 110 ? 29.612 -32.579 22.361 1.00 9.97  ? 116 CYS   C CA  1 
ATOM   1948 C  C   . CYS   B 1 110 ? 28.785 -33.676 23.062 1.00 11.31 ? 116 CYS   C C   1 
ATOM   1949 O  O   . CYS   B 1 110 ? 27.560 -33.790 22.862 1.00 11.42 ? 116 CYS   C O   1 
ATOM   1950 C  CB  . CYS   B 1 110 ? 30.423 -31.766 23.369 1.00 9.79  ? 116 CYS   C CB  1 
ATOM   1951 S  SG  . CYS   B 1 110 ? 29.421 -31.114 24.745 1.00 10.14 ? 116 CYS   C SG  1 
ATOM   1952 N  N   . GLN   B 1 111 ? 29.448 -34.516 23.916 1.00 12.74 ? 117 GLN   C N   1 
ATOM   1953 C  CA  . GLN   B 1 111 ? 28.678 -35.573 24.601 1.00 13.84 ? 117 GLN   C CA  1 
ATOM   1954 C  C   . GLN   B 1 111 ? 27.603 -35.019 25.543 1.00 14.39 ? 117 GLN   C C   1 
ATOM   1955 O  O   . GLN   B 1 111 ? 26.660 -35.738 25.902 1.00 15.97 ? 117 GLN   C O   1 
ATOM   1956 C  CB  . GLN   B 1 111 ? 29.605 -36.527 25.405 1.00 14.80 ? 117 GLN   C CB  1 
ATOM   1957 C  CG  . GLN   B 1 111 ? 30.285 -35.833 26.590 1.00 19.24 ? 117 GLN   C CG  1 
ATOM   1958 C  CD  . GLN   B 1 111 ? 31.238 -36.731 27.348 1.00 29.67 ? 117 GLN   C CD  1 
ATOM   1959 O  OE1 . GLN   B 1 111 ? 32.441 -36.738 27.075 1.00 32.65 ? 117 GLN   C OE1 1 
ATOM   1960 N  NE2 . GLN   B 1 111 ? 30.718 -37.454 28.334 1.00 30.12 ? 117 GLN   C NE2 1 
ATOM   1961 N  N   . HIS   B 1 112 ? 27.690 -33.729 25.930 1.00 12.17 ? 118 HIS   C N   1 
ATOM   1962 C  CA  . HIS   B 1 112 ? 26.733 -33.144 26.871 1.00 12.20 ? 118 HIS   C CA  1 
ATOM   1963 C  C   . HIS   B 1 112 ? 25.539 -32.457 26.220 1.00 12.36 ? 118 HIS   C C   1 
ATOM   1964 O  O   . HIS   B 1 112 ? 24.581 -32.072 26.910 1.00 13.74 ? 118 HIS   C O   1 
ATOM   1965 C  CB  . HIS   B 1 112 ? 27.450 -32.165 27.806 1.00 12.85 ? 118 HIS   C CB  1 
ATOM   1966 C  CG  . HIS   B 1 112 ? 28.632 -32.792 28.497 1.00 11.46 ? 118 HIS   C CG  1 
ATOM   1967 N  ND1 . HIS   B 1 112 ? 29.947 -32.547 28.101 1.00 11.74 ? 118 HIS   C ND1 1 
ATOM   1968 C  CD2 . HIS   B 1 112 ? 28.657 -33.635 29.565 1.00 13.90 ? 118 HIS   C CD2 1 
ATOM   1969 C  CE1 . HIS   B 1 112 ? 30.719 -33.242 28.921 1.00 12.63 ? 118 HIS   C CE1 1 
ATOM   1970 N  NE2 . HIS   B 1 112 ? 29.988 -33.892 29.831 1.00 14.95 ? 118 HIS   C NE2 1 
ATOM   1971 N  N   . GLY   B 1 113 ? 25.606 -32.216 24.903 1.00 11.26 ? 119 GLY   C N   1 
ATOM   1972 C  CA  . GLY   B 1 113 ? 24.533 -31.524 24.204 1.00 11.75 ? 119 GLY   C CA  1 
ATOM   1973 C  C   . GLY   B 1 113 ? 25.051 -30.458 23.250 1.00 10.36 ? 119 GLY   C C   1 
ATOM   1974 O  O   . GLY   B 1 113 ? 26.169 -30.564 22.730 1.00 9.76  ? 119 GLY   C O   1 
ATOM   1975 N  N   . VAL   B 1 114 ? 24.193 -29.455 22.969 1.00 9.42  ? 120 VAL   C N   1 
ATOM   1976 C  CA  . VAL   B 1 114 ? 24.522 -28.384 22.039 1.00 9.67  ? 120 VAL   C CA  1 
ATOM   1977 C  C   . VAL   B 1 114 ? 25.464 -27.381 22.714 1.00 9.86  ? 120 VAL   C C   1 
ATOM   1978 O  O   . VAL   B 1 114 ? 25.158 -26.818 23.783 1.00 10.25 ? 120 VAL   C O   1 
ATOM   1979 C  CB  . VAL   B 1 114 ? 23.230 -27.690 21.566 1.00 10.54 ? 120 VAL   C CB  1 
ATOM   1980 C  CG1 . VAL   B 1 114 ? 23.578 -26.480 20.699 1.00 12.11 ? 120 VAL   C CG1 1 
ATOM   1981 C  CG2 . VAL   B 1 114 ? 22.291 -28.661 20.832 1.00 12.48 ? 120 VAL   C CG2 1 
ATOM   1982 N  N   . VAL   B 1 115 ? 26.620 -27.146 22.084 1.00 8.70  ? 121 VAL   C N   1 
ATOM   1983 C  CA  . VAL   B 1 115 ? 27.634 -26.205 22.599 1.00 8.80  ? 121 VAL   C CA  1 
ATOM   1984 C  C   . VAL   B 1 115 ? 27.411 -24.783 22.067 1.00 9.27  ? 121 VAL   C C   1 
ATOM   1985 O  O   . VAL   B 1 115 ? 27.636 -23.796 22.789 1.00 9.94  ? 121 VAL   C O   1 
ATOM   1986 C  CB  . VAL   B 1 115 ? 29.035 -26.741 22.182 1.00 8.95  ? 121 VAL   C CB  1 
ATOM   1987 C  CG1 . VAL   B 1 115 ? 30.114 -25.737 22.569 1.00 10.93 ? 121 VAL   C CG1 1 
ATOM   1988 C  CG2 . VAL   B 1 115 ? 29.292 -28.122 22.808 1.00 10.26 ? 121 VAL   C CG2 1 
ATOM   1989 N  N   . GLY   B 1 116 ? 27.041 -24.689 20.802 1.00 8.65  ? 122 GLY   C N   1 
ATOM   1990 C  CA  . GLY   B 1 116 ? 26.823 -23.388 20.177 1.00 9.84  ? 122 GLY   C CA  1 
ATOM   1991 C  C   . GLY   B 1 116 ? 26.465 -23.551 18.716 1.00 8.97  ? 122 GLY   C C   1 
ATOM   1992 O  O   . GLY   B 1 116 ? 26.162 -24.672 18.278 1.00 9.37  ? 122 GLY   C O   1 
ATOM   1993 N  N   . ILE   B 1 117 ? 26.472 -22.411 17.978 1.00 8.22  ? 123 ILE   C N   1 
ATOM   1994 C  CA  . ILE   B 1 117 ? 26.127 -22.434 16.555 1.00 8.49  ? 123 ILE   C CA  1 
ATOM   1995 C  C   . ILE   B 1 117 ? 27.162 -21.701 15.745 1.00 8.04  ? 123 ILE   C C   1 
ATOM   1996 O  O   . ILE   B 1 117 ? 27.812 -20.731 16.209 1.00 9.75  ? 123 ILE   C O   1 
ATOM   1997 C  CB  . ILE   B 1 117 ? 24.711 -21.806 16.292 1.00 9.47  ? 123 ILE   C CB  1 
ATOM   1998 C  CG1 . ILE   B 1 117 ? 24.610 -20.406 16.913 1.00 10.35 ? 123 ILE   C CG1 1 
ATOM   1999 C  CG2 . ILE   B 1 117 ? 23.572 -22.737 16.746 1.00 11.44 ? 123 ILE   C CG2 1 
ATOM   2000 C  CD1 . ILE   B 1 117 ? 23.255 -19.639 16.496 1.00 11.53 ? 123 ILE   C CD1 1 
ATOM   2001 N  N   . VAL   B 1 118 ? 27.328 -22.137 14.487 1.00 8.38  ? 124 VAL   C N   1 
ATOM   2002 C  CA  . VAL   B 1 118 ? 28.265 -21.453 13.576 1.00 8.34  ? 124 VAL   C CA  1 
ATOM   2003 C  C   . VAL   B 1 118 ? 27.892 -19.968 13.458 1.00 8.70  ? 124 VAL   C C   1 
ATOM   2004 O  O   . VAL   B 1 118 ? 26.698 -19.633 13.261 1.00 9.11  ? 124 VAL   C O   1 
ATOM   2005 C  CB  . VAL   B 1 118 ? 28.245 -22.124 12.184 1.00 8.85  ? 124 VAL   C CB  1 
ATOM   2006 C  CG1 . VAL   B 1 118 ? 29.115 -21.365 11.180 1.00 10.03 ? 124 VAL   C CG1 1 
ATOM   2007 C  CG2 . VAL   B 1 118 ? 28.710 -23.578 12.266 1.00 9.70  ? 124 VAL   C CG2 1 
ATOM   2008 N  N   . SER   B 1 119 ? 28.920 -19.083 13.559 1.00 8.76  ? 125 SER   C N   1 
ATOM   2009 C  CA  . SER   B 1 119 ? 28.715 -17.636 13.447 1.00 9.06  ? 125 SER   C CA  1 
ATOM   2010 C  C   . SER   B 1 119 ? 29.716 -16.943 12.525 1.00 10.04 ? 125 SER   C C   1 
ATOM   2011 O  O   . SER   B 1 119 ? 29.384 -15.876 11.973 1.00 10.48 ? 125 SER   C O   1 
ATOM   2012 C  CB  . SER   B 1 119 ? 28.745 -17.044 14.852 1.00 9.39  ? 125 SER   C CB  1 
ATOM   2013 O  OG  . SER   B 1 119 ? 28.646 -15.611 14.823 1.00 10.81 ? 125 SER   C OG  1 
ATOM   2014 N  N   . THR   B 1 120 ? 30.949 -17.487 12.389 1.00 9.55  ? 126 THR   C N   1 
ATOM   2015 C  CA  . THR   B 1 120 ? 31.964 -16.803 11.565 1.00 10.16 ? 126 THR   C CA  1 
ATOM   2016 C  C   . THR   B 1 120 ? 32.669 -17.826 10.669 1.00 9.87  ? 126 THR   C C   1 
ATOM   2017 O  O   . THR   B 1 120 ? 32.613 -19.054 10.917 1.00 10.12 ? 126 THR   C O   1 
ATOM   2018 C  CB  . THR   B 1 120 ? 33.043 -16.073 12.451 1.00 10.18 ? 126 THR   C CB  1 
ATOM   2019 O  OG1 . THR   B 1 120 ? 33.906 -17.031 13.098 1.00 11.60 ? 126 THR   C OG1 1 
ATOM   2020 C  CG2 . THR   B 1 120 ? 32.452 -15.157 13.483 1.00 11.37 ? 126 THR   C CG2 1 
ATOM   2021 N  N   . GLY   B 1 121 ? 33.371 -17.338 9.663  1.00 11.16 ? 127 GLY   C N   1 
ATOM   2022 C  CA  . GLY   B 1 121 ? 34.166 -18.208 8.790  1.00 12.65 ? 127 GLY   C CA  1 
ATOM   2023 C  C   . GLY   B 1 121 ? 35.179 -17.391 8.022  1.00 17.03 ? 127 GLY   C C   1 
ATOM   2024 O  O   . GLY   B 1 121 ? 34.923 -16.227 7.702  1.00 18.02 ? 127 GLY   C O   1 
ATOM   2025 N  N   . GLY   B 1 122 ? 36.307 -17.974 7.717  1.00 21.51 ? 128 GLY   C N   1 
ATOM   2026 C  CA  . GLY   B 1 122 ? 37.346 -17.253 6.976  1.00 24.04 ? 128 GLY   C CA  1 
ATOM   2027 C  C   . GLY   B 1 122 ? 38.711 -17.776 7.295  1.00 23.51 ? 128 GLY   C C   1 
ATOM   2028 O  O   . GLY   B 1 122 ? 38.940 -18.232 8.401  1.00 23.24 ? 128 GLY   C O   1 
ATOM   2029 N  N   . ASN   B 1 123 ? 39.647 -17.674 6.332  1.00 23.06 ? 129 ASN   C N   1 
ATOM   2030 C  CA  . ASN   B 1 123 ? 41.028 -18.113 6.505  1.00 22.93 ? 129 ASN   C CA  1 
ATOM   2031 C  C   . ASN   B 1 123 ? 41.124 -19.595 6.912  1.00 20.31 ? 129 ASN   C C   1 
ATOM   2032 O  O   . ASN   B 1 123 ? 42.094 -19.945 7.585  1.00 22.77 ? 129 ASN   C O   1 
ATOM   2033 C  CB  . ASN   B 1 123 ? 41.776 -17.220 7.525  1.00 26.74 ? 129 ASN   C CB  1 
ATOM   2034 C  CG  . ASN   B 1 123 ? 42.525 -16.065 6.908  1.00 33.32 ? 129 ASN   C CG  1 
ATOM   2035 O  OD1 . ASN   B 1 123 ? 42.814 -16.039 5.707  1.00 33.87 ? 129 ASN   C OD1 1 
ATOM   2036 N  ND2 . ASN   B 1 123 ? 42.881 -15.074 7.718  1.00 36.19 ? 129 ASN   C ND2 1 
ATOM   2037 N  N   . GLY   B 1 124 ? 40.169 -20.458 6.497  1.00 18.37 ? 130 GLY   C N   1 
ATOM   2038 C  CA  . GLY   B 1 124 ? 40.183 -21.878 6.878  1.00 16.84 ? 130 GLY   C CA  1 
ATOM   2039 C  C   . GLY   B 1 124 ? 39.782 -22.146 8.322  1.00 14.57 ? 130 GLY   C C   1 
ATOM   2040 O  O   . GLY   B 1 124 ? 40.035 -23.236 8.858  1.00 14.21 ? 130 GLY   C O   1 
ATOM   2041 N  N   . LEU   B 1 125 ? 39.133 -21.141 8.955  1.00 14.12 ? 131 LEU   C N   1 
ATOM   2042 C  CA  . LEU   B 1 125 ? 38.671 -21.245 10.341 1.00 13.22 ? 131 LEU   C CA  1 
ATOM   2043 C  C   . LEU   B 1 125 ? 37.158 -21.151 10.360 1.00 12.90 ? 131 LEU   C C   1 
ATOM   2044 O  O   . LEU   B 1 125 ? 36.532 -20.534 9.460  1.00 15.64 ? 131 LEU   C O   1 
ATOM   2045 C  CB  . LEU   B 1 125 ? 39.281 -20.129 11.235 1.00 15.31 ? 131 LEU   C CB  1 
ATOM   2046 C  CG  . LEU   B 1 125 ? 40.816 -20.122 11.333 1.00 18.75 ? 131 LEU   C CG  1 
ATOM   2047 C  CD1 . LEU   B 1 125 ? 41.352 -18.779 11.813 1.00 22.34 ? 131 LEU   C CD1 1 
ATOM   2048 C  CD2 . LEU   B 1 125 ? 41.333 -21.245 12.159 1.00 19.65 ? 131 LEU   C CD2 1 
ATOM   2049 N  N   . VAL   B 1 126 ? 36.552 -21.788 11.333 1.00 10.20 ? 132 VAL   C N   1 
ATOM   2050 C  CA  . VAL   B 1 126 ? 35.118 -21.681 11.558 1.00 9.86  ? 132 VAL   C CA  1 
ATOM   2051 C  C   . VAL   B 1 126 ? 34.963 -21.223 13.036 1.00 9.10  ? 132 VAL   C C   1 
ATOM   2052 O  O   . VAL   B 1 126 ? 35.655 -21.744 13.928 1.00 9.79  ? 132 VAL   C O   1 
ATOM   2053 C  CB  . VAL   B 1 126 ? 34.363 -23.027 11.327 1.00 10.38 ? 132 VAL   C CB  1 
ATOM   2054 C  CG1 . VAL   B 1 126 ? 34.991 -24.209 12.047 1.00 12.65 ? 132 VAL   C CG1 1 
ATOM   2055 C  CG2 . VAL   B 1 126 ? 32.869 -22.913 11.693 1.00 10.94 ? 132 VAL   C CG2 1 
ATOM   2056 N  N   . GLY   B 1 127 ? 34.105 -20.234 13.267 1.00 8.55  ? 133 GLY   C N   1 
ATOM   2057 C  CA  . GLY   B 1 127 ? 33.872 -19.738 14.618 1.00 8.62  ? 133 GLY   C CA  1 
ATOM   2058 C  C   . GLY   B 1 127 ? 32.452 -20.082 15.051 1.00 9.12  ? 133 GLY   C C   1 
ATOM   2059 O  O   . GLY   B 1 127 ? 31.503 -19.937 14.255 1.00 9.39  ? 133 GLY   C O   1 
ATOM   2060 N  N   . PHE   B 1 128 ? 32.327 -20.448 16.325 1.00 8.12  ? 134 PHE   C N   1 
ATOM   2061 C  CA  . PHE   B 1 128 ? 31.029 -20.826 16.931 1.00 8.62  ? 134 PHE   C CA  1 
ATOM   2062 C  C   . PHE   B 1 128 ? 30.698 -19.885 18.080 1.00 8.59  ? 134 PHE   C C   1 
ATOM   2063 O  O   . PHE   B 1 128 ? 31.547 -19.629 18.940 1.00 9.22  ? 134 PHE   C O   1 
ATOM   2064 C  CB  . PHE   B 1 128 ? 31.102 -22.270 17.506 1.00 8.47  ? 134 PHE   C CB  1 
ATOM   2065 C  CG  . PHE   B 1 128 ? 31.622 -23.289 16.517 1.00 8.40  ? 134 PHE   C CG  1 
ATOM   2066 C  CD1 . PHE   B 1 128 ? 30.771 -23.873 15.581 1.00 8.29  ? 134 PHE   C CD1 1 
ATOM   2067 C  CD2 . PHE   B 1 128 ? 32.970 -23.656 16.517 1.00 8.99  ? 134 PHE   C CD2 1 
ATOM   2068 C  CE1 . PHE   B 1 128 ? 31.249 -24.844 14.708 1.00 9.29  ? 134 PHE   C CE1 1 
ATOM   2069 C  CE2 . PHE   B 1 128 ? 33.454 -24.613 15.607 1.00 9.23  ? 134 PHE   C CE2 1 
ATOM   2070 C  CZ  . PHE   B 1 128 ? 32.594 -25.216 14.726 1.00 9.25  ? 134 PHE   C CZ  1 
ATOM   2071 N  N   . ALA   B 1 129 ? 29.448 -19.389 18.107 1.00 8.48  ? 135 ALA   C N   1 
ATOM   2072 C  CA  . ALA   B 1 129 ? 28.964 -18.583 19.221 1.00 8.58  ? 135 ALA   C CA  1 
ATOM   2073 C  C   . ALA   B 1 129 ? 28.572 -19.572 20.348 1.00 9.24  ? 135 ALA   C C   1 
ATOM   2074 O  O   . ALA   B 1 129 ? 27.656 -20.398 20.192 1.00 9.89  ? 135 ALA   C O   1 
ATOM   2075 C  CB  . ALA   B 1 129 ? 27.736 -17.780 18.764 1.00 9.48  ? 135 ALA   C CB  1 
ATOM   2076 N  N   . ASP   B 1 130 ? 29.245 -19.487 21.488 1.00 9.19  ? 136 ASP   C N   1 
ATOM   2077 C  CA  . ASP   B 1 130 ? 28.979 -20.370 22.631 1.00 9.34  ? 136 ASP   C CA  1 
ATOM   2078 C  C   . ASP   B 1 130 ? 27.634 -20.027 23.243 1.00 9.74  ? 136 ASP   C C   1 
ATOM   2079 O  O   . ASP   B 1 130 ? 27.255 -18.838 23.325 1.00 10.43 ? 136 ASP   C O   1 
ATOM   2080 C  CB  . ASP   B 1 130 ? 30.071 -20.137 23.699 1.00 10.70 ? 136 ASP   C CB  1 
ATOM   2081 C  CG  . ASP   B 1 130 ? 29.962 -21.067 24.894 1.00 13.31 ? 136 ASP   C CG  1 
ATOM   2082 O  OD1 . ASP   B 1 130 ? 29.819 -22.286 24.697 1.00 12.49 ? 136 ASP   C OD1 1 
ATOM   2083 O  OD2 . ASP   B 1 130 ? 29.944 -20.557 26.042 1.00 15.77 ? 136 ASP   C OD2 1 
ATOM   2084 N  N   . VAL   B 1 131 ? 26.925 -21.052 23.740 1.00 9.52  ? 137 VAL   C N   1 
ATOM   2085 C  CA  . VAL   B 1 131 ? 25.680 -20.846 24.517 1.00 9.83  ? 137 VAL   C CA  1 
ATOM   2086 C  C   . VAL   B 1 131 ? 25.746 -21.523 25.889 1.00 10.71 ? 137 VAL   C C   1 
ATOM   2087 O  O   . VAL   B 1 131 ? 24.768 -21.465 26.648 1.00 10.95 ? 137 VAL   C O   1 
ATOM   2088 C  CB  . VAL   B 1 131 ? 24.392 -21.293 23.771 1.00 10.01 ? 137 VAL   C CB  1 
ATOM   2089 C  CG1 . VAL   B 1 131 ? 24.212 -20.470 22.467 1.00 10.53 ? 137 VAL   C CG1 1 
ATOM   2090 C  CG2 . VAL   B 1 131 ? 24.405 -22.788 23.463 1.00 10.50 ? 137 VAL   C CG2 1 
ATOM   2091 N  N   . ARG   B 1 132 ? 26.860 -22.190 26.224 1.00 9.72  ? 138 ARG   C N   1 
ATOM   2092 C  CA  . ARG   B 1 132 ? 26.942 -22.969 27.477 1.00 9.98  ? 138 ARG   C CA  1 
ATOM   2093 C  C   . ARG   B 1 132 ? 26.889 -22.139 28.752 1.00 10.62 ? 138 ARG   C C   1 
ATOM   2094 O  O   . ARG   B 1 132 ? 26.596 -22.691 29.830 1.00 11.99 ? 138 ARG   C O   1 
ATOM   2095 C  CB  . ARG   B 1 132 ? 28.207 -23.823 27.460 1.00 10.05 ? 138 ARG   C CB  1 
ATOM   2096 C  CG  . ARG   B 1 132 ? 28.208 -24.865 26.334 1.00 9.53  ? 138 ARG   C CG  1 
ATOM   2097 C  CD  . ARG   B 1 132 ? 29.515 -25.637 26.369 1.00 10.02 ? 138 ARG   C CD  1 
ATOM   2098 N  NE  . ARG   B 1 132 ? 30.611 -24.750 25.949 1.00 9.69  ? 138 ARG   C NE  1 
ATOM   2099 C  CZ  . ARG   B 1 132 ? 31.870 -25.143 25.789 1.00 10.65 ? 138 ARG   C CZ  1 
ATOM   2100 N  NH1 . ARG   B 1 132 ? 32.247 -26.379 26.142 1.00 10.49 ? 138 ARG   C NH1 1 
ATOM   2101 N  NH2 . ARG   B 1 132 ? 32.781 -24.293 25.320 1.00 11.38 ? 138 ARG   C NH2 1 
ATOM   2102 N  N   . ASP   B 1 133 ? 27.205 -20.842 28.676 1.00 10.36 ? 139 ASP   C N   1 
ATOM   2103 C  CA  . ASP   B 1 133 ? 27.151 -19.967 29.842 1.00 10.75 ? 139 ASP   C CA  1 
ATOM   2104 C  C   . ASP   B 1 133 ? 25.737 -19.423 30.106 1.00 12.06 ? 139 ASP   C C   1 
ATOM   2105 O  O   . ASP   B 1 133 ? 25.545 -18.813 31.172 1.00 12.82 ? 139 ASP   C O   1 
ATOM   2106 C  CB  . ASP   B 1 133 ? 28.128 -18.771 29.686 1.00 12.67 ? 139 ASP   C CB  1 
ATOM   2107 C  CG  . ASP   B 1 133 ? 27.742 -17.853 28.550 1.00 13.49 ? 139 ASP   C CG  1 
ATOM   2108 O  OD1 . ASP   B 1 133 ? 27.383 -18.365 27.464 1.00 12.49 ? 139 ASP   C OD1 1 
ATOM   2109 O  OD2 . ASP   B 1 133 ? 27.751 -16.597 28.754 1.00 16.69 ? 139 ASP   C OD2 1 
ATOM   2110 N  N   . LEU   B 1 134 ? 24.776 -19.627 29.167 1.00 11.49 ? 140 LEU   C N   1 
ATOM   2111 C  CA  . LEU   B 1 134 ? 23.417 -19.070 29.259 1.00 11.52 ? 140 LEU   C CA  1 
ATOM   2112 C  C   . LEU   B 1 134 ? 22.543 -20.016 30.046 1.00 11.72 ? 140 LEU   C C   1 
ATOM   2113 O  O   . LEU   B 1 134 ? 21.741 -20.770 29.487 1.00 11.73 ? 140 LEU   C O   1 
ATOM   2114 C  CB  . LEU   B 1 134 ? 22.849 -18.804 27.850 1.00 11.12 ? 140 LEU   C CB  1 
ATOM   2115 C  CG  . LEU   B 1 134 ? 23.718 -17.855 26.983 1.00 12.10 ? 140 LEU   C CG  1 
ATOM   2116 C  CD1 . LEU   B 1 134 ? 23.121 -17.745 25.537 1.00 13.55 ? 140 LEU   C CD1 1 
ATOM   2117 C  CD2 . LEU   B 1 134 ? 23.830 -16.455 27.619 1.00 13.94 ? 140 LEU   C CD2 1 
ATOM   2118 N  N   . LEU   B 1 135 ? 22.766 -20.058 31.380 1.00 11.95 ? 141 LEU   C N   1 
ATOM   2119 C  CA  . LEU   B 1 135 ? 22.129 -21.092 32.216 1.00 12.80 ? 141 LEU   C CA  1 
ATOM   2120 C  C   . LEU   B 1 135 ? 20.617 -20.996 32.259 1.00 12.50 ? 141 LEU   C C   1 
ATOM   2121 O  O   . LEU   B 1 135 ? 19.951 -22.016 32.458 1.00 13.88 ? 141 LEU   C O   1 
ATOM   2122 C  CB  . LEU   B 1 135 ? 22.721 -21.101 33.654 1.00 12.57 ? 141 LEU   C CB  1 
ATOM   2123 C  CG  . LEU   B 1 135 ? 24.276 -21.086 33.728 1.00 13.09 ? 141 LEU   C CG  1 
ATOM   2124 C  CD1 . LEU   B 1 135 ? 24.774 -21.097 35.193 1.00 13.85 ? 141 LEU   C CD1 1 
ATOM   2125 C  CD2 . LEU   B 1 135 ? 24.904 -22.243 32.924 1.00 13.96 ? 141 LEU   C CD2 1 
ATOM   2126 N  N   . TRP   B 1 136 ? 20.091 -19.782 32.046 1.00 12.60 ? 142 TRP   C N   1 
ATOM   2127 C  CA  . TRP   B 1 136 ? 18.657 -19.524 32.091 1.00 13.90 ? 142 TRP   C CA  1 
ATOM   2128 C  C   . TRP   B 1 136 ? 17.917 -20.230 30.940 1.00 14.46 ? 142 TRP   C C   1 
ATOM   2129 O  O   . TRP   B 1 136 ? 16.693 -20.386 31.014 1.00 16.24 ? 142 TRP   C O   1 
ATOM   2130 C  CB  . TRP   B 1 136 ? 18.399 -18.010 32.098 1.00 13.93 ? 142 TRP   C CB  1 
ATOM   2131 C  CG  . TRP   B 1 136 ? 19.091 -17.257 30.995 1.00 13.98 ? 142 TRP   C CG  1 
ATOM   2132 C  CD1 . TRP   B 1 136 ? 20.281 -16.588 31.071 1.00 14.98 ? 142 TRP   C CD1 1 
ATOM   2133 C  CD2 . TRP   B 1 136 ? 18.583 -17.022 29.660 1.00 14.15 ? 142 TRP   C CD2 1 
ATOM   2134 N  NE1 . TRP   B 1 136 ? 20.572 -15.990 29.850 1.00 15.45 ? 142 TRP   C NE1 1 
ATOM   2135 C  CE2 . TRP   B 1 136 ? 19.534 -16.233 28.975 1.00 14.81 ? 142 TRP   C CE2 1 
ATOM   2136 C  CE3 . TRP   B 1 136 ? 17.438 -17.436 28.978 1.00 14.70 ? 142 TRP   C CE3 1 
ATOM   2137 C  CZ2 . TRP   B 1 136 ? 19.359 -15.841 27.632 1.00 14.67 ? 142 TRP   C CZ2 1 
ATOM   2138 C  CZ3 . TRP   B 1 136 ? 17.229 -16.981 27.679 1.00 15.08 ? 142 TRP   C CZ3 1 
ATOM   2139 C  CH2 . TRP   B 1 136 ? 18.198 -16.223 27.014 1.00 15.43 ? 142 TRP   C CH2 1 
ATOM   2140 N  N   . LEU   B 1 137 ? 18.629 -20.696 29.898 1.00 13.05 ? 143 LEU   C N   1 
ATOM   2141 C  CA  . LEU   B 1 137 ? 17.959 -21.465 28.832 1.00 13.49 ? 143 LEU   C CA  1 
ATOM   2142 C  C   . LEU   B 1 137 ? 17.357 -22.772 29.394 1.00 16.06 ? 143 LEU   C C   1 
ATOM   2143 O  O   . LEU   B 1 137 ? 16.434 -23.322 28.789 1.00 17.74 ? 143 LEU   C O   1 
ATOM   2144 C  CB  . LEU   B 1 137 ? 18.918 -21.799 27.683 1.00 12.91 ? 143 LEU   C CB  1 
ATOM   2145 C  CG  . LEU   B 1 137 ? 19.351 -20.614 26.812 1.00 12.63 ? 143 LEU   C CG  1 
ATOM   2146 C  CD1 . LEU   B 1 137 ? 20.486 -21.034 25.845 1.00 13.60 ? 143 LEU   C CD1 1 
ATOM   2147 C  CD2 . LEU   B 1 137 ? 18.181 -20.052 25.996 1.00 13.71 ? 143 LEU   C CD2 1 
ATOM   2148 N  N   . ASP   B 1 138 ? 17.864 -23.264 30.560 1.00 14.95 ? 144 ASP   C N   1 
ATOM   2149 C  CA  . ASP   B 1 138 ? 17.403 -24.529 31.156 1.00 16.08 ? 144 ASP   C CA  1 
ATOM   2150 C  C   . ASP   B 1 138 ? 16.170 -24.371 32.050 1.00 19.75 ? 144 ASP   C C   1 
ATOM   2151 O  O   . ASP   B 1 138 ? 15.722 -25.379 32.610 1.00 20.76 ? 144 ASP   C O   1 
ATOM   2152 C  CB  . ASP   B 1 138 ? 18.522 -25.197 31.989 1.00 15.54 ? 144 ASP   C CB  1 
ATOM   2153 C  CG  . ASP   B 1 138 ? 19.751 -25.635 31.197 1.00 16.73 ? 144 ASP   C CG  1 
ATOM   2154 O  OD1 . ASP   B 1 138 ? 19.691 -25.649 29.951 1.00 16.04 ? 144 ASP   C OD1 1 
ATOM   2155 O  OD2 . ASP   B 1 138 ? 20.782 -25.984 31.841 1.00 18.70 ? 144 ASP   C OD2 1 
ATOM   2156 N  N   . GLU   B 1 139 ? 15.639 -23.161 32.214 1.00 22.00 ? 145 GLU   C N   1 
ATOM   2157 C  CA  . GLU   B 1 139 ? 14.492 -22.948 33.114 1.00 26.57 ? 145 GLU   C CA  1 
ATOM   2158 C  C   . GLU   B 1 139 ? 13.424 -22.003 32.523 1.00 31.34 ? 145 GLU   C C   1 
ATOM   2159 O  O   . GLU   B 1 139 ? 13.671 -21.316 31.533 1.00 32.27 ? 145 GLU   C O   1 
ATOM   2160 C  CB  . GLU   B 1 139 ? 15.033 -22.361 34.437 1.00 31.10 ? 145 GLU   C CB  1 
ATOM   2161 C  CG  . GLU   B 1 139 ? 15.680 -21.002 34.235 1.00 37.91 ? 145 GLU   C CG  1 
ATOM   2162 C  CD  . GLU   B 1 139 ? 16.677 -20.554 35.288 1.00 46.38 ? 145 GLU   C CD  1 
ATOM   2163 O  OE1 . GLU   B 1 139 ? 16.938 -19.332 35.380 1.00 45.40 ? 145 GLU   C OE1 1 
ATOM   2164 O  OE2 . GLU   B 1 139 ? 17.191 -21.426 36.025 1.00 50.49 ? 145 GLU   C OE2 1 
ATOM   2165 N  N   . GLU   B 1 140 ? 12.275 -21.888 33.221 1.00 34.25 ? 146 GLU   C N   1 
ATOM   2166 C  CA  . GLU   B 1 140 ? 11.146 -20.972 32.976 1.00 37.17 ? 146 GLU   C CA  1 
ATOM   2167 C  C   . GLU   B 1 140 ? 11.083 -20.325 31.601 1.00 38.76 ? 146 GLU   C C   1 
ATOM   2168 O  O   . GLU   B 1 140 ? 10.566 -19.215 31.455 1.00 39.21 ? 146 GLU   C O   1 
ATOM   2169 C  CB  . GLU   B 1 140 ? 11.133 -19.877 34.056 1.00 40.85 ? 146 GLU   C CB  1 
ATOM   2170 C  CG  . GLU   B 1 140 ? 12.355 -18.975 34.054 1.00 47.62 ? 146 GLU   C CG  1 
ATOM   2171 C  CD  . GLU   B 1 140 ? 12.077 -17.517 33.724 1.00 57.13 ? 146 GLU   C CD  1 
ATOM   2172 O  OE1 . GLU   B 1 140 ? 13.016 -16.698 33.846 1.00 59.54 ? 146 GLU   C OE1 1 
ATOM   2173 O  OE2 . GLU   B 1 140 ? 10.928 -17.194 33.335 1.00 59.25 ? 146 GLU   C OE2 1 
HETATM 2174 N  N1  . A1BQJ C 2 .   ? 9.997  17.413  17.661 1.00 15.04 ? 201 A1BQJ A N1  1 
HETATM 2175 C  C4  . A1BQJ C 2 .   ? 6.084  13.087  25.105 1.00 17.74 ? 201 A1BQJ A C4  1 
HETATM 2176 C  C5  . A1BQJ C 2 .   ? 6.971  13.851  24.357 1.00 18.24 ? 201 A1BQJ A C5  1 
HETATM 2177 C  C6  . A1BQJ C 2 .   ? 7.915  13.241  23.528 1.00 18.27 ? 201 A1BQJ A C6  1 
HETATM 2178 C  C7  . A1BQJ C 2 .   ? 9.001  14.027  22.828 1.00 17.63 ? 201 A1BQJ A C7  1 
HETATM 2179 C  C8  . A1BQJ C 2 .   ? 8.769  15.525  22.641 1.00 18.57 ? 201 A1BQJ A C8  1 
HETATM 2180 C  C10 . A1BQJ C 2 .   ? 10.623 15.945  19.476 1.00 16.93 ? 201 A1BQJ A C10 1 
HETATM 2181 C  C13 . A1BQJ C 2 .   ? 10.781 16.675  21.730 1.00 19.14 ? 201 A1BQJ A C13 1 
HETATM 2182 O  O2  . A1BQJ C 2 .   ? 11.224 17.028  22.823 1.00 19.90 ? 201 A1BQJ A O2  1 
HETATM 2183 C  C12 . A1BQJ C 2 .   ? 11.374 16.948  20.377 1.00 16.99 ? 201 A1BQJ A C12 1 
HETATM 2184 C  C11 . A1BQJ C 2 .   ? 10.564 16.268  17.993 1.00 16.26 ? 201 A1BQJ A C11 1 
HETATM 2185 O  O1  . A1BQJ C 2 .   ? 10.961 15.460  17.151 1.00 15.50 ? 201 A1BQJ A O1  1 
HETATM 2186 C  C9  . A1BQJ C 2 .   ? 9.251  15.881  20.129 1.00 17.58 ? 201 A1BQJ A C9  1 
HETATM 2187 N  N   . A1BQJ C 2 .   ? 9.607  16.029  21.544 1.00 18.64 ? 201 A1BQJ A N   1 
HETATM 2188 C  C1  . A1BQJ C 2 .   ? 7.893  11.852  23.411 1.00 17.90 ? 201 A1BQJ A C1  1 
HETATM 2189 O  O   . A1BQJ C 2 .   ? 8.829  11.344  22.545 1.00 19.06 ? 201 A1BQJ A O   1 
HETATM 2190 C  C   . A1BQJ C 2 .   ? 8.944  9.924   22.434 1.00 19.54 ? 201 A1BQJ A C   1 
HETATM 2191 C  C3  . A1BQJ C 2 .   ? 6.116  11.706  25.020 1.00 17.72 ? 201 A1BQJ A C3  1 
HETATM 2192 C  C2  . A1BQJ C 2 .   ? 7.004  11.083  24.155 1.00 17.11 ? 201 A1BQJ A C2  1 
HETATM 2193 ZN ZN  . ZN    D 3 .   ? 11.178 -4.052  5.831  1.00 17.36 2 202 ZN    A ZN  1 
HETATM 2194 S  S   . DMS   E 4 .   ? 18.957 -2.118  24.559 1.00 85.11 ? 203 DMS   A S   1 
HETATM 2195 O  O   . DMS   E 4 .   ? 19.631 -0.788  24.362 1.00 85.05 ? 203 DMS   A O   1 
HETATM 2196 C  C1  . DMS   E 4 .   ? 18.140 -2.552  23.007 1.00 85.05 ? 203 DMS   A C1  1 
HETATM 2197 C  C2  . DMS   E 4 .   ? 20.226 -3.408  24.470 1.00 85.16 ? 203 DMS   A C2  1 
HETATM 2198 ZN ZN  . ZN    F 3 .   ? 30.639 -31.184 26.693 1.00 10.85 2 201 ZN    C ZN  1 
HETATM 2199 S  S   . DMS   G 4 .   ? 20.852 -32.347 9.359  1.00 81.10 ? 202 DMS   C S   1 
HETATM 2200 O  O   . DMS   G 4 .   ? 22.002 -32.725 8.482  1.00 81.35 ? 202 DMS   C O   1 
HETATM 2201 C  C1  . DMS   G 4 .   ? 21.425 -32.357 11.065 1.00 81.04 ? 202 DMS   C C1  1 
HETATM 2202 C  C2  . DMS   G 4 .   ? 20.633 -30.551 9.253  1.00 80.99 ? 202 DMS   C C2  1 
HETATM 2203 O  O   . HOH   H 5 .   ? 11.259 8.755   4.202  1.00 19.85 ? 301 HOH   A O   1 
HETATM 2204 O  O   . HOH   H 5 .   ? 1.853  23.053  20.835 1.00 27.44 ? 302 HOH   A O   1 
HETATM 2205 O  O   . HOH   H 5 .   ? 2.999  9.452   8.816  1.00 26.19 ? 303 HOH   A O   1 
HETATM 2206 O  O   . HOH   H 5 .   ? 35.320 -3.872  7.819  1.00 21.32 ? 304 HOH   A O   1 
HETATM 2207 O  O   . HOH   H 5 .   ? 27.970 7.961   1.830  1.00 31.77 ? 305 HOH   A O   1 
HETATM 2208 O  O   . HOH   H 5 .   ? 14.123 17.422  4.228  1.00 33.01 ? 306 HOH   A O   1 
HETATM 2209 O  O   . HOH   H 5 .   ? 14.018 2.784   1.206  1.00 24.13 ? 307 HOH   A O   1 
HETATM 2210 O  O   . HOH   H 5 .   ? 37.508 15.011  13.927 1.00 48.63 ? 308 HOH   A O   1 
HETATM 2211 O  O   . HOH   H 5 .   ? 31.151 -2.106  15.632 1.00 48.00 ? 309 HOH   A O   1 
HETATM 2212 O  O   . HOH   H 5 .   ? 29.266 22.316  19.381 1.00 33.99 ? 310 HOH   A O   1 
HETATM 2213 O  O   . HOH   H 5 .   ? -3.182 9.908   27.814 1.00 35.56 ? 311 HOH   A O   1 
HETATM 2214 O  O   . HOH   H 5 .   ? 0.376  -1.017  19.267 1.00 24.54 ? 312 HOH   A O   1 
HETATM 2215 O  O   . HOH   H 5 .   ? 12.243 15.666  24.845 1.00 24.33 ? 313 HOH   A O   1 
HETATM 2216 O  O   . HOH   H 5 .   ? 30.414 10.628  15.697 1.00 26.99 ? 314 HOH   A O   1 
HETATM 2217 O  O   . HOH   H 5 .   ? 17.326 1.015   28.254 1.00 21.34 ? 315 HOH   A O   1 
HETATM 2218 O  O   . HOH   H 5 .   ? 23.393 21.745  7.217  1.00 25.53 ? 316 HOH   A O   1 
HETATM 2219 O  O   . HOH   H 5 .   ? 7.365  20.521  17.147 1.00 17.23 ? 317 HOH   A O   1 
HETATM 2220 O  O   . HOH   H 5 .   ? 4.475  -3.629  28.788 1.00 27.25 ? 318 HOH   A O   1 
HETATM 2221 O  O   . HOH   H 5 .   ? 8.713  19.199  19.352 1.00 16.85 ? 319 HOH   A O   1 
HETATM 2222 O  O   . HOH   H 5 .   ? 2.520  -2.924  20.668 1.00 27.54 ? 320 HOH   A O   1 
HETATM 2223 O  O   . HOH   H 5 .   ? 35.347 8.076   9.649  1.00 46.74 ? 321 HOH   A O   1 
HETATM 2224 O  O   . HOH   H 5 .   ? 19.207 10.140  19.591 1.00 10.68 ? 322 HOH   A O   1 
HETATM 2225 O  O   . HOH   H 5 .   ? 24.847 5.150   21.453 1.00 26.50 ? 323 HOH   A O   1 
HETATM 2226 O  O   . HOH   H 5 .   ? 36.315 -2.518  11.028 1.00 26.10 ? 324 HOH   A O   1 
HETATM 2227 O  O   . HOH   H 5 .   ? 33.759 14.227  9.780  1.00 31.30 ? 325 HOH   A O   1 
HETATM 2228 O  O   . HOH   H 5 .   ? 28.190 3.200   5.036  1.00 29.26 ? 326 HOH   A O   1 
HETATM 2229 O  O   . HOH   H 5 .   ? -0.142 1.286   15.721 1.00 11.47 ? 327 HOH   A O   1 
HETATM 2230 O  O   . HOH   H 5 .   ? 9.605  22.025  10.160 1.00 41.62 ? 328 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 5 .   ? 12.207 22.251  12.345 1.00 29.50 ? 329 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 5 .   ? 3.146  21.149  24.169 1.00 35.64 ? 330 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 5 .   ? 11.526 18.127  4.928  1.00 29.59 ? 331 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 5 .   ? 3.947  9.511   27.837 1.00 27.25 ? 332 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 5 .   ? 33.540 11.049  15.700 1.00 38.77 ? 333 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 14.951 11.324  0.018  1.00 28.39 ? 334 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 10.303 10.069  31.342 1.00 20.12 ? 335 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 29.436 11.208  3.319  1.00 51.69 ? 336 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? 15.750 24.004  14.589 1.00 37.17 ? 337 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 13.930 13.692  23.843 1.00 15.55 ? 338 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 22.575 0.911   17.426 1.00 13.95 ? 339 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? 5.334  5.334   32.571 1.00 17.88 ? 340 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? 8.247  25.065  23.491 1.00 21.95 ? 341 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? 18.384 21.917  9.505  1.00 16.46 ? 342 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 13.611 4.047   23.460 1.00 10.93 ? 343 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? 11.307 12.616  10.920 1.00 13.13 ? 344 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 29.778 11.683  18.434 1.00 26.25 ? 345 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 20.930 -4.134  14.203 1.00 14.45 ? 346 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 6.123  2.287   5.405  1.00 21.97 ? 347 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 20.708 -1.026  3.040  1.00 29.61 ? 348 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? 5.013  8.257   2.204  1.00 29.59 ? 349 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 16.495 3.908   23.655 1.00 14.00 ? 350 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? 19.762 20.417  5.817  1.00 42.83 ? 351 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? 29.344 12.039  21.408 1.00 29.25 ? 352 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 3.708  -8.129  9.710  1.00 52.12 ? 353 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? 21.951 2.463   -0.844 1.00 30.02 ? 354 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 9.213  2.969   2.744  1.00 30.15 ? 355 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? 30.508 3.041   14.904 1.00 21.57 ? 356 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 11.958 11.097  29.598 1.00 17.23 ? 357 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 21.307 4.897   24.713 1.00 40.95 ? 358 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? -1.639 13.883  22.142 1.00 53.16 ? 359 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 31.581 20.031  11.793 1.00 21.72 ? 360 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? 3.100  0.323   28.995 1.00 36.50 ? 361 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 16.994 -3.389  27.770 1.00 29.95 ? 362 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 23.563 3.712   -2.273 1.00 40.64 ? 363 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 23.234 -6.436  11.993 1.00 30.29 ? 364 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? 6.041  17.214  21.067 1.00 21.85 ? 365 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 20.098 17.832  24.034 1.00 32.92 ? 366 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 9.399  4.027   33.434 1.00 11.19 ? 367 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 13.258 11.395  9.097  1.00 11.37 ? 368 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? 20.807 -2.536  16.917 1.00 12.55 ? 369 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 22.593 19.563  19.948 1.00 26.21 ? 370 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? 28.897 3.400   12.776 1.00 13.90 ? 371 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 29.985 -1.336  8.685  1.00 29.69 ? 372 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 5.318  14.635  20.338 1.00 22.00 ? 373 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 15.276 -4.864  0.427  1.00 37.69 ? 374 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 7.193  26.384  13.994 1.00 31.13 ? 375 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 23.245 11.676  21.967 1.00 29.43 ? 376 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 18.114 17.849  4.250  1.00 34.51 ? 377 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 5.577  18.067  23.608 1.00 27.79 ? 378 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 24.205 -3.385  16.112 1.00 34.94 ? 379 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 30.427 4.587   5.858  1.00 21.20 ? 380 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? 3.946  0.095   23.974 1.00 18.27 ? 381 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 26.965 -1.228  8.943  1.00 25.71 ? 382 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 16.428 21.395  19.032 1.00 23.51 ? 383 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 1.921  11.281  27.268 1.00 29.52 ? 384 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 17.509 19.990  16.985 1.00 13.52 ? 385 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 34.009 -2.346  13.691 1.00 33.94 ? 386 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 6.529  -6.944  23.752 1.00 24.05 ? 387 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 3.956  -4.047  6.052  1.00 27.57 ? 388 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? 16.362 9.420   -1.676 1.00 19.38 ? 389 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 36.425 18.281  14.741 1.00 30.93 ? 390 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 17.461 10.802  26.036 1.00 18.00 ? 391 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 28.938 15.798  4.344  1.00 30.84 ? 392 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 8.078  6.630   33.779 1.00 15.04 ? 393 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 8.528  -6.450  9.685  1.00 28.11 ? 394 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 16.849 6.334   26.983 1.00 22.71 ? 395 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? 32.244 2.025   6.080  1.00 33.17 ? 396 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 0.606  -1.219  9.081  1.00 40.52 ? 397 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? 