data_7HWS
# 
_entry.id   7HWS 
# 
_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   7HWS         pdb_00007hws 10.2210/pdb7hws/pdb 
WWPDB D_1001408028 ?            ?                   
# 
_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                        7HWS 
_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-[(2R)-2-phenyl-2-(phenylsulfanyl)acetyl]piperidine-3-carboxamide' 354.466   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                      78.133    1   ?         ? ? ? 
5 water       nat water                                                                     18.015    317 ?         ? ? ? 
# 
_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-[(2R)-2-phenyl-2-(phenylsulfanyl)acetyl]piperidine-3-carboxamide' A1BOO 
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 
A1BOO non-polymer         . '(3S)-1-[(2R)-2-phenyl-2-(phenylsulfanyl)acetyl]piperidine-3-carboxamide' ? 'C20 H22 N2 O2 S' 354.466 
ALA   'L-peptide linking' y ALANINE                                                                   ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                                                  ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                           ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                  ? 'C3 H7 N O2 S'    121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                      ? 'C2 H6 O S'       78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                 ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                           ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                                   ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                 ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                                     ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                                   ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                                    ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                                ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                             ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                                   ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                                    ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                                 ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                                  ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                                    ? 'C5 H11 N O2'     117.146 
ZN    non-polymer         . 'ZINC ION'                                                                ? 'Zn 2'            65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 ?   ?   ?   C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BOO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BOO 
_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 A1BOO 1   201 201 A1BOO LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 6   DMS   DMS A . 
F 2 A1BOO 1   201 201 A1BOO LIG C . 
G 3 ZN    1   202 1   ZN    ZN  C . 
H 5 HOH   1   301 514 HOH   HOH A . 
H 5 HOH   2   302 128 HOH   HOH A . 
H 5 HOH   3   303 408 HOH   HOH A . 
H 5 HOH   4   304 134 HOH   HOH A . 
H 5 HOH   5   305 511 HOH   HOH A . 
H 5 HOH   6   306 62  HOH   HOH A . 
H 5 HOH   7   307 168 HOH   HOH A . 
H 5 HOH   8   308 87  HOH   HOH A . 
H 5 HOH   9   309 505 HOH   HOH A . 
H 5 HOH   10  310 10  HOH   HOH A . 
H 5 HOH   11  311 474 HOH   HOH A . 
H 5 HOH   12  312 189 HOH   HOH A . 
H 5 HOH   13  313 22  HOH   HOH A . 
H 5 HOH   14  314 443 HOH   HOH A . 
H 5 HOH   15  315 479 HOH   HOH A . 
H 5 HOH   16  316 12  HOH   HOH A . 
H 5 HOH   17  317 426 HOH   HOH A . 
H 5 HOH   18  318 195 HOH   HOH A . 
H 5 HOH   19  319 47  HOH   HOH A . 
H 5 HOH   20  320 2   HOH   HOH A . 
H 5 HOH   21  321 94  HOH   HOH A . 
H 5 HOH   22  322 395 HOH   HOH A . 
H 5 HOH   23  323 52  HOH   HOH A . 
H 5 HOH   24  324 89  HOH   HOH A . 
H 5 HOH   25  325 76  HOH   HOH A . 
H 5 HOH   26  326 40  HOH   HOH A . 
H 5 HOH   27  327 442 HOH   HOH A . 
H 5 HOH   28  328 475 HOH   HOH A . 
H 5 HOH   29  329 272 HOH   HOH A . 
H 5 HOH   30  330 53  HOH   HOH A . 
H 5 HOH   31  331 57  HOH   HOH A . 
H 5 HOH   32  332 29  HOH   HOH A . 
H 5 HOH   33  333 434 HOH   HOH A . 
H 5 HOH   34  334 108 HOH   HOH A . 
H 5 HOH   35  335 424 HOH   HOH A . 
H 5 HOH   36  336 476 HOH   HOH A . 
H 5 HOH   37  337 96  HOH   HOH A . 
H 5 HOH   38  338 234 HOH   HOH A . 
H 5 HOH   39  339 13  HOH   HOH A . 
H 5 HOH   40  340 116 HOH   HOH A . 
H 5 HOH   41  341 490 HOH   HOH A . 
H 5 HOH   42  342 63  HOH   HOH A . 
H 5 HOH   43  343 55  HOH   HOH A . 
H 5 HOH   44  344 120 HOH   HOH A . 
H 5 HOH   45  345 9   HOH   HOH A . 
H 5 HOH   46  346 325 HOH   HOH A . 
H 5 HOH   47  347 81  HOH   HOH A . 
H 5 HOH   48  348 185 HOH   HOH A . 
H 5 HOH   49  349 54  HOH   HOH A . 
H 5 HOH   50  350 184 HOH   HOH A . 
H 5 HOH   51  351 522 HOH   HOH A . 
H 5 HOH   52  352 69  HOH   HOH A . 
H 5 HOH   53  353 229 HOH   HOH A . 
H 5 HOH   54  354 78  HOH   HOH A . 
H 5 HOH   55  355 14  HOH   HOH A . 
H 5 HOH   56  356 436 HOH   HOH A . 
H 5 HOH   57  357 449 HOH   HOH A . 
H 5 HOH   58  358 31  HOH   HOH A . 
H 5 HOH   59  359 60  HOH   HOH A . 
H 5 HOH   60  360 17  HOH   HOH A . 
H 5 HOH   61  361 1   HOH   HOH A . 
H 5 HOH   62  362 140 HOH   HOH A . 
H 5 HOH   63  363 26  HOH   HOH A . 
H 5 HOH   64  364 423 HOH   HOH A . 
H 5 HOH   65  365 48  HOH   HOH A . 
H 5 HOH   66  366 139 HOH   HOH A . 
H 5 HOH   67  367 136 HOH   HOH A . 
H 5 HOH   68  368 239 HOH   HOH A . 
H 5 HOH   69  369 171 HOH   HOH A . 
H 5 HOH   70  370 456 HOH   HOH A . 
H 5 HOH   71  371 41  HOH   HOH A . 
H 5 HOH   72  372 59  HOH   HOH A . 
H 5 HOH   73  373 5   HOH   HOH A . 
H 5 HOH   74  374 91  HOH   HOH A . 
H 5 HOH   75  375 458 HOH   HOH A . 
H 5 HOH   76  376 498 HOH   HOH A . 
H 5 HOH   77  377 173 HOH   HOH A . 
H 5 HOH   78  378 494 HOH   HOH A . 
H 5 HOH   79  379 118 HOH   HOH A . 
H 5 HOH   80  380 472 HOH   HOH A . 
H 5 HOH   81  381 18  HOH   HOH A . 
H 5 HOH   82  382 492 HOH   HOH A . 
H 5 HOH   83  383 170 HOH   HOH A . 
H 5 HOH   84  384 262 HOH   HOH A . 
H 5 HOH   85  385 104 HOH   HOH A . 
H 5 HOH   86  386 166 HOH   HOH A . 
H 5 HOH   87  387 84  HOH   HOH A . 
H 5 HOH   88  388 27  HOH   HOH A . 
H 5 HOH   89  389 482 HOH   HOH A . 
H 5 HOH   90  390 484 HOH   HOH A . 
H 5 HOH   91  391 461 HOH   HOH A . 
H 5 HOH   92  392 450 HOH   HOH A . 
H 5 HOH   93  393 261 HOH   HOH A . 
H 5 HOH   94  394 109 HOH   HOH A . 
H 5 HOH   95  395 507 HOH   HOH A . 
H 5 HOH   96  396 486 HOH   HOH A . 
H 5 HOH   97  397 65  HOH   HOH A . 
H 5 HOH   98  398 480 HOH   HOH A . 
H 5 HOH   99  399 177 HOH   HOH A . 
H 5 HOH   100 400 438 HOH   HOH A . 
H 5 HOH   101 401 451 HOH   HOH A . 
H 5 HOH   102 402 44  HOH   HOH A . 
H 5 HOH   103 403 125 HOH   HOH A . 
H 5 HOH   104 404 463 HOH   HOH A . 
H 5 HOH   105 405 519 HOH   HOH A . 
H 5 HOH   106 406 183 HOH   HOH A . 
H 5 HOH   107 407 38  HOH   HOH A . 
H 5 HOH   108 408 430 HOH   HOH A . 
H 5 HOH   109 409 446 HOH   HOH A . 
H 5 HOH   110 410 122 HOH   HOH A . 
H 5 HOH   111 411 86  HOH   HOH A . 
H 5 HOH   112 412 465 HOH   HOH A . 
H 5 HOH   113 413 6   HOH   HOH A . 
H 5 HOH   114 414 162 HOH   HOH A . 
H 5 HOH   115 415 452 HOH   HOH A . 
H 5 HOH   116 416 99  HOH   HOH A . 
H 5 HOH   117 417 428 HOH   HOH A . 
H 5 HOH   118 418 473 HOH   HOH A . 
H 5 HOH   119 419 148 HOH   HOH A . 
H 5 HOH   120 420 459 HOH   HOH A . 
H 5 HOH   121 421 433 HOH   HOH A . 
H 5 HOH   122 422 51  HOH   HOH A . 
H 5 HOH   123 423 516 HOH   HOH A . 
H 5 HOH   124 424 493 HOH   HOH A . 
H 5 HOH   125 425 470 HOH   HOH A . 
H 5 HOH   126 426 499 HOH   HOH A . 
H 5 HOH   127 427 520 HOH   HOH A . 
H 5 HOH   128 428 203 HOH   HOH A . 
H 5 HOH   129 429 277 HOH   HOH A . 
H 5 HOH   130 430 390 HOH   HOH A . 
H 5 HOH   131 431 196 HOH   HOH A . 
H 5 HOH   132 432 521 HOH   HOH A . 
H 5 HOH   133 433 418 HOH   HOH A . 
H 5 HOH   134 434 515 HOH   HOH A . 
H 5 HOH   135 435 509 HOH   HOH A . 
H 5 HOH   136 436 238 HOH   HOH A . 
H 5 HOH   137 437 508 HOH   HOH A . 
H 5 HOH   138 438 377 HOH   HOH A . 
H 5 HOH   139 439 146 HOH   HOH A . 
H 5 HOH   140 440 512 HOH   HOH A . 
H 5 HOH   141 441 200 HOH   HOH A . 
H 5 HOH   142 442 369 HOH   HOH A . 
H 5 HOH   143 443 256 HOH   HOH A . 
H 5 HOH   144 444 469 HOH   HOH A . 
H 5 HOH   145 445 483 HOH   HOH A . 
H 5 HOH   146 446 487 HOH   HOH A . 
H 5 HOH   147 447 202 HOH   HOH A . 
H 5 HOH   148 448 391 HOH   HOH A . 
H 5 HOH   149 449 513 HOH   HOH A . 
H 5 HOH   150 450 397 HOH   HOH A . 
H 5 HOH   151 451 204 HOH   HOH A . 
H 5 HOH   152 452 243 HOH   HOH A . 
H 5 HOH   153 453 366 HOH   HOH A . 
H 5 HOH   154 454 385 HOH   HOH A . 
H 5 HOH   155 455 421 HOH   HOH A . 
H 5 HOH   156 456 218 HOH   HOH A . 
I 5 HOH   1   301 24  HOH   HOH C . 
I 5 HOH   2   302 517 HOH   HOH C . 
I 5 HOH   3   303 491 HOH   HOH C . 
I 5 HOH   4   304 163 HOH   HOH C . 
I 5 HOH   5   305 85  HOH   HOH C . 
I 5 HOH   6   306 150 HOH   HOH C . 
I 5 HOH   7   307 45  HOH   HOH C . 
I 5 HOH   8   308 43  HOH   HOH C . 
I 5 HOH   9   309 16  HOH   HOH C . 
I 5 HOH   10  310 144 HOH   HOH C . 
I 5 HOH   11  311 111 HOH   HOH C . 
I 5 HOH   12  312 496 HOH   HOH C . 
I 5 HOH   13  313 50  HOH   HOH C . 
I 5 HOH   14  314 174 HOH   HOH C . 
I 5 HOH   15  315 73  HOH   HOH C . 
I 5 HOH   16  316 504 HOH   HOH C . 
I 5 HOH   17  317 130 HOH   HOH C . 
I 5 HOH   18  318 485 HOH   HOH C . 
I 5 HOH   19  319 217 HOH   HOH C . 
I 5 HOH   20  320 503 HOH   HOH C . 
I 5 HOH   21  321 101 HOH   HOH C . 
I 5 HOH   22  322 105 HOH   HOH C . 
I 5 HOH   23  323 445 HOH   HOH C . 
I 5 HOH   24  324 74  HOH   HOH C . 
I 5 HOH   25  325 447 HOH   HOH C . 
I 5 HOH   26  326 250 HOH   HOH C . 
I 5 HOH   27  327 114 HOH   HOH C . 
I 5 HOH   28  328 37  HOH   HOH C . 
I 5 HOH   29  329 500 HOH   HOH C . 
I 5 HOH   30  330 61  HOH   HOH C . 
I 5 HOH   31  331 25  HOH   HOH C . 
I 5 HOH   32  332 464 HOH   HOH C . 
I 5 HOH   33  333 233 HOH   HOH C . 
I 5 HOH   34  334 471 HOH   HOH C . 
I 5 HOH   35  335 432 HOH   HOH C . 
I 5 HOH   36  336 425 HOH   HOH C . 
I 5 HOH   37  337 266 HOH   HOH C . 
I 5 HOH   38  338 117 HOH   HOH C . 
I 5 HOH   39  339 219 HOH   HOH C . 
I 5 HOH   40  340 19  HOH   HOH C . 
I 5 HOH   41  341 143 HOH   HOH C . 
I 5 HOH   42  342 237 HOH   HOH C . 
I 5 HOH   43  343 455 HOH   HOH C . 
I 5 HOH   44  344 165 HOH   HOH C . 
I 5 HOH   45  345 497 HOH   HOH C . 
I 5 HOH   46  346 4   HOH   HOH C . 
I 5 HOH   47  347 131 HOH   HOH C . 
I 5 HOH   48  348 501 HOH   HOH C . 
I 5 HOH   49  349 441 HOH   HOH C . 
I 5 HOH   50  350 39  HOH   HOH C . 
I 5 HOH   51  351 82  HOH   HOH C . 
I 5 HOH   52  352 20  HOH   HOH C . 
I 5 HOH   53  353 265 HOH   HOH C . 
I 5 HOH   54  354 72  HOH   HOH C . 
I 5 HOH   55  355 280 HOH   HOH C . 
I 5 HOH   56  356 71  HOH   HOH C . 
I 5 HOH   57  357 457 HOH   HOH C . 
I 5 HOH   58  358 98  HOH   HOH C . 
I 5 HOH   59  359 33  HOH   HOH C . 
I 5 HOH   60  360 75  HOH   HOH C . 
I 5 HOH   61  361 468 HOH   HOH C . 
I 5 HOH   62  362 440 HOH   HOH C . 
I 5 HOH   63  363 32  HOH   HOH C . 
I 5 HOH   64  364 178 HOH   HOH C . 
I 5 HOH   65  365 502 HOH   HOH C . 
I 5 HOH   66  366 422 HOH   HOH C . 
I 5 HOH   67  367 209 HOH   HOH C . 
I 5 HOH   68  368 95  HOH   HOH C . 
I 5 HOH   69  369 34  HOH   HOH C . 
I 5 HOH   70  370 46  HOH   HOH C . 
I 5 HOH   71  371 478 HOH   HOH C . 
I 5 HOH   72  372 429 HOH   HOH C . 
I 5 HOH   73  373 444 HOH   HOH C . 
I 5 HOH   74  374 439 HOH   HOH C . 
I 5 HOH   75  375 88  HOH   HOH C . 
I 5 HOH   76  376 495 HOH   HOH C . 
I 5 HOH   77  377 23  HOH   HOH C . 
I 5 HOH   78  378 460 HOH   HOH C . 
I 5 HOH   79  379 453 HOH   HOH C . 
I 5 HOH   80  380 112 HOH   HOH C . 
I 5 HOH   81  381 80  HOH   HOH C . 
I 5 HOH   82  382 8   HOH   HOH C . 
I 5 HOH   83  383 435 HOH   HOH C . 
I 5 HOH   84  384 3   HOH   HOH C . 
I 5 HOH   85  385 510 HOH   HOH C . 
I 5 HOH   86  386 372 HOH   HOH C . 
I 5 HOH   87  387 381 HOH   HOH C . 
I 5 HOH   88  388 68  HOH   HOH C . 
I 5 HOH   89  389 126 HOH   HOH C . 
I 5 HOH   90  390 462 HOH   HOH C . 
I 5 HOH   91  391 467 HOH   HOH C . 
I 5 HOH   92  392 42  HOH   HOH C . 
I 5 HOH   93  393 506 HOH   HOH C . 
I 5 HOH   94  394 437 HOH   HOH C . 
I 5 HOH   95  395 466 HOH   HOH C . 
I 5 HOH   96  396 7   HOH   HOH C . 
I 5 HOH   97  397 113 HOH   HOH C . 
I 5 HOH   98  398 153 HOH   HOH C . 
I 5 HOH   99  399 489 HOH   HOH C . 
I 5 HOH   100 400 15  HOH   HOH C . 
I 5 HOH   101 401 58  HOH   HOH C . 
I 5 HOH   102 402 36  HOH   HOH C . 
I 5 HOH   103 403 49  HOH   HOH C . 
I 5 HOH   104 404 386 HOH   HOH C . 
I 5 HOH   105 405 431 HOH   HOH C . 
I 5 HOH   106 406 477 HOH   HOH C . 
I 5 HOH   107 407 172 HOH   HOH C . 
I 5 HOH   108 408 454 HOH   HOH C . 
I 5 HOH   109 409 147 HOH   HOH C . 
I 5 HOH   110 410 315 HOH   HOH C . 
I 5 HOH   111 411 137 HOH   HOH C . 
I 5 HOH   112 412 488 HOH   HOH C . 
I 5 HOH   113 413 35  HOH   HOH C . 
I 5 HOH   114 414 448 HOH   HOH C . 
I 5 HOH   115 415 77  HOH   HOH C . 
I 5 HOH   116 416 11  HOH   HOH C . 
I 5 HOH   117 417 115 HOH   HOH C . 
I 5 HOH   118 418 481 HOH   HOH C . 
I 5 HOH   119 419 127 HOH   HOH C . 
I 5 HOH   120 420 106 HOH   HOH C . 
I 5 HOH   121 421 221 HOH   HOH C . 
I 5 HOH   122 422 30  HOH   HOH C . 
I 5 HOH   123 423 66  HOH   HOH C . 
I 5 HOH   124 424 97  HOH   HOH C . 
I 5 HOH   125 425 145 HOH   HOH C . 
I 5 HOH   126 426 119 HOH   HOH C . 
I 5 HOH   127 427 21  HOH   HOH C . 
I 5 HOH   128 428 210 HOH   HOH C . 
I 5 HOH   129 429 267 HOH   HOH C . 
I 5 HOH   130 430 192 HOH   HOH C . 
I 5 HOH   131 431 181 HOH   HOH C . 
I 5 HOH   132 432 393 HOH   HOH C . 
I 5 HOH   133 433 367 HOH   HOH C . 
I 5 HOH   134 434 28  HOH   HOH C . 
I 5 HOH   135 435 374 HOH   HOH C . 
I 5 HOH   136 436 373 HOH   HOH C . 
I 5 HOH   137 437 305 HOH   HOH C . 
I 5 HOH   138 438 201 HOH   HOH C . 
I 5 HOH   139 439 518 HOH   HOH C . 
I 5 HOH   140 440 224 HOH   HOH C . 
I 5 HOH   141 441 102 HOH   HOH C . 
I 5 HOH   142 442 370 HOH   HOH C . 
I 5 HOH   143 443 211 HOH   HOH C . 
I 5 HOH   144 444 271 HOH   HOH C . 
I 5 HOH   145 445 400 HOH   HOH C . 
I 5 HOH   146 446 382 HOH   HOH C . 
I 5 HOH   147 447 396 HOH   HOH C . 
I 5 HOH   148 448 230 HOH   HOH C . 
I 5 HOH   149 449 67  HOH   HOH C . 
I 5 HOH   150 450 380 HOH   HOH C . 
I 5 HOH   151 451 394 HOH   HOH C . 
I 5 HOH   152 452 167 HOH   HOH C . 
I 5 HOH   153 453 154 HOH   HOH C . 
I 5 HOH   154 454 384 HOH   HOH C . 
I 5 HOH   155 455 406 HOH   HOH C . 
I 5 HOH   156 456 398 HOH   HOH C . 
I 5 HOH   157 457 368 HOH   HOH C . 
I 5 HOH   158 458 110 HOH   HOH C . 
I 5 HOH   159 459 379 HOH   HOH C . 
I 5 HOH   160 460 376 HOH   HOH C . 
I 5 HOH   161 461 286 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           7HWS 
_cell.length_a           72.695 
_cell.length_b           61.881 
_cell.length_c           65.165 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.81 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HWS 
_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          7HWS 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.30 
_exptl_crystal.density_percent_sol   46.59 
_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                     7HWS 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             32.54 
_reflns.d_resolution_high            1.29 
_reflns.number_obs                   68643 
_reflns.percent_possible_obs         94.5 
_reflns.pdbx_Rmerge_I_obs            0.069 
_reflns.pdbx_netI_over_sigmaI        11.1 
_reflns.pdbx_redundancy              5.7 
_reflns.pdbx_Rrim_I_all              0.075 
_reflns.pdbx_Rpim_I_all              0.030 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     394688 
_reflns.pdbx_chi_squared             0.50 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.29 
_reflns_shell.d_res_low                   1.31 
_reflns_shell.number_measured_all         5836 
_reflns_shell.number_unique_obs           2119 
_reflns_shell.Rmerge_I_obs                1.220 
_reflns_shell.pdbx_chi_squared            0.13 
_reflns_shell.pdbx_redundancy             2.8 
_reflns_shell.percent_possible_obs        57.5 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.3 
_reflns_shell.pdbx_Rrim_I_all             1.529 
_reflns_shell.pdbx_Rpim_I_all             0.896 
_reflns_shell.pdbx_CC_half                0.294 
_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                                 7HWS 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     68202 
_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                             18.80 
_refine.ls_d_res_high                            1.290 
_refine.ls_percent_reflns_obs                    94.1 
_refine.ls_R_factor_obs                          0.1998 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1989 
_refine.ls_R_factor_R_free                       0.2253 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 3.320 
_refine.ls_number_reflns_R_free                  2265 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.955 
_refine.B_iso_mean                               22.92 
_refine.aniso_B[1][1]                            -0.86110 
_refine.aniso_B[2][2]                            0.59770 
_refine.aniso_B[3][3]                            0.26340 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.27290 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.054 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.057 
_refine.pdbx_overall_SU_R_Blow_DPI               0.057 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.059 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HWS 
_refine_analyze.Luzzati_coordinate_error_obs    0.18 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_refine_hist.number_atoms_solvent             317 
_refine_hist.number_atoms_total               2521 
_refine_hist.d_res_high                       1.290 
_refine_hist.d_res_low                        18.80 
# 
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  2265 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.09  ? 2.00  3081 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  756  '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  418  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2265 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.70  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.20 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  278  '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  2001 '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                       1.29 
_refine_ls_shell.d_res_low                        1.31 
_refine_ls_shell.number_reflns_R_work             1318 
_refine_ls_shell.R_factor_R_work                  0.3585 
_refine_ls_shell.percent_reflns_obs               51.09 
_refine_ls_shell.R_factor_R_free                  0.3524 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            3.44 
_refine_ls_shell.number_reflns_R_free             47 
_refine_ls_shell.number_reflns_all                1365 
_refine_ls_shell.R_factor_all                     0.3583 
# 
_struct.entry_id                  7HWS 
_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-0034383-001 (A71EV2A-x3986)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HWS 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 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 7HWS A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HWS 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 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P6  AA6 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P7  AA7 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P8  AA8 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P9  AA9 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P10 AB1 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P11 AB2 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 ? ? ? ? ? ? ? 2.334 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.283 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.311 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 G ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
# 
_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_555 110.3 ? 
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_555 107.0 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.0 ? 
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_555 108.9 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 103.0 ? 
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_555 112.5 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.4 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.4 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 116.6 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 107.9 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 102.1 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 113.1 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O 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                   7HWS 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    349 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    357 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.11 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    C 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -132.65 
_pdbx_validate_torsion.psi             -30.08 
# 
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 14.9941 7.7042   14.3586 -0.0228 -0.0231 -0.0112 -0.0004 0.0097 -0.0026 1.0963 1.4454 0.5575 
0.7065  -0.3268 -0.2391 -0.0496 0.0085  0.0926 -0.0333 0.0582 -0.0493 0.0337  -0.0508 -0.0086 
'X-RAY DIFFRACTION' 2 ? refined 19.4631 -23.0926 18.3450 -0.0157 -0.0142 -0.0095 -0.0035 0.0043 0.0050  0.6760 1.2002 0.4875 
-0.3777 0.1272  0.0999  -0.0352 -0.0264 0.0550 -0.0454 0.0516 0.0411  -0.0190 0.0150  -0.0164 
# 
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_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 454 ? 5.84 . 
2 1 O ? A HOH 455 ? 6.17 . 
3 1 O ? A HOH 456 ? 6.19 . 
4 1 O ? C HOH 461 ? 8.39 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 146 ? A GLU 140 
2  1 Y 1 A ALA 147 ? A ALA 141 
3  1 Y 1 A MET 148 ? A MET 142 
4  1 Y 1 A GLU 149 ? A GLU 143 
5  1 Y 1 A GLN 150 ? A GLN 144 
6  1 Y 1 C GLU 146 ? B GLU 140 
7  1 Y 1 C ALA 147 ? B ALA 141 
8  1 Y 1 C MET 148 ? B MET 142 
9  1 Y 1 C GLU 149 ? B GLU 143 
10 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BOO N1   N  N N 1   
A1BOO C4   C  N N 2   
A1BOO C5   C  N N 3   
A1BOO C6   C  N S 4   
A1BOO C7   C  Y N 5   
A1BOO C8   C  Y N 6   
A1BOO C10  C  Y N 7   
A1BOO C13  C  Y N 8   
A1BOO C15  C  Y N 9   
A1BOO C17  C  Y N 10  
A1BOO O1   O  N N 11  
A1BOO C3   C  N N 12  
A1BOO C2   C  N N 13  
A1BOO C19  C  N N 14  
A1BOO C1   C  N S 15  
A1BOO C    C  N N 16  
A1BOO O    O  N N 17  
A1BOO N    N  N N 18  
A1BOO C18  C  Y N 19  
A1BOO C16  C  Y N 20  
A1BOO C14  C  Y N 21  
A1BOO S    S  N N 22  
A1BOO C12  C  Y N 23  
A1BOO C11  C  Y N 24  
A1BOO C9   C  Y N 25  
A1BOO H8   H  N N 26  
A1BOO H9   H  N N 27  
A1BOO H1   H  N N 28  
A1BOO H10  H  N N 29  
A1BOO H12  H  N N 30  
A1BOO H16  H  N N 31  
A1BOO H18  H  N N 32  
A1BOO H7   H  N N 33  
A1BOO H6   H  N N 34  
A1BOO H5   H  N N 35  
A1BOO H4   H  N N 36  
A1BOO H21  H  N N 37  
A1BOO H20  H  N N 38  
A1BOO H    H  N N 39  
A1BOO H2   H  N N 40  
A1BOO H3   H  N N 41  
A1BOO H19  H  N N 42  
A1BOO H17  H  N N 43  
A1BOO H15  H  N N 44  
A1BOO H14  H  N N 45  
A1BOO H13  H  N N 46  
A1BOO H11  H  N N 47  
ALA   N    N  N N 48  
ALA   CA   C  N S 49  
ALA   C    C  N N 50  
ALA   O    O  N N 51  
ALA   CB   C  N N 52  
ALA   OXT  O  N N 53  
ALA   H    H  N N 54  
ALA   H2   H  N N 55  
ALA   HA   H  N N 56  
ALA   HB1  H  N N 57  
ALA   HB2  H  N N 58  
ALA   HB3  H  N N 59  
ALA   HXT  H  N N 60  
ARG   N    N  N N 61  
ARG   CA   C  N S 62  
ARG   C    C  N N 63  
ARG   O    O  N N 64  
ARG   CB   C  N N 65  
ARG   CG   C  N N 66  
ARG   CD   C  N N 67  
ARG   NE   N  N N 68  
ARG   CZ   C  N N 69  
ARG   NH1  N  N N 70  
ARG   NH2  N  N N 71  
ARG   OXT  O  N N 72  
ARG   H    H  N N 73  
ARG   H2   H  N N 74  
ARG   HA   H  N N 75  
ARG   HB2  H  N N 76  
ARG   HB3  H  N N 77  
ARG   HG2  H  N N 78  
ARG   HG3  H  N N 79  
ARG   HD2  H  N N 80  
ARG   HD3  H  N N 81  
ARG   HE   H  N N 82  
ARG   HH11 H  N N 83  
ARG   HH12 H  N N 84  
ARG   HH21 H  N N 85  
ARG   HH22 H  N N 86  
ARG   HXT  H  N N 87  
ASN   N    N  N N 88  
ASN   CA   C  N S 89  
ASN   C    C  N N 90  
ASN   O    O  N N 91  
ASN   CB   C  N N 92  
ASN   CG   C  N N 93  
ASN   OD1  O  N N 94  
ASN   ND2  N  N N 95  
ASN   OXT  O  N N 96  
ASN   H    H  N N 97  
ASN   H2   H  N N 98  
ASN   HA   H  N N 99  
ASN   HB2  H  N N 100 
ASN   HB3  H  N N 101 
ASN   HD21 H  N N 102 
ASN   HD22 H  N N 103 
ASN   HXT  H  N N 104 
ASP   N    N  N N 105 
ASP   CA   C  N S 106 
ASP   C    C  N N 107 
ASP   O    O  N N 108 
ASP   CB   C  N N 109 
ASP   CG   C  N N 110 
ASP   OD1  O  N N 111 
ASP   OD2  O  N N 112 
ASP   OXT  O  N N 113 
ASP   H    H  N N 114 
ASP   H2   H  N N 115 
ASP   HA   H  N N 116 
ASP   HB2  H  N N 117 
ASP   HB3  H  N N 118 
ASP   HD2  H  N N 119 
ASP   HXT  H  N N 120 
CYS   N    N  N N 121 
CYS   CA   C  N R 122 
CYS   C    C  N N 123 
CYS   O    O  N N 124 
CYS   CB   C  N N 125 
CYS   SG   S  N N 126 
CYS   OXT  O  N N 127 
CYS   H    H  N N 128 
CYS   H2   H  N N 129 
CYS   HA   H  N N 130 
CYS   HB2  H  N N 131 
CYS   HB3  H  N N 132 
CYS   HG   H  N N 133 
CYS   HXT  H  N N 134 
DMS   S    S  N N 135 
DMS   O    O  N N 136 
DMS   C1   C  N N 137 
DMS   C2   C  N N 138 
DMS   H11  H  N N 139 
DMS   H12  H  N N 140 
DMS   H13  H  N N 141 
DMS   H21  H  N N 142 
DMS   H22  H  N N 143 
DMS   H23  H  N N 144 
GLN   N    N  N N 145 
GLN   CA   C  N S 146 
GLN   C    C  N N 147 
GLN   O    O  N N 148 
GLN   CB   C  N N 149 
GLN   CG   C  N N 150 
GLN   CD   C  N N 151 
GLN   OE1  O  N N 152 
GLN   NE2  N  N N 153 
GLN   OXT  O  N N 154 
GLN   H    H  N N 155 
GLN   H2   H  N N 156 
GLN   HA   H  N N 157 
GLN   HB2  H  N N 158 
GLN   HB3  H  N N 159 
GLN   HG2  H  N N 160 
GLN   HG3  H  N N 161 
GLN   HE21 H  N N 162 
GLN   HE22 H  N N 163 
GLN   HXT  H  N N 164 
GLU   N    N  N N 165 
GLU   CA   C  N S 166 
GLU   C    C  N N 167 
GLU   O    O  N N 168 
GLU   CB   C  N N 169 
GLU   CG   C  N N 170 
GLU   CD   C  N N 171 
GLU   OE1  O  N N 172 
GLU   OE2  O  N N 173 
GLU   OXT  O  N N 174 
GLU   H    H  N N 175 
GLU   H2   H  N N 176 
GLU   HA   H  N N 177 
GLU   HB2  H  N N 178 
GLU   HB3  H  N N 179 
GLU   HG2  H  N N 180 
GLU   HG3  H  N N 181 
GLU   HE2  H  N N 182 
GLU   HXT  H  N N 183 
GLY   N    N  N N 184 
GLY   CA   C  N N 185 
GLY   C    C  N N 186 
GLY   O    O  N N 187 
GLY   OXT  O  N N 188 
GLY   H    H  N N 189 
GLY   H2   H  N N 190 
GLY   HA2  H  N N 191 
GLY   HA3  H  N N 192 
GLY   HXT  H  N N 193 
HIS   N    N  N N 194 
HIS   CA   C  N S 195 
HIS   C    C  N N 196 
HIS   O    O  N N 197 
HIS   CB   C  N N 198 
HIS   CG   C  Y N 199 
HIS   ND1  N  Y N 200 
HIS   CD2  C  Y N 201 
HIS   CE1  C  Y N 202 
HIS   NE2  N  Y N 203 
HIS   OXT  O  N N 204 
HIS   H    H  N N 205 
HIS   H2   H  N N 206 
HIS   HA   H  N N 207 
HIS   HB2  H  N N 208 
HIS   HB3  H  N N 209 
HIS   HD1  H  N N 210 
HIS   HD2  H  N N 211 
HIS   HE1  H  N N 212 
HIS   HE2  H  N N 213 
HIS   HXT  H  N N 214 
HOH   O    O  N N 215 
HOH   H1   H  N N 216 
HOH   H2   H  N N 217 
ILE   N    N  N N 218 
ILE   CA   C  N S 219 
ILE   C    C  N N 220 
ILE   O    O  N N 221 
ILE   CB   C  N S 222 
ILE   CG1  C  N N 223 
ILE   CG2  C  N N 224 
ILE   CD1  C  N N 225 
ILE   OXT  O  N N 226 
ILE   H    H  N N 227 
ILE   H2   H  N N 228 
ILE   HA   H  N N 229 
ILE   HB   H  N N 230 
ILE   HG12 H  N N 231 
ILE   HG13 H  N N 232 
ILE   HG21 H  N N 233 
ILE   HG22 H  N N 234 
ILE   HG23 H  N N 235 
ILE   HD11 H  N N 236 
ILE   HD12 H  N N 237 
ILE   HD13 H  N N 238 
ILE   HXT  H  N N 239 
LEU   N    N  N N 240 
LEU   CA   C  N S 241 
LEU   C    C  N N 242 
LEU   O    O  N N 243 
LEU   CB   C  N N 244 
LEU   CG   C  N N 245 
LEU   CD1  C  N N 246 
LEU   CD2  C  N N 247 
LEU   OXT  O  N N 248 
LEU   H    H  N N 249 
LEU   H2   H  N N 250 
LEU   HA   H  N N 251 
LEU   HB2  H  N N 252 
LEU   HB3  H  N N 253 
LEU   HG   H  N N 254 
LEU   HD11 H  N N 255 
LEU   HD12 H  N N 256 
LEU   HD13 H  N N 257 
LEU   HD21 H  N N 258 
LEU   HD22 H  N N 259 
LEU   HD23 H  N N 260 
LEU   HXT  H  N N 261 
LYS   N    N  N N 262 
LYS   CA   C  N S 263 
LYS   C    C  N N 264 
LYS   O    O  N N 265 
LYS   CB   C  N N 266 
LYS   CG   C  N N 267 
LYS   CD   C  N N 268 
LYS   CE   C  N N 269 
LYS   NZ   N  N N 270 
LYS   OXT  O  N N 271 
LYS   H    H  N N 272 
LYS   H2   H  N N 273 
LYS   HA   H  N N 274 
LYS   HB2  H  N N 275 
LYS   HB3  H  N N 276 
LYS   HG2  H  N N 277 
LYS   HG3  H  N N 278 
LYS   HD2  H  N N 279 
LYS   HD3  H  N N 280 
LYS   HE2  H  N N 281 
LYS   HE3  H  N N 282 
LYS   HZ1  H  N N 283 
LYS   HZ2  H  N N 284 
LYS   HZ3  H  N N 285 
LYS   HXT  H  N N 286 
MET   N    N  N N 287 
MET   CA   C  N S 288 
MET   C    C  N N 289 
MET   O    O  N N 290 
MET   CB   C  N N 291 
MET   CG   C  N N 292 
MET   SD   S  N N 293 
MET   CE   C  N N 294 
MET   OXT  O  N N 295 
MET   H    H  N N 296 
MET   H2   H  N N 297 
MET   HA   H  N N 298 
MET   HB2  H  N N 299 
MET   HB3  H  N N 300 
MET   HG2  H  N N 301 
MET   HG3  H  N N 302 
MET   HE1  H  N N 303 
MET   HE2  H  N N 304 
MET   HE3  H  N N 305 
MET   HXT  H  N N 306 
PHE   N    N  N N 307 
PHE   CA   C  N S 308 
PHE   C    C  N N 309 
PHE   O    O  N N 310 
PHE   CB   C  N N 311 
PHE   CG   C  Y N 312 
PHE   CD1  C  Y N 313 
PHE   CD2  C  Y N 314 
PHE   CE1  C  Y N 315 
PHE   CE2  C  Y N 316 
PHE   CZ   C  Y N 317 
PHE   OXT  O  N N 318 
PHE   H    H  N N 319 
PHE   H2   H  N N 320 
PHE   HA   H  N N 321 
PHE   HB2  H  N N 322 
PHE   HB3  H  N N 323 
PHE   HD1  H  N N 324 
PHE   HD2  H  N N 325 
PHE   HE1  H  N N 326 
PHE   HE2  H  N N 327 
PHE   HZ   H  N N 328 
PHE   HXT  H  N N 329 
PRO   N    N  N N 330 
PRO   CA   C  N S 331 
PRO   C    C  N N 332 
PRO   O    O  N N 333 
PRO   CB   C  N N 334 
PRO   CG   C  N N 335 
PRO   CD   C  N N 336 
PRO   OXT  O  N N 337 
PRO   H    H  N N 338 
PRO   HA   H  N N 339 
PRO   HB2  H  N N 340 
PRO   HB3  H  N N 341 
PRO   HG2  H  N N 342 
PRO   HG3  H  N N 343 
PRO   HD2  H  N N 344 
PRO   HD3  H  N N 345 
PRO   HXT  H  N N 346 
SER   N    N  N N 347 
SER   CA   C  N S 348 
SER   C    C  N N 349 
SER   O    O  N N 350 
SER   CB   C  N N 351 
SER   OG   O  N N 352 
SER   OXT  O  N N 353 
SER   H    H  N N 354 
SER   H2   H  N N 355 
SER   HA   H  N N 356 
SER   HB2  H  N N 357 
SER   HB3  H  N N 358 
SER   HG   H  N N 359 
SER   HXT  H  N N 360 
THR   N    N  N N 361 
THR   CA   C  N S 362 
THR   C    C  N N 363 
THR   O    O  N N 364 
THR   CB   C  N R 365 
THR   OG1  O  N N 366 
THR   CG2  C  N N 367 
THR   OXT  O  N N 368 
THR   H    H  N N 369 
THR   H2   H  N N 370 
THR   HA   H  N N 371 
THR   HB   H  N N 372 
THR   HG1  H  N N 373 
THR   HG21 H  N N 374 
THR   HG22 H  N N 375 
THR   HG23 H  N N 376 
THR   HXT  H  N N 377 
TRP   N    N  N N 378 
TRP   CA   C  N S 379 
TRP   C    C  N N 380 
TRP   O    O  N N 381 
TRP   CB   C  N N 382 
TRP   CG   C  Y N 383 
TRP   CD1  C  Y N 384 
TRP   CD2  C  Y N 385 
TRP   NE1  N  Y N 386 
TRP   CE2  C  Y N 387 
TRP   CE3  C  Y N 388 
TRP   CZ2  C  Y N 389 
TRP   CZ3  C  Y N 390 
TRP   CH2  C  Y N 391 
TRP   OXT  O  N N 392 
TRP   H    H  N N 393 
TRP   H2   H  N N 394 
TRP   HA   H  N N 395 
TRP   HB2  H  N N 396 
TRP   HB3  H  N N 397 
TRP   HD1  H  N N 398 
TRP   HE1  H  N N 399 
TRP   HE3  H  N N 400 
TRP   HZ2  H  N N 401 
TRP   HZ3  H  N N 402 
TRP   HH2  H  N N 403 
TRP   HXT  H  N N 404 
TYR   N    N  N N 405 
TYR   CA   C  N S 406 
TYR   C    C  N N 407 
TYR   O    O  N N 408 
TYR   CB   C  N N 409 
TYR   CG   C  Y N 410 
TYR   CD1  C  Y N 411 
TYR   CD2  C  Y N 412 
TYR   CE1  C  Y N 413 
TYR   CE2  C  Y N 414 
TYR   CZ   C  Y N 415 
TYR   OH   O  N N 416 
TYR   OXT  O  N N 417 
TYR   H    H  N N 418 
TYR   H2   H  N N 419 
TYR   HA   H  N N 420 
TYR   HB2  H  N N 421 
TYR   HB3  H  N N 422 
TYR   HD1  H  N N 423 
TYR   HD2  H  N N 424 
TYR   HE1  H  N N 425 
TYR   HE2  H  N N 426 
TYR   HH   H  N N 427 
TYR   HXT  H  N N 428 
VAL   N    N  N N 429 
VAL   CA   C  N S 430 
VAL   C    C  N N 431 
VAL   O    O  N N 432 
VAL   CB   C  N N 433 
VAL   CG1  C  N N 434 
VAL   CG2  C  N N 435 
VAL   OXT  O  N N 436 
VAL   H    H  N N 437 
VAL   H2   H  N N 438 
VAL   HA   H  N N 439 
VAL   HB   H  N N 440 
VAL   HG11 H  N N 441 
VAL   HG12 H  N N 442 
VAL   HG13 H  N N 443 
VAL   HG21 H  N N 444 
VAL   HG22 H  N N 445 
VAL   HG23 H  N N 446 
VAL   HXT  H  N N 447 
ZN    ZN   ZN N N 448 
# 
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 
A1BOO N   C    sing N N 1   
A1BOO O   C    doub N N 2   
A1BOO C   C1   sing N N 3   
A1BOO C1  C2   sing N N 4   
A1BOO C2  C3   sing N N 5   
A1BOO C3  C4   sing N N 6   
A1BOO C4  N1   sing N N 7   
A1BOO N1  C5   sing N N 8   
A1BOO C5  O1   doub N N 9   
A1BOO C6  C5   sing N N 10  
A1BOO S   C6   sing N N 11  
A1BOO C7  S    sing N N 12  
A1BOO C7  C8   doub Y N 13  
A1BOO C8  C9   sing Y N 14  
A1BOO C9  C10  doub Y N 15  
A1BOO C10 C11  sing Y N 16  
A1BOO C11 C12  doub Y N 17  
A1BOO C12 C7   sing Y N 18  
A1BOO C13 C6   sing N N 19  
A1BOO C13 C14  doub Y N 20  
A1BOO C14 C15  sing Y N 21  
A1BOO C15 C16  doub Y N 22  
A1BOO C16 C17  sing Y N 23  
A1BOO C17 C18  doub Y N 24  
A1BOO C18 C13  sing Y N 25  
A1BOO C19 N1   sing N N 26  
A1BOO C1  C19  sing N N 27  
A1BOO C4  H8   sing N N 28  
A1BOO C4  H9   sing N N 29  
A1BOO C6  H1   sing N N 30  
A1BOO C8  H10  sing N N 31  
A1BOO C10 H12  sing N N 32  
A1BOO C15 H16  sing N N 33  
A1BOO C17 H18  sing N N 34  
A1BOO C3  H7   sing N N 35  
A1BOO C3  H6   sing N N 36  
A1BOO C2  H5   sing N N 37  
A1BOO C2  H4   sing N N 38  
A1BOO C19 H21  sing N N 39  
A1BOO C19 H20  sing N N 40  
A1BOO C1  H    sing N N 41  
A1BOO N   H2   sing N N 42  
A1BOO N   H3   sing N N 43  
A1BOO C18 H19  sing N N 44  
A1BOO C16 H17  sing N N 45  
A1BOO C14 H15  sing N N 46  
A1BOO C12 H14  sing N N 47  
A1BOO C11 H13  sing N N 48  
A1BOO C9  H11  sing N N 49  
ALA   N   CA   sing N N 50  
ALA   N   H    sing N N 51  
ALA   N   H2   sing N N 52  
ALA   CA  C    sing N N 53  
ALA   CA  CB   sing N N 54  
ALA   CA  HA   sing N N 55  
ALA   C   O    doub N N 56  
ALA   C   OXT  sing N N 57  
ALA   CB  HB1  sing N N 58  
ALA   CB  HB2  sing N N 59  
ALA   CB  HB3  sing N N 60  
ALA   OXT HXT  sing N N 61  
ARG   N   CA   sing N N 62  
ARG   N   H    sing N N 63  
ARG   N   H2   sing N N 64  
ARG   CA  C    sing N N 65  
ARG   CA  CB   sing N N 66  
ARG   CA  HA   sing N N 67  
ARG   C   O    doub N N 68  
ARG   C   OXT  sing N N 69  
ARG   CB  CG   sing N N 70  
ARG   CB  HB2  sing N N 71  
ARG   CB  HB3  sing N N 72  
ARG   CG  CD   sing N N 73  
ARG   CG  HG2  sing N N 74  
ARG   CG  HG3  sing N N 75  
ARG   CD  NE   sing N N 76  
ARG   CD  HD2  sing N N 77  
ARG   CD  HD3  sing N N 78  
ARG   NE  CZ   sing N N 79  
ARG   NE  HE   sing N N 80  
ARG   CZ  NH1  sing N N 81  
ARG   CZ  NH2  doub N N 82  
ARG   NH1 HH11 sing N N 83  
ARG   NH1 HH12 sing N N 84  
ARG   NH2 HH21 sing N N 85  
ARG   NH2 HH22 sing N N 86  
ARG   OXT HXT  sing N N 87  
ASN   N   CA   sing N N 88  
ASN   N   H    sing N N 89  
ASN   N   H2   sing N N 90  
ASN   CA  C    sing N N 91  
ASN   CA  CB   sing N N 92  
ASN   CA  HA   sing N N 93  
ASN   C   O    doub N N 94  
ASN   C   OXT  sing N N 95  
ASN   CB  CG   sing N N 96  
ASN   CB  HB2  sing N N 97  
ASN   CB  HB3  sing N N 98  
ASN   CG  OD1  doub N N 99  
ASN   CG  ND2  sing N N 100 
ASN   ND2 HD21 sing N N 101 
ASN   ND2 HD22 sing N N 102 
ASN   OXT HXT  sing N N 103 
ASP   N   CA   sing N N 104 
ASP   N   H    sing N N 105 
ASP   N   H2   sing N N 106 
ASP   CA  C    sing N N 107 
ASP   CA  CB   sing N N 108 
ASP   CA  HA   sing N N 109 
ASP   C   O    doub N N 110 
ASP   C   OXT  sing N N 111 
ASP   CB  CG   sing N N 112 
ASP   CB  HB2  sing N N 113 
ASP   CB  HB3  sing N N 114 
ASP   CG  OD1  doub N N 115 
ASP   CG  OD2  sing N N 116 
ASP   OD2 HD2  sing N N 117 
ASP   OXT HXT  sing N N 118 
CYS   N   CA   sing N N 119 
CYS   N   H    sing N N 120 
CYS   N   H2   sing N N 121 
CYS   CA  C    sing N N 122 
CYS   CA  CB   sing N N 123 
CYS   CA  HA   sing N N 124 
CYS   C   O    doub N N 125 
CYS   C   OXT  sing N N 126 
CYS   CB  SG   sing N N 127 
CYS   CB  HB2  sing N N 128 
CYS   CB  HB3  sing N N 129 
CYS   SG  HG   sing N N 130 
CYS   OXT HXT  sing N N 131 
DMS   S   O    doub N N 132 
DMS   S   C1   sing N N 133 
DMS   S   C2   sing N N 134 
DMS   C1  H11  sing N N 135 
DMS   C1  H12  sing N N 136 
DMS   C1  H13  sing N N 137 
DMS   C2  H21  sing N N 138 
DMS   C2  H22  sing N N 139 
DMS   C2  H23  sing N N 140 
GLN   N   CA   sing N N 141 
GLN   N   H    sing N N 142 
GLN   N   H2   sing N N 143 
GLN   CA  C    sing N N 144 
GLN   CA  CB   sing N N 145 
GLN   CA  HA   sing N N 146 
GLN   C   O    doub N N 147 
GLN   C   OXT  sing N N 148 
GLN   CB  CG   sing N N 149 
GLN   CB  HB2  sing N N 150 
GLN   CB  HB3  sing N N 151 
GLN   CG  CD   sing N N 152 
GLN   CG  HG2  sing N N 153 
GLN   CG  HG3  sing N N 154 
GLN   CD  OE1  doub N N 155 
GLN   CD  NE2  sing N N 156 
GLN   NE2 HE21 sing N N 157 
GLN   NE2 HE22 sing N N 158 
GLN   OXT HXT  sing N N 159 
GLU   N   CA   sing N N 160 
GLU   N   H    sing N N 161 
GLU   N   H2   sing N N 162 
GLU   CA  C    sing N N 163 
GLU   CA  CB   sing N N 164 
GLU   CA  HA   sing N N 165 
GLU   C   O    doub N N 166 
GLU   C   OXT  sing N N 167 
GLU   CB  CG   sing N N 168 
GLU   CB  HB2  sing N N 169 
GLU   CB  HB3  sing N N 170 
GLU   CG  CD   sing N N 171 
GLU   CG  HG2  sing N N 172 
GLU   CG  HG3  sing N N 173 
GLU   CD  OE1  doub N N 174 
GLU   CD  OE2  sing N N 175 
GLU   OE2 HE2  sing N N 176 
GLU   OXT HXT  sing N N 177 
GLY   N   CA   sing N N 178 
GLY   N   H    sing N N 179 
GLY   N   H2   sing N N 180 
GLY   CA  C    sing N N 181 
GLY   CA  HA2  sing N N 182 
GLY   CA  HA3  sing N N 183 
GLY   C   O    doub N N 184 
GLY   C   OXT  sing N N 185 
GLY   OXT HXT  sing N N 186 
HIS   N   CA   sing N N 187 
HIS   N   H    sing N N 188 
HIS   N   H2   sing N N 189 
HIS   CA  C    sing N N 190 
HIS   CA  CB   sing N N 191 
HIS   CA  HA   sing N N 192 
HIS   C   O    doub N N 193 
HIS   C   OXT  sing N N 194 
HIS   CB  CG   sing N N 195 
HIS   CB  HB2  sing N N 196 
HIS   CB  HB3  sing N N 197 
HIS   CG  ND1  sing Y N 198 
HIS   CG  CD2  doub Y N 199 
HIS   ND1 CE1  doub Y N 200 
HIS   ND1 HD1  sing N N 201 
HIS   CD2 NE2  sing Y N 202 
HIS   CD2 HD2  sing N N 203 
HIS   CE1 NE2  sing Y N 204 
HIS   CE1 HE1  sing N N 205 
HIS   NE2 HE2  sing N N 206 
HIS   OXT HXT  sing N N 207 
HOH   O   H1   sing N N 208 
HOH   O   H2   sing N N 209 
ILE   N   CA   sing N N 210 
ILE   N   H    sing N N 211 
ILE   N   H2   sing N N 212 
ILE   CA  C    sing N N 213 
ILE   CA  CB   sing N N 214 
ILE   CA  HA   sing N N 215 
ILE   C   O    doub N N 216 
ILE   C   OXT  sing N N 217 
ILE   CB  CG1  sing N N 218 
ILE   CB  CG2  sing N N 219 
ILE   CB  HB   sing N N 220 
ILE   CG1 CD1  sing N N 221 
ILE   CG1 HG12 sing N N 222 
ILE   CG1 HG13 sing N N 223 
ILE   CG2 HG21 sing N N 224 
ILE   CG2 HG22 sing N N 225 
ILE   CG2 HG23 sing N N 226 
ILE   CD1 HD11 sing N N 227 
ILE   CD1 HD12 sing N N 228 
ILE   CD1 HD13 sing N N 229 
ILE   OXT HXT  sing N N 230 
LEU   N   CA   sing N N 231 
LEU   N   H    sing N N 232 
LEU   N   H2   sing N N 233 
LEU   CA  C    sing N N 234 
LEU   CA  CB   sing N N 235 
LEU   CA  HA   sing N N 236 
LEU   C   O    doub N N 237 
LEU   C   OXT  sing N N 238 
LEU   CB  CG   sing N N 239 
LEU   CB  HB2  sing N N 240 
LEU   CB  HB3  sing N N 241 
LEU   CG  CD1  sing N N 242 
LEU   CG  CD2  sing N N 243 
LEU   CG  HG   sing N N 244 
LEU   CD1 HD11 sing N N 245 
LEU   CD1 HD12 sing N N 246 
LEU   CD1 HD13 sing N N 247 
LEU   CD2 HD21 sing N N 248 
LEU   CD2 HD22 sing N N 249 
LEU   CD2 HD23 sing N N 250 
LEU   OXT HXT  sing N N 251 
LYS   N   CA   sing N N 252 
LYS   N   H    sing N N 253 
LYS   N   H2   sing N N 254 
LYS   CA  C    sing N N 255 
LYS   CA  CB   sing N N 256 
LYS   CA  HA   sing N N 257 
LYS   C   O    doub N N 258 
LYS   C   OXT  sing N N 259 
LYS   CB  CG   sing N N 260 
LYS   CB  HB2  sing N N 261 
LYS   CB  HB3  sing N N 262 
LYS   CG  CD   sing N N 263 
LYS   CG  HG2  sing N N 264 
LYS   CG  HG3  sing N N 265 
LYS   CD  CE   sing N N 266 
LYS   CD  HD2  sing N N 267 
LYS   CD  HD3  sing N N 268 
LYS   CE  NZ   sing N N 269 
LYS   CE  HE2  sing N N 270 
LYS   CE  HE3  sing N N 271 
LYS   NZ  HZ1  sing N N 272 
LYS   NZ  HZ2  sing N N 273 
LYS   NZ  HZ3  sing N N 274 
LYS   OXT HXT  sing N N 275 
MET   N   CA   sing N N 276 
MET   N   H    sing N N 277 
MET   N   H2   sing N N 278 
MET   CA  C    sing N N 279 
MET   CA  CB   sing N N 280 
MET   CA  HA   sing N N 281 
MET   C   O    doub N N 282 
MET   C   OXT  sing N N 283 
MET   CB  CG   sing N N 284 
MET   CB  HB2  sing N N 285 
MET   CB  HB3  sing N N 286 
MET   CG  SD   sing N N 287 
MET   CG  HG2  sing N N 288 
MET   CG  HG3  sing N N 289 
MET   SD  CE   sing N N 290 
MET   CE  HE1  sing N N 291 
MET   CE  HE2  sing N N 292 
MET   CE  HE3  sing N N 293 
MET   OXT HXT  sing N N 294 
PHE   N   CA   sing N N 295 
PHE   N   H    sing N N 296 
PHE   N   H2   sing N N 297 
PHE   CA  C    sing N N 298 
PHE   CA  CB   sing N N 299 
PHE   CA  HA   sing N N 300 
PHE   C   O    doub N N 301 
PHE   C   OXT  sing N N 302 
PHE   CB  CG   sing N N 303 
PHE   CB  HB2  sing N N 304 
PHE   CB  HB3  sing N N 305 
PHE   CG  CD1  doub Y N 306 
PHE   CG  CD2  sing Y N 307 
PHE   CD1 CE1  sing Y N 308 
PHE   CD1 HD1  sing N N 309 
PHE   CD2 CE2  doub Y N 310 
PHE   CD2 HD2  sing N N 311 
PHE   CE1 CZ   doub Y N 312 
PHE   CE1 HE1  sing N N 313 
PHE   CE2 CZ   sing Y N 314 
PHE   CE2 HE2  sing N N 315 
PHE   CZ  HZ   sing N N 316 
PHE   OXT HXT  sing N N 317 
PRO   N   CA   sing N N 318 
PRO   N   CD   sing N N 319 
PRO   N   H    sing N N 320 
PRO   CA  C    sing N N 321 
PRO   CA  CB   sing N N 322 
PRO   CA  HA   sing N N 323 
PRO   C   O    doub N N 324 
PRO   C   OXT  sing N N 325 
PRO   CB  CG   sing N N 326 
PRO   CB  HB2  sing N N 327 
PRO   CB  HB3  sing N N 328 
PRO   CG  CD   sing N N 329 
PRO   CG  HG2  sing N N 330 
PRO   CG  HG3  sing N N 331 
PRO   CD  HD2  sing N N 332 
PRO   CD  HD3  sing N N 333 
PRO   OXT HXT  sing N N 334 
SER   N   CA   sing N N 335 
SER   N   H    sing N N 336 
SER   N   H2   sing N N 337 
SER   CA  C    sing N N 338 
SER   CA  CB   sing N N 339 
SER   CA  HA   sing N N 340 
SER   C   O    doub N N 341 
SER   C   OXT  sing N N 342 
SER   CB  OG   sing N N 343 
SER   CB  HB2  sing N N 344 
SER   CB  HB3  sing N N 345 
SER   OG  HG   sing N N 346 
SER   OXT HXT  sing N N 347 
THR   N   CA   sing N N 348 
THR   N   H    sing N N 349 
THR   N   H2   sing N N 350 
THR   CA  C    sing N N 351 
THR   CA  CB   sing N N 352 
THR   CA  HA   sing N N 353 
THR   C   O    doub N N 354 
THR   C   OXT  sing N N 355 
THR   CB  OG1  sing N N 356 
THR   CB  CG2  sing N N 357 
THR   CB  HB   sing N N 358 
THR   OG1 HG1  sing N N 359 
THR   CG2 HG21 sing N N 360 
THR   CG2 HG22 sing N N 361 
THR   CG2 HG23 sing N N 362 
THR   OXT HXT  sing N N 363 
TRP   N   CA   sing N N 364 
TRP   N   H    sing N N 365 
TRP   N   H2   sing N N 366 
TRP   CA  C    sing N N 367 
TRP   CA  CB   sing N N 368 
TRP   CA  HA   sing N N 369 
TRP   C   O    doub N N 370 
TRP   C   OXT  sing N N 371 
TRP   CB  CG   sing N N 372 
TRP   CB  HB2  sing N N 373 
TRP   CB  HB3  sing N N 374 
TRP   CG  CD1  doub Y N 375 
TRP   CG  CD2  sing Y N 376 
TRP   CD1 NE1  sing Y N 377 
TRP   CD1 HD1  sing N N 378 
TRP   CD2 CE2  doub Y N 379 
TRP   CD2 CE3  sing Y N 380 
TRP   NE1 CE2  sing Y N 381 
TRP   NE1 HE1  sing N N 382 
TRP   CE2 CZ2  sing Y N 383 
TRP   CE3 CZ3  doub Y N 384 
TRP   CE3 HE3  sing N N 385 
TRP   CZ2 CH2  doub Y N 386 
TRP   CZ2 HZ2  sing N N 387 
TRP   CZ3 CH2  sing Y N 388 
TRP   CZ3 HZ3  sing N N 389 
TRP   CH2 HH2  sing N N 390 
TRP   OXT HXT  sing N N 391 
TYR   N   CA   sing N N 392 
TYR   N   H    sing N N 393 
TYR   N   H2   sing N N 394 
TYR   CA  C    sing N N 395 
TYR   CA  CB   sing N N 396 
TYR   CA  HA   sing N N 397 
TYR   C   O    doub N N 398 
TYR   C   OXT  sing N N 399 
TYR   CB  CG   sing N N 400 
TYR   CB  HB2  sing N N 401 
TYR   CB  HB3  sing N N 402 
TYR   CG  CD1  doub Y N 403 
TYR   CG  CD2  sing Y N 404 
TYR   CD1 CE1  sing Y N 405 
TYR   CD1 HD1  sing N N 406 
TYR   CD2 CE2  doub Y N 407 
TYR   CD2 HD2  sing N N 408 
TYR   CE1 CZ   doub Y N 409 
TYR   CE1 HE1  sing N N 410 
TYR   CE2 CZ   sing Y N 411 
TYR   CE2 HE2  sing N N 412 
TYR   CZ  OH   sing N N 413 
TYR   OH  HH   sing N N 414 
TYR   OXT HXT  sing N N 415 
VAL   N   CA   sing N N 416 
VAL   N   H    sing N N 417 
VAL   N   H2   sing N N 418 
VAL   CA  C    sing N N 419 
VAL   CA  CB   sing N N 420 
VAL   CA  HA   sing N N 421 
VAL   C   O    doub N N 422 
VAL   C   OXT  sing N N 423 
VAL   CB  CG1  sing N N 424 
VAL   CB  CG2  sing N N 425 
VAL   CB  HB   sing N N 426 
VAL   CG1 HG11 sing N N 427 
VAL   CG1 HG12 sing N N 428 
VAL   CG1 HG13 sing N N 429 
VAL   CG2 HG21 sing N N 430 
VAL   CG2 HG22 sing N N 431 
VAL   CG2 HG23 sing N N 432 
VAL   OXT HXT  sing N N 433 
# 
_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                    7HWS 
_atom_sites.fract_transf_matrix[1][1]   0.013756 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000675 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016160 
_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]   0.015364 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.401 7.279   24.491 1.00 21.29 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.621 7.418   23.701 1.00 21.00 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.807 6.268   22.727 1.00 20.67 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.249 5.191   22.913 1.00 22.16 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.830 7.549   24.640 1.00 23.43 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.016 6.328   25.341 1.00 26.49 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.623 6.487   21.687 1.00 19.10 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.939 5.438   20.722 1.00 18.41 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.248 5.975   19.338 1.00 17.42 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.883 7.109   19.020 1.00 18.17 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.978 5.201   18.538 1.00 15.30 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.371 5.643   17.211 1.00 15.92 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.428 4.454   16.270 1.00 15.76 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.517 3.286   16.724 1.00 17.41 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.773 6.308   17.290 1.00 17.51 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.440 4.726   14.951 1.00 14.37 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.669 3.742   13.910 1.00 14.69 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.081 3.969   13.391 1.00 15.95 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.458 5.111   13.110 1.00 16.47 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.685 3.896   12.735 1.00 15.23 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.221 3.858   13.232 1.00 14.95 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.896 2.809   11.668 1.00 16.55 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.222 4.399   12.128 1.00 16.25 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.852 2.909   13.252 1.00 16.75 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.233 3.015   12.742 1.00 17.50 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.333 2.243   11.450 1.00 17.29 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.277 1.016   11.489 1.00 18.80 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.244 2.475   13.779 1.00 18.79 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.299 3.306   15.036 1.00 20.07 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 26.512 2.994   16.130 1.00 21.31 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 28.107 4.431   15.112 1.00 21.07 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 26.525 3.777   17.273 1.00 22.16 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 28.128 5.228   16.248 1.00 21.60 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.341 4.888   17.331 1.00 22.58 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.308 5.685   18.444 1.00 24.45 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.378 2.913   10.309 1.00 17.47 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.404 2.256   8.997  1.00 18.97 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.535 2.839   8.179  1.00 20.64 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.630 4.065   8.041  1.00 20.98 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.023 2.386   8.278  1.00 21.55 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.545 3.839   8.235  1.00 21.58 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.088 1.818   6.864  1.00 23.10 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.464 1.989   7.715  1.00 22.33 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.607 2.477   6.956  1.00 22.04 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.418 3.455   7.796  1.00 21.56 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.648 3.192   8.988  1.00 22.22 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.712 4.633   7.238  1.00 21.34 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.398 5.656   8.027  1.00 21.93 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.434 6.752   8.475  1.00 20.15 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.809 7.931   8.563  1.00 20.17 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.595 6.233   7.263  1.00 24.93 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.723 5.247   7.144  1.00 33.49 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.383 4.903   8.131  1.00 37.21 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.940 4.744   5.944  1.00 34.10 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.190 6.360   8.809  1.00 18.27 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.166 7.331   9.248  1.00 17.39 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.588 6.907   10.598 1.00 15.97 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.490 5.707   10.893 1.00 16.79 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.989 7.359   8.246  1.00 17.79 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.390 7.897   6.888  1.00 18.67 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.982 9.149   6.758  1.00 20.20 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.136 7.178   5.733  1.00 21.03 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.335 9.657   5.512  1.00 21.92 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.500 7.671   4.480  1.00 22.21 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.114 8.907   4.378  1.00 23.97 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.457 9.428   3.143  1.00 27.67 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.212 7.898   11.414 1.00 15.16 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.493 7.720   12.659 1.00 15.65 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.171 8.532   12.507 1.00 16.04 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.209 9.726   12.182 1.00 15.78 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.334 8.239   13.838 1.00 15.79 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.578 8.547   15.131 1.00 18.00 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.499 8.928   16.294 1.00 19.40 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.886 9.923   17.190 1.00 19.49 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.387 9.671   18.395 1.00 21.75 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.302 8.413   18.841 1.00 23.19 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.890 10.660  19.135 1.00 22.11 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.007 7.866   12.671 1.00 16.37 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.689 8.498   12.570 1.00 15.00 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.125 8.639   13.971 1.00 14.74 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.969 7.633   14.676 1.00 14.46 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.712 7.673   11.680 1.00 15.47 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.423 8.488   11.428 1.00 15.47 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.385 7.229   10.365 1.00 15.13 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.848 9.873   14.389 1.00 13.55 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.296 10.109  15.722 1.00 14.45 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.053 11.020  15.628 1.00 14.55 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.804 11.719  14.605 1.00 14.86 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.349 10.765  16.632 1.00 16.45 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.486 9.799   16.904 1.00 21.45 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.851 12.090  16.013 1.00 16.05 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.274 11.112  16.730 1.00 12.71 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.201 12.117  16.779 1.00 12.36 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 18.889 13.491  16.796 1.00 13.70 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 19.828 13.707  17.589 1.00 13.56 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.430 11.981  18.108 1.00 12.67 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.621 10.713  18.155 1.00 14.23 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.082 9.685   18.639 1.00 15.51 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.390 10.761  17.616 1.00 14.18 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.446 14.411  15.945 1.00 12.86 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.086 15.733  15.868 1.00 13.47 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.109 16.440  17.249 1.00 14.81 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.125 17.065  17.609 1.00 15.49 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.400 16.585  14.823 1.00 13.40 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.180 17.862  14.506 1.00 13.79 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.251 18.703  13.625 1.00 14.54 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 18.857 19.961  13.109 1.00 15.77 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 18.880 21.108  13.772 1.00 16.61 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.438 21.171  15.023 1.00 17.66 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.361 22.210  13.194 1.00 16.93 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.027 16.253  18.042 1.00 13.94 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 17.966 16.963  19.340 1.00 14.50 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 18.897 16.390  20.375 1.00 16.35 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.077 17.037  21.417 1.00 19.08 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.493 17.082  19.859 1.00 15.55 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 15.886 15.802  20.354 1.00 17.37 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.335 14.881  19.482 1.00 17.54 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 15.733 15.359  21.623 1.00 18.62 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 14.848 13.900  20.252 1.00 18.20 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.071 14.149  21.553 1.00 18.76 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.469 15.186  20.114 1.00 15.37 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.436 14.563  21.022 1.00 15.31 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 21.866 14.587  20.464 1.00 16.37 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 22.774 14.037  21.102 1.00 17.64 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.016 13.127  21.345 1.00 15.48 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.635 13.005  21.996 1.00 16.78 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.311 11.521  22.229 1.00 18.26 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.585 13.772  23.333 1.00 17.52 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.087 15.261  19.297 1.00 16.37 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.434 15.284  18.729 1.00 15.83 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.422 15.979  19.681 1.00 16.40 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.088 16.943  20.334 1.00 16.83 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.411 15.999  17.385 1.00 15.81 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.651 15.481  19.671 1.00 16.43 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 26.717 16.007  20.549 1.00 18.24 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.516 17.085  19.841 1.00 19.44 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.393 17.269  18.625 1.00 18.66 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.662 14.832  20.957 1.00 21.00 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.372 14.360  19.795 1.00 20.89 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 26.929 13.680  21.623 1.00 21.76 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.459 17.737  20.580 1.00 20.28 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.359 18.710  19.928 1.00 21.72 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.180 18.000  18.838 1.00 19.78 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.347 18.518  17.728 1.00 19.97 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.340 19.308  20.968 1.00 25.96 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 29.664 20.113  22.037 1.00 35.84 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 28.926 21.242  21.729 1.00 40.59 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 29.679 19.957  23.385 1.00 39.32 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 28.488 21.717  22.887 1.00 41.26 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 28.915 20.976  23.914 1.00 41.40 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.601 16.730  19.116 1.00 19.44 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.387 15.982  18.131 1.00 20.22 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.571 15.651  16.886 1.00 19.18 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.094 15.671  15.768 1.00 19.17 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 31.969 14.721  18.740 1.00 23.17 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.457 14.774  18.710 1.00 30.80 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.070 15.829  19.022 1.00 27.93 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.065 13.716  18.172 1.00 37.08 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.277 15.335  17.061 1.00 16.71 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.405 15.120  15.879 1.00 16.18 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.372 16.369  14.996 1.00 16.19 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.514 16.265  13.779 1.00 16.80 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 26.967 14.790  16.334 1.00 16.20 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 26.804 13.382  16.856 1.00 20.13 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.424 12.477  16.292 1.00 19.62 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.055 13.202  17.869 1.00 19.24 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.176 17.549  15.619 1.00 15.86 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.116 18.776  14.832 1.00 16.44 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.464 19.128  14.174 1.00 18.59 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.486 19.626  13.028 1.00 19.21 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.573 19.905  15.698 1.00 16.45 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.067 19.926  15.801 1.00 16.58 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.310 19.510  16.851 1.00 18.27 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.150 20.432  14.820 1.00 15.89 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 23.959 19.673  16.560 1.00 17.78 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 23.840 20.261  15.332 1.00 17.56 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.310 20.995  13.553 1.00 17.56 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 22.696 20.643  14.617 1.00 17.56 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.177 21.417  12.867 1.00 18.46 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 22.892 21.237  13.392 1.00 18.51 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.593 18.823  14.854 1.00 18.49 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 31.917 19.068  14.260 1.00 19.73 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.206 18.137  13.054 1.00 20.50 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.115 18.413  12.248 1.00 21.85 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 32.985 18.893  15.316 1.00 21.32 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.534 16.975  12.988 1.00 18.73 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.741 16.055  11.884 1.00 19.25 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.412 15.916  11.074 1.00 18.51 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.104 14.857  10.533 1.00 17.67 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.139 14.714  12.473 1.00 19.84 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.518 14.793  13.079 1.00 21.99 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.518 14.855  12.334 1.00 23.78 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.598 14.864  14.417 1.00 22.40 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.674 17.012  10.947 1.00 17.05 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.362 16.996  10.282 1.00 16.27 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.423 16.601  8.828  1.00 18.05 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.242 17.127  8.061  1.00 20.35 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.770 18.401  10.389 1.00 16.69 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.394 18.573  9.738  1.00 16.31 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.329 17.736  10.473 1.00 16.89 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 25.983 20.037  9.761  1.00 17.86 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.515 15.692  8.415  1.00 16.68 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.349 15.310  7.009  1.00 18.05 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.014 15.899  6.502  1.00 19.26 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.950 16.527  5.427  1.00 21.18 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.324 13.759  6.873  1.00 19.03 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.963 13.330  5.449  1.00 20.73 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.674 13.180  7.272  1.00 19.57 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.952 15.756  7.319  1.00 17.92 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.608 16.190  6.902  1.00 17.86 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.732 16.281  8.146  1.00 16.84 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.871 15.439  9.050  1.00 16.63 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.987 15.181  5.891  1.00 18.63 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.510 15.364  5.589  1.00 19.80 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.949 16.213  4.677  1.00 21.32 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.431 14.620  6.163  1.00 19.46 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.563 16.086  4.703  1.00 21.19 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.234 15.078  5.572  1.00 20.28 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.364 13.617  7.123  1.00 19.41 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.986 14.535  5.895  1.00 19.34 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.134 13.071  7.429  1.00 19.35 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.962 13.546  6.835  1.00 18.94 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.826 17.241  8.178  1.00 16.33 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.855 17.323  9.280  1.00 16.58 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.540 17.888  8.757  1.00 16.74 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.536 18.691  7.826  1.00 17.50 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.375 18.117  10.497 1.00 17.48 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 21.929 19.499  10.173 1.00 17.55 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 20.908 20.600  9.954  1.00 20.54 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.224 21.538  9.179  1.00 24.53 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 19.818 20.565  10.566 1.00 17.95 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.424 17.523  9.409  1.00 15.88 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.122 18.007  9.000  1.00 16.08 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.242 18.147  10.231 1.00 15.51 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.808 17.151  10.798 1.00 15.76 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.519 17.109  7.911  1.00 18.04 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.195 17.591  7.333  1.00 25.66 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.454 18.268  8.051  1.00 28.32 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.894 17.255  6.156  1.00 23.34 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.035 19.404  10.686 1.00 15.31 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.225 19.691  11.853 0.50 16.56 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.228 19.642  11.877 0.50 16.49 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 13.795 19.142  11.692 1.00 16.77 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.195 18.657  12.663 1.00 17.97 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.214 21.201  12.097 0.50 19.71 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.240 21.122  12.260 0.50 19.48 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.398 21.547  13.197 0.50 23.47 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.548 21.864  11.274 0.50 22.87 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.246 19.222  10.459 1.00 16.78 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 11.853 18.747  10.264 1.00 17.62 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.751 17.240  10.438 1.00 18.62 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.652 16.784  10.641 1.00 20.25 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.287 19.134  8.900  1.00 21.32 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.835 18.375  7.840  1.00 26.90 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.845 16.497  10.316 1.00 15.78 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.829 15.028  10.502 1.00 14.36 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.410 14.586  11.854 1.00 15.01 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.382 13.380  12.178 1.00 14.07 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.691 14.349  9.404  1.00 14.41 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.090 14.544  8.001  1.00 15.56 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.912 13.908  6.905  1.00 15.60 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.931 12.439  7.023  1.00 15.59 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.157 11.609  6.004  1.00 16.73 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.325 12.089  4.764  1.00 18.71 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.167 10.289  6.203  1.00 15.23 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 13.953 15.509  12.638 1.00 13.87 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.670 15.190  13.886 1.00 13.74 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 15.849 14.236  13.625 1.00 14.48 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.142 13.374  14.474 1.00 14.20 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.760 14.610  14.981 1.00 14.77 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.459 14.402  16.323 1.00 14.89 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.278 15.296  16.737 1.00 14.78 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.158 13.372  17.004 1.00 15.29 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.541 14.402  12.478 1.00 13.41 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.717 13.551  12.195 1.00 13.41 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 18.995 14.335  11.987 1.00 12.90 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 18.964 15.437  11.408 1.00 14.23 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.508 12.715  10.915 1.00 14.04 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.486 11.579  10.996 1.00 14.50 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.418 10.879  9.624  1.00 15.42 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.852 10.595  12.107 1.00 14.87 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.122 13.742  12.375 1.00 12.46 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.447 14.281  12.099 1.00 12.72 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.357 13.117  11.808 1.00 14.04 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.255 12.062  12.460 1.00 14.28 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 21.967 15.165  13.253 1.00 12.84 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.351 15.832  13.009 1.00 14.71 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.400 17.151  13.761 1.00 15.04 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.506 14.935  13.495 1.00 15.52 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.194 13.252  10.775 1.00 13.85 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.184 12.215  10.400 1.00 14.48 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.571 12.854  10.479 1.00 15.21 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.788 13.970  9.964  1.00 15.94 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.930 11.695  8.973  1.00 15.87 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.008 10.663  8.572  1.00 17.08 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.539 11.059  8.899  1.00 15.50 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.464 12.180  11.166 1.00 15.50 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.852 12.628  11.304 1.00 15.33 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.778 11.557  10.732 1.00 17.65 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.394 10.385  10.577 1.00 17.20 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.185 12.917  12.768 1.00 17.21 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.014 11.805  13.638 1.00 19.58 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.037 11.955  10.436 1.00 18.42 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.011 10.986  9.918  1.00 19.92 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.794 10.286  11.038 1.00 20.57 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.992 10.839  12.113 1.00 20.94 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.953 11.670  8.923  1.00 22.60 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.583 12.744  9.587  1.00 24.48 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.249 9.055   10.788 1.00 21.32 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.994 8.291   11.791 1.00 24.09 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.319 7.818   11.167 1.00 27.01 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.431 7.734   9.939  1.00 28.11 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.202 7.052   12.282 1.00 25.32 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.127 6.116   11.214 1.00 27.12 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.803 7.385   12.734 1.00 24.79 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.282 7.476   12.004 1.00 29.49 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.548 6.920   11.530 1.00 32.00 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.468 5.389   11.451 1.00 33.51 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.159 4.773   10.634 1.00 35.95 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.695 7.370   12.452 1.00 34.62 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.344 7.026   13.802 1.00 36.53 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.940 8.867   12.374 1.00 35.47 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.659 4.763   12.315 1.00 31.73 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.535 3.313   12.351 1.00 31.47 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.342 2.849   11.511 1.00 31.16 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.354 3.572   11.390 1.00 30.75 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.358 2.859   13.793 1.00 31.69 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.416 1.641   10.961 1.00 30.75 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.317 1.063   10.160 1.00 31.38 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.167 0.604   11.070 1.00 30.92 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.427 -0.046  12.082 1.00 31.65 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.878 -0.142  9.385  1.00 35.21 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.844 -0.925  8.592  1.00 42.01 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.500 -0.271  7.269  1.00 49.62 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.152 0.689   6.809  1.00 51.54 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.452 -0.790  6.623  1.00 50.66 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.924 0.938   10.731 1.00 29.60 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.779 0.638   11.598 1.00 29.12 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.277 -0.791  11.616 1.00 30.07 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.489 -1.512  10.652 1.00 32.50 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.492 -1.145  12.668 1.00 27.20 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.933 -2.474  12.902 1.00 26.06 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.573 -2.765  12.199 1.00 24.87 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 26.203 -3.935  12.080 1.00 23.67 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 27.816 -2.708  14.410 1.00 27.59 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 26.745 -1.516  15.283 1.00 28.03 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.845 -1.736  11.732 1.00 24.47 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.464 -1.877  11.182 1.00 23.39 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 24.302 -1.929  9.635  1.00 22.93 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 25.178 -1.422  8.927  1.00 25.67 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.627 -0.698  11.743 1.00 21.49 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.458 -0.755  13.252 1.00 25.21 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.707 0.281   13.936 1.00 20.90 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.073 -1.840  13.762 1.00 27.45 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 23.101 -2.428  9.132  1.00 22.20 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.567 -2.591  7.751  1.00 24.93 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 21.195 -1.827  7.682  1.00 22.67 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 20.403 -1.981  8.603  1.00 22.14 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 22.315 -4.148  7.445  1.00 31.54 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 23.514 -4.680  6.901  1.00 36.70 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 21.103 -4.450  6.474  1.00 32.95 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.918 -1.029  6.606  1.00 20.28 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.646 -0.299  6.476  1.00 18.17 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.679 -1.053  5.568  1.00 18.63 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 19.068 -1.539  4.477  1.00 19.54 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.882 1.116   5.865  1.00 17.08 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 21.003 1.874   6.602  1.00 19.12 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.587 1.946   5.858  1.00 17.53 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.698 2.089   8.102  1.00 19.44 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.425 -1.215  6.010  1.00 17.33 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.371 -1.834  5.224  1.00 17.67 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 16.025 -0.928  4.033  1.00 18.10 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.984 0.301   4.144  1.00 17.17 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 15.100 -2.019  6.091  1.00 17.30 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.780 -1.560  2.873  1.00 18.72 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 15.326 -0.849  1.664  1.00 19.03 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 14.063 -1.608  1.258  1.00 21.05 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 14.099 -2.599  0.510  1.00 22.11 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 16.394 -0.858  0.561  1.00 18.99 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.727 -0.280  1.013  1.00 20.20 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.671 1.204   1.400  1.00 21.65 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 19.003 1.671   1.794  1.00 20.70 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 19.237 2.824   2.421  1.00 22.27 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.237 3.642   2.719  1.00 19.51 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.471 3.156   2.769  1.00 22.91 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.931 -1.161  1.806  1.00 20.44 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.684 -1.903  1.709  1.00 20.46 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.488 -1.000  2.080  1.00 20.85 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.653 0.154   2.509  1.00 20.78 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.760 -3.105  2.657  1.00 19.82 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.742 -2.606  4.415  1.00 19.26 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 9.264  -1.603  2.007  1.00 21.65 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 8.045  -0.925  2.414  1.00 21.94 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 7.372  -1.662  3.581  1.00 22.00 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 6.155  -1.580  3.722  1.00 23.13 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 7.050  -0.789  1.238  1.00 26.13 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 6.607  -2.094  0.617  1.00 35.29 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 7.055  -3.171  1.086  1.00 35.52 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 5.809  -2.050  -0.349 1.00 42.41 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 8.151  -2.347  4.451  1.00 20.88 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.558  -3.026  5.625  1.00 19.25 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.799  -2.026  6.499  1.00 18.90 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 7.214  -0.857  6.649  1.00 18.84 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.648  -3.717  6.442  1.00 19.25 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 9.305  -5.268  5.724  1.00 20.79 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.704  -2.467  7.086  1.00 17.31 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.916  -1.708  8.067  1.00 17.26 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.750  -2.512  9.363  1.00 15.78 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.871  -2.202  10.175 1.00 15.64 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.532  -1.330  7.539  1.00 20.79 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.561  -0.183  6.581  1.00 25.45 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 2.129  0.171   6.210  1.00 30.02 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.694  -0.045  5.073  1.00 31.58 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.372  0.753   7.150  1.00 28.04 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.556  -3.599  9.536  1.00 15.46 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.664  -4.302  10.820 1.00 15.15 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 7.165  -4.457  11.122 1.00 14.53 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 8.019  -4.530  10.211 1.00 15.71 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.963  -5.661  10.823 1.00 17.32 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.623  -6.511  9.881  1.00 20.08 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.474  -5.547  10.474 1.00 18.09 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.473  -4.516  12.391 1.00 14.19 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.860  -4.675  12.827 1.00 13.18 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.915  -4.768  14.342 1.00 12.69 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.892  -5.007  14.986 1.00 13.62 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.130 -4.673  14.865 1.00 12.27 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.385 -4.790  16.296 1.00 12.38 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.241 -3.591  16.686 1.00 12.58 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.258 -3.311  16.036 1.00 13.54 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.085 -6.151  16.607 1.00 14.53 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.440 -6.233  18.109 1.00 16.28 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.145 -7.315  16.258 1.00 15.82 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.884 -2.940  17.820 1.00 12.29 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.741 -1.851  18.311 1.00 11.50 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.269 -2.105  19.709 1.00 12.74 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.653 -2.830  20.476 1.00 13.38 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.034 -0.445  18.248 1.00 12.47 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.045 -0.176  19.370 1.00 12.26 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.762  -0.733  19.346 1.00 13.06 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.342 0.721   20.390 1.00 13.49 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.817  -0.423  20.327 1.00 13.45 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.407  1.008   21.398 1.00 14.24 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.164  0.402   21.382 1.00 14.77 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.189  0.651   22.340 1.00 16.28 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.408 -1.470  20.033 1.00 12.08 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 13.933 -1.575  21.392 1.00 12.63 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.427 -0.387  22.221 1.00 13.27 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.581 0.775   21.850 1.00 13.20 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.473 -1.600  21.375 1.00 13.32 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.034 -1.720  22.765 1.00 14.77 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.830 -2.861  23.506 1.00 16.15 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.696 -0.652  23.361 1.00 16.13 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.303 -2.967  24.808 1.00 17.32 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.149 -0.729  24.664 1.00 17.26 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 16.965 -1.893  25.371 1.00 18.93 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.439 -1.997  26.658 1.00 23.26 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 12.853 -0.716  23.390 1.00 13.77 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.333 0.291   24.323 1.00 13.40 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.241 0.304   25.605 1.00 14.53 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.104 -0.572  26.465 1.00 14.59 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 10.884 -0.056  24.644 1.00 14.74 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.152 0.979   25.958 1.00 15.43 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.109 1.325   25.732 1.00 14.74 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.043 1.370   26.848 1.00 15.93 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.368 1.501   28.197 1.00 15.56 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 14.816 0.895   29.184 1.00 16.93 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.071 2.475   26.645 1.00 20.19 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.478 3.752   26.579 1.00 27.28 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.212 2.207   28.231 1.00 14.63 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.470 2.382   29.505 1.00 15.46 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 11.768 1.121   29.998 1.00 15.54 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.206 1.152   31.107 1.00 16.13 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.468 3.528   29.444 1.00 16.27 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.457 3.197   28.498 1.00 15.53 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 11.841 0.019   29.237 1.00 14.98 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.351 -1.283  29.661 1.00 15.49 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.445 -2.369  29.535 1.00 16.27 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.166 -3.546  29.825 1.00 17.05 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.124 -1.678  28.814 1.00 15.72 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 8.905  -0.777  29.032 1.00 16.61 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.232  -1.085  30.372 1.00 17.30 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.059  -0.231  30.582 1.00 17.45 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.095  0.966   31.169 1.00 18.20 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.246  1.462   31.618 1.00 17.66 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 5.973  1.665   31.342 1.00 18.66 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.635 -2.012  29.037 1.00 17.38 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.695 -2.993  28.716 1.00 19.88 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.145 -4.142  27.870 1.00 20.10 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.421 -5.326  28.149 1.00 21.42 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.358 -3.538  29.993 1.00 22.73 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.337 -2.575  30.524 1.00 27.05 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.210 -3.262  31.581 1.00 28.00 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 17.898 -2.275  32.390 1.00 29.42 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.678 -2.107  33.699 1.00 30.47 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 16.794 -2.877  34.340 1.00 31.88 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.297 -1.138  34.360 1.00 29.93 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.277 -3.822  26.895 1.00 18.18 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.599 -4.908  26.142 1.00 18.37 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.399 -4.529  24.700 1.00 17.05 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.276 -3.346  24.396 1.00 15.91 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.175 -5.109  26.697 1.00 22.12 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.007 -6.057  27.892 1.00 30.69 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.517  -6.206  28.167 1.00 36.38 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.165  -7.358  29.092 1.00 42.16 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.231  -6.981  30.526 1.00 45.02 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.299 -5.510  23.833 1.00 16.00 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 11.903 -5.298  22.445 1.00 15.43 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.398 -5.589  22.308 1.00 16.13 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 9.860  -6.556  22.892 1.00 16.78 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.670 -6.258  21.516 1.00 14.77 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.145 -6.059  21.514 1.00 15.71 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.797 -5.293  20.537 1.00 18.24 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.068 -6.536  22.368 1.00 16.13 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.096 -5.341  20.856 1.00 17.10 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.304 -6.076  21.932 1.00 20.10 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.706  -4.804  21.480 1.00 13.65 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.274  -4.986  21.251 1.00 13.76 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.959  -5.032  19.744 1.00 14.42 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.475  -4.243  18.968 1.00 13.76 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.464  -3.769  21.821 1.00 14.63 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.453  -3.674  23.328 1.00 15.70 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.679  -4.547  24.100 1.00 17.41 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.152  -2.673  23.980 1.00 16.09 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.640  -4.439  25.491 1.00 18.58 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.133  -2.567  25.366 1.00 16.74 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.350  -3.431  26.114 1.00 19.20 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.335  -3.292  27.496 1.00 21.66 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.064  -5.931  19.345 1.00 13.91 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.626  -5.961  17.936 1.00 14.71 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.587  -4.842  17.710 1.00 15.91 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.754  -4.570  18.610 1.00 18.57 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.990  -7.346  17.807 1.00 16.03 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.437  -7.630  19.224 1.00 16.57 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.415  -6.997  20.159 1.00 14.77 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.619  -4.211  16.527 1.00 14.01 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.677  -3.109  16.247 1.00 15.08 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.223  -3.116  14.812 1.00 14.02 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.943  -3.565  13.911 1.00 15.07 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.286  -1.707  16.500 1.00 17.10 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.307  -1.361  17.987 1.00 18.92 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.656  -1.589  15.903 1.00 17.41 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.000  -2.608  14.590 1.00 15.18 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.491  -2.261  13.252 1.00 15.16 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.599  -0.720  13.172 1.00 14.85 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.144  -0.050  14.095 1.00 16.29 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.021  -2.631  13.131 1.00 18.84 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.953  -4.046  13.098 1.00 25.75 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.236  -0.176  12.128 1.00 13.41 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.432  1.267   12.068 1.00 14.03 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.945  1.851   10.764 1.00 14.59 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.869  1.170   9.721  1.00 15.65 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.928  1.592   12.351 1.00 14.07 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.971  0.835   11.526 1.00 13.86 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.479  -0.383  11.955 1.00 15.19 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.455  1.360   10.327 1.00 14.47 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.459  -1.064  11.204 1.00 15.39 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.429  0.673   9.565  1.00 15.20 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.910  -0.541  10.002 1.00 15.23 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.554  3.165   10.829 1.00 14.22 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.090  3.863   9.637  1.00 15.70 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.232  4.202   8.676  1.00 16.24 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.408  4.153   9.045  1.00 16.07 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.331  5.133   10.019 1.00 17.46 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.178  6.027   10.732 1.00 18.93 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.896  4.436   7.386  1.00 16.07 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.924  4.833   6.411  1.00 17.74 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.480  6.196   6.776  1.00 18.44 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.798  6.997   7.399  1.00 18.94 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.308  4.887   4.991  1.00 19.83 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 3.026  3.476   4.490  1.00 21.65 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.522  3.541   3.030  1.00 29.18 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.397  2.118   2.568  1.00 35.87 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.677  2.038   1.289  1.00 40.52 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.733  6.499   6.396  1.00 18.04 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.302  7.813   6.744  1.00 18.00 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.429  8.965   6.276  1.00 19.10 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.019  9.012   5.112  1.00 19.97 