25.161 17.651  4.448  1.00 35.90 ? 398 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 14.401 -2.424  17.932 1.00 16.80 ? 399 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 0.134  5.651   5.917  1.00 28.35 ? 400 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 19.372 2.985   19.404 1.00 19.24 ? 401 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? 2.112  14.453  16.747 1.00 33.93 ? 402 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 32.815 16.642  9.356  1.00 31.91 ? 403 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 36.748 2.357   10.070 1.00 35.13 ? 404 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? 22.929 -0.699  5.431  1.00 20.92 ? 405 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 17.357 0.813   20.252 1.00 17.24 ? 406 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 3.026  7.810   24.414 1.00 17.45 ? 407 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 36.254 -0.277  12.645 1.00 31.45 ? 408 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 2.838  16.015  19.125 1.00 23.28 ? 409 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 32.019 8.819   7.713  1.00 23.84 ? 410 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 27.105 -1.331  15.975 1.00 23.91 ? 411 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 14.940 15.006  3.087  1.00 26.98 ? 412 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 30.577 15.788  22.981 1.00 25.70 ? 413 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 15.058 21.802  8.209  1.00 27.11 ? 414 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 3.803  13.252  17.117 1.00 36.44 ? 415 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 27.773 17.585  24.250 1.00 21.02 ? 416 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 33.857 18.718  10.868 1.00 26.34 ? 417 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 6.113  23.825  10.239 1.00 28.97 ? 418 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 7.315  13.718  4.572  1.00 21.21 ? 419 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 20.714 -4.712  11.483 1.00 27.61 ? 420 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 5.168  26.711  19.752 1.00 23.02 ? 421 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 35.754 15.395  11.134 1.00 38.65 ? 422 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 25.236 19.762  21.667 1.00 28.91 ? 423 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 14.274 24.557  17.753 1.00 31.93 ? 424 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 23.266 19.141  6.364  1.00 18.80 ? 425 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 33.870 5.172   16.713 1.00 28.78 ? 426 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 16.781 -4.056  2.836  1.00 22.69 ? 427 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 35.301 10.744  12.560 1.00 45.78 ? 428 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 3.271  -0.379  21.221 1.00 26.54 ? 429 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 10.154 17.846  25.542 1.00 37.71 ? 430 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 19.710 13.238  2.107  1.00 32.65 ? 431 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 0.478  -1.225  16.671 1.00 19.82 ? 432 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 17.760 24.415  10.360 1.00 33.52 ? 433 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? -0.659 15.798  11.474 1.00 26.43 ? 434 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 20.868 10.011  21.884 1.00 14.02 ? 435 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 22.635 3.492   20.868 1.00 18.39 ? 436 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 10.539 4.989   3.254  1.00 24.92 ? 437 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 17.536 23.829  17.078 1.00 38.65 ? 438 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 5.890  2.997   6.733  1.00 33.88 ? 439 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 17.130 -2.381  19.655 1.00 18.33 ? 440 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 1.088  -5.010  17.504 1.00 36.45 ? 441 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 19.364 -0.462  33.204 1.00 34.47 ? 442 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 34.110 7.871   16.740 1.00 32.91 ? 443 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 17.031 -5.643  12.209 1.00 34.34 ? 444 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? -1.010 15.852  15.277 1.00 48.13 ? 445 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 5.909  -3.627  31.387 1.00 27.28 ? 446 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 19.765 9.264   -0.905 1.00 25.22 ? 447 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 23.238 8.262   21.722 1.00 24.45 ? 448 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 8.551  21.033  7.484  1.00 49.65 ? 449 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 20.507 20.589  18.631 1.00 41.31 ? 450 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 18.586 2.113   22.655 1.00 32.54 ? 451 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 18.928 -3.414  33.750 1.00 38.46 ? 452 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? 31.630 9.216   17.458 1.00 41.43 ? 453 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 2.728  11.812  17.741 1.00 23.71 ? 454 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 15.689 13.054  25.899 1.00 22.58 ? 455 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 2.038  -5.590  14.626 1.00 45.44 ? 456 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 18.423 3.270   25.864 1.00 34.85 ? 457 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 29.667 0.689   16.579 1.00 32.63 ? 458 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 2.504  -0.330  26.413 1.00 35.18 ? 459 HOH   A O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? 11.707 24.440  14.380 1.00 34.45 ? 460 HOH   A O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? 23.730 1.133   19.879 1.00 29.59 ? 461 HOH   A O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? 0.058  0.126   23.057 1.00 26.48 ? 462 HOH   A O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? 30.212 7.070   17.955 1.00 32.76 ? 463 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 20.743 -0.443  35.514 1.00 37.10 ? 464 HOH   A O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? 12.152 -5.005  33.072 1.00 28.44 ? 465 HOH   A O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? 21.178 -0.927  18.926 1.00 27.60 ? 466 HOH   A O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? 5.057  28.656  17.842 1.00 32.01 ? 467 HOH   A O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? 37.670 -4.595  6.736  1.00 29.39 ? 468 HOH   A O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? 31.240 4.643   17.111 1.00 23.37 ? 469 HOH   A O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? 2.332  -5.190  22.389 1.00 40.51 ? 470 HOH   A O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? 2.464  -1.706  22.735 1.00 31.80 ? 471 HOH   A O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 7.515  17.342  25.592 1.00 37.68 ? 472 HOH   A O   1 
HETATM 2375 O  O   . HOH   I 5 .   ? 30.993 -32.790 0.858  1.00 36.30 ? 301 HOH   C O   1 
HETATM 2376 O  O   . HOH   I 5 .   ? 31.252 -17.803 -0.003 1.00 36.53 ? 302 HOH   C O   1 
HETATM 2377 O  O   . HOH   I 5 .   ? 17.431 -33.417 24.169 1.00 36.96 ? 303 HOH   C O   1 
HETATM 2378 O  O   . HOH   I 5 .   ? 14.765 -18.742 31.832 1.00 34.64 ? 304 HOH   C O   1 
HETATM 2379 O  O   . HOH   I 5 .   ? 38.980 -18.727 21.588 1.00 24.26 ? 305 HOH   C O   1 
HETATM 2380 O  O   . HOH   I 5 .   ? 18.844 -32.325 19.859 1.00 34.33 ? 306 HOH   C O   1 
HETATM 2381 O  O   . HOH   I 5 .   ? 30.761 -18.192 26.844 1.00 15.73 ? 307 HOH   C O   1 
HETATM 2382 O  O   . HOH   I 5 .   ? 38.269 -7.402  7.003  1.00 19.27 ? 308 HOH   C O   1 
HETATM 2383 O  O   . HOH   I 5 .   ? 10.163 -17.505 18.373 1.00 25.44 ? 309 HOH   C O   1 
HETATM 2384 O  O   . HOH   I 5 .   ? 21.680 -26.069 34.343 1.00 22.90 ? 310 HOH   C O   1 
HETATM 2385 O  O   . HOH   I 5 .   ? 17.838 -6.068  24.110 1.00 24.85 ? 311 HOH   C O   1 
HETATM 2386 O  O   . HOH   I 5 .   ? 14.757 -23.830 12.363 1.00 28.79 ? 312 HOH   C O   1 
HETATM 2387 O  O   . HOH   I 5 .   ? 20.705 -18.751 12.825 1.00 12.18 ? 313 HOH   C O   1 
HETATM 2388 O  O   . HOH   I 5 .   ? 44.571 -23.305 27.056 1.00 24.97 ? 314 HOH   C O   1 
HETATM 2389 O  O   . HOH   I 5 .   ? 22.915 -5.957  21.099 1.00 16.64 ? 315 HOH   C O   1 
HETATM 2390 O  O   . HOH   I 5 .   ? 19.708 -4.096  20.177 1.00 20.18 ? 316 HOH   C O   1 
HETATM 2391 O  O   . HOH   I 5 .   ? 17.838 -27.575 16.514 1.00 14.96 ? 317 HOH   C O   1 
HETATM 2392 O  O   . HOH   I 5 .   ? 24.788 -15.730 7.372  1.00 16.47 ? 318 HOH   C O   1 
HETATM 2393 O  O   . HOH   I 5 .   ? 24.477 -9.774  26.957 1.00 34.20 ? 319 HOH   C O   1 
HETATM 2394 O  O   . HOH   I 5 .   ? 23.918 -8.173  9.517  1.00 21.51 ? 320 HOH   C O   1 
HETATM 2395 O  O   . HOH   I 5 .   ? 21.253 -24.977 4.201  1.00 39.72 ? 321 HOH   C O   1 
HETATM 2396 O  O   . HOH   I 5 .   ? 35.999 -17.720 11.510 1.00 26.49 ? 322 HOH   C O   1 
HETATM 2397 O  O   . HOH   I 5 .   ? 37.315 -18.763 28.138 1.00 22.03 ? 323 HOH   C O   1 
HETATM 2398 O  O   . HOH   I 5 .   ? 37.157 -10.457 4.899  1.00 32.94 ? 324 HOH   C O   1 
HETATM 2399 O  O   . HOH   I 5 .   ? 18.593 -8.833  13.822 1.00 23.56 ? 325 HOH   C O   1 
HETATM 2400 O  O   . HOH   I 5 .   ? 17.507 -24.095 8.572  1.00 35.33 ? 326 HOH   C O   1 
HETATM 2401 O  O   . HOH   I 5 .   ? 16.345 -17.222 10.968 1.00 34.74 ? 327 HOH   C O   1 
HETATM 2402 O  O   . HOH   I 5 .   ? 35.312 -32.621 3.330  1.00 34.23 ? 328 HOH   C O   1 
HETATM 2403 O  O   . HOH   I 5 .   ? 37.339 -31.916 10.868 1.00 23.11 ? 329 HOH   C O   1 
HETATM 2404 O  O   . HOH   I 5 .   ? 21.881 -28.697 4.791  1.00 25.22 ? 330 HOH   C O   1 
HETATM 2405 O  O   . HOH   I 5 .   ? 26.550 -5.469  10.020 1.00 20.85 ? 331 HOH   C O   1 
HETATM 2406 O  O   . HOH   I 5 .   ? 31.006 -21.527 28.367 1.00 13.51 ? 332 HOH   C O   1 
HETATM 2407 O  O   . HOH   I 5 .   ? 6.789  -9.339  22.714 1.00 37.13 ? 333 HOH   C O   1 
HETATM 2408 O  O   . HOH   I 5 .   ? 13.912 -24.254 29.297 1.00 28.76 ? 334 HOH   C O   1 
HETATM 2409 O  O   . HOH   I 5 .   ? 40.442 -27.298 15.110 1.00 11.30 ? 335 HOH   C O   1 
HETATM 2410 O  O   . HOH   I 5 .   ? 13.242 -11.246 28.455 1.00 33.18 ? 336 HOH   C O   1 
HETATM 2411 O  O   . HOH   I 5 .   ? 40.108 -29.607 11.845 1.00 21.89 ? 337 HOH   C O   1 
HETATM 2412 O  O   . HOH   I 5 .   ? 36.109 -26.305 34.240 1.00 28.91 ? 338 HOH   C O   1 
HETATM 2413 O  O   . HOH   I 5 .   ? 28.264 -5.222  18.547 1.00 39.64 ? 339 HOH   C O   1 
HETATM 2414 O  O   . HOH   I 5 .   ? 7.146  -30.278 21.795 1.00 24.57 ? 340 HOH   C O   1 
HETATM 2415 O  O   . HOH   I 5 .   ? 25.967 -25.291 8.781  1.00 11.50 ? 341 HOH   C O   1 
HETATM 2416 O  O   . HOH   I 5 .   ? 26.488 -15.289 30.834 1.00 29.69 ? 342 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 5 .   ? 9.880  -8.894  23.986 1.00 26.32 ? 343 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 5 .   ? 31.050 -23.873 -1.259 1.00 23.85 ? 344 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 5 .   ? 32.511 -23.708 29.095 1.00 14.11 ? 345 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 5 .   ? 10.504 -16.821 12.527 1.00 31.93 ? 346 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 5 .   ? 29.614 -31.397 32.729 1.00 22.32 ? 347 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 5 .   ? 29.873 -15.291 19.567 1.00 13.10 ? 348 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 5 .   ? 35.095 -13.164 8.690  1.00 18.29 ? 349 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 5 .   ? 35.948 -28.431 2.857  1.00 43.27 ? 350 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 5 .   ? 30.130 -10.632 27.742 1.00 37.73 ? 351 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 5 .   ? 19.176 -27.751 28.177 1.00 17.60 ? 352 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 5 .   ? 31.613 -35.026 31.808 1.00 35.22 ? 353 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 5 .   ? 29.692 -13.117 12.971 1.00 14.28 ? 354 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 5 .   ? 10.396 -16.904 15.213 1.00 27.91 ? 355 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 5 .   ? 31.207 -6.121  5.659  1.00 33.76 ? 356 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 5 .   ? 11.880 -24.282 21.697 1.00 14.77 ? 357 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 5 .   ? 20.729 -25.729 13.855 1.00 20.39 ? 358 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 5 .   ? 36.191 -21.277 6.758  1.00 21.76 ? 359 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 5 .   ? 9.269  -8.082  21.468 1.00 24.67 ? 360 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 5 .   ? 25.647 -37.846 24.300 1.00 29.43 ? 361 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 5 .   ? 26.973 -35.637 20.788 1.00 24.39 ? 362 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 5 .   ? 14.575 -28.843 25.598 1.00 34.78 ? 363 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 5 .   ? 31.932 -10.481 13.712 1.00 17.05 ? 364 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 5 .   ? 23.140 -25.384 8.968  1.00 17.54 ? 365 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 5 .   ? 22.872 -8.547  14.036 1.00 13.27 ? 366 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 5 .   ? 3.807  -8.344  14.632 1.00 26.62 ? 367 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 5 .   ? 5.883  -16.884 22.538 1.00 52.75 ? 368 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 5 .   ? 13.048 -29.423 19.072 1.00 26.09 ? 369 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 5 .   ? 4.698  -25.096 25.477 1.00 41.90 ? 370 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 5 .   ? 32.939 -9.843  11.121 1.00 12.67 ? 371 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 5 .   ? 23.572 -33.670 29.060 1.00 25.87 ? 372 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 5 .   ? 41.442 -25.057 7.149  1.00 33.04 ? 373 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 5 .   ? 10.927 -6.452  13.226 1.00 21.36 ? 374 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 5 .   ? 37.785 -31.385 25.765 1.00 25.54 ? 375 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 23.797 -3.392  19.094 1.00 36.69 ? 376 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 22.211 -23.694 6.036  1.00 28.82 ? 377 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 37.760 -23.574 4.284  1.00 39.78 ? 378 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 43.227 -25.673 23.554 1.00 19.05 ? 379 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 35.545 -24.683 24.601 1.00 15.72 ? 380 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 31.458 -13.415 4.303  1.00 29.32 ? 381 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 11.533 -22.661 28.701 1.00 23.75 ? 382 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 28.110 -16.397 22.043 1.00 11.47 ? 383 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 14.609 -18.376 10.484 1.00 33.60 ? 384 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 22.813 -28.129 12.636 1.00 19.30 ? 385 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 30.012 -15.903 30.424 1.00 29.14 ? 386 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 37.803 -20.286 4.832  1.00 34.97 ? 387 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 26.761 -12.089 27.516 1.00 23.37 ? 388 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 6.325  -18.632 25.189 1.00 47.12 ? 389 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 4.235  -10.408 19.713 1.00 30.69 ? 390 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? 28.794 -36.320 7.836  1.00 18.91 ? 391 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 37.942 -13.751 10.627 1.00 35.00 ? 392 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 21.631 -18.971 5.907  1.00 24.29 ? 393 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 31.187 -12.205 10.689 1.00 13.57 ? 394 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 38.794 -12.971 25.776 1.00 24.69 ? 395 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 36.913 -29.259 10.085 1.00 19.33 ? 396 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 9.973  -24.830 19.798 1.00 18.84 ? 397 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 10.607 -11.920 9.121  1.00 26.80 ? 398 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 26.259 -31.257 14.786 1.00 18.10 ? 399 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 34.300 -13.513 25.532 1.00 17.82 ? 400 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 34.820 -35.077 18.093 1.00 30.19 ? 401 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 22.570 -13.849 29.967 1.00 31.05 ? 402 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 26.029 -31.053 30.804 1.00 15.55 ? 403 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 10.243 -30.925 25.037 1.00 28.35 ? 404 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 8.728  -13.289 10.835 1.00 21.29 ? 405 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 36.379 -32.460 25.076 1.00 37.92 ? 406 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 10.900 -21.810 13.602 1.00 44.33 ? 407 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 20.394 -23.668 34.855 1.00 25.22 ? 408 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 35.674 -28.601 7.688  1.00 16.53 ? 409 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 30.157 -18.126 8.386  1.00 22.75 ? 410 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 39.550 -28.377 28.095 1.00 48.22 ? 411 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 38.292 -25.991 28.265 1.00 33.17 ? 412 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 9.745  -18.444 26.669 1.00 27.74 ? 413 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 36.653 -16.115 12.463 1.00 33.13 ? 414 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 6.814  -17.014 18.681 1.00 40.19 ? 415 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 4.703  -28.148 23.128 1.00 34.09 ? 416 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 41.730 -12.298 18.032 1.00 23.11 ? 417 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 32.311 -34.431 24.737 1.00 26.04 ? 418 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 26.605 -6.099  22.169 1.00 27.19 ? 419 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 23.277 -30.940 13.444 1.00 31.57 ? 420 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 6.420  -22.944 18.439 1.00 33.35 ? 421 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 5 .   ? 35.083 -4.141  17.610 1.00 25.51 ? 422 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 5 .   ? 35.074 -13.758 6.005  1.00 33.26 ? 423 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 5 .   ? 32.984 -30.370 31.653 1.00 18.64 ? 424 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 5 .   ? 20.157 -32.338 22.252 1.00 25.30 ? 425 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 5 .   ? 39.389 -33.681 13.925 1.00 47.85 ? 426 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 5 .   ? 4.044  -12.739 17.197 1.00 39.15 ? 427 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 5 .   ? 22.958 -33.513 5.355  1.00 33.82 ? 428 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 5 .   ? 38.877 -14.712 13.442 1.00 34.65 ? 429 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 5 .   ? 32.718 -14.397 9.373  1.00 13.59 ? 430 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 5 .   ? 17.162 -25.337 12.713 1.00 21.55 ? 431 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 5 .   ? 18.580 -8.333  25.546 1.00 18.65 ? 432 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 5 .   ? 18.766 -19.127 10.813 1.00 17.20 ? 433 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 5 .   ? 34.620 -23.211 -0.893 1.00 39.77 ? 434 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 5 .   ? 6.426  -20.070 18.289 1.00 33.13 ? 435 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 5 .   ? 38.757 -16.642 3.562  1.00 43.66 ? 436 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 5 .   ? 15.037 -30.136 18.195 1.00 34.83 ? 437 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 5 .   ? 16.377 -20.564 11.597 1.00 25.85 ? 438 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 5 .   ? 39.959 -29.950 14.517 1.00 16.01 ? 439 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 5 .   ? 33.545 -20.570 -1.836 1.00 33.24 ? 440 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 5 .   ? 34.094 -15.696 27.319 1.00 31.24 ? 441 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 5 .   ? 30.878 -37.574 8.872  1.00 40.25 ? 442 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 5 .   ? 23.450 -17.592 33.254 1.00 18.97 ? 443 HOH   C O   1 
HETATM 2518 O  O   . HOH   I 5 .   ? 9.766  -24.713 29.444 1.00 38.49 ? 444 HOH   C O   1 
HETATM 2519 O  O   . HOH   I 5 .   ? 44.204 -20.681 27.458 1.00 29.50 ? 445 HOH   C O   1 
HETATM 2520 O  O   . HOH   I 5 .   ? 24.272 -16.532 3.262  1.00 38.98 ? 446 HOH   C O   1 
HETATM 2521 O  O   . HOH   I 5 .   ? 37.051 -31.240 29.124 1.00 48.61 ? 447 HOH   C O   1 
HETATM 2522 O  O   . HOH   I 5 .   ? 33.500 -32.893 0.839  1.00 47.37 ? 448 HOH   C O   1 
HETATM 2523 O  O   . HOH   I 5 .   ? 41.882 -31.470 15.635 1.00 30.05 ? 449 HOH   C O   1 
HETATM 2524 O  O   . HOH   I 5 .   ? 31.494 -15.761 7.124  1.00 25.64 ? 450 HOH   C O   1 
HETATM 2525 O  O   . HOH   I 5 .   ? 41.041 -15.418 10.450 1.00 59.91 ? 451 HOH   C O   1 
HETATM 2526 O  O   . HOH   I 5 .   ? 36.525 -24.600 27.216 1.00 29.29 ? 452 HOH   C O   1 
HETATM 2527 O  O   . HOH   I 5 .   ? 34.300 -31.886 29.530 1.00 22.84 ? 453 HOH   C O   1 
HETATM 2528 O  O   . HOH   I 5 .   ? 20.399 -19.712 36.104 1.00 30.74 ? 454 HOH   C O   1 
HETATM 2529 O  O   . HOH   I 5 .   ? 21.185 -17.534 34.587 1.00 21.77 ? 455 HOH   C O   1 
HETATM 2530 O  O   . HOH   I 5 .   ? 23.868 -15.665 31.522 1.00 29.14 ? 456 HOH   C O   1 
HETATM 2531 O  O   . HOH   I 5 .   ? 26.143 -35.536 7.492  1.00 25.59 ? 457 HOH   C O   1 
HETATM 2532 O  O   . HOH   I 5 .   ? 22.766 -16.646 5.460  1.00 34.55 ? 458 HOH   C O   1 
HETATM 2533 O  O   . HOH   I 5 .   ? 16.382 -27.538 14.218 1.00 32.80 ? 459 HOH   C O   1 
HETATM 2534 O  O   . HOH   I 5 .   ? 28.030 -12.668 30.269 1.00 43.74 ? 460 HOH   C O   1 
HETATM 2535 O  O   . HOH   I 5 .   ? 32.542 -19.343 28.995 1.00 25.03 ? 461 HOH   C O   1 
HETATM 2536 O  O   . HOH   I 5 .   ? 41.852 -15.141 13.967 1.00 38.59 ? 462 HOH   C O   1 
HETATM 2537 O  O   . HOH   I 5 .   ? 5.422  -10.093 9.537  1.00 46.97 ? 463 HOH   C O   1 
HETATM 2538 O  O   . HOH   I 5 .   ? 22.245 -7.922  11.471 1.00 30.36 ? 464 HOH   C O   1 
HETATM 2539 O  O   . HOH   I 5 .   ? 9.976  -21.309 16.381 1.00 32.04 ? 465 HOH   C O   1 
HETATM 2540 O  O   . HOH   I 5 .   ? 18.042 -17.935 8.349  1.00 36.17 ? 466 HOH   C O   1 
HETATM 2541 O  O   . HOH   I 5 .   ? 35.393 -20.280 29.424 1.00 30.78 ? 467 HOH   C O   1 
HETATM 2542 O  O   . HOH   I 5 .   ? 8.991  -23.402 17.660 1.00 29.54 ? 468 HOH   C O   1 
HETATM 2543 O  O   . HOH   I 5 .   ? 35.182 -23.054 29.006 1.00 23.17 ? 469 HOH   C O   1 
HETATM 2544 O  O   . HOH   I 5 .   ? 39.204 -2.623  10.801 1.00 35.39 ? 470 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   ? 0.1701 0.1640 0.1568 0.0011  -0.0064 -0.0094 7   SER   A N   
2    C CA  . SER   A 1   ? 0.1747 0.1695 0.1660 0.0018  -0.0085 -0.0083 7   SER   A CA  
3    C C   . SER   A 1   ? 0.1636 0.1584 0.1583 0.0046  -0.0099 -0.0044 7   SER   A C   
4    O O   . SER   A 1   ? 0.1793 0.1738 0.1721 0.0054  -0.0098 -0.0022 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2088 0.2080 0.1977 -0.0013 -0.0117 -0.0086 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2379 0.2407 0.2240 -0.0017 -0.0146 -0.0048 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1509 0.1459 0.1506 0.0057  -0.0105 -0.0037 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1365 0.1311 0.1398 0.0078  -0.0108 -0.0009 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1355 0.1289 0.1435 0.0086  -0.0095 -0.0017 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1537 0.1460 0.1621 0.0082  -0.0080 -0.0036 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1220 0.1157 0.1338 0.0097  -0.0095 -0.0002 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1248 0.1180 0.1405 0.0099  -0.0079 -0.0010 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1215 0.1132 0.1391 0.0106  -0.0061 -0.0002 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1373 0.1283 0.1551 0.0113  -0.0062 0.0014  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1348 0.1305 0.1546 0.0095  -0.0094 -0.0014 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1186 0.1098 0.1376 0.0098  -0.0040 -0.0013 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1123 0.1022 0.1333 0.0095  -0.0014 -0.0018 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1216 0.1128 0.1487 0.0100  -0.0008 -0.0022 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1211 0.1141 0.1491 0.0094  -0.0015 -0.0029 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1217 0.1116 0.1395 0.0072  0.0007  -0.0029 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1411 0.1314 0.1542 0.0066  -0.0001 -0.0020 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1414 0.1297 0.1602 0.0057  0.0042  -0.0045 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1396 0.1324 0.1506 0.0043  0.0009  -0.0018 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1190 0.1093 0.1511 0.0112  0.0008  -0.0017 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1317 0.1237 0.1710 0.0120  0.0019  -0.0018 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1282 0.1174 0.1694 0.0109  0.0071  -0.0043 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1348 0.1210 0.1791 0.0118  0.0097  -0.0041 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1412 0.1354 0.1869 0.0147  -0.0003 0.0015  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1255 0.1235 0.1684 0.0144  -0.0052 0.0032  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1350 0.1369 0.1799 0.0134  -0.0070 0.0025  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1458 0.1435 0.1836 0.0145  -0.0075 0.0049  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1438 0.1487 0.1853 0.0122  -0.0108 0.0029  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1568 0.1580 0.1912 0.0133  -0.0113 0.0054  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1563 0.1608 0.1923 0.0119  -0.0128 0.0041  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.1831 0.1908 0.2151 0.0098  -0.0158 0.0036  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1363 0.1264 0.1756 0.0084  0.0089  -0.0067 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1364 0.1247 0.1758 0.0059  0.0142  -0.0099 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1504 0.1410 0.1949 0.0054  0.0161  -0.0111 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1325 0.1261 0.1758 0.0049  0.0135  -0.0103 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1590 0.1474 0.1893 0.0019  0.0148  -0.0113 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1769 0.1688 0.2035 0.0012  0.0113  -0.0095 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.1849 0.1725 0.2141 -0.0021 0.0204  -0.0152 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1651 0.1542 0.2165 0.0059  0.0209  -0.0130 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1537 0.1454 0.2109 0.0055  0.0232  -0.0142 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1458 0.1418 0.2080 0.0081  0.0183  -0.0110 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1470 0.1438 0.2127 0.0112  0.0149  -0.0078 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1354 0.1346 0.1966 0.0062  0.0175  -0.0115 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1352 0.1384 0.1998 0.0075  0.0129  -0.0091 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1329 0.1357 0.1892 0.0060  0.0090  -0.0083 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1367 0.1419 0.1939 0.0051  0.0071  -0.0079 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1465 0.1533 0.2182 0.0068  0.0151  -0.0100 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.1934 0.2019 0.2767 0.0095  0.0179  -0.0095 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2193 0.2321 0.3103 0.0122  0.0148  -0.0063 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.1803 0.1857 0.2653 0.0088  0.0242  -0.0124 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1217 0.1217 0.1713 0.0060  0.0081  -0.0080 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1190 0.1184 0.1622 0.0052  0.0051  -0.0070 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1147 0.1130 0.1558 0.0072  0.0020  -0.0056 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1221 0.1190 0.1637 0.0085  0.0027  -0.0051 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1400 0.1380 0.1767 0.0027  0.0071  -0.0074 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1483 0.1480 0.1852 -0.0002 0.0100  -0.0084 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1558 0.1572 0.1949 -0.0009 0.0093  -0.0077 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1785 0.1782 0.2129 -0.0028 0.0139  -0.0104 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1691 0.1723 0.2078 -0.0040 0.0120  -0.0081 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.1905 0.1923 0.2238 -0.0064 0.0167  -0.0113 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.1979 0.2017 0.2335 -0.0067 0.0156  -0.0099 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2439 0.2501 0.2781 -0.0104 0.0184  -0.0103 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1133 0.1119 0.1519 0.0070  -0.0008 -0.0050 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1141 0.1119 0.1491 0.0079  -0.0033 -0.0042 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1115 0.1071 0.1414 0.0070  -0.0029 -0.0043 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1169 0.1124 0.1475 0.0060  -0.0026 -0.0045 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1134 0.1140 0.1505 0.0078  -0.0063 -0.0040 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1178 0.1177 0.1499 0.0075  -0.0084 -0.0041 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1328 0.1369 0.1664 0.0061  -0.0115 -0.0041 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1521 0.1549 0.1808 0.0040  -0.0120 -0.0063 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.1778 0.1808 0.2015 0.0034  -0.0133 -0.0064 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.1864 0.1908 0.2093 0.0050  -0.0147 -0.0037 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.1669 0.1682 0.1865 0.0010  -0.0126 -0.0093 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1076 0.1019 0.1336 0.0074  -0.0026 -0.0036 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1062 0.0996 0.1289 0.0069  -0.0022 -0.0028 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1102 0.1026 0.1306 0.0078  -0.0035 -0.0029 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1197 0.1119 0.1381 0.0085  -0.0043 -0.0027 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1156 0.1095 0.1354 0.0059  -0.0007 -0.0020 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1293 0.1242 0.1475 0.0055  -0.0006 0.0001  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1327 0.1277 0.1536 0.0041  0.0014  -0.0028 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1015 0.0927 0.1222 0.0077  -0.0033 -0.0033 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1190 0.1090 0.1374 0.0079  -0.0036 -0.0044 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1140 0.1024 0.1332 0.0084  -0.0016 -0.0036 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1310 0.1195 0.1531 0.0085  -0.0004 -0.0016 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1457 0.1358 0.1646 0.0066  -0.0047 -0.0068 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.1858 0.1790 0.2050 0.0065  -0.0072 -0.0064 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1413 0.1303 0.1640 0.0055  -0.0034 -0.0078 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1196 0.1066 0.1368 0.0088  -0.0009 -0.0047 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1168 0.1020 0.1368 0.0096  0.0019  -0.0041 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1304 0.1127 0.1540 0.0088  0.0036  -0.0059 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1302 0.1117 0.1520 0.0069  0.0029  -0.0093 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1158 0.0997 0.1332 0.0097  0.0033  -0.0061 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1208 0.1071 0.1349 0.0103  0.0021  -0.0044 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1433 0.1306 0.1531 0.0094  0.0000  -0.0053 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1382 0.1262 0.1549 0.0116  0.0032  -0.0015 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1186 0.0997 0.1475 0.0098  0.0057  -0.0032 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1248 0.1022 0.1576 0.0088  0.0078  -0.0048 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1470 0.1202 0.1789 0.0075  0.0104  -0.0098 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1541 0.1255 0.1855 0.0049  0.0108  -0.0135 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1303 0.1068 0.1698 0.0105  0.0101  0.0001  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1340 0.1064 0.1785 0.0095  0.0126  -0.0005 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1387 0.1105 0.1905 0.0116  0.0149  0.0057  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1610 0.1288 0.2182 0.0107  0.0173  0.0064  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1914 0.1522 0.2536 0.0106  0.0219  0.0037  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1890 0.1463 0.2505 0.0108  0.0246  -0.0009 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2011 0.1580 0.2690 0.0098  0.0244  0.0052  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1337 0.1062 0.1649 0.0086  0.0123  -0.0104 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1487 0.1170 0.1786 0.0067  0.0159  -0.0159 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1642 0.1346 0.1862 0.0031  0.0131  -0.0204 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.1797 0.1474 0.1994 -0.0001 0.0158  -0.0258 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1658 0.1327 0.1982 0.0089  0.0196  -0.0153 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1459 0.1169 0.1724 0.0093  0.0171  -0.0147 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.1550 0.1304 0.1823 0.0117  0.0145  -0.0094 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.1613 0.1326 0.1814 0.0071  0.0175  -0.0188 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.1548 0.1325 0.1765 0.0111  0.0133  -0.0104 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.1681 0.1435 0.1855 0.0086  0.0150  -0.0156 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1550 0.1304 0.1732 0.0032  0.0082  -0.0182 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1506 0.1296 0.1628 0.0001  0.0048  -0.0205 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1700 0.1517 0.1837 -0.0013 0.0017  -0.0201 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.1838 0.1700 0.1942 -0.0034 -0.0017 -0.0206 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1560 0.1386 0.1638 0.0014  0.0020  -0.0180 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.1695 0.1504 0.1755 0.0022  0.0049  -0.0187 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.1688 0.1530 0.1707 0.0031  0.0022  -0.0160 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2015 0.1804 0.2037 -0.0015 0.0079  -0.0243 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1578 0.1376 0.1770 -0.0001 0.0030  -0.0185 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1577 0.1403 0.1790 -0.0014 0.0006  -0.0182 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1752 0.1589 0.1948 -0.0060 0.0002  -0.0227 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.1877 0.1673 0.2067 -0.0084 0.0037  -0.0267 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1524 0.1326 0.1794 -0.0001 0.0026  -0.0160 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1689 0.1586 0.1886 -0.0075 -0.0037 -0.0219 24  THR   A N   
135  C CA  . THR   A 18  ? 0.1730 0.1660 0.1911 -0.0126 -0.0051 -0.0255 24  THR   A CA  
136  C C   . THR   A 18  ? 0.1723 0.1639 0.1957 -0.0143 -0.0035 -0.0269 24  THR   A C   
137  O O   . THR   A 18  ? 0.1642 0.1530 0.1924 -0.0113 -0.0020 -0.0242 24  THR   A O   
138  C CB  . THR   A 18  ? 0.1956 0.1975 0.2129 -0.0131 -0.0105 -0.0227 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.1911 0.1953 0.2147 -0.0103 -0.0118 -0.0191 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2051 0.2086 0.2177 -0.0113 -0.0122 -0.0203 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.1806 0.1748 0.2031 -0.0198 -0.0040 -0.0308 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.1787 0.1724 0.2064 -0.0220 -0.0029 -0.0320 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.1650 0.1642 0.1979 -0.0192 -0.0060 -0.0273 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.1683 0.1646 0.2060 -0.0180 -0.0038 -0.0262 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.1951 0.1927 0.2203 -0.0293 -0.0037 -0.0371 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.3079 0.3075 0.3388 -0.0321 -0.0036 -0.0378 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.3694 0.3608 0.4040 -0.0330 0.0015  -0.0401 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.3528 0.3617 0.3873 -0.0334 -0.0080 -0.0355 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.3778 0.3737 0.4169 -0.0357 0.0002  -0.0400 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.3857 0.3925 0.4253 -0.0359 -0.0055 -0.0373 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.1547 0.1616 0.1871 -0.0180 -0.0105 -0.0242 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.1574 0.1689 0.1959 -0.0151 -0.0123 -0.0201 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1424 0.1483 0.1825 -0.0104 -0.0095 -0.0177 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1438 0.1503 0.1889 -0.0094 -0.0085 -0.0162 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.1868 0.2066 0.2260 -0.0140 -0.0169 -0.0166 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.2906 0.3151 0.3380 -0.0114 -0.0178 -0.0131 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3316 0.3610 0.3842 -0.0139 -0.0184 -0.0136 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3231 0.3459 0.3721 -0.0067 -0.0170 -0.0099 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1336 0.1346 0.1694 -0.0080 -0.0082 -0.0172 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1337 0.1307 0.1705 -0.0045 -0.0058 -0.0148 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1277 0.1204 0.1676 -0.0055 -0.0025 -0.0152 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1314 0.1244 0.1741 -0.0044 -0.0015 -0.0129 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1390 0.1323 0.1711 -0.0026 -0.0049 -0.0143 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.1530 0.1496 0.1824 -0.0010 -0.0075 -0.0127 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.1467 0.1469 0.1790 0.0004  -0.0090 -0.0105 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.1556 0.1509 0.1805 -0.0011 -0.0076 -0.0136 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1263 0.1147 0.1656 -0.0080 -0.0004 -0.0183 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1307 0.1143 0.1739 -0.0089 0.0032  -0.0182 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1381 0.1250 0.1853 -0.0112 0.0027  -0.0184 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1507 0.1353 0.2014 -0.0109 0.0049  -0.0162 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1410 0.1184 0.1835 -0.0112 0.0065  -0.0221 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1446 0.1172 0.1858 -0.0082 0.0089  -0.0209 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.1682 0.1404 0.2049 -0.0081 0.0088  -0.0232 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1498 0.1183 0.1949 -0.0051 0.0118  -0.0166 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.1652 0.1330 0.2035 -0.0049 0.0118  -0.0210 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1558 0.1220 0.1995 -0.0028 0.0132  -0.0164 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1692 0.1371 0.2190 -0.0041 0.0129  -0.0122 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1751 0.1385 0.2232 0.0005  0.0158  -0.0117 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.1741 0.1398 0.2271 -0.0011 0.0149  -0.0071 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1833 0.1467 0.2360 0.0013  0.0164  -0.0068 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1290 0.1220 0.1764 -0.0137 -0.0003 -0.0204 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1409 0.1383 0.1933 -0.0161 -0.0009 -0.0206 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.1495 0.1511 0.2050 -0.0131 -0.0017 -0.0169 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.1650 0.1699 0.2254 -0.0146 -0.0013 -0.0167 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1668 0.1707 0.2189 -0.0200 -0.0041 -0.0234 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1386 0.1401 0.1916 -0.0094 -0.0024 -0.0146 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1351 0.1397 0.1906 -0.0070 -0.0022 -0.0121 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1332 0.1333 0.1850 -0.0048 -0.0001 -0.0100 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1341 0.1354 0.1845 -0.0027 -0.0003 -0.0087 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1450 0.1551 0.2016 -0.0053 -0.0052 -0.0113 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.1750 0.1918 0.2368 -0.0077 -0.0075 -0.0121 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2067 0.2274 0.2747 -0.0082 -0.0066 -0.0116 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.1897 0.2087 0.2488 -0.0100 -0.0103 -0.0135 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1379 0.1333 0.1886 -0.0056 0.0019  -0.0094 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1302 0.1225 0.1778 -0.0038 0.0032  -0.0066 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1409 0.1355 0.1886 -0.0039 0.0045  -0.0041 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.1547 0.1505 0.2052 -0.0058 0.0060  -0.0037 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1291 0.1161 0.1779 -0.0044 0.0054  -0.0059 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1400 0.1248 0.1874 -0.0024 0.0065  -0.0019 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1463 0.1309 0.1900 -0.0002 0.0052  -0.0025 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1702 0.1496 0.2214 -0.0027 0.0094  -0.0003 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1272 0.1225 0.1712 -0.0025 0.0043  -0.0025 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1366 0.1343 0.1789 -0.0037 0.0059  -0.0004 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.1425 0.1391 0.1828 -0.0037 0.0063  0.0039  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.1634 0.1616 0.2038 -0.0057 0.0076  0.0070  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.1312 0.1310 0.1710 -0.0030 0.0058  -0.0018 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.1567 0.1589 0.1930 -0.0053 0.0078  -0.0003 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.1441 0.1456 0.1882 -0.0025 0.0057  -0.0047 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1255 0.1203 0.1642 -0.0017 0.0052  0.0047  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1348 0.1299 0.1731 -0.0012 0.0055  0.0095  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1425 0.1344 0.1815 0.0014  0.0050  0.0092  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1393 0.1305 0.1760 0.0024  0.0039  0.0056  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.1545 0.1546 0.1881 -0.0028 0.0050  0.0115  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.1655 0.1683 0.1982 -0.0025 0.0044  0.0169  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.1944 0.2002 0.2290 -0.0038 0.0047  0.0231  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.1562 0.1601 0.1869 -0.0011 0.0032  0.0174  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2066 0.2160 0.2410 -0.0031 0.0035  0.0277  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.1829 0.1912 0.2147 -0.0015 0.0027  0.0239  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.1663 0.1683 0.1947 0.0005  0.0025  0.0134  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.1892 0.2005 0.2200 -0.0007 0.0015  0.0260  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.1708 0.1750 0.1975 0.0011  0.0015  0.0152  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.1803 0.1892 0.2084 0.0006  0.0011  0.0213  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1540 0.1442 0.1965 0.0026  0.0062  0.0131  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1462 0.1336 0.1899 0.0051  0.0066  0.0127  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1598 0.1488 0.2073 0.0065  0.0075  0.0194  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1663 0.1563 0.2175 0.0058  0.0083  0.0243  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1642 0.1455 0.2105 0.0054  0.0084  0.0083  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1768 0.1544 0.2288 0.0044  0.0110  0.0096  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.1823 0.1565 0.2411 0.0064  0.0140  0.0145  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2112 0.1838 0.2749 0.0057  0.0159  0.0183  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.1697 0.1428 0.2298 0.0087  0.0150  0.0149  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1436 0.1333 0.1912 0.0085  0.0073  0.0202  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1418 0.1344 0.1946 0.0103  0.0080  0.0272  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1443 0.1337 0.2000 0.0132  0.0097  0.0256  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1428 0.1342 0.1938 0.0133  0.0083  0.0231  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1670 0.1683 0.2155 0.0083  0.0051  0.0315  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.1981 0.2052 0.2521 0.0094  0.0048  0.0401  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2416 0.2463 0.3019 0.0128  0.0066  0.0418  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2345 0.2492 0.2861 0.0066  0.0027  0.0452  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1451 0.1290 0.2088 0.0153  0.0135  0.0267  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1447 0.1248 0.2122 0.0178  0.0166  0.0247  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1570 0.1372 0.2240 0.0178  0.0164  0.0244  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1547 0.1414 0.2246 0.0199  0.0155  0.0303  36  SER   A C   
244  O O   . SER   A 30  ? 0.1607 0.1471 0.2288 0.0208  0.0162  0.0271  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1536 0.1262 0.2306 0.0194  0.0218  0.0254  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2028 0.1749 0.2785 0.0192  0.0218  0.0238  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.1698 0.1385 0.2519 0.0219  0.0260  0.0236  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2703 0.2441 0.3546 0.0207  0.0228  0.0325  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1516 0.1453 0.2253 0.0200  0.0137  0.0389  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1544 0.1561 0.2309 0.0213  0.0122  0.0449  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1466 0.1531 0.2132 0.0190  0.0088  0.0412  37  SER   A C   
252  O O   . SER   A 31  ? 0.1567 0.1682 0.2251 0.0200  0.0083  0.0436  37  SER   A O   
253  C CB  . SER   A 31  ? 0.1711 0.1812 0.2528 0.0209  0.0102  0.0555  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2420 0.2582 0.3147 0.0164  0.0061  0.0559  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1290 0.1339 0.1862 0.0160  0.0068  0.0354  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1308 0.1386 0.1793 0.0139  0.0043  0.0315  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1246 0.1256 0.1688 0.0145  0.0054  0.0235  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1219 0.1241 0.1596 0.0132  0.0038  0.0204  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1388 0.1498 0.1805 0.0100  0.0019  0.0308  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1498 0.1696 0.1928 0.0078  0.0001  0.0385  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1466 0.1693 0.1824 0.0032  -0.0013 0.0369  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1293 0.1532 0.1575 0.0008  -0.0022 0.0319  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1487 0.1777 0.1706 -0.0040 -0.0031 0.0314  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.1688 0.2034 0.1899 -0.0073 -0.0037 0.0356  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1478 0.1763 0.1640 -0.0059 -0.0030 0.0265  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1187 0.1125 0.1659 0.0159  0.0082  0.0201  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1131 0.1017 0.1555 0.0153  0.0087  0.0129  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1161 0.1056 0.1515 0.0129  0.0057  0.0097  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1241 0.1126 0.1544 0.0123  0.0047  0.0058  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1306 0.1194 0.1714 0.0163  0.0097  0.0109  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1324 0.1166 0.1680 0.0152  0.0103  0.0042  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1491 0.1287 0.1858 0.0144  0.0120  0.0008  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1486 0.1344 0.1788 0.0146  0.0089  0.0024  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1153 0.1064 0.1510 0.0115  0.0047  0.0116  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1095 0.1012 0.1403 0.0096  0.0027  0.0086  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1087 0.0979 0.1415 0.0086  0.0033  0.0067  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1206 0.1087 0.1580 0.0087  0.0048  0.0093  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1099 0.1070 0.1382 0.0078  0.0014  0.0115  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1306 0.1310 0.1552 0.0074  0.0004  0.0121  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1484 0.1540 0.1700 0.0043  -0.0003 0.0139  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1434 0.1409 0.1643 0.0079  -0.0001 0.0076  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1077 0.0963 0.1376 0.0076  0.0020  0.0029  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1101 0.0979 0.1419 0.0062  0.0021  0.0011  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1149 0.1052 0.1444 0.0054  0.0005  -0.0005 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1228 0.1137 0.1495 0.0061  -0.0008 -0.0018 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1210 0.1051 0.1542 0.0058  0.0029  -0.0024 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1227 0.1064 0.1581 0.0038  0.0029  -0.0045 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1381 0.1171 0.1762 0.0026  0.0053  -0.0070 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1399 0.1267 0.1735 0.0028  0.0003  -0.0071 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1184 0.1102 0.1497 0.0040  0.0009  -0.0003 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1043 0.0983 0.1355 0.0035  0.0005  -0.0018 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1087 0.1032 0.1438 0.0025  0.0004  -0.0036 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1187 0.1126 0.1560 0.0013  0.0016  -0.0028 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1070 0.1034 0.1365 0.0020  0.0019  -0.0004 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1348 0.1325 0.1656 0.0015  0.0028  -0.0026 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1305 0.1276 0.1561 0.0022  0.0016  0.0014  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1062 0.1023 0.1427 0.0030  -0.0010 -0.0053 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1060 0.1043 0.1471 0.0019  -0.0015 -0.0066 43  SER   A CA  
299  C C   . SER   A 37  ? 0.1179 0.1193 0.1624 0.0026  -0.0010 -0.0066 43  SER   A C   
300  O O   . SER   A 37  ? 0.1249 0.1259 0.1680 0.0039  -0.0003 -0.0061 43  SER   A O   
301  C CB  . SER   A 37  ? 0.1277 0.1266 0.1686 0.0014  -0.0039 -0.0082 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1342 0.1344 0.1730 0.0029  -0.0059 -0.0076 43  SER   A OG  
303  N N   . SER   A 38  ? 0.1235 0.1279 0.1734 0.0016  -0.0007 -0.0073 44  SER   A N   
304  C CA  . SER   A 38  ? 0.1374 0.1450 0.1927 0.0024  0.0006  -0.0072 44  SER   A CA  
305  C C   . SER   A 38  ? 0.1561 0.1674 0.2158 0.0041  -0.0023 -0.0062 44  SER   A C   
306  O O   . SER   A 38  ? 0.1773 0.1906 0.2364 0.0032  -0.0055 -0.0062 44  SER   A O   
307  C CB  . SER   A 38  ? 0.1638 0.1736 0.2238 0.0005  0.0027  -0.0080 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.1967 0.2087 0.2592 -0.0009 0.0004  -0.0084 44  SER   A OG  
309  N N   . THR   A 39  ? 0.1535 0.1659 0.2178 0.0063  -0.0009 -0.0053 45  THR   A N   
310  C CA  . THR   A 39  ? 0.1652 0.1818 0.2350 0.0084  -0.0035 -0.0027 45  THR   A CA  
311  C C   . THR   A 39  ? 0.1889 0.2100 0.2697 0.0097  -0.0015 -0.0018 45  THR   A C   
312  O O   . THR   A 39  ? 0.1848 0.2039 0.2678 0.0095  0.0032  -0.0037 45  THR   A O   
313  C CB  . THR   A 39  ? 0.1818 0.1951 0.2489 0.0107  -0.0033 -0.0013 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.1956 0.2054 0.2645 0.0116  0.0016  -0.0025 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.1894 0.1986 0.2463 0.0097  -0.0048 -0.0021 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.1980 0.2256 0.2860 0.0109  -0.0048 0.0015  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2150 0.2478 0.3157 0.0128  -0.0029 0.0033  46  THR   A CA  
318  C C   . THR   A 40  ? 0.2136 0.2431 0.3195 0.0166  0.0007  0.0050  46  THR   A C   
319  O O   . THR   A 40  ? 0.2401 0.2683 0.3530 0.0177  0.0062  0.0036  46  THR   A O   
320  C CB  . THR   A 40  ? 0.2665 0.3092 0.3738 0.0123  -0.0082 0.0070  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3245 0.3687 0.4285 0.0131  -0.0125 0.0105  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.2739 0.3191 0.3766 0.0078  -0.0105 0.0043  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2118 0.2392 0.3137 0.0181  -0.0017 0.0075  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2281 0.2513 0.3347 0.0214  0.0019  0.0092  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.2225 0.2366 0.3197 0.0201  0.0062  0.0047  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.2143 0.2259 0.3002 0.0175  0.0043  0.0024  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2566 0.2827 0.3642 0.0234  -0.0028 0.0149  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.2047 0.2140 0.3069 0.0217  0.0122  0.0036  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.2072 0.2087 0.3009 0.0197  0.0165  -0.0007 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.2060 0.2042 0.2939 0.0206  0.0140  0.0015  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.2254 0.2251 0.3199 0.0238  0.0121  0.0064  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.2356 0.2330 0.3368 0.0202  0.0247  -0.0037 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.3016 0.3011 0.4049 0.0178  0.0285  -0.0076 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.3814 0.3766 0.4917 0.0177  0.0376  -0.0115 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.3747 0.3703 0.4989 0.0216  0.0408  -0.0092 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.4215 0.4126 0.5227 0.0129  0.0422  -0.0173 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.1692 0.1637 0.2453 0.0177  0.0139  -0.0015 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.1578 0.1491 0.2275 0.0179  0.0120  0.0000  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.1525 0.1372 0.2224 0.0175  0.0177  -0.0022 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.1704 0.1524 0.2428 0.0159  0.0236  -0.0061 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.1542 0.1361 0.2203 0.0181  0.0162  -0.0001 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.1646 0.1397 0.2311 0.0174  0.0216  -0.0018 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.1674 0.1397 0.2223 0.0134  0.0220  -0.0052 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.1818 0.1485 0.2361 0.0118  0.0268  -0.0074 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.1739 0.1476 0.2474 0.0213  0.0206  0.0038  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.2200 0.1969 0.3107 0.0262  0.0218  0.0087  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.1416 0.1178 0.1881 0.0117  0.0175  -0.0053 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.1452 0.1203 0.1820 0.0081  0.0176  -0.0076 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.1701 0.1449 0.2037 0.0037  0.0220  -0.0124 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.1887 0.1658 0.2249 0.0033  0.0230  -0.0137 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.1411 0.1205 0.1718 0.0082  0.0119  -0.0056 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.1592 0.1393 0.1905 0.0111  0.0078  -0.0016 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.1658 0.1427 0.1982 0.0119  0.0090  0.0000  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.1629 0.1467 0.1930 0.0119  0.0038  -0.0001 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.1824 0.1552 0.2101 -0.0002 0.0246  -0.0150 52  THR   A N   
356  C CA  . THR   A 46  ? 0.1902 0.1643 0.2126 -0.0059 0.0282  -0.0195 52  THR   A CA  
357  C C   . THR   A 46  ? 0.1805 0.1593 0.1940 -0.0089 0.0242  -0.0182 52  THR   A C   
358  O O   . THR   A 46  ? 0.2015 0.1800 0.2128 -0.0078 0.0216  -0.0160 52  THR   A O   
359  C CB  . THR   A 46  ? 0.2459 0.2143 0.2688 -0.0093 0.0352  -0.0241 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3071 0.2729 0.3275 -0.0094 0.0343  -0.0229 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.2622 0.2254 0.2963 -0.0057 0.0401  -0.0249 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.1758 0.1596 0.1849 -0.0125 0.0238  -0.0190 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.1651 0.1546 0.1678 -0.0149 0.0200  -0.0166 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.1663 0.1572 0.1625 -0.0216 0.0229  -0.0196 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.1749 0.1654 0.1689 -0.0266 0.0277  -0.0241 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.1624 0.1573 0.1643 -0.0155 0.0177  -0.0145 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.1754 0.1688 0.1837 -0.0100 0.0157  -0.0126 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.1676 0.1687 0.1650 -0.0170 0.0137  -0.0105 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.1826 0.1747 0.1928 -0.0053 0.0115  -0.0094 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.1485 0.1420 0.1412 -0.0224 0.0202  -0.0175 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.1558 0.1527 0.1419 -0.0294 0.0219  -0.0196 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.1707 0.1765 0.1518 -0.0347 0.0206  -0.0184 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.1655 0.1762 0.1482 -0.0319 0.0164  -0.0136 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.1542 0.1532 0.1390 -0.0284 0.0185  -0.0164 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.1922 0.2006 0.1673 -0.0427 0.0243  -0.0227 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.1916 0.2098 0.1607 -0.0491 0.0228  -0.0212 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.2239 0.2477 0.1862 -0.0568 0.0232  -0.0226 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.2398 0.2627 0.1967 -0.0643 0.0283  -0.0290 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.1958 0.2125 0.1635 -0.0527 0.0278  -0.0259 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.1932 0.2043 0.1685 -0.0454 0.0280  -0.0251 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.1811 0.1973 0.1592 -0.0407 0.0219  -0.0178 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.1685 0.1796 0.1535 -0.0348 0.0225  -0.0178 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.1839 0.1957 0.1734 -0.0293 0.0182  -0.0128 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.1836 0.2009 0.1720 -0.0287 0.0136  -0.0072 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.2186 0.2263 0.2142 -0.0249 0.0189  -0.0134 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2154 0.2454 0.1782 -0.0553 0.0180  -0.0169 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2293 0.2647 0.1876 -0.0611 0.0175  -0.0173 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.2416 0.2874 0.2017 -0.0593 0.0110  -0.0089 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.2599 0.3074 0.2253 -0.0530 0.0074  -0.0031 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.2244 0.2490 0.1852 -0.0583 0.0208  -0.0214 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2077 0.2274 0.1769 -0.0468 0.0167  -0.0159 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.2726 0.3248 0.2295 -0.0646 0.0100  -0.0086 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.2958 0.3581 0.2562 -0.0626 0.0045  -0.0007 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.2734 0.3311 0.2364 -0.0598 0.0049  -0.0016 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.2811 0.3481 0.2447 -0.0620 0.0020  0.0024  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3851 0.4634 0.3402 -0.0719 0.0017  0.0029  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.5038 0.5846 0.4507 -0.0824 0.0048  -0.0034 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5244 0.5930 0.4698 -0.0826 0.0100  -0.0113 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5689 0.6643 0.5112 -0.0908 0.0020  -0.0004 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.2359 0.2802 0.2009 -0.0549 0.0083  -0.0062 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2097 0.2494 0.1772 -0.0519 0.0086  -0.0064 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2089 0.2542 0.1824 -0.0458 0.0041  0.0007  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2140 0.2600 0.1917 -0.0403 0.0018  0.0047  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2112 0.2364 0.1809 -0.0470 0.0124  -0.0108 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2336 0.2498 0.1989 -0.0535 0.0197  -0.0198 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.1814 0.2302 0.1555 -0.0469 0.0033  0.0021  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.1734 0.2258 0.1538 -0.0410 0.0005  0.0077  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.1548 0.1989 0.1361 -0.0379 0.0025  0.0054  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.1648 0.2123 0.1501 -0.0347 0.0011  0.0089  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2048 0.2723 0.1873 -0.0446 -0.0028 0.0135  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.2484 0.3258 0.2331 -0.0451 -0.0059 0.0191  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3022 0.3953 0.2913 -0.0476 -0.0095 0.0265  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.3265 0.4315 0.3119 -0.0555 -0.0114 0.0284  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.2460 0.3410 0.2437 -0.0411 -0.0105 0.0314  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1416 0.1751 0.1194 -0.0390 0.0061  -0.0002 60  THR   A N   
416  C CA  . THR   A 54  ? 0.1502 0.1748 0.1288 -0.0357 0.0080  -0.0017 60  THR   A CA  
417  C C   . THR   A 54  ? 0.1471 0.1602 0.1264 -0.0315 0.0100  -0.0044 60  THR   A C   
418  O O   . THR   A 54  ? 0.1713 0.1819 0.1491 -0.0337 0.0118  -0.0073 60  THR   A O   