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.669  7.829   6.026  1.00 19.25 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 8.008  6.367   5.752  1.00 20.94 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.659  5.655   5.616  1.00 17.84 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.134  9.887   7.201  1.00 18.07 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.234  10.977  6.862  1.00 19.96 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.504  12.232  7.687  1.00 18.98 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.405  12.252  8.542  1.00 18.02 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.781  10.496  6.975  1.00 24.72 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.431  10.423  8.337  1.00 31.75 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.767  13.329  7.354  1.00 18.43 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.908  14.611  8.050  1.00 20.23 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 2.908  14.617  9.201  1.00 21.22 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.692  14.557  8.938  1.00 22.87 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.545  15.703  7.038  1.00 21.99 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 3.944  17.098  7.351  1.00 25.99 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 5.450  17.267  7.442  1.00 26.11 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 3.342  18.051  6.330  1.00 28.33 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.389  14.682  10.464 1.00 21.08 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.573  14.561  11.676 1.00 22.55 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 2.833  15.730  12.596 1.00 23.59 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 3.996  16.074  12.835 1.00 22.30 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 2.922  13.218  12.355 1.00 24.45 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.523  12.050  11.446 1.00 25.83 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.304  13.111  13.760 1.00 26.04 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.887  10.759  11.911 1.00 27.03 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 1.765  16.345  13.140 1.00 23.62 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 1.940  17.472  14.048 1.00 24.67 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.544  16.991  15.384 1.00 25.75 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.103  15.992  15.957 1.00 26.79 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 0.580  18.150  14.311 1.00 25.35 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 0.685  19.338  15.226 1.00 28.37 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.161  20.547  14.761 1.00 30.66 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.402  19.218  16.581 1.00 29.89 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.282  21.633  15.615 1.00 31.96 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 0.488  20.314  17.420 1.00 31.16 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 0.923  21.509  16.935 1.00 31.46 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.599  17.700  15.851 1.00 24.66 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.251  17.389  17.107 1.00 23.77 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.242  18.644  17.978 1.00 24.88 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 4.676  19.720  17.536 1.00 26.39 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 5.709  16.899  16.866 1.00 23.28 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 6.408  16.672  18.208 1.00 24.42 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 5.706  15.607  16.051 1.00 23.23 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 3.786  18.504  19.227 1.00 25.54 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 3.656  19.611  20.184 1.00 26.28 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.016  20.211  20.531 1.00 26.27 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.038  19.523  20.417 1.00 25.47 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 2.997  19.100  21.494 1.00 30.34 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.659  20.182  22.513 1.00 42.47 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.676  21.242  22.052 1.00 54.81 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 0.452  21.010  22.185 1.00 58.04 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 2.130  22.311  21.575 1.00 58.81 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.040  21.505  20.931 1.00 26.66 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 6.280  22.170  21.317 1.00 26.80 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 6.920  21.440  22.499 1.00 26.90 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 6.217  20.912  23.380 1.00 27.80 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 5.992  23.608  21.726 1.00 27.07 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 8.255  21.393  22.506 1.00 25.89 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 9.024  20.778  23.578 1.00 24.81 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 10.185 21.749  23.876 1.00 25.68 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 10.223 22.845  23.312 1.00 25.96 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 9.567  19.417  23.101 1.00 25.78 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 10.559 19.587  22.094 1.00 25.58 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 11.118 21.376  24.762 1.00 26.00 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 12.293 22.221  25.005 1.00 27.91 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 13.223 22.255  23.773 1.00 27.52 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 14.062 23.159  23.647 1.00 28.91 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 13.104 21.703  26.221 1.00 34.15 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 12.286 20.988  27.289 1.00 43.73 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 12.135 19.491  27.051 1.00 54.60 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 12.995 18.728  27.550 1.00 58.16 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 11.158 19.079  26.378 1.00 56.08 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 13.076 21.277  22.852 1.00 26.15 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 13.954 21.154  21.710 1.00 25.50 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 13.442 21.785  20.445 1.00 24.28 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.250 22.155  19.595 1.00 24.85 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 14.234 19.669  21.444 1.00 25.22 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 14.782 18.927  22.645 1.00 26.30 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 13.958 18.146  23.441 1.00 27.75 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 16.130 18.987  22.971 1.00 27.23 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 14.458 17.451  24.535 1.00 29.18 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 16.641 18.302  24.068 1.00 28.60 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 15.798 17.554  24.862 1.00 30.51 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.340 16.857  25.929 1.00 33.20 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.107 21.857  20.270 1.00 22.90 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 11.552 22.419  19.034 1.00 22.78 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.282 23.190  19.293 1.00 25.41 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 9.499  22.819  20.175 1.00 25.72 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.146 21.275  18.069 1.00 21.26 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.256 20.368  17.582 1.00 19.51 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.148 20.790  16.615 1.00 19.89 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 12.363 19.064  18.038 1.00 19.29 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.161 19.956  16.147 1.00 18.39 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 13.361 18.205  17.554 1.00 17.92 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.240 18.646  16.586 1.00 17.86 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.263 17.837  16.131 1.00 16.38 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 9.983  24.187  18.447 1.00 26.68 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 8.645  24.800  18.523 1.00 27.21 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.622  23.774  18.032 1.00 27.36 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 7.961  22.745  17.404 1.00 27.78 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 8.748  25.981  17.545 1.00 28.41 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 9.743  25.489  16.502 1.00 29.94 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 10.769 24.698  17.303 1.00 28.12 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.343  24.061  18.248 1.00 27.49 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.253  23.240  17.728 1.00 27.70 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.379  23.238  16.167 1.00 27.67 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.661  24.294  15.584 1.00 27.87 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 3.924  23.854  18.149 1.00 28.92 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.360  22.041  15.532 1.00 26.73 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.616  21.977  14.089 1.00 25.66 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.158  20.633  13.498 1.00 24.89 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 4.776  19.734  14.243 1.00 25.91 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.158  22.145  13.870 1.00 26.09 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 7.912  20.847  14.310 1.00 27.16 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.356  21.028  14.726 1.00 24.70 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.226 19.899  14.335 1.00 23.37 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.246 18.715  14.940 1.00 21.68 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.113 17.775  14.554 1.00 21.07 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.374  18.440  15.904 1.00 22.12 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.223  20.500  12.174 1.00 23.97 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 4.968  19.204  11.553 1.00 23.99 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.315  18.520  11.394 1.00 22.47 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.242  19.096  10.821 1.00 24.03 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.321  19.347  10.170 1.00 25.95 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 2.899  19.827  10.273 1.00 27.93 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.607  21.180  10.292 1.00 29.84 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 1.854  18.934  10.444 1.00 28.48 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 1.308  21.637  10.457 1.00 31.81 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 0.533  19.382  10.566 1.00 30.98 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.275  20.734  10.584 1.00 32.84 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -1.017 21.215  10.710 1.00 37.27 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.425  17.305  11.899 1.00 19.39 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.646  16.515  11.720 1.00 17.39 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.394  15.597  10.525 1.00 16.81 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.332  14.926  10.454 1.00 18.72 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 7.996  15.701  12.978 1.00 17.91 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.234  14.796  12.751 1.00 17.13 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 9.902  14.345  14.048 1.00 17.90 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 9.987  15.093  15.043 1.00 18.51 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.403 13.112  14.063 1.00 14.98 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.294  15.609  9.551  1.00 15.84 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.132  14.816  8.342  1.00 15.10 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.826  13.428  8.495  1.00 16.39 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.692  13.241  9.387  1.00 15.92 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.711  15.576  7.146  1.00 17.66 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.103 15.803  7.349  1.00 18.58 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.462  12.499  7.588  1.00 15.22 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.060  11.164  7.510  1.00 15.94 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.898  10.422  8.852  1.00 15.61 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.754  9.602   9.201  1.00 15.15 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.548 11.263  7.091  1.00 17.44 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.732 11.861  5.720  1.00 19.22 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.851 11.062  4.585  1.00 20.78 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.802 13.157  5.352  1.00 18.41 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.987 11.909  3.560  1.00 21.15 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.951 13.172  3.971  1.00 20.24 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.767  10.660  9.540  1.00 14.53 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.518  10.051  10.854 1.00 15.53 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.480  8.920   10.721 1.00 15.31 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.501  9.042   9.977  1.00 16.18 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 6.946  11.143  11.810 1.00 16.12 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.735  10.704  13.298 1.00 17.85 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.088  10.349  13.997 1.00 16.48 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.132  11.917  14.110 1.00 19.95 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.740  7.812   11.426 1.00 14.80 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.855  6.634   11.411 1.00 14.63 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.344  6.406   12.802 1.00 14.58 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.145  6.376   13.728 1.00 15.44 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.666  5.423   10.971 1.00 15.29 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.229  5.613   9.559  1.00 16.90 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.359  4.310   9.035  1.00 19.38 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.719  4.517   10.201 1.00 20.97 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.019  6.281   12.986 1.00 14.25 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.476  6.070   14.333 1.00 15.40 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.060  4.620   14.562 1.00 14.77 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.600  3.946   13.645 1.00 14.86 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.202  6.940   14.601 1.00 18.03 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.415  8.424   14.610 1.00 23.08 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.092  9.166   14.973 1.00 24.60 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.503  8.844   15.581 1.00 24.12 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.146  4.208   15.810 1.00 14.06 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.664  2.894   16.208 1.00 13.46 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.147  2.962   17.647 1.00 14.17 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.429  3.918   18.372 1.00 14.64 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 3.821  1.871   16.187 1.00 14.75 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.326  1.972   18.039 1.00 13.40 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.898  1.844   19.416 1.00 14.35 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.976  1.076   20.181 1.00 15.44 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.343  -0.060  19.824 1.00 17.34 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.465 1.129   19.495 1.00 15.87 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.879 0.945   20.966 1.00 16.34 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.502 1.928   18.732 1.00 17.34 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.485  1.722   21.214 1.00 15.11 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.561  1.136   22.002 1.00 17.06 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.043  2.113   23.043 1.00 16.94 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.715  3.309   23.013 1.00 17.47 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.770  1.603   24.050 1.00 17.05 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.291  2.469   25.083 1.00 16.80 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.525  3.227   24.642 1.00 16.51 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.455  2.622   24.086 1.00 16.92 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.643  1.636   26.326 1.00 17.28 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.134  2.487   27.447 1.00 16.41 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.300  3.400   28.069 1.00 17.69 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.399  2.632   27.948 1.00 16.11 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.057  4.040   28.951 1.00 17.69 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.341  3.624   28.892 1.00 16.78 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.615  4.508   24.979 1.00 16.92 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 7.772  5.344   24.688 1.00 17.71 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 7.753  6.549   25.645 1.00 20.70 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 6.707  7.187   25.794 1.00 23.67 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 7.683  5.863   23.248 1.00 20.28 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 8.755  6.736   22.887 1.00 27.42 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 8.842  6.794   26.325 1.00 17.53 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 8.911  7.966   27.197 1.00 19.80 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.258 8.638   26.989 1.00 24.35 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.141 8.119   26.289 1.00 25.21 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 8.614  7.550   28.674 1.00 23.46 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.639  6.585   29.181 1.00 24.30 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.350  6.136   30.606 1.00 23.86 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 9.922  6.781   31.513 1.00 26.31 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.601  5.149   30.813 1.00 21.21 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.413 9.894   27.482 1.00 26.84 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 11.708 10.557  27.385 1.00 28.46 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 12.815 9.657   27.881 1.00 27.28 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 12.733 9.095   29.002 1.00 29.16 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 11.549 11.763  28.322 1.00 29.94 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.121 12.080  28.228 1.00 29.99 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 9.450  10.719  28.224 1.00 26.83 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 13.815 9.542   27.028 1.00 24.17 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 14.957 8.672   27.212 1.00 22.25 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 14.935 7.549   26.176 1.00 19.85 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 15.974 6.952   25.899 1.00 20.04 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 13.735 7.218   25.607 1.00 16.93 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 13.660 6.125   24.626 1.00 15.04 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.105 6.531   23.232 1.00 14.33 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.275 5.658   22.382 1.00 13.83 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.217 5.542   24.530 1.00 14.85 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 11.918 4.676   25.757 1.00 15.75 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 10.722 4.656   26.215 1.00 15.10 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 12.862 4.072   26.284 1.00 17.14 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.307 7.838   22.983 1.00 14.10 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 14.746 8.297   21.648 1.00 14.12 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.045 7.623   21.279 1.00 13.42 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 16.911 7.462   22.139 1.00 15.35 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 14.872 9.832   21.541 1.00 14.92 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.273 10.645  21.366 1.00 18.76 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.142 7.202   20.040 1.00 13.59 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.361 6.545   19.587 1.00 13.30 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.254 5.027   19.546 1.00 14.38 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.065 4.375   18.895 1.00 15.31 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.214 4.466   20.164 1.00 12.95 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 15.976 3.015   20.062 1.00 12.25 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.727 2.644   18.599 1.00 12.74 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 14.969 3.320   17.909 1.00 13.45 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.303 1.526   18.178 1.00 13.00 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.144 1.101   16.777 1.00 12.54 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.884 0.300   16.511 1.00 13.16 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.540 -0.597  17.305 1.00 14.03 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.435 0.331   16.353 1.00 14.22 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.565 1.370   16.123 1.00 15.62 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.248 -0.516  15.088 1.00 15.90 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.983 0.671   15.817 1.00 18.27 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.246 0.579   15.367 1.00 12.07 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.120 -0.195  14.808 1.00 12.20 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.736 -0.976  13.629 1.00 13.16 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.415 -0.376  12.771 1.00 13.31 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.038 0.771   14.260 1.00 12.74 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.910 0.095   13.456 1.00 14.16 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.101 -0.853  14.371 1.00 14.70 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.982  1.191   12.828 1.00 15.36 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.573 -2.331  13.653 1.00 13.67 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 14.103 -3.201  12.607 1.00 14.81 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.983 -4.058  12.045 1.00 14.57 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 12.098 -4.539  12.770 1.00 15.53 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 15.147 -4.177  13.250 1.00 17.67 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.531 -3.592  13.519 1.00 21.45 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.584 -4.612  14.102 1.00 24.52 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 18.987 -4.127  13.891 1.00 25.13 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 19.775 -4.486  12.881 1.00 27.33 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.310 -5.275  11.908 1.00 25.22 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 21.014 -3.997  12.787 1.00 30.76 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 13.106 -4.353  10.761 1.00 14.26 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 12.266 -5.398  10.143 1.00 15.75 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 13.214 -6.525  9.689  1.00 16.50 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.428 -6.495  9.976  1.00 17.20 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.501 -4.808  8.967  1.00 17.33 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.604 -4.325  7.588  1.00 16.70 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.685 -7.561  8.976  1.00 18.34 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.544 -8.653  8.515  1.00 20.07 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.657 -8.189  7.536  1.00 20.68 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.627 -8.943  7.329  1.00 22.40 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.684 -9.771  7.859  1.00 22.50 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 12.072 -9.299  6.532  1.00 28.79 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 11.048 -10.261 5.976  1.00 38.95 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.820  -10.030 6.029  1.00 43.16 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 11.541 -11.344 5.427  1.00 38.76 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 14.569 -6.972  6.976  1.00 19.51 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 15.542 -6.463  5.985  1.00 18.53 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.650 -5.601  6.576  1.00 18.32 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.644 -5.346  5.883  1.00 18.91 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.860 -5.660  4.854  1.00 18.46 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.737 -6.423  4.207  1.00 20.94 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 12.408 -6.133  4.453  1.00 20.75 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.795 -7.472  3.336  1.00 23.82 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.694 -7.006  3.758  1.00 23.88 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 12.479 -7.859  3.093  1.00 24.18 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.485 -5.189  7.841  1.00 16.69 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.476 -4.338  8.469  1.00 15.65 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.854 -3.198  9.264  1.00 14.50 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.672 -3.232  9.615  1.00 15.19 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.650 -2.171  9.489  1.00 14.70 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.201 -0.997  10.270 1.00 14.55 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.208 -0.143  9.481  1.00 13.69 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.486 0.234   8.323  1.00 15.05 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.406 -0.160  10.721 1.00 15.34 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.908 1.136   11.399 1.00 15.68 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.301 -0.968  11.671 1.00 17.27 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 15.061 0.163   10.103 1.00 13.96 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 14.016 0.962   9.469  1.00 13.91 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.103 2.443   9.944  1.00 14.23 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.883 3.376   9.175  1.00 14.03 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.630 0.378   9.844  1.00 14.57 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.481 1.299   9.408  1.00 15.50 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.443 -1.034  9.271  1.00 14.99 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.378 2.641   11.244 1.00 12.68 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.379 4.017   11.783 1.00 13.94 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.663 4.032   13.271 1.00 12.72 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.033 2.993   13.833 1.00 13.28 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.551 5.231   13.889 1.00 11.85 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.845 5.335   15.328 1.00 12.31 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.706 6.023   16.037 1.00 12.45 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.044 6.893   15.458 1.00 12.16 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.171 6.093   15.603 1.00 13.97 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.203 7.420   14.836 1.00 15.87 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.374 5.218   15.303 1.00 16.86 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.487 8.259   15.303 1.00 17.74 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.478 5.675   17.346 1.00 11.67 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.429 6.372   18.118 1.00 11.30 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.701 7.888   18.149 1.00 11.79 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 13.852 8.274   18.389 1.00 12.26 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.410 5.819   19.564 1.00 12.24 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.424 6.625   20.429 1.00 13.38 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.011 4.327   19.569 1.00 13.09 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.678 8.697   17.931 1.00 12.33 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 11.803 10.141  17.921 1.00 13.03 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 10.702 10.832  18.730 1.00 15.11 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 10.911 11.952  19.194 1.00 15.58 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 11.812 10.612  16.459 1.00 13.51 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 11.861 12.041  16.359 1.00 14.89 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.498  10.211  18.825 1.00 15.32 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.391  10.839  19.584 1.00 16.45 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.675  9.764   20.445 1.00 17.06 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 7.880  8.565   20.242 1.00 16.54 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.363  11.547  18.635 1.00 19.30 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.547  10.551  18.011 1.00 21.46 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 7.984  12.458  17.599 1.00 20.64 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 6.812  10.197  21.373 1.00 18.52 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.087  9.230   22.197 1.00 20.76 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 4.986  9.857   23.013 1.00 21.13 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 4.618  10.978  22.746 1.00 21.65 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.537  9.153   24.047 1.00 23.34 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.475  9.600   24.934 1.00 22.18 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.126  9.024   24.569 1.00 21.67 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.885  8.590   23.435 1.00 21.01 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.236  9.013   25.537 1.00 21.89 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? -0.160 8.572   25.324 1.00 23.54 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.302 7.151   24.782 1.00 21.12 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.341 6.857   24.169 1.00 22.66 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.862 9.547   24.332 1.00 27.65 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.856 11.023  24.707 1.00 32.48 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.188 11.387  25.830 1.00 34.26 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.547 11.903  23.748 1.00 31.97 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.666  6.262   24.984 1.00 18.59 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.584  4.902   24.462 1.00 17.61 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 0.938  4.798   22.982 1.00 16.45 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.772  3.733   22.374 1.00 17.40 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.573  5.872   22.435 1.00 15.27 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.071  5.882   21.059 1.00 14.40 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.599  5.954   21.049 1.00 14.15 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.214  6.457   21.981 1.00 15.67 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.542  7.106   20.292 1.00 15.28 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.005  7.076   20.052 1.00 18.40 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.546 8.473   19.736 1.00 20.80 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.365 6.069   18.928 1.00 18.31 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.184  5.534   19.921 1.00 12.69 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.629  5.638   19.738 1.00 12.26 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.818  6.063   18.263 1.00 13.30 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.136  5.539   17.375 1.00 14.60 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.411  4.357   20.091 1.00 13.27 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 5.892  3.110   19.377 1.00 16.40 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 7.912  4.577   19.838 1.00 13.98 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.639  7.094   18.041 1.00 13.21 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 6.880  7.592   16.691 1.00 13.73 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.325  7.391   16.285 1.00 12.89 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.225  7.579   17.100 1.00 14.39 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.545  6.935   15.050 1.00 12.44 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.900  6.586   14.569 1.00 11.99 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.257 7.475   13.362 1.00 12.83 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.452  7.589   12.417 1.00 13.51 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.943  5.118   14.085 1.00 11.98 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.454  4.092   15.102 1.00 12.92 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.303 3.616   16.074 1.00 12.88 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.131  3.643   15.081 1.00 14.63 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.865  2.686   17.002 1.00 12.27 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.695  2.664   15.974 1.00 14.14 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.554  2.236   16.976 1.00 13.23 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.473 8.007   13.387 1.00 12.35 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 11.991 8.755   12.251 1.00 12.76 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.499 7.709   11.233 1.00 12.07 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.443 6.959   11.533 1.00 12.63 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.142 9.661   12.707 1.00 13.19 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.924 7.692   10.013 1.00 12.51 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.345 6.750   8.987  1.00 13.60 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.719 7.116   8.449  1.00 14.29 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.043 8.313   8.297  1.00 13.92 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.362 6.801   7.812  1.00 15.48 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.602 5.754   6.743  1.00 19.43 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.780 4.590   7.088  1.00 18.67 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.662 6.130   5.542  1.00 23.74 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.528 6.064   8.099  1.00 13.43 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.812 6.303   7.447  1.00 13.86 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.926 5.541   6.117  1.00 14.58 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.974 5.621   5.465  1.00 15.01 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.039 5.982   8.330  1.00 14.88 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.028 6.857   9.611  1.00 15.21 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.078 4.482   8.674  1.00 14.55 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.862 4.811   5.705  1.00 14.37 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.963 3.919   4.532  1.00 15.04 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 15.111 4.636   3.227  1.00 17.82 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.597 4.035   2.262  1.00 19.76 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.744 2.984   4.472  1.00 15.38 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.691 1.993   5.644  1.00 16.45 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.426 1.191   5.532  1.00 16.36 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.264 2.024   5.827  1.00 15.32 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 10.023 1.550   5.947  1.00 18.63 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.761  0.264   5.669  1.00 16.97 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 9.034  2.354   6.336  1.00 18.00 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.726 5.933   3.187  1.00 16.51 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.839 6.715   1.949  1.00 18.38 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 16.234 7.321   1.776  1.00 18.45 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.511 7.873   0.710  1.00 19.21 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.805 7.849   1.917  1.00 19.86 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.980 8.869   3.013  1.00 21.22 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.155 8.453   4.190  1.00 21.55 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.924 10.099  2.709  1.00 23.91 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.097 7.262   2.790  1.00 17.37 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.449 7.863   2.726  1.00 16.36 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.396 6.878   2.073  1.00 17.34 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 20.202 6.219   2.732  1.00 17.43 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.890 8.223   4.152  1.00 16.09 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.916 9.182   4.875  1.00 17.52 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.330 9.395   6.310  1.00 18.02 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.784 10.545  4.162  1.00 17.75 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 19.277 6.749   0.729  1.00 17.01 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 20.073 5.698   0.046  1.00 19.67 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.569 5.909   0.113  1.00 20.48 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 22.339 4.929   0.057  1.00 21.29 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.648 5.564   -1.415 1.00 20.66 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 18.145 5.447   -1.701 1.00 23.15 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.954 5.028   -3.158 1.00 24.53 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.419 4.467   -0.760 1.00 23.24 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.985 7.190   0.244  1.00 19.94 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.390 7.537   0.314  1.00 20.97 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 24.075 6.976   1.560  1.00 21.91 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.312 6.943   1.601  1.00 24.23 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.570 9.065   0.194  1.00 21.20 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.748 9.868   1.186  1.00 20.48 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.490 10.380  1.007  1.00 20.45 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 23.127 10.195  2.528  1.00 19.98 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 21.103 11.089  2.135  1.00 20.31 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 22.102 11.004  3.075  1.00 19.68 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.283 9.965   3.285  1.00 20.59 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.173 11.528  4.369  1.00 20.10 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.374 10.517  4.549  1.00 20.68 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.322 11.293  5.072  1.00 20.47 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.312 6.524   2.590  1.00 20.19 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.955 5.958   3.787  1.00 21.33 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.757 4.687   3.436  1.00 25.20 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.683 4.343   4.175  1.00 26.07 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.913 5.580   4.846  1.00 20.35 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.272 6.743   5.598  1.00 19.61 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.139 6.203   6.487  1.00 20.73 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.329 7.524   6.494  1.00 19.00 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.363 3.987   2.334  1.00 28.38 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.944 2.720   1.854  1.00 32.47 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 26.193 2.893   1.036  1.00 36.89 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.773 1.881   0.664  1.00 38.87 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.957 1.994   0.916  1.00 34.67 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.686 1.485   1.509  1.00 40.32 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 22.647 1.291   2.736  1.00 41.36 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.713 1.269   0.738  1.00 45.15 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.549 4.121   0.650  1.00 38.95 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.729 4.375   -0.164 1.00 42.26 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 28.621 5.395   0.546  1.00 44.01 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 29.646 5.795   -0.008 1.00 45.72 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 27.305 4.894   -1.550 1.00 45.59 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 26.584 6.232   -1.481 1.00 52.50 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 25.620 6.512   -2.616 1.00 61.77 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 25.491 7.696   -3.009 1.00 63.85 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 24.982 5.550   -3.104 1.00 64.73 ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 15.217 -23.982 8.494  1.00 27.86 ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 14.086 -23.826 9.424  1.00 27.67 ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 14.043 -24.965 10.452 1.00 25.54 ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 14.643 -26.034 10.234 1.00 26.38 ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 12.757 -23.765 8.659  1.00 30.19 ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 12.544 -25.007 8.004  1.00 33.56 ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 13.322 -24.755 11.551 1.00 22.12 ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 13.167 -25.784 12.575 1.00 20.16 ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 12.925 -25.205 13.954 1.00 18.27 ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 13.294 -24.057 14.219 1.00 19.78 ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 12.284 -25.966 14.821 1.00 17.43 ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 11.955 -25.515 16.178 1.00 16.76 ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 12.000 -26.671 17.173 1.00 15.64 ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 11.915 -27.859 16.784 1.00 17.11 ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 10.543 -24.886 16.194 1.00 17.16 ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 12.075 -26.348 18.470 1.00 15.27 ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 11.958 -27.283 19.563 1.00 14.95 ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 10.596 -27.070 20.220 1.00 16.24 ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 10.213 -25.954 20.497 1.00 16.60 ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 13.073 -27.044 20.613 1.00 15.44 ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 14.458 -27.080 19.964 1.00 16.34 ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 12.989 -28.062 21.751 1.00 17.00 ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 15.567 -26.462 20.930 1.00 17.88 ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 9.857  -28.148 20.478 1.00 17.71 ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 8.542  -28.085 21.092 1.00 17.96 ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 8.594  -28.814 22.414 1.00 18.91 ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 8.747  -30.037 22.428 1.00 20.06 ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 7.496  -28.736 20.162 1.00 18.25 ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 7.309  -27.948 18.884 1.00 18.16 ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 6.441  -26.864 18.834 1.00 19.27 ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 8.052  -28.240 17.747 1.00 20.11 ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 6.296  -26.109 17.672 1.00 21.99 ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 7.920  -27.481 16.581 1.00 21.79 ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 7.046  -26.417 16.549 1.00 23.33 ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 6.960  -25.658 15.402 1.00 25.29 ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 8.506  -28.099 23.519 1.00 19.41 ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 8.621  -28.701 24.840 1.00 20.50 ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 7.544  -28.097 25.725 1.00 20.90 ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 7.421  -26.877 25.820 1.00 20.41 ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 10.061 -28.521 25.426 1.00 22.47 ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 10.517 -27.067 25.356 1.00 22.80 ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 10.137 -29.062 26.853 1.00 23.95 ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 6.659  -28.935 26.289 1.00 22.50 ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 5.575  -28.429 27.129 1.00 23.98 ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 4.678  -27.514 26.319 1.00 24.31 ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 4.386  -27.826 25.162 1.00 25.47 ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 4.376  -26.315 26.834 1.00 23.08 ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 3.608  -25.350 26.053 1.00 23.27 ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 4.514  -24.257 25.475 1.00 21.07 ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 4.090  -23.090 25.366 1.00 21.28 ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 2.466  -24.754 26.863 1.00 26.74 ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 1.374  -25.767 27.117 1.00 34.89 ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 0.658  -26.196 26.193 1.00 38.26 ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 1.234  -26.170 28.371 1.00 36.19 ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 5.745  -24.627 25.082 1.00 19.92 ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 6.706  -23.680 24.519 1.00 18.37 ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 7.193  -24.140 23.147 1.00 17.54 ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 7.342  -25.357 22.890 1.00 18.42 ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 7.961  -23.585 25.416 1.00 18.72 ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 7.682  -23.026 26.788 1.00 20.31 ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 7.028  -21.807 26.941 1.00 22.21 ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 8.067  -23.715 27.934 1.00 21.01 ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 6.746  -21.297 28.203 1.00 24.09 ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 7.797  -23.209 29.205 1.00 22.47 ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 7.152  -21.990 29.330 1.00 24.80 ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 6.876  -21.463 30.575 1.00 28.00 ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 7.487  -23.158 22.282 1.00 15.29 ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 8.109  -23.363 20.957 1.00 15.48 ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 9.384  -22.522 20.975 1.00 15.36 ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 9.324  -21.324 21.249 1.00 15.80 ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 7.161  -22.933 19.832 1.00 16.36 ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 7.808  -22.625 18.480 1.00 17.44 ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 6.778  -22.302 17.385 1.00 17.85 ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 7.261  -21.315 16.406 1.00 20.03 ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 7.712  -21.598 15.182 1.00 22.47 ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 7.871  -22.869 14.798 1.00 21.71 ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 8.084  -20.618 14.362 1.00 21.94 ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 10.564 -23.150 20.752 1.00 14.71 ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 11.871 -22.493 20.721 1.00 14.16 ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 12.334 -22.373 19.271 1.00 14.41 ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 12.467 -23.390 18.591 1.00 15.75 ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 12.939 -23.262 21.551 1.00 16.31 ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 14.215 -22.411 21.687 1.00 16.87 ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 12.405 -23.675 22.926 1.00 16.72 ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 12.552 -21.153 18.792 1.00 14.02 ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 12.981 -20.944 17.411 1.00 14.49 ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 14.198 -19.990 17.370 1.00 14.30 ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 14.467 -19.244 18.342 1.00 14.32 ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 11.823 -20.346 16.575 1.00 17.15 ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 10.697 -21.355 16.426 1.00 21.51 ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 11.315 -19.025 17.186 1.00 15.77 ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 14.885 -19.928 16.208 1.00 13.22 ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 15.904 -18.898 16.023 1.00 13.42 ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 15.158 -17.533 16.061 1.00 14.72 ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 14.163 -17.361 15.325 1.00 14.94 ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 16.578 -19.026 14.642 1.00 14.42 ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.424 -20.277 14.539 1.00 15.96 ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 16.964 -21.337 14.113 1.00 15.45 ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 18.691 -20.168 14.970 1.00 15.66 ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 15.656 -16.582 16.853 1.00 14.15 ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 14.981 -15.277 16.954 1.00 13.67 ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 14.823 -14.605 15.582 1.00 16.02 ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 13.765 -14.029 15.304 1.00 15.95 ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 15.729 -14.386 17.935 1.00 14.41 ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 14.954 -13.092 18.288 1.00 14.81 ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 15.905 -12.219 19.088 1.00 15.57 ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 15.321 -10.957 19.621 1.00 16.37 ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 15.262 -9.816  18.954 1.00 17.98 ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 15.595 -9.769  17.671 1.00 18.30 ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 14.786 -8.722  19.542 1.00 17.25 ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 15.848 -14.770 14.697 1.00 15.56 ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 15.761 -14.086 13.395 1.00 16.24 ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 14.748 -14.718 12.450 1.00 16.13 ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 14.440 -14.127 11.417 1.00 17.86 ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.165 -13.952 12.752 1.00 16.33 ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 17.776 -15.202 12.217 1.00 17.19 ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 18.423 -16.101 13.052 1.00 16.54 ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 17.855 -15.643 10.941 1.00 18.44 ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 18.887 -17.072 12.261 1.00 17.58 ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 18.578 -16.833 10.977 1.00 19.66 ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 14.268 -15.940 12.758 1.00 15.24 ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 13.261 -16.592 11.928 1.00 16.08 ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 11.875 -16.591 12.602 1.00 17.35 ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 10.943 -17.195 12.059 1.00 18.02 ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 13.710 -18.051 11.637 1.00 16.39 ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 15.018 -18.147 10.850 1.00 18.34 ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 15.378 -19.626 10.589 1.00 20.06 ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 14.923 -17.370 9.477  1.00 18.31 ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 11.726 -15.911 13.782 1.00 16.31 ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 10.429 -15.907 14.462 1.00 17.46 ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 9.362  -15.267 13.574 1.00 17.17 ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 9.630  -14.291 12.890 1.00 17.54 ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 10.531 -15.131 15.774 1.00 17.25 ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 8.145  -15.780 13.680 1.00 17.57 ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 7.002  -15.295 12.873 1.00 18.20 ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 6.226  -14.190 13.616 1.00 19.53 ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 6.456  -13.973 14.815 1.00 18.97 ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 6.053  -16.484 12.564 1.00 20.31 ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 5.455  -16.921 13.797 1.00 21.82 ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 6.764  -17.630 11.865 1.00 19.28 ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 5.226  -13.557 12.945 1.00 19.78 ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 4.367  -12.587 13.654 1.00 20.08 ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 3.649  -13.299 14.829 1.00 19.70 ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 3.529  -12.747 15.922 1.00 19.95 ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 3.272  -12.073 12.684 1.00 23.35 ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 3.803  -11.239 11.564 1.00 31.61 ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 4.542  -10.083 11.799 1.00 35.58 ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 3.621  -11.374 10.229 1.00 35.24 ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 4.784  -9.557  10.606 1.00 36.88 ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 4.262  -10.303 9.630  1.00 37.13 ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 3.240  -14.570 14.610 1.00 19.54 ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 2.551  -15.307 15.692 1.00 19.88 ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 3.477  -15.552 16.857 1.00 19.17 ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 3.048  -15.497 18.011 1.00 19.05 ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 2.005  -16.631 15.189 1.00 22.09 ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 1.106  -17.295 16.203 1.00 30.30 ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? -0.002 -16.815 16.491 1.00 32.91 ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 1.564  -18.438 16.734 1.00 31.17 ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 4.775  -15.876 16.584 1.00 18.35 ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 5.718  -16.054 17.690 1.00 17.93 ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 5.834  -14.769 18.523 1.00 17.61 ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 5.785  -14.830 19.750 1.00 18.85 ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 7.118  -16.401 17.153 1.00 17.31 ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 7.237  -17.819 16.618 1.00 19.39 ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 6.650  -18.737 17.236 1.00 20.29 ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 7.921  -18.003 15.580 1.00 18.40 ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 5.946  -13.614 17.854 1.00 17.69 ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 6.044  -12.355 18.584 1.00 18.89 ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 4.748  -11.983 19.337 1.00 20.32 ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 4.822  -11.416 20.432 1.00 21.34 ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 6.506  -11.231 17.635 1.00 18.78 ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 7.988  -11.187 17.427 1.00 16.91 ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 8.685  -11.631 16.346 1.00 17.91 ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 8.951  -10.617 18.333 1.00 16.96 ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 10.041 -11.428 16.546 1.00 18.05 ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 10.222 -10.766 17.742 1.00 17.61 ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 8.853  -9.993  19.582 1.00 18.16 ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 11.393 -10.316 18.368 1.00 18.21 ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 10.015 -9.557  20.209 1.00 18.74 ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 11.268 -9.740  19.606 1.00 18.00 ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 3.586  -12.338 18.785 1.00 19.35 ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 2.318  -12.039 19.452 1.00 20.26 ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 2.117  -12.933 20.702 1.00 21.45 ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 1.213  -12.653 21.491 1.00 23.08 ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 1.161  -12.264 18.473 1.00 19.52 ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 2.800  -14.107 20.768 1.00 19.50 ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 2.673  -15.029 21.891 1.00 18.36 ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 4.065  -15.172 22.586 1.00 18.67 ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 4.437  -16.238 23.028 1.00 18.08 ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 2.206  -16.372 21.371 1.00 19.35 ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 0.766  -16.224 20.894 1.00 22.90 ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? -0.170 -16.118 21.698 1.00 22.16 ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 0.591  -16.127 19.583 1.00 24.46 ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 4.780  -14.077 22.670 1.00 18.84 ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 6.138  -14.070 23.209 1.00 18.15 ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 6.215  -14.440 24.684 1.00 19.62 ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 5.483  -13.886 25.505 1.00 21.82 ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 6.706  -12.663 23.016 1.00 18.56 ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 8.131  -12.462 23.538 1.00 18.99 ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 9.122  -13.313 22.735 1.00 19.87 ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 8.523  -11.005 23.424 1.00 18.86 ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 7.151  -15.343 25.038 1.00 17.84 ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 7.440  -15.691 26.429 1.00 18.82 ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 8.791  -15.047 26.813 1.00 20.04 ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 8.939  -14.428 27.880 1.00 21.05 ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 7.518  -17.234 26.594 1.00 20.36 ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 8.017  -17.624 27.998 1.00 20.84 ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 6.157  -17.868 26.292 1.00 21.25 ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 9.798  -15.189 25.937 1.00 18.00 ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 11.156 -14.727 26.229 1.00 17.49 ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 11.923 -14.640 24.932 1.00 17.05 ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 11.746 -15.487 24.050 1.00 17.41 ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 11.864 -15.696 27.225 1.00 18.68 ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 13.345 -15.471 27.417 1.00 18.98 ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 13.955 -14.607 28.281 1.00 21.05 ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 14.408 -16.200 26.760 1.00 17.58 ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 15.343 -14.718 28.160 1.00 21.18 ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 15.635 -15.709 27.256 1.00 19.47 ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 14.433 -17.226 25.803 1.00 17.85 ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 16.874 -16.241 26.849 1.00 18.44 ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 15.660 -17.758 25.418 1.00 18.52 ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 16.862 -17.248 25.913 1.00 17.84 ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 12.799 -13.645 24.807 1.00 16.45 ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 13.688 -13.569 23.650 1.00 16.66 ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 15.010 -12.974 24.069 1.00 17.49 ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 15.052 -12.157 24.992 1.00 17.58 ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 13.067 -12.813 22.449 1.00 17.36 ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 12.515 -11.424 22.780 1.00 19.26 ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 13.530 -10.296 22.903 1.00 22.52 ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 13.276 -9.317  23.653 1.00 24.31 ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 14.569 -10.349 22.212 1.00 19.67 ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 16.079 -13.337 23.353 1.00 17.07 ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.405 -12.802 23.661 1.00 16.83 ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 18.174 -12.654 22.364 1.00 15.79 ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 18.593 -13.636 21.756 1.00 15.84 ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 18.110 -13.669 24.709 1.00 17.23 ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 19.457 -13.159 25.175 1.00 21.89 ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 20.136 -12.495 24.393 1.00 24.39 ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 19.855 -13.488 26.320 1.00 21.74 ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 18.320 -11.391 21.893 1.00 15.23 ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 19.018 -11.107 20.662 0.50 15.56 ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 19.016 -11.152 20.638 0.50 15.45 ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 20.471 -11.607 20.701 1.00 16.43 ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 20.970 -12.102 19.695 1.00 17.56 ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 18.973 -9.601  20.397 0.50 17.54 ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 18.941 -9.678  20.240 0.50 17.10 ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 19.676 -9.249  19.226 0.50 20.59 ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 19.697 -8.923  21.168 0.50 19.58 ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 21.120 -11.508 21.885 1.00 15.10 ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 22.525 -11.930 21.961 1.00 15.07 ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 22.651 -13.438 21.787 1.00 16.46 ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 23.748 -13.862 21.468 1.00 18.37 ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 23.181 -11.522 23.278 1.00 19.11 ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 22.758 -12.290 24.390 1.00 24.17 ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 21.602 -14.199 22.001 1.00 13.88 ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 21.655 -15.672 21.824 1.00 13.81 ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 20.985 -16.157 20.529 1.00 13.78 ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 21.025 -17.363 20.211 1.00 13.05 ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 20.908 -16.375 23.000 1.00 14.34 ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 21.624 -16.134 24.317 1.00 15.01 ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 20.902 -16.767 25.514 1.00 15.07 ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 20.931 -18.218 25.433 1.00 14.20 ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 20.858 -19.027 26.485 1.00 14.76 ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 20.799 -18.530 27.716 1.00 16.21 ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 20.900 -20.349 26.317 1.00 15.53 ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 20.345 -15.269 19.792 1.00 13.95 ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 19.525 -15.638 18.620 1.00 13.43 ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 18.415 -16.627 18.982 1.00 13.64 ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 18.082 -17.477 18.170 1.00 13.49 ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 20.376 -16.215 17.440 1.00 13.53 ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 19.596 -16.457 16.148 1.00 14.86 ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 18.698 -15.607 15.800 1.00 15.72 ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 19.842 -17.518 15.467 1.00 13.90 ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 17.802 -16.461 20.173 1.00 13.11 ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 16.688 -17.331 20.554 1.00 13.16 ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 15.412 -16.574 20.856 1.00 14.07 ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 15.458 -15.471 21.418 1.00 14.75 ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 17.024 -18.144 21.822 1.00 13.86 ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 18.085 -19.235 21.677 1.00 15.32 ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 18.311 -19.912 23.069 1.00 16.30 ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 17.673 -20.255 20.615 1.00 16.63 ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 14.280 -17.207 20.551 1.00 13.05 ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 12.963 -16.670 20.919 1.00 14.06 ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 12.099 -17.865 21.318 1.00 14.29 ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 12.185 -18.934 20.700 1.00 14.58 ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 12.358 -15.829 19.797 1.00 14.79 ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 10.992 -15.190 20.126 1.00 14.22 ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 10.833 -13.858 19.345 1.00 14.67 ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 9.806  -16.137 19.744 1.00 16.00 ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 11.324 -17.724 22.402 1.00 14.53 ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 10.413 -18.772 22.876 1.00 14.80 ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 9.007  -18.156 22.871 1.00 14.91 ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 8.795  -17.052 23.405 1.00 15.28 ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 10.791 -19.247 24.293 1.00 15.70 ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 9.767  -20.263 24.811 1.00 16.58 ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 12.204 -19.855 24.276 1.00 15.37 ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 8.070  -18.868 22.261 1.00 15.16 ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 6.668  -18.445 22.229 1.00 15.84 ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 5.809  -19.533 22.890 1.00 18.34 ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 6.234  -20.685 23.039 1.00 18.46 ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 6.228  -18.201 20.792 1.00 17.17 ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 6.366  -19.339 19.950 1.00 19.09 ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 4.565  -19.161 23.254 1.00 19.19 ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 3.674  -20.126 23.886 1.00 21.60 ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 2.826  -20.876 22.831 1.00 23.35 ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 2.505  -20.340 21.765 1.00 23.92 ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 2.775  -19.421 24.885 1.00 22.97 ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 2.041  -18.404 24.231 1.00 25.70 ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 2.481  -22.131 23.141 1.00 24.07 ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 1.667  -22.962 22.246 1.00 27.13 ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 0.437  -23.471 23.002 1.00 30.46 ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 0.428  -23.501 24.236 1.00 30.31 ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 2.484  -24.202 21.783 1.00 28.52 ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 2.685  -25.071 22.891 1.00 30.36 ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 3.829  -23.844 21.190 1.00 29.00 ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? -0.588 -23.890 22.262 1.00 32.72 ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? -1.768 -24.488 22.863 1.00 35.08 ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? -1.600 -26.010 22.989 1.00 36.19 ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? -2.169 -26.608 23.902 1.00 38.25 ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? -3.014 -24.125 22.048 1.00 37.16 ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? -2.789 -24.492 20.687 1.00 39.51 ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? -3.337 -22.629 22.124 1.00 37.67 ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? -0.850 -26.636 22.070 1.00 34.98 ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? -0.618 -28.079 22.066 1.00 34.90 ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 0.620  -28.460 22.886 1.00 34.79 ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 1.570  -27.692 22.946 1.00 34.58 ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? -0.447 -28.566 20.636 1.00 35.10 ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 0.613  -29.645 23.482 1.00 34.15 ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 1.717  -30.134 24.302 1.00 34.72 ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 2.864  -30.629 23.413 1.00 33.50 ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 2.648  -31.426 22.505 1.00 34.81 ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 1.200  -31.267 25.217 1.00 37.98 ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 2.279  -31.979 26.028 1.00 44.20 ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 2.717  -31.224 27.260 1.00 52.24 ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 2.085  -30.247 27.687 1.00 54.65 ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 3.812  -31.679 27.869 1.00 54.15 ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 4.071  -30.121 23.677 1.00 30.21 ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 5.276  -30.513 22.950 1.00 28.77 ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 5.938  -31.658 23.674 1.00 27.48 ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 5.924  -31.689 24.913 1.00 28.12 ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 6.518  -32.591 22.925 1.00 25.85 ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 7.104  -33.769 23.549 1.00 25.52 ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 8.625  -33.890 23.414 1.00 24.05 ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 9.141  -34.993 23.650 1.00 24.89 ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 6.407  -35.035 23.065 1.00 27.17 ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 4.631  -35.065 23.409 1.00 34.39 ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 9.338  -32.829 23.020 1.00 20.47 ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 10.810 -32.931 22.968 1.00 19.53 ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 11.367 -32.929 24.391 1.00 21.20 ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 10.827 -32.241 25.284 1.00 23.89 ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 11.422 -31.765 22.156 1.00 21.06 ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 11.102 -31.809 20.667 1.00 26.63 ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 10.743 -32.893 20.166 1.00 28.15 ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 11.197 -30.754 19.999 1.00 25.31 ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 12.433 -33.688 24.615 1.00 20.00 ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 13.093 -33.719 25.926 1.00 20.98 ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 14.354 -32.858 25.792 1.00 19.29 ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 15.128 -33.092 24.879 1.00 19.42 ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 13.535 -35.165 26.262 1.00 26.75 ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 12.353 -35.969 26.490 1.00 29.68 ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 14.439 -35.207 27.494 1.00 27.62 ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 14.558 -31.890 26.686 1.00 18.11 ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 15.769 -31.064 26.662 1.00 17.11 ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 16.878 -31.729 27.481 1.00 16.31 ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 16.637 -32.210 28.606 1.00 16.50 ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 15.492 -29.662 27.252 1.00 18.82 ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 14.261 -28.982 26.621 1.00 21.29 ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 16.744 -28.766 27.140 1.00 18.47 ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 14.421 -28.798 25.100 1.00 22.80 ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 18.077 -31.830 26.908 1.00 14.96 ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 19.231 -32.367 27.623 1.00 14.95 ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 19.637 -31.440 28.760 1.00 13.70 ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 19.603 -30.220 28.618 1.00 14.05 ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 20.415 -32.495 26.646 1.00 14.31 ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 20.041 -32.046 29.903 1.00 13.89 ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 20.525 -31.294 31.085 1.00 13.71 ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 21.861 -31.960 31.388 1.00 14.08 ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 21.937 -32.984 32.083 1.00 15.58 ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 19.544 -31.380 32.270 1.00 13.20 ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 18.141 -30.866 31.903 1.00 15.59 ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 18.107 -29.373 31.516 1.00 17.10 ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 16.719 -28.958 31.218 1.00 17.30 ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 16.391 -27.835 30.583 1.00 18.43 ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.327 -26.998 30.188 1.00 16.52 ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 15.111 -27.551 30.333 1.00 20.43 ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 22.934 -31.409 30.795 1.00 13.88 ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 24.233 -32.044 30.784 1.00 14.58 ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 25.351 -31.124 30.282 1.00 15.36 ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 25.088 -30.007 29.860 1.00 14.63 ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 24.129 -33.264 29.864 1.00 14.01 ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 23.997 -32.828 28.085 1.00 14.27 ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 26.629 -31.651 30.283 1.00 15.10 ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 27.757 -30.939 29.712 1.00 15.85 ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 28.372 -31.718 28.535 1.00 16.85 ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 29.569 -31.611 28.271 1.00 16.17 ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 28.834 -30.626 30.769 1.00 18.52 ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 29.459 -31.836 31.392 1.00 23.09 ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 29.047 -32.982 31.054 1.00 23.38 ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 30.415 -31.657 32.213 1.00 29.13 ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 27.563 -32.481 27.800 1.00 15.27 ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 28.045 -33.256 26.632 1.00 14.83 ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 28.718 -32.322 25.651 1.00 13.58 ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 28.300 -31.164 25.462 1.00 13.59 ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 26.876 -33.953 25.928 1.00 14.21 ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 26.352 -35.463 26.758 1.00 15.90 ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 29.728 -32.874 24.971 1.00 12.75 ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 30.418 -32.202 23.866 1.00 12.73 ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 30.428 -33.078 22.639 1.00 13.33 ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 31.232 -32.838 21.723 1.00 13.88 ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 31.858 -31.789 24.216 1.00 13.86 ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 31.870 -30.509 25.121 1.00 14.09 ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 33.288 -30.102 25.418 1.00 17.49 ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 33.787 -30.285 26.552 1.00 18.89 ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 33.958 -29.599 24.385 1.00 16.41 ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 29.564 -34.133 22.587 1.00 13.28 ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 29.410 -34.919 21.356 1.00 13.47 ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 27.908 -35.113 21.164 1.00 13.28 ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 27.135 -35.193 22.133 1.00 14.60 ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 30.098 -36.274 21.407 1.00 18.37 ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 29.581 -37.042 22.500 1.00 22.06 ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 31.595 -36.174 21.593 1.00 19.30 ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 27.501 -35.162 19.888 1.00 12.33 ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 26.076 -35.333 19.582 1.00 12.54 ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 25.883 -35.462 18.084 1.00 11.78 ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 26.846 -35.682 17.357 1.00 14.52 ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 24.635 -35.405 17.656 1.00 11.40 ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 24.280 -35.550 16.241 1.00 11.98 ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 23.387 -34.371 15.876 1.00 12.95 ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 22.422 -34.109 16.595 1.00 12.42 ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 23.541 -36.910 16.018 1.00 13.04 ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 23.086 -37.074 14.546 1.00 14.60 ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 24.451 -38.069 16.383 1.00 13.92 ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 23.654 -33.734 14.696 1.00 12.98 ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 22.729 -32.670 14.258 1.00 11.86 ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 22.121 -32.955 12.890 1.00 12.99 ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 22.696 -33.695 12.087 1.00 12.73 ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 23.401 -31.248 14.252 1.00 12.59 ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 24.315 -30.978 13.061 1.00 13.02 ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 25.603 -31.509 13.008 1.00 14.25 ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 23.930 -30.105 12.051 1.00 12.75 ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 26.474 -31.215 11.954 1.00 15.58 ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 24.788 -29.809 10.981 1.00 14.09 ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 26.044 -30.399 10.923 1.00 15.65 ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 26.922 -30.116 9.902  1.00 17.69 ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 20.951 -32.368 12.644 1.00 13.28 ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 20.317 -32.496 11.338 1.00 12.99 ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 20.746 -31.350 10.448 1.00 13.45 ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 20.589 -30.185 10.794 1.00 13.43 ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 18.785 -32.575 11.458 1.00 14.25 ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 18.144 -32.742 10.098 1.00 16.37 ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 18.330 -33.904 9.368  1.00 17.28 ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.431 -31.708 9.513  1.00 18.73 ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 17.779 -34.060 8.088  1.00 19.32 ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 16.868 -31.857 8.244  1.00 18.94 ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 17.052 -33.025 7.540  1.00 19.84 ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 16.506 -33.175 6.268  1.00 22.27 ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 21.236 -31.711 9.239  1.00 13.76 ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 21.671 -30.710 8.247  1.00 13.58 ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 20.696 -30.769 7.015  1.00 14.81 ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 20.787 -31.675 6.174  1.00 16.30 ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 23.110 -31.011 7.860  1.00 14.36 ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 23.725 -29.998 6.477  1.00 16.90 ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 19.793 -29.769 6.915  1.00 15.45 ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 18.794 -29.795 5.850  1.00 18.17 ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 19.405 -29.676 4.479  1.00 18.78 ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 18.916 -30.326 3.538  1.00 19.61 ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 17.722 -28.734 6.076  1.00 23.39 ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 18.254 -27.428 6.086  1.00 32.06 ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 20.519 -28.934 4.355  1.00 17.54 ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 21.169 -28.776 3.034  1.00 18.12 ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 21.890 -30.012 2.528  1.00 19.04 ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 22.358 -30.012 1.364  1.00 19.68 ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 22.113 -27.584 3.035  1.00 17.93 ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 23.206 -27.839 3.896  1.00 17.93 ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 21.932 -31.092 3.328  1.00 17.19 ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 22.443 -32.376 2.893  1.00 16.90 ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 21.396 -33.498 3.115  1.00 17.46 ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 21.696 -34.674 2.833  1.00 18.77 ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 23.731 -32.720 3.663  1.00 18.25 ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 24.886 -31.763 3.389  1.00 20.04 ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 25.497 -32.041 2.010  1.00 20.73 ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 26.627 -31.151 1.743  1.00 23.96 ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 26.524 -29.974 1.139  1.00 25.82 ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 25.335 -29.526 0.731  1.00 25.43 ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 27.612 -29.244 0.908  1.00 25.61 ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 20.212 -33.161 3.670  1.00 18.02 ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 19.172 -34.151 4.045  1.00 19.83 ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 19.781 -35.271 4.879  1.00 21.28 ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 19.530 -36.462 4.643  1.00 22.48 ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 18.463 -34.715 2.796  1.00 22.55 ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 17.492 -33.716 2.198  1.00 27.62 ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 16.677 -34.401 1.117  1.00 34.73 ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 16.116 -33.446 0.161  1.00 41.30 ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 16.270 -33.529 -1.158 1.00 47.36 ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 16.978 -34.520 -1.691 1.00 48.34 ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 15.740 -32.604 -1.956 1.00 48.07 ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 20.690 -34.907 5.818  1.00 19.51 ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 21.432 -35.953 6.550  1.00 19.39 ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 21.693 -35.523 7.974  1.00 17.31 ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 21.814 -34.322 8.233  1.00 16.56 ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 22.859 -36.106 5.925  1.00 24.31 ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 23.010 -37.079 4.772  1.00 35.08 ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 24.504 -37.184 4.440  1.00 42.64 ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 24.869 -38.368 3.566  1.00 49.33 ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 24.758 -38.052 2.123  1.00 52.66 ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 21.879 -36.486 8.853  1.00 15.57 ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 22.352 -36.233 10.208 1.00 14.89 ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 23.848 -36.479 10.264 1.00 16.55 ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 24.366 -37.466 9.669  1.00 18.99 ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 21.666 -37.187 11.200 1.00 14.79 ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 20.191 -36.984 11.307 1.00 16.21 ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 19.607 -36.214 12.310 1.00 18.30 ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 19.209 -37.485 10.519 1.00 16.75 ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 18.291 -36.279 12.091 1.00 17.84 ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 18.017 -37.029 11.032 1.00 20.03 ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 24.573 -35.658 11.038 1.00 14.39 ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 26.024 -35.845 11.172 1.00 13.66 ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 26.412 -35.883 12.653 1.00 13.76 ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 25.981 -35.044 13.443 1.00 14.17 ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 26.762 -34.621 10.572 1.00 15.25 ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 26.706 -34.518 9.067  1.00 17.15 ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 27.466 -35.359 8.267  1.00 18.40 ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 25.953 -33.530 8.445  1.00 17.95 ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 27.432 -35.254 6.883  1.00 19.61 ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 25.901 -33.431 7.065  1.00 19.05 ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 26.681 -34.263 6.292  1.00 21.17 ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 26.645 -34.124 4.914  1.00 23.31 ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 27.287 -36.836 13.021 1.00 13.17 ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 27.811 -36.870 14.390 1.00 13.72 ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 28.942 -35.825 14.497 1.00 15.24 ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 29.743 -35.710 13.550 1.00 16.73 ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 28.335 -38.313 14.527 1.00 13.98 ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 28.719 -38.693 13.149 1.00 14.97 ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 27.805 -37.949 12.183 1.00 13.89 ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 28.968 -35.034 15.588 1.00 14.38 ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 30.012 -33.980 15.763 1.00 14.78 ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 30.472 -33.905 17.199 1.00 13.44 ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 29.695 -34.175 18.135 1.00 14.68 ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 29.431 -32.557 15.428 1.00 17.64 ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 29.369 -32.307 13.907 1.00 21.05 ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 28.085 -32.297 16.121 1.00 17.85 ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 31.735 -33.473 17.386 1.00 13.29 ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 32.194 -32.970 18.670 1.00 13.47 ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 31.905 -31.420 18.599 1.00 13.16 ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 32.030 -30.787 17.520 1.00 14.99 ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 33.705 -33.187 18.835 1.00 16.35 ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 33.973 -34.585 18.848 1.00 21.46 ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 31.559 -30.817 19.732 1.00 12.79 ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 31.266 -29.367 19.742 1.00 13.13 ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 31.843 -28.701 20.990 1.00 13.53 ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 32.085 -29.376 21.999 1.00 14.69 ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 29.755 -29.065 19.571 1.00 13.13 ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 28.830 -29.799 20.511 1.00 13.10 ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 28.333 -31.049 20.185 1.00 13.55 ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 28.441 -29.219 21.711 1.00 13.83 ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 27.468 -31.723 21.059 1.00 14.00 ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 27.587 -29.871 22.581 1.00 13.13 ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 27.102 -31.133 22.258 1.00 13.00 ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 32.062 -27.385 20.935 1.00 12.43 ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 32.713 -26.687 22.044 1.00 13.78 ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 31.779 -26.416 23.223 1.00 15.24 ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 30.581 -26.740 23.195 1.00 15.83 ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 33.274 -25.364 21.517 1.00 14.61 ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 32.231 -24.475 21.148 1.00 16.32 ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 32.316 -25.810 24.262 1.00 15.77 ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 31.472 -25.380 25.374 1.00 16.34 ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 30.749 -24.075 24.965 1.00 16.16 ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 31.305 -23.271 24.188 1.00 19.12 ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 32.380 -25.129 26.587 1.00 20.34 ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 33.046 -26.452 27.008 1.00 26.48 ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 33.363 -26.543 28.506 1.00 37.94 ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 33.466 -27.991 28.974 1.00 45.86 ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? 32.688 -28.279 30.235 1.00 50.77 ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 29.561 -23.799 25.516 1.00 15.52 ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 28.852 -22.544 25.164 1.00 15.79 ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 29.699 -21.325 25.511 1.00 17.76 ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 30.272 -21.230 26.626 1.00 19.02 ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 27.578 -22.561 26.022 1.00 17.57 ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 27.368 -23.999 26.389 1.00 19.30 ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 28.772 -24.638 26.443 1.00 16.21 ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 29.828 -20.424 24.546 1.00 17.23 ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 30.704 -19.282 24.750 1.00 18.82 ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 30.305 -18.074 23.901 1.00 17.88 ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 29.322 -18.134 23.138 1.00 16.18 ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 32.155 -19.701 24.515 1.00 25.38 ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 32.397 -19.813 23.125 1.00 31.41 ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 31.001 -16.939 24.125 1.00 18.57 ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 30.771 -15.686 23.410 1.00 20.08 ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 31.677 -15.723 22.150 1.00 20.51 ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 32.923 -15.742 22.294 1.00 21.69 ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 31.274 -14.530 24.306 1.00 22.53 ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 30.353 -13.491 24.923 1.00 27.77 ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 31.164 -12.265 25.311 1.00 29.66 ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 29.261 -13.055 24.035 1.00 28.74 ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 31.088 -15.680 20.950 1.00 18.88 ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 31.776 -15.797 19.659 1.00 21.15 ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 31.376 -14.650 18.727 1.00 22.42 ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 30.189 -14.347 18.609 1.00 21.00 ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 31.394 -17.177 19.045 1.00 23.37 ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 31.883 -18.307 19.975 1.00 26.01 ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 31.858 -17.308 17.591 1.00 24.87 ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 31.571 -19.647 19.606 1.00 29.21 ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 32.337 -14.004 18.058 1.00 23.19 ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 32.025 -12.885 17.163 1.00 24.61 ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 31.306 -13.374 15.915 1.00 25.47 ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 31.705 -14.368 15.307 1.00 26.41 ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 33.327 -12.141 16.753 1.00 25.93 ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 33.089 -10.932 15.873 1.00 27.84 ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 32.586 -9.756  16.403 1.00 29.76 ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 33.244 -11.016 14.506 1.00 30.00 ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 32.318 -8.650  15.577 1.00 31.70 ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 33.015 -9.904  13.691 1.00 31.15 ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 32.547 -8.736  14.231 1.00 31.66 ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 30.209 -12.683 15.557 1.00 24.52 ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 29.434 -13.012 14.371 1.00 24.32 ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 29.301 -11.745 13.511 1.00 24.66 ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 28.867 -10.696 13.995 1.00 24.05 ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 28.036 -13.585 14.763 1.00 23.61 ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 27.208 -13.878 13.503 1.00 23.54 ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 28.188 -14.858 15.599 1.00 22.46 ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 29.631 -11.857 12.215 1.00 26.48 ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 29.544 -10.767 11.254 1.00 27.87 ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 28.132 -10.196 11.084 1.00 26.73 ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 27.163 -10.933 11.264 1.00 25.14 ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 30.012 -11.272 9.879  1.00 33.52 ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 31.304 -12.067 9.907  1.00 43.59 ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 31.110 -13.566 9.848  1.00 56.09 ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 30.214 -14.092 10.552 1.00 58.51 ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 31.883 -14.222 9.113  1.00 60.44 ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 28.002 -8.899  10.696 1.00 26.49 ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 26.679 -8.309  10.466 1.00 26.12 ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 25.945 -9.081  9.366  1.00 25.50 ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 26.569 -9.631  8.444  1.00 26.30 ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 26.809 -6.839  10.017 1.00 26.65 ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 24.626 -9.138  9.492  1.00 23.02 ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 23.734 -9.707  8.502  1.00 22.01 ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 22.518 -8.734  8.410  1.00 22.78 ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 22.475 -7.687  9.107  1.00 23.10 ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 23.277 -11.107 8.958  1.00 20.99 ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 22.538 -10.991 10.162 1.00 20.21 ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 21.533 -9.054  7.558  1.00 23.36 ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 20.294 -8.270  7.508  1.00 24.82 ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 19.557 -8.338  8.851  1.00 24.67 ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 18.753 -7.454  9.153  1.00 26.19 ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 19.324 -8.848  6.462  1.00 30.51 ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 19.684 -8.634  5.007  1.00 39.20 ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 18.786 -9.547  4.188  1.00 50.19 ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 18.942 -10.786 4.309  1.00 54.51 ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 17.868 -9.035  3.505  1.00 50.45 ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 19.793 -9.413  9.636  1.00 23.13 ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 19.087 -9.664  10.871 1.00 22.85 ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 19.698 -9.030  12.105 1.00 22.76 ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 18.970 -8.765  13.083 1.00 25.11 ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 19.015 -11.174 11.091 1.00 22.41 ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 18.434 -11.925 9.918  1.00 23.75 ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 17.065 -11.940 9.685  1.00 25.74 ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 19.241 -12.668 9.082  1.00 24.74 ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 16.520 -12.657 8.622  1.00 27.58 ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 18.715 -13.373 8.007  1.00 26.92 ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 17.345 -13.385 7.793  1.00 29.04 ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 16.805 -14.140 6.764  1.00 33.17 ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 21.015 -8.849  12.111 1.00 21.16 ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 21.709 -8.363  13.297 1.00 21.99 ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 22.872 -7.486  12.925 1.00 24.11 ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 23.597 -7.759  11.945 1.00 23.64 ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 22.345 -9.545  14.106 1.00 20.61 ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 21.352 -10.483 14.716 1.00 19.14 ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 21.182 -11.761 14.215 1.00 18.92 ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 20.606 -10.109 15.828 1.00 18.65 ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 20.285 -12.641 14.779 1.00 18.40 ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 19.721 -10.986 16.416 1.00 18.11 ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 19.582 -12.262 15.901 1.00 17.42 ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 18.650 -13.101 16.427 1.00 17.12 ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 23.192 -6.512  13.796 1.00 25.15 ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 24.450 -5.833  13.615 1.00 24.46 ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 25.608 -6.805  13.898 1.00 23.82 ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 25.425 -7.858  14.532 1.00 23.40 ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 24.410 -4.726  14.700 1.00 25.47 ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 23.564 -5.342  15.793 1.00 26.80 ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 22.517 -6.132  15.061 1.00 25.13 ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 26.828 -6.443  13.523 1.00 23.53 ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 28.035 -7.205  13.892 1.00 23.90 ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 28.102 -7.223  15.459 1.00 24.06 ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 27.829 -6.183  16.076 1.00 23.92 ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 29.269 -6.507  13.338 1.00 25.22 ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 28.279 -8.406  16.084 1.00 23.28 ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 28.186 -8.501  17.545 1.00 22.35 ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 28.780 -9.817  18.069 1.00 22.05 ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 29.131 -10.710 17.292 1.00 22.81 ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 26.694 -8.438  17.938 1.00 22.91 ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 25.964 -9.768  17.537 1.00 19.68 ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 24.482 -9.630  17.331 1.00 19.99 ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 23.704 -10.790 17.763 1.00 19.67 ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 23.688 -11.981 17.166 1.00 21.21 ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 22.918 -12.947 17.633 1.00 19.07 ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 24.441 -12.209 16.090 1.00 20.02 ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 28.860 -9.953  19.411 1.00 22.56 ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 29.252 -11.231 19.993 1.00 23.37 ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 27.955 -11.968 20.295 1.00 20.67 ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 27.070 -11.416 20.955 1.00 20.73 ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 30.016 -11.040 21.302 1.00 25.25 ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 31.416 -10.561 21.041 1.00 29.48 ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 32.425 -11.453 20.722 1.00 31.91 ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 31.716 -9.206  21.032 1.00 32.42 ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 33.716 -11.013 20.449 1.00 34.71 ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 33.010 -8.756  20.778 1.00 34.63 ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 33.991 -9.664  20.440 1.00 36.59 ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? 35.267 -9.252  20.153 1.00 41.44 ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 27.836 -13.196 19.794 1.00 17.22 ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 26.675 -14.025 20.130 1.00 16.80 ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 27.067 -14.886 21.322 1.00 16.77 ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 28.131 -15.527 21.304 1.00 17.78 ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 26.239 -14.875 18.926 1.00 16.08 ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 25.052 -15.824 19.280 1.00 15.27 ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 24.275 -16.301 18.059 1.00 15.45 ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 24.099 -15.588 17.077 1.00 15.96 ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 23.829 -17.571 18.114 1.00 15.15 ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 26.231 -14.913 22.354 1.00 16.04 ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 26.521 -15.668 23.556 1.00 15.35 ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 25.875 -17.086 23.513 1.00 14.94 ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 24.952 -17.349 22.706 1.00 15.20 ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 26.033 -14.899 24.798 1.00 16.76 ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 24.629 -14.722 24.727 1.00 18.43 ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 26.353 -17.964 24.422 1.00 14.40 ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 25.841 -19.320 24.612 1.00 14.24 ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 25.911 -20.110 23.269 1.00 14.48 ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 25.032 -20.936 22.998 1.00 14.79 ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 24.383 -19.248 25.136 1.00 14.44 ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 24.277 -18.614 26.493 1.00 15.16 ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 24.305 -19.376 27.651 1.00 18.09 ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 24.177 -17.300 26.824 1.00 17.12 ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 24.178 -18.514 28.665 1.00 17.92 ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 24.144 -17.245 28.226 1.00 18.76 ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 26.961 -19.848 22.462 1.00 14.48 ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 27.119 -20.467 21.137 1.00 14.72 ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 28.189 -21.573 21.201 1.00 15.24 ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 29.227 -21.388 21.837 1.00 14.96 ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 27.514 -19.388 20.095 1.00 15.13 ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 27.631 -19.845 18.632 1.00 17.50 ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 26.234 -20.249 18.079 1.00 16.79 ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 28.114 -18.646 17.737 1.00 19.92 ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 27.922 -22.719 20.558 1.00 13.94 ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 28.875 -23.851 20.532 1.00 13.91 ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 29.279 -24.123 19.099 1.00 14.33 ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 28.397 -24.126 18.237 1.00 15.26 ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 28.183 -25.100 21.092 1.00 13.78 ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 27.773 -24.852 22.510 1.00 17.30 ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 26.756 -26.139 23.157 1.00 19.32 ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 25.225 -26.014 22.084 1.00 14.86 ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 30.580 -24.290 18.825 1.00 14.14 ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 31.020 -24.550 17.448 1.00 13.67 ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 31.411 -25.993 17.228 1.00 13.99 ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 31.960 -26.635 18.134 1.00 13.32 ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 32.247 -23.671 17.033 1.00 15.14 ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 32.013 -22.162 17.091 1.00 16.20 ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 33.294 -21.398 16.652 1.00 17.90 ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 30.831 -21.746 16.184 1.00 18.11 ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 31.231 -26.452 15.993 1.00 13.66 ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 31.712 -27.786 15.603 1.00 13.61 ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 32.255 -27.641 14.160 1.00 13.90 ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 31.892 -26.694 13.431 1.00 14.49 ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 30.565 -28.827 15.605 1.00 14.36 ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 33.093 -28.599 13.749 1.00 14.08 ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 33.538 -28.704 12.379 1.00 15.10 ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 32.455 -29.474 11.613 1.00 16.29 ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 32.172 -30.639 11.922 1.00 17.50 ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? 34.913 -29.432 12.316 1.00 16.34 ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? 35.371 -29.555 10.869 1.00 16.82 ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? 35.956 -28.635 13.126 1.00 17.86 ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 31.884 -28.828 10.621 1.00 17.75 ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 30.825 -29.459 9.839  1.00 19.30 ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 30.205 -28.491 8.866  1.00 19.99 ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 30.476 -27.280 8.872  1.00 20.36 ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 29.294 -29.000 8.040  1.00 18.87 ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 28.623 -28.181 7.036  1.00 19.28 ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 27.366 -27.508 7.555  1.00 18.99 ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 26.526 -28.164 8.187  1.00 18.90 ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 28.241 -29.089 5.839  1.00 19.16 ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 27.609 -28.311 4.739  1.00 19.59 ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 28.332 -27.338 4.036  1.00 21.16 ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 26.308 -28.263 4.334  1.00 19.69 ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 27.465 -26.770 3.204  1.00 22.25 ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 26.238 -27.277 3.357  1.00 22.50 ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 27.196 -26.216 7.231  1.00 19.09 ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 26.039 -25.411 7.599  1.00 21.18 ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 25.892 -24.308 6.549  1.00 22.98 ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 26.882 -23.620 6.263  1.00 25.54 ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 26.277 -24.768 8.971  1.00 23.54 ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 25.165 -24.040 9.486  1.00 30.32 ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 24.683 -24.132 5.993  1.00 19.71 ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 24.390 -23.011 5.075  1.00 21.82 ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 23.027 -22.398 5.472  1.00 24.33 ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 22.378 -22.960 6.329  1.00 25.02 ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 24.558 -23.393 3.599  1.00 24.93 ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 23.811 -24.618 3.184  1.00 28.63 ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 24.114 -24.933 1.732  1.00 30.93 ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 23.555 -24.229 0.868  1.00 37.83 ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 24.926 -25.846 1.459  1.00 29.66 ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 22.692 -21.132 5.116  1.00 26.43 ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 21.579 -20.421 5.828  1.00 28.25 ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 20.253 -21.156 6.176  1.00 27.33 ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 19.737 -21.002 7.336  1.00 29.46 ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 21.314 -19.229 4.926  1.00 29.98 ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 22.709 -18.878 4.414  1.00 29.78 ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 23.454 -20.204 4.256  1.00 27.23 ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 19.696 -21.880 5.201  1.00 23.74 ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 18.491 -22.683 5.341  1.00 22.66 ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 18.629 -23.807 6.366  1.00 20.49 ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 17.648 -24.486 6.676  1.00 20.64 ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 19.840 -23.984 6.919  1.00 18.20 ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 20.069 -25.003 7.955  1.00 16.29 ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 19.701 -24.523 9.346  1.00 15.77 ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 19.646 -25.369 10.239 1.00 15.92 ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 21.543 -25.498 7.943  1.00 16.58 ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 21.851 -26.376 6.724  1.00 19.13 ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 20.946 -27.052 6.252  1.00 19.03 ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 23.007 -26.322 6.215  1.00 18.07 ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 19.497 -23.189 9.572  1.00 15.50 ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 19.122 -22.716 10.933 1.00 16.61 ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 17.893 -23.422 11.422 1.00 15.96 ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 16.964 -23.638 10.639 1.00 16.87 ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 18.944 -21.191 11.026 1.00 18.73 ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 20.514 -20.303 11.064 1.00 21.20 ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 17.906 -23.803 12.681 1.00 14.72 ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 16.761 -24.489 13.255 1.00 15.49 ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 16.937 -25.998 13.324 1.00 15.60 ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 16.209 -26.663 14.058 1.00 16.88 ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 17.956 -26.531 12.623 1.00 14.25 ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 18.254 -27.965 12.733 1.00 13.28 ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 18.629 -28.304 14.178 1.00 13.12 ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 19.391 -27.568 14.792 1.00 13.94 ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 18.137 -29.446 14.681 1.00 13.16 ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 18.401 -29.804 16.065 1.00 13.43 ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 19.696 -30.560 16.255 1.00 12.88 ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 20.016 -31.463 15.447 1.00 13.27 ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.165 -30.594 16.617 1.00 16.76 ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 16.010 -29.582 16.881 1.00 19.56 ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.488 -31.357 17.924 1.00 18.43 ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 14.652 -30.301 17.366 1.00 23.09 ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 20.415 -30.226 17.354 1.00 11.96 ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 21.594 -30.972 17.820 1.00 11.58 ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 21.107 -31.736 19.059 1.00 12.15 ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 20.491 -31.147 19.958 1.00 12.90 ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 22.699 -29.970 18.239 1.00 11.95 ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 23.898 -30.589 18.958 1.00 13.57 ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 24.667 -31.554 18.002 1.00 14.56 ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 24.852 -29.454 19.494 1.00 13.81 ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 21.318 -33.071 19.050 1.00 12.18 ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 20.889 -33.956 20.145 1.00 13.92 ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 22.065 -34.750 20.661 1.00 14.16 ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 22.895 -35.226 19.883 1.00 14.42 ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 19.843 -34.971 19.598 1.00 17.45 ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 18.439 -34.422 19.382 1.00 25.61 ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 17.465 -35.482 18.799 1.00 33.13 ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 16.614 -36.064 19.852 1.00 42.07 ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 15.446 -35.558 20.231 1.00 47.55 ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 14.905 -34.548 19.560 1.00 47.70 ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 14.756 -36.130 21.206 1.00 51.33 ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 22.068 -34.974 21.946 1.00 13.78 ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 23.033 -35.904 22.561 1.00 14.81 ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 22.239 -37.080 23.147 1.00 16.87 ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 21.014 -37.158 22.987 1.00 16.17 ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 23.857 -35.197 23.631 1.00 14.69 ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 22.862 -34.692 25.081 1.00 13.38 ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 22.937 -37.975 23.895 1.00 18.27 ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 22.246 -39.108 24.495 1.00 20.47 ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 21.158 -38.673 25.526 1.00 20.56 ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 20.271 -39.462 25.872 1.00 23.07 ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 23.270 -40.079 25.136 1.00 23.51 ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 23.926 -39.481 26.371 1.00 27.07 ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 24.973 -40.399 26.968 1.00 35.76 ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 26.182 -40.126 26.887 1.00 37.35 ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 24.520 -41.481 27.602 1.00 36.67 ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 21.174 -37.404 25.996 1.00 18.51 ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 20.236 -36.920 27.008 1.00 18.10 ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 19.022 -36.180 26.435 1.00 19.42 ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 18.082 -35.884 27.175 1.00 21.22 ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 20.931 -36.017 28.027 1.00 17.46 ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 22.133 -36.674 28.654 1.00 16.75 ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 23.414 -36.314 28.324 1.00 15.91 ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 22.187 -37.633 29.607 1.00 18.42 ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 24.228 -37.081 29.032 1.00 19.19 ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 23.546 -37.911 29.821 1.00 20.09 ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 19.063 -35.832 25.142 1.00 17.31 ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 17.967 -35.087 24.536 1.00 15.94 ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 18.452 -33.939 23.664 1.00 14.27 ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 19.591 -33.926 23.194 1.00 13.71 ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 17.596 -32.941 23.508 1.00 14.10 ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 17.928 -31.772 22.678 1.00 13.98 ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 18.939 -30.844 23.343 1.00 13.66 ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 18.717 -30.403 24.508 1.00 14.14 ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 16.642 -30.991 22.323 1.00 15.57 ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 16.993 -29.696 21.582 1.00 16.01 ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 15.695 -31.858 21.474 1.00 16.41 ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 20.040 -30.509 22.634 1.00 12.82 ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 21.073 -29.652 23.161 1.00 12.86 ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 20.913 -28.217 22.680 1.00 13.22 ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 21.144 -27.266 23.430 1.00 13.24 ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 22.465 -30.179 22.690 1.00 13.11 ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 23.590 -29.208 23.033 1.00 14.69 ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 22.732 -31.552 23.288 1.00 13.54 ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 20.507 -28.054 21.406 1.00 12.64 ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 20.412 -26.699 20.851 1.00 14.27 ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 20.026 -26.735 19.388 1.00 12.81 ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 19.644 -27.803 18.877 1.00 13.25 ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 20.061 -25.561 18.741 1.00 12.77 ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 19.649 -25.501 17.336 1.00 12.67 ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 20.684 -24.775 16.519 1.00 13.06 ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 21.358 -23.873 17.013 1.00 13.21 ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 18.293 -24.801 17.156 1.00 13.94 ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 18.272 -23.451 17.871 1.00 15.30 ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.116 -25.711 17.555 1.00 15.88 ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 16.901 -22.656 17.536 1.00 17.01 ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 20.817 -25.151 15.206 1.00 11.71 ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 21.798 -24.458 14.343 1.00 11.98 ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 21.465 -22.944 14.291 1.00 12.10 ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 20.269 -22.597 14.107 1.00 12.87 ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 21.754 -25.038 12.916 1.00 12.66 ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 22.610 -24.197 11.955 1.00 15.13 ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 22.185 -26.506 12.922 1.00 14.04 ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 22.465 -22.092 14.432 1.00 12.93 ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 22.292 -20.648 14.434 1.00 12.75 ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 23.283 -19.914 13.534 1.00 15.26 ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 22.971 -18.810 13.045 1.00 15.45 ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 22.344 -20.153 15.881 1.00 13.54 ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 22.240 -18.720 15.925 1.00 14.33 ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 24.488 -20.460 13.354 1.00 14.92 ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 25.522 -19.812 12.509 1.00 16.47 ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 26.244 -20.847 11.647 1.00 16.38 ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 26.130 -22.053 11.907 1.00 16.32 ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 26.586 -19.051 13.381 1.00 18.84 ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 27.475 -19.996 13.993 1.00 20.25 ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 25.996 -18.170 14.442 1.00 19.01 ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 26.995 -20.399 10.632 1.00 18.41 ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 27.737 -21.358 9.806  1.00 21.06 ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 28.743 -20.710 8.907  1.00 23.24 ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 28.939 -19.514 8.998  1.00 22.82 ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 29.315 -21.491 7.998  1.00 25.71 ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 30.328 -20.997 7.066  1.00 26.54 ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 31.742 -21.329 7.491  1.00 27.42 ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 31.980 -21.686 8.646  1.00 26.40 ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 32.719 -21.209 6.552  1.00 27.63 ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 34.122 -21.535 6.880  1.00 28.42 ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 34.300 -22.970 7.398  1.00 26.25 ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? 35.267 -23.248 8.120  1.00 27.68 ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? 34.683 -20.571 7.934  1.00 31.49 ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? 35.499 -19.428 7.402  1.00 35.92 ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? 35.565 -19.202 6.186  1.00 38.08 ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? 36.137 -18.692 8.320  1.00 36.05 ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 33.385 -23.870 7.033  1.00 23.14 ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 33.473 -25.241 7.478  1.00 21.21 ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 33.157 -25.446 8.946  1.00 18.42 ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 33.472 -26.498 9.490  1.00 18.74 ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 32.516 -24.483 9.578  1.00 17.80 ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 32.112 -24.596 10.970 1.00 17.20 ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 30.564 -24.485 11.042 1.00 18.22 ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 29.932 -23.885 10.159 1.00 20.99 ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 32.721 -23.452 11.765 1.00 19.05 ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 34.246 -23.329 11.708 1.00 22.04 ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? 34.678 -21.957 12.282 1.00 24.00 ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? 34.915 -24.447 12.494 1.00 22.42 ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 29.981 -25.028 12.103 1.00 14.22 ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 28.548 -24.878 12.340 1.00 14.86 ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 28.440 -24.431 13.791 1.00 15.23 ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 29.138 -24.950 14.679 1.00 14.78 ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 27.778 -26.165 12.069 1.00 15.64 ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 28.398 -27.394 12.681 1.00 18.86 ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 26.280 -26.029 12.432 1.00 15.23 ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 27.561 -23.456 14.015 1.00 13.67 ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 27.369 -22.945 15.369 1.00 14.23 ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 25.965 -23.232 15.852 1.00 13.30 ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 25.002 -23.093 15.092 1.00 14.12 ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 25.870 -23.703 17.107 1.00 12.09 ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 24.579 -24.075 17.700 1.00 12.50 ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 24.278 -23.191 18.916 1.00 12.14 ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 25.147 -23.024 19.784 1.00 13.88 ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 24.629 -25.549 18.215 1.00 12.53 ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 25.074 -26.570 17.184 1.00 12.99 ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 24.169 -27.104 16.294 1.00 12.62 ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 26.410 -26.956 17.092 1.00 14.03 ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 24.582 -28.026 15.328 1.00 13.26 ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 26.808 -27.927 16.163 1.00 14.95 ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 25.889 -28.433 15.271 1.00 14.02 ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 23.042 -22.671 18.962 1.00 11.90 ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 22.601 -21.922 20.130 1.00 12.30 ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 22.201 -22.960 21.195 1.00 12.75 ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 21.256 -23.737 20.992 1.00 13.16 ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 21.386 -21.061 19.739 1.00 13.29 ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 22.884 -22.913 22.365 1.00 12.62 ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 22.575 -23.840 23.446 1.00 12.25 ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 21.253 -23.546 24.094 1.00 13.90 ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 20.885 -22.372 24.257 1.00 13.47 ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 23.683 -23.696 24.532 1.00 13.56 ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 23.580 -24.726 25.644 1.00 19.12 ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 23.427 -25.892 25.340 1.00 18.43 ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 23.634 -24.335 26.817 1.00 22.30 ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 20.518 -24.618 24.515 1.00 12.97 ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 19.275 -24.376 25.294 1.00 13.08 ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 19.313 -25.132 26.632 1.00 14.72 ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 18.339 -25.091 27.386 1.00 15.07 ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 17.978 -24.791 24.522 1.00 14.18 ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 17.821 -23.943 23.234 1.00 15.04 ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 17.979 -26.303 24.189 1.00 15.16 ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 20.438 -25.814 26.953 1.00 13.57 ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 20.481 -26.687 28.117 1.00 13.46 ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 20.407 -25.925 29.441 1.00 14.79 ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 20.062 -26.537 30.464 1.00 15.99 ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 21.760 -27.534 28.084 1.00 13.29 ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 21.760 -28.522 26.921 1.00 14.44 ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 23.091 -29.255 26.925 1.00 14.25 ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 24.184 -28.365 26.535 1.00 12.60 ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 25.433 -28.775 26.300 1.00 14.72 ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 25.795 -30.021 26.582 1.00 13.71 ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 26.347 -27.919 25.842 1.00 15.32 ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 20.768 -24.639 29.445 1.00 14.26 ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 20.698 -23.842 30.665 1.00 15.91 ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 19.306 -23.270 30.916 1.00 16.96 ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 19.091 -22.717 32.001 1.00 18.78 ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 21.672 -22.670 30.613 1.00 17.17 ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 21.398 -21.674 29.515 1.00 19.51 ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 21.159 -22.109 28.369 1.00 18.92 ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 21.440 -20.427 29.810 1.00 19.98 ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 18.360 -23.380 29.966 1.00 15.89 ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.004 -22.805 30.144 1.00 16.60 ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 16.141 -23.803 30.888 1.00 17.21 ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 15.276 -24.480 30.308 1.00 17.32 ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 16.416 -22.476 28.758 1.00 16.67 ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.286 -21.541 27.929 1.00 18.26 ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 16.725 -21.389 26.533 1.00 19.55 ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.439 -20.167 28.578 1.00 18.21 ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 16.365 -23.890 32.208 1.00 16.46 ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 15.676 -24.941 32.998 1.00 18.29 ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 14.174 -24.743 33.064 1.00 19.91 ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 13.435 -25.722 33.217 1.00 21.23 ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 16.237 -25.059 34.400 1.00 18.19 ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 17.751 -25.114 34.551 1.00 19.28 ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 18.138 -25.369 35.971 1.00 21.35 ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 18.410 -26.082 33.594 1.00 19.22 ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 13.726 -23.475 32.952 1.00 19.75 ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 12.305 -23.151 33.021 1.00 19.90 ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 11.507 -23.750 31.840 1.00 20.52 ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 10.280 -23.808 31.915 1.00 21.13 ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 12.114 -21.624 33.091 1.00 19.56 ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 12.799 -20.853 31.995 1.00 19.47 ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 14.046 -20.302 32.023 1.00 19.34 ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 12.255 -20.560 30.686 1.00 19.02 ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 14.301 -19.652 30.833 1.00 19.48 ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 13.200 -19.773 30.013 1.00 18.99 ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 11.028 -20.843 30.057 1.00 19.89 ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 12.979 -19.307 28.717 1.00 20.62 ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 10.786 -20.321 28.799 1.00 21.73 ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 11.753 -19.551 28.151 1.00 21.10 ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 12.174 -24.217 30.766 1.00 19.91 ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 11.431 -24.838 29.648 1.00 20.59 ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 10.696 -26.107 30.124 1.00 24.52 ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 9.704  -26.471 29.490 1.00 25.81 ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 12.394 -25.227 28.512 1.00 19.57 ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 12.940 -24.077 27.661 1.00 19.32 ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 14.017 -24.619 26.707 1.00 19.01 ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 11.784 -23.364 26.842 1.00 19.15 ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 11.220 -26.773 31.183 1.00 26.42 ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 10.740 -28.041 31.771 1.00 30.46 ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 9.573  -27.860 32.712 1.00 34.18 ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 9.064  -28.862 33.199 1.00 35.61 ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 11.851 -28.706 32.607 1.00 32.48 ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 13.076 -29.223 31.887 1.00 35.49 ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 12.999 -29.448 30.669 1.00 35.83 ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 14.134 -29.422 32.568 1.00 38.19 ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 9.221  -26.626 33.076 1.00 35.25 ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 8.116  -26.371 33.995 1.00 38.02 ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 7.130  -25.390 33.341 1.00 40.26 ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 6.140  -25.017 33.976 1.00 42.35 ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 8.661  -25.791 35.312 1.00 40.99 ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 9.323  -24.438 35.136 1.00 46.92 ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 10.382 -24.099 36.168 1.00 57.62 ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 10.524 -22.898 36.506 1.00 58.71 ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 11.080 -25.032 36.628 1.00 61.12 ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1BOO C 2 .   ? 9.044  14.881  22.097 1.00 30.64 ? 201 A1BOO A N1  1 
HETATM 2156 C  C4  . A1BOO C 2 .   ? 9.989  15.669  22.909 1.00 28.92 ? 201 A1BOO A C4  1 
HETATM 2157 C  C5  . A1BOO C 2 .   ? 8.263  13.880  22.559 1.00 35.71 ? 201 A1BOO A C5  1 
HETATM 2158 C  C6  . A1BOO C 2 .   ? 8.458  13.471  24.022 1.00 42.55 ? 201 A1BOO A C6  1 
HETATM 2159 C  C7  . A1BOO C 2 .   ? 5.665  13.800  24.547 1.00 51.58 ? 201 A1BOO A C7  1 
HETATM 2160 C  C8  . A1BOO C 2 .   ? 4.671  13.068  25.181 1.00 52.19 ? 201 A1BOO A C8  1 
HETATM 2161 C  C10 . A1BOO C 2 .   ? 3.008  14.119  23.810 1.00 52.95 ? 201 A1BOO A C10 1 
HETATM 2162 C  C13 . A1BOO C 2 .   ? 8.922  12.035  23.931 1.00 42.96 ? 201 A1BOO A C13 1 
HETATM 2163 C  C15 . A1BOO C 2 .   ? 8.563  9.688   24.289 1.00 42.84 ? 201 A1BOO A C15 1 
HETATM 2164 C  C17 . A1BOO C 2 .   ? 10.416 10.400  22.985 1.00 43.14 ? 201 A1BOO A C17 1 
HETATM 2165 O  O1  . A1BOO C 2 .   ? 7.526  13.250  21.825 1.00 34.43 ? 201 A1BOO A O1  1 
HETATM 2166 C  C3  . A1BOO C 2 .   ? 11.414 15.535  22.390 1.00 27.59 ? 201 A1BOO A C3  1 
HETATM 2167 C  C2  . A1BOO C 2 .   ? 11.487 15.847  20.891 1.00 25.85 ? 201 A1BOO A C2  1 
HETATM 2168 C  C19 . A1BOO C 2 .   ? 9.025  15.260  20.684 1.00 26.89 ? 201 A1BOO A C19 1 
HETATM 2169 C  C1  . A1BOO C 2 .   ? 10.426 15.070  20.098 1.00 24.17 ? 201 A1BOO A C1  1 
HETATM 2170 C  C   . A1BOO C 2 .   ? 10.450 15.428  18.623 1.00 22.29 ? 201 A1BOO A C   1 
HETATM 2171 O  O   . A1BOO C 2 .   ? 10.825 14.609  17.775 1.00 22.71 ? 201 A1BOO A O   1 
HETATM 2172 N  N   . A1BOO C 2 .   ? 10.046 16.646  18.309 1.00 20.59 ? 201 A1BOO A N   1 
HETATM 2173 C  C18 . A1BOO C 2 .   ? 10.046 11.719  23.183 1.00 42.97 ? 201 A1BOO A C18 1 
HETATM 2174 C  C16 . A1BOO C 2 .   ? 9.676  9.390   23.536 1.00 42.79 ? 201 A1BOO A C16 1 
HETATM 2175 C  C14 . A1BOO C 2 .   ? 8.195  11.004  24.500 1.00 42.80 ? 201 A1BOO A C14 1 
HETATM 2176 S  S   . A1BOO C 2 .   ? 7.241  13.831  25.365 1.00 49.71 ? 201 A1BOO A S   1 
HETATM 2177 C  C12 . A1BOO C 2 .   ? 5.323  14.672  23.524 1.00 52.64 ? 201 A1BOO A C12 1 
HETATM 2178 C  C11 . A1BOO C 2 .   ? 3.992  14.834  23.168 1.00 53.03 ? 201 A1BOO A C11 1 
HETATM 2179 C  C9  . A1BOO C 2 .   ? 3.345  13.239  24.814 1.00 52.68 ? 201 A1BOO A C9  1 
HETATM 2180 ZN ZN  . ZN    D 3 .   ? 11.554 -4.618  5.582  1.00 19.54 2 202 ZN    A ZN  1 
HETATM 2181 S  S   . DMS   E 4 .   ? 19.646 0.552   20.293 1.00 40.86 ? 203 DMS   A S   1 
HETATM 2182 O  O   . DMS   E 4 .   ? 18.288 0.199   19.740 1.00 36.07 ? 203 DMS   A O   1 
HETATM 2183 C  C1  . DMS   E 4 .   ? 19.650 1.091   22.021 1.00 41.43 ? 203 DMS   A C1  1 
HETATM 2184 C  C2  . DMS   E 4 .   ? 20.291 2.073   19.494 1.00 40.11 ? 203 DMS   A C2  1 
HETATM 2185 N  N1  . A1BOO F 2 .   ? 24.375 -15.782 9.952  1.00 24.57 ? 201 A1BOO C N1  1 
HETATM 2186 C  C4  . A1BOO F 2 .   ? 23.357 -14.998 9.228  1.00 22.84 ? 201 A1BOO C C4  1 
HETATM 2187 C  C5  . A1BOO F 2 .   ? 25.126 -16.802 9.469  1.00 30.27 ? 201 A1BOO C C5  1 
HETATM 2188 C  C6  . A1BOO F 2 .   ? 24.643 -17.355 8.137  1.00 38.26 ? 201 A1BOO C C6  1 
HETATM 2189 C  C7  . A1BOO F 2 .   ? 27.046 -16.282 7.073  1.00 48.53 ? 201 A1BOO C C7  1 
HETATM 2190 C  C8  . A1BOO F 2 .   ? 28.027 -17.213 7.374  1.00 49.33 ? 201 A1BOO C C8  1 
HETATM 2191 C  C10 . A1BOO F 2 .   ? 29.722 -15.552 7.034  1.00 50.12 ? 201 A1BOO C C10 1 
HETATM 2192 C  C13 . A1BOO F 2 .   ? 24.547 -18.853 8.316  1.00 38.31 ? 201 A1BOO C C13 1 
HETATM 2193 C  C15 . A1BOO F 2 .   ? 23.492 -20.757 9.340  1.00 38.46 ? 201 A1BOO C C15 1 
HETATM 2194 C  C17 . A1BOO F 2 .   ? 25.233 -21.083 7.762  1.00 38.09 ? 201 A1BOO C C17 1 
HETATM 2195 O  O1  . A1BOO F 2 .   ? 26.014 -17.339 10.130 1.00 26.49 ? 201 A1BOO C O1  1 
HETATM 2196 C  C3  . A1BOO F 2 .   ? 21.970 -15.212 9.815  1.00 21.72 ? 201 A1BOO C C3  1 
HETATM 2197 C  C2  . A1BOO F 2 .   ? 21.956 -14.908 11.315 1.00 21.01 ? 201 A1BOO C C2  1 
HETATM 2198 C  C19 . A1BOO F 2 .   ? 24.478 -15.407 11.362 1.00 20.93 ? 201 A1BOO C C19 1 
HETATM 2199 C  C1  . A1BOO F 2 .   ? 23.124 -15.608 12.037 1.00 19.27 ? 201 A1BOO C C1  1 
HETATM 2200 C  C   . A1BOO F 2 .   ? 23.263 -15.146 13.476 1.00 17.99 ? 201 A1BOO C C   1 
HETATM 2201 O  O   . A1BOO F 2 .   ? 23.641 -13.989 13.744 1.00 17.16 ? 201 A1BOO C O   1 
HETATM 2202 N  N   . A1BOO F 2 .   ? 23.022 -16.076 14.396 1.00 16.66 ? 201 A1BOO C N   1 
HETATM 2203 C  C18 . A1BOO F 2 .   ? 25.363 -19.717 7.609  1.00 38.08 ? 201 A1BOO C C18 1 
HETATM 2204 C  C16 . A1BOO F 2 .   ? 24.300 -21.598 8.630  1.00 38.03 ? 201 A1BOO C C16 1 
HETATM 2205 C  C14 . A1BOO F 2 .   ? 23.610 -19.389 9.186  1.00 38.55 ? 201 A1BOO C C14 1 
HETATM 2206 S  S   . A1BOO F 2 .   ? 25.428 -16.801 6.570  1.00 46.30 ? 201 A1BOO C S   1 
HETATM 2207 C  C12 . A1BOO F 2 .   ? 27.406 -14.968 6.819  1.00 49.70 ? 201 A1BOO C C12 1 
HETATM 2208 C  C11 . A1BOO F 2 .   ? 28.745 -14.612 6.786  1.00 50.18 ? 201 A1BOO C C11 1 
HETATM 2209 C  C9  . A1BOO F 2 .   ? 29.364 -16.846 7.337  1.00 49.74 ? 201 A1BOO C C9  1 
HETATM 2210 ZN ZN  . ZN    G 3 .   ? 24.118 -34.855 27.014 1.00 15.03 2 202 ZN    C ZN  1 
HETATM 2211 O  O   . HOH   H 5 .   ? 19.936 23.210  8.108  1.00 24.10 ? 301 HOH   A O   1 
HETATM 2212 O  O   . HOH   H 5 .   ? 12.389 7.634   30.920 1.00 33.19 ? 302 HOH   A O   1 
HETATM 2213 O  O   . HOH   H 5 .   ? 33.888 18.283  19.036 1.00 46.44 ? 303 HOH   A O   1 
HETATM 2214 O  O   . HOH   H 5 .   ? 3.808  -1.548  2.859  1.00 47.38 ? 304 HOH   A O   1 
HETATM 2215 O  O   . HOH   H 5 .   ? 10.911 8.281   4.470  1.00 22.93 ? 305 HOH   A O   1 
HETATM 2216 O  O   . HOH   H 5 .   ? 23.060 13.595  23.566 1.00 49.99 ? 306 HOH   A O   1 
HETATM 2217 O  O   . HOH   H 5 .   ? 3.070  8.173   9.523  1.00 33.58 ? 307 HOH   A O   1 