419  C CB  . THR   A 54  ? 0.1948 0.2185 0.1701 -0.0416 0.0106  -0.0046 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2710 0.2901 0.2423 -0.0471 0.0142  -0.0099 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.1913 0.2275 0.1664 -0.0463 0.0084  -0.0018 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1298 0.1372 0.1116 -0.0257 0.0096  -0.0030 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1371 0.1355 0.1205 -0.0216 0.0108  -0.0043 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1311 0.1252 0.1160 -0.0167 0.0100  -0.0021 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1405 0.1366 0.1245 -0.0175 0.0099  -0.0008 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1242 0.1131 0.1114 -0.0122 0.0095  -0.0017 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1154 0.1010 0.1032 -0.0084 0.0086  0.0005  62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1232 0.1099 0.1129 -0.0043 0.0060  0.0017  62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1339 0.1198 0.1256 -0.0035 0.0060  0.0007  62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1382 0.1159 0.1273 -0.0083 0.0112  0.0002  62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.1661 0.1413 0.1559 -0.0045 0.0095  0.0035  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.1458 0.1215 0.1329 -0.0129 0.0144  -0.0015 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1197 0.1082 0.1088 -0.0020 0.0043  0.0034  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1058 0.0947 0.0963 0.0012  0.0023  0.0038  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1194 0.1059 0.1084 0.0029  0.0013  0.0052  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1305 0.1164 0.1171 0.0021  0.0019  0.0063  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1148 0.1086 0.1064 0.0020  0.0016  0.0040  63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1151 0.1107 0.1054 0.0025  0.0020  0.0046  63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1281 0.1263 0.1176 0.0005  0.0032  0.0054  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1183 0.1134 0.1083 0.0044  0.0016  0.0041  63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1450 0.1451 0.1338 0.0009  0.0041  0.0058  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1282 0.1248 0.1169 0.0044  0.0029  0.0040  63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1435 0.1426 0.1319 0.0029  0.0042  0.0050  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.1724 0.1733 0.1600 0.0028  0.0061  0.0047  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1165 0.1026 0.1069 0.0049  -0.0004 0.0053  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1194 0.1053 0.1078 0.0058  -0.0020 0.0069  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1129 0.1015 0.0987 0.0057  -0.0024 0.0056  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1174 0.1072 0.1049 0.0064  -0.0024 0.0038  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1269 0.1119 0.1184 0.0073  -0.0038 0.0079  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.1321 0.1187 0.1214 0.0074  -0.0060 0.0105  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.1318 0.1171 0.1194 0.0069  -0.0059 0.0138  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.1386 0.1282 0.1269 0.0073  -0.0082 0.0098  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.1604 0.1484 0.1450 0.0063  -0.0083 0.0169  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.1440 0.1364 0.1289 0.0062  -0.0106 0.0122  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.1549 0.1469 0.1381 0.0058  -0.0109 0.0162  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.1963 0.1923 0.1755 0.0041  -0.0136 0.0194  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1151 0.1043 0.0969 0.0047  -0.0022 0.0065  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1217 0.1131 0.1003 0.0039  -0.0014 0.0046  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.1285 0.1209 0.1029 0.0028  -0.0035 0.0055  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.1331 0.1259 0.1038 0.0015  -0.0040 0.0081  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.1325 0.1248 0.1093 0.0028  0.0009  0.0047  65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.1490 0.1435 0.1225 0.0017  0.0033  0.0019  65  CYS   A SG  
463  N N   . SER   A 60  ? 0.1340 0.1274 0.1088 0.0027  -0.0047 0.0036  66  SER   A N   
464  C CA  . SER   A 60  ? 0.1445 0.1406 0.1151 0.0007  -0.0072 0.0046  66  SER   A CA  
465  C C   . SER   A 60  ? 0.1458 0.1440 0.1092 -0.0024 -0.0059 0.0034  66  SER   A C   
466  O O   . SER   A 60  ? 0.1610 0.1620 0.1197 -0.0046 -0.0082 0.0063  66  SER   A O   
467  C CB  . SER   A 60  ? 0.1661 0.1634 0.1385 0.0004  -0.0085 0.0023  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.1832 0.1796 0.1547 -0.0006 -0.0056 -0.0027 66  SER   A OG  
469  N N   . SER   A 61  ? 0.1343 0.1313 0.0973 -0.0026 -0.0020 -0.0003 67  SER   A N   
470  C CA  . SER   A 61  ? 0.1321 0.1307 0.0888 -0.0057 0.0004  -0.0024 67  SER   A CA  
471  C C   . SER   A 61  ? 0.1404 0.1396 0.0938 -0.0065 0.0006  0.0012  67  SER   A C   
472  O O   . SER   A 61  ? 0.1494 0.1504 0.0969 -0.0094 0.0026  0.0001  67  SER   A O   
473  C CB  . SER   A 61  ? 0.1370 0.1341 0.0965 -0.0051 0.0054  -0.0073 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.1512 0.1473 0.1164 -0.0023 0.0072  -0.0061 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.1414 0.1390 0.0987 -0.0043 -0.0011 0.0054  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.1464 0.1436 0.1013 -0.0051 -0.0012 0.0095  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.1669 0.1633 0.1236 -0.0042 -0.0047 0.0151  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.1709 0.1661 0.1267 -0.0047 -0.0047 0.0192  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.1499 0.1452 0.1088 -0.0038 0.0016  0.0089  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.1601 0.1572 0.1190 -0.0044 0.0054  0.0049  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.1578 0.1567 0.1102 -0.0074 0.0073  0.0052  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.1841 0.1846 0.1379 -0.0077 0.0118  0.0012  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.1744 0.1758 0.1263 -0.0088 0.0143  -0.0031 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.1887 0.1901 0.1364 -0.0103 0.0122  -0.0044 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.1858 0.1883 0.1407 -0.0086 0.0193  -0.0064 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.1682 0.1649 0.1286 -0.0026 -0.0073 0.0155  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.1849 0.1805 0.1499 -0.0008 -0.0098 0.0208  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2121 0.2026 0.1815 0.0008  -0.0074 0.0223  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.2289 0.2177 0.1999 0.0011  -0.0078 0.0275  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.2319 0.2315 0.1930 -0.0028 -0.0128 0.0264  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.2505 0.2553 0.2101 -0.0041 -0.0160 0.0260  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.2633 0.2729 0.2221 -0.0053 -0.0200 0.0340  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.2524 0.2691 0.2065 -0.0087 -0.0231 0.0328  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.2070 0.2287 0.1512 -0.0138 -0.0237 0.0319  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.2187 0.2395 0.1572 -0.0156 -0.0216 0.0330  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.2334 0.2614 0.1732 -0.0177 -0.0261 0.0296  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.1803 0.1687 0.1516 0.0013  -0.0048 0.0182  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.1882 0.1726 0.1622 0.0014  -0.0023 0.0186  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.1689 0.1521 0.1471 0.0023  -0.0009 0.0150  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.1641 0.1498 0.1424 0.0027  -0.0011 0.0119  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.2377 0.2232 0.2072 -0.0009 -0.0001 0.0179  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.3502 0.3352 0.3160 -0.0024 -0.0004 0.0226  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.4642 0.4498 0.4265 -0.0049 0.0023  0.0218  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5390 0.5246 0.4969 -0.0068 0.0020  0.0267  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.5905 0.5806 0.5431 -0.0077 -0.0006 0.0282  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.1566 0.1359 0.1381 0.0021  0.0010  0.0154  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.1488 0.1274 0.1330 0.0015  0.0028  0.0120  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.1657 0.1452 0.1478 -0.0012 0.0049  0.0108  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2030 0.1799 0.1838 -0.0028 0.0065  0.0125  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.1342 0.1079 0.1233 0.0021  0.0043  0.0124  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.1490 0.1227 0.1419 0.0049  0.0023  0.0138  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.1948 0.1696 0.1905 0.0057  0.0022  0.0111  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.1566 0.1305 0.1511 0.0067  0.0003  0.0181  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.1711 0.1461 0.1705 0.0081  0.0003  0.0135  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.1948 0.1699 0.1938 0.0087  -0.0011 0.0179  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1415 0.1251 0.1237 -0.0020 0.0051  0.0084  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1474 0.1341 0.1285 -0.0048 0.0067  0.0077  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.1363 0.1248 0.1192 -0.0072 0.0077  0.0057  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1355 0.1261 0.1201 -0.0061 0.0066  0.0048  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.1574 0.1498 0.1381 -0.0038 0.0062  0.0075  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.1656 0.1576 0.1431 -0.0030 0.0060  0.0086  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.1791 0.1706 0.1537 -0.0050 0.0074  0.0100  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.1592 0.1515 0.1360 -0.0009 0.0048  0.0080  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.1928 0.1848 0.1635 -0.0050 0.0075  0.0109  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.1776 0.1705 0.1502 -0.0013 0.0049  0.0084  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.1933 0.1863 0.1627 -0.0034 0.0063  0.0099  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.2289 0.2230 0.1932 -0.0044 0.0065  0.0103  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.1438 0.1321 0.1256 -0.0110 0.0097  0.0051  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.1418 0.1340 0.1241 -0.0147 0.0104  0.0030  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.1593 0.1607 0.1429 -0.0149 0.0087  0.0042  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2066 0.2110 0.1904 -0.0143 0.0088  0.0057  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.1647 0.1541 0.1452 -0.0195 0.0134  0.0017  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.1878 0.1744 0.1673 -0.0181 0.0138  0.0041  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.1492 0.1343 0.1290 -0.0128 0.0115  0.0062  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1268 0.1328 0.1118 -0.0159 0.0077  0.0039  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1558 0.1713 0.1439 -0.0156 0.0060  0.0063  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1391 0.1613 0.1270 -0.0202 0.0053  0.0063  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1432 0.1627 0.1289 -0.0225 0.0059  0.0040  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.1924 0.2080 0.1837 -0.0104 0.0046  0.0077  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2091 0.2212 0.2002 -0.0071 0.0053  0.0079  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.1946 0.2057 0.1855 -0.0092 0.0040  0.0063  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1376 0.1702 0.1287 -0.0215 0.0040  0.0095  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1328 0.1753 0.1251 -0.0253 0.0022  0.0116  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1226 0.1686 0.1208 -0.0201 0.0003  0.0156  75  SER   A C   
545  O O   . SER   A 69  ? 0.1368 0.1826 0.1397 -0.0153 0.0007  0.0175  75  SER   A O   
546  C CB  . SER   A 69  ? 0.1805 0.2335 0.1745 -0.0295 0.0016  0.0141  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2850 0.3347 0.2737 -0.0350 0.0037  0.0103  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1210 0.1696 0.1191 -0.0212 -0.0011 0.0166  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1277 0.1782 0.1315 -0.0164 -0.0024 0.0203  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1308 0.1929 0.1370 -0.0196 -0.0049 0.0253  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1488 0.2156 0.1497 -0.0263 -0.0055 0.0242  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1388 0.1786 0.1408 -0.0128 -0.0015 0.0170  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1281 0.1639 0.1243 -0.0166 -0.0009 0.0131  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1251 0.1530 0.1167 -0.0180 0.0012  0.0084  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1392 0.1782 0.1351 -0.0183 -0.0019 0.0142  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1405 0.1640 0.1283 -0.0211 0.0029  0.0046  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1504 0.1853 0.1412 -0.0219 -0.0004 0.0099  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1392 0.1663 0.1264 -0.0233 0.0022  0.0050  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1309 0.1979 0.1452 -0.0154 -0.0059 0.0309  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1316 0.2106 0.1496 -0.0178 -0.0086 0.0375  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1299 0.2067 0.1436 -0.0197 -0.0094 0.0366  77  SER   A C   
562  O O   . SER   A 71  ? 0.1389 0.2045 0.1493 -0.0174 -0.0076 0.0315  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1504 0.2345 0.1804 -0.0119 -0.0089 0.0445  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1708 0.2448 0.2042 -0.0057 -0.0068 0.0431  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1306 0.2187 0.1446 -0.0240 -0.0120 0.0418  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.1398 0.2269 0.1499 -0.0262 -0.0126 0.0416  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.1527 0.2347 0.1703 -0.0190 -0.0121 0.0449  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.1590 0.2434 0.1861 -0.0139 -0.0122 0.0502  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.1667 0.2692 0.1746 -0.0336 -0.0158 0.0472  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.2043 0.3104 0.2030 -0.0423 -0.0154 0.0420  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.2966 0.4184 0.2910 -0.0513 -0.0185 0.0466  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.3771 0.5012 0.3612 -0.0610 -0.0172 0.0399  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.4402 0.5774 0.4172 -0.0710 -0.0194 0.0421  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.1507 0.2262 0.1650 -0.0188 -0.0113 0.0422  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.1533 0.2235 0.1746 -0.0126 -0.0106 0.0448  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.1536 0.2340 0.1842 -0.0111 -0.0126 0.0551  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.1745 0.2666 0.2035 -0.0163 -0.0153 0.0605  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.1832 0.2478 0.1982 -0.0149 -0.0098 0.0406  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2202 0.2848 0.2255 -0.0212 -0.0092 0.0345  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.1679 0.2405 0.1723 -0.0246 -0.0104 0.0361  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.1411 0.2176 0.1816 -0.0043 -0.0109 0.0578  80  SER   A N   
582  C CA  . SER   A 74  ? 0.1589 0.2444 0.2108 -0.0017 -0.0120 0.0682  80  SER   A CA  
583  C C   . SER   A 74  ? 0.1444 0.2207 0.2063 0.0057  -0.0086 0.0692  80  SER   A C   
584  O O   . SER   A 74  ? 0.1399 0.2038 0.1990 0.0082  -0.0058 0.0615  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2254 0.3227 0.2818 -0.0030 -0.0137 0.0733  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.2796 0.3694 0.3396 0.0017  -0.0105 0.0688  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1573 0.2406 0.2318 0.0088  -0.0087 0.0792  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.1675 0.2426 0.2535 0.0156  -0.0046 0.0810  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.1822 0.2566 0.2765 0.0199  -0.0015 0.0805  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2007 0.2868 0.3032 0.0203  -0.0029 0.0883  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.1777 0.2610 0.2739 0.0166  -0.0060 0.0930  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2080 0.2823 0.3165 0.0229  -0.0014 0.0956  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2211 0.2821 0.3220 0.0224  0.0005  0.0874  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2224 0.3069 0.3430 0.0241  -0.0031 0.1099  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.1770 0.2388 0.2687 0.0225  0.0025  0.0714  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.1952 0.2548 0.2920 0.0257  0.0062  0.0685  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2026 0.2508 0.3081 0.0311  0.0124  0.0659  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.1961 0.2342 0.2973 0.0311  0.0140  0.0605  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2266 0.2813 0.3096 0.0224  0.0055  0.0587  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2659 0.3304 0.3398 0.0164  0.0003  0.0599  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2485 0.2989 0.3344 0.0252  0.0098  0.0542  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3040 0.3807 0.3829 0.0152  -0.0010 0.0652  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2074 0.2574 0.3254 0.0353  0.0166  0.0689  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2188 0.2577 0.3455 0.0399  0.0238  0.0654  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2282 0.2572 0.3439 0.0383  0.0265  0.0533  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.2534 0.2859 0.3627 0.0364  0.0252  0.0502  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2323 0.2765 0.3773 0.0450  0.0283  0.0728  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2730 0.3058 0.4295 0.0496  0.0364  0.0708  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.3056 0.3341 0.4686 0.0513  0.0374  0.0753  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.3065 0.3319 0.4661 0.0516  0.0436  0.0635  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.3329 0.3496 0.5064 0.0551  0.0457  0.0726  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.3146 0.3283 0.4839 0.0550  0.0520  0.0603  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3293 0.3387 0.5062 0.0568  0.0531  0.0650  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.1995 0.2168 0.3114 0.0382  0.0295  0.0465  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.1932 0.2019 0.2944 0.0361  0.0316  0.0357  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.1819 0.1811 0.2917 0.0390  0.0401  0.0313  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.1809 0.1748 0.2985 0.0409  0.0431  0.0331  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.1810 0.1851 0.2695 0.0325  0.0276  0.0309  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.2053 0.2016 0.2833 0.0301  0.0294  0.0206  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.1891 0.2018 0.2700 0.0295  0.0205  0.0347  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.1800 0.1767 0.2875 0.0386  0.0441  0.0252  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.1969 0.1847 0.3116 0.0404  0.0531  0.0198  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.2016 0.1787 0.3095 0.0377  0.0550  0.0121  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.2085 0.1851 0.3033 0.0340  0.0494  0.0089  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.2377 0.2257 0.3480 0.0391  0.0565  0.0138  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.3273 0.3253 0.4472 0.0420  0.0566  0.0207  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.4673 0.4668 0.6077 0.0477  0.0620  0.0283  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.5062 0.4964 0.6546 0.0496  0.0706  0.0240  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.5349 0.5449 0.6836 0.0499  0.0576  0.0388  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.2170 0.1853 0.3341 0.0393  0.0636  0.0085  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.2345 0.1922 0.3461 0.0360  0.0669  0.0001  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.2400 0.1965 0.3345 0.0305  0.0647  -0.0091 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.2646 0.2239 0.3550 0.0296  0.0659  -0.0119 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.2470 0.1955 0.3711 0.0380  0.0780  -0.0035 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.2378 0.1911 0.3223 0.0265  0.0611  -0.0133 87  SER   A N   
636  C CA  . SER   A 81  ? 0.2371 0.1902 0.3058 0.0210  0.0584  -0.0210 87  SER   A CA  
637  C C   . SER   A 81  ? 0.2484 0.1934 0.3135 0.0168  0.0618  -0.0288 87  SER   A C   
638  O O   . SER   A 81  ? 0.2637 0.2023 0.3387 0.0183  0.0669  -0.0285 87  SER   A O   
639  C CB  . SER   A 81  ? 0.2412 0.2014 0.3006 0.0200  0.0486  -0.0170 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.2331 0.1920 0.2943 0.0202  0.0455  -0.0142 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.2580 0.2038 0.3090 0.0113  0.0582  -0.0348 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.2605 0.2008 0.3067 0.0062  0.0600  -0.0419 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.2356 0.1756 0.2853 0.0073  0.0557  -0.0375 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.2407 0.1748 0.2916 0.0044  0.0589  -0.0419 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.3244 0.2692 0.3549 0.0004  0.0549  -0.0466 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.4233 0.3652 0.4466 -0.0062 0.0555  -0.0541 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.5128 0.4613 0.5217 -0.0116 0.0493  -0.0565 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.5040 0.4575 0.5078 -0.0110 0.0470  -0.0545 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.5485 0.4979 0.5519 -0.0166 0.0467  -0.0598 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.2225 0.1687 0.2739 0.0110  0.0492  -0.0290 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.2123 0.1592 0.2653 0.0114  0.0448  -0.0251 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.2079 0.1543 0.2733 0.0161  0.0461  -0.0173 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.2089 0.1537 0.2766 0.0157  0.0447  -0.0153 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.2193 0.1739 0.2633 0.0105  0.0362  -0.0223 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.2241 0.1797 0.2565 0.0054  0.0340  -0.0289 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.2652 0.2190 0.2941 0.0012  0.0332  -0.0332 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.2533 0.2123 0.2788 0.0044  0.0329  -0.0304 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.2975 0.2542 0.3161 -0.0039 0.0305  -0.0381 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.2836 0.2448 0.2985 -0.0006 0.0305  -0.0353 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.3235 0.2839 0.3352 -0.0048 0.0292  -0.0389 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.3820 0.3462 0.3837 -0.0101 0.0264  -0.0428 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.1994 0.1477 0.2733 0.0206  0.0487  -0.0121 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.1972 0.1464 0.2841 0.0251  0.0498  -0.0031 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.1980 0.1451 0.2973 0.0291  0.0571  -0.0012 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.2091 0.1584 0.3052 0.0290  0.0583  -0.0041 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.1953 0.1548 0.2803 0.0268  0.0421  0.0053  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.1641 0.1270 0.2385 0.0236  0.0351  0.0047  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.1682 0.1299 0.2448 0.0231  0.0337  0.0075  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.1653 0.1324 0.2285 0.0214  0.0304  0.0016  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.1583 0.1233 0.2262 0.0203  0.0280  0.0067  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.1659 0.1360 0.2214 0.0191  0.0248  0.0016  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.1578 0.1269 0.2158 0.0185  0.0238  0.0037  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.1516 0.1236 0.2029 0.0163  0.0190  0.0032  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.2159 0.1597 0.3297 0.0328  0.0615  0.0047  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.2190 0.1628 0.3475 0.0378  0.0679  0.0091  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.2357 0.1921 0.3656 0.0406  0.0617  0.0183  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.2250 0.1888 0.3458 0.0387  0.0533  0.0215  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.2345 0.1725 0.3783 0.0410  0.0728  0.0150  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.2351 0.1761 0.3724 0.0389  0.0656  0.0186  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.2209 0.1621 0.3397 0.0331  0.0606  0.0093  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.2394 0.1990 0.3815 0.0448  0.0660  0.0228  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.2342 0.2069 0.3785 0.0469  0.0602  0.0317  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2232 0.2022 0.3731 0.0483  0.0549  0.0429  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.2376 0.2116 0.3986 0.0507  0.0587  0.0471  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.2433 0.2181 0.4024 0.0515  0.0668  0.0349  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2003 0.1891 0.3405 0.0458  0.0463  0.0466  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.1900 0.1850 0.3315 0.0454  0.0408  0.0555  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.1828 0.1907 0.3159 0.0428  0.0329  0.0595  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.1984 0.2081 0.3234 0.0412  0.0317  0.0541  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.1952 0.1822 0.3271 0.0420  0.0396  0.0496  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.2026 0.1912 0.3162 0.0370  0.0337  0.0424  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.2048 0.1841 0.3105 0.0341  0.0346  0.0340  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.1898 0.1726 0.2819 0.0301  0.0282  0.0313  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.1936 0.1791 0.2750 0.0279  0.0249  0.0266  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2007 0.1865 0.2819 0.0288  0.0270  0.0239  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.1680 0.1557 0.2393 0.0247  0.0200  0.0246  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.1831 0.1991 0.3164 0.0416  0.0276  0.0680  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.1913 0.2184 0.3147 0.0376  0.0204  0.0706  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.1758 0.1983 0.2839 0.0330  0.0171  0.0633  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.1783 0.1959 0.2864 0.0325  0.0175  0.0634  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.1967 0.2361 0.3283 0.0378  0.0167  0.0838  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.1986 0.2469 0.3448 0.0416  0.0182  0.0924  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.1952 0.2544 0.3379 0.0396  0.0146  0.0937  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2184 0.2636 0.3827 0.0475  0.0239  0.0987  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2151 0.2833 0.3720 0.0431  0.0161  0.1015  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2303 0.2840 0.4097 0.0515  0.0257  0.1069  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2371 0.3027 0.4127 0.0493  0.0216  0.1082  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.2732 0.3483 0.4644 0.0532  0.0233  0.1164  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1566 0.1811 0.2524 0.0296  0.0140  0.0573  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1464 0.1679 0.2287 0.0255  0.0108  0.0510  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1337 0.1662 0.2102 0.0215  0.0055  0.0556  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1378 0.1786 0.2148 0.0207  0.0038  0.0586  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1515 0.1666 0.2250 0.0246  0.0119  0.0412  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1387 0.1512 0.2003 0.0209  0.0089  0.0355  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.1492 0.1543 0.2038 0.0204  0.0102  0.0266  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.1555 0.1540 0.2132 0.0222  0.0140  0.0230  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1393 0.1453 0.1843 0.0176  0.0072  0.0231  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1269 0.1598 0.1975 0.0183  0.0032  0.0557  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1288 0.1717 0.1929 0.0134  -0.0011 0.0590  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1306 0.1709 0.1822 0.0097  -0.0024 0.0505  96  SER   A C   
721  O O   . SER   A 90  ? 0.1448 0.1757 0.1928 0.0109  -0.0007 0.0429  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1519 0.1975 0.2173 0.0117  -0.0023 0.0645  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2022 0.2380 0.2631 0.0115  -0.0007 0.0577  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1318 0.1810 0.1773 0.0048  -0.0054 0.0522  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1307 0.1780 0.1652 0.0006  -0.0061 0.0450  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1270 0.1680 0.1598 0.0029  -0.0046 0.0389  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1365 0.1711 0.1625 0.0017  -0.0040 0.0321  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1520 0.1933 0.1815 -0.0009 -0.0055 0.0406  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.1631 0.2109 0.1927 -0.0041 -0.0068 0.0462  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2010 0.2552 0.2226 -0.0105 -0.0081 0.0455  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.1818 0.2307 0.2184 -0.0021 -0.0067 0.0525  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.1996 0.2592 0.2227 -0.0124 -0.0091 0.0515  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.1980 0.2546 0.2304 -0.0073 -0.0084 0.0563  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1154 0.1588 0.1543 0.0057  -0.0039 0.0417  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1212 0.1593 0.1587 0.0076  -0.0022 0.0366  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1141 0.1597 0.1486 0.0044  -0.0036 0.0375  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1225 0.1785 0.1610 0.0028  -0.0054 0.0440  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1305 0.1655 0.1776 0.0129  0.0008  0.0385  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1549 0.1844 0.2006 0.0147  0.0032  0.0331  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1657 0.1862 0.2040 0.0142  0.0036  0.0260  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.1878 0.2149 0.2437 0.0193  0.0072  0.0348  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1204 0.1609 0.1483 0.0033  -0.0030 0.0314  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1187 0.1646 0.1431 -0.0002 -0.0037 0.0311  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1239 0.1656 0.1497 0.0028  -0.0016 0.0287  99  MET   A C   
745  O O   . MET   A 93  ? 0.1403 0.1731 0.1637 0.0051  -0.0001 0.0240  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1359 0.1783 0.1508 -0.0046 -0.0041 0.0258  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1490 0.1953 0.1615 -0.0083 -0.0054 0.0272  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.1798 0.2204 0.1827 -0.0132 -0.0042 0.0202  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2334 0.2617 0.2372 -0.0077 -0.0026 0.0158  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1125 0.1614 0.1421 0.0024  -0.0016 0.0317  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1234 0.1691 0.1543 0.0047  0.0009  0.0295  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1237 0.1702 0.1481 0.0009  0.0006  0.0267  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1411 0.1946 0.1631 -0.0038 -0.0013 0.0283  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1516 0.2040 0.1937 0.0080  0.0024  0.0349  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.1891 0.2398 0.2402 0.0125  0.0040  0.0381  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2106 0.2667 0.2742 0.0163  0.0070  0.0428  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2190 0.2576 0.2669 0.0149  0.0064  0.0320  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1278 0.1676 0.1494 0.0024  0.0027  0.0227  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1159 0.1555 0.1321 -0.0008 0.0030  0.0204  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1120 0.1494 0.1301 0.0018  0.0058  0.0192  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1236 0.1572 0.1450 0.0056  0.0077  0.0185  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1392 0.1704 0.1469 -0.0028 0.0026  0.0159  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1155 0.1548 0.1309 -0.0009 0.0065  0.0186  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1223 0.1590 0.1374 0.0006  0.0093  0.0169  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1521 0.1793 0.1583 -0.0001 0.0093  0.0128  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.1776 0.2027 0.1786 -0.0032 0.0081  0.0119  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1153 0.1594 0.1321 -0.0023 0.0100  0.0187  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1338 0.1749 0.1489 -0.0015 0.0132  0.0165  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1136 0.1689 0.1406 -0.0014 0.0095  0.0239  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1641 0.1862 0.1694 0.0025  0.0108  0.0107  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.1705 0.1852 0.1683 0.0020  0.0103  0.0080  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.1688 0.1801 0.1661 0.0041  0.0121  0.0056  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.1723 0.1849 0.1754 0.0065  0.0138  0.0055  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.1798 0.1870 0.1701 0.0029  0.0121  0.0038  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.1863 0.1909 0.1745 0.0036  0.0138  0.0010  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.1765 0.1780 0.1655 0.0050  0.0121  -0.0002 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.1733 0.1731 0.1606 0.0048  0.0089  0.0009  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.1847 0.1871 0.1645 0.0011  0.0136  0.0003  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.1958 0.1968 0.1723 0.0005  0.0155  -0.0032 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2001 0.2024 0.1788 0.0005  0.0203  -0.0059 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2031 0.2018 0.1746 -0.0006 0.0136  -0.0046 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.2073 0.2074 0.1818 -0.0009 0.0215  -0.0096 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2010 0.1995 0.1705 -0.0019 0.0171  -0.0088 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.1798 0.1804 0.1716 0.0062  0.0146  -0.0026 105 SER   A N   