HETATM 2218 O  O   . HOH   H 5 .   ? 23.424 22.397  8.070  1.00 26.45 ? 308 HOH   A O   1 
HETATM 2219 O  O   . HOH   H 5 .   ? 18.636 -2.246  18.807 1.00 36.84 ? 309 HOH   A O   1 
HETATM 2220 O  O   . HOH   H 5 .   ? 10.705 4.915   3.377  1.00 24.99 ? 310 HOH   A O   1 
HETATM 2221 O  O   . HOH   H 5 .   ? 3.734  -4.501  21.071 1.00 29.62 ? 311 HOH   A O   1 
HETATM 2222 O  O   . HOH   H 5 .   ? 0.900  -2.307  19.591 1.00 35.99 ? 312 HOH   A O   1 
HETATM 2223 O  O   . HOH   H 5 .   ? 19.708 9.522   19.209 1.00 15.97 ? 313 HOH   A O   1 
HETATM 2224 O  O   . HOH   H 5 .   ? 29.809 -4.166  10.342 1.00 45.30 ? 314 HOH   A O   1 
HETATM 2225 O  O   . HOH   H 5 .   ? 27.775 16.522  3.446  1.00 34.43 ? 315 HOH   A O   1 
HETATM 2226 O  O   . HOH   H 5 .   ? 2.729  3.891   27.422 1.00 30.16 ? 316 HOH   A O   1 
HETATM 2227 O  O   . HOH   H 5 .   ? 17.502 21.622  9.652  1.00 21.80 ? 317 HOH   A O   1 
HETATM 2228 O  O   . HOH   H 5 .   ? 18.722 0.159   27.678 1.00 31.36 ? 318 HOH   A O   1 
HETATM 2229 O  O   . HOH   H 5 .   ? 6.300  -5.241  29.069 1.00 32.15 ? 319 HOH   A O   1 
HETATM 2230 O  O   . HOH   H 5 .   ? 0.293  0.043   16.076 1.00 15.26 ? 320 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 5 .   ? 25.801 4.919   20.570 1.00 33.96 ? 321 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 5 .   ? 10.664 9.373   31.163 1.00 35.50 ? 322 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 5 .   ? 28.319 3.884   3.687  1.00 45.36 ? 323 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 5 .   ? 23.040 -0.616  4.638  1.00 25.43 ? 324 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 5 .   ? 16.914 -6.771  11.058 1.00 24.76 ? 325 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 7.614  20.048  17.663 1.00 24.12 ? 326 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 27.945 -0.962  8.466  1.00 35.14 ? 327 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 5.038  26.819  16.444 1.00 35.74 ? 328 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? 18.006 5.339   26.785 1.00 33.29 ? 329 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 9.174  18.843  19.846 1.00 22.26 ? 330 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 36.583 16.669  12.258 1.00 27.95 ? 331 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? 23.564 0.741   16.655 1.00 23.36 ? 332 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? 16.114 -10.764 5.319  1.00 32.17 ? 333 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? 30.472 10.791  14.420 1.00 33.86 ? 334 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 11.186 11.878  11.270 1.00 14.25 ? 335 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? 15.081 10.398  24.723 1.00 26.62 ? 336 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 29.572 3.987   11.494 1.00 22.79 ? 337 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 24.282 17.902  3.699  1.00 46.52 ? 338 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 14.508 2.995   23.225 1.00 15.50 ? 339 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 14.194 -11.952 4.900  1.00 58.65 ? 340 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? 6.530  17.318  22.034 1.00 40.95 ? 341 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 11.137 2.719   33.405 1.00 17.39 ? 342 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? 4.981  8.024   27.814 1.00 31.81 ? 343 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? 31.102 19.053  8.835  1.00 30.00 ? 344 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 3.965  5.965   24.716 1.00 18.77 ? 345 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? 18.153 -6.235  3.287  1.00 35.28 ? 346 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 30.488 20.986  10.806 1.00 26.15 ? 347 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? 30.324 11.430  2.594  1.00 52.97 ? 348 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 22.307 18.954  19.533 1.00 39.69 ? 349 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 34.542 20.821  12.080 1.00 42.20 ? 350 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? 6.178  18.292  24.380 1.00 40.66 ? 351 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 0.569  1.536   24.107 1.00 19.67 ? 352 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? -0.214 16.190  7.679  1.00 42.70 ? 353 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 6.836  4.068   32.715 1.00 23.30 ? 354 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 5.087  -1.198  24.147 1.00 21.63 ? 355 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 9.228  2.580   2.745  1.00 25.46 ? 356 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? 21.259 19.641  17.835 1.00 25.03 ? 357 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 17.442 19.410  17.015 1.00 16.09 ? 358 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 17.450 3.029   23.252 1.00 22.97 ? 359 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 14.673 12.909  24.069 1.00 22.26 ? 360 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? 6.323  1.689   5.773  1.00 22.58 ? 361 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 16.817 21.014  19.129 1.00 26.60 ? 362 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? 14.685 -4.188  17.263 1.00 27.95 ? 363 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 13.072 10.802  9.321  1.00 14.10 ? 364 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 14.844 -5.284  -0.145 1.00 47.84 ? 365 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 17.581 1.067   29.921 1.00 34.65 ? 366 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 7.654  8.137   32.632 1.00 44.92 ? 367 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 9.045  21.313  10.555 1.00 40.04 ? 368 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 4.860  7.284   2.820  1.00 38.06 ? 369 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 29.644 11.782  19.939 1.00 34.86 ? 370 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 9.714  5.098   33.843 1.00 19.94 ? 371 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 31.840 9.470   6.354  1.00 34.95 ? 372 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? 4.320  -4.849  6.202  1.00 29.43 ? 373 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 2.063  10.042  28.114 1.00 40.97 ? 374 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 11.690 21.717  12.185 1.00 29.11 ? 375 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 17.946 19.698  5.617  1.00 37.56 ? 376 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 35.256 3.283   3.805  1.00 64.07 ? 377 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 36.752 -0.038  11.386 1.00 38.79 ? 378 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 4.077  -2.122  20.920 1.00 34.24 ? 379 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 2.831  15.836  19.885 1.00 33.18 ? 380 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? -0.912 15.446  12.415 1.00 29.98 ? 381 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 9.835  -7.744  7.842  1.00 36.85 ? 382 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 30.397 5.209   4.391  1.00 34.80 ? 383 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 5.481  -6.904  6.980  1.00 64.96 ? 384 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 18.085 9.877   25.812 1.00 25.26 ? 385 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 30.096 11.755  17.264 1.00 40.66 ? 386 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 0.177  3.983   6.382  1.00 29.45 ? 387 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? -0.139 -5.516  10.806 1.00 40.53 ? 388 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 22.123 4.000   23.933 1.00 50.36 ? 389 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? -3.837 21.930  10.285 1.00 56.90 ? 390 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 1.567  10.854  21.578 1.00 33.22 ? 391 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 12.231 -7.467  13.123 1.00 30.85 ? 392 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 7.421  -7.843  23.953 1.00 31.24 ? 393 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? 1.694  13.112  5.241  1.00 35.37 ? 394 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 32.110 2.103   4.414  1.00 49.49 ? 395 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 4.049  10.695  19.623 1.00 47.92 ? 396 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? 16.375 -4.339  1.980  1.00 31.35 ? 397 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 19.997 -3.206  16.540 1.00 33.03 ? 398 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 14.109 21.317  8.376  1.00 33.06 ? 399 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 6.725  12.880  5.192  1.00 24.86 ? 400 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 18.829 12.986  1.711  1.00 34.79 ? 401 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 8.581  -7.454  9.911  1.00 50.53 ? 402 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 22.644 -1.746  16.729 1.00 30.37 ? 403 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 5.448  26.750  19.250 1.00 33.00 ? 404 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 5.028  13.756  20.226 1.00 65.31 ? 405 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 30.896 15.837  21.983 1.00 25.41 ? 406 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 21.437 9.385   21.464 1.00 20.95 ? 407 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 1.771  -1.727  17.371 1.00 26.02 ? 408 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 17.132 23.262  16.784 1.00 36.39 ? 409 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 19.343 16.565  26.248 1.00 51.30 ? 410 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 14.593 14.934  3.663  1.00 32.36 ? 411 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 16.526 -2.840  17.972 1.00 33.01 ? 412 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 22.356 19.432  6.095  1.00 27.24 ? 413 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 30.395 21.549  17.221 1.00 41.35 ? 414 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 4.568  -1.034  28.950 1.00 43.72 ? 415 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 23.629 3.116   20.124 1.00 26.91 ? 416 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 19.537 24.050  15.679 1.00 22.28 ? 417 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 8.274  -5.519  2.698  1.00 37.18 ? 418 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 31.200 3.504   13.618 1.00 31.66 ? 419 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 5.869  23.018  10.480 1.00 39.13 ? 420 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 2.627  -6.101  14.731 1.00 44.13 ? 421 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 28.163 17.219  23.643 1.00 34.08 ? 422 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 18.517 9.171   -1.397 1.00 30.19 ? 423 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 1.919  -5.906  17.607 1.00 44.34 ? 424 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 14.967 -9.014  12.070 1.00 39.35 ? 425 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 15.686 24.235  14.706 1.00 55.76 ? 426 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 10.856 15.724  26.313 1.00 63.03 ? 427 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? -2.073 21.381  24.516 1.00 58.80 ? 428 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 11.154 20.108  4.886  1.00 56.02 ? 429 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 36.465 7.283   6.100  1.00 67.54 ? 430 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 29.171 3.145   20.293 1.00 72.17 ? 431 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 13.500 14.578  26.249 1.00 48.75 ? 432 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 30.023 0.805   15.445 1.00 43.71 ? 433 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 1.799  1.647   26.483 1.00 31.88 ? 434 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 11.366 23.834  13.848 1.00 36.77 ? 435 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 3.811  -1.922  26.603 1.00 42.23 ? 436 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 20.881 22.560  17.770 1.00 29.15 ? 437 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 32.586 22.497  24.005 1.00 58.19 ? 438 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 6.587  2.700   3.159  1.00 29.94 ? 439 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 0.933  -1.282  23.459 1.00 28.26 ? 440 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 31.318 11.704  5.064  1.00 42.16 ? 441 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 9.223  7.523   2.466  1.00 42.50 ? 442 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 2.163  12.546  28.052 1.00 71.81 ? 443 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 9.649  -8.165  12.509 1.00 39.48 ? 444 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? 39.749 6.797   17.326 1.00 39.36 ? 445 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 2.807  26.378  20.360 1.00 47.71 ? 446 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 32.931 22.225  20.308 1.00 52.02 ? 447 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 3.180  -4.663  27.348 1.00 57.86 ? 448 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 3.356  -3.034  22.993 1.00 31.74 ? 449 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 32.330 10.181  0.987  1.00 66.21 ? 450 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 1.672  -4.717  6.905  1.00 51.43 ? 451 HOH   A O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? 3.619  18.433  26.564 1.00 62.83 ? 452 HOH   A O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? 27.567 0.267   19.060 1.00 57.64 ? 453 HOH   A O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? 31.007 -1.448  17.925 1.00 56.33 ? 454 HOH   A O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? 37.156 -2.013  15.524 1.00 70.10 ? 455 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 31.366 15.979  26.617 1.00 67.73 ? 456 HOH   A O   1 
HETATM 2367 O  O   . HOH   I 5 .   ? 14.412 -7.622  24.836 1.00 29.19 ? 301 HOH   C O   1 
HETATM 2368 O  O   . HOH   I 5 .   ? 32.090 -22.193 22.123 1.00 35.07 ? 302 HOH   C O   1 
HETATM 2369 O  O   . HOH   I 5 .   ? 9.785  -36.713 21.882 1.00 42.58 ? 303 HOH   C O   1 
HETATM 2370 O  O   . HOH   I 5 .   ? 20.614 -18.957 31.746 1.00 41.02 ? 304 HOH   C O   1 
HETATM 2371 O  O   . HOH   I 5 .   ? 3.815  -9.775  22.134 1.00 39.48 ? 305 HOH   C O   1 
HETATM 2372 O  O   . HOH   I 5 .   ? 30.484 -35.327 11.119 1.00 30.00 ? 306 HOH   C O   1 
HETATM 2373 O  O   . HOH   I 5 .   ? 24.528 -22.095 27.766 1.00 22.94 ? 307 HOH   C O   1 
HETATM 2374 O  O   . HOH   I 5 .   ? 11.222 -30.471 17.420 1.00 25.93 ? 308 HOH   C O   1 
HETATM 2375 O  O   . HOH   I 5 .   ? 14.246 -21.654 13.799 1.00 16.56 ? 309 HOH   C O   1 
HETATM 2376 O  O   . HOH   I 5 .   ? 11.887 -35.274 20.038 1.00 46.06 ? 310 HOH   C O   1 
HETATM 2377 O  O   . HOH   I 5 .   ? 24.804 -25.373 28.953 1.00 17.92 ? 311 HOH   C O   1 
HETATM 2378 O  O   . HOH   I 5 .   ? 28.249 -15.959 10.521 1.00 43.72 ? 312 HOH   C O   1 
HETATM 2379 O  O   . HOH   I 5 .   ? 10.986 -8.455  24.690 1.00 24.00 ? 313 HOH   C O   1 
HETATM 2380 O  O   . HOH   I 5 .   ? 17.270 -36.985 29.461 1.00 35.37 ? 314 HOH   C O   1 
HETATM 2381 O  O   . HOH   I 5 .   ? 22.420 -28.689 -0.948 1.00 20.83 ? 315 HOH   C O   1 
HETATM 2382 O  O   . HOH   I 5 .   ? 22.337 -21.897 1.308  1.00 38.05 ? 316 HOH   C O   1 
HETATM 2383 O  O   . HOH   I 5 .   ? 22.793 -19.562 31.949 1.00 36.72 ? 317 HOH   C O   1 
HETATM 2384 O  O   . HOH   I 5 .   ? 8.285  -21.985 32.793 1.00 42.53 ? 318 HOH   C O   1 
HETATM 2385 O  O   . HOH   I 5 .   ? 32.469 -16.681 10.015 1.00 55.04 ? 319 HOH   C O   1 
HETATM 2386 O  O   . HOH   I 5 .   ? 7.191  -14.336 29.917 1.00 41.85 ? 320 HOH   C O   1 
HETATM 2387 O  O   . HOH   I 5 .   ? 7.943  -26.579 13.076 1.00 39.46 ? 321 HOH   C O   1 
HETATM 2388 O  O   . HOH   I 5 .   ? 3.909  -20.409 19.469 1.00 34.80 ? 322 HOH   C O   1 
HETATM 2389 O  O   . HOH   I 5 .   ? 7.171  -26.899 30.306 1.00 41.17 ? 323 HOH   C O   1 
HETATM 2390 O  O   . HOH   I 5 .   ? 4.338  -19.364 13.573 1.00 31.57 ? 324 HOH   C O   1 
HETATM 2391 O  O   . HOH   I 5 .   ? 4.585  -24.511 14.832 1.00 40.11 ? 325 HOH   C O   1 
HETATM 2392 O  O   . HOH   I 5 .   ? 13.150 -26.736 36.940 1.00 77.78 ? 326 HOH   C O   1 
HETATM 2393 O  O   . HOH   I 5 .   ? 20.418 -22.075 2.605  1.00 39.26 ? 327 HOH   C O   1 
HETATM 2394 O  O   . HOH   I 5 .   ? 29.786 -24.741 7.597  1.00 28.32 ? 328 HOH   C O   1 
HETATM 2395 O  O   . HOH   I 5 .   ? -0.984 -14.291 16.661 1.00 38.84 ? 329 HOH   C O   1 
HETATM 2396 O  O   . HOH   I 5 .   ? 24.270 -11.808 12.087 1.00 19.94 ? 330 HOH   C O   1 
HETATM 2397 O  O   . HOH   I 5 .   ? 33.904 -30.753 15.555 1.00 15.48 ? 331 HOH   C O   1 
HETATM 2398 O  O   . HOH   I 5 .   ? 29.767 -30.172 34.417 1.00 33.11 ? 332 HOH   C O   1 
HETATM 2399 O  O   . HOH   I 5 .   ? 18.139 -13.154 28.424 1.00 44.86 ? 333 HOH   C O   1 
HETATM 2400 O  O   . HOH   I 5 .   ? 28.451 -22.615 4.255  1.00 47.35 ? 334 HOH   C O   1 
HETATM 2401 O  O   . HOH   I 5 .   ? 25.974 -10.523 14.208 1.00 20.18 ? 335 HOH   C O   1 
HETATM 2402 O  O   . HOH   I 5 .   ? 23.392 -18.768 20.956 1.00 15.27 ? 336 HOH   C O   1 
HETATM 2403 O  O   . HOH   I 5 .   ? 10.252 -19.847 11.979 1.00 41.08 ? 337 HOH   C O   1 
HETATM 2404 O  O   . HOH   I 5 .   ? 24.226 -26.616 -1.080 1.00 32.80 ? 338 HOH   C O   1 
HETATM 2405 O  O   . HOH   I 5 .   ? 37.474 -23.753 6.570  1.00 35.85 ? 339 HOH   C O   1 
HETATM 2406 O  O   . HOH   I 5 .   ? 19.407 -28.103 9.450  1.00 16.11 ? 340 HOH   C O   1 
HETATM 2407 O  O   . HOH   I 5 .   ? 4.385  -30.527 30.295 1.00 57.85 ? 341 HOH   C O   1 
HETATM 2408 O  O   . HOH   I 5 .   ? 18.513 -38.027 22.234 1.00 45.02 ? 342 HOH   C O   1 
HETATM 2409 O  O   . HOH   I 5 .   ? 12.564 -11.552 15.172 1.00 26.49 ? 343 HOH   C O   1 
HETATM 2410 O  O   . HOH   I 5 .   ? 36.177 -30.612 27.885 1.00 36.77 ? 344 HOH   C O   1 
HETATM 2411 O  O   . HOH   I 5 .   ? 27.013 -26.854 -0.328 1.00 40.26 ? 345 HOH   C O   1 
HETATM 2412 O  O   . HOH   I 5 .   ? 16.923 -9.273  23.162 1.00 20.39 ? 346 HOH   C O   1 
HETATM 2413 O  O   . HOH   I 5 .   ? 15.023 -30.962 5.536  1.00 33.51 ? 347 HOH   C O   1 
HETATM 2414 O  O   . HOH   I 5 .   ? 4.008  -19.568 16.100 1.00 35.97 ? 348 HOH   C O   1 
HETATM 2415 O  O   . HOH   I 5 .   ? 12.641 -31.501 28.849 1.00 29.52 ? 349 HOH   C O   1 
HETATM 2416 O  O   . HOH   I 5 .   ? 5.320  -27.219 22.572 1.00 25.22 ? 350 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 5 .   ? 16.572 -11.131 27.073 1.00 35.55 ? 351 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 5 .   ? 22.124 -5.278  10.448 1.00 26.41 ? 352 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 5 .   ? 14.028 -14.314 6.460  1.00 61.16 ? 353 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 5 .   ? 18.764 -18.019 8.445  1.00 25.34 ? 354 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 5 .   ? 33.932 -15.974 14.744 1.00 32.37 ? 355 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 5 .   ? 26.337 -27.507 29.624 1.00 20.26 ? 356 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 5 .   ? 30.956 -22.716 28.915 1.00 29.05 ? 357 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 5 .   ? 3.439  -9.932  16.048 1.00 27.64 ? 358 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 5 .   ? 16.505 -28.065 9.596  1.00 24.01 ? 359 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 5 .   ? 16.290 -11.588 15.617 1.00 17.38 ? 360 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 5 .   ? 17.989 -7.714  15.532 1.00 38.44 ? 361 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 5 .   ? 16.258 -30.110 2.559  1.00 40.52 ? 362 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 5 .   ? 11.381 -12.093 13.310 1.00 41.14 ? 363 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 5 .   ? 15.441 -21.500 7.113  1.00 35.99 ? 364 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 5 .   ? 27.756 -41.019 29.093 1.00 68.24 ? 365 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 5 .   ? 21.669 -19.873 23.124 1.00 14.20 ? 366 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 5 .   ? 30.259 -29.645 1.902  1.00 57.62 ? 367 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 5 .   ? 34.163 -28.622 7.707  1.00 36.70 ? 368 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 5 .   ? 26.661 -34.208 32.044 1.00 21.65 ? 369 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 5 .   ? 8.353  -32.364 18.680 1.00 31.05 ? 370 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 5 .   ? 33.829 -32.945 12.298 1.00 31.85 ? 371 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 5 .   ? 23.675 -35.068 33.002 1.00 33.06 ? 372 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 5 .   ? 21.512 -11.310 5.781  1.00 36.36 ? 373 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 5 .   ? 27.809 -36.303 3.449  1.00 36.26 ? 374 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 5 .   ? 4.925  -25.642 29.585 1.00 41.99 ? 375 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 5 .   ? 20.270 -9.460  23.944 1.00 33.33 ? 376 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 5 .   ? 29.154 -28.307 25.298 1.00 18.20 ? 377 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 5 .   ? 3.416  -21.353 27.583 1.00 36.20 ? 378 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 5 .   ? 26.640 -4.704  18.266 1.00 40.54 ? 379 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 5 .   ? 15.147 -26.476 7.020  1.00 50.25 ? 380 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 5 .   ? 19.913 -35.116 15.542 1.00 20.67 ? 381 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 5 .   ? 30.863 -35.442 25.733 1.00 30.76 ? 382 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 5 .   ? 23.797 -35.505 1.000  1.00 30.11 ? 383 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 28.981 -31.886 8.274  1.00 24.69 ? 384 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 16.017 -30.797 13.206 1.00 21.81 ? 385 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 5.185  -19.093 30.714 1.00 57.80 ? 386 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 12.887 -13.947 8.953  1.00 36.56 ? 387 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 26.095 -37.758 23.064 1.00 26.53 ? 388 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 8.236  -32.178 26.632 1.00 40.66 ? 389 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 16.460 -10.268 13.384 1.00 32.33 ? 390 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 33.082 -17.139 26.214 1.00 32.02 ? 391 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 28.191 -17.515 26.701 1.00 23.73 ? 392 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 24.091 -14.426 29.151 1.00 48.72 ? 393 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 6.105  -32.582 19.979 1.00 39.75 ? 394 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 13.850 -11.210 11.353 1.00 39.55 ? 395 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 20.454 -15.786 28.818 1.00 29.85 ? 396 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 19.506 -34.788 30.937 1.00 24.28 ? 397 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 24.978 -9.305  21.317 1.00 38.70 ? 398 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? -1.782 -31.351 22.907 1.00 46.09 ? 399 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 12.319 -11.488 26.836 1.00 28.23 ? 400 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 28.422 -7.512  21.103 1.00 34.22 ? 401 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 16.465 -17.572 30.979 1.00 38.00 ? 402 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 5.454  -14.039 9.984  1.00 33.90 ? 403 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 16.237 -12.414 29.890 1.00 60.98 ? 404 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 33.277 -33.261 14.800 1.00 24.04 ? 405 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 35.050 -34.934 16.047 1.00 45.58 ? 406 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 30.481 -32.668 10.444 1.00 33.84 ? 407 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 35.153 -15.003 18.555 1.00 30.69 ? 408 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 16.663 -11.505 2.225  1.00 62.96 ? 409 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 3.516  -27.965 20.624 1.00 29.20 ? 410 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 2.581  -15.755 11.886 1.00 25.83 ? 411 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 31.937 -20.164 3.798  1.00 48.75 ? 412 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 15.185 -6.678  17.308 1.00 25.77 ? 413 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 22.612 -8.986  20.093 1.00 32.28 ? 414 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 9.849  -23.042 12.439 1.00 34.32 ? 415 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 22.699 -38.298 19.636 1.00 32.15 ? 416 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 3.486  -25.702 35.418 1.00 56.80 ? 417 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 18.025 -13.624 3.457  1.00 68.63 ? 418 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 17.919 -33.736 14.990 1.00 34.44 ? 419 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 10.572 -28.313 13.644 1.00 30.86 ? 420 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 15.751 -15.008 31.266 1.00 70.51 ? 421 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 12.369 -21.724 11.801 1.00 23.20 ? 422 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 27.625 -35.631 29.720 1.00 25.98 ? 423 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 25.933 -7.271  6.117  1.00 52.70 ? 424 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 27.845 -19.488 28.244 1.00 44.97 ? 425 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 13.982 -8.364  14.991 1.00 36.25 ? 426 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 30.206 -28.201 27.776 1.00 36.13 ? 427 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 3.864  -23.200 30.204 1.00 46.62 ? 428 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 0.078  -24.660 18.684 1.00 53.84 ? 429 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 5 .   ? 6.749  -29.539 30.598 1.00 54.53 ? 430 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 5 .   ? 2.904  -21.806 17.237 1.00 41.43 ? 431 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 5 .   ? 3.946  -30.256 19.235 1.00 43.31 ? 432 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 5 .   ? 10.196 -15.244 8.960  1.00 58.67 ? 433 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 5 .   ? 25.867 -42.386 31.110 1.00 56.87 ? 434 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 5 .   ? 6.435  -23.456 37.549 1.00 60.56 ? 435 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 5 .   ? 5.956  -28.405 12.691 1.00 70.09 ? 436 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 5 .   ? 36.748 -22.934 4.429  1.00 45.63 ? 437 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 5 .   ? 30.511 -17.182 28.083 1.00 55.03 ? 438 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 5 .   ? 28.926 -26.947 29.687 1.00 32.36 ? 439 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 5 .   ? 17.166 -18.337 5.673  1.00 71.65 ? 440 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 5 .   ? 26.036 -23.068 29.857 1.00 31.64 ? 441 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 5 .   ? 1.901  -8.638  18.040 1.00 36.77 ? 442 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 5 .   ? 27.898 -38.145 30.162 1.00 56.61 ? 443 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 5 .   ? 37.034 -15.480 21.437 1.00 79.80 ? 444 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 5 .   ? 18.692 -40.160 21.068 1.00 42.13 ? 445 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 5 .   ? 14.054 -12.915 31.804 1.00 59.44 ? 446 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 5 .   ? 12.298 -35.579 0.435  1.00 56.65 ? 447 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 5 .   ? -0.879 -22.454 29.359 1.00 73.50 ? 448 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 5 .   ? 11.739 -20.568 9.324  1.00 43.42 ? 449 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 5 .   ? -0.706 -31.421 30.901 1.00 79.90 ? 450 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 5 .   ? 33.558 -5.126  20.632 1.00 60.31 ? 451 HOH   C O   1 
HETATM 2518 O  O   . HOH   I 5 .   ? 0.746  -20.861 27.892 1.00 53.55 ? 452 HOH   C O   1 
HETATM 2519 O  O   . HOH   I 5 .   ? 37.092 -15.587 3.937  1.00 51.43 ? 453 HOH   C O   1 
HETATM 2520 O  O   . HOH   I 5 .   ? 31.996 -6.399  18.307 1.00 74.53 ? 454 HOH   C O   1 
HETATM 2521 O  O   . HOH   I 5 .   ? 4.659  -29.732 16.368 1.00 62.18 ? 455 HOH   C O   1 
HETATM 2522 O  O   . HOH   I 5 .   ? -0.588 -8.972  23.989 1.00 67.86 ? 456 HOH   C O   1 
HETATM 2523 O  O   . HOH   I 5 .   ? 4.984  -7.657  23.437 1.00 38.51 ? 457 HOH   C O   1 
HETATM 2524 O  O   . HOH   I 5 .   ? 26.062 -6.171  20.732 1.00 60.30 ? 458 HOH   C O   1 
HETATM 2525 O  O   . HOH   I 5 .   ? 24.512 -7.991  25.939 1.00 61.58 ? 459 HOH   C O   1 
HETATM 2526 O  O   . HOH   I 5 .   ? 6.866  -30.679 15.154 1.00 52.03 ? 460 HOH   C O   1 
HETATM 2527 O  O   . HOH   I 5 .   ? 29.280 -16.444 0.570  1.00 61.20 ? 461 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   ? 0.2732 0.2737 0.2619 -0.0037 -0.0127 -0.0132 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2647 0.2673 0.2659 -0.0018 -0.0150 -0.0113 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2583 0.2609 0.2661 0.0012  -0.0133 -0.0069 7   SER   A C   
4    O O   . SER   A 1   ? 0.2795 0.2807 0.2819 0.0015  -0.0126 -0.0044 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2945 0.2993 0.2965 -0.0046 -0.0223 -0.0101 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3345 0.3398 0.3322 -0.0053 -0.0269 -0.0049 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2343 0.2379 0.2536 0.0031  -0.0119 -0.0064 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2237 0.2262 0.2495 0.0053  -0.0090 -0.0033 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2089 0.2107 0.2422 0.0062  -0.0042 -0.0047 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2187 0.2207 0.2510 0.0055  -0.0029 -0.0074 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1797 0.1804 0.2211 0.0074  -0.0013 -0.0029 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1861 0.1855 0.2332 0.0073  0.0040  -0.0042 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1851 0.1804 0.2333 0.0076  0.0099  -0.0033 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2061 0.2001 0.2555 0.0087  0.0095  -0.0011 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2008 0.2034 0.2612 0.0078  0.0021  -0.0041 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1686 0.1612 0.2162 0.0060  0.0158  -0.0049 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1742 0.1617 0.2224 0.0049  0.0230  -0.0055 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1855 0.1731 0.2475 0.0056  0.0270  -0.0059 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1903 0.1802 0.2553 0.0049  0.0265  -0.0067 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1865 0.1703 0.2220 0.0010  0.0271  -0.0070 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1862 0.1713 0.2105 0.0003  0.0229  -0.0062 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2062 0.1833 0.2394 -0.0016 0.0354  -0.0086 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2064 0.1905 0.2206 -0.0038 0.0243  -0.0063 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1932 0.1784 0.2650 0.0071  0.0315  -0.0054 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1971 0.1827 0.2852 0.0079  0.0366  -0.0058 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1978 0.1754 0.2836 0.0054  0.0481  -0.0088 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2178 0.1910 0.3055 0.0064  0.0518  -0.0087 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2057 0.1961 0.3123 0.0121  0.0322  -0.0020 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2191 0.2169 0.3267 0.0130  0.0209  0.0005  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2375 0.2365 0.3355 0.0134  0.0136  0.0026  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2270 0.2299 0.3437 0.0125  0.0183  0.0001  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2472 0.2518 0.3432 0.0129  0.0043  0.0039  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2321 0.2408 0.3477 0.0121  0.0085  0.0013  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2481 0.2573 0.3527 0.0121  0.0017  0.0030  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2716 0.2851 0.3723 0.0105  -0.0069 0.0032  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2031 0.1779 0.2828 0.0016  0.0539  -0.0116 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2272 0.1933 0.3003 -0.0027 0.0655  -0.0153 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2454 0.2106 0.3282 -0.0042 0.0732  -0.0172 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2489 0.2178 0.3303 -0.0054 0.0698  -0.0164 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2691 0.2311 0.3185 -0.0084 0.0650  -0.0166 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2702 0.2370 0.3127 -0.0097 0.0583  -0.0146 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2953 0.2477 0.3347 -0.0147 0.0768  -0.0208 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2642 0.2248 0.3596 -0.0038 0.0837  -0.0195 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2569 0.2168 0.3638 -0.0052 0.0925  -0.0215 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2414 0.2116 0.3662 -0.0010 0.0845  -0.0179 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2432 0.2200 0.3811 0.0042  0.0760  -0.0142 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2389 0.2105 0.3614 -0.0040 0.0856  -0.0185 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2382 0.2191 0.3758 -0.0012 0.0775  -0.0156 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2197 0.2036 0.3423 -0.0022 0.0667  -0.0139 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2172 0.2049 0.3443 -0.0029 0.0635  -0.0131 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2715 0.2527 0.4230 -0.0031 0.0864  -0.0171 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3724 0.3533 0.5469 -0.0004 0.0957  -0.0180 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4096 0.3982 0.6058 0.0047  0.0898  -0.0146 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3843 0.3564 0.5549 -0.0043 0.1105  -0.0224 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2019 0.1840 0.3082 -0.0021 0.0615  -0.0133 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1942 0.1787 0.2877 -0.0027 0.0524  -0.0118 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1751 0.1637 0.2681 0.0010  0.0431  -0.0100 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1855 0.1727 0.2797 0.0027  0.0441  -0.0097 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2085 0.1868 0.2806 -0.0074 0.0552  -0.0124 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2228 0.1962 0.2902 -0.0126 0.0635  -0.0135 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2391 0.2150 0.3134 -0.0131 0.0627  -0.0125 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2597 0.2253 0.3142 -0.0177 0.0721  -0.0156 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2644 0.2354 0.3332 -0.0185 0.0704  -0.0129 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2786 0.2391 0.3263 -0.0237 0.0800  -0.0165 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2974 0.2607 0.3525 -0.0238 0.0791  -0.0148 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3488 0.3066 0.3960 -0.0302 0.0869  -0.0151 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1639 0.1570 0.2550 0.0018  0.0347  -0.0090 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1706 0.1668 0.2571 0.0039  0.0264  -0.0079 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1811 0.1758 0.2526 0.0022  0.0240  -0.0082 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1776 0.1725 0.2495 0.0008  0.0238  -0.0085 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1661 0.1687 0.2650 0.0056  0.0192  -0.0070 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1959 0.2011 0.2868 0.0061  0.0107  -0.0068 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2082 0.2193 0.3096 0.0062  0.0033  -0.0059 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2121 0.2239 0.3046 0.0046  -0.0023 -0.0079 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2429 0.2559 0.3274 0.0042  -0.0084 -0.0077 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2615 0.2750 0.3446 0.0056  -0.0103 -0.0046 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2503 0.2629 0.3271 0.0020  -0.0116 -0.0107 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1897 0.1826 0.2495 0.0021  0.0228  -0.0078 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1762 0.1687 0.2249 0.0009  0.0205  -0.0074 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1723 0.1681 0.2196 0.0029  0.0142  -0.0076 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1693 0.1656 0.2147 0.0041  0.0126  -0.0072 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1874 0.1761 0.2242 -0.0018 0.0239  -0.0067 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1898 0.1794 0.2187 -0.0032 0.0211  -0.0051 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1849 0.1689 0.2209 -0.0049 0.0314  -0.0075 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1564 0.1538 0.2045 0.0030  0.0114  -0.0084 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1681 0.1675 0.2135 0.0040  0.0068  -0.0097 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1711 0.1698 0.2121 0.0038  0.0071  -0.0099 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1749 0.1723 0.2172 0.0029  0.0093  -0.0084 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1902 0.1918 0.2430 0.0040  0.0032  -0.0115 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2506 0.2543 0.3103 0.0047  0.0017  -0.0100 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1831 0.1840 0.2428 0.0031  0.0049  -0.0124 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1489 0.1484 0.1857 0.0043  0.0051  -0.0116 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1445 0.1436 0.1814 0.0046  0.0061  -0.0122 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1594 0.1572 0.2039 0.0044  0.0063  -0.0141 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1569 0.1549 0.2034 0.0036  0.0042  -0.0169 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1501 0.1496 0.1818 0.0048  0.0053  -0.0149 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1718 0.1724 0.1965 0.0048  0.0055  -0.0130 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1894 0.1901 0.2099 0.0045  0.0038  -0.0127 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1709 0.1724 0.1954 0.0051  0.0073  -0.0111 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1476 0.1441 0.1967 0.0046  0.0082  -0.0121 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1536 0.1479 0.2105 0.0042  0.0089  -0.0134 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1707 0.1636 0.2284 0.0039  0.0085  -0.0190 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1783 0.1701 0.2401 0.0023  0.0076  -0.0219 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1517 0.1444 0.2132 0.0046  0.0107  -0.0093 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1548 0.1445 0.2247 0.0039  0.0119  -0.0096 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1632 0.1513 0.2381 0.0046  0.0131  -0.0042 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1772 0.1615 0.2605 0.0038  0.0146  -0.0029 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1863 0.1671 0.2778 0.0047  0.0163  -0.0062 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1998 0.1801 0.2911 0.0058  0.0171  -0.0120 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1890 0.1658 0.2883 0.0038  0.0178  -0.0041 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1612 0.1541 0.2144 0.0046  0.0094  -0.0209 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1696 0.1598 0.2215 0.0032  0.0104  -0.0271 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1951 0.1863 0.2398 0.0004  0.0065  -0.0303 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2316 0.2201 0.2734 -0.0023 0.0067  -0.0358 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1838 0.1729 0.2343 0.0045  0.0143  -0.0286 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2089 0.2009 0.2499 0.0044  0.0134  -0.0279 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2101 0.2056 0.2506 0.0059  0.0124  -0.0224 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2283 0.2195 0.2595 0.0022  0.0134  -0.0321 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2210 0.2177 0.2527 0.0052  0.0122  -0.0234 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2310 0.2252 0.2567 0.0030  0.0128  -0.0288 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1825 0.1772 0.2243 0.0007  0.0030  -0.0268 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1825 0.1793 0.2200 -0.0017 -0.0020 -0.0278 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1921 0.1912 0.2387 -0.0021 -0.0047 -0.0258 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2072 0.2093 0.2538 -0.0038 -0.0096 -0.0252 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1867 0.1855 0.2162 -0.0010 -0.0036 -0.0250 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2066 0.2036 0.2274 -0.0011 -0.0007 -0.0269 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2272 0.2260 0.2407 -0.0007 -0.0024 -0.0235 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2192 0.2133 0.2332 -0.0048 -0.0007 -0.0329 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1896 0.1876 0.2448 -0.0009 -0.0015 -0.0244 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1789 0.1791 0.2436 -0.0015 -0.0026 -0.0227 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1844 0.1857 0.2529 -0.0049 -0.0068 -0.0262 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.1920 0.1901 0.2575 -0.0071 -0.0065 -0.0306 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1773 0.1752 0.2483 -0.0006 0.0020  -0.0208 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1807 0.1865 0.2570 -0.0057 -0.0103 -0.0241 24  THR   A N   
135  C CA  . THR   A 18  ? 0.2011 0.2097 0.2823 -0.0097 -0.0159 -0.0263 24  THR   A CA  
136  C C   . THR   A 18  ? 0.2125 0.2205 0.3057 -0.0110 -0.0134 -0.0274 24  THR   A C   
137  O O   . THR   A 18  ? 0.2017 0.2076 0.2995 -0.0086 -0.0077 -0.0254 24  THR   A O   