785  C CA  . SER   A 99  ? 0.1607 0.1583 0.1527 0.0068  0.0136  -0.0044 105 SER   A CA  
786  C C   . SER   A 99  ? 0.1838 0.1792 0.1756 0.0063  0.0176  -0.0087 105 SER   A C   
787  O O   . SER   A 99  ? 0.2082 0.2047 0.2041 0.0070  0.0221  -0.0098 105 SER   A O   
788  C CB  . SER   A 99  ? 0.1768 0.1751 0.1751 0.0089  0.0120  -0.0021 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.1903 0.1909 0.1968 0.0109  0.0150  -0.0009 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.1731 0.1658 0.1607 0.0048  0.0163  -0.0114 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.1853 0.1754 0.1716 0.0031  0.0197  -0.0166 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.1922 0.1799 0.1815 0.0038  0.0180  -0.0171 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.1796 0.1682 0.1700 0.0051  0.0137  -0.0138 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.2015 0.1923 0.1773 -0.0014 0.0189  -0.0191 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.2150 0.2080 0.1876 -0.0023 0.0209  -0.0183 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.2309 0.2257 0.1928 -0.0071 0.0203  -0.0197 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.2831 0.2776 0.2396 -0.0106 0.0207  -0.0236 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.2219 0.2189 0.1806 -0.0077 0.0192  -0.0166 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.1927 0.1772 0.1841 0.0030  0.0219  -0.0216 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.1995 0.1815 0.1950 0.0038  0.0208  -0.0218 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.1973 0.1810 0.1881 0.0024  0.0148  -0.0203 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.1881 0.1718 0.1833 0.0045  0.0122  -0.0173 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.2186 0.1962 0.2149 0.0016  0.0267  -0.0282 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.2261 0.2035 0.2247 0.0024  0.0323  -0.0294 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.1994 0.1816 0.1910 0.0014  0.0286  -0.0267 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.1802 0.1659 0.1626 -0.0012 0.0125  -0.0217 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.1726 0.1609 0.1517 -0.0024 0.0070  -0.0195 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.1497 0.1399 0.1304 0.0003  0.0032  -0.0140 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.1653 0.1573 0.1454 0.0001  -0.0008 -0.0117 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.1447 0.1346 0.1279 0.0026  0.0047  -0.0118 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.1403 0.1312 0.1253 0.0046  0.0020  -0.0075 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1334 0.1235 0.1244 0.0066  0.0013  -0.0063 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1298 0.1204 0.1219 0.0074  -0.0007 -0.0037 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.1364 0.1282 0.1217 0.0053  0.0039  -0.0059 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.1469 0.1397 0.1256 0.0031  0.0040  -0.0060 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.1499 0.1434 0.1244 0.0016  0.0010  -0.0048 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.1537 0.1472 0.1321 0.0028  0.0070  -0.0067 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1340 0.1225 0.1289 0.0071  0.0033  -0.0084 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1350 0.1233 0.1351 0.0086  0.0025  -0.0068 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1328 0.1217 0.1316 0.0080  -0.0009 -0.0061 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.1437 0.1332 0.1394 0.0063  -0.0025 -0.0074 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1527 0.1385 0.1571 0.0089  0.0053  -0.0089 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.1601 0.1455 0.1706 0.0111  0.0099  -0.0077 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1256 0.1152 0.1271 0.0090  -0.0019 -0.0038 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1271 0.1172 0.1291 0.0088  -0.0042 -0.0030 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.1299 0.1202 0.1303 0.0090  -0.0050 -0.0010 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1342 0.1244 0.1367 0.0093  -0.0058 -0.0002 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1218 0.1121 0.1191 0.0087  -0.0043 -0.0005 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1187 0.1084 0.1149 0.0085  -0.0045 0.0014  112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1111 0.1006 0.1096 0.0083  -0.0033 0.0016  112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1149 0.1060 0.1144 0.0080  -0.0023 0.0014  112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1172 0.1050 0.1168 0.0081  -0.0029 0.0023  113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1143 0.1018 0.1150 0.0067  -0.0011 0.0015  113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1122 0.1004 0.1103 0.0047  0.0003  0.0016  113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1186 0.1052 0.1149 0.0046  0.0006  0.0024  113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1188 0.1036 0.1228 0.0071  -0.0002 0.0013  113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.1361 0.1220 0.1435 0.0083  -0.0011 0.0008  113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.1294 0.1125 0.1333 0.0047  0.0030  -0.0003 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.1716 0.1556 0.1840 0.0094  -0.0003 0.0012  113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1047 0.0958 0.1027 0.0027  0.0011  0.0012  114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1048 0.0977 0.1005 -0.0005 0.0024  0.0010  114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1115 0.1025 0.1072 -0.0032 0.0047  -0.0012 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1163 0.1082 0.1133 -0.0034 0.0048  -0.0020 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1112 0.1105 0.1074 -0.0015 0.0016  0.0027  114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1186 0.1223 0.1126 -0.0059 0.0024  0.0029  114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1425 0.1455 0.1348 -0.0065 0.0031  0.0030  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1459 0.1576 0.1419 -0.0067 0.0010  0.0060  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1158 0.1038 0.1100 -0.0055 0.0070  -0.0026 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1189 0.1038 0.1132 -0.0086 0.0104  -0.0057 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.1304 0.1162 0.1212 -0.0137 0.0128  -0.0075 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.1350 0.1215 0.1241 -0.0142 0.0122  -0.0062 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.1327 0.1107 0.1312 -0.0056 0.0123  -0.0059 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.1412 0.1153 0.1398 -0.0045 0.0127  -0.0042 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.1547 0.1231 0.1591 -0.0013 0.0142  -0.0030 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.1749 0.1457 0.1816 0.0029  0.0103  0.0000  115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.1723 0.1428 0.1842 0.0053  0.0101  0.0004  115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.1934 0.1613 0.2089 0.0042  0.0139  -0.0024 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.1843 0.1577 0.1976 0.0082  0.0063  0.0031  115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.1496 0.1350 0.1389 -0.0183 0.0160  -0.0111 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.1864 0.1721 0.1716 -0.0248 0.0191  -0.0142 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2272 0.2046 0.2142 -0.0267 0.0250  -0.0188 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2131 0.1850 0.2053 -0.0222 0.0261  -0.0186 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.1939 0.1891 0.1748 -0.0301 0.0176  -0.0143 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.1830 0.1792 0.1630 -0.0328 0.0197  -0.0173 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.2614 0.2378 0.2445 -0.0338 0.0292  -0.0232 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.2898 0.2573 0.2752 -0.0359 0.0361  -0.0283 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.2884 0.2554 0.2758 -0.0358 0.0384  -0.0310 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.3212 0.2799 0.3137 -0.0347 0.0440  -0.0340 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.3413 0.3077 0.3216 -0.0448 0.0410  -0.0338 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.4072 0.3834 0.3799 -0.0527 0.0403  -0.0365 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.4934 0.4705 0.4599 -0.0626 0.0443  -0.0418 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.5207 0.5053 0.4834 -0.0660 0.0409  -0.0396 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.4973 0.4675 0.4629 -0.0681 0.0520  -0.0491 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.2423 0.2179 0.2266 -0.0365 0.0344  -0.0294 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.2351 0.2114 0.2202 -0.0372 0.0364  -0.0318 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.2236 0.1985 0.2156 -0.0292 0.0336  -0.0281 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.2615 0.2360 0.2557 -0.0291 0.0358  -0.0300 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.2254 0.2124 0.2031 -0.0434 0.0338  -0.0317 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.2355 0.2259 0.2059 -0.0524 0.0361  -0.0353 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.2630 0.2617 0.2297 -0.0546 0.0314  -0.0316 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.2784 0.2653 0.2451 -0.0602 0.0430  -0.0426 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.2936 0.2943 0.2541 -0.0638 0.0348  -0.0364 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.2998 0.2933 0.2596 -0.0677 0.0420  -0.0435 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2030 0.1781 0.1977 -0.0232 0.0287  -0.0229 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.1913 0.1663 0.1916 -0.0167 0.0257  -0.0195 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.1599 0.1404 0.1586 -0.0137 0.0193  -0.0147 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.1571 0.1402 0.1523 -0.0149 0.0174  -0.0131 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.1406 0.1227 0.1425 -0.0097 0.0166  -0.0125 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1352 0.1214 0.1366 -0.0068 0.0116  -0.0087 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1165 0.1095 0.1140 -0.0099 0.0100  -0.0076 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.1260 0.1216 0.1226 -0.0127 0.0110  -0.0086 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.1370 0.1225 0.1433 -0.0023 0.0097  -0.0072 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.1498 0.1386 0.1554 -0.0001 0.0057  -0.0044 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.1578 0.1385 0.1688 0.0010  0.0104  -0.0067 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1144 0.1107 0.1103 -0.0094 0.0074  -0.0049 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1196 0.1233 0.1135 -0.0119 0.0056  -0.0024 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1194 0.1249 0.1168 -0.0079 0.0029  0.0010  121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1290 0.1397 0.1270 -0.0091 0.0019  0.0035  121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1352 0.1419 0.1268 -0.0139 0.0051  -0.0012 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.1610 0.1769 0.1526 -0.0155 0.0026  0.0029  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.1541 0.1589 0.1419 -0.0190 0.0083  -0.0050 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1183 0.1200 0.1180 -0.0035 0.0019  0.0013  122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1214 0.1238 0.1244 -0.0003 0.0003  0.0035  122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1117 0.1101 0.1155 0.0030  -0.0003 0.0028  122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1164 0.1115 0.1188 0.0032  0.0001  0.0013  122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1091 0.1076 0.1151 0.0053  -0.0010 0.0038  123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1072 0.1026 0.1128 0.0074  -0.0014 0.0026  123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1049 0.1017 0.1116 0.0084  -0.0007 0.0037  123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1142 0.1138 0.1243 0.0088  -0.0002 0.0059  123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1192 0.1124 0.1267 0.0085  -0.0021 0.0012  123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1362 0.1304 0.1472 0.0087  -0.0015 0.0021  123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1389 0.1307 0.1464 0.0081  -0.0025 0.0002  123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.1568 0.1487 0.1696 0.0093  -0.0019 0.0002  123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1100 0.1051 0.1144 0.0090  -0.0005 0.0025  124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1089 0.1049 0.1146 0.0099  0.0011  0.0027  124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1092 0.1038 0.1191 0.0113  0.0023  0.0021  124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1166 0.1085 0.1258 0.0111  0.0017  0.0000  124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1147 0.1087 0.1160 0.0096  0.0013  0.0008  124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1313 0.1256 0.1341 0.0103  0.0039  0.0000  124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1272 0.1219 0.1251 0.0084  0.0006  0.0018  124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1163 0.1128 0.1313 0.0126  0.0042  0.0043  125 SER   A N   
922  C CA  . SER   A 119 ? 0.1176 0.1121 0.1383 0.0140  0.0063  0.0043  125 SER   A CA  
923  C C   . SER   A 119 ? 0.1334 0.1275 0.1586 0.0157  0.0100  0.0043  125 SER   A C   
924  O O   . SER   A 119 ? 0.1473 0.1374 0.1762 0.0166  0.0130  0.0023  125 SER   A O   
925  C CB  . SER   A 119 ? 0.1282 0.1256 0.1531 0.0142  0.0053  0.0084  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1312 0.1266 0.1628 0.0159  0.0076  0.0097  125 SER   A OG  
927  N N   . THR   A 120 ? 0.1312 0.1292 0.1572 0.0161  0.0106  0.0063  126 THR   A N   
928  C CA  . THR   A 120 ? 0.1484 0.1465 0.1806 0.0180  0.0149  0.0065  126 THR   A CA  
929  C C   . THR   A 120 ? 0.1712 0.1715 0.1992 0.0170  0.0152  0.0054  126 THR   A C   
930  O O   . THR   A 120 ? 0.1512 0.1530 0.1724 0.0150  0.0120  0.0053  126 THR   A O   
931  C CB  . THR   A 120 ? 0.1515 0.1548 0.1940 0.0204  0.0156  0.0130  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.1628 0.1735 0.2042 0.0192  0.0127  0.0170  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.1614 0.1637 0.2082 0.0211  0.0148  0.0157  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.1739 0.1745 0.2067 0.0184  0.0195  0.0049  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.1842 0.1876 0.2139 0.0174  0.0203  0.0043  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.1972 0.1994 0.2320 0.0187  0.0263  0.0020  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.2020 0.2006 0.2434 0.0206  0.0303  0.0008  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.2079 0.2122 0.2387 0.0173  0.0272  0.0008  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.2120 0.2155 0.2458 0.0177  0.0333  -0.0021 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.2077 0.2183 0.2451 0.0180  0.0337  0.0015  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.2055 0.2223 0.2474 0.0188  0.0302  0.0071  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.1922 0.2026 0.2275 0.0168  0.0379  -0.0019 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.1901 0.2073 0.2297 0.0169  0.0395  0.0008  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.1819 0.2047 0.2176 0.0150  0.0336  0.0050  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.1920 0.2225 0.2349 0.0157  0.0336  0.0095  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.2079 0.2290 0.2636 0.0212  0.0440  0.0045  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.2676 0.2825 0.3280 0.0227  0.0519  -0.0008 129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.3107 0.3232 0.3657 0.0204  0.0563  -0.0063 129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.2900 0.3018 0.3598 0.0260  0.0539  0.0005  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.1623 0.1813 0.1865 0.0121  0.0295  0.0032  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.1668 0.1892 0.1864 0.0097  0.0250  0.0060  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.1461 0.1714 0.1690 0.0102  0.0208  0.0099  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.1610 0.1894 0.1807 0.0077  0.0177  0.0118  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1376 0.1610 0.1653 0.0128  0.0208  0.0105  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1322 0.1578 0.1613 0.0126  0.0167  0.0138  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1448 0.1630 0.1674 0.0123  0.0148  0.0106  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.1613 0.1736 0.1813 0.0130  0.0170  0.0066  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1328 0.1632 0.1739 0.0158  0.0179  0.0184  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.1415 0.1815 0.1915 0.0164  0.0192  0.0232  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.1669 0.2103 0.2309 0.0207  0.0218  0.0278  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.1450 0.1931 0.1921 0.0125  0.0145  0.0267  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1207 0.1397 0.1407 0.0109  0.0111  0.0121  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1261 0.1394 0.1420 0.0109  0.0094  0.0099  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1248 0.1419 0.1448 0.0109  0.0072  0.0135  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1320 0.1552 0.1525 0.0088  0.0056  0.0164  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1302 0.1395 0.1372 0.0085  0.0075  0.0074  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1324 0.1452 0.1373 0.0057  0.0059  0.0091  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1422 0.1468 0.1467 0.0088  0.0058  0.0056  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1230 0.1369 0.1451 0.0124  0.0072  0.0131  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1187 0.1360 0.1438 0.0120  0.0052  0.0166  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1141 0.1266 0.1339 0.0108  0.0035  0.0139  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1374 0.1439 0.1547 0.0117  0.0041  0.0102  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1060 0.1219 0.1243 0.0085  0.0015  0.0157  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1067 0.1188 0.1209 0.0072  0.0003  0.0131  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1211 0.1358 0.1383 0.0068  -0.0004 0.0159  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1277 0.1495 0.1472 0.0052  -0.0013 0.0202  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1154 0.1283 0.1238 0.0037  -0.0004 0.0116  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1148 0.1260 0.1203 0.0035  0.0002  0.0099  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1190 0.1240 0.1215 0.0046  0.0005  0.0070  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1317 0.1482 0.1376 0.0018  0.0004  0.0119  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1217 0.1254 0.1212 0.0041  0.0011  0.0062  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1295 0.1443 0.1326 0.0013  0.0013  0.0105  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1211 0.1292 0.1209 0.0024  0.0017  0.0077  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1095 0.1194 0.1268 0.0077  -0.0002 0.0138  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1224 0.1341 0.1417 0.0070  -0.0008 0.0161  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1170 0.1306 0.1311 0.0032  -0.0016 0.0147  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1222 0.1311 0.1329 0.0028  -0.0013 0.0106  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1240 0.1298 0.1453 0.0089  0.0001  0.0138  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1163 0.1368 0.1298 0.0000  -0.0025 0.0181  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1242 0.1466 0.1321 -0.0046 -0.0024 0.0161  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1274 0.1464 0.1351 -0.0049 -0.0017 0.0142  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1393 0.1584 0.1510 -0.0030 -0.0020 0.0169  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.1494 0.1819 0.1566 -0.0089 -0.0037 0.0208  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2350 0.2701 0.2354 -0.0151 -0.0031 0.0180  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.1886 0.2193 0.1851 -0.0165 -0.0014 0.0129  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3425 0.3837 0.3415 -0.0187 -0.0037 0.0207  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1193 0.1356 0.1230 -0.0073 -0.0002 0.0097  137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1185 0.1327 0.1222 -0.0082 0.0010  0.0077  137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.1299 0.1476 0.1286 -0.0141 0.0027  0.0058  137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.1261 0.1426 0.1245 -0.0156 0.0045  0.0036  137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1195 0.1266 0.1253 -0.0050 0.0019  0.0038  137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1315 0.1357 0.1411 -0.0005 0.0004  0.0050  137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1314 0.1350 0.1349 -0.0057 0.0035  0.0002  137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.1309 0.1532 0.1256 -0.0181 0.0027  0.0060  138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.1386 0.1635 0.1274 -0.0248 0.0051  0.0027  138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.1448 0.1764 0.1313 -0.0291 0.0049  0.0051  138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.1557 0.1883 0.1372 -0.0349 0.0079  0.0011  138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.1441 0.1729 0.1289 -0.0288 0.0050  0.0023  138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.1433 0.1645 0.1293 -0.0257 0.0063  -0.0010 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.1579 0.1835 0.1399 -0.0303 0.0062  -0.0012 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.1526 0.1858 0.1372 -0.0287 0.0023  0.0051  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.1814 0.2201 0.1646 -0.0313 0.0012  0.0067  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.1790 0.2168 0.1572 -0.0369 0.0036  0.0021  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.1878 0.2330 0.1754 -0.0288 -0.0019 0.0128  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.1377 0.1742 0.1277 -0.0270 0.0018  0.0117  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.1470 0.1903 0.1350 -0.0311 0.0013  0.0153  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.1423 0.1804 0.1327 -0.0291 0.0032  0.0134  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.1618 0.2047 0.1501 -0.0330 0.0035  0.0156  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.1679 0.2191 0.1601 -0.0297 -0.0025 0.0244  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.2014 0.2464 0.2022 -0.0217 -0.0033 0.0269  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.1839 0.2213 0.1866 -0.0174 -0.0025 0.0229  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.2199 0.2675 0.2252 -0.0202 -0.0044 0.0329  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.1330 0.1621 0.1280 -0.0235 0.0042  0.0098  140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.1386 0.1631 0.1372 -0.0212 0.0056  0.0082  140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.1434 0.1654 0.1392 -0.0245 0.0097  0.0019  140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.1439 0.1596 0.1425 -0.0217 0.0116  -0.0026 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.1450 0.1627 0.1498 -0.0145 0.0045  0.0077  140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.1575 0.1765 0.1658 -0.0111 0.0018  0.0131  140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.1564 0.1686 0.1691 -0.0058 0.0014  0.0110  140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.1727 0.1956 0.1836 -0.0117 0.0010  0.0188  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.1432 0.1709 0.1334 -0.0310 0.0114  0.0016  141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.1473 0.1729 0.1342 -0.0354 0.0165  -0.0052 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.1504 0.1706 0.1430 -0.0323 0.0192  -0.0083 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.1649 0.1805 0.1589 -0.0326 0.0236  -0.0142 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.1646 0.1985 0.1430 -0.0444 0.0181  -0.0053 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.1890 0.2309 0.1621 -0.0484 0.0146  -0.0009 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.2118 0.2625 0.1757 -0.0584 0.0164  -0.0018 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.2045 0.2428 0.1774 -0.0472 0.0148  -0.0041 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.1392 0.1600 0.1360 -0.0292 0.0169  -0.0043 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.1437 0.1607 0.1462 -0.0266 0.0189  -0.0066 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.1618 0.1723 0.1708 -0.0209 0.0190  -0.0094 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.1777 0.1859 0.1921 -0.0192 0.0213  -0.0120 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.1555 0.1748 0.1607 -0.0254 0.0164  -0.0013 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.1496 0.1680 0.1576 -0.0210 0.0120  0.0036  142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.1556 0.1785 0.1615 -0.0220 0.0093  0.0094  142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.1552 0.1683 0.1692 -0.0153 0.0103  0.0031  142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.1625 0.1822 0.1733 -0.0168 0.0067  0.0120  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.1582 0.1719 0.1731 -0.0131 0.0073  0.0079  142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.1677 0.1765 0.1866 -0.0121 0.0110  -0.0006 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.1729 0.1820 0.1923 -0.0084 0.0056  0.0079  142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.1774 0.1829 0.2003 -0.0078 0.0085  0.0002  142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.1773 0.1826 0.1998 -0.0063 0.0062  0.0038  142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.1430 0.1514 0.1519 -0.0179 0.0165  -0.0085 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.1624 0.1656 0.1768 -0.0131 0.0164  -0.0104 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.1892 0.1895 0.2055 -0.0143 0.0216  -0.0154 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.1966 0.1936 0.2197 -0.0103 0.0221  -0.0163 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.1556 0.1575 0.1684 -0.0108 0.0134  -0.0086 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.1542 0.1572 0.1678 -0.0081 0.0093  -0.0044 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.1736 0.1759 0.1848 -0.0067 0.0073  -0.0031 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.1681 0.1687 0.1877 -0.0042 0.0080  -0.0044 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.2167 0.2185 0.2275 -0.0201 0.0255  -0.0185 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.2572 0.2552 0.2699 -0.0219 0.0319  -0.0241 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.3023 0.3007 0.3193 -0.0230 0.0364  -0.0270 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.3171 0.3120 0.3369 -0.0245 0.0427  -0.0320 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.2674 0.2668 0.2713 -0.0288 0.0349  -0.0273 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.3225 0.3218 0.3224 -0.0288 0.0318  -0.0256 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.3390 0.3356 0.3431 -0.0229 0.0281  -0.0225 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.3979 0.4004 0.3900 -0.0352 0.0331  -0.0272 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.3157 0.3178 0.3337 -0.0227 0.0340  -0.0242 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.3486 0.3517 0.3706 -0.0243 0.0385  -0.0269 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.3567 0.3607 0.3865 -0.0195 0.0354  -0.0237 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.3627 0.3670 0.3928 -0.0163 0.0296  -0.0195 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.4138 0.4220 0.4267 -0.0318 0.0404  -0.0275 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.5014 0.5143 0.5099 -0.0320 0.0341  -0.0210 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.5975 0.6168 0.5957 -0.0394 0.0340  -0.0194 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.5852 0.6089 0.5818 -0.0399 0.0302  -0.0136 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.6523 0.6725 0.6443 -0.0449 0.0378  -0.0237 145 GLU   A OE2 
1078 N N   . SER   B 1   ? 0.1954 0.1994 0.2070 0.0008  -0.0158 0.0287  7   SER   C N   
1079 C CA  . SER   B 1   ? 0.1892 0.1951 0.2094 -0.0001 -0.0164 0.0290  7   SER   C CA  
1080 C C   . SER   B 1   ? 0.1779 0.1822 0.1975 -0.0007 -0.0157 0.0256  7   SER   C C   
1081 O O   . SER   B 1   ? 0.1999 0.2015 0.2122 -0.0006 -0.0158 0.0233  7   SER   C O   
1082 C CB  . SER   B 1   ? 0.2272 0.2345 0.2491 -0.0012 -0.0208 0.0316  7   SER   C CB  
1083 O OG  . SER   B 1   ? 0.2853 0.2904 0.3000 -0.0024 -0.0239 0.0299  7   SER   C OG  
1084 N N   . GLY   B 2   ? 0.1738 0.1792 0.2008 -0.0010 -0.0147 0.0255  8   GLY   C N   
1085 C CA  . GLY   B 2   ? 0.1703 0.1739 0.1966 -0.0014 -0.0137 0.0230  8   GLY   C CA  
1086 C C   . GLY   B 2   ? 0.1492 0.1534 0.1821 -0.0010 -0.0106 0.0226  8   GLY   C C   
1087 O O   . GLY   B 2   ? 0.1515 0.1571 0.1881 -0.0002 -0.0087 0.0232  8   GLY   C O   
1088 N N   . ALA   B 3   ? 0.1323 0.1354 0.1668 -0.0016 -0.0099 0.0215  9   ALA   C N   
1089 C CA  . ALA   B 3   ? 0.1286 0.1315 0.1679 -0.0011 -0.0065 0.0210  9   ALA   C CA  
1090 C C   . ALA   B 3   ? 0.1254 0.1253 0.1606 -0.0009 -0.0050 0.0188  9   ALA   C C   
1091 O O   . ALA   B 3   ? 0.1508 0.1490 0.1816 -0.0015 -0.0067 0.0182  9   ALA   C O   
1092 C CB  . ALA   B 3   ? 0.1618 0.1668 0.2106 -0.0019 -0.0065 0.0235  9   ALA   C CB  
1093 N N   . ILE   B 4   ? 0.1191 0.1179 0.1554 0.0000  -0.0017 0.0177  10  ILE   C N   
1094 C CA  . ILE   B 4   ? 0.1213 0.1171 0.1543 0.0003  0.0003  0.0164  10  ILE   C CA  
1095 C C   . ILE   B 4   ? 0.1211 0.1169 0.1613 -0.0003 0.0027  0.0178  10  ILE   C C   
1096 O O   . ILE   B 4   ? 0.1304 0.1277 0.1767 -0.0001 0.0043  0.0187  10  ILE   C O   
1097 C CB  . ILE   B 4   ? 0.1294 0.1236 0.1575 0.0019  0.0024  0.0141  10  ILE   C CB  
1098 C CG1 . ILE   B 4   ? 0.1365 0.1316 0.1602 0.0026  0.0004  0.0128  10  ILE   C CG1 
1099 C CG2 . ILE   B 4   ? 0.1582 0.1489 0.1815 0.0025  0.0042  0.0131  10  ILE   C CG2 
1100 C CD1 . ILE   B 4   ? 0.1561 0.1507 0.1774 0.0038  0.0018  0.0106  10  ILE   C CD1 
1101 N N   . TYR   B 5   ? 0.1259 0.1199 0.1663 -0.0010 0.0032  0.0182  11  TYR   C N   
1102 C CA  . TYR   B 5   ? 0.1309 0.1248 0.1790 -0.0015 0.0060  0.0198  11  TYR   C CA  
1103 C C   . TYR   B 5   ? 0.1357 0.1254 0.1789 -0.0005 0.0099  0.0187  11  TYR   C C   
1104 O O   . TYR   B 5   ? 0.1583 0.1456 0.1975 -0.0008 0.0094  0.0185  11  TYR   C O   
1105 C CB  . TYR   B 5   ? 0.1391 0.1347 0.1933 -0.0036 0.0030  0.0216  11  TYR   C CB  
1106 C CG  . TYR   B 5   ? 0.1352 0.1348 0.1939 -0.0044 -0.0010 0.0232  11  TYR   C CG  
1107 C CD1 . TYR   B 5   ? 0.1446 0.1472 0.2128 -0.0044 -0.0001 0.0254  11  TYR   C CD1 
1108 C CD2 . TYR   B 5   ? 0.1516 0.1517 0.2045 -0.0048 -0.0052 0.0226  11  TYR   C CD2 
1109 C CE1 . TYR   B 5   ? 0.1517 0.1578 0.2237 -0.0048 -0.0038 0.0273  11  TYR   C CE1 
1110 C CE2 . TYR   B 5   ? 0.1667 0.1700 0.2223 -0.0053 -0.0087 0.0243  11  TYR   C CE2 
1111 C CZ  . TYR   B 5   ? 0.1688 0.1753 0.2339 -0.0053 -0.0082 0.0268  11  TYR   C CZ  
1112 O OH  . TYR   B 5   ? 0.1987 0.2082 0.2660 -0.0055 -0.0116 0.0289  11  TYR   C OH  
1113 N N   . VAL   B 6   ? 0.1480 0.1362 0.1904 0.0008  0.0138  0.0180  12  VAL   C N   
1114 C CA  . VAL   B 6   ? 0.1593 0.1431 0.1955 0.0021  0.0177  0.0171  12  VAL   C CA  
1115 C C   . VAL   B 6   ? 0.1618 0.1445 0.2042 0.0023  0.0229  0.0182  12  VAL   C C   
1116 O O   . VAL   B 6   ? 0.1380 0.1223 0.1851 0.0025  0.0240  0.0180  12  VAL   C O   
1117 C CB  . VAL   B 6   ? 0.1758 0.1579 0.2021 0.0037  0.0173  0.0144  12  VAL   C CB  
1118 C CG1 . VAL   B 6   ? 0.1776 0.1618 0.2063 0.0040  0.0171  0.0132  12  VAL   C CG1 
1119 C CG2 . VAL   B 6   ? 0.2066 0.1839 0.2255 0.0053  0.0211  0.0138  12  VAL   C CG2 
1120 N N   . GLY   B 7   ? 0.1788 0.1587 0.2223 0.0023  0.0265  0.0195  13  GLY   C N   
1121 C CA  . GLY   B 7   ? 0.1777 0.1564 0.2278 0.0026  0.0322  0.0207  13  GLY   C CA  
1122 C C   . GLY   B 7   ? 0.1715 0.1551 0.2351 0.0014  0.0312  0.0226  13  GLY   C C   
1123 O O   . GLY   B 7   ? 0.1797 0.1668 0.2489 -0.0003 0.0266  0.0240  13  GLY   C O   
1124 N N   . ASN   B 8   ? 0.1666 0.1501 0.2342 0.0022  0.0347  0.0225  14  ASN   C N   
1125 C CA  . ASN   B 8   ? 0.1692 0.1574 0.2496 0.0014  0.0336  0.0245  14  ASN   C CA  
1126 C C   . ASN   B 8   ? 0.1565 0.1467 0.2350 0.0017  0.0305  0.0232  14  ASN   C C   
1127 O O   . ASN   B 8   ? 0.1545 0.1465 0.2410 0.0020  0.0319  0.0241  14  ASN   C O   
1128 C CB  . ASN   B 8   ? 0.1893 0.1764 0.2791 0.0020  0.0402  0.0261  14  ASN   C CB  
1129 C CG  . ASN   B 8   ? 0.2742 0.2612 0.3710 0.0010  0.0423  0.0286  14  ASN   C CG  
1130 O OD1 . ASN   B 8   ? 0.2972 0.2887 0.4063 -0.0005 0.0397  0.0313  14  ASN   C OD1 
1131 N ND2 . ASN   B 8   ? 0.3085 0.2905 0.3974 0.0019  0.0465  0.0278  14  ASN   C ND2 
1132 N N   . TYR   B 9   ? 0.1359 0.1261 0.2049 0.0017  0.0263  0.0213  15  TYR   C N   
1133 C CA  . TYR   B 9   ? 0.1271 0.1191 0.1942 0.0019  0.0234  0.0201  15  TYR   C CA  
1134 C C   . TYR   B 9   ? 0.1224 0.1177 0.1886 0.0008  0.0173  0.0210  15  TYR   C C   
1135 O O   . TYR   B 9   ? 0.1320 0.1265 0.1934 0.0002  0.0151  0.0208  15  TYR   C O   
1136 C CB  . TYR   B 9   ? 0.1450 0.1334 0.2007 0.0032  0.0245  0.0165  15  TYR   C CB  
1137 C CG  . TYR   B 9   ? 0.1594 0.1437 0.2133 0.0044  0.0303  0.0148  15  TYR   C CG  
1138 C CD1 . TYR   B 9   ? 0.1839 0.1684 0.2453 0.0047  0.0337  0.0150  15  TYR   C CD1 
1139 C CD2 . TYR   B 9   ? 0.1989 0.1786 0.2427 0.0054  0.0326  0.0131  15  TYR   C CD2 
1140 C CE1 . TYR   B 9   ? 0.2126 0.1925 0.2711 0.0059  0.0394  0.0131  15  TYR   C CE1 
1141 C CE2 . TYR   B 9   ? 0.2311 0.2065 0.2713 0.0066  0.0380  0.0114  15  TYR   C CE2 
1142 C CZ  . TYR   B 9   ? 0.2605 0.2358 0.3079 0.0068  0.0414  0.0112  15  TYR   C CZ  
1143 O OH  . TYR   B 9   ? 0.3285 0.2987 0.3715 0.0080  0.0471  0.0091  15  TYR   C OH  
1144 N N   . ARG   B 10  ? 0.1117 0.1101 0.1819 0.0007  0.0149  0.0219  16  ARG   C N   
1145 C CA  . ARG   B 10  ? 0.1138 0.1148 0.1817 0.0000  0.0097  0.0226  16  ARG   C CA  
1146 C C   . ARG   B 10  ? 0.1108 0.1114 0.1742 0.0009  0.0097  0.0207  16  ARG   C C   
1147 O O   . ARG   B 10  ? 0.1194 0.1204 0.1878 0.0014  0.0119  0.0209  16  ARG   C O   
1148 C CB  . ARG   B 10  ? 0.1303 0.1353 0.2080 -0.0009 0.0071  0.0262  16  ARG   C CB  
1149 C CG  . ARG   B 10  ? 0.1351 0.1425 0.2102 -0.0013 0.0023  0.0272  16  ARG   C CG  
1150 C CD  . ARG   B 10  ? 0.1358 0.1471 0.2198 -0.0021 -0.0009 0.0310  16  ARG   C CD  
1151 N NE  . ARG   B 10  ? 0.1483 0.1617 0.2328 -0.0016 -0.0031 0.0329  16  ARG   C NE  
1152 C CZ  . ARG   B 10  ? 0.1544 0.1687 0.2331 -0.0020 -0.0075 0.0336  16  ARG   C CZ  
1153 N NH1 . ARG   B 10  ? 0.1778 0.1908 0.2493 -0.0030 -0.0102 0.0320  16  ARG   C NH1 
1154 N NH2 . ARG   B 10  ? 0.1737 0.1896 0.2532 -0.0014 -0.0087 0.0358  16  ARG   C NH2 
1155 N N   . VAL   B 11  ? 0.1122 0.1120 0.1668 0.0010  0.0073  0.0189  17  VAL   C N   
1156 C CA  . VAL   B 11  ? 0.1058 0.1057 0.1569 0.0017  0.0071  0.0171  17  VAL   C CA  
1157 C C   . VAL   B 11  ? 0.1088 0.1112 0.1596 0.0013  0.0036  0.0187  17  VAL   C C   
1158 O O   . VAL   B 11  ? 0.1178 0.1202 0.1639 0.0009  0.0009  0.0189  17  VAL   C O   
1159 C CB  . VAL   B 11  ? 0.1173 0.1146 0.1593 0.0025  0.0073  0.0139  17  VAL   C CB  
1160 C CG1 . VAL   B 11  ? 0.1403 0.1380 0.1806 0.0030  0.0070  0.0119  17  VAL   C CG1 
1161 C CG2 . VAL   B 11  ? 0.1371 0.1311 0.1767 0.0030  0.0105  0.0126  17  VAL   C CG2 
1162 N N   . VAL   B 12  ? 0.1036 0.1078 0.1590 0.0015  0.0038  0.0198  18  VAL   C N   
1163 C CA  A VAL   B 12  ? 0.0973 0.1035 0.1521 0.0014  0.0010  0.0218  18  VAL   C CA  
1164 C CA  B VAL   B 12  ? 0.1169 0.1231 0.1717 0.0013  0.0010  0.0219  18  VAL   C CA  
1165 C C   . VAL   B 12  ? 0.1061 0.1126 0.1612 0.0020  0.0022  0.0210  18  VAL   C C   
1166 O O   . VAL   B 12  ? 0.1223 0.1278 0.1800 0.0023  0.0049  0.0190  18  VAL   C O   
1167 C CB  A VAL   B 12  ? 0.0990 0.1077 0.1609 0.0009  -0.0003 0.0258  18  VAL   C CB  
1168 C CB  B VAL   B 12  ? 0.1558 0.1644 0.2185 0.0009  0.0000  0.0258  18  VAL   C CB  
1169 C CG1 A VAL   B 12  ? 0.1251 0.1343 0.1866 0.0000  -0.0030 0.0270  18  VAL   C CG1 
1170 C CG1 B VAL   B 12  ? 0.1575 0.1679 0.2189 0.0008  -0.0031 0.0285  18  VAL   C CG1 
1171 C CG2 A VAL   B 12  ? 0.0626 0.0718 0.1339 0.0014  0.0028  0.0269  18  VAL   C CG2 
1172 C CG2 B VAL   B 12  ? 0.1918 0.2004 0.2564 0.0001  -0.0010 0.0265  18  VAL   C CG2 
1173 N N   . ASN   B 13  ? 0.0985 0.1062 0.1512 0.0021  0.0005  0.0224  19  ASN   C N   
1174 C CA  . ASN   B 13  ? 0.1031 0.1112 0.1581 0.0026  0.0020  0.0223  19  ASN   C CA  
1175 C C   . ASN   B 13  ? 0.1048 0.1139 0.1690 0.0026  0.0037  0.0247  19  ASN   C C   
1176 O O   . ASN   B 13  ? 0.1000 0.1104 0.1673 0.0025  0.0024  0.0281  19  ASN   C O   
1177 C CB  . ASN   B 13  ? 0.1144 0.1234 0.1656 0.0028  0.0004  0.0243  19  ASN   C CB  
1178 C CG  . ASN   B 13  ? 0.1131 0.1210 0.1560 0.0030  -0.0008 0.0220  19  ASN   C CG  
1179 O OD1 . ASN   B 13  ? 0.1284 0.1356 0.1664 0.0027  -0.0030 0.0225  19  ASN   C OD1 
1180 N ND2 . ASN   B 13  ? 0.1151 0.1228 0.1572 0.0035  0.0005  0.0196  19  ASN   C ND2 
1181 N N   . ARG   B 14  ? 0.1029 0.1111 0.1714 0.0028  0.0065  0.0229  20  ARG   C N   
1182 C CA  . ARG   B 14  ? 0.0912 0.0998 0.1690 0.0030  0.0088  0.0250  20  ARG   C CA  
1183 C C   . ARG   B 14  ? 0.1100 0.1205 0.1907 0.0034  0.0076  0.0298  20  ARG   C C   
1184 O O   . ARG   B 14  ? 0.1191 0.1306 0.2060 0.0036  0.0077  0.0332  20  ARG   C O   
1185 C CB  . ARG   B 14  ? 0.0967 0.1036 0.1781 0.0029  0.0118  0.0219  20  ARG   C CB  
1186 C CG  . ARG   B 14  ? 0.0988 0.1051 0.1899 0.0032  0.0149  0.0233  20  ARG   C CG  
1187 C CD  . ARG   B 14  ? 0.1176 0.1217 0.2115 0.0028  0.0176  0.0195  20  ARG   C CD  
1188 N NE  . ARG   B 14  ? 0.1176 0.1200 0.2204 0.0030  0.0212  0.0198  20  ARG   C NE  
1189 C CZ  . ARG   B 14  ? 0.1200 0.1229 0.2310 0.0034  0.0228  0.0232  20  ARG   C CZ  
1190 N NH1 . ARG   B 14  ? 0.1361 0.1414 0.2470 0.0037  0.0210  0.0271  20  ARG   C NH1 
1191 N NH2 . ARG   B 14  ? 0.1189 0.1197 0.2380 0.0036  0.0265  0.0227  20  ARG   C NH2 
1192 N N   . HIS   B 15  ? 0.1035 0.1144 0.1793 0.0035  0.0066  0.0304  21  HIS   C N   
1193 C CA  . HIS   B 15  ? 0.1117 0.1238 0.1890 0.0041  0.0058  0.0352  21  HIS   C CA  
1194 C C   . HIS   B 15  ? 0.1186 0.1320 0.1924 0.0041  0.0021  0.0385  21  HIS   C C   
1195 O O   . HIS   B 15  ? 0.1487 0.1632 0.2241 0.0047  0.0011  0.0429  21  HIS   C O   
1196 C CB  . HIS   B 15  ? 0.1246 0.1364 0.1982 0.0044  0.0067  0.0352  21  HIS   C CB  
1197 C CG  . HIS   B 15  ? 0.1162 0.1277 0.1797 0.0044  0.0045  0.0338  21  HIS   C CG  
1198 N ND1 . HIS   B 15  ? 0.1236 0.1344 0.1833 0.0040  0.0045  0.0294  21  HIS   C ND1 
1199 C CD2 . HIS   B 15  ? 0.1271 0.1386 0.1839 0.0047  0.0024  0.0365  21  HIS   C CD2 
1200 C CE1 . HIS   B 15  ? 0.1377 0.1481 0.1893 0.0042  0.0028  0.0295  21  HIS   C CE1 
1201 N NE2 . HIS   B 15  ? 0.1414 0.1520 0.1906 0.0046  0.0016  0.0334  21  HIS   C NE2 
1202 N N   . LEU   B 16  ? 0.1184 0.1316 0.1882 0.0034  0.0000  0.0364  22  LEU   C N   
1203 C CA  . LEU   B 16  ? 0.1243 0.1388 0.1920 0.0030  -0.0039 0.0388  22  LEU   C CA  
1204 C C   . LEU   B 16  ? 0.1304 0.1460 0.2058 0.0026  -0.0039 0.0395  22  LEU   C C   
1205 O O   . LEU   B 16  ? 0.1493 0.1661 0.2244 0.0019  -0.0074 0.0410  22  LEU   C O   
1206 C CB  . LEU   B 16  ? 0.1386 0.1519 0.1962 0.0024  -0.0061 0.0363  22  LEU   C CB  
1207 C CG  . LEU   B 16  ? 0.1497 0.1619 0.1997 0.0030  -0.0059 0.0360  22  LEU   C CG  
1208 C CD1 . LEU   B 16  ? 0.1593 0.1698 0.2000 0.0025  -0.0076 0.0332  22  LEU   C CD1 
1209 C CD2 . LEU   B 16  ? 0.1513 0.1642 0.2004 0.0036  -0.0072 0.0406  22  LEU   C CD2 
1210 N N   . ALA   B 17  ? 0.1291 0.1440 0.2115 0.0029  -0.0001 0.0381  23  ALA   C N   
1211 C CA  . ALA   B 17  ? 0.1271 0.1426 0.2171 0.0027  0.0008  0.0386  23  ALA   C CA  
1212 C C   . ALA   B 17  ? 0.1303 0.1487 0.2282 0.0030  -0.0013 0.0438  23  ALA   C C   
1213 O O   . ALA   B 17  ? 0.1437 0.1630 0.2443 0.0039  -0.0014 0.0471  23  ALA   C O   
1214 C CB  . ALA   B 17  ? 0.1389 0.1525 0.2343 0.0031  0.0058  0.0361  23  ALA   C CB  
1215 N N   . THR   B 18  ? 0.1308 0.1508 0.2329 0.0024  -0.0031 0.0449  24  THR   C N   
1216 C CA  . THR   B 18  ? 0.1398 0.1632 0.2507 0.0027  -0.0058 0.0499  24  THR   C CA  
1217 C C   . THR   B 18  ? 0.1434 0.1673 0.2672 0.0037  -0.0014 0.0514  24  THR   C C   
1218 O O   . THR   B 18  ? 0.1469 0.1680 0.2720 0.0039  0.0036  0.0480  24  THR   C O   
1219 C CB  . THR   B 18  ? 0.1583 0.1835 0.2688 0.0013  -0.0101 0.0502  24  THR   C CB  
1220 O OG1 . THR   B 18  ? 0.1630 0.1872 0.2778 0.0009  -0.0068 0.0477  24  THR   C OG1 
1221 C CG2 . THR   B 18  ? 0.1826 0.2066 0.2803 0.0003  -0.0141 0.0482  24  THR   C CG2 
1222 N N   . HIS   B 19  ? 0.1503 0.1775 0.2841 0.0043  -0.0035 0.0566  25  HIS   C N   
1223 C CA  . HIS   B 19  ? 0.1523 0.1801 0.2996 0.0053  0.0008  0.0582  25  HIS   C CA  
1224 C C   . HIS   B 19  ? 0.1296 0.1566 0.2800 0.0046  0.0034  0.0554  25  HIS   C C   
1225 O O   . HIS   B 19  ? 0.1467 0.1711 0.3016 0.0052  0.0093  0.0533  25  HIS   C O   
1226 C CB  . HIS   B 19  ? 0.1677 0.1999 0.3256 0.0062  -0.0029 0.0646  25  HIS   C CB  
1227 C CG  . HIS   B 19  ? 0.1926 0.2260 0.3660 0.0071  0.0011  0.0667  25  HIS   C CG  
1228 N ND1 . HIS   B 19  ? 0.2179 0.2491 0.3982 0.0087  0.0070  0.0669  25  HIS   C ND1 
1229 C CD2 . HIS   B 19  ? 0.2091 0.2451 0.3918 0.0067  0.0005  0.0679  25  HIS   C CD2 
1230 C CE1 . HIS   B 19  ? 0.2033 0.2361 0.3972 0.0094  0.0096  0.0690  25  HIS   C CE1 
1231 N NE2 . HIS   B 19  ? 0.2035 0.2394 0.3995 0.0082  0.0061  0.0695  25  HIS   C NE2 
1232 N N   . ASN   B 20  ? 0.1374 0.1659 0.2846 0.0031  -0.0006 0.0549  26  ASN   C N   
1233 C CA  . ASN   B 20  ? 0.1463 0.1736 0.2962 0.0024  0.0024  0.0524  26  ASN   C CA  
1234 C C   . ASN   B 20  ? 0.1374 0.1598 0.2785 0.0025  0.0074  0.0471  26  ASN   C C   
1235 O O   . ASN   B 20  ? 0.1294 0.1496 0.2745 0.0029  0.0127  0.0454  26  ASN   C O   
1236 C CB  . ASN   B 20  ? 0.1733 0.2027 0.3213 0.0006  -0.0028 0.0526  26  ASN   C CB  
1237 C CG  . ASN   B 20  ? 0.2491 0.2777 0.4026 0.0000  0.0009  0.0511  26  ASN   C CG  
1238 O OD1 . ASN   B 20  ? 0.2739 0.3045 0.4408 0.0005  0.0032  0.0537  26  ASN   C OD1 
1239 N ND2 . ASN   B 20  ? 0.2767 0.3018 0.4203 -0.0009 0.0022  0.0470  26  ASN   C ND2 
1240 N N   . ASP   B 21  ? 0.1276 0.1479 0.2565 0.0023  0.0059  0.0444  27  ASP   C N   
1241 C CA  . ASP   B 21  ? 0.1320 0.1480 0.2529 0.0024  0.0100  0.0395  27  ASP   C CA  
1242 C C   . ASP   B 21  ? 0.1207 0.1345 0.2475 0.0037  0.0157  0.0386  27  ASP   C C   
1243 O O   . ASP   B 21  ? 0.1334 0.1439 0.2591 0.0039  0.0203  0.0354  27  ASP   C O   
1244 C CB  . ASP   B 21  ? 0.1289 0.1440 0.2383 0.0022  0.0073  0.0375  27  ASP   C CB  
1245 C CG  . ASP   B 21  ? 0.1385 0.1539 0.2396 0.0010  0.0031  0.0367  27  ASP   C CG  
1246 O OD1 . ASP   B 21  ? 0.1467 0.1613 0.2475 0.0004  0.0036  0.0355  27  ASP   C OD1 
1247 O OD2 . ASP   B 21  ? 0.1325 0.1487 0.2275 0.0009  -0.0005 0.0374  27  ASP   C OD2 
1248 N N   . TRP   B 22  ? 0.1283 0.1435 0.2610 0.0045  0.0155  0.0415  28  TRP   C N   
1249 C CA  . TRP   B 22  ? 0.1362 0.1489 0.2751 0.0055  0.0209  0.0406  28  TRP   C CA  
1250 C C   . TRP   B 22  ? 0.1314 0.1440 0.2815 0.0063  0.0252  0.0419  28  TRP   C C   
1251 O O   . TRP   B 22  ? 0.1405 0.1493 0.2923 0.0069  0.0309  0.0391  28  TRP   C O   
1252 C CB  . TRP   B 22  ? 0.1303 0.1445 0.2737 0.0063  0.0199  0.0438  28  TRP   C CB  
1253 C CG  . TRP   B 22  ? 0.1273 0.1399 0.2610 0.0059  0.0187  0.0413  28  TRP   C CG  
1254 C CD1 . TRP   B 22  ? 0.1441 0.1586 0.2710 0.0055  0.0141  0.0429  28  TRP   C CD1 
1255 C CD2 . TRP   B 22  ? 0.1168 0.1256 0.2473 0.0058  0.0224  0.0367  28  TRP   C CD2 
1256 N NE1 . TRP   B 22  ? 0.1507 0.1631 0.2714 0.0053  0.0151  0.0399  28  TRP   C NE1 
1257 C CE2 . TRP   B 22  ? 0.1354 0.1446 0.2585 0.0053  0.0197  0.0361  28  TRP   C CE2 
1258 C CE3 . TRP   B 22  ? 0.1430 0.1481 0.2764 0.0060  0.0276  0.0331  28  TRP   C CE3 
1259 C CZ2 . TRP   B 22  ? 0.1379 0.1445 0.2583 0.0050  0.0218  0.0323  28  TRP   C CZ2 
1260 C CZ3 . TRP   B 22  ? 0.1595 0.1615 0.2886 0.0056  0.0293  0.0288  28  TRP   C CZ3 
1261 C CH2 . TRP   B 22  ? 0.1546 0.1578 0.2779 0.0051  0.0262  0.0286  28  TRP   C CH2 
1262 N N   . ALA   B 23  ? 0.1257 0.1423 0.2832 0.0061  0.0225  0.0459  29  ALA   C N   
1263 C CA  . ALA   B 23  ? 0.1392 0.1563 0.3089 0.0068  0.0266  0.0477  29  ALA   C CA  
1264 C C   . ALA   B 23  ? 0.1549 0.1688 0.3201 0.0063  0.0304  0.0439  29  ALA   C C   
1265 O O   . ALA   B 23  ? 0.1601 0.1731 0.3340 0.0070  0.0354  0.0445  29  ALA   C O   
1266 C CB  . ALA   B 23  ? 0.1419 0.1648 0.3216 0.0066  0.0217  0.0534  29  ALA   C CB  
1267 N N   . ASN   B 24  ? 0.1489 0.1610 0.3006 0.0052  0.0282  0.0404  30  ASN   C N   
1268 C CA  . ASN   B 24  ? 0.1416 0.1502 0.2873 0.0049  0.0314  0.0371  30  ASN   C CA  
1269 C C   . ASN   B 24  ? 0.1407 0.1448 0.2723 0.0049  0.0325  0.0319  30  ASN   C C   
1270 O O   . ASN   B 24  ? 0.1378 0.1402 0.2596 0.0043  0.0315  0.0295  30  ASN   C O   
1271 C CB  . ASN   B 24  ? 0.1592 0.1709 0.3039 0.0034  0.0267  0.0387  30  ASN   C CB  
1272 C CG  . ASN   B 24  ? 0.1748 0.1908 0.3347 0.0033  0.0261  0.0434  30  ASN   C CG  
1273 O OD1 . ASN   B 24  ? 0.1864 0.2015 0.3542 0.0038  0.0312  0.0440  30  ASN   C OD1 
1274 N ND2 . ASN   B 24  ? 0.1842 0.2051 0.3486 0.0028  0.0198  0.0471  30  ASN   C ND2 
1275 N N   . LEU   B 25  ? 0.1417 0.1440 0.2729 0.0055  0.0343  0.0303  31  LEU   C N   
1276 C CA  . LEU   B 25  ? 0.1395 0.1385 0.2588 0.0053  0.0340  0.0256  31  LEU   C CA  
1277 C C   . LEU   B 25  ? 0.1603 0.1541 0.2719 0.0057  0.0385  0.0212  31  LEU   C C   
1278 O O   . LEU   B 25  ? 0.1785 0.1694 0.2949 0.0065  0.0441  0.0207  31  LEU   C O   
1279 C CB  . LEU   B 25  ? 0.1452 0.1436 0.2686 0.0058  0.0352  0.0253  31  LEU   C CB  
1280 C CG  . LEU   B 25  ? 0.1488 0.1445 0.2623 0.0054  0.0344  0.0207  31  LEU   C CG  
1281 C CD1 . LEU   B 25  ? 0.1587 0.1573 0.2648 0.0046  0.0285  0.0213  31  LEU   C CD1 
1282 C CD2 . LEU   B 25  ? 0.1656 0.1601 0.2852 0.0057  0.0366  0.0203  31  LEU   C CD2 
1283 N N   . VAL   B 26  ? 0.1479 0.1402 0.2472 0.0052  0.0361  0.0181  32  VAL   C N   
1284 C CA  . VAL   B 26  ? 0.1610 0.1481 0.2508 0.0057  0.0395  0.0137  32  VAL   C CA  
1285 C C   . VAL   B 26  ? 0.1679 0.1527 0.2511 0.0056  0.0387  0.0095  32  VAL   C C   
1286 O O   . VAL   B 26  ? 0.1871 0.1674 0.2677 0.0061  0.0427  0.0059  32  VAL   C O   
1287 C CB  . VAL   B 26  ? 0.1651 0.1518 0.2459 0.0054  0.0373  0.0135  32  VAL   C CB  
1288 C CG1 . VAL   B 26  ? 0.2017 0.1830 0.2705 0.0061  0.0399  0.0091  32  VAL   C CG1 
1289 C CG2 . VAL   B 26  ? 0.1689 0.1573 0.2568 0.0052  0.0386  0.0172  32  VAL   C CG2 
1290 N N   . TRP   B 27  ? 0.1438 0.1317 0.2247 0.0049  0.0336  0.0098  33  TRP   C N   
1291 C CA  . TRP   B 27  ? 0.1496 0.1359 0.2253 0.0046  0.0324  0.0059  33  TRP   C CA  
1292 C C   . TRP   B 27  ? 0.1429 0.1334 0.2208 0.0040  0.0278  0.0079  33  TRP   C C   
1293 O O   . TRP   B 27  ? 0.1418 0.1355 0.2191 0.0038  0.0247  0.0110  33  TRP   C O   
1294 C CB  . TRP   B 27  ? 0.1724 0.1558 0.2354 0.0048  0.0314  0.0020  33  TRP   C CB  
1295 C CG  . TRP   B 27  ? 0.1785 0.1615 0.2358 0.0044  0.0285  -0.0018 33  TRP   C CG  
1296 C CD1 . TRP   B 27  ? 0.2068 0.1867 0.2628 0.0041  0.0300  -0.0061 33  TRP   C CD1 
1297 C CD2 . TRP   B 27  ? 0.1622 0.1483 0.2153 0.0040  0.0236  -0.0016 33  TRP   C CD2 
1298 N NE1 . TRP   B 27  ? 0.2122 0.1934 0.2640 0.0036  0.0259  -0.0085 33  TRP   C NE1 
1299 C CE2 . TRP   B 27  ? 0.1822 0.1671 0.2322 0.0036  0.0222  -0.0057 33  TRP   C CE2 
1300 C CE3 . TRP   B 27  ? 0.1653 0.1546 0.2172 0.0039  0.0203  0.0015  33  TRP   C CE3 
1301 C CZ2 . TRP   B 27  ? 0.1801 0.1675 0.2266 0.0034  0.0180  -0.0064 33  TRP   C CZ2 
1302 C CZ3 . TRP   B 27  ? 0.1861 0.1772 0.2334 0.0038  0.0165  0.0005  33  TRP   C CZ3 
1303 C CH2 . TRP   B 27  ? 0.1856 0.1761 0.2311 0.0035  0.0155  -0.0031 33  TRP   C CH2 
1304 N N   . GLU   B 28  ? 0.1358 0.1263 0.2160 0.0037  0.0276  0.0063  34  GLU   C N   
1305 C CA  . GLU   B 28  ? 0.1379 0.1319 0.2196 0.0032  0.0241  0.0082  34  GLU   C CA  
1306 C C   . GLU   B 28  ? 0.1377 0.1305 0.2180 0.0027  0.0238  0.0043  34  GLU   C C   
1307 O O   . GLU   B 28  ? 0.1465 0.1359 0.2285 0.0025  0.0267  0.0010  34  GLU   C O   
1308 C CB  . GLU   B 28  ? 0.1477 0.1444 0.2393 0.0034  0.0243  0.0132  34  GLU   C CB  
1309 C CG  . GLU   B 28  ? 0.1518 0.1466 0.2527 0.0037  0.0286  0.0133  34  GLU   C CG  
1310 C CD  . GLU   B 28  ? 0.1755 0.1692 0.2799 0.0033  0.0296  0.0115  34  GLU   C CD  
1311 O OE1 . GLU   B 28  ? 0.2069 0.1974 0.3164 0.0034  0.0336  0.0094  34  GLU   C OE1 
1312 O OE2 . GLU   B 28  ? 0.1634 0.1593 0.2662 0.0029  0.0267  0.0121  34  GLU   C OE2 
1313 N N   . ASP   B 29  ? 0.1321 0.1274 0.2099 0.0023  0.0204  0.0046  35  ASP   C N   
1314 C CA  . ASP   B 29  ? 0.1314 0.1262 0.2094 0.0016  0.0197  0.0012  35  ASP   C CA  
1315 C C   . ASP   B 29  ? 0.1266 0.1250 0.2076 0.0015  0.0177  0.0043  35  ASP   C C   
1316 O O   . ASP   B 29  ? 0.1294 0.1298 0.2050 0.0017  0.0149  0.0054  35  ASP   C O   
1317 C CB  . ASP   B 29  ? 0.1517 0.1449 0.2203 0.0016  0.0178  -0.0033 35  ASP   C CB  
1318 C CG  . ASP   B 29  ? 0.2108 0.2038 0.2798 0.0007  0.0165  -0.0073 35  ASP   C CG  
1319 O OD1 . ASP   B 29  ? 0.2196 0.2152 0.2943 0.0002  0.0157  -0.0059 35  ASP   C OD1 
1320 O OD2 . ASP   B 29  ? 0.2333 0.2238 0.2963 0.0006  0.0157  -0.0118 35  ASP   C OD2 
1321 N N   . SER   B 30  ? 0.1236 0.1223 0.2133 0.0012  0.0195  0.0058  36  SER   C N   
1322 C CA  A SER   B 30  ? 0.1245 0.1261 0.2173 0.0011  0.0185  0.0091  36  SER   C CA  
1323 C CA  B SER   B 30  ? 0.1245 0.1261 0.2169 0.0012  0.0184  0.0092  36  SER   C CA  
1324 C C   . SER   B 30  ? 0.1308 0.1335 0.2198 0.0007  0.0163  0.0063  36  SER   C C   
1325 O O   . SER   B 30  ? 0.1295 0.1345 0.2161 0.0010  0.0147  0.0089  36  SER   C O   
1326 C CB  A SER   B 30  ? 0.1476 0.1486 0.2506 0.0010  0.0215  0.0110  36  SER   C CB  
1327 C CB  B SER   B 30  ? 0.1456 0.1468 0.2480 0.0011  0.0212  0.0118  36  SER   C CB  
1328 O OG  A SER   B 30  ? 0.1481 0.1512 0.2538 0.0009  0.0211  0.0137  36  SER   C OG  
1329 O OG  B SER   B 30  ? 0.1506 0.1493 0.2573 0.0002  0.0233  0.0073  36  SER   C OG  
1330 N N   . SER   B 31  ? 0.1334 0.1344 0.2217 -0.0001 0.0161  0.0011  37  SER   C N   
1331 C CA  . SER   B 31  ? 0.1366 0.1393 0.2229 -0.0005 0.0136  -0.0014 37  SER   C CA  
1332 C C   . SER   B 31  ? 0.1298 0.1339 0.2071 0.0003  0.0107  -0.0010 37  SER   C C   
1333 O O   . SER   B 31  ? 0.1393 0.1457 0.2160 0.0004  0.0089  -0.0012 37  SER   C O   
1334 C CB  . SER   B 31  ? 0.1674 0.1682 0.2544 -0.0016 0.0131  -0.0072 37  SER   C CB  
1335 O OG  . SER   B 31  ? 0.2386 0.2371 0.3171 -0.0012 0.0119  -0.0104 37  SER   C OG  
1336 N N   . ARG   B 32  ? 0.1171 0.1199 0.1883 0.0010  0.0105  -0.0002 38  ARG   C N   
1337 C CA  . ARG   B 32  ? 0.1182 0.1217 0.1810 0.0018  0.0080  0.0003  38  ARG   C CA  
1338 C C   . ARG   B 32  ? 0.1115 0.1165 0.1736 0.0023  0.0079  0.0051  38  ARG   C C   
1339 O O   . ARG   B 32  ? 0.1098 0.1153 0.1656 0.0029  0.0061  0.0058  38  ARG   C O   
1340 C CB  . ARG   B 32  ? 0.1406 0.1414 0.1969 0.0022  0.0080  -0.0019 38  ARG   C CB  
1341 C CG  . ARG   B 32  ? 0.1598 0.1587 0.2137 0.0018  0.0074  -0.0069 38  ARG   C CG  
1342 C CD  . ARG   B 32  ? 0.1334 0.1289 0.1796 0.0024  0.0080  -0.0087 38  ARG   C CD  
1343 N NE  . ARG   B 32  ? 0.1289 0.1248 0.1675 0.0034  0.0059  -0.0076 38  ARG   C NE  
1344 C CZ  . ARG   B 32  ? 0.1399 0.1334 0.1701 0.0042  0.0051  -0.0096 38  ARG   C CZ  
1345 N NH1 . ARG   B 32  ? 0.1590 0.1493 0.1863 0.0041  0.0061  -0.0132 38  ARG   C NH1 
1346 N NH2 . ARG   B 32  ? 0.1394 0.1334 0.1638 0.0051  0.0033  -0.0082 38  ARG   C NH2 
1347 N N   . ASP   B 33  ? 0.0999 0.1054 0.1682 0.0022  0.0097  0.0084  39  ASP   C N   
1348 C CA  . ASP   B 33  ? 0.1016 0.1083 0.1688 0.0026  0.0090  0.0128  39  ASP   C CA  
1349 C C   . ASP   B 33  ? 0.1023 0.1079 0.1648 0.0027  0.0081  0.0130  39  ASP   C C   
1350 O O   . ASP   B 33  ? 0.1073 0.1137 0.1657 0.0029  0.0063  0.0151  39  ASP   C O   
1351 C CB  . ASP   B 33  ? 0.1085 0.1168 0.1722 0.0029  0.0076  0.0147  39  ASP   C CB  
1352 C CG  . ASP   B 33  ? 0.1193 0.1283 0.1812 0.0032  0.0066  0.0191  39  ASP   C CG  
1353 O OD1 . ASP   B 33  ? 0.1273 0.1365 0.1944 0.0032  0.0075  0.0219  39  ASP   C OD1 
1354 O OD2 . ASP   B 33  ? 0.1079 0.1171 0.1634 0.0036  0.0049  0.0196  39  ASP   C OD2 
1355 N N   . LEU   B 34  ? 0.1025 0.1061 0.1658 0.0026  0.0097  0.0108  40  LEU   C N   
1356 C CA  . LEU   B 34  ? 0.1104 0.1128 0.1703 0.0028  0.0096  0.0112  40  LEU   C CA  
1357 C C   . LEU   B 34  ? 0.1088 0.1105 0.1753 0.0028  0.0122  0.0127  40  LEU   C C   
1358 O O   . LEU   B 34  ? 0.1205 0.1211 0.1923 0.0027  0.0148  0.0114  40  LEU   C O   
1359 C CB  . LEU   B 34  ? 0.1193 0.1195 0.1723 0.0030  0.0096  0.0074  40  LEU   C CB  
1360 C CG  . LEU   B 34  ? 0.1239 0.1246 0.1697 0.0034  0.0068  0.0062  40  LEU   C CG  
1361 C CD1 . LEU   B 34  ? 0.1401 0.1383 0.1793 0.0039  0.0068  0.0028  40  LEU   C CD1 
1362 C CD2 . LEU   B 34  ? 0.1356 0.1374 0.1786 0.0034  0.0050  0.0091  40  LEU   C CD2 
1363 N N   . LEU   B 35  ? 0.1011 0.1034 0.1679 0.0028  0.0117  0.0151  41  LEU   C N   
1364 C CA  . LEU   B 35  ? 0.1106 0.1123 0.1841 0.0029  0.0143  0.0167  41  LEU   C CA  
1365 C C   . LEU   B 35  ? 0.1091 0.1101 0.1793 0.0028  0.0141  0.0169  41  LEU   C C   
1366 O O   . LEU   B 35  ? 0.1227 0.1248 0.1886 0.0024  0.0110  0.0179  41  LEU   C O   
1367 C CB  . LEU   B 35  ? 0.1083 0.1128 0.1903 0.0029  0.0137  0.0212  41  LEU   C CB  
1368 C CG  . LEU   B 35  ? 0.1051 0.1097 0.1962 0.0032  0.0164  0.0234  41  LEU   C CG  
1369 C CD1 . LEU   B 35  ? 0.1304 0.1364 0.2306 0.0036  0.0172  0.0267  41  LEU   C CD1 
1370 C CD2 . LEU   B 35  ? 0.1073 0.1137 0.1993 0.0028  0.0144  0.0260  41  LEU   C CD2 
1371 N N   . VAL   B 36  ? 0.1157 0.1143 0.1879 0.0031  0.0177  0.0158  42  VAL   C N   
1372 C CA  . VAL   B 36  ? 0.1134 0.1109 0.1841 0.0031  0.0187  0.0163  42  VAL   C CA  
1373 C C   . VAL   B 36  ? 0.1113 0.1096 0.1924 0.0032  0.0215  0.0191  42  VAL   C C   
1374 O O   . VAL   B 36  ? 0.1283 0.1252 0.2146 0.0037  0.0251  0.0185  42  VAL   C O   
1375 C CB  . VAL   B 36  ? 0.1312 0.1245 0.1932 0.0036  0.0210  0.0125  42  VAL   C CB  
1376 C CG1 . VAL   B 36  ? 0.1429 0.1347 0.2038 0.0037  0.0227  0.0135  42  VAL   C CG1 
1377 C CG2 . VAL   B 36  ? 0.1448 0.1379 0.1977 0.0037  0.0177  0.0101  42  VAL   C CG2 
1378 N N   . SER   B 37  ? 0.1184 0.1190 0.2034 0.0026  0.0197  0.0222  43  SER   C N   
1379 C CA  . SER   B 37  ? 0.1189 0.1209 0.2150 0.0026  0.0219  0.0252  43  SER   C CA  
1380 C C   . SER   B 37  ? 0.1234 0.1239 0.2190 0.0023  0.0238  0.0252  43  SER   C C   
1381 O O   . SER   B 37  ? 0.1279 0.1268 0.2146 0.0020  0.0223  0.0236  43  SER   C O   
1382 C CB  . SER   B 37  ? 0.1244 0.1311 0.2281 0.0021  0.0176  0.0294  43  SER   C CB  
1383 O OG  . SER   B 37  ? 0.1384 0.1467 0.2368 0.0010  0.0127  0.0300  43  SER   C OG  
1384 N N   . SER   B 38  ? 0.1310 0.1318 0.2368 0.0026  0.0276  0.0273  44  SER   C N   
1385 C CA  . SER   B 38  ? 0.1490 0.1485 0.2562 0.0023  0.0301  0.0278  44  SER   C CA  
1386 C C   . SER   B 38  ? 0.1686 0.1725 0.2831 0.0009  0.0257  0.0313  44  SER   C C   
1387 O O   . SER   B 38  ? 0.1718 0.1799 0.2936 0.0004  0.0218  0.0340  44  SER   C O   
1388 C CB  . SER   B 38  ? 0.1797 0.1768 0.2941 0.0035  0.0373  0.0280  44  SER   C CB  
1389 O OG  . SER   B 38  ? 0.2240 0.2250 0.3522 0.0036  0.0372  0.0315  44  SER   C OG  
1390 N N   . THR   B 39  ? 0.1641 0.1667 0.2762 0.0001  0.0260  0.0311  45  THR   C N   
1391 C CA  . THR   B 39  ? 0.1686 0.1747 0.2871 -0.0017 0.0215  0.0336  45  THR   C CA  
1392 C C   . THR   B 39  ? 0.1975 0.2032 0.3257 -0.0020 0.0260  0.0353  45  THR   C C   
1393 O O   . THR   B 39  ? 0.1998 0.2012 0.3248 -0.0009 0.0323  0.0340  45  THR   C O   
1394 C CB  . THR   B 39  ? 0.1840 0.1887 0.2911 -0.0027 0.0172  0.0317  45  THR   C CB  
1395 O OG1 . THR   B 39  ? 0.1906 0.1905 0.2902 -0.0021 0.0215  0.0296  45  THR   C OG1 
1396 C CG2 . THR   B 39  ? 0.1931 0.1981 0.2906 -0.0023 0.0133  0.0300  45  THR   C CG2 
1397 N N   . THR   B 40  ? 0.2181 0.2282 0.3575 -0.0035 0.0225  0.0383  46  THR   C N   
1398 C CA  . THR   B 40  ? 0.2372 0.2475 0.3875 -0.0042 0.0263  0.0402  46  THR   C CA  
1399 C C   . THR   B 40  ? 0.2411 0.2481 0.3840 -0.0053 0.0263  0.0386  46  THR   C C   
1400 O O   . THR   B 40  ? 0.2703 0.2736 0.4132 -0.0047 0.0326  0.0384  46  THR   C O   
1401 C CB  . THR   B 40  ? 0.2884 0.3051 0.4551 -0.0055 0.0221  0.0441  46  THR   C CB  
1402 O OG1 . THR   B 40  ? 0.3517 0.3712 0.5146 -0.0073 0.0136  0.0440  46  THR   C OG1 
1403 C CG2 . THR   B 40  ? 0.2767 0.2963 0.4514 -0.0040 0.0229  0.0461  46  THR   C CG2 
1404 N N   . ALA   B 41  ? 0.2126 0.2203 0.3479 -0.0067 0.0196  0.0374  47  ALA   C N   
1405 C CA  . ALA   B 41  ? 0.2162 0.2206 0.3446 -0.0077 0.0194  0.0359  47  ALA   C CA  
1406 C C   . ALA   B 41  ? 0.2036 0.2027 0.3154 -0.0061 0.0214  0.0327  47  ALA   C C   
1407 O O   . ALA   B 41  ? 0.2033 0.2025 0.3081 -0.0050 0.0201  0.0313  47  ALA   C O   
1408 C CB  . ALA   B 41  ? 0.2393 0.2465 0.3684 -0.0101 0.0114  0.0359  47  ALA   C CB  
1409 N N   . GLN   B 42  ? 0.1939 0.1887 0.3003 -0.0061 0.0246  0.0319  48  GLN   C N   
1410 C CA  . GLN   B 42  ? 0.2101 0.2000 0.3011 -0.0045 0.0259  0.0292  48  GLN   C CA  
1411 C C   . GLN   B 42  ? 0.2036 0.1941 0.2863 -0.0053 0.0194  0.0275  48  GLN   C C   
1412 O O   . GLN   B 42  ? 0.2205 0.2128 0.3075 -0.0074 0.0152  0.0281  48  GLN   C O   
1413 C CB  . GLN   B 42  ? 0.2681 0.2530 0.3560 -0.0039 0.0317  0.0295  48  GLN   C CB  
1414 C CG  . GLN   B 42  ? 0.3760 0.3586 0.4666 -0.0021 0.0393  0.0303  48  GLN   C CG  
1415 C CD  . GLN   B 42  ? 0.5053 0.4821 0.5909 -0.0012 0.0452  0.0308  48  GLN   C CD  
1416 O OE1 . GLN   B 42  ? 0.5569 0.5335 0.6503 -0.0026 0.0467  0.0329  48  GLN   C OE1 
1417 N NE2 . GLN   B 42  ? 0.5379 0.5099 0.6105 0.0011  0.0487  0.0292  48  GLN   C NE2 
1418 N N   . GLY   B 43  ? 0.1790 0.1679 0.2506 -0.0038 0.0187  0.0254  49  GLY   C N   
1419 C CA  . GLY   B 43  ? 0.1783 0.1671 0.2412 -0.0040 0.0137  0.0236  49  GLY   C CA  
1420 C C   . GLY   B 43  ? 0.1792 0.1632 0.2326 -0.0032 0.0154  0.0224  49  GLY   C C   
1421 O O   . GLY   B 43  ? 0.2193 0.1999 0.2709 -0.0020 0.0205  0.0227  49  GLY   C O   
1422 N N   . CYS   B 44  ? 0.1605 0.1439 0.2076 -0.0035 0.0115  0.0210  50  CYS   C N   
1423 C CA  . CYS   B 44  ? 0.1746 0.1536 0.2140 -0.0027 0.0128  0.0202  50  CYS   C CA  
1424 C C   . CYS   B 44  ? 0.1938 0.1714 0.2224 -0.0009 0.0112  0.0183  50  CYS   C C   
1425 O O   . CYS   B 44  ? 0.2249 0.1990 0.2472 -0.0001 0.0117  0.0178  50  CYS   C O   
1426 C CB  . CYS   B 44  ? 0.1801 0.1584 0.2232 -0.0049 0.0104  0.0206  50  CYS   C CB  
1427 S SG  . CYS   B 44  ? 0.2311 0.2113 0.2889 -0.0073 0.0118  0.0231  50  CYS   C SG  
1428 N N   . ASP   B 45  ? 0.1605 0.1409 0.1875 -0.0003 0.0094  0.0173  51  ASP   C N   
1429 C CA  . ASP   B 45  ? 0.1587 0.1385 0.1770 0.0014  0.0080  0.0155  51  ASP   C CA  
1430 C C   . ASP   B 45  ? 0.1735 0.1505 0.1862 0.0035  0.0114  0.0149  51  ASP   C C   
1431 O O   . ASP   B 45  ? 0.2018 0.1784 0.2172 0.0037  0.0148  0.0155  51  ASP   C O   
1432 C CB  . ASP   B 45  ? 0.1720 0.1557 0.1916 0.0012  0.0053  0.0148  51  ASP   C CB  
1433 C CG  . ASP   B 45  ? 0.1942 0.1802 0.2166 -0.0004 0.0015  0.0153  51  ASP   C CG  
1434 O OD1 . ASP   B 45  ? 0.2078 0.1919 0.2278 -0.0011 0.0000  0.0150  51  ASP   C OD1 
1435 O OD2 . ASP   B 45  ? 0.1658 0.1550 0.1923 -0.0010 0.0000  0.0159  51  ASP   C OD2 
1436 N N   . THR   B 46  ? 0.1604 0.1354 0.1650 0.0051  0.0106  0.0139  52  THR   C N   
1437 C CA  . THR   B 46  ? 0.1653 0.1379 0.1630 0.0072  0.0127  0.0131  52  THR   C CA  
1438 C C   . THR   B 46  ? 0.1709 0.1462 0.1658 0.0081  0.0099  0.0111  52  THR   C C   
1439 O O   . THR   B 46  ? 0.1744 0.1513 0.1687 0.0080  0.0069  0.0106  52  THR   C O   
1440 C CB  . THR   B 46  ? 0.1986 0.1672 0.1897 0.0086  0.0134  0.0138  52  THR   C CB  
1441 O OG1 . THR   B 46  ? 0.2301 0.1960 0.2246 0.0077  0.0163  0.0158  52  THR   C OG1 
1442 C CG2 . THR   B 46  ? 0.2282 0.1943 0.2105 0.0112  0.0144  0.0131  52  THR   C CG2 
1443 N N   . ILE   B 47  ? 0.1649 0.1403 0.1582 0.0089  0.0112  0.0099  53  ILE   C N   
1444 C CA  . ILE   B 47  ? 0.1600 0.1377 0.1514 0.0095  0.0086  0.0078  53  ILE   C CA  
1445 C C   . ILE   B 47  ? 0.1501 0.1258 0.1331 0.0116  0.0074  0.0069  53  ILE   C C   
1446 O O   . ILE   B 47  ? 0.1701 0.1421 0.1472 0.0129  0.0095  0.0073  53  ILE   C O   
1447 C CB  . ILE   B 47  ? 0.1657 0.1438 0.1590 0.0094  0.0104  0.0064  53  ILE   C CB  
1448 C CG1 . ILE   B 47  ? 0.1731 0.1529 0.1752 0.0077  0.0122  0.0077  53  ILE   C CG1 
1449 C CG2 . ILE   B 47  ? 0.1798 0.1604 0.1724 0.0097  0.0076  0.0040  53  ILE   C CG2 
1450 C CD1 . ILE   B 47  ? 0.1947 0.1786 0.2027 0.0064  0.0090  0.0086  53  ILE   C CD1 
1451 N N   . ALA   B 48  ? 0.1440 0.1221 0.1265 0.0121  0.0041  0.0060  54  ALA   C N   
1452 C CA  . ALA   B 48  ? 0.1493 0.1264 0.1252 0.0142  0.0023  0.0054  54  ALA   C CA  
1453 C C   . ALA   B 48  ? 0.1483 0.1249 0.1202 0.0150  0.0021  0.0033  54  ALA   C C   
1454 O O   . ALA   B 48  ? 0.1513 0.1300 0.1273 0.0138  0.0020  0.0016  54  ALA   C O   
1455 C CB  . ALA   B 48  ? 0.1452 0.1256 0.1235 0.0144  -0.0009 0.0048  54  ALA   C CB  
1456 N N   . ARG   B 49  ? 0.1462 0.1198 0.1099 0.0170  0.0018  0.0034  55  ARG   C N   
1457 C CA  . ARG   B 49  ? 0.1498 0.1224 0.1079 0.0179  0.0009  0.0011  55  ARG   C CA  
1458 C C   . ARG   B 49  ? 0.1621 0.1355 0.1155 0.0199  -0.0032 0.0009  55  ARG   C C   
1459 O O   . ARG   B 49  ? 0.1848 0.1549 0.1313 0.0218  -0.0029 0.0028  55  ARG   C O   
1460 C CB  . ARG   B 49  ? 0.1637 0.1311 0.1151 0.0185  0.0049  0.0015  55  ARG   C CB  
1461 C CG  . ARG   B 49  ? 0.1524 0.1193 0.1103 0.0166  0.0092  0.0022  55  ARG   C CG  
1462 C CD  . ARG   B 49  ? 0.1716 0.1415 0.1357 0.0150  0.0089  -0.0003 55  ARG   C CD  
1463 N NE  . ARG   B 49  ? 0.1701 0.1394 0.1407 0.0136  0.0130  0.0008  55  ARG   C NE  
1464 C CZ  . ARG   B 49  ? 0.1686 0.1408 0.1475 0.0120  0.0132  0.0000  55  ARG   C CZ  
1465 N NH1 . ARG   B 49  ? 0.1710 0.1463 0.1521 0.0116  0.0101  -0.0022 55  ARG   C NH1 
1466 N NH2 . ARG   B 49  ? 0.1794 0.1515 0.1649 0.0110  0.0167  0.0016  55  ARG   C NH2 