138  C CB  . THR   A 18  ? 0.2320 0.2472 0.3187 -0.0097 -0.0219 -0.0221 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2255 0.2430 0.3253 -0.0068 -0.0183 -0.0183 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2454 0.2608 0.3208 -0.0085 -0.0244 -0.0200 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2207 0.2309 0.3190 -0.0155 -0.0183 -0.0300 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2345 0.2447 0.3460 -0.0172 -0.0161 -0.0307 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2042 0.2188 0.3286 -0.0144 -0.0136 -0.0256 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2052 0.2173 0.3361 -0.0135 -0.0074 -0.0248 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2858 0.2992 0.4015 -0.0234 -0.0231 -0.0339 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4173 0.4249 0.5196 -0.0277 -0.0243 -0.0404 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4811 0.4804 0.5808 -0.0275 -0.0175 -0.0447 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4646 0.4733 0.5562 -0.0327 -0.0311 -0.0432 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4948 0.4898 0.5829 -0.0321 -0.0191 -0.0508 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4972 0.4974 0.5784 -0.0358 -0.0272 -0.0504 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.1968 0.2173 0.3245 -0.0128 -0.0174 -0.0218 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2011 0.2250 0.3422 -0.0101 -0.0135 -0.0177 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1919 0.2102 0.3265 -0.0067 -0.0049 -0.0166 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1892 0.2069 0.3322 -0.0062 0.0015  -0.0153 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2341 0.2646 0.3817 -0.0088 -0.0191 -0.0136 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3211 0.3590 0.4900 -0.0103 -0.0217 -0.0113 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.2821 0.3220 0.4570 -0.0145 -0.0248 -0.0137 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3950 0.4365 0.5774 -0.0069 -0.0187 -0.0071 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1670 0.1814 0.2863 -0.0051 -0.0045 -0.0171 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1644 0.1738 0.2764 -0.0031 0.0025  -0.0158 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1653 0.1705 0.2792 -0.0046 0.0072  -0.0165 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1733 0.1763 0.2886 -0.0047 0.0132  -0.0145 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1707 0.1773 0.2676 -0.0018 0.0013  -0.0163 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2210 0.2300 0.3140 0.0000  -0.0013 -0.0145 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2118 0.2222 0.3114 0.0012  0.0012  -0.0121 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2130 0.2218 0.2964 -0.0002 -0.0052 -0.0156 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1620 0.1654 0.2753 -0.0064 0.0048  -0.0194 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1699 0.1687 0.2861 -0.0077 0.0090  -0.0194 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1921 0.1926 0.3216 -0.0098 0.0117  -0.0186 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2008 0.1975 0.3314 -0.0106 0.0174  -0.0164 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1721 0.1674 0.2856 -0.0090 0.0068  -0.0233 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1785 0.1700 0.2815 -0.0067 0.0079  -0.0231 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2025 0.1945 0.2972 -0.0060 0.0051  -0.0256 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1718 0.1589 0.2730 -0.0052 0.0120  -0.0197 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.1992 0.1879 0.2884 -0.0037 0.0079  -0.0243 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1958 0.1818 0.2896 -0.0032 0.0114  -0.0203 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1925 0.1768 0.2977 -0.0059 0.0158  -0.0155 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1972 0.1802 0.2897 -0.0014 0.0139  -0.0164 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2062 0.1869 0.3082 -0.0045 0.0177  -0.0114 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2086 0.1892 0.3054 -0.0021 0.0164  -0.0117 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1853 0.1919 0.3253 -0.0111 0.0078  -0.0197 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1948 0.2044 0.3503 -0.0130 0.0108  -0.0188 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2037 0.2132 0.3618 -0.0114 0.0180  -0.0157 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2172 0.2271 0.3860 -0.0131 0.0236  -0.0149 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2085 0.2258 0.3760 -0.0148 0.0038  -0.0199 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1845 0.1936 0.3335 -0.0086 0.0185  -0.0143 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1914 0.1990 0.3409 -0.0078 0.0261  -0.0125 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1905 0.1913 0.3215 -0.0077 0.0296  -0.0113 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1826 0.1816 0.3073 -0.0070 0.0334  -0.0105 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1951 0.2077 0.3511 -0.0052 0.0238  -0.0117 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2129 0.2331 0.3896 -0.0057 0.0204  -0.0113 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2304 0.2520 0.4213 -0.0067 0.0269  -0.0109 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2156 0.2411 0.3943 -0.0058 0.0103  -0.0113 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1757 0.1727 0.2995 -0.0089 0.0284  -0.0110 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1726 0.1646 0.2811 -0.0089 0.0297  -0.0087 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1985 0.1864 0.3008 -0.0116 0.0372  -0.0064 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2265 0.2125 0.3342 -0.0145 0.0424  -0.0058 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1793 0.1682 0.2866 -0.0096 0.0275  -0.0080 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1799 0.1647 0.2749 -0.0096 0.0276  -0.0043 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1893 0.1762 0.2764 -0.0068 0.0236  -0.0051 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1996 0.1810 0.2980 -0.0099 0.0265  -0.0028 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1862 0.1721 0.2755 -0.0116 0.0380  -0.0052 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2088 0.1896 0.2874 -0.0157 0.0446  -0.0032 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2295 0.2074 0.2950 -0.0174 0.0414  0.0011  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2573 0.2309 0.3167 -0.0216 0.0443  0.0047  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2230 0.2033 0.2966 -0.0154 0.0480  -0.0051 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2517 0.2257 0.3101 -0.0209 0.0547  -0.0038 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2234 0.2069 0.3132 -0.0135 0.0517  -0.0081 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2128 0.1931 0.2751 -0.0142 0.0350  0.0014  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2156 0.1944 0.2686 -0.0153 0.0315  0.0061  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2003 0.1828 0.2566 -0.0107 0.0256  0.0048  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1963 0.1816 0.2540 -0.0082 0.0244  0.0011  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2312 0.2077 0.2690 -0.0194 0.0337  0.0081  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2486 0.2257 0.2779 -0.0205 0.0284  0.0133  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2701 0.2452 0.2948 -0.0240 0.0265  0.0200  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2446 0.2249 0.2700 -0.0185 0.0244  0.0130  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2690 0.2469 0.2893 -0.0238 0.0209  0.0241  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2566 0.2375 0.2767 -0.0207 0.0200  0.0195  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2428 0.2255 0.2693 -0.0152 0.0239  0.0085  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2445 0.2290 0.2613 -0.0198 0.0157  0.0210  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2429 0.2282 0.2643 -0.0146 0.0201  0.0098  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2386 0.2250 0.2559 -0.0168 0.0162  0.0157  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1936 0.1756 0.2511 -0.0099 0.0224  0.0083  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1950 0.1798 0.2551 -0.0061 0.0183  0.0070  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1977 0.1822 0.2562 -0.0064 0.0157  0.0131  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2079 0.1898 0.2673 -0.0087 0.0161  0.0184  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2028 0.1880 0.2733 -0.0034 0.0174  0.0022  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2020 0.1838 0.2811 -0.0044 0.0189  0.0034  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2394 0.2187 0.3226 -0.0034 0.0179  0.0078  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2897 0.2653 0.3771 -0.0052 0.0194  0.0117  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2058 0.1866 0.2896 -0.0008 0.0161  0.0076  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1859 0.1735 0.2438 -0.0039 0.0131  0.0129  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1874 0.1763 0.2473 -0.0037 0.0103  0.0192  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1771 0.1685 0.2439 0.0006  0.0094  0.0162  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1811 0.1753 0.2426 0.0012  0.0088  0.0135  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2157 0.2060 0.2639 -0.0080 0.0084  0.0243  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3103 0.3032 0.3614 -0.0087 0.0040  0.0326  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3393 0.3342 0.4024 -0.0045 0.0029  0.0333  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2843 0.2772 0.3255 -0.0140 0.0018  0.0386  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1712 0.1606 0.2500 0.0032  0.0103  0.0162  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1843 0.1747 0.2703 0.0068  0.0113  0.0125  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1834 0.1740 0.2691 0.0068  0.0113  0.0124  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1852 0.1805 0.2715 0.0076  0.0091  0.0171  36  SER   A C   
244  O O   . SER   A 30  ? 0.1998 0.1973 0.2858 0.0094  0.0103  0.0129  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2210 0.2071 0.3207 0.0089  0.0137  0.0125  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2183 0.2045 0.3174 0.0090  0.0139  0.0114  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2662 0.2521 0.3734 0.0120  0.0163  0.0084  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2584 0.2445 0.3661 0.0093  0.0124  0.0205  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1846 0.1819 0.2712 0.0055  0.0058  0.0261  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1925 0.1956 0.2812 0.0057  0.0028  0.0313  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2088 0.2148 0.2839 0.0035  0.0020  0.0280  37  SER   A C   
252  O O   . SER   A 31  ? 0.2270 0.2377 0.3046 0.0040  0.0006  0.0298  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2379 0.2430 0.3290 0.0028  -0.0022 0.0426  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3144 0.3186 0.3891 -0.0031 -0.0044 0.0449  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1778 0.1810 0.2407 0.0011  0.0032  0.0237  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1633 0.1680 0.2143 -0.0008 0.0032  0.0204  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1724 0.1759 0.2221 0.0020  0.0060  0.0122  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1630 0.1673 0.2045 0.0011  0.0062  0.0096  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1690 0.1708 0.2077 -0.0056 0.0035  0.0212  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1846 0.1873 0.2192 -0.0105 0.0001  0.0296  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1913 0.1898 0.2118 -0.0164 0.0018  0.0295  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1948 0.1929 0.2047 -0.0185 0.0037  0.0250  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2150 0.2098 0.2110 -0.0249 0.0053  0.0252  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2432 0.2354 0.2321 -0.0306 0.0047  0.0301  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1990 0.1925 0.1873 -0.0263 0.0077  0.0206  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1563 0.1574 0.2132 0.0046  0.0080  0.0083  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1561 0.1558 0.2104 0.0058  0.0095  0.0011  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1684 0.1670 0.2149 0.0039  0.0092  -0.0005 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1662 0.1653 0.2079 0.0043  0.0090  -0.0041 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1690 0.1709 0.2211 0.0071  0.0101  -0.0018 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1725 0.1726 0.2205 0.0074  0.0109  -0.0084 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1708 0.1681 0.2226 0.0075  0.0115  -0.0118 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1796 0.1810 0.2203 0.0071  0.0106  -0.0101 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1556 0.1525 0.2015 0.0018  0.0097  0.0023  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1575 0.1531 0.1990 0.0003  0.0111  0.0005  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1497 0.1431 0.1974 -0.0001 0.0125  -0.0008 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1656 0.1574 0.2178 -0.0008 0.0130  0.0018  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1686 0.1631 0.2015 -0.0033 0.0122  0.0038  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1764 0.1727 0.2017 -0.0042 0.0112  0.0045  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1922 0.1861 0.2077 -0.0093 0.0127  0.0071  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1814 0.1780 0.2057 -0.0021 0.0115  0.0002  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1436 0.1372 0.1926 0.0000  0.0133  -0.0039 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1448 0.1373 0.2011 -0.0008 0.0151  -0.0049 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1617 0.1543 0.2176 -0.0015 0.0176  -0.0058 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1650 0.1592 0.2185 -0.0002 0.0163  -0.0069 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1434 0.1369 0.2075 0.0005  0.0127  -0.0084 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1642 0.1573 0.2377 -0.0009 0.0141  -0.0094 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1667 0.1587 0.2461 -0.0009 0.0124  -0.0120 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1717 0.1680 0.2500 -0.0007 0.0132  -0.0112 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1591 0.1496 0.2175 -0.0038 0.0220  -0.0049 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1664 0.1563 0.2276 -0.0045 0.0264  -0.0061 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1707 0.1620 0.2452 -0.0045 0.0279  -0.0074 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1797 0.1695 0.2566 -0.0063 0.0292  -0.0065 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1888 0.1741 0.2400 -0.0084 0.0322  -0.0047 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2033 0.1867 0.2591 -0.0091 0.0389  -0.0069 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1886 0.1732 0.2273 -0.0092 0.0298  -0.0032 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1700 0.1645 0.2542 -0.0026 0.0272  -0.0088 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1619 0.1593 0.2614 -0.0027 0.0281  -0.0097 43  SER   A CA  
299  C C   . SER   A 37  ? 0.1886 0.1857 0.2963 -0.0026 0.0347  -0.0098 43  SER   A C   
300  O O   . SER   A 37  ? 0.1854 0.1804 0.2875 -0.0018 0.0370  -0.0098 43  SER   A O   
301  C CB  . SER   A 37  ? 0.1813 0.1841 0.2884 -0.0009 0.0201  -0.0106 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2109 0.2162 0.3168 0.0013  0.0162  -0.0101 43  SER   A OG  
303  N N   . SER   A 38  ? 0.1928 0.1919 0.3153 -0.0034 0.0383  -0.0102 44  SER   A N   
304  C CA  . SER   A 38  ? 0.2080 0.2070 0.3421 -0.0030 0.0459  -0.0107 44  SER   A CA  
305  C C   . SER   A 38  ? 0.2082 0.2141 0.3594 0.0007  0.0407  -0.0094 44  SER   A C   
306  O O   . SER   A 38  ? 0.2091 0.2207 0.3659 0.0015  0.0316  -0.0085 44  SER   A O   
307  C CB  . SER   A 38  ? 0.2397 0.2371 0.3821 -0.0061 0.0540  -0.0114 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2576 0.2605 0.4119 -0.0061 0.0482  -0.0110 44  SER   A OG  
309  N N   . THR   A 39  ? 0.2151 0.2201 0.3748 0.0025  0.0464  -0.0091 45  THR   A N   
310  C CA  . THR   A 39  ? 0.2420 0.2536 0.4198 0.0061  0.0412  -0.0063 45  THR   A CA  
311  C C   . THR   A 39  ? 0.2708 0.2838 0.4716 0.0070  0.0505  -0.0062 45  THR   A C   
312  O O   . THR   A 39  ? 0.2879 0.2944 0.4856 0.0047  0.0625  -0.0091 45  THR   A O   
313  C CB  . THR   A 39  ? 0.2613 0.2704 0.4305 0.0086  0.0388  -0.0049 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2873 0.2889 0.4541 0.0082  0.0505  -0.0069 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2628 0.2696 0.4094 0.0076  0.0323  -0.0055 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2919 0.3131 0.5155 0.0099  0.0451  -0.0025 46  THR   A N   
317  C CA  . THR   A 40  ? 0.3140 0.3376 0.5641 0.0116  0.0538  -0.0016 46  THR   A CA  
318  C C   . THR   A 40  ? 0.3327 0.3523 0.5884 0.0152  0.0594  -0.0005 46  THR   A C   
319  O O   . THR   A 40  ? 0.3597 0.3760 0.6302 0.0160  0.0721  -0.0021 46  THR   A O   
320  C CB  . THR   A 40  ? 0.3347 0.3706 0.6103 0.0126  0.0445  0.0027  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3580 0.3990 0.6309 0.0144  0.0303  0.0072  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3452 0.3840 0.6185 0.0085  0.0416  0.0007  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3138 0.3331 0.5587 0.0172  0.0507  0.0022  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3102 0.3251 0.5603 0.0206  0.0550  0.0039  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3190 0.3220 0.5428 0.0181  0.0632  -0.0012 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3226 0.3232 0.5225 0.0149  0.0597  -0.0036 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3100 0.3311 0.5630 0.0234  0.0406  0.0105  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3145 0.3102 0.5437 0.0195  0.0739  -0.0026 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3345 0.3186 0.5391 0.0163  0.0818  -0.0075 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3342 0.3180 0.5228 0.0174  0.0713  -0.0047 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3375 0.3257 0.5394 0.0217  0.0643  0.0008  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3813 0.3572 0.5994 0.0172  0.0972  -0.0103 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4795 0.4427 0.6740 0.0131  0.1058  -0.0156 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.5853 0.5414 0.7587 0.0057  0.1150  -0.0222 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6069 0.5663 0.7853 0.0039  0.1175  -0.0231 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6099 0.5561 0.7589 0.0007  0.1198  -0.0264 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3280 0.3073 0.4894 0.0134  0.0700  -0.0078 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3269 0.3066 0.4729 0.0140  0.0604  -0.0054 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3424 0.3149 0.4852 0.0148  0.0647  -0.0054 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3755 0.3396 0.5197 0.0131  0.0770  -0.0093 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3080 0.2825 0.4430 0.0163  0.0550  -0.0017 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.2967 0.2649 0.4284 0.0172  0.0571  -0.0006 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.2926 0.2530 0.3994 0.0122  0.0614  -0.0053 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.2806 0.2336 0.3851 0.0118  0.0664  -0.0060 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3127 0.2873 0.4483 0.0207  0.0446  0.0064  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3231 0.3043 0.4377 0.0183  0.0320  0.0068  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.2927 0.2547 0.3823 0.0082  0.0592  -0.0081 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.2882 0.2453 0.3550 0.0031  0.0603  -0.0110 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2889 0.2379 0.3442 -0.0033 0.0710  -0.0167 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3218 0.2701 0.3836 -0.0042 0.0769  -0.0187 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.2654 0.2299 0.3213 0.0026  0.0499  -0.0093 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3092 0.2797 0.3691 0.0066  0.0401  -0.0048 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.2512 0.2287 0.3144 0.0082  0.0329  -0.0031 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3389 0.3064 0.3977 0.0075  0.0397  -0.0030 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2879 0.2315 0.3242 -0.0086 0.0724  -0.0190 52  THR   A N   
356  C CA  . THR   A 46  ? 0.3309 0.2666 0.3496 -0.0168 0.0800  -0.0239 52  THR   A CA  
357  C C   . THR   A 46  ? 0.3066 0.2472 0.3075 -0.0207 0.0711  -0.0220 52  THR   A C   
358  O O   . THR   A 46  ? 0.2988 0.2438 0.2985 -0.0182 0.0636  -0.0190 52  THR   A O   
359  C CB  . THR   A 46  ? 0.4195 0.3444 0.4345 -0.0197 0.0886  -0.0275 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4829 0.4008 0.5107 -0.0190 0.1007  -0.0311 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.4475 0.3663 0.4382 -0.0293 0.0907  -0.0311 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2808 0.2207 0.2691 -0.0268 0.0722  -0.0231 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2569 0.2018 0.2317 -0.0303 0.0637  -0.0202 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2709 0.2095 0.2273 -0.0390 0.0665  -0.0225 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2883 0.2180 0.2360 -0.0456 0.0758  -0.0270 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2425 0.1911 0.2153 -0.0320 0.0615  -0.0183 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2607 0.2143 0.2515 -0.0248 0.0602  -0.0170 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2492 0.2040 0.2129 -0.0341 0.0520  -0.0139 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2589 0.2203 0.2593 -0.0177 0.0512  -0.0139 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2551 0.1980 0.2054 -0.0399 0.0591  -0.0199 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2664 0.2053 0.1998 -0.0488 0.0595  -0.0212 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2759 0.2158 0.1959 -0.0564 0.0573  -0.0195 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2602 0.2073 0.1847 -0.0536 0.0511  -0.0150 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2593 0.2051 0.1929 -0.0470 0.0510  -0.0178 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2922 0.2239 0.1950 -0.0669 0.0626  -0.0231 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.3016 0.2335 0.1879 -0.0764 0.0596  -0.0206 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3325 0.2634 0.2038 -0.0853 0.0560  -0.0207 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3541 0.2747 0.2113 -0.0941 0.0636  -0.0266 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3074 0.2292 0.1848 -0.0824 0.0706  -0.0255 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.3166 0.2393 0.2115 -0.0736 0.0754  -0.0262 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3285 0.2616 0.2324 -0.0681 0.0659  -0.0191 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.3109 0.2442 0.2312 -0.0608 0.0710  -0.0205 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3238 0.2652 0.2569 -0.0540 0.0646  -0.0160 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2866 0.2358 0.2188 -0.0529 0.0539  -0.0100 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.3269 0.2685 0.2750 -0.0484 0.0693  -0.0176 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3198 0.2614 0.1955 -0.0831 0.0447  -0.0144 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3224 0.2655 0.1895 -0.0897 0.0401  -0.0137 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3205 0.2774 0.1944 -0.0877 0.0272  -0.0050 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3132 0.2773 0.1991 -0.0804 0.0227  -0.0002 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3130 0.2521 0.1879 -0.0847 0.0452  -0.0184 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2947 0.2442 0.1930 -0.0697 0.0397  -0.0141 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3314 0.2916 0.1996 -0.0938 0.0220  -0.0034 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3275 0.3010 0.2052 -0.0918 0.0108  0.0045  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.3235 0.3007 0.2117 -0.0866 0.0103  0.0034  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3335 0.3197 0.2257 -0.0888 0.0028  0.0083  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3840 0.3611 0.2478 -0.1045 0.0028  0.0097  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.5080 0.4781 0.3547 -0.1163 0.0054  0.0047  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5141 0.4754 0.3601 -0.1143 0.0144  -0.0031 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.6015 0.5745 0.4354 -0.1280 -0.0017 0.0088  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3096 0.2804 0.2035 -0.0797 0.0180  -0.0022 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2848 0.2585 0.1879 -0.0748 0.0178  -0.0027 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2713 0.2577 0.1893 -0.0678 0.0104  0.0035  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2665 0.2571 0.1923 -0.0621 0.0082  0.0063  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2858 0.2513 0.1942 -0.0676 0.0260  -0.0078 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.3150 0.2645 0.2106 -0.0748 0.0369  -0.0158 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2476 0.2397 0.1703 -0.0683 0.0074  0.0052  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2382 0.2413 0.1761 -0.0617 0.0027  0.0097  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2183 0.2200 0.1613 -0.0569 0.0066  0.0071  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2104 0.2202 0.1638 -0.0536 0.0041  0.0099  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2783 0.2919 0.2197 -0.0674 -0.0052 0.0159  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3359 0.3538 0.2775 -0.0697 -0.0110 0.0213  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3872 0.4171 0.3363 -0.0745 -0.0197 0.0289  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4101 0.4410 0.3489 -0.0848 -0.0249 0.0319  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3526 0.3921 0.3205 -0.0676 -0.0216 0.0324  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2201 0.2111 0.1562 -0.0569 0.0131  0.0020  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2155 0.2039 0.1562 -0.0516 0.0167  0.0003  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2105 0.1904 0.1512 -0.0461 0.0217  -0.0028 60  THR   A C   
418  O O   . THR   A 54  ? 0.2293 0.2028 0.1646 -0.0485 0.0248  -0.0053 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2463 0.2307 0.1813 -0.0576 0.0190  -0.0014 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2886 0.2619 0.2127 -0.0633 0.0239  -0.0057 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2525 0.2462 0.1888 -0.0638 0.0136  0.0020  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2039 0.1842 0.1511 -0.0393 0.0226  -0.0024 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1922 0.1662 0.1423 -0.0339 0.0260  -0.0040 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1837 0.1594 0.1391 -0.0280 0.0251  -0.0023 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1944 0.1737 0.1494 -0.0290 0.0239  -0.0009 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1779 0.1505 0.1377 -0.0228 0.0259  -0.0023 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1780 0.1513 0.1410 -0.0181 0.0243  -0.0003 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1774 0.1547 0.1459 -0.0134 0.0214  0.0000  62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1891 0.1643 0.1611 -0.0122 0.0225  -0.0011 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2080 0.1725 0.1717 -0.0173 0.0277  0.0005  62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2291 0.1946 0.1951 -0.0131 0.0247  0.0040  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2277 0.1877 0.1857 -0.0227 0.0310  -0.0003 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1719 0.1543 0.1409 -0.0111 0.0184  0.0011  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1594 0.1446 0.1328 -0.0073 0.0156  0.0009  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1757 0.1600 0.1483 -0.0051 0.0133  0.0027  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1860 0.1690 0.1535 -0.0063 0.0136  0.0042  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1688 0.1607 0.1442 -0.0071 0.0141  -0.0003 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1657 0.1611 0.1389 -0.0072 0.0139  -0.0004 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1761 0.1731 0.1470 -0.0100 0.0157  0.0003  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1807 0.1777 0.1542 -0.0051 0.0126  -0.0016 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1802 0.1805 0.1504 -0.0102 0.0169  -0.0002 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1903 0.1896 0.1611 -0.0059 0.0141  -0.0027 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1969 0.1978 0.1664 -0.0082 0.0167  -0.0019 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.2159 0.2190 0.1838 -0.0092 0.0196  -0.0031 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1655 0.1507 0.1427 -0.0024 0.0105  0.0029  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1732 0.1583 0.1484 -0.0013 0.0068  0.0051  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1814 0.1707 0.1523 -0.0019 0.0051  0.0028  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1782 0.1704 0.1530 -0.0011 0.0049  0.0001  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1793 0.1636 0.1630 0.0012  0.0040  0.0071  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.1982 0.1832 0.1796 0.0014  -0.0015 0.0105  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2184 0.2000 0.1952 0.0005  -0.0025 0.0149  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2139 0.2026 0.1963 0.0015  -0.0060 0.0096  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2344 0.2166 0.2071 -0.0005 -0.0086 0.0191  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2296 0.2190 0.2072 0.0000  -0.0120 0.0129  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2535 0.2398 0.2260 -0.0010 -0.0135 0.0180  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.3101 0.2970 0.2765 -0.0033 -0.0203 0.0223  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1906 0.1794 0.1531 -0.0038 0.0046  0.0038  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1871 0.1783 0.1438 -0.0052 0.0047  0.0008  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.2040 0.1938 0.1543 -0.0065 -0.0004 0.0026  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2083 0.1955 0.1504 -0.0086 -0.0017 0.0060  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.2059 0.1973 0.1569 -0.0075 0.0091  0.0000  65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2169 0.2095 0.1599 -0.0100 0.0118  -0.0043 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.2050 0.1967 0.1585 -0.0060 -0.0036 0.0006  66  SER   A N   
464  C CA  . SER   A 60  ? 0.2221 0.2133 0.1700 -0.0082 -0.0098 0.0028  66  SER   A CA  
465  C C   . SER   A 60  ? 0.2232 0.2126 0.1555 -0.0129 -0.0093 0.0012  66  SER   A C   
466  O O   . SER   A 60  ? 0.2439 0.2318 0.1676 -0.0159 -0.0143 0.0056  66  SER   A O   
467  C CB  . SER   A 60  ? 0.2728 0.2666 0.2278 -0.0074 -0.0130 0.0004  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3627 0.3572 0.3167 -0.0081 -0.0090 -0.0059 66  SER   A OG  
469  N N   . SER   A 61  ? 0.2124 0.2020 0.1415 -0.0139 -0.0026 -0.0044 67  SER   A N   
470  C CA  . SER   A 61  ? 0.2288 0.2159 0.1427 -0.0190 0.0003  -0.0071 67  SER   A CA  
471  C C   . SER   A 61  ? 0.2335 0.2181 0.1387 -0.0210 0.0019  -0.0030 67  SER   A C   
472  O O   . SER   A 61  ? 0.2466 0.2286 0.1376 -0.0260 0.0046  -0.0047 67  SER   A O   
473  C CB  . SER   A 61  ? 0.2382 0.2259 0.1540 -0.0191 0.0082  -0.0145 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2250 0.2150 0.1502 -0.0160 0.0132  -0.0139 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.2240 0.2086 0.1365 -0.0180 0.0007  0.0022  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.2339 0.2154 0.1394 -0.0199 0.0014  0.0072  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2429 0.2224 0.1528 -0.0182 -0.0053 0.0150  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2553 0.2313 0.1611 -0.0193 -0.0051 0.0201  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2344 0.2169 0.1461 -0.0185 0.0084  0.0056  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.2454 0.2302 0.1555 -0.0201 0.0156  -0.0006 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.2603 0.2419 0.1551 -0.0254 0.0190  -0.0008 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.2612 0.2448 0.1569 -0.0267 0.0275  -0.0072 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.2721 0.2554 0.1641 -0.0283 0.0302  -0.0131 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.2681 0.2493 0.1536 -0.0295 0.0243  -0.0136 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.2763 0.2610 0.1719 -0.0291 0.0392  -0.0187 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2529 0.2345 0.1730 -0.0152 -0.0103 0.0159  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2818 0.2621 0.2116 -0.0124 -0.0152 0.0230  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2837 0.2606 0.2193 -0.0102 -0.0101 0.0248  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.3015 0.2745 0.2380 -0.0101 -0.0120 0.0314  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3212 0.2999 0.2427 -0.0156 -0.0230 0.0303  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.3749 0.3572 0.2956 -0.0172 -0.0299 0.0298  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.3885 0.3703 0.3049 -0.0201 -0.0397 0.0394  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.4079 0.3929 0.3171 -0.0246 -0.0467 0.0382  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.4285 0.4118 0.3173 -0.0321 -0.0506 0.0392  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.4528 0.4313 0.3272 -0.0354 -0.0477 0.0419  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.4234 0.4091 0.3048 -0.0370 -0.0565 0.0368  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2579 0.2360 0.1969 -0.0093 -0.0037 0.0193  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2605 0.2351 0.2023 -0.0090 0.0013  0.0202  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2403 0.2166 0.1908 -0.0072 0.0052  0.0157  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2238 0.2046 0.1759 -0.0067 0.0055  0.0114  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.3117 0.2859 0.2430 -0.0127 0.0055  0.0188  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.4251 0.3949 0.3459 -0.0158 0.0041  0.0244  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.4997 0.4697 0.4130 -0.0193 0.0103  0.0218  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5779 0.5424 0.4815 -0.0227 0.0107  0.0275  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6192 0.5831 0.5082 -0.0266 0.0081  0.0290  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2269 0.1993 0.1819 -0.0069 0.0085  0.0165  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2178 0.1910 0.1774 -0.0072 0.0125  0.0124  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2282 0.2023 0.1822 -0.0107 0.0162  0.0108  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2393 0.2100 0.1884 -0.0128 0.0176  0.0133  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2090 0.1763 0.1759 -0.0061 0.0150  0.0134  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2180 0.1849 0.1940 -0.0024 0.0124  0.0152  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2472 0.2160 0.2299 -0.0010 0.0134  0.0120  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2224 0.1877 0.2028 -0.0002 0.0085  0.0205  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2297 0.1984 0.2218 0.0022  0.0107  0.0150  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2684 0.2353 0.2600 0.0028  0.0072  0.0205  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1947 0.1735 0.1505 -0.0118 0.0176  0.0073  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1959 0.1774 0.1495 -0.0153 0.0203  0.0062  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2030 0.1851 0.1598 -0.0176 0.0216  0.0044  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1928 0.1768 0.1532 -0.0163 0.0204  0.0030  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2044 0.1931 0.1586 -0.0150 0.0202  0.0044  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2202 0.2082 0.1680 -0.0149 0.0202  0.0051  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2447 0.2306 0.1862 -0.0178 0.0227  0.0068  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2251 0.2143 0.1720 -0.0128 0.0179  0.0038  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2627 0.2474 0.1958 -0.0188 0.0231  0.0074  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2367 0.2246 0.1749 -0.0141 0.0179  0.0040  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2710 0.2567 0.2018 -0.0173 0.0206  0.0058  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.3064 0.2903 0.2262 -0.0197 0.0209  0.0059  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.1979 0.1785 0.1523 -0.0219 0.0240  0.0045  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2075 0.1891 0.1625 -0.0259 0.0244  0.0029  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2179 0.2094 0.1772 -0.0267 0.0222  0.0030  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2493 0.2456 0.2106 -0.0262 0.0226  0.0038  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2274 0.2038 0.1781 -0.0307 0.0274  0.0031  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2342 0.2117 0.1837 -0.0296 0.0281  0.0054  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2112 0.1886 0.1613 -0.0241 0.0261  0.0064  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1923 0.1865 0.1534 -0.0283 0.0203  0.0026  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2004 0.2042 0.1683 -0.0288 0.0175  0.0040  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1867 0.1927 0.1534 -0.0345 0.0150  0.0050  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2044 0.2040 0.1643 -0.0373 0.0158  0.0035  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2231 0.2301 0.1967 -0.0234 0.0159  0.0039  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2453 0.2530 0.2205 -0.0192 0.0176  0.0030  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2299 0.2312 0.2005 -0.0220 0.0157  0.0026  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1960 0.2112 0.1697 -0.0368 0.0122  0.0078  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1940 0.2139 0.1683 -0.0422 0.0076  0.0105  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1847 0.2108 0.1688 -0.0375 0.0047  0.0131  75  SER   A C   
545  O O   . SER   A 69  ? 0.1977 0.2290 0.1921 -0.0327 0.0057  0.0138  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2362 0.2639 0.2157 -0.0475 0.0053  0.0134  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3292 0.3501 0.2990 -0.0526 0.0081  0.0108  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1682 0.1927 0.1488 -0.0390 0.0021  0.0141  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1714 0.2003 0.1613 -0.0344 -0.0002 0.0167  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1763 0.2104 0.1677 -0.0395 -0.0063 0.0222  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1941 0.2258 0.1745 -0.0473 -0.0085 0.0228  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1759 0.1972 0.1616 -0.0295 0.0029  0.0130  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1804 0.1928 0.1535 -0.0332 0.0049  0.0102  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.2020 0.2070 0.1682 -0.0335 0.0093  0.0063  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1901 0.2009 0.1589 -0.0364 0.0031  0.0117  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2104 0.2067 0.1676 -0.0364 0.0126  0.0034  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2060 0.2079 0.1635 -0.0401 0.0068  0.0083  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2105 0.2052 0.1631 -0.0399 0.0119  0.0039  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1645 0.2057 0.1701 -0.0355 -0.0092 0.0267  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1802 0.2270 0.1892 -0.0398 -0.0161 0.0337  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1933 0.2332 0.1907 -0.0419 -0.0167 0.0335  77  SER   A C   
562  O O   . SER   A 71  ? 0.1956 0.2277 0.1873 -0.0382 -0.0115 0.0280  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1925 0.2484 0.2225 -0.0344 -0.0183 0.0391  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2109 0.2627 0.2458 -0.0267 -0.0139 0.0357  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1917 0.2343 0.1845 -0.0492 -0.0231 0.0395  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2189 0.2549 0.2002 -0.0521 -0.0232 0.0398  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2236 0.2601 0.2170 -0.0442 -0.0224 0.0415  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2217 0.2652 0.2327 -0.0387 -0.0241 0.0450  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2470 0.2864 0.2200 -0.0625 -0.0311 0.0471  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.2769 0.3127 0.2331 -0.0721 -0.0307 0.0436  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3753 0.4136 0.3197 -0.0842 -0.0390 0.0505  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4683 0.5005 0.3939 -0.0943 -0.0368 0.0449  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.5302 0.5658 0.4434 -0.1076 -0.0458 0.0514  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2239 0.2526 0.2090 -0.0438 -0.0190 0.0387  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2195 0.2481 0.2161 -0.0368 -0.0181 0.0399  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2265 0.2628 0.2363 -0.0368 -0.0250 0.0497  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2390 0.2776 0.2424 -0.0442 -0.0312 0.0566  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2427 0.2623 0.2262 -0.0394 -0.0145 0.0369  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2716 0.2851 0.2389 -0.0450 -0.0105 0.0310  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2309 0.2503 0.1967 -0.0500 -0.0152 0.0340  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2059 0.2460 0.2345 -0.0287 -0.0238 0.0504  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2218 0.2694 0.2674 -0.0275 -0.0296 0.0600  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2039 0.2505 0.2668 -0.0187 -0.0257 0.0589  80  SER   A C   
584  O O   . SER   A 74  ? 0.1947 0.2352 0.2548 -0.0143 -0.0192 0.0505  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2756 0.3330 0.3306 -0.0295 -0.0340 0.0645  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3601 0.4192 0.4269 -0.0227 -0.0280 0.0588  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1890 0.2413 0.2700 -0.0169 -0.0302 0.0682  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2061 0.2570 0.3056 -0.0090 -0.0261 0.0677  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2110 0.2673 0.3280 -0.0036 -0.0221 0.0651  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2246 0.2899 0.3546 -0.0048 -0.0267 0.0726  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2234 0.2774 0.3347 -0.0101 -0.0329 0.0800  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2703 0.3201 0.3972 -0.0038 -0.0294 0.0809  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2801 0.3196 0.3925 -0.0036 -0.0243 0.0731  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2938 0.3481 0.4347 -0.0052 -0.0372 0.0953  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2108 0.2619 0.3282 0.0015  -0.0137 0.0549  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2244 0.2787 0.3537 0.0056  -0.0079 0.0502  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2348 0.2841 0.3773 0.0120  -0.0006 0.0454  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2243 0.2656 0.3574 0.0128  0.0022  0.0397  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2557 0.3072 0.3662 0.0034  -0.0047 0.0416  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2756 0.3314 0.3746 -0.0034 -0.0111 0.0460  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2728 0.3252 0.3913 0.0071  0.0028  0.0352  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2976 0.3499 0.3795 -0.0059 -0.0085 0.0392  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2262 0.2801 0.3912 0.0161  0.0033  0.0472  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2372 0.2852 0.4151 0.0216  0.0117  0.0415  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2581 0.2994 0.4209 0.0218  0.0196  0.0285  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.2729 0.3169 0.4282 0.0201  0.0214  0.0249  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2339 0.2883 0.4410 0.0258  0.0153  0.0463  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2696 0.3169 0.4912 0.0311  0.0255  0.0398  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.2969 0.3392 0.5289 0.0336  0.0250  0.0434  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.2900 0.3340 0.5118 0.0327  0.0363  0.0292  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.3119 0.3462 0.5564 0.0378  0.0353  0.0365  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.3048 0.3410 0.5383 0.0364  0.0466  0.0223  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3063 0.3376 0.5516 0.0390  0.0462  0.0257  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.2492 0.2814 0.4065 0.0232  0.0236  0.0219  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.2449 0.2705 0.3877 0.0226  0.0298  0.0104  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.2570 0.2762 0.4122 0.0258  0.0386  0.0042  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.2743 0.2895 0.4388 0.0276  0.0384  0.0063  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.2474 0.2682 0.3690 0.0195  0.0254  0.0076  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.2685 0.2829 0.3766 0.0186  0.0306  -0.0031 84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.2493 0.2749 0.3584 0.0160  0.0185  0.0124  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.2664 0.2834 0.4205 0.0259  0.0470  -0.0039 85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.2748 0.2845 0.4392 0.0280  0.0575  -0.0116 85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.2820 0.2822 0.4340 0.0262  0.0580  -0.0185 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.2786 0.2781 0.4112 0.0231  0.0517  -0.0194 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.3284 0.3371 0.4872 0.0265  0.0665  -0.0199 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.4810 0.4819 0.6507 0.0278  0.0795  -0.0288 85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.6258 0.6289 0.8277 0.0332  0.0845  -0.0235 85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.6593 0.6687 0.8772 0.0352  0.0893  -0.0210 85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.6745 0.6729 0.8871 0.0355  0.0840  -0.0216 85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.2851 0.2780 0.4499 0.0281  0.0657  -0.0231 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.2934 0.2770 0.4480 0.0258  0.0667  -0.0302 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.3042 0.2840 0.4339 0.0206  0.0680  -0.0400 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.3171 0.2974 0.4417 0.0192  0.0737  -0.0447 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.2935 0.2690 0.4662 0.0281  0.0768  -0.0349 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.2975 0.2740 0.4124 0.0174  0.0625  -0.0425 87  SER   A N   
636  C CA  . SER   A 81  ? 0.2925 0.2656 0.3846 0.0120  0.0618  -0.0504 87  SER   A CA  
637  C C   . SER   A 81  ? 0.3073 0.2725 0.3960 0.0091  0.0621  -0.0564 87  SER   A C   
638  O O   . SER   A 81  ? 0.3067 0.2686 0.4110 0.0117  0.0644  -0.0549 87  SER   A O   
639  C CB  . SER   A 81  ? 0.3071 0.2870 0.3855 0.0108  0.0519  -0.0446 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.3036 0.2846 0.3838 0.0115  0.0447  -0.0396 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.3189 0.2811 0.3880 0.0035  0.0595  -0.0627 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.3463 0.3022 0.4119 -0.0001 0.0583  -0.0679 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.3379 0.2979 0.4099 0.0020  0.0499  -0.0602 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.3557 0.3110 0.4316 0.0004  0.0496  -0.0626 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.4337 0.3872 0.4766 -0.0075 0.0554  -0.0749 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.5597 0.5126 0.5893 -0.0103 0.0600  -0.0792 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.6972 0.6585 0.7189 -0.0090 0.0531  -0.0719 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.7471 0.7099 0.7527 -0.0132 0.0458  -0.0717 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.7108 0.6772 0.7430 -0.0039 0.0547  -0.0661 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.3177 0.2858 0.3903 0.0051  0.0438  -0.0513 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.3072 0.2787 0.3829 0.0062  0.0368  -0.0445 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.2858 0.2585 0.3782 0.0105  0.0374  -0.0369 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.2919 0.2643 0.3881 0.0105  0.0340  -0.0331 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.3052 0.2835 0.3698 0.0058  0.0301  -0.0400 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.3244 0.3022 0.3727 0.0015  0.0279  -0.0453 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.3454 0.3243 0.3848 0.0006  0.0300  -0.0471 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.3384 0.3153 0.3809 -0.0021 0.0232  -0.0477 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.3690 0.3473 0.3924 -0.0038 0.0272  -0.0508 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.3604 0.3377 0.3886 -0.0064 0.0197  -0.0512 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.3880 0.3655 0.4059 -0.0075 0.0217  -0.0526 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.4271 0.4047 0.4297 -0.0123 0.0173  -0.0547 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.2644 0.2390 0.3669 0.0139  0.0412  -0.0337 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.2566 0.2335 0.3756 0.0176  0.0403  -0.0245 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.2846 0.2598 0.4209 0.0211  0.0475  -0.0245 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.2890 0.2648 0.4235 0.0211  0.0525  -0.0292 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.2359 0.2211 0.3509 0.0183  0.0338  -0.0158 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.2178 0.2053 0.3184 0.0155  0.0274  -0.0143 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.2224 0.2086 0.3247 0.0147  0.0243  -0.0103 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.2185 0.2092 0.3051 0.0137  0.0251  -0.0164 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.2066 0.1945 0.2976 0.0123  0.0200  -0.0093 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.2041 0.1965 0.2803 0.0117  0.0202  -0.0148 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.2029 0.1941 0.2818 0.0111  0.0180  -0.0114 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.1864 0.1788 0.2570 0.0091  0.0147  -0.0105 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.2951 0.2691 0.4496 0.0241  0.0480  -0.0178 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.2946 0.2690 0.4700 0.0284  0.0541  -0.0151 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.2927 0.2775 0.4696 0.0297  0.0497  -0.0074 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.3006 0.2912 0.4637 0.0275  0.0417  -0.0029 91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.3049 0.2763 0.4982 0.0310  0.0530  -0.0073 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.3276 0.3021 0.5078 0.0282  0.0435  -0.0012 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.3126 0.2856 0.4703 0.0239  0.0427  -0.0109 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.2873 0.2747 0.4826 0.0332  0.0551  -0.0054 92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.2845 0.2824 0.4857 0.0344  0.0508  0.0030  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2811 0.2845 0.4859 0.0342  0.0400  0.0164  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.2808 0.2803 0.4976 0.0359  0.0394  0.0212  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.2910 0.2903 0.5177 0.0388  0.0591  0.0038  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2715 0.2822 0.4621 0.0311  0.0319  0.0213  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2574 0.2716 0.4458 0.0291  0.0223  0.0324  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2487 0.2716 0.4255 0.0256  0.0152  0.0374  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2631 0.2885 0.4329 0.0249  0.0178  0.0318  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.2707 0.2776 0.4429 0.0264  0.0210  0.0284  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.2923 0.2993 0.4403 0.0228  0.0199  0.0209  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.2676 0.2674 0.4035 0.0212  0.0217  0.0130  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.2566 0.2578 0.3733 0.0174  0.0171  0.0123  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.2389 0.2422 0.3429 0.0160  0.0170  0.0077  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2359 0.2393 0.3253 0.0131  0.0138  0.0072  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.2429 0.2480 0.3494 0.0174  0.0207  0.0039  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2370 0.2634 0.4104 0.0225  0.0067  0.0475  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2400 0.2727 0.3987 0.0176  0.0003  0.0509  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2307 0.2577 0.3653 0.0138  -0.0003 0.0450  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2535 0.2754 0.3840 0.0128  -0.0013 0.0463  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2605 0.2997 0.4256 0.0147  -0.0089 0.0649  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2744 0.3215 0.4655 0.0181  -0.0096 0.0723  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2912 0.3366 0.5061 0.0231  -0.0074 0.0773  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2775 0.3332 0.4713 0.0168  -0.0115 0.0737  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.3044 0.3571 0.5470 0.0272  -0.0069 0.0840  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2973 0.3613 0.5184 0.0203  -0.0117 0.0808  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3130 0.3756 0.5591 0.0257  -0.0092 0.0859  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3562 0.4269 0.6328 0.0298  -0.0086 0.0932  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1963 0.2241 0.3163 0.0119  0.0008  0.0387  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1792 0.2025 0.2788 0.0085  0.0003  0.0338  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1745 0.2015 0.2628 0.0028  -0.0059 0.0401  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1960 0.2293 0.2860 0.0012  -0.0084 0.0432  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1897 0.2109 0.2800 0.0094  0.0049  0.0239  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1872 0.2044 0.2593 0.0063  0.0041  0.0200  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2003 0.2141 0.2656 0.0077  0.0080  0.0111  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2068 0.2182 0.2782 0.0104  0.0116  0.0063  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1679 0.1810 0.2202 0.0054  0.0072  0.0088  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1670 0.1902 0.2446 -0.0010 -0.0080 0.0423  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1614 0.1864 0.2259 -0.0077 -0.0130 0.0476  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1849 0.2065 0.2315 -0.0107 -0.0103 0.0402  96  SER   A C   