1467 N N   . CYS   B 50  ? 0.1592 0.1371 0.1174 0.0195  -0.0068 -0.0009 56  CYS   C N   
1468 C CA  . CYS   B 50  ? 0.1426 0.1226 0.0999 0.0212  -0.0108 -0.0006 56  CYS   C CA  
1469 C C   . CYS   B 50  ? 0.1460 0.1312 0.1104 0.0203  -0.0140 -0.0030 56  CYS   C C   
1470 O O   . CYS   B 50  ? 0.1557 0.1424 0.1254 0.0183  -0.0129 -0.0046 56  CYS   C O   
1471 C CB  . CYS   B 50  ? 0.1427 0.1226 0.1026 0.0217  -0.0098 0.0022  56  CYS   C CB  
1472 S SG  . CYS   B 50  ? 0.1510 0.1345 0.1212 0.0193  -0.0088 0.0022  56  CYS   C SG  
1473 N N   . ASP   B 51  ? 0.1617 0.1496 0.1270 0.0218  -0.0178 -0.0028 57  ASP   C N   
1474 C CA  . ASP   B 51  ? 0.1656 0.1587 0.1391 0.0211  -0.0206 -0.0045 57  ASP   C CA  
1475 C C   . ASP   B 51  ? 0.1695 0.1650 0.1486 0.0220  -0.0206 -0.0024 57  ASP   C C   
1476 O O   . ASP   B 51  ? 0.1755 0.1751 0.1603 0.0225  -0.0233 -0.0030 57  ASP   C O   
1477 C CB  . ASP   B 51  ? 0.1984 0.1933 0.1699 0.0220  -0.0254 -0.0069 57  ASP   C CB  
1478 C CG  . ASP   B 51  ? 0.2597 0.2540 0.2256 0.0248  -0.0284 -0.0051 57  ASP   C CG  
1479 O OD1 . ASP   B 51  ? 0.2483 0.2402 0.2116 0.0262  -0.0263 -0.0021 57  ASP   C OD1 
1480 O OD2 . ASP   B 51  ? 0.3426 0.3389 0.3073 0.0257  -0.0332 -0.0068 57  ASP   C OD2 
1481 N N   . CYS   B 52  ? 0.1533 0.1463 0.1315 0.0219  -0.0173 -0.0001 58  CYS   C N   
1482 C CA  . CYS   B 52  ? 0.1438 0.1382 0.1265 0.0226  -0.0167 0.0015  58  CYS   C CA  
1483 C C   . CYS   B 52  ? 0.1333 0.1320 0.1245 0.0212  -0.0169 0.0004  58  CYS   C C   
1484 O O   . CYS   B 52  ? 0.1376 0.1375 0.1318 0.0192  -0.0160 -0.0010 58  CYS   C O   
1485 C CB  . CYS   B 52  ? 0.1498 0.1405 0.1304 0.0219  -0.0133 0.0033  58  CYS   C CB  
1486 S SG  . CYS   B 52  ? 0.1610 0.1462 0.1332 0.0238  -0.0122 0.0055  58  CYS   C SG  
1487 N N   . GLN   B 53  ? 0.1286 0.1297 0.1242 0.0225  -0.0175 0.0011  59  GLN   C N   
1488 C CA  . GLN   B 53  ? 0.1324 0.1370 0.1361 0.0217  -0.0166 0.0008  59  GLN   C CA  
1489 C C   . GLN   B 53  ? 0.1401 0.1433 0.1443 0.0223  -0.0139 0.0025  59  GLN   C C   
1490 O O   . GLN   B 53  ? 0.1382 0.1439 0.1483 0.0223  -0.0128 0.0026  59  GLN   C O   
1491 C CB  . GLN   B 53  ? 0.1400 0.1495 0.1505 0.0225  -0.0197 -0.0003 59  GLN   C CB  
1492 C CG  . GLN   B 53  ? 0.1948 0.2061 0.2065 0.0211  -0.0223 -0.0029 59  GLN   C CG  
1493 C CD  . GLN   B 53  ? 0.2188 0.2353 0.2389 0.0213  -0.0255 -0.0042 59  GLN   C CD  
1494 O OE1 . GLN   B 53  ? 0.2250 0.2426 0.2434 0.0223  -0.0297 -0.0054 59  GLN   C OE1 
1495 N NE2 . GLN   B 53  ? 0.1846 0.2042 0.2137 0.0205  -0.0236 -0.0040 59  GLN   C NE2 
1496 N N   . THR   B 54  ? 0.1418 0.1405 0.1397 0.0229  -0.0125 0.0038  60  THR   C N   
1497 C CA  . THR   B 54  ? 0.1503 0.1467 0.1477 0.0230  -0.0099 0.0048  60  THR   C CA  
1498 C C   . THR   B 54  ? 0.1492 0.1416 0.1415 0.0213  -0.0082 0.0052  60  THR   C C   
1499 O O   . THR   B 54  ? 0.1569 0.1473 0.1453 0.0211  -0.0087 0.0053  60  THR   C O   
1500 C CB  . THR   B 54  ? 0.1838 0.1788 0.1805 0.0256  -0.0098 0.0060  60  THR   C CB  
1501 O OG1 . THR   B 54  ? 0.2259 0.2176 0.2168 0.0266  -0.0107 0.0068  60  THR   C OG1 
1502 C CG2 . THR   B 54  ? 0.1833 0.1827 0.1862 0.0275  -0.0117 0.0059  60  THR   C CG2 
1503 N N   . GLY   B 55  ? 0.1229 0.1141 0.1155 0.0201  -0.0062 0.0053  61  GLY   C N   
1504 C CA  . GLY   B 55  ? 0.1325 0.1204 0.1215 0.0182  -0.0052 0.0056  61  GLY   C CA  
1505 C C   . GLY   B 55  ? 0.1238 0.1106 0.1125 0.0172  -0.0037 0.0056  61  GLY   C C   
1506 O O   . GLY   B 55  ? 0.1392 0.1262 0.1288 0.0185  -0.0027 0.0055  61  GLY   C O   
1507 N N   . VAL   B 56  ? 0.1197 0.1048 0.1068 0.0151  -0.0035 0.0058  62  VAL   C N   
1508 C CA  . VAL   B 56  ? 0.1164 0.0999 0.1017 0.0140  -0.0027 0.0056  62  VAL   C CA  
1509 C C   . VAL   B 56  ? 0.1148 0.1003 0.1020 0.0119  -0.0034 0.0061  62  VAL   C C   
1510 O O   . VAL   B 56  ? 0.1307 0.1165 0.1191 0.0109  -0.0041 0.0065  62  VAL   C O   
1511 C CB  . VAL   B 56  ? 0.1302 0.1087 0.1113 0.0135  -0.0025 0.0054  62  VAL   C CB  
1512 C CG1 . VAL   B 56  ? 0.1534 0.1298 0.1316 0.0118  -0.0024 0.0049  62  VAL   C CG1 
1513 C CG2 . VAL   B 56  ? 0.1504 0.1265 0.1300 0.0159  -0.0014 0.0052  62  VAL   C CG2 
1514 N N   . TYR   B 57  ? 0.1150 0.1017 0.1024 0.0114  -0.0030 0.0064  63  TYR   C N   
1515 C CA  . TYR   B 57  ? 0.1019 0.0903 0.0912 0.0096  -0.0037 0.0074  63  TYR   C CA  
1516 C C   . TYR   B 57  ? 0.1173 0.1035 0.1024 0.0084  -0.0041 0.0076  63  TYR   C C   
1517 O O   . TYR   B 57  ? 0.1354 0.1191 0.1162 0.0092  -0.0031 0.0070  63  TYR   C O   
1518 C CB  . TYR   B 57  ? 0.1135 0.1060 0.1079 0.0099  -0.0031 0.0080  63  TYR   C CB  
1519 C CG  . TYR   B 57  ? 0.1117 0.1047 0.1056 0.0105  -0.0015 0.0085  63  TYR   C CG  
1520 C CD1 . TYR   B 57  ? 0.1338 0.1266 0.1275 0.0123  0.0001  0.0079  63  TYR   C CD1 
1521 C CD2 . TYR   B 57  ? 0.1205 0.1141 0.1142 0.0095  -0.0014 0.0100  63  TYR   C CD2 
1522 C CE1 . TYR   B 57  ? 0.1407 0.1337 0.1341 0.0130  0.0023  0.0086  63  TYR   C CE1 
1523 C CE2 . TYR   B 57  ? 0.1318 0.1254 0.1243 0.0102  0.0007  0.0109  63  TYR   C CE2 
1524 C CZ  . TYR   B 57  ? 0.1484 0.1416 0.1408 0.0119  0.0028  0.0101  63  TYR   C CZ  
1525 O OH  . TYR   B 57  ? 0.1649 0.1580 0.1566 0.0128  0.0056  0.0111  63  TYR   C OH  
1526 N N   . TYR   B 58  ? 0.1193 0.1063 0.1056 0.0066  -0.0057 0.0087  64  TYR   C N   
1527 C CA  . TYR   B 58  ? 0.1280 0.1134 0.1102 0.0053  -0.0070 0.0091  64  TYR   C CA  
1528 C C   . TYR   B 58  ? 0.1230 0.1106 0.1056 0.0056  -0.0065 0.0107  64  TYR   C C   
1529 O O   . TYR   B 58  ? 0.1235 0.1144 0.1116 0.0053  -0.0065 0.0122  64  TYR   C O   
1530 C CB  . TYR   B 58  ? 0.1361 0.1214 0.1201 0.0032  -0.0095 0.0097  64  TYR   C CB  
1531 C CG  . TYR   B 58  ? 0.1495 0.1329 0.1286 0.0018  -0.0118 0.0098  64  TYR   C CG  
1532 C CD1 . TYR   B 58  ? 0.1628 0.1419 0.1348 0.0018  -0.0118 0.0080  64  TYR   C CD1 
1533 C CD2 . TYR   B 58  ? 0.1487 0.1345 0.1300 0.0006  -0.0139 0.0118  64  TYR   C CD2 
1534 C CE1 . TYR   B 58  ? 0.1832 0.1601 0.1493 0.0006  -0.0141 0.0077  64  TYR   C CE1 
1535 C CE2 . TYR   B 58  ? 0.1651 0.1493 0.1411 -0.0006 -0.0167 0.0120  64  TYR   C CE2 
1536 C CZ  . TYR   B 58  ? 0.1788 0.1584 0.1468 -0.0007 -0.0169 0.0097  64  TYR   C CZ  
1537 O OH  . TYR   B 58  ? 0.2257 0.2030 0.1869 -0.0019 -0.0198 0.0094  64  TYR   C OH  
1538 N N   . CYS   B 59  ? 0.1273 0.1123 0.1036 0.0060  -0.0057 0.0104  65  CYS   C N   
1539 C CA  . CYS   B 59  ? 0.1340 0.1201 0.1089 0.0065  -0.0047 0.0122  65  CYS   C CA  
1540 C C   . CYS   B 59  ? 0.1510 0.1348 0.1193 0.0051  -0.0073 0.0129  65  CYS   C C   
1541 O O   . CYS   B 59  ? 0.1632 0.1429 0.1235 0.0051  -0.0073 0.0114  65  CYS   C O   
1542 C CB  . CYS   B 59  ? 0.1397 0.1246 0.1122 0.0084  -0.0011 0.0116  65  CYS   C CB  
1543 S SG  . CYS   B 59  ? 0.1685 0.1537 0.1385 0.0092  0.0013  0.0140  65  CYS   C SG  
1544 N N   . SER   B 60  ? 0.1610 0.1475 0.1328 0.0039  -0.0097 0.0151  66  SER   C N   
1545 C CA  A SER   B 60  ? 0.1768 0.1617 0.1430 0.0024  -0.0132 0.0158  66  SER   C CA  
1546 C CA  B SER   B 60  ? 0.1666 0.1516 0.1330 0.0025  -0.0131 0.0159  66  SER   C CA  
1547 C C   . SER   B 60  ? 0.1771 0.1593 0.1342 0.0033  -0.0121 0.0166  66  SER   C C   
1548 O O   . SER   B 60  ? 0.2026 0.1814 0.1514 0.0024  -0.0146 0.0155  66  SER   C O   
1549 C CB  A SER   B 60  ? 0.2108 0.1994 0.1838 0.0012  -0.0160 0.0184  66  SER   C CB  
1550 C CB  B SER   B 60  ? 0.1707 0.1595 0.1438 0.0014  -0.0157 0.0187  66  SER   C CB  
1551 O OG  A SER   B 60  ? 0.2489 0.2405 0.2266 0.0023  -0.0140 0.0211  66  SER   C OG  
1552 O OG  B SER   B 60  ? 0.1629 0.1505 0.1309 0.0000  -0.0198 0.0195  66  SER   C OG  
1553 N N   . SER   B 61  ? 0.1631 0.1466 0.1216 0.0050  -0.0084 0.0182  67  SER   C N   
1554 C CA  . SER   B 61  ? 0.1784 0.1589 0.1278 0.0061  -0.0065 0.0193  67  SER   C CA  
1555 C C   . SER   B 61  ? 0.2017 0.1772 0.1424 0.0070  -0.0042 0.0163  67  SER   C C   
1556 O O   . SER   B 61  ? 0.2330 0.2047 0.1640 0.0077  -0.0027 0.0166  67  SER   C O   
1557 C CB  . SER   B 61  ? 0.1927 0.1758 0.1470 0.0077  -0.0026 0.0221  67  SER   C CB  
1558 O OG  . SER   B 61  ? 0.1937 0.1782 0.1541 0.0089  0.0012  0.0207  67  SER   C OG  
1559 N N   . ARG   B 62  ? 0.1830 0.1577 0.1266 0.0069  -0.0037 0.0134  68  ARG   C N   
1560 C CA  . ARG   B 62  ? 0.1921 0.1616 0.1282 0.0077  -0.0017 0.0104  68  ARG   C CA  
1561 C C   . ARG   B 62  ? 0.1921 0.1588 0.1256 0.0058  -0.0054 0.0076  68  ARG   C C   
1562 O O   . ARG   B 62  ? 0.2156 0.1775 0.1436 0.0062  -0.0040 0.0048  68  ARG   C O   
1563 C CB  . ARG   B 62  ? 0.1995 0.1700 0.1414 0.0097  0.0026  0.0096  68  ARG   C CB  
1564 C CG  . ARG   B 62  ? 0.2499 0.2232 0.1958 0.0114  0.0067  0.0120  68  ARG   C CG  
1565 C CD  . ARG   B 62  ? 0.2518 0.2206 0.1882 0.0128  0.0103  0.0121  68  ARG   C CD  
1566 N NE  . ARG   B 62  ? 0.2886 0.2598 0.2293 0.0144  0.0148  0.0147  68  ARG   C NE  
1567 C CZ  . ARG   B 62  ? 0.3374 0.3099 0.2772 0.0143  0.0151  0.0179  68  ARG   C CZ  
1568 N NH1 . ARG   B 62  ? 0.3673 0.3392 0.3018 0.0127  0.0107  0.0190  68  ARG   C NH1 
1569 N NH2 . ARG   B 62  ? 0.3385 0.3126 0.2826 0.0158  0.0199  0.0203  68  ARG   C NH2 
1570 N N   . ARG   B 63  ? 0.2005 0.1699 0.1391 0.0039  -0.0097 0.0084  69  ARG   C N   
1571 C CA  . ARG   B 63  ? 0.2136 0.1811 0.1526 0.0019  -0.0129 0.0061  69  ARG   C CA  
1572 C C   . ARG   B 63  ? 0.2242 0.1896 0.1653 0.0029  -0.0101 0.0038  69  ARG   C C   
1573 O O   . ARG   B 63  ? 0.2483 0.2089 0.1846 0.0023  -0.0105 0.0010  69  ARG   C O   
1574 C CB  . ARG   B 63  ? 0.2229 0.1857 0.1517 0.0003  -0.0161 0.0043  69  ARG   C CB  
1575 C CG  . ARG   B 63  ? 0.2561 0.2208 0.1827 -0.0010 -0.0202 0.0066  69  ARG   C CG  
1576 C CD  . ARG   B 63  ? 0.3198 0.2894 0.2564 -0.0027 -0.0240 0.0084  69  ARG   C CD  
1577 N NE  . ARG   B 63  ? 0.3705 0.3410 0.3040 -0.0042 -0.0291 0.0100  69  ARG   C NE  
1578 C CZ  . ARG   B 63  ? 0.3741 0.3484 0.3098 -0.0035 -0.0298 0.0139  69  ARG   C CZ  
1579 N NH1 . ARG   B 63  ? 0.3467 0.3239 0.2877 -0.0016 -0.0255 0.0161  69  ARG   C NH1 
1580 N NH2 . ARG   B 63  ? 0.3843 0.3595 0.3174 -0.0049 -0.0350 0.0156  69  ARG   C NH2 
1581 N N   . LYS   B 64  ? 0.1998 0.1685 0.1477 0.0047  -0.0071 0.0048  70  LYS   C N   
1582 C CA  . LYS   B 64  ? 0.2106 0.1777 0.1603 0.0062  -0.0045 0.0032  70  LYS   C CA  
1583 C C   . LYS   B 64  ? 0.1763 0.1477 0.1350 0.0068  -0.0042 0.0044  70  LYS   C C   
1584 O O   . LYS   B 64  ? 0.1749 0.1508 0.1386 0.0070  -0.0042 0.0063  70  LYS   C O   
1585 C CB  . LYS   B 64  ? 0.2613 0.2268 0.2076 0.0086  -0.0002 0.0030  70  LYS   C CB  
1586 C CG  . LYS   B 64  ? 0.4066 0.3654 0.3428 0.0086  0.0008  0.0005  70  LYS   C CG  
1587 C CD  . LYS   B 64  ? 0.5170 0.4740 0.4513 0.0114  0.0060  0.0001  70  LYS   C CD  
1588 C CE  . LYS   B 64  ? 0.5924 0.5421 0.5158 0.0114  0.0076  -0.0025 70  LYS   C CE  
1589 N NZ  . LYS   B 64  ? 0.6534 0.6013 0.5680 0.0099  0.0054  -0.0022 70  LYS   C NZ  
1590 N N   . HIS   B 65  ? 0.1651 0.1349 0.1254 0.0074  -0.0037 0.0032  71  HIS   C N   
1591 C CA  . HIS   B 65  ? 0.1659 0.1389 0.1330 0.0084  -0.0031 0.0039  71  HIS   C CA  
1592 C C   . HIS   B 65  ? 0.1867 0.1596 0.1544 0.0111  -0.0001 0.0036  71  HIS   C C   
1593 O O   . HIS   B 65  ? 0.2292 0.1980 0.1930 0.0121  0.0015  0.0022  71  HIS   C O   
1594 C CB  . HIS   B 65  ? 0.1636 0.1346 0.1319 0.0076  -0.0042 0.0034  71  HIS   C CB  
1595 C CG  . HIS   B 65  ? 0.1496 0.1212 0.1195 0.0050  -0.0069 0.0039  71  HIS   C CG  
1596 N ND1 . HIS   B 65  ? 0.1874 0.1627 0.1633 0.0045  -0.0076 0.0054  71  HIS   C ND1 
1597 C CD2 . HIS   B 65  ? 0.1630 0.1322 0.1297 0.0029  -0.0091 0.0031  71  HIS   C CD2 
1598 C CE1 . HIS   B 65  ? 0.1630 0.1380 0.1399 0.0022  -0.0099 0.0057  71  HIS   C CE1 
1599 N NE2 . HIS   B 65  ? 0.1889 0.1605 0.1607 0.0011  -0.0112 0.0044  71  HIS   C NE2 
1600 N N   . TYR   B 66  ? 0.1465 0.1239 0.1197 0.0122  0.0006  0.0047  72  TYR   C N   
1601 C CA  . TYR   B 66  ? 0.1480 0.1263 0.1236 0.0147  0.0031  0.0046  72  TYR   C CA  
1602 C C   . TYR   B 66  ? 0.1341 0.1149 0.1148 0.0159  0.0023  0.0048  72  TYR   C C   
1603 O O   . TYR   B 66  ? 0.1358 0.1198 0.1201 0.0151  0.0006  0.0054  72  TYR   C O   
1604 C CB  . TYR   B 66  ? 0.1611 0.1429 0.1398 0.0151  0.0046  0.0057  72  TYR   C CB  
1605 C CG  . TYR   B 66  ? 0.1696 0.1488 0.1424 0.0147  0.0063  0.0059  72  TYR   C CG  
1606 C CD1 . TYR   B 66  ? 0.2062 0.1820 0.1750 0.0163  0.0094  0.0051  72  TYR   C CD1 
1607 C CD2 . TYR   B 66  ? 0.1792 0.1597 0.1508 0.0131  0.0050  0.0072  72  TYR   C CD2 
1608 C CE1 . TYR   B 66  ? 0.2227 0.1956 0.1848 0.0161  0.0113  0.0053  72  TYR   C CE1 
1609 C CE2 . TYR   B 66  ? 0.2005 0.1783 0.1655 0.0129  0.0064  0.0077  72  TYR   C CE2 
1610 C CZ  . TYR   B 66  ? 0.2269 0.2009 0.1867 0.0145  0.0096  0.0066  72  TYR   C CZ  
1611 O OH  . TYR   B 66  ? 0.2453 0.2163 0.1973 0.0144  0.0111  0.0072  72  TYR   C OH  
1612 N N   . PRO   B 67  ? 0.1384 0.1176 0.1193 0.0180  0.0034  0.0044  73  PRO   C N   
1613 C CA  . PRO   B 67  ? 0.1413 0.1233 0.1268 0.0195  0.0022  0.0049  73  PRO   C CA  
1614 C C   . PRO   B 67  ? 0.1505 0.1377 0.1425 0.0203  0.0025  0.0053  73  PRO   C C   
1615 O O   . PRO   B 67  ? 0.1768 0.1644 0.1702 0.0212  0.0049  0.0054  73  PRO   C O   
1616 C CB  . PRO   B 67  ? 0.1707 0.1493 0.1548 0.0216  0.0035  0.0047  73  PRO   C CB  
1617 C CG  . PRO   B 67  ? 0.2031 0.1780 0.1834 0.0217  0.0062  0.0038  73  PRO   C CG  
1618 C CD  . PRO   B 67  ? 0.1523 0.1269 0.1291 0.0192  0.0058  0.0035  73  PRO   C CD  
1619 N N   . VAL   B 68  ? 0.1246 0.1155 0.1205 0.0200  0.0003  0.0055  74  VAL   C N   
1620 C CA  . VAL   B 68  ? 0.1265 0.1223 0.1293 0.0204  0.0002  0.0056  74  VAL   C CA  
1621 C C   . VAL   B 68  ? 0.1276 0.1262 0.1337 0.0213  -0.0026 0.0052  74  VAL   C C   
1622 O O   . VAL   B 68  ? 0.1313 0.1282 0.1338 0.0210  -0.0043 0.0050  74  VAL   C O   
1623 C CB  . VAL   B 68  ? 0.1473 0.1451 0.1518 0.0182  0.0003  0.0058  74  VAL   C CB  
1624 C CG1 . VAL   B 68  ? 0.1891 0.1850 0.1910 0.0177  0.0030  0.0065  74  VAL   C CG1 
1625 C CG2 . VAL   B 68  ? 0.1632 0.1600 0.1651 0.0165  -0.0017 0.0056  74  VAL   C CG2 
1626 N N   . SER   B 69  ? 0.1293 0.1321 0.1425 0.0222  -0.0030 0.0051  75  SER   C N   
1627 C CA  . SER   B 69  ? 0.1257 0.1323 0.1433 0.0225  -0.0062 0.0043  75  SER   C CA  
1628 C C   . SER   B 69  ? 0.1138 0.1230 0.1353 0.0203  -0.0063 0.0036  75  SER   C C   
1629 O O   . SER   B 69  ? 0.1202 0.1301 0.1445 0.0194  -0.0038 0.0041  75  SER   C O   
1630 C CB  . SER   B 69  ? 0.1454 0.1556 0.1702 0.0245  -0.0067 0.0045  75  SER   C CB  
1631 O OG  . SER   B 69  ? 0.1934 0.2012 0.2155 0.0268  -0.0064 0.0054  75  SER   C OG  
1632 N N   . PHE   B 70  ? 0.1097 0.1194 0.1303 0.0193  -0.0088 0.0024  76  PHE   C N   
1633 C CA  . PHE   B 70  ? 0.1055 0.1170 0.1298 0.0172  -0.0087 0.0016  76  PHE   C CA  
1634 C C   . PHE   B 70  ? 0.1136 0.1280 0.1416 0.0170  -0.0120 -0.0005 76  PHE   C C   
1635 O O   . PHE   B 70  ? 0.1175 0.1313 0.1419 0.0183  -0.0147 -0.0011 76  PHE   C O   
1636 C CB  . PHE   B 70  ? 0.1210 0.1294 0.1401 0.0156  -0.0075 0.0020  76  PHE   C CB  
1637 C CG  . PHE   B 70  ? 0.1120 0.1173 0.1242 0.0159  -0.0088 0.0017  76  PHE   C CG  
1638 C CD1 . PHE   B 70  ? 0.1265 0.1284 0.1330 0.0167  -0.0081 0.0028  76  PHE   C CD1 
1639 C CD2 . PHE   B 70  ? 0.1177 0.1229 0.1290 0.0152  -0.0103 0.0003  76  PHE   C CD2 
1640 C CE1 . PHE   B 70  ? 0.1199 0.1188 0.1208 0.0170  -0.0088 0.0029  76  PHE   C CE1 
1641 C CE2 . PHE   B 70  ? 0.1273 0.1293 0.1320 0.0155  -0.0107 0.0004  76  PHE   C CE2 
1642 C CZ  . PHE   B 70  ? 0.1282 0.1272 0.1280 0.0165  -0.0099 0.0018  76  PHE   C CZ  
1643 N N   . SER   B 71  ? 0.1054 0.1223 0.1400 0.0155  -0.0118 -0.0014 77  SER   C N   
1644 C CA  . SER   B 71  ? 0.1145 0.1342 0.1535 0.0150  -0.0150 -0.0039 77  SER   C CA  
1645 C C   . SER   B 71  ? 0.1182 0.1352 0.1510 0.0141  -0.0166 -0.0057 77  SER   C C   
1646 O O   . SER   B 71  ? 0.1331 0.1466 0.1596 0.0137  -0.0148 -0.0047 77  SER   C O   
1647 C CB  . SER   B 71  ? 0.1096 0.1327 0.1590 0.0136  -0.0139 -0.0044 77  SER   C CB  
1648 O OG  . SER   B 71  ? 0.1373 0.1589 0.1871 0.0119  -0.0111 -0.0038 77  SER   C OG  
1649 N N   . LYS   B 72  ? 0.1364 0.1549 0.1712 0.0136  -0.0198 -0.0084 78  LYS   C N   
1650 C CA  . LYS   B 72  ? 0.1381 0.1536 0.1663 0.0128  -0.0209 -0.0105 78  LYS   C CA  
1651 C C   . LYS   B 72  ? 0.1316 0.1464 0.1637 0.0106  -0.0182 -0.0112 78  LYS   C C   
1652 O O   . LYS   B 72  ? 0.1479 0.1655 0.1890 0.0095  -0.0172 -0.0113 78  LYS   C O   
1653 C CB  . LYS   B 72  ? 0.1748 0.1921 0.2032 0.0131  -0.0258 -0.0134 78  LYS   C CB  
1654 C CG  . LYS   B 72  ? 0.2054 0.2235 0.2303 0.0156  -0.0288 -0.0122 78  LYS   C CG  
1655 C CD  . LYS   B 72  ? 0.3335 0.3535 0.3580 0.0160  -0.0344 -0.0150 78  LYS   C CD  
1656 C CE  . LYS   B 72  ? 0.4385 0.4588 0.4583 0.0188  -0.0377 -0.0134 78  LYS   C CE  
1657 N NZ  . LYS   B 72  ? 0.5077 0.5264 0.5192 0.0193  -0.0424 -0.0157 78  LYS   C NZ  
1658 N N   . PRO   B 73  ? 0.1401 0.1511 0.1663 0.0100  -0.0166 -0.0116 79  PRO   C N   
1659 C CA  . PRO   B 73  ? 0.1430 0.1533 0.1737 0.0081  -0.0138 -0.0120 79  PRO   C CA  
1660 C C   . PRO   B 73  ? 0.1422 0.1545 0.1801 0.0067  -0.0152 -0.0151 79  PRO   C C   
1661 O O   . PRO   B 73  ? 0.1616 0.1735 0.1969 0.0067  -0.0185 -0.0184 79  PRO   C O   
1662 C CB  . PRO   B 73  ? 0.1695 0.1755 0.1926 0.0081  -0.0124 -0.0125 79  PRO   C CB  
1663 C CG  . PRO   B 73  ? 0.1954 0.1996 0.2099 0.0099  -0.0137 -0.0114 79  PRO   C CG  
1664 C CD  . PRO   B 73  ? 0.1559 0.1632 0.1718 0.0112  -0.0170 -0.0114 79  PRO   C CD  
1665 N N   . SER   B 74  ? 0.1258 0.1400 0.1728 0.0054  -0.0130 -0.0143 80  SER   C N   
1666 C CA  A SER   B 74  ? 0.1360 0.1523 0.1918 0.0039  -0.0142 -0.0171 80  SER   C CA  
1667 C CA  B SER   B 74  ? 0.1332 0.1494 0.1888 0.0039  -0.0142 -0.0172 80  SER   C CA  
1668 C C   . SER   B 74  ? 0.1378 0.1540 0.2014 0.0024  -0.0103 -0.0158 80  SER   C C   
1669 O O   . SER   B 74  ? 0.1329 0.1479 0.1950 0.0028  -0.0072 -0.0124 80  SER   C O   
1670 C CB  A SER   B 74  ? 0.1671 0.1879 0.2291 0.0045  -0.0166 -0.0169 80  SER   C CB  
1671 C CB  B SER   B 74  ? 0.1557 0.1763 0.2171 0.0044  -0.0171 -0.0175 80  SER   C CB  
1672 O OG  A SER   B 74  ? 0.2026 0.2236 0.2577 0.0062  -0.0201 -0.0174 80  SER   C OG  
1673 O OG  B SER   B 74  ? 0.1612 0.1838 0.2273 0.0050  -0.0144 -0.0138 80  SER   C OG  
1674 N N   . LEU   B 75  ? 0.1381 0.1557 0.2107 0.0008  -0.0108 -0.0184 81  LEU   C N   
1675 C CA  . LEU   B 75  ? 0.1507 0.1682 0.2322 -0.0006 -0.0070 -0.0171 81  LEU   C CA  
1676 C C   . LEU   B 75  ? 0.1590 0.1803 0.2486 -0.0003 -0.0058 -0.0142 81  LEU   C C   
1677 O O   . LEU   B 75  ? 0.1806 0.2051 0.2766 -0.0007 -0.0081 -0.0160 81  LEU   C O   
1678 C CB  . LEU   B 75  ? 0.1699 0.1862 0.2571 -0.0027 -0.0079 -0.0217 81  LEU   C CB  
1679 C CG  . LEU   B 75  ? 0.1955 0.2110 0.2921 -0.0041 -0.0039 -0.0207 81  LEU   C CG  
1680 C CD1 . LEU   B 75  ? 0.1937 0.2055 0.2856 -0.0036 -0.0004 -0.0183 81  LEU   C CD1 
1681 C CD2 . LEU   B 75  ? 0.2220 0.2365 0.3251 -0.0063 -0.0053 -0.0260 81  LEU   C CD2 
1682 N N   . ILE   B 76  ? 0.1580 0.1790 0.2468 0.0005  -0.0023 -0.0097 82  ILE   C N   
1683 C CA  . ILE   B 76  ? 0.1687 0.1924 0.2626 0.0012  -0.0004 -0.0065 82  ILE   C CA  
1684 C C   . ILE   B 76  ? 0.1623 0.1855 0.2629 0.0005  0.0041  -0.0034 82  ILE   C C   
1685 O O   . ILE   B 76  ? 0.1557 0.1762 0.2527 0.0004  0.0058  -0.0016 82  ILE   C O   
1686 C CB  . ILE   B 76  ? 0.2042 0.2271 0.2883 0.0032  -0.0003 -0.0037 82  ILE   C CB  
1687 C CG1 . ILE   B 76  ? 0.2425 0.2658 0.3199 0.0043  -0.0043 -0.0060 82  ILE   C CG1 
1688 C CG2 . ILE   B 76  ? 0.2305 0.2550 0.3175 0.0041  0.0028  0.0000  82  ILE   C CG2 
1689 C CD1 . ILE   B 76  ? 0.2770 0.3040 0.3597 0.0050  -0.0062 -0.0068 82  ILE   C CD1 
1690 N N   . PHE   B 77  ? 0.1652 0.1908 0.2754 0.0002  0.0061  -0.0022 83  PHE   C N   
1691 C CA  . PHE   B 77  ? 0.1700 0.1949 0.2861 -0.0002 0.0108  0.0015  83  PHE   C CA  
1692 C C   . PHE   B 77  ? 0.1809 0.2050 0.2893 0.0017  0.0131  0.0062  83  PHE   C C   
1693 O O   . PHE   B 77  ? 0.2066 0.2320 0.3121 0.0029  0.0128  0.0068  83  PHE   C O   
1694 C CB  . PHE   B 77  ? 0.1743 0.2019 0.3039 -0.0012 0.0128  0.0013  83  PHE   C CB  
1695 C CG  . PHE   B 77  ? 0.1829 0.2090 0.3191 -0.0018 0.0177  0.0049  83  PHE   C CG  
1696 C CD1 . PHE   B 77  ? 0.1897 0.2134 0.3292 -0.0032 0.0182  0.0036  83  PHE   C CD1 
1697 C CD2 . PHE   B 77  ? 0.2013 0.2277 0.3388 -0.0006 0.0221  0.0098  83  PHE   C CD2 
1698 C CE1 . PHE   B 77  ? 0.2042 0.2264 0.3499 -0.0035 0.0228  0.0073  83  PHE   C CE1 
1699 C CE2 . PHE   B 77  ? 0.2065 0.2310 0.3488 -0.0008 0.0266  0.0137  83  PHE   C CE2 
1700 C CZ  . PHE   B 77  ? 0.2109 0.2336 0.3579 -0.0022 0.0268  0.0125  83  PHE   C CZ  
1701 N N   . VAL   B 78  ? 0.1450 0.1665 0.2495 0.0019  0.0150  0.0092  84  VAL   C N   
1702 C CA  . VAL   B 78  ? 0.1420 0.1623 0.2380 0.0034  0.0165  0.0133  84  VAL   C CA  
1703 C C   . VAL   B 78  ? 0.1400 0.1596 0.2408 0.0036  0.0209  0.0178  84  VAL   C C   
1704 O O   . VAL   B 78  ? 0.1389 0.1576 0.2455 0.0026  0.0223  0.0185  84  VAL   C O   
1705 C CB  . VAL   B 78  ? 0.1503 0.1683 0.2376 0.0035  0.0144  0.0135  84  VAL   C CB  
1706 C CG1 . VAL   B 78  ? 0.1697 0.1863 0.2482 0.0048  0.0151  0.0173  84  VAL   C CG1 
1707 C CG2 . VAL   B 78  ? 0.1635 0.1815 0.2462 0.0034  0.0106  0.0093  84  VAL   C CG2 
1708 N N   . GLU   B 79  ? 0.1301 0.1497 0.2278 0.0049  0.0235  0.0210  85  GLU   C N   
1709 C CA  . GLU   B 79  ? 0.1412 0.1595 0.2412 0.0054  0.0279  0.0259  85  GLU   C CA  
1710 C C   . GLU   B 79  ? 0.1374 0.1533 0.2311 0.0058  0.0275  0.0291  85  GLU   C C   
1711 O O   . GLU   B 79  ? 0.1389 0.1540 0.2250 0.0058  0.0241  0.0279  85  GLU   C O   
1712 C CB  . GLU   B 79  ? 0.1787 0.1969 0.2746 0.0070  0.0310  0.0284  85  GLU   C CB  
1713 C CG  . GLU   B 79  ? 0.2333 0.2543 0.3385 0.0069  0.0324  0.0263  85  GLU   C CG  
1714 C CD  . GLU   B 79  ? 0.3457 0.3682 0.4655 0.0054  0.0349  0.0263  85  GLU   C CD  
1715 O OE1 . GLU   B 79  ? 0.3926 0.4134 0.5151 0.0056  0.0389  0.0303  85  GLU   C OE1 
1716 O OE2 . GLU   B 79  ? 0.3809 0.4061 0.5093 0.0041  0.0326  0.0221  85  GLU   C OE2 
1717 N N   . ALA   B 80  ? 0.1465 0.1613 0.2440 0.0060  0.0311  0.0335  86  ALA   C N   
1718 C CA  . ALA   B 80  ? 0.1607 0.1735 0.2534 0.0065  0.0307  0.0372  86  ALA   C CA  
1719 C C   . ALA   B 80  ? 0.1777 0.1893 0.2568 0.0078  0.0284  0.0387  86  ALA   C C   
1720 O O   . ALA   B 80  ? 0.2014 0.2126 0.2747 0.0087  0.0296  0.0391  86  ALA   C O   
1721 C CB  . ALA   B 80  ? 0.1743 0.1859 0.2722 0.0072  0.0354  0.0425  86  ALA   C CB  
1722 N N   . SER   B 81  ? 0.1645 0.1755 0.2392 0.0076  0.0252  0.0392  87  SER   C N   
1723 C CA  . SER   B 81  ? 0.1801 0.1899 0.2428 0.0084  0.0225  0.0405  87  SER   C CA  
1724 C C   . SER   B 81  ? 0.1992 0.2079 0.2602 0.0089  0.0220  0.0455  87  SER   C C   
1725 O O   . SER   B 81  ? 0.1937 0.2026 0.2631 0.0089  0.0242  0.0480  87  SER   C O   
1726 C CB  . SER   B 81  ? 0.1734 0.1838 0.2327 0.0076  0.0184  0.0362  87  SER   C CB  
1727 O OG  . SER   B 81  ? 0.1821 0.1929 0.2465 0.0068  0.0169  0.0360  87  SER   C OG  
1728 N N   . GLU   B 82  ? 0.2180 0.2257 0.2687 0.0094  0.0188  0.0469  88  GLU   C N   
1729 C CA  . GLU   B 82  ? 0.2332 0.2405 0.2828 0.0099  0.0175  0.0518  88  GLU   C CA  
1730 C C   . GLU   B 82  ? 0.2292 0.2380 0.2876 0.0091  0.0158  0.0513  88  GLU   C C   
1731 O O   . GLU   B 82  ? 0.2455 0.2544 0.3074 0.0096  0.0157  0.0556  88  GLU   C O   
1732 C CB  . GLU   B 82  ? 0.2976 0.3034 0.3343 0.0105  0.0141  0.0535  88  GLU   C CB  
1733 C CG  . GLU   B 82  ? 0.3974 0.4038 0.4298 0.0095  0.0094  0.0500  88  GLU   C CG  
1734 C CD  . GLU   B 82  ? 0.4716 0.4765 0.4923 0.0098  0.0057  0.0521  88  GLU   C CD  
1735 O OE1 . GLU   B 82  ? 0.4999 0.5024 0.5120 0.0109  0.0074  0.0539  88  GLU   C OE1 
1736 O OE2 . GLU   B 82  ? 0.4871 0.4929 0.5072 0.0090  0.0013  0.0517  88  GLU   C OE2 
1737 N N   . TYR   B 83  ? 0.1880 0.1978 0.2505 0.0079  0.0150  0.0462  89  TYR   C N   
1738 C CA  . TYR   B 83  ? 0.1862 0.1969 0.2557 0.0072  0.0137  0.0453  89  TYR   C CA  
1739 C C   . TYR   B 83  ? 0.1908 0.2017 0.2704 0.0063  0.0164  0.0420  89  TYR   C C   
1740 O O   . TYR   B 83  ? 0.2086 0.2195 0.2944 0.0060  0.0163  0.0417  89  TYR   C O   
1741 C CB  . TYR   B 83  ? 0.1768 0.1878 0.2404 0.0066  0.0096  0.0428  89  TYR   C CB  
1742 C CG  . TYR   B 83  ? 0.1657 0.1764 0.2230 0.0062  0.0089  0.0383  89  TYR   C CG  
1743 C CD1 . TYR   B 83  ? 0.1734 0.1831 0.2209 0.0067  0.0078  0.0388  89  TYR   C CD1 
1744 C CD2 . TYR   B 83  ? 0.1671 0.1781 0.2279 0.0055  0.0095  0.0336  89  TYR   C CD2 
1745 C CE1 . TYR   B 83  ? 0.1582 0.1674 0.2007 0.0066  0.0075  0.0350  89  TYR   C CE1 
1746 C CE2 . TYR   B 83  ? 0.1676 0.1783 0.2231 0.0054  0.0086  0.0301  89  TYR   C CE2 
1747 C CZ  . TYR   B 83  ? 0.1561 0.1660 0.2029 0.0060  0.0077  0.0308  89  TYR   C CZ  
1748 O OH  . TYR   B 83  ? 0.1873 0.1968 0.2298 0.0062  0.0074  0.0276  89  TYR   C OH  
1749 N N   . TYR   B 84  ? 0.1587 0.1696 0.2407 0.0060  0.0187  0.0395  90  TYR   C N   
1750 C CA  . TYR   B 84  ? 0.1539 0.1648 0.2458 0.0050  0.0210  0.0363  90  TYR   C CA  
1751 C C   . TYR   B 84  ? 0.1516 0.1626 0.2484 0.0051  0.0245  0.0374  90  TYR   C C   
1752 O O   . TYR   B 84  ? 0.1552 0.1665 0.2465 0.0058  0.0250  0.0385  90  TYR   C O   
1753 C CB  . TYR   B 84  ? 0.1482 0.1595 0.2386 0.0040  0.0190  0.0301  90  TYR   C CB  
1754 C CG  . TYR   B 84  ? 0.1271 0.1380 0.2149 0.0037  0.0165  0.0283  90  TYR   C CG  
1755 C CD1 . TYR   B 84  ? 0.1284 0.1384 0.2228 0.0034  0.0177  0.0285  90  TYR   C CD1 
1756 C CD2 . TYR   B 84  ? 0.1222 0.1333 0.2017 0.0038  0.0137  0.0261  90  TYR   C CD2 
1757 C CE1 . TYR   B 84  ? 0.1288 0.1383 0.2214 0.0032  0.0162  0.0268  90  TYR   C CE1 
1758 C CE2 . TYR   B 84  ? 0.1162 0.1267 0.1938 0.0035  0.0120  0.0247  90  TYR   C CE2 
1759 C CZ  . TYR   B 84  ? 0.1247 0.1345 0.2089 0.0032  0.0134  0.0249  90  TYR   C CZ  
1760 O OH  . TYR   B 84  ? 0.1300 0.1390 0.2126 0.0031  0.0124  0.0236  90  TYR   C OH  
1761 N N   . PRO   B 85  ? 0.1529 0.1635 0.2605 0.0043  0.0273  0.0366  91  PRO   C N   
1762 C CA  . PRO   B 85  ? 0.1440 0.1549 0.2580 0.0040  0.0306  0.0367  91  PRO   C CA  
1763 C C   . PRO   B 85  ? 0.1412 0.1538 0.2547 0.0031  0.0289  0.0311  91  PRO   C C   
1764 O O   . PRO   B 85  ? 0.1411 0.1541 0.2494 0.0027  0.0254  0.0272  91  PRO   C O   
1765 C CB  . PRO   B 85  ? 0.1466 0.1563 0.2728 0.0030  0.0333  0.0365  91  PRO   C CB  
1766 C CG  . PRO   B 85  ? 0.1570 0.1662 0.2827 0.0022  0.0306  0.0324  91  PRO   C CG  
1767 C CD  . PRO   B 85  ? 0.1551 0.1647 0.2701 0.0034  0.0275  0.0346  91  PRO   C CD  
1768 N N   . ALA   B 86  ? 0.1333 0.1469 0.2530 0.0028  0.0315  0.0308  92  ALA   C N   
1769 C CA  . ALA   B 86  ? 0.1550 0.1706 0.2767 0.0019  0.0298  0.0257  92  ALA   C CA  
1770 C C   . ALA   B 86  ? 0.1558 0.1713 0.2832 0.0001  0.0276  0.0204  92  ALA   C C   
1771 O O   . ALA   B 86  ? 0.1761 0.1901 0.3119 -0.0008 0.0297  0.0207  92  ALA   C O   
1772 C CB  . ALA   B 86  ? 0.1614 0.1784 0.2916 0.0017  0.0334  0.0269  92  ALA   C CB  
1773 N N   . ARG   B 87  ? 0.1377 0.1540 0.2597 -0.0002 0.0236  0.0160  93  ARG   C N   
1774 C CA  . ARG   B 87  ? 0.1398 0.1552 0.2645 -0.0016 0.0215  0.0109  93  ARG   C CA  
1775 C C   . ARG   B 87  ? 0.1402 0.1569 0.2587 -0.0017 0.0172  0.0063  93  ARG   C C   
1776 O O   . ARG   B 87  ? 0.1410 0.1589 0.2523 -0.0004 0.0159  0.0074  93  ARG   C O   
1777 C CB  . ARG   B 87  ? 0.1546 0.1674 0.2756 -0.0013 0.0217  0.0122  93  ARG   C CB  
1778 C CG  . ARG   B 87  ? 0.1366 0.1494 0.2458 0.0000  0.0191  0.0131  93  ARG   C CG  
1779 C CD  . ARG   B 87  ? 0.1562 0.1669 0.2633 0.0003  0.0194  0.0146  93  ARG   C CD  
1780 N NE  . ARG   B 87  ? 0.1585 0.1692 0.2554 0.0010  0.0166  0.0144  93  ARG   C NE  
1781 C CZ  . ARG   B 87  ? 0.1730 0.1822 0.2670 0.0010  0.0157  0.0133  93  ARG   C CZ  
1782 N NH1 . ARG   B 87  ? 0.1717 0.1792 0.2719 0.0004  0.0176  0.0122  93  ARG   C NH1 
1783 N NH2 . ARG   B 87  ? 0.1804 0.1897 0.2660 0.0016  0.0134  0.0130  93  ARG   C NH2 
1784 N N   . TYR   B 88  ? 0.1440 0.1596 0.2638 -0.0030 0.0151  0.0012  94  TYR   C N   
1785 C CA  . TYR   B 88  ? 0.1634 0.1795 0.2755 -0.0027 0.0109  -0.0027 94  TYR   C CA  
1786 C C   . TYR   B 88  ? 0.1521 0.1659 0.2542 -0.0018 0.0102  -0.0018 94  TYR   C C   
1787 O O   . TYR   B 88  ? 0.1657 0.1771 0.2690 -0.0021 0.0121  -0.0012 94  TYR   C O   
1788 C CB  . TYR   B 88  ? 0.1883 0.2040 0.3046 -0.0044 0.0086  -0.0087 94  TYR   C CB  
1789 C CG  . TYR   B 88  ? 0.2224 0.2412 0.3485 -0.0055 0.0080  -0.0102 94  TYR   C CG  
1790 C CD1 . TYR   B 88  ? 0.2432 0.2652 0.3675 -0.0049 0.0047  -0.0113 94  TYR   C CD1 
1791 C CD2 . TYR   B 88  ? 0.2471 0.2657 0.3852 -0.0070 0.0109  -0.0099 94  TYR   C CD2 
1792 C CE1 . TYR   B 88  ? 0.2606 0.2860 0.3955 -0.0058 0.0043  -0.0123 94  TYR   C CE1 
1793 C CE2 . TYR   B 88  ? 0.2606 0.2824 0.4093 -0.0081 0.0106  -0.0111 94  TYR   C CE2 
1794 C CZ  . TYR   B 88  ? 0.2791 0.3045 0.4264 -0.0075 0.0072  -0.0123 94  TYR   C CZ  
1795 O OH  . TYR   B 88  ? 0.3104 0.3393 0.4697 -0.0086 0.0070  -0.0133 94  TYR   C OH  
1796 N N   . GLN   B 89  ? 0.1417 0.1562 0.2350 -0.0006 0.0079  -0.0017 95  GLN   C N   
1797 C CA  . GLN   B 89  ? 0.1290 0.1415 0.2132 0.0002  0.0070  -0.0013 95  GLN   C CA  
1798 C C   . GLN   B 89  ? 0.1255 0.1376 0.2039 0.0003  0.0037  -0.0056 95  GLN   C C   
1799 O O   . GLN   B 89  ? 0.1411 0.1554 0.2193 0.0006  0.0015  -0.0069 95  GLN   C O   
1800 C CB  . GLN   B 89  ? 0.1383 0.1514 0.2170 0.0015  0.0073  0.0030  95  GLN   C CB  
1801 C CG  . GLN   B 89  ? 0.1419 0.1531 0.2129 0.0020  0.0066  0.0038  95  GLN   C CG  
1802 C CD  . GLN   B 89  ? 0.1304 0.1417 0.1975 0.0028  0.0071  0.0082  95  GLN   C CD  
1803 O OE1 . GLN   B 89  ? 0.1437 0.1555 0.2142 0.0029  0.0089  0.0116  95  GLN   C OE1 
1804 N NE2 . GLN   B 89  ? 0.1386 0.1490 0.1981 0.0034  0.0054  0.0081  95  GLN   C NE2 
1805 N N   . SER   B 90  ? 0.1172 0.1264 0.1908 0.0002  0.0034  -0.0076 96  SER   C N   
1806 C CA  . SER   B 90  ? 0.1272 0.1354 0.1940 0.0004  0.0005  -0.0115 96  SER   C CA  
1807 C C   . SER   B 90  ? 0.1214 0.1287 0.1785 0.0019  -0.0005 -0.0097 96  SER   C C   
1808 O O   . SER   B 90  ? 0.1218 0.1288 0.1776 0.0024  0.0012  -0.0061 96  SER   C O   
1809 C CB  . SER   B 90  ? 0.1427 0.1474 0.2091 -0.0005 0.0012  -0.0152 96  SER   C CB  
1810 O OG  . SER   B 90  ? 0.1512 0.1534 0.2155 -0.0001 0.0041  -0.0130 96  SER   C OG  
1811 N N   . HIS   B 91  ? 0.1198 0.1268 0.1704 0.0026  -0.0034 -0.0123 97  HIS   C N   
1812 C CA  . HIS   B 91  ? 0.1144 0.1201 0.1559 0.0040  -0.0043 -0.0110 97  HIS   C CA  
1813 C C   . HIS   B 91  ? 0.1161 0.1236 0.1576 0.0048  -0.0039 -0.0072 97  HIS   C C   
1814 O O   . HIS   B 91  ? 0.1264 0.1325 0.1629 0.0053  -0.0031 -0.0050 97  HIS   C O   
1815 C CB  . HIS   B 91  ? 0.1317 0.1336 0.1685 0.0040  -0.0021 -0.0108 97  HIS   C CB  
1816 C CG  . HIS   B 91  ? 0.1530 0.1520 0.1879 0.0034  -0.0019 -0.0149 97  HIS   C CG  
1817 N ND1 . HIS   B 91  ? 0.1806 0.1770 0.2062 0.0043  -0.0035 -0.0171 97  HIS   C ND1 
1818 C CD2 . HIS   B 91  ? 0.1687 0.1666 0.2092 0.0022  -0.0003 -0.0171 97  HIS   C CD2 
1819 C CE1 . HIS   B 91  ? 0.1826 0.1762 0.2076 0.0036  -0.0028 -0.0207 97  HIS   C CE1 
1820 N NE2 . HIS   B 91  ? 0.1928 0.1872 0.2269 0.0022  -0.0008 -0.0211 97  HIS   C NE2 
1821 N N   . LEU   B 92  ? 0.1083 0.1188 0.1555 0.0047  -0.0043 -0.0065 98  LEU   C N   
1822 C CA  . LEU   B 92  ? 0.1095 0.1214 0.1565 0.0054  -0.0034 -0.0033 98  LEU   C CA  
1823 C C   . LEU   B 92  ? 0.1027 0.1161 0.1474 0.0068  -0.0057 -0.0039 98  LEU   C C   
1824 O O   . LEU   B 92  ? 0.1169 0.1321 0.1646 0.0068  -0.0079 -0.0064 98  LEU   C O   
1825 C CB  . LEU   B 92  ? 0.1190 0.1328 0.1746 0.0047  -0.0012 -0.0016 98  LEU   C CB  
1826 C CG  . LEU   B 92  ? 0.1246 0.1391 0.1792 0.0055  0.0004  0.0020  98  LEU   C CG  
1827 C CD1 . LEU   B 92  ? 0.1345 0.1468 0.1837 0.0055  0.0012  0.0046  98  LEU   C CD1 
1828 C CD2 . LEU   B 92  ? 0.1475 0.1638 0.2104 0.0049  0.0029  0.0038  98  LEU   C CD2 
1829 N N   . MET   B 93  ? 0.0970 0.1097 0.1367 0.0079  -0.0053 -0.0016 99  MET   C N   
1830 C CA  . MET   B 93  ? 0.0917 0.1053 0.1292 0.0094  -0.0068 -0.0017 99  MET   C CA  
1831 C C   . MET   B 93  ? 0.1058 0.1202 0.1450 0.0099  -0.0046 0.0009  99  MET   C C   
1832 O O   . MET   B 93  ? 0.1202 0.1329 0.1566 0.0095  -0.0028 0.0029  99  MET   C O   
1833 C CB  . MET   B 93  ? 0.1114 0.1221 0.1400 0.0104  -0.0079 -0.0015 99  MET   C CB  
1834 C CG  . MET   B 93  ? 0.1408 0.1499 0.1661 0.0101  -0.0094 -0.0038 99  MET   C CG  
1835 S SD  . MET   B 93  ? 0.1500 0.1551 0.1654 0.0112  -0.0095 -0.0030 99  MET   C SD  
1836 C CE  . MET   B 93  ? 0.1607 0.1642 0.1762 0.0100  -0.0067 -0.0005 99  MET   C CE  
1837 N N   . LEU   B 94  ? 0.1025 0.1193 0.1459 0.0109  -0.0046 0.0008  100 LEU   C N   
1838 C CA  . LEU   B 94  ? 0.1075 0.1245 0.1520 0.0116  -0.0018 0.0032  100 LEU   C CA  
1839 C C   . LEU   B 94  ? 0.1124 0.1284 0.1521 0.0135  -0.0021 0.0036  100 LEU   C C   
1840 O O   . LEU   B 94  ? 0.1277 0.1445 0.1672 0.0145  -0.0045 0.0022  100 LEU   C O   
1841 C CB  . LEU   B 94  ? 0.1197 0.1402 0.1743 0.0114  -0.0003 0.0033  100 LEU   C CB  
1842 C CG  . LEU   B 94  ? 0.1262 0.1479 0.1876 0.0096  0.0006  0.0030  100 LEU   C CG  
1843 C CD1 . LEU   B 94  ? 0.1615 0.1865 0.2337 0.0095  0.0025  0.0035  100 LEU   C CD1 
1844 C CD2 . LEU   B 94  ? 0.1592 0.1783 0.2168 0.0088  0.0028  0.0053  100 LEU   C CD2 
1845 N N   . ALA   B 95  ? 0.1120 0.1260 0.1481 0.0140  0.0006  0.0055  101 ALA   C N   
1846 C CA  . ALA   B 95  ? 0.1161 0.1286 0.1486 0.0158  0.0015  0.0060  101 ALA   C CA  
1847 C C   . ALA   B 95  ? 0.1136 0.1258 0.1475 0.0163  0.0055  0.0078  101 ALA   C C   
1848 O O   . ALA   B 95  ? 0.1132 0.1254 0.1481 0.0151  0.0072  0.0091  101 ALA   C O   
1849 C CB  . ALA   B 95  ? 0.1260 0.1342 0.1489 0.0158  0.0007  0.0061  101 ALA   C CB  
1850 N N   . VAL   B 96  ? 0.1170 0.1286 0.1505 0.0181  0.0072  0.0080  102 VAL   C N   
1851 C CA  . VAL   B 96  ? 0.1334 0.1434 0.1659 0.0189  0.0116  0.0097  102 VAL   C CA  
1852 C C   . VAL   B 96  ? 0.1402 0.1451 0.1614 0.0186  0.0122  0.0100  102 VAL   C C   
1853 O O   . VAL   B 96  ? 0.1638 0.1659 0.1794 0.0193  0.0109  0.0090  102 VAL   C O   
1854 C CB  . VAL   B 96  ? 0.1456 0.1570 0.1831 0.0211  0.0136  0.0096  102 VAL   C CB  
1855 C CG1 . VAL   B 96  ? 0.1657 0.1746 0.2009 0.0221  0.0190  0.0112  102 VAL   C CG1 
1856 C CG2 . VAL   B 96  ? 0.1523 0.1693 0.2020 0.0211  0.0121  0.0091  102 VAL   C CG2 
1857 N N   . GLY   B 97  ? 0.1489 0.1525 0.1669 0.0175  0.0136  0.0115  103 GLY   C N   
1858 C CA  . GLY   B 97  ? 0.1674 0.1664 0.1748 0.0169  0.0133  0.0117  103 GLY   C CA  
1859 C C   . GLY   B 97  ? 0.1646 0.1630 0.1696 0.0157  0.0141  0.0138  103 GLY   C C   
1860 O O   . GLY   B 97  ? 0.1789 0.1804 0.1908 0.0153  0.0152  0.0151  103 GLY   C O   
1861 N N   . HIS   B 98  ? 0.1702 0.1647 0.1657 0.0152  0.0135  0.0140  104 HIS   C N   
1862 C CA  . HIS   B 98  ? 0.1694 0.1629 0.1610 0.0143  0.0138  0.0163  104 HIS   C CA  
1863 C C   . HIS   B 98  ? 0.1625 0.1578 0.1563 0.0125  0.0101  0.0169  104 HIS   C C   
1864 O O   . HIS   B 98  ? 0.1695 0.1642 0.1617 0.0116  0.0070  0.0153  104 HIS   C O   
1865 C CB  . HIS   B 98  ? 0.2058 0.1942 0.1857 0.0145  0.0143  0.0161  104 HIS   C CB  
1866 C CG  . HIS   B 98  ? 0.2534 0.2407 0.2284 0.0140  0.0147  0.0187  104 HIS   C CG  
1867 N ND1 . HIS   B 98  ? 0.2777 0.2657 0.2551 0.0151  0.0188  0.0212  104 HIS   C ND1 
1868 C CD2 . HIS   B 98  ? 0.2804 0.2661 0.2492 0.0126  0.0113  0.0195  104 HIS   C CD2 
1869 C CE1 . HIS   B 98  ? 0.3079 0.2946 0.2796 0.0144  0.0178  0.0236  104 HIS   C CE1 
1870 N NE2 . HIS   B 98  ? 0.3146 0.3000 0.2810 0.0130  0.0130  0.0226  104 HIS   C NE2 
1871 N N   . SER   B 99  ? 0.1630 0.1600 0.1601 0.0119  0.0108  0.0194  105 SER   C N   
1872 C CA  . SER   B 99  ? 0.1662 0.1648 0.1661 0.0104  0.0079  0.0204  105 SER   C CA  
1873 C C   . SER   B 99  ? 0.1853 0.1842 0.1854 0.0103  0.0092  0.0240  105 SER   C C   
1874 O O   . SER   B 99  ? 0.1996 0.2002 0.2059 0.0109  0.0123  0.0254  105 SER   C O   
1875 C CB  . SER   B 99  ? 0.1746 0.1766 0.1841 0.0100  0.0073  0.0190  105 SER   C CB  
1876 O OG  . SER   B 99  ? 0.1877 0.1911 0.2008 0.0087  0.0054  0.0200  105 SER   C OG  
1877 N N   . GLU   B 100 ? 0.1884 0.1855 0.1819 0.0097  0.0068  0.0256  106 GLU   C N   
1878 C CA  . GLU   B 100 ? 0.1948 0.1920 0.1875 0.0097  0.0070  0.0296  106 GLU   C CA  
1879 C C   . GLU   B 100 ? 0.1781 0.1781 0.1783 0.0084  0.0043  0.0304  106 GLU   C C   
1880 O O   . GLU   B 100 ? 0.1628 0.1635 0.1653 0.0075  0.0019  0.0279  106 GLU   C O   
1881 C CB  . GLU   B 100 ? 0.2367 0.2303 0.2172 0.0095  0.0047  0.0306  106 GLU   C CB  
1882 C CG  . GLU   B 100 ? 0.3230 0.3126 0.2934 0.0105  0.0066  0.0291  106 GLU   C CG  
1883 C CD  . GLU   B 100 ? 0.3810 0.3688 0.3477 0.0121  0.0113  0.0318  106 GLU   C CD  
1884 O OE1 . GLU   B 100 ? 0.3704 0.3604 0.3432 0.0125  0.0130  0.0351  106 GLU   C OE1 
1885 O OE2 . GLU   B 100 ? 0.3986 0.3827 0.3568 0.0132  0.0137  0.0305  106 GLU   C OE2 
1886 N N   . PRO   B 101 ? 0.1765 0.1776 0.1803 0.0085  0.0047  0.0340  107 PRO   C N   
1887 C CA  . PRO   B 101 ? 0.1637 0.1671 0.1750 0.0075  0.0025  0.0349  107 PRO   C CA  
1888 C C   . PRO   B 101 ? 0.1673 0.1705 0.1753 0.0064  -0.0020 0.0339  107 PRO   C C   
1889 O O   . PRO   B 101 ? 0.1657 0.1704 0.1800 0.0055  -0.0030 0.0324  107 PRO   C O   
1890 C CB  . PRO   B 101 ? 0.1940 0.1978 0.2071 0.0081  0.0036  0.0398  107 PRO   C CB  
1891 C CG  . PRO   B 101 ? 0.2260 0.2281 0.2354 0.0094  0.0077  0.0411  107 PRO   C CG  
1892 C CD  . PRO   B 101 ? 0.1989 0.1990 0.2009 0.0097  0.0081  0.0376  107 PRO   C CD  
1893 N N   . GLY   B 102 ? 0.1595 0.1603 0.1577 0.0062  -0.0044 0.0343  108 GLY   C N   
1894 C CA  . GLY   B 102 ? 0.1605 0.1612 0.1568 0.0049  -0.0089 0.0333  108 GLY   C CA  
1895 C C   . GLY   B 102 ? 0.1571 0.1570 0.1534 0.0042  -0.0092 0.0290  108 GLY   C C   
1896 O O   . GLY   B 102 ? 0.1851 0.1849 0.1815 0.0030  -0.0123 0.0280  108 GLY   C O   
1897 N N   . ASP   B 103 ? 0.1389 0.1381 0.1350 0.0051  -0.0060 0.0267  109 ASP   C N   
1898 C CA  . ASP   B 103 ? 0.1315 0.1299 0.1277 0.0048  -0.0061 0.0232  109 ASP   C CA  
1899 C C   . ASP   B 103 ? 0.1228 0.1236 0.1277 0.0044  -0.0059 0.0223  109 ASP   C C   
1900 O O   . ASP   B 103 ? 0.1292 0.1294 0.1342 0.0042  -0.0063 0.0199  109 ASP   C O   
1901 C CB  . ASP   B 103 ? 0.1426 0.1397 0.1361 0.0062  -0.0031 0.0213  109 ASP   C CB  
1902 C CG  . ASP   B 103 ? 0.1750 0.1686 0.1586 0.0067  -0.0029 0.0212  109 ASP   C CG  
1903 O OD1 . ASP   B 103 ? 0.1823 0.1738 0.1602 0.0057  -0.0058 0.0207  109 ASP   C OD1 
1904 O OD2 . ASP   B 103 ? 0.1848 0.1776 0.1666 0.0080  0.0004  0.0215  109 ASP   C OD2 
1905 N N   . CYS   B 104 ? 0.1167 0.1199 0.1288 0.0044  -0.0049 0.0243  110 CYS   C N   
1906 C CA  . CYS   B 104 ? 0.1117 0.1165 0.1315 0.0040  -0.0043 0.0233  110 CYS   C CA  
1907 C C   . CYS   B 104 ? 0.1181 0.1225 0.1379 0.0030  -0.0066 0.0228  110 CYS   C C   
1908 O O   . CYS   B 104 ? 0.1356 0.1399 0.1538 0.0022  -0.0091 0.0246  110 CYS   C O   
1909 C CB  . CYS   B 104 ? 0.1119 0.1187 0.1392 0.0041  -0.0030 0.0258  110 CYS   C CB  
1910 S SG  . CYS   B 104 ? 0.1393 0.1469 0.1701 0.0051  0.0006  0.0258  110 CYS   C SG  
1911 N N   . GLY   B 105 ? 0.0969 0.1009 0.1184 0.0029  -0.0059 0.0203  111 GLY   C N   
1912 C CA  . GLY   B 105 ? 0.1249 0.1282 0.1471 0.0020  -0.0072 0.0199  111 GLY   C CA  
1913 C C   . GLY   B 105 ? 0.1227 0.1235 0.1385 0.0020  -0.0081 0.0178  111 GLY   C C   
1914 O O   . GLY   B 105 ? 0.1309 0.1307 0.1475 0.0014  -0.0084 0.0170  111 GLY   C O   
1915 N N   . GLY   B 106 ? 0.1140 0.1134 0.1238 0.0027  -0.0080 0.0169  112 GLY   C N   
1916 C CA  . GLY   B 106 ? 0.1173 0.1139 0.1214 0.0029  -0.0084 0.0149  112 GLY   C CA  
1917 C C   . GLY   B 106 ? 0.1133 0.1095 0.1187 0.0036  -0.0069 0.0130  112 GLY   C C   
1918 O O   . GLY   B 106 ? 0.1128 0.1106 0.1211 0.0045  -0.0055 0.0125  112 GLY   C O   
1919 N N   . ILE   B 107 ? 0.1135 0.1074 0.1166 0.0034  -0.0073 0.0121  113 ILE   C N   
1920 C CA  . ILE   B 107 ? 0.1164 0.1094 0.1196 0.0043  -0.0060 0.0107  113 ILE   C CA  
1921 C C   . ILE   B 107 ? 0.1146 0.1066 0.1139 0.0059  -0.0054 0.0093  113 ILE   C C   
1922 O O   . ILE   B 107 ? 0.1185 0.1087 0.1138 0.0062  -0.0057 0.0090  113 ILE   C O   
1923 C CB  . ILE   B 107 ? 0.1504 0.1411 0.1534 0.0034  -0.0062 0.0108  113 ILE   C CB  
1924 C CG1 . ILE   B 107 ? 0.1809 0.1735 0.1903 0.0023  -0.0057 0.0122  113 ILE   C CG1 
1925 C CG2 . ILE   B 107 ? 0.1574 0.1457 0.1573 0.0047  -0.0049 0.0097  113 ILE   C CG2 
1926 C CD1 . ILE   B 107 ? 0.2378 0.2288 0.2495 0.0011  -0.0055 0.0129  113 ILE   C CD1 
1927 N N   . LEU   B 108 ? 0.1052 0.0983 0.1060 0.0071  -0.0047 0.0084  114 LEU   C N   
1928 C CA  . LEU   B 108 ? 0.1098 0.1023 0.1081 0.0088  -0.0045 0.0072  114 LEU   C CA  
1929 C C   . LEU   B 108 ? 0.1142 0.1043 0.1100 0.0093  -0.0043 0.0069  114 LEU   C C   
1930 O O   . LEU   B 108 ? 0.1107 0.1010 0.1080 0.0089  -0.0038 0.0068  114 LEU   C O   
1931 C CB  . LEU   B 108 ? 0.1023 0.0978 0.1041 0.0096  -0.0044 0.0064  114 LEU   C CB  
1932 C CG  . LEU   B 108 ? 0.1144 0.1102 0.1150 0.0114  -0.0050 0.0052  114 LEU   C CG  
1933 C CD1 . LEU   B 108 ? 0.1329 0.1279 0.1317 0.0126  -0.0046 0.0055  114 LEU   C CD1 
1934 C CD2 . LEU   B 108 ? 0.1306 0.1296 0.1359 0.0117  -0.0055 0.0041  114 LEU   C CD2 
1935 N N   . ARG   B 109 ? 0.1158 0.1031 0.1076 0.0103  -0.0043 0.0068  115 ARG   C N   
1936 C CA  . ARG   B 109 ? 0.1226 0.1071 0.1117 0.0109  -0.0037 0.0070  115 ARG   C CA  
1937 C C   . ARG   B 109 ? 0.1362 0.1196 0.1222 0.0132  -0.0040 0.0066  115 ARG   C C   
1938 O O   . ARG   B 109 ? 0.1433 0.1270 0.1292 0.0141  -0.0043 0.0064  115 ARG   C O   
1939 C CB  . ARG   B 109 ? 0.1648 0.1462 0.1530 0.0095  -0.0032 0.0077  115 ARG   C CB  
1940 C CG  . ARG   B 109 ? 0.2026 0.1819 0.1883 0.0097  -0.0036 0.0074  115 ARG   C CG  
1941 C CD  . ARG   B 109 ? 0.2651 0.2412 0.2503 0.0080  -0.0035 0.0076  115 ARG   C CD  
1942 N NE  . ARG   B 109 ? 0.3089 0.2869 0.2970 0.0058  -0.0047 0.0079  115 ARG   C NE  
1943 C CZ  . ARG   B 109 ? 0.3821 0.3596 0.3731 0.0039  -0.0051 0.0086  115 ARG   C CZ  
1944 N NH1 . ARG   B 109 ? 0.3871 0.3616 0.3783 0.0038  -0.0038 0.0090  115 ARG   C NH1 
1945 N NH2 . ARG   B 109 ? 0.4003 0.3801 0.3945 0.0021  -0.0066 0.0092  115 ARG   C NH2 
1946 N N   . CYS   B 110 ? 0.1407 0.1226 0.1241 0.0143  -0.0038 0.0069  116 CYS   C N   
1947 C CA  . CYS   B 110 ? 0.1393 0.1199 0.1195 0.0168  -0.0043 0.0071  116 CYS   C CA  
1948 C C   . CYS   B 110 ? 0.1592 0.1352 0.1355 0.0172  -0.0028 0.0085  116 CYS   C C   
1949 O O   . CYS   B 110 ? 0.1609 0.1350 0.1380 0.0154  -0.0013 0.0090  116 CYS   C O   
1950 C CB  . CYS   B 110 ? 0.1362 0.1194 0.1162 0.0180  -0.0060 0.0063  116 CYS   C CB  
1951 S SG  . CYS   B 110 ? 0.1422 0.1239 0.1191 0.0176  -0.0051 0.0061  116 CYS   C SG  
1952 N N   . GLN   B 111 ? 0.1792 0.1532 0.1516 0.0197  -0.0031 0.0094  117 GLN   C N   
1953 C CA  . GLN   B 111 ? 0.1960 0.1651 0.1648 0.0202  -0.0011 0.0111  117 GLN   C CA  
1954 C C   . GLN   B 111 ? 0.2039 0.1719 0.1711 0.0194  0.0005  0.0115  117 GLN   C C   
1955 O O   . GLN   B 111 ? 0.2257 0.1898 0.1915 0.0190  0.0029  0.0130  117 GLN   C O   
1956 C CB  . GLN   B 111 ? 0.2102 0.1773 0.1750 0.0233  -0.0017 0.0125  117 GLN   C CB  
1957 C CG  . GLN   B 111 ? 0.2667 0.2359 0.2283 0.0251  -0.0038 0.0123  117 GLN   C CG  
1958 C CD  . GLN   B 111 ? 0.4006 0.3684 0.3584 0.0284  -0.0051 0.0140  117 GLN   C CD  
1959 O OE1 . GLN   B 111 ? 0.4364 0.4073 0.3968 0.0298  -0.0075 0.0136  117 GLN   C OE1 
1960 N NE2 . GLN   B 111 ? 0.4096 0.3730 0.3618 0.0297  -0.0035 0.0162  117 GLN   C NE2 
1961 N N   . HIS   B 112 ? 0.1745 0.1455 0.1423 0.0189  -0.0005 0.0102  118 HIS   C N   
1962 C CA  . HIS   B 112 ? 0.1761 0.1456 0.1419 0.0184  0.0015  0.0103  118 HIS   C CA  
1963 C C   . HIS   B 112 ? 0.1759 0.1465 0.1474 0.0157  0.0032  0.0101  118 HIS   C C   
1964 O O   . HIS   B 112 ? 0.1940 0.1629 0.1651 0.0152  0.0057  0.0105  118 HIS   C O   
1965 C CB  . HIS   B 112 ? 0.1848 0.1561 0.1475 0.0195  -0.0002 0.0088  118 HIS   C CB  
1966 C CG  . HIS   B 112 ? 0.1690 0.1399 0.1266 0.0222  -0.0026 0.0092  118 HIS   C CG  
1967 N ND1 . HIS   B 112 ? 0.1704 0.1451 0.1305 0.0230  -0.0060 0.0080  118 HIS   C ND1 
1968 C CD2 . HIS   B 112 ? 0.2036 0.1705 0.1540 0.0245  -0.0019 0.0110  118 HIS   C CD2 
1969 C CE1 . HIS   B 112 ? 0.1838 0.1573 0.1389 0.0256  -0.0077 0.0091  118 HIS   C CE1 
1970 N NE2 . HIS   B 112 ? 0.2169 0.1857 0.1656 0.0266  -0.0055 0.0109  118 HIS   C NE2 
1971 N N   . GLY   B 113 ? 0.1593 0.1326 0.1359 0.0141  0.0019  0.0095  119 GLY   C N   
1972 C CA  . GLY   B 113 ? 0.1631 0.1380 0.1455 0.0117  0.0027  0.0095  119 GLY   C CA  
1973 C C   . GLY   B 113 ? 0.1427 0.1219 0.1291 0.0109  0.0007  0.0083  119 GLY   C C   
1974 O O   . GLY   B 113 ? 0.1349 0.1155 0.1205 0.0117  -0.0011 0.0076  119 GLY   C O   
1975 N N   . VAL   B 114 ? 0.1286 0.1096 0.1198 0.0092  0.0014  0.0085  120 VAL   C N   
1976 C CA  . VAL   B 114 ? 0.1291 0.1138 0.1246 0.0083  0.0000  0.0079  120 VAL   C CA  
1977 C C   . VAL   B 114 ? 0.1310 0.1175 0.1260 0.0093  -0.0005 0.0063  120 VAL   C C   
1978 O O   . VAL   B 114 ? 0.1367 0.1222 0.1308 0.0097  0.0009  0.0055  120 VAL   C O   
1979 C CB  . VAL   B 114 ? 0.1377 0.1235 0.1391 0.0065  0.0008  0.0090  120 VAL   C CB  
1980 C CG1 . VAL   B 114 ? 0.1550 0.1444 0.1606 0.0058  -0.0003 0.0089  120 VAL   C CG1 
1981 C CG2 . VAL   B 114 ? 0.1623 0.1468 0.1650 0.0051  0.0005  0.0104  120 VAL   C CG2 
1982 N N   . VAL   B 115 ? 0.1154 0.1042 0.1111 0.0098  -0.0022 0.0055  121 VAL   C N   
1983 C CA  . VAL   B 115 ? 0.1155 0.1065 0.1122 0.0105  -0.0032 0.0038  121 VAL   C CA  
1984 C C   . VAL   B 115 ? 0.1186 0.1122 0.1215 0.0091  -0.0027 0.0035  121 VAL   C C   
1985 O O   . VAL   B 115 ? 0.1264 0.1206 0.1307 0.0090  -0.0025 0.0019  121 VAL   C O   
1986 C CB  . VAL   B 115 ? 0.1173 0.1097 0.1132 0.0117  -0.0050 0.0034  121 VAL   C CB  
1987 C CG1 . VAL   B 115 ? 0.1404 0.1357 0.1392 0.0121  -0.0063 0.0016  121 VAL   C CG1 
1988 C CG2 . VAL   B 115 ? 0.1366 0.1263 0.1269 0.0134  -0.0054 0.0039  121 VAL   C CG2 
1989 N N   . GLY   B 116 ? 0.1093 0.1041 0.1154 0.0081  -0.0026 0.0051  122 GLY   C N   
1990 C CA  . GLY   B 116 ? 0.1216 0.1187 0.1335 0.0070  -0.0021 0.0056  122 GLY   C CA  
1991 C C   . GLY   B 116 ? 0.1099 0.1078 0.1232 0.0062  -0.0025 0.0076  122 GLY   C C   
1992 O O   . GLY   B 116 ? 0.1166 0.1129 0.1264 0.0062  -0.0032 0.0083  122 GLY   C O   
1993 N N   . ILE   B 117 ? 0.0980 0.0981 0.1163 0.0056  -0.0022 0.0086  123 ILE   C N   
1994 C CA  . ILE   B 117 ? 0.1011 0.1019 0.1198 0.0049  -0.0028 0.0108  123 ILE   C CA  
1995 C C   . ILE   B 117 ? 0.0941 0.0968 0.1148 0.0053  -0.0024 0.0113  123 ILE   C C   
1996 O O   . ILE   B 117 ? 0.1138 0.1180 0.1388 0.0055  -0.0015 0.0104  123 ILE   C O   
1997 C CB  . ILE   B 117 ? 0.1118 0.1131 0.1349 0.0038  -0.0027 0.0129  123 ILE   C CB  
1998 C CG1 . ILE   B 117 ? 0.1205 0.1230 0.1497 0.0037  -0.0010 0.0126  123 ILE   C CG1 
1999 C CG2 . ILE   B 117 ? 0.1379 0.1374 0.1596 0.0032  -0.0030 0.0131  123 ILE   C CG2 
2000 C CD1 . ILE   B 117 ? 0.1330 0.1366 0.1683 0.0029  -0.0006 0.0153  123 ILE   C CD1 
2001 N N   . VAL   B 118 ? 0.0993 0.1018 0.1171 0.0053  -0.0029 0.0127  124 VAL   C N   
2002 C CA  . VAL   B 118 ? 0.0978 0.1017 0.1172 0.0058  -0.0018 0.0137  124 VAL   C CA  
2003 C C   . VAL   B 118 ? 0.0997 0.1053 0.1257 0.0052  -0.0008 0.0154  124 VAL   C C   
2004 O O   . VAL   B 118 ? 0.1043 0.1099 0.1320 0.0045  -0.0015 0.0171  124 VAL   C O   
2005 C CB  . VAL   B 118 ? 0.1067 0.1092 0.1205 0.0059  -0.0023 0.0153  124 VAL   C CB  
2006 C CG1 . VAL   B 118 ? 0.1208 0.1243 0.1358 0.0065  -0.0005 0.0169  124 VAL   C CG1 
2007 C CG2 . VAL   B 118 ? 0.1202 0.1204 0.1279 0.0066  -0.0028 0.0135  124 VAL   C CG2 
2008 N N   . SER   B 119 ? 0.0984 0.1055 0.1291 0.0056  0.0008  0.0149  125 SER   C N   
2009 C CA  . SER   B 119 ? 0.0993 0.1078 0.1371 0.0051  0.0022  0.0163  125 SER   C CA  
2010 C C   . SER   B 119 ? 0.1104 0.1199 0.1511 0.0055  0.0042  0.0179  125 SER   C C   
2011 O O   . SER   B 119 ? 0.1144 0.1244 0.1595 0.0053  0.0055  0.0205  125 SER   C O   
2012 C CB  . SER   B 119 ? 0.1019 0.1106 0.1442 0.0047  0.0025  0.0136  125 SER   C CB  
2013 O OG  . SER   B 119 ? 0.1172 0.1267 0.1670 0.0042  0.0043  0.0145  125 SER   C OG  
2014 N N   . THR   B 120 ? 0.1046 0.1144 0.1437 0.0063  0.0048  0.0167  126 THR   C N   
2015 C CA  . THR   B 120 ? 0.1107 0.1216 0.1537 0.0067  0.0074  0.0184  126 THR   C CA  
2016 C C   . THR   B 120 ? 0.1095 0.1193 0.1461 0.0079  0.0081  0.0189  126 THR   C C   
2017 O O   . THR   B 120 ? 0.1151 0.1237 0.1457 0.0083  0.0065  0.0173  126 THR   C O   
2018 C CB  . THR   B 120 ? 0.1075 0.1204 0.1589 0.0065  0.0083  0.0159  126 THR   C CB  
2019 O OG1 . THR   B 120 ? 0.1258 0.1394 0.1755 0.0071  0.0070  0.0132  126 THR   C OG1 
2020 C CG2 . THR   B 120 ? 0.1207 0.1339 0.1774 0.0054  0.0077  0.0143  126 THR   C CG2 
2021 N N   . GLY   B 121 ? 0.1253 0.1353 0.1635 0.0085  0.0110  0.0212  127 GLY   C N   
2022 C CA  . GLY   B 121 ? 0.1465 0.1551 0.1791 0.0097  0.0128  0.0217  127 GLY   C CA  
2023 C C   . GLY   B 121 ? 0.2001 0.2095 0.2377 0.0104  0.0169  0.0239  127 GLY   C C   
2024 O O   . GLY   B 121 ? 0.2108 0.2207 0.2530 0.0099  0.0183  0.0263  127 GLY   C O   
2025 N N   . GLY   B 122 ? 0.2569 0.2663 0.2942 0.0115  0.0192  0.0234  128 GLY   C N   
2026 C CA  . GLY   B 122 ? 0.2869 0.2969 0.3297 0.0123  0.0239  0.0256  128 GLY   C CA  
2027 C C   . GLY   B 122 ? 0.2778 0.2896 0.3259 0.0132  0.0257  0.0238  128 GLY   C C   
2028 O O   . GLY   B 122 ? 0.2726 0.2863 0.3240 0.0129  0.0227  0.0207  128 GLY   C O   
2029 N N   . ASN   B 123 ? 0.2718 0.2830 0.3213 0.0144  0.0306  0.0259  129 ASN   C N   
2030 C CA  . ASN   B 123 ? 0.2672 0.2804 0.3235 0.0155  0.0330  0.0248  129 ASN   C CA  
2031 C C   . ASN   B 123 ? 0.2365 0.2487 0.2866 0.0165  0.0307  0.0221  129 ASN   C C   
2032 O O   . ASN   B 123 ? 0.2641 0.2792 0.3219 0.0171  0.0305  0.0203  129 ASN   C O   
2033 C CB  . ASN   B 123 ? 0.3088 0.3269 0.3802 0.0144  0.0322  0.0232  129 ASN   C CB  
2034 C CG  . ASN   B 123 ? 0.3885 0.4078 0.4696 0.0142  0.0371  0.0259  129 ASN   C CG  
2035 O OD1 . ASN   B 123 ? 0.3975 0.4144 0.4752 0.0155  0.0423  0.0292  129 ASN   C OD1 
2036 N ND2 . ASN   B 123 ? 0.4196 0.4423 0.5132 0.0126  0.0360  0.0246  129 ASN   C ND2 
2037 N N   . GLY   B 124 ? 0.2175 0.2258 0.2549 0.0168  0.0291  0.0220  130 GLY   C N   
2038 C CA  . GLY   B 124 ? 0.2004 0.2072 0.2321 0.0177  0.0271  0.0195  130 GLY   C CA  
2039 C C   . GLY   B 124 ? 0.1700 0.1790 0.2045 0.0167  0.0219  0.0168  130 GLY   C C   
2040 O O   . GLY   B 124 ? 0.1663 0.1748 0.1988 0.0177  0.0204  0.0149  130 GLY   C O   
2041 N N   . LEU   B 125 ? 0.1624 0.1733 0.2010 0.0150  0.0194  0.0167  131 LEU   C N   
2042 C CA  . LEU   B 125 ? 0.1498 0.1623 0.1901 0.0141  0.0148  0.0142  131 LEU   C CA  
2043 C C   . LEU   B 125 ? 0.1488 0.1591 0.1824 0.0129  0.0125  0.0145  131 LEU   C C   
2044 O O   . LEU   B 125 ? 0.1848 0.1938 0.2159 0.0123  0.0138  0.0169  131 LEU   C O   
2045 C CB  . LEU   B 125 ? 0.1709 0.1877 0.2230 0.0132  0.0140  0.0131  131 LEU   C CB  
2046 C CG  . LEU   B 125 ? 0.2104 0.2303 0.2719 0.0142  0.0157  0.0126  131 LEU   C CG  
2047 C CD1 . LEU   B 125 ? 0.2506 0.2742 0.3241 0.0128  0.0157  0.0121  131 LEU   C CD1 
2048 C CD2 . LEU   B 125 ? 0.2216 0.2425 0.2825 0.0154  0.0130  0.0106  131 LEU   C CD2 
2049 N N   . VAL   B 126 ? 0.1158 0.1256 0.1464 0.0125  0.0091  0.0126  132 VAL   C N   
2050 C CA  . VAL   B 126 ? 0.1133 0.1216 0.1397 0.0113  0.0069  0.0127  132 VAL   C CA  
2051 C C   . VAL   B 126 ? 0.1015 0.1117 0.1327 0.0105  0.0045  0.0106  132 VAL   C C   
2052 O O   . VAL   B 126 ? 0.1094 0.1207 0.1420 0.0112  0.0031  0.0086  132 VAL   C O   
2053 C CB  . VAL   B 126 ? 0.1242 0.1290 0.1411 0.0115  0.0055  0.0124  132 VAL   C CB  
2054 C CG1 . VAL   B 126 ? 0.1536 0.1579 0.1691 0.0127  0.0047  0.0104  132 VAL   C CG1 
2055 C CG2 . VAL   B 126 ? 0.1325 0.1363 0.1469 0.0101  0.0031  0.0125  132 VAL   C CG2 
2056 N N   . GLY   B 127 ? 0.0935 0.1040 0.1272 0.0092  0.0040  0.0111  133 GLY   C N   
2057 C CA  . GLY   B 127 ? 0.0929 0.1045 0.1302 0.0085  0.0022  0.0089  133 GLY   C CA  
2058 C C   . GLY   B 127 ? 0.1016 0.1110 0.1339 0.0078  0.0008  0.0088  133 GLY   C C   
2059 O O   . GLY   B 127 ? 0.1060 0.1143 0.1364 0.0073  0.0013  0.0110  133 GLY   C O   
2060 N N   . PHE   B 128 ? 0.0896 0.0986 0.1205 0.0079  -0.0009 0.0066  134 PHE   C N   
2061 C CA  . PHE   B 128 ? 0.0979 0.1047 0.1248 0.0075  -0.0017 0.0064  134 PHE   C CA  
2062 C C   . PHE   B 128 ? 0.0964 0.1034 0.1266 0.0068  -0.0018 0.0046  134 PHE   C C   
2063 O O   . PHE   B 128 ? 0.1035 0.1113 0.1354 0.0070  -0.0026 0.0023  134 PHE   C O   
2064 C CB  . PHE   B 128 ? 0.0987 0.1037 0.1192 0.0085  -0.0030 0.0055  134 PHE   C CB  
2065 C CG  . PHE   B 128 ? 0.0993 0.1036 0.1164 0.0093  -0.0028 0.0065  134 PHE   C CG  
2066 C CD1 . PHE   B 128 ? 0.1000 0.1022 0.1130 0.0088  -0.0025 0.0080  134 PHE   C CD1 
2067 C CD2 . PHE   B 128 ? 0.1059 0.1114 0.1242 0.0106  -0.0027 0.0057  134 PHE   C CD2 
2068 C CE1 . PHE   B 128 ? 0.1144 0.1152 0.1233 0.0096  -0.0021 0.0084  134 PHE   C CE1 
2069 C CE2 . PHE   B 128 ? 0.1104 0.1148 0.1255 0.0116  -0.0018 0.0065  134 PHE   C CE2 
2070 C CZ  . PHE   B 128 ? 0.1134 0.1150 0.1231 0.0111  -0.0014 0.0077  134 PHE   C CZ  
2071 N N   . ALA   B 129 ? 0.0951 0.1010 0.1262 0.0059  -0.0009 0.0057  135 ALA   C N   
2072 C CA  . ALA   B 129 ? 0.0958 0.1009 0.1292 0.0054  -0.0003 0.0039  135 ALA   C CA  
2073 C C   . ALA   B 129 ? 0.1071 0.1099 0.1340 0.0060  -0.0011 0.0024  135 ALA   C C   
2074 O O   . ALA   B 129 ? 0.1170 0.1183 0.1406 0.0060  -0.0009 0.0039  135 ALA   C O   
2075 C CB  . ALA   B 129 ? 0.1060 0.1108 0.1434 0.0045  0.0013  0.0060  135 ALA   C CB  
2076 N N   . ASP   B 130 ? 0.1072 0.1096 0.1324 0.0064  -0.0020 -0.0004 136 ASP   C N   
2077 C CA  . ASP   B 130 ? 0.1124 0.1121 0.1305 0.0073  -0.0026 -0.0016 136 ASP   C CA  
2078 C C   . ASP   B 130 ? 0.1185 0.1156 0.1360 0.0068  -0.0004 -0.0015 136 ASP   C C   
2079 O O   . ASP   B 130 ? 0.1256 0.1228 0.1479 0.0060  0.0012  -0.0021 136 ASP   C O   
2080 C CB  . ASP   B 130 ? 0.1300 0.1300 0.1466 0.0079  -0.0046 -0.0048 136 ASP   C CB  
2081 C CG  . ASP   B 130 ? 0.1667 0.1640 0.1749 0.0091  -0.0056 -0.0057 136 ASP   C CG  
2082 O OD1 . ASP   B 130 ? 0.1580 0.1543 0.1621 0.0101  -0.0058 -0.0039 136 ASP   C OD1 
2083 O OD2 . ASP   B 130 ? 0.1994 0.1950 0.2047 0.0092  -0.0058 -0.0082 136 ASP   C OD2 
2084 N N   . VAL   B 131 ? 0.1184 0.1130 0.1303 0.0074  0.0002  -0.0007 137 VAL   C N   
2085 C CA  . VAL   B 131 ? 0.1236 0.1153 0.1345 0.0072  0.0029  -0.0006 137 VAL   C CA  
2086 C C   . VAL   B 131 ? 0.1386 0.1270 0.1412 0.0084  0.0031  -0.0021 137 VAL   C C   
2087 O O   . VAL   B 131 ? 0.1434 0.1288 0.1441 0.0086  0.0059  -0.0021 137 VAL   C O   
2088 C CB  . VAL   B 131 ? 0.1249 0.1166 0.1388 0.0065  0.0044  0.0024  137 VAL   C CB  
2089 C CG1 . VAL   B 131 ? 0.1279 0.1226 0.1494 0.0055  0.0041  0.0042  137 VAL   C CG1 
2090 C CG2 . VAL   B 131 ? 0.1329 0.1238 0.1423 0.0070  0.0032  0.0038  137 VAL   C CG2 
2091 N N   . ARG   B 132 ? 0.1276 0.1163 0.1253 0.0096  0.0004  -0.0031 138 ARG   C N   
2092 C CA  . ARG   B 132 ? 0.1350 0.1203 0.1239 0.0111  0.0002  -0.0039 138 ARG   C CA  
2093 C C   . ARG   B 132 ? 0.1454 0.1281 0.1301 0.0113  0.0011  -0.0068 138 ARG   C C   
2094 O O   . ARG   B 132 ? 0.1668 0.1456 0.1433 0.0125  0.0021  -0.0069 138 ARG   C O   
2095 C CB  . ARG   B 132 ? 0.1365 0.1233 0.1222 0.0124  -0.0033 -0.0040 138 ARG   C CB  
2096 C CG  . ARG   B 132 ? 0.1289 0.1168 0.1166 0.0125  -0.0035 -0.0013 138 ARG   C CG  
2097 C CD  . ARG   B 132 ? 0.1354 0.1246 0.1208 0.0140  -0.0066 -0.0015 138 ARG   C CD  
2098 N NE  . ARG   B 132 ? 0.1280 0.1212 0.1190 0.0136  -0.0087 -0.0031 138 ARG   C NE  
2099 C CZ  . ARG   B 132 ? 0.1390 0.1346 0.1311 0.0147  -0.0113 -0.0033 138 ARG   C CZ  
2100 N NH1 . ARG   B 132 ? 0.1390 0.1332 0.1263 0.0165  -0.0124 -0.0022 138 ARG   C NH1 
2101 N NH2 . ARG   B 132 ? 0.1447 0.1441 0.1435 0.0140  -0.0126 -0.0046 138 ARG   C NH2 
2102 N N   . ASP   B 133 ? 0.1399 0.1241 0.1295 0.0102  0.0008  -0.0091 139 ASP   C N   
2103 C CA  . ASP   B 133 ? 0.1471 0.1284 0.1329 0.0101  0.0017  -0.0125 139 ASP   C CA  
2104 C C   . ASP   B 133 ? 0.1643 0.1424 0.1514 0.0097  0.0068  -0.0120 139 ASP   C C   
2105 O O   . ASP   B 133 ? 0.1768 0.1512 0.1591 0.0099  0.0085  -0.0148 139 ASP   C O   
2106 C CB  . ASP   B 133 ? 0.1687 0.1525 0.1600 0.0090  -0.0007 -0.0156 139 ASP   C CB  
2107 C CG  . ASP   B 133 ? 0.1747 0.1611 0.1769 0.0075  0.0013  -0.0144 139 ASP   C CG  
2108 O OD1 . ASP   B 133 ? 0.1599 0.1484 0.1661 0.0073  0.0018  -0.0109 139 ASP   C OD1 
2109 O OD2 . ASP   B 133 ? 0.2140 0.1998 0.2204 0.0064  0.0024  -0.0169 139 ASP   C OD2 
2110 N N   . LEU   B 134 ? 0.1545 0.1338 0.1481 0.0090  0.0091  -0.0086 140 LEU   C N   
2111 C CA  . LEU   B 134 ? 0.1542 0.1315 0.1518 0.0086  0.0138  -0.0077 140 LEU   C CA  
2112 C C   . LEU   B 134 ? 0.1602 0.1336 0.1514 0.0097  0.0169  -0.0062 140 LEU   C C   
2113 O O   . LEU   B 134 ? 0.1590 0.1331 0.1535 0.0095  0.0181  -0.0029 140 LEU   C O   
2114 C CB  . LEU   B 134 ? 0.1444 0.1255 0.1527 0.0074  0.0141  -0.0046 140 LEU   C CB  
2115 C CG  . LEU   B 134 ? 0.1534 0.1382 0.1683 0.0064  0.0117  -0.0054 140 LEU   C CG  
2116 C CD1 . LEU   B 134 ? 0.1677 0.1559 0.1913 0.0056  0.0118  -0.0017 140 LEU   C CD1 
2117 C CD2 . LEU   B 134 ? 0.1764 0.1595 0.1936 0.0060  0.0135  -0.0087 140 LEU   C CD2 
2118 N N   . LEU   B 135 ? 0.1680 0.1370 0.1492 0.0108  0.0178  -0.0086 141 LEU   C N   
2119 C CA  . LEU   B 135 ? 0.1827 0.1475 0.1561 0.0122  0.0206  -0.0070 141 LEU   C CA  
2120 C C   . LEU   B 135 ? 0.1779 0.1407 0.1562 0.0120  0.0265  -0.0048 141 LEU   C C   
2121 O O   . LEU   B 135 ? 0.1968 0.1576 0.1729 0.0126  0.0288  -0.0021 141 LEU   C O   
2122 C CB  . LEU   B 135 ? 0.1857 0.1458 0.1460 0.0138  0.0202  -0.0100 141 LEU   C CB  
2123 C CG  . LEU   B 135 ? 0.1929 0.1554 0.1492 0.0140  0.0139  -0.0125 141 LEU   C CG  
2124 C CD1 . LEU   B 135 ? 0.2086 0.1664 0.1513 0.0155  0.0130  -0.0155 141 LEU   C CD1 
2125 C CD2 . LEU   B 135 ? 0.2020 0.1683 0.1601 0.0144  0.0101  -0.0097 141 LEU   C CD2 
2126 N N   . TRP   B 136 ? 0.1766 0.1398 0.1624 0.0110  0.0289  -0.0058 142 TRP   C N   
2127 C CA  . TRP   B 136 ? 0.1914 0.1531 0.1837 0.0109  0.0347  -0.0038 142 TRP   C CA  
2128 C C   . TRP   B 136 ? 0.1940 0.1597 0.1958 0.0099  0.0341  0.0005  142 TRP   C C   
2129 O O   . TRP   B 136 ? 0.2150 0.1797 0.2222 0.0098  0.0384  0.0029  142 TRP   C O   
2130 C CB  . TRP   B 136 ? 0.1897 0.1512 0.1884 0.0102  0.0371  -0.0059 142 TRP   C CB  
2131 C CG  . TRP   B 136 ? 0.1861 0.1526 0.1927 0.0089  0.0329  -0.0063 142 TRP   C CG  
2132 C CD1 . TRP   B 136 ? 0.1993 0.1664 0.2033 0.0085  0.0294  -0.0098 142 TRP   C CD1 
2133 C CD2 . TRP   B 136 ? 0.1825 0.1538 0.2014 0.0078  0.0320  -0.0030 142 TRP   C CD2 
2134 N NE1 . TRP   B 136 ? 0.2003 0.1723 0.2144 0.0073  0.0270  -0.0086 142 TRP   C NE1 
2135 C CE2 . TRP   B 136 ? 0.1886 0.1631 0.2112 0.0070  0.0284  -0.0044 142 TRP   C CE2 
2136 C CE3 . TRP   B 136 ? 0.1860 0.1595 0.2131 0.0074  0.0335  0.0010  142 TRP   C CE3 
2137 C CZ2 . TRP   B 136 ? 0.1818 0.1609 0.2147 0.0060  0.0268  -0.0016 142 TRP   C CZ2 
2138 C CZ3 . TRP   B 136 ? 0.1857 0.1640 0.2233 0.0064  0.0314  0.0035  142 TRP   C CZ3 
2139 C CH2 . TRP   B 136 ? 0.1886 0.1695 0.2283 0.0058  0.0281  0.0023  142 TRP   C CH2 
2140 N N   . LEU   B 137 ? 0.1739 0.1439 0.1779 0.0092  0.0288  0.0015  143 LEU   C N   
2141 C CA  . LEU   B 137 ? 0.1760 0.1492 0.1873 0.0082  0.0278  0.0051  143 LEU   C CA  
2142 C C   . LEU   B 137 ? 0.2111 0.1811 0.2180 0.0088  0.0301  0.0070  143 LEU   C C   
2143 O O   . LEU   B 137 ? 0.2295 0.2010 0.2436 0.0079  0.0308  0.0099  143 LEU   C O   
2144 C CB  . LEU   B 137 ? 0.1670 0.1443 0.1791 0.0075  0.0221  0.0053  143 LEU   C CB  
2145 C CG  . LEU   B 137 ? 0.1601 0.1410 0.1788 0.0066  0.0200  0.0047  143 LEU   C CG  
2146 C CD1 . LEU   B 137 ? 0.1718 0.1558 0.1890 0.0063  0.0151  0.0047  143 LEU   C CD1 
2147 C CD2 . LEU   B 137 ? 0.1693 0.1526 0.1991 0.0056  0.0215  0.0074  143 LEU   C CD2 
2148 N N   . ASP   B 138 ? 0.2023 0.1679 0.1979 0.0104  0.0312  0.0056  144 ASP   C N   
2149 C CA  . ASP   B 138 ? 0.2195 0.1815 0.2100 0.0113  0.0337  0.0077  144 ASP   C CA  
2150 C C   . ASP   B 138 ? 0.2670 0.2250 0.2585 0.0119  0.0407  0.0088  144 ASP   C C   
2151 O O   . ASP   B 138 ? 0.2822 0.2367 0.2699 0.0126  0.0437  0.0108  144 ASP   C O   
2152 C CB  . ASP   B 138 ? 0.2181 0.1771 0.1954 0.0131  0.0317  0.0063  144 ASP   C CB  
2153 C CG  . ASP   B 138 ? 0.2323 0.1949 0.2085 0.0129  0.0254  0.0058  144 ASP   C CG  
2154 O OD1 . ASP   B 138 ? 0.2194 0.1862 0.2039 0.0114  0.0230  0.0067  144 ASP   C OD1 
2155 O OD2 . ASP   B 138 ? 0.2609 0.2219 0.2277 0.0144  0.0231  0.0045  144 ASP   C OD2 
2156 N N   . GLU   B 139 ? 0.2938 0.2517 0.2904 0.0116  0.0438  0.0077  145 GLU   C N   
2157 C CA  . GLU   B 139 ? 0.3528 0.3064 0.3504 0.0124  0.0512  0.0086  145 GLU   C CA  
2158 C C   . GLU   B 139 ? 0.4074 0.3640 0.4195 0.0112  0.0539  0.0098  145 GLU   C C   
2159 O O   . GLU   B 139 ? 0.4151 0.3764 0.4347 0.0100  0.0500  0.0094  145 GLU   C O   
2160 C CB  . GLU   B 139 ? 0.4164 0.3644 0.4010 0.0141  0.0537  0.0051  145 GLU   C CB  
2161 C CG  . GLU   B 139 ? 0.5015 0.4513 0.4876 0.0136  0.0512  0.0014  145 GLU   C CG  
2162 C CD  . GLU   B 139 ? 0.6147 0.5603 0.5870 0.0147  0.0501  -0.0029 145 GLU   C CD  
2163 O OE1 . GLU   B 139 ? 0.6020 0.5474 0.5757 0.0143  0.0501  -0.0062 145 GLU   C OE1 
2164 O OE2 . GLU   B 139 ? 0.6719 0.6144 0.6322 0.0161  0.0490  -0.0030 145 GLU   C OE2 
2165 N N   . GLU   B 140 ? 0.4442 0.3975 0.4597 0.0119  0.0612  0.0112  146 GLU   C N   
2166 C CA  . GLU   B 140 ? 0.4762 0.4310 0.5051 0.0114  0.0654  0.0125  146 GLU   C CA  
2167 C C   . GLU   B 140 ? 0.4897 0.4514 0.5315 0.0097  0.0606  0.0135  146 GLU   C C   
2168 O O   . GLU   B 140 ? 0.4921 0.4549 0.5427 0.0097  0.0631  0.0135  146 GLU   C O   
2169 C CB  . GLU   B 140 ? 0.5264 0.4759 0.5496 0.0129  0.0710  0.0093  146 GLU   C CB  
2170 C CG  . GLU   B 140 ? 0.6145 0.5641 0.6308 0.0128  0.0666  0.0050  146 GLU   C CG  
2171 C CD  . GLU   B 140 ? 0.7312 0.6822 0.7572 0.0124  0.0682  0.0037  146 GLU   C CD  
2172 O OE1 . GLU   B 140 ? 0.7637 0.7139 0.7845 0.0123  0.0656  -0.0001 146 GLU   C OE1 
2173 O OE2 . GLU   B 140 ? 0.7529 0.7059 0.7924 0.0122  0.0719  0.0067  146 GLU   C OE2 
2174 N N1  . A1BQJ C .   ? 0.1766 0.1581 0.2368 0.0237  0.0255  0.0087  201 A1BQJ A N1  
2175 C C4  . A1BQJ C .   ? 0.2223 0.2079 0.2440 0.0134  0.0347  -0.0155 201 A1BQJ A C4  
2176 C C5  . A1BQJ C .   ? 0.2283 0.2110 0.2539 0.0145  0.0337  -0.0148 201 A1BQJ A C5  
2177 C C6  . A1BQJ C .   ? 0.2293 0.2136 0.2515 0.0142  0.0274  -0.0118 201 A1BQJ A C6  
2178 C C7  . A1BQJ C .   ? 0.2211 0.2024 0.2463 0.0146  0.0263  -0.0117 201 A1BQJ A C7  
2179 C C8  . A1BQJ C .   ? 0.2312 0.2081 0.2664 0.0167  0.0320  -0.0123 201 A1BQJ A C8  
2180 C C10 . A1BQJ C .   ? 0.2071 0.1867 0.2496 0.0190  0.0233  -0.0017 201 A1BQJ A C10 
2181 C C13 . A1BQJ C .   ? 0.2396 0.2109 0.2769 0.0157  0.0302  -0.0131 201 A1BQJ A C13 
2182 O O2  . A1BQJ C .   ? 0.2521 0.2194 0.2846 0.0126  0.0328  -0.0197 201 A1BQJ A O2  
2183 C C12 . A1BQJ C .   ? 0.2104 0.1827 0.2524 0.0173  0.0273  -0.0081 201 A1BQJ A C12 
2184 C C11 . A1BQJ C .   ? 0.1951 0.1780 0.2445 0.0210  0.0215  0.0053  201 A1BQJ A C11 
2185 O O1  . A1BQJ C .   ? 0.1854 0.1726 0.2309 0.0200  0.0168  0.0080  201 A1BQJ A O1  
2186 C C9  . A1BQJ C .   ? 0.2138 0.1948 0.2593 0.0205  0.0268  -0.0016 201 A1BQJ A C9  
2187 N N   . A1BQJ C .   ? 0.2309 0.2070 0.2702 0.0178  0.0298  -0.0092 201 A1BQJ A N   
2188 C C1  . A1BQJ C .   ? 0.2253 0.2136 0.2411 0.0131  0.0226  -0.0095 201 A1BQJ A C1  
2189 O O   . A1BQJ C .   ? 0.2404 0.2295 0.2542 0.0129  0.0177  -0.0071 201 A1BQJ A O   
2190 C C   . A1BQJ C .   ? 0.2476 0.2395 0.2554 0.0117  0.0136  -0.0053 201 A1BQJ A C   
2191 C C3  . A1BQJ C .   ? 0.2231 0.2127 0.2377 0.0121  0.0294  -0.0129 201 A1BQJ A C3  
2192 C C2  . A1BQJ C .   ? 0.2158 0.2065 0.2278 0.0121  0.0235  -0.0099 201 A1BQJ A C2  
# 