721  O O   . SER   A 90  ? 0.1810 0.1985 0.2254 -0.0075 -0.0054 0.0322  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1959 0.2177 0.2573 -0.0112 -0.0158 0.0540  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2119 0.2265 0.2677 -0.0100 -0.0108 0.0476  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1736 0.1967 0.2079 -0.0173 -0.0136 0.0432  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1896 0.2084 0.2074 -0.0210 -0.0107 0.0371  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1843 0.2040 0.2047 -0.0166 -0.0071 0.0304  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1831 0.1979 0.1948 -0.0166 -0.0032 0.0242  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2140 0.2253 0.2234 -0.0220 -0.0066 0.0334  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2391 0.2486 0.2426 -0.0277 -0.0093 0.0399  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2657 0.2719 0.2518 -0.0362 -0.0095 0.0408  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2259 0.2356 0.2378 -0.0265 -0.0115 0.0457  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2718 0.2767 0.2551 -0.0403 -0.0122 0.0474  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2543 0.2614 0.2534 -0.0344 -0.0138 0.0511  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1647 0.1905 0.1969 -0.0136 -0.0085 0.0322  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1766 0.2030 0.2106 -0.0101 -0.0048 0.0263  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1739 0.2044 0.2035 -0.0141 -0.0067 0.0278  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1814 0.2178 0.2154 -0.0175 -0.0115 0.0345  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1774 0.2069 0.2282 -0.0042 -0.0030 0.0262  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1992 0.2283 0.2508 -0.0010 0.0018  0.0195  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1875 0.2098 0.2287 0.0002  0.0048  0.0125  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2195 0.2506 0.2880 0.0039  0.0050  0.0190  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1712 0.1986 0.1924 -0.0141 -0.0033 0.0221  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1698 0.1999 0.1861 -0.0181 -0.0041 0.0225  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1667 0.1986 0.1888 -0.0141 -0.0006 0.0190  99  MET   A C   
745  O O   . MET   A 93  ? 0.1800 0.2073 0.1993 -0.0106 0.0031  0.0140  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1858 0.2088 0.1862 -0.0222 -0.0022 0.0189  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2100 0.2299 0.2022 -0.0273 -0.0042 0.0213  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2504 0.2602 0.2260 -0.0316 0.0007  0.0157  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2702 0.2756 0.2511 -0.0237 0.0055  0.0104  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1574 0.1963 0.1879 -0.0151 -0.0016 0.0220  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1698 0.2101 0.2052 -0.0119 0.0030  0.0184  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1652 0.2047 0.1914 -0.0158 0.0040  0.0169  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1669 0.2085 0.1891 -0.0213 0.0005  0.0200  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1939 0.2427 0.2484 -0.0096 0.0033  0.0221  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2535 0.3027 0.3206 -0.0050 0.0038  0.0234  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2628 0.3200 0.3517 -0.0022 0.0057  0.0268  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2711 0.3126 0.3326 -0.0011 0.0087  0.0164  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1580 0.1947 0.1814 -0.0135 0.0087  0.0124  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1530 0.1888 0.1695 -0.0167 0.0105  0.0113  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1605 0.1972 0.1807 -0.0140 0.0158  0.0084  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1653 0.2011 0.1898 -0.0100 0.0185  0.0060  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1773 0.2041 0.1788 -0.0180 0.0111  0.0084  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1509 0.1891 0.1692 -0.0171 0.0178  0.0085  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1632 0.2007 0.1813 -0.0158 0.0237  0.0056  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1854 0.2137 0.1876 -0.0156 0.0250  0.0025  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.2139 0.2378 0.2070 -0.0183 0.0233  0.0033  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1786 0.2220 0.2026 -0.0195 0.0256  0.0076  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1859 0.2275 0.2077 -0.0188 0.0329  0.0042  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1875 0.2413 0.2299 -0.0195 0.0232  0.0119  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1832 0.2084 0.1828 -0.0127 0.0278  -0.0008 103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.2149 0.2324 0.2008 -0.0125 0.0277  -0.0026 103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.2149 0.2302 0.1986 -0.0103 0.0299  -0.0063 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2174 0.2359 0.2107 -0.0083 0.0319  -0.0081 103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2225 0.2319 0.1935 -0.0113 0.0298  -0.0075 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.2219 0.2285 0.1879 -0.0108 0.0313  -0.0113 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.2179 0.2232 0.1860 -0.0083 0.0268  -0.0120 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2246 0.2279 0.1905 -0.0077 0.0220  -0.0093 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2350 0.2362 0.1854 -0.0138 0.0315  -0.0111 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2277 0.2257 0.1700 -0.0151 0.0327  -0.0153 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2430 0.2417 0.1873 -0.0161 0.0400  -0.0203 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2280 0.2223 0.1618 -0.0157 0.0276  -0.0153 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.2477 0.2421 0.1822 -0.0180 0.0394  -0.0240 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2391 0.2313 0.1673 -0.0179 0.0313  -0.0208 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.2218 0.2272 0.1937 -0.0072 0.0289  -0.0159 105 SER   A N   
785  C CA  . SER   A 99  ? 0.2317 0.2357 0.2057 -0.0053 0.0252  -0.0171 105 SER   A CA  
786  C C   . SER   A 99  ? 0.2706 0.2724 0.2434 -0.0060 0.0293  -0.0229 105 SER   A C   
787  O O   . SER   A 99  ? 0.3052 0.3087 0.2854 -0.0056 0.0356  -0.0254 105 SER   A O   
788  C CB  . SER   A 99  ? 0.2586 0.2663 0.2458 -0.0025 0.0236  -0.0147 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.3483 0.3547 0.3388 -0.0009 0.0207  -0.0158 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.2348 0.2327 0.1987 -0.0076 0.0262  -0.0250 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.2655 0.2601 0.2267 -0.0094 0.0302  -0.0313 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.3232 0.3164 0.2855 -0.0090 0.0247  -0.0321 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.3328 0.3277 0.2974 -0.0074 0.0183  -0.0277 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.3189 0.3094 0.2632 -0.0148 0.0335  -0.0344 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.3347 0.3233 0.2654 -0.0175 0.0257  -0.0306 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.3367 0.3210 0.2488 -0.0236 0.0281  -0.0324 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.3728 0.3532 0.2738 -0.0281 0.0273  -0.0366 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.3046 0.2891 0.2121 -0.0247 0.0304  -0.0294 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.3556 0.3456 0.3186 -0.0103 0.0281  -0.0382 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.3763 0.3650 0.3400 -0.0108 0.0229  -0.0394 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.3652 0.3538 0.3176 -0.0136 0.0148  -0.0361 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.3948 0.3810 0.3323 -0.0182 0.0142  -0.0367 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.3983 0.3816 0.3579 -0.0143 0.0288  -0.0476 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.3960 0.3796 0.3640 -0.0122 0.0381  -0.0497 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.3565 0.3434 0.3195 -0.0120 0.0374  -0.0447 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.3222 0.3134 0.2827 -0.0110 0.0089  -0.0322 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2988 0.2913 0.2553 -0.0121 0.0009  -0.0275 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.2652 0.2603 0.2286 -0.0082 -0.0005 -0.0212 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.2661 0.2626 0.2330 -0.0073 -0.0059 -0.0171 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.2271 0.2230 0.1931 -0.0062 0.0047  -0.0206 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.2012 0.1986 0.1718 -0.0037 0.0038  -0.0155 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1878 0.1868 0.1700 -0.0008 0.0037  -0.0144 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1804 0.1797 0.1655 0.0004  0.0032  -0.0109 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.1992 0.1972 0.1677 -0.0039 0.0086  -0.0149 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.2156 0.2113 0.1714 -0.0070 0.0085  -0.0142 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.2086 0.2043 0.1606 -0.0085 0.0137  -0.0161 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.2356 0.2298 0.1860 -0.0082 0.0034  -0.0114 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1826 0.1820 0.1710 -0.0002 0.0046  -0.0174 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1791 0.1796 0.1776 0.0020  0.0046  -0.0159 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1696 0.1700 0.1703 0.0024  0.0011  -0.0132 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.1949 0.1951 0.1933 0.0013  -0.0026 -0.0133 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1873 0.1873 0.1924 0.0024  0.0061  -0.0191 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.2340 0.2347 0.2441 0.0035  0.0115  -0.0203 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1702 0.1707 0.1754 0.0035  0.0024  -0.0107 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1654 0.1652 0.1748 0.0041  0.0010  -0.0087 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.1807 0.1789 0.1867 0.0041  0.0015  -0.0059 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1912 0.1880 0.2023 0.0048  0.0024  -0.0043 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1653 0.1631 0.1635 0.0031  0.0019  -0.0056 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1583 0.1537 0.1533 0.0028  0.0030  -0.0030 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1645 0.1582 0.1613 0.0022  0.0069  -0.0029 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1731 0.1685 0.1694 0.0012  0.0083  -0.0038 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1684 0.1586 0.1671 0.0023  0.0087  -0.0014 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1638 0.1508 0.1619 0.0004  0.0132  -0.0021 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1747 0.1602 0.1650 -0.0025 0.0151  -0.0019 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1872 0.1712 0.1745 -0.0025 0.0147  -0.0006 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1840 0.1669 0.1894 0.0015  0.0161  -0.0016 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.1979 0.1833 0.2121 0.0032  0.0152  -0.0023 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2082 0.1854 0.2103 -0.0015 0.0223  -0.0031 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2286 0.2111 0.2543 0.0050  0.0184  -0.0016 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1619 0.1477 0.1489 -0.0056 0.0169  -0.0027 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1664 0.1509 0.1464 -0.0098 0.0186  -0.0026 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1816 0.1593 0.1592 -0.0129 0.0235  -0.0042 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1833 0.1602 0.1624 -0.0136 0.0250  -0.0051 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1718 0.1618 0.1505 -0.0121 0.0163  -0.0016 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1920 0.1818 0.1641 -0.0177 0.0169  -0.0009 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1995 0.1894 0.1696 -0.0180 0.0172  -0.0006 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.2044 0.2009 0.1785 -0.0196 0.0134  0.0016  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1910 0.1632 0.1652 -0.0148 0.0267  -0.0047 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2090 0.1731 0.1806 -0.0182 0.0330  -0.0073 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2103 0.1713 0.1719 -0.0246 0.0348  -0.0084 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2224 0.1853 0.1824 -0.0248 0.0326  -0.0069 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2443 0.2028 0.2241 -0.0142 0.0363  -0.0070 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.2878 0.2478 0.2792 -0.0092 0.0360  -0.0063 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3246 0.2798 0.3272 -0.0052 0.0386  -0.0046 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.3278 0.2839 0.3431 -0.0019 0.0402  -0.0047 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.3560 0.3061 0.3764 -0.0030 0.0485  -0.0077 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.3349 0.2768 0.3466 -0.0082 0.0559  -0.0116 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.3943 0.3463 0.4280 0.0001  0.0498  -0.0074 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2106 0.1659 0.1653 -0.0305 0.0395  -0.0114 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2346 0.1846 0.1791 -0.0378 0.0424  -0.0136 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2480 0.1859 0.1929 -0.0391 0.0518  -0.0178 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2543 0.1897 0.2096 -0.0335 0.0551  -0.0180 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2572 0.2101 0.1911 -0.0455 0.0399  -0.0136 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2531 0.1999 0.1816 -0.0493 0.0454  -0.0169 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.2773 0.2073 0.2122 -0.0468 0.0567  -0.0214 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.3032 0.2202 0.2392 -0.0483 0.0673  -0.0262 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.3124 0.2249 0.2484 -0.0494 0.0738  -0.0298 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.3353 0.2381 0.2779 -0.0482 0.0835  -0.0334 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.3411 0.2497 0.2641 -0.0579 0.0717  -0.0304 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.4263 0.3354 0.3323 -0.0685 0.0706  -0.0329 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.5614 0.4647 0.4537 -0.0790 0.0723  -0.0362 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.6139 0.5255 0.5005 -0.0833 0.0639  -0.0330 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.5652 0.4542 0.4532 -0.0836 0.0833  -0.0428 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.2971 0.2164 0.2277 -0.0514 0.0692  -0.0285 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.2868 0.2019 0.2155 -0.0537 0.0754  -0.0316 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.2768 0.1975 0.2216 -0.0446 0.0741  -0.0289 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.2850 0.2014 0.2320 -0.0453 0.0810  -0.0318 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.2906 0.2085 0.2024 -0.0627 0.0718  -0.0314 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.3290 0.2426 0.2240 -0.0732 0.0716  -0.0337 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.3251 0.2479 0.2156 -0.0756 0.0613  -0.0290 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.3739 0.2748 0.2565 -0.0822 0.0811  -0.0404 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.3716 0.2880 0.2476 -0.0859 0.0636  -0.0324 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.3821 0.2848 0.2520 -0.0904 0.0756  -0.0397 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2497 0.1794 0.2051 -0.0368 0.0657  -0.0238 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2298 0.1653 0.1996 -0.0291 0.0631  -0.0212 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2110 0.1578 0.1821 -0.0256 0.0524  -0.0165 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2206 0.1713 0.1852 -0.0272 0.0470  -0.0146 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2089 0.1606 0.1889 -0.0213 0.0501  -0.0150 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2030 0.1642 0.1856 -0.0178 0.0413  -0.0114 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1944 0.1591 0.1668 -0.0227 0.0379  -0.0103 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2145 0.1762 0.1811 -0.0273 0.0411  -0.0115 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2075 0.1722 0.2030 -0.0125 0.0402  -0.0106 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2087 0.1816 0.2054 -0.0101 0.0323  -0.0081 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2283 0.1918 0.2360 -0.0073 0.0410  -0.0098 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1964 0.1672 0.1669 -0.0221 0.0315  -0.0077 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1963 0.1717 0.1606 -0.0261 0.0272  -0.0052 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1953 0.1773 0.1680 -0.0215 0.0224  -0.0026 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1927 0.1768 0.1638 -0.0239 0.0204  -0.0002 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2051 0.1834 0.1652 -0.0282 0.0239  -0.0037 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2149 0.2004 0.1736 -0.0310 0.0181  0.0003  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2159 0.1870 0.1667 -0.0340 0.0287  -0.0065 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1719 0.1568 0.1531 -0.0155 0.0205  -0.0028 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1837 0.1739 0.1722 -0.0118 0.0167  -0.0013 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1656 0.1578 0.1599 -0.0068 0.0150  -0.0024 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1738 0.1633 0.1674 -0.0058 0.0163  -0.0033 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1515 0.1475 0.1513 -0.0041 0.0123  -0.0022 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1559 0.1532 0.1587 -0.0008 0.0106  -0.0037 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1563 0.1572 0.1597 -0.0001 0.0092  -0.0037 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1506 0.1539 0.1574 -0.0005 0.0089  -0.0023 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1747 0.1717 0.1842 0.0013  0.0098  -0.0050 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1971 0.1951 0.2109 0.0009  0.0099  -0.0046 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2116 0.2056 0.2235 0.0014  0.0116  -0.0050 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2182 0.2163 0.2395 0.0027  0.0089  -0.0063 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1471 0.1484 0.1480 0.0010  0.0086  -0.0051 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1411 0.1452 0.1431 0.0015  0.0090  -0.0062 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1447 0.1495 0.1538 0.0031  0.0090  -0.0077 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1508 0.1539 0.1611 0.0037  0.0077  -0.0093 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1554 0.1584 0.1513 0.0015  0.0089  -0.0079 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1689 0.1737 0.1656 0.0016  0.0111  -0.0104 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1686 0.1703 0.1584 0.0000  0.0093  -0.0059 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1488 0.1561 0.1636 0.0036  0.0103  -0.0070 125 SER   A N   
922  C CA  . SER   A 119 ? 0.1549 0.1621 0.1779 0.0051  0.0111  -0.0081 125 SER   A CA  
923  C C   . SER   A 119 ? 0.1791 0.1876 0.2074 0.0062  0.0143  -0.0102 125 SER   A C   
924  O O   . SER   A 119 ? 0.1840 0.1905 0.2175 0.0073  0.0163  -0.0132 125 SER   A O   
925  C CB  . SER   A 119 ? 0.1589 0.1671 0.1874 0.0047  0.0097  -0.0037 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1733 0.1810 0.2113 0.0064  0.0105  -0.0038 125 SER   A OG  
927  N N   . THR   A 120 ? 0.1807 0.1924 0.2090 0.0057  0.0157  -0.0085 126 THR   A N   
928  C CA  . THR   A 120 ? 0.1920 0.2052 0.2276 0.0068  0.0203  -0.0106 126 THR   A CA  
929  C C   . THR   A 120 ? 0.2021 0.2162 0.2300 0.0051  0.0226  -0.0120 126 THR   A C   
930  O O   . THR   A 120 ? 0.1983 0.2125 0.2175 0.0034  0.0199  -0.0101 126 THR   A O   
931  C CB  . THR   A 120 ? 0.2215 0.2395 0.2722 0.0083  0.0203  -0.0054 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.2476 0.2705 0.2973 0.0064  0.0180  -0.0008 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.2366 0.2538 0.2938 0.0093  0.0174  -0.0021 126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.2192 0.2335 0.2510 0.0055  0.0283  -0.0153 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.2497 0.2647 0.2743 0.0034  0.0312  -0.0166 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.2516 0.2674 0.2841 0.0039  0.0391  -0.0201 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.2529 0.2698 0.2998 0.0064  0.0419  -0.0203 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.2831 0.2975 0.3061 0.0013  0.0432  -0.0229 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.2665 0.2809 0.2953 0.0009  0.0524  -0.0271 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.2539 0.2755 0.2938 0.0011  0.0546  -0.0230 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.2413 0.2686 0.2883 0.0019  0.0487  -0.0165 128 GLY   A O   
942  N N   . ASN   A 123 ? 0.2565 0.2777 0.2975 -0.0004 0.0635  -0.0269 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.2703 0.2990 0.3250 -0.0004 0.0671  -0.0235 129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.2408 0.2732 0.2883 -0.0029 0.0606  -0.0179 129 ASN   A C   
945  O O   . ASN   A 123 ? 0.2530 0.2934 0.3147 -0.0029 0.0602  -0.0132 129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.3110 0.3470 0.3925 0.0039  0.0666  -0.0189 129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.3692 0.4017 0.4632 0.0071  0.0738  -0.0236 129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.3939 0.4216 0.4863 0.0060  0.0843  -0.0308 129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.3579 0.3920 0.4650 0.0106  0.0689  -0.0196 129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.2173 0.2444 0.2447 -0.0053 0.0557  -0.0181 130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.2065 0.2354 0.2273 -0.0078 0.0505  -0.0133 130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.1888 0.2212 0.2152 -0.0066 0.0420  -0.0080 130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2015 0.2355 0.2242 -0.0092 0.0382  -0.0044 130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1719 0.2039 0.2045 -0.0036 0.0393  -0.0080 131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1593 0.1932 0.1945 -0.0032 0.0318  -0.0034 131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1625 0.1894 0.1857 -0.0024 0.0285  -0.0054 131 LEU   A C   
957  O O   . LEU   A 125 ? 0.1850 0.2073 0.2030 -0.0014 0.0311  -0.0099 131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1623 0.2019 0.2164 -0.0005 0.0310  -0.0002 131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.1932 0.2418 0.2641 -0.0011 0.0327  0.0038  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2147 0.2682 0.3076 0.0027  0.0341  0.0063  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.1911 0.2446 0.2599 -0.0052 0.0257  0.0097  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1450 0.1717 0.1653 -0.0033 0.0228  -0.0021 132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1441 0.1653 0.1566 -0.0024 0.0199  -0.0034 132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1545 0.1780 0.1730 -0.0025 0.0157  0.0006  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1692 0.1963 0.1892 -0.0052 0.0135  0.0044  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1630 0.1791 0.1621 -0.0041 0.0187  -0.0041 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.2035 0.2204 0.1993 -0.0073 0.0176  -0.0011 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1747 0.1864 0.1702 -0.0027 0.0159  -0.0049 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1528 0.1744 0.1747 -0.0003 0.0148  -0.0002 133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1576 0.1804 0.1837 -0.0008 0.0113  0.0038  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1513 0.1688 0.1695 -0.0012 0.0098  0.0024  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1725 0.1864 0.1880 0.0007  0.0109  -0.0013 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1472 0.1642 0.1614 -0.0042 0.0074  0.0054  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1455 0.1571 0.1529 -0.0049 0.0075  0.0040  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1552 0.1668 0.1655 -0.0061 0.0059  0.0069  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1626 0.1773 0.1736 -0.0092 0.0035  0.0114  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1495 0.1582 0.1473 -0.0086 0.0081  0.0039  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1627 0.1711 0.1570 -0.0084 0.0095  0.0023  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1644 0.1691 0.1559 -0.0062 0.0107  -0.0002 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1830 0.1953 0.1775 -0.0109 0.0091  0.0042  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1583 0.1622 0.1456 -0.0065 0.0118  -0.0008 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1784 0.1899 0.1691 -0.0113 0.0110  0.0029  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1697 0.1766 0.1563 -0.0089 0.0124  0.0005  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1499 0.1581 0.1613 -0.0043 0.0068  0.0049  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1551 0.1620 0.1677 -0.0059 0.0061  0.0075  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1512 0.1542 0.1534 -0.0104 0.0075  0.0075  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1605 0.1597 0.1598 -0.0098 0.0102  0.0039  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1594 0.1640 0.1776 -0.0028 0.0072  0.0048  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1582 0.1618 0.1553 -0.0155 0.0058  0.0115  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1776 0.1762 0.1629 -0.0211 0.0082  0.0106  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1882 0.1819 0.1728 -0.0214 0.0119  0.0088  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1811 0.1758 0.1718 -0.0197 0.0107  0.0110  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2028 0.2037 0.1815 -0.0278 0.0045  0.0158  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2600 0.2549 0.2235 -0.0355 0.0074  0.0141  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2530 0.2443 0.2122 -0.0358 0.0111  0.0096  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3178 0.3109 0.2733 -0.0415 0.0064  0.0172  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1816 0.1693 0.1594 -0.0237 0.0171  0.0049  137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1888 0.1716 0.1663 -0.0248 0.0220  0.0031  137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2046 0.1810 0.1683 -0.0328 0.0267  0.0019  137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2123 0.1836 0.1745 -0.0347 0.0325  -0.0002 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1990 0.1803 0.1860 -0.0195 0.0255  -0.0010 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1977 0.1844 0.1958 -0.0132 0.0209  -0.0004 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1970 0.1748 0.1810 -0.0195 0.0288  -0.0040 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.2055 0.1818 0.1588 -0.0381 0.0248  0.0029  138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.2216 0.1903 0.1595 -0.0468 0.0301  0.0004  138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.2610 0.2273 0.1886 -0.0539 0.0304  0.0031  138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2925 0.2507 0.2075 -0.0611 0.0373  -0.0005 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.2285 0.1981 0.1577 -0.0515 0.0272  0.0007  138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2397 0.2091 0.1760 -0.0461 0.0289  -0.0027 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2409 0.2116 0.1691 -0.0513 0.0258  -0.0018 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2227 0.2033 0.1562 -0.0501 0.0170  0.0042  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2638 0.2488 0.1952 -0.0532 0.0127  0.0063  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2479 0.2274 0.1694 -0.0591 0.0160  0.0027  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2496 0.2442 0.1901 -0.0508 0.0056  0.0119  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2406 0.2130 0.1736 -0.0523 0.0236  0.0095  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2684 0.2385 0.1916 -0.0593 0.0229  0.0138  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2690 0.2348 0.1971 -0.0571 0.0295  0.0114  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2832 0.2453 0.2016 -0.0635 0.0308  0.0141  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2826 0.2608 0.2112 -0.0586 0.0127  0.0228  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.2915 0.2750 0.2398 -0.0484 0.0103  0.0241  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2919 0.2770 0.2499 -0.0414 0.0121  0.0194  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3230 0.3087 0.2768 -0.0478 0.0067  0.0301  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2503 0.2167 0.1929 -0.0487 0.0331  0.0070  140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.2358 0.1994 0.1864 -0.0463 0.0389  0.0049  140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.2533 0.2085 0.1969 -0.0506 0.0497  -0.0013 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.2514 0.2054 0.2056 -0.0457 0.0549  -0.0062 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.2243 0.1932 0.1939 -0.0362 0.0366  0.0035  140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2375 0.2136 0.2144 -0.0319 0.0276  0.0084  140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2376 0.2176 0.2296 -0.0237 0.0261  0.0057  140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2403 0.2170 0.2172 -0.0342 0.0246  0.0143  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2574 0.2063 0.1827 -0.0607 0.0535  -0.0009 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.2970 0.2362 0.2140 -0.0661 0.0657  -0.0081 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.3038 0.2403 0.2339 -0.0624 0.0750  -0.0119 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.3151 0.2455 0.2485 -0.0623 0.0853  -0.0184 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.3202 0.2524 0.2123 -0.0791 0.0683  -0.0074 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.3553 0.2909 0.2332 -0.0850 0.0581  -0.0023 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.3847 0.3113 0.2359 -0.0996 0.0626  -0.0036 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.3534 0.2924 0.2373 -0.0804 0.0547  -0.0045 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.2924 0.2333 0.2318 -0.0591 0.0716  -0.0078 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.3012 0.2408 0.2547 -0.0559 0.0793  -0.0107 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.3047 0.2483 0.2797 -0.0464 0.0802  -0.0141 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.3298 0.2723 0.3183 -0.0441 0.0879  -0.0172 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.3013 0.2446 0.2594 -0.0552 0.0746  -0.0051 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2864 0.2383 0.2535 -0.0487 0.0621  0.0002  142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2880 0.2427 0.2462 -0.0508 0.0530  0.0064  142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2712 0.2296 0.2582 -0.0393 0.0580  -0.0007 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2790 0.2410 0.2516 -0.0430 0.0449  0.0089  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2651 0.2290 0.2537 -0.0364 0.0478  0.0043  142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2726 0.2328 0.2768 -0.0338 0.0619  -0.0048 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2632 0.2330 0.2674 -0.0287 0.0425  0.0040  142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2665 0.2335 0.2856 -0.0266 0.0550  -0.0041 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2630 0.2340 0.2807 -0.0245 0.0459  -0.0003 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.2797 0.2284 0.2588 -0.0411 0.0724  -0.0132 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.2867 0.2390 0.2846 -0.0329 0.0724  -0.0154 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.3370 0.2823 0.3383 -0.0341 0.0840  -0.0209 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.3407 0.2885 0.3612 -0.0280 0.0861  -0.0221 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2728 0.2301 0.2705 -0.0287 0.0632  -0.0135 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2597 0.2246 0.2610 -0.0250 0.0526  -0.0091 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2736 0.2419 0.2721 -0.0224 0.0458  -0.0080 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2440 0.2139 0.2639 -0.0189 0.0507  -0.0091 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.3862 0.3227 0.3694 -0.0423 0.0913  -0.0240 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.4409 0.3684 0.4244 -0.0449 0.1041  -0.0302 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.4968 0.4189 0.4859 -0.0477 0.1168  -0.0339 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.5234 0.4377 0.5159 -0.0493 0.1290  -0.0395 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.4799 0.3991 0.4383 -0.0546 0.1071  -0.0328 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.5528 0.4750 0.5041 -0.0537 0.0977  -0.0307 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.5588 0.4873 0.5253 -0.0451 0.0917  -0.0286 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.6224 0.5408 0.5524 -0.0624 0.0963  -0.0308 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.5221 0.4471 0.5108 -0.0494 0.1154  -0.0311 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.5640 0.4840 0.5577 -0.0527 0.1280  -0.0344 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.5755 0.5046 0.5919 -0.0456 0.1237  -0.0310 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.5953 0.5224 0.6194 -0.0476 0.1328  -0.0328 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.6174 0.5302 0.5845 -0.0644 0.1317  -0.0343 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.7051 0.6247 0.6649 -0.0648 0.1184  -0.0266 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.8341 0.7483 0.7647 -0.0759 0.1162  -0.0239 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.8615 0.7779 0.7868 -0.0786 0.1111  -0.0181 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.8794 0.7872 0.7927 -0.0824 0.1191  -0.0271 145 GLU   A OE2 
1078 N N   . SER   B 1   ? 0.3770 0.3365 0.3451 -0.0045 -0.0220 0.0129  7   SER   C N   
1079 C CA  . SER   B 1   ? 0.3682 0.3333 0.3499 -0.0047 -0.0243 0.0127  7   SER   C CA  
1080 C C   . SER   B 1   ? 0.3360 0.3077 0.3266 -0.0056 -0.0222 0.0114  7   SER   C C   
1081 O O   . SER   B 1   ? 0.3485 0.3192 0.3347 -0.0058 -0.0213 0.0103  7   SER   C O   
1082 C CB  . SER   B 1   ? 0.4010 0.3621 0.3842 -0.0034 -0.0321 0.0125  7   SER   C CB  
1083 O OG  . SER   B 1   ? 0.4455 0.4039 0.4257 -0.0031 -0.0361 0.0108  7   SER   C OG  
1084 N N   . GLY   B 2   ? 0.2868 0.2645 0.2891 -0.0058 -0.0212 0.0117  8   GLY   C N   
1085 C CA  . GLY   B 2   ? 0.2575 0.2407 0.2678 -0.0064 -0.0188 0.0113  8   GLY   C CA  
1086 C C   . GLY   B 2   ? 0.2287 0.2182 0.2473 -0.0060 -0.0146 0.0120  8   GLY   C C   
1087 O O   . GLY   B 2   ? 0.2484 0.2381 0.2651 -0.0054 -0.0128 0.0120  8   GLY   C O   
1088 N N   . ALA   B 3   ? 0.2136 0.2076 0.2411 -0.0061 -0.0131 0.0125  9   ALA   C N   
1089 C CA  . ALA   B 3   ? 0.2009 0.2006 0.2352 -0.0051 -0.0086 0.0131  9   ALA   C CA  
1090 C C   . ALA   B 3   ? 0.1846 0.1874 0.2221 -0.0052 -0.0046 0.0141  9   ALA   C C   
1091 O O   . ALA   B 3   ? 0.2035 0.2046 0.2420 -0.0065 -0.0062 0.0144  9   ALA   C O   
1092 C CB  . ALA   B 3   ? 0.2018 0.2038 0.2466 -0.0044 -0.0108 0.0137  9   ALA   C CB  
1093 N N   . ILE   B 4   ? 0.1781 0.1848 0.2171 -0.0036 0.0003  0.0146  10  ILE   C N   
1094 C CA  . ILE   B 4   ? 0.1724 0.1817 0.2140 -0.0030 0.0048  0.0163  10  ILE   C CA  
1095 C C   . ILE   B 4   ? 0.1834 0.1972 0.2363 -0.0023 0.0073  0.0180  10  ILE   C C   
1096 O O   . ILE   B 4   ? 0.1866 0.2025 0.2416 -0.0006 0.0079  0.0172  10  ILE   C O   
1097 C CB  . ILE   B 4   ? 0.1811 0.1912 0.2144 -0.0008 0.0087  0.0155  10  ILE   C CB  
1098 C CG1 . ILE   B 4   ? 0.1965 0.2033 0.2208 -0.0015 0.0065  0.0135  10  ILE   C CG1 
1099 C CG2 . ILE   B 4   ? 0.2003 0.2117 0.2338 0.0004  0.0133  0.0177  10  ILE   C CG2 
1100 C CD1 . ILE   B 4   ? 0.2178 0.2258 0.2357 0.0008  0.0088  0.0117  10  ILE   C CD1 
1101 N N   . TYR   B 5   ? 0.1988 0.2141 0.2599 -0.0035 0.0091  0.0203  11  TYR   C N   
1102 C CA  . TYR   B 5   ? 0.1960 0.2163 0.2700 -0.0030 0.0125  0.0224  11  TYR   C CA  
1103 C C   . TYR   B 5   ? 0.2078 0.2297 0.2808 -0.0018 0.0200  0.0253  11  TYR   C C   
1104 O O   . TYR   B 5   ? 0.2230 0.2427 0.2964 -0.0035 0.0207  0.0273  11  TYR   C O   
1105 C CB  . TYR   B 5   ? 0.1953 0.2159 0.2824 -0.0060 0.0079  0.0229  11  TYR   C CB  
1106 C CG  . TYR   B 5   ? 0.1948 0.2134 0.2819 -0.0064 0.0002  0.0202  11  TYR   C CG  
1107 C CD1 . TYR   B 5   ? 0.2052 0.2271 0.3000 -0.0050 -0.0009 0.0196  11  TYR   C CD1 
1108 C CD2 . TYR   B 5   ? 0.2245 0.2370 0.3024 -0.0076 -0.0056 0.0184  11  TYR   C CD2 
1109 C CE1 . TYR   B 5   ? 0.2411 0.2599 0.3344 -0.0048 -0.0082 0.0175  11  TYR   C CE1 
1110 C CE2 . TYR   B 5   ? 0.2477 0.2571 0.3230 -0.0074 -0.0122 0.0164  11  TYR   C CE2 
1111 C CZ  . TYR   B 5   ? 0.2638 0.2759 0.3465 -0.0060 -0.0137 0.0161  11  TYR   C CZ  
1112 O OH  . TYR   B 5   ? 0.2916 0.2994 0.3700 -0.0055 -0.0205 0.0145  11  TYR   C OH  
1113 N N   . VAL   B 6   ? 0.2141 0.2388 0.2845 0.0015  0.0254  0.0257  12  VAL   C N   
1114 C CA  . VAL   B 6   ? 0.2292 0.2544 0.2954 0.0037  0.0328  0.0286  12  VAL   C CA  
1115 C C   . VAL   B 6   ? 0.2300 0.2604 0.3037 0.0063  0.0391  0.0301  12  VAL   C C   
1116 O O   . VAL   B 6   ? 0.2235 0.2557 0.2963 0.0087  0.0384  0.0274  12  VAL   C O   
1117 C CB  . VAL   B 6   ? 0.2610 0.2825 0.3102 0.0065  0.0329  0.0267  12  VAL   C CB  
1118 C CG1 . VAL   B 6   ? 0.2668 0.2888 0.3107 0.0086  0.0302  0.0226  12  VAL   C CG1 
1119 C CG2 . VAL   B 6   ? 0.2820 0.3031 0.3247 0.0098  0.0402  0.0298  12  VAL   C CG2 
1120 N N   . GLY   B 7   ? 0.2463 0.2792 0.3293 0.0056  0.0453  0.0344  13  GLY   C N   
1121 C CA  . GLY   B 7   ? 0.2603 0.2989 0.3519 0.0082  0.0525  0.0362  13  GLY   C CA  
1122 C C   . GLY   B 7   ? 0.2585 0.3016 0.3637 0.0073  0.0482  0.0336  13  GLY   C C   
1123 O O   . GLY   B 7   ? 0.2701 0.3130 0.3847 0.0035  0.0414  0.0329  13  GLY   C O   
1124 N N   . ASN   B 8   ? 0.2422 0.2883 0.3465 0.0114  0.0505  0.0316  14  ASN   C N   
1125 C CA  . ASN   B 8   ? 0.2395 0.2891 0.3555 0.0112  0.0456  0.0289  14  ASN   C CA  
1126 C C   . ASN   B 8   ? 0.2171 0.2621 0.3213 0.0123  0.0384  0.0243  14  ASN   C C   
1127 O O   . ASN   B 8   ? 0.2181 0.2648 0.3258 0.0147  0.0366  0.0217  14  ASN   C O   
1128 C CB  . ASN   B 8   ? 0.2775 0.3339 0.4045 0.0147  0.0528  0.0297  14  ASN   C CB  
1129 C CG  . ASN   B 8   ? 0.3731 0.4351 0.5175 0.0125  0.0590  0.0343  14  ASN   C CG  
1130 O OD1 . ASN   B 8   ? 0.4093 0.4740 0.5704 0.0085  0.0542  0.0347  14  ASN   C OD1 
1131 N ND2 . ASN   B 8   ? 0.3903 0.4537 0.5311 0.0150  0.0697  0.0379  14  ASN   C ND2 
1132 N N   . TYR   B 9   ? 0.2088 0.2480 0.3000 0.0106  0.0343  0.0234  15  TYR   C N   
1133 C CA  . TYR   B 9   ? 0.1942 0.2289 0.2749 0.0110  0.0283  0.0196  15  TYR   C CA  
1134 C C   . TYR   B 9   ? 0.1855 0.2161 0.2649 0.0069  0.0208  0.0192  15  TYR   C C   
1135 O O   . TYR   B 9   ? 0.1967 0.2262 0.2769 0.0043  0.0207  0.0211  15  TYR   C O   
1136 C CB  . TYR   B 9   ? 0.2052 0.2365 0.2697 0.0135  0.0307  0.0184  15  TYR   C CB  
1137 C CG  . TYR   B 9   ? 0.2257 0.2592 0.2869 0.0185  0.0373  0.0179  15  TYR   C CG  
1138 C CD1 . TYR   B 9   ? 0.2474 0.2830 0.3133 0.0214  0.0375  0.0156  15  TYR   C CD1 
1139 C CD2 . TYR   B 9   ? 0.2378 0.2705 0.2899 0.0210  0.0432  0.0197  15  TYR   C CD2 
1140 C CE1 . TYR   B 9   ? 0.2721 0.3093 0.3340 0.0267  0.0437  0.0148  15  TYR   C CE1 
1141 C CE2 . TYR   B 9   ? 0.2576 0.2915 0.3045 0.0264  0.0494  0.0192  15  TYR   C CE2 
1142 C CZ  . TYR   B 9   ? 0.2848 0.3210 0.3365 0.0292  0.0497  0.0165  15  TYR   C CZ  
1143 O OH  . TYR   B 9   ? 0.3272 0.3641 0.3728 0.0352  0.0558  0.0155  15  TYR   C OH  
1144 N N   . ARG   B 10  ? 0.1590 0.1866 0.2355 0.0067  0.0150  0.0166  16  ARG   C N   
1145 C CA  . ARG   B 10  ? 0.1646 0.1872 0.2362 0.0037  0.0083  0.0159  16  ARG   C CA  
1146 C C   . ARG   B 10  ? 0.1687 0.1873 0.2277 0.0046  0.0074  0.0136  16  ARG   C C   
1147 O O   . ARG   B 10  ? 0.1745 0.1929 0.2330 0.0068  0.0073  0.0119  16  ARG   C O   
1148 C CB  . ARG   B 10  ? 0.1729 0.1952 0.2534 0.0028  0.0022  0.0155  16  ARG   C CB  
1149 C CG  . ARG   B 10  ? 0.1916 0.2074 0.2638 0.0012  -0.0046 0.0143  16  ARG   C CG  
1150 C CD  . ARG   B 10  ? 0.1946 0.2092 0.2746 0.0010  -0.0114 0.0141  16  ARG   C CD  
1151 N NE  . ARG   B 10  ? 0.2273 0.2354 0.2982 0.0014  -0.0164 0.0131  16  ARG   C NE  
1152 C CZ  . ARG   B 10  ? 0.2631 0.2650 0.3256 0.0000  -0.0214 0.0131  16  ARG   C CZ  
1153 N NH1 . ARG   B 10  ? 0.2541 0.2553 0.3155 -0.0020 -0.0225 0.0133  16  ARG   C NH1 
1154 N NH2 . ARG   B 10  ? 0.2612 0.2569 0.3154 0.0006  -0.0249 0.0130  16  ARG   C NH2 
1155 N N   . VAL   B 11  ? 0.1646 0.1801 0.2143 0.0031  0.0069  0.0134  17  VAL   C N   
1156 C CA  . VAL   B 11  ? 0.1620 0.1743 0.2017 0.0033  0.0061  0.0113  17  VAL   C CA  
1157 C C   . VAL   B 11  ? 0.1680 0.1755 0.2039 0.0008  0.0013  0.0111  17  VAL   C C   
1158 O O   . VAL   B 11  ? 0.1859 0.1920 0.2205 -0.0011 -0.0003 0.0120  17  VAL   C O   
1159 C CB  . VAL   B 11  ? 0.1916 0.2041 0.2241 0.0040  0.0092  0.0110  17  VAL   C CB  
1160 C CG1 . VAL   B 11  ? 0.2017 0.2122 0.2270 0.0045  0.0084  0.0083  17  VAL   C CG1 
1161 C CG2 . VAL   B 11  ? 0.1951 0.2111 0.2293 0.0067  0.0144  0.0122  17  VAL   C CG2 
1162 N N   . VAL   B 12  ? 0.1648 0.1694 0.1986 0.0009  -0.0010 0.0101  18  VAL   C N   
1163 C CA  . VAL   B 12  ? 0.1742 0.1734 0.2029 -0.0010 -0.0048 0.0105  18  VAL   C CA  
1164 C C   . VAL   B 12  ? 0.1749 0.1711 0.1974 -0.0014 -0.0040 0.0093  18  VAL   C C   
1165 O O   . VAL   B 12  ? 0.1741 0.1720 0.1979 0.0000  -0.0021 0.0077  18  VAL   C O   
1166 C CB  . VAL   B 12  ? 0.2071 0.2041 0.2404 -0.0006 -0.0092 0.0114  18  VAL   C CB  
1167 C CG1 . VAL   B 12  ? 0.2587 0.2586 0.2999 -0.0009 -0.0109 0.0123  18  VAL   C CG1 
1168 C CG2 . VAL   B 12  ? 0.1877 0.1856 0.2257 0.0016  -0.0089 0.0105  18  VAL   C CG2 
1169 N N   . ASN   B 13  ? 0.1649 0.1563 0.1810 -0.0033 -0.0055 0.0101  19  ASN   C N   
1170 C CA  . ASN   B 13  ? 0.1697 0.1580 0.1823 -0.0042 -0.0046 0.0096  19  ASN   C CA  
1171 C C   . ASN   B 13  ? 0.1858 0.1715 0.2019 -0.0030 -0.0066 0.0097  19  ASN   C C   
1172 O O   . ASN   B 13  ? 0.1892 0.1721 0.2062 -0.0024 -0.0100 0.0112  19  ASN   C O   
1173 C CB  . ASN   B 13  ? 0.1867 0.1696 0.1916 -0.0061 -0.0051 0.0113  19  ASN   C CB  
1174 C CG  . ASN   B 13  ? 0.2067 0.1917 0.2081 -0.0070 -0.0030 0.0107  19  ASN   C CG  
1175 O OD1 . ASN   B 13  ? 0.2008 0.1856 0.2006 -0.0068 -0.0045 0.0112  19  ASN   C OD1 
1176 N ND2 . ASN   B 13  ? 0.2023 0.1892 0.2033 -0.0078 0.0001  0.0094  19  ASN   C ND2 
1177 N N   . ARG   B 14  ? 0.1779 0.1638 0.1960 -0.0024 -0.0053 0.0079  20  ARG   C N   
1178 C CA  . ARG   B 14  ? 0.1716 0.1546 0.1932 -0.0009 -0.0073 0.0076  20  ARG   C CA  
1179 C C   . ARG   B 14  ? 0.2052 0.1806 0.2230 -0.0021 -0.0101 0.0104  20  ARG   C C   
1180 O O   . ARG   B 14  ? 0.2041 0.1771 0.2247 -0.0004 -0.0133 0.0112  20  ARG   C O   
1181 C CB  . ARG   B 14  ? 0.1803 0.1635 0.2038 -0.0004 -0.0059 0.0047  20  ARG   C CB  
1182 C CG  . ARG   B 14  ? 0.1847 0.1652 0.2126 0.0020  -0.0079 0.0035  20  ARG   C CG  
1183 C CD  . ARG   B 14  ? 0.1944 0.1737 0.2234 0.0020  -0.0073 0.0002  20  ARG   C CD  
1184 N NE  . ARG   B 14  ? 0.2043 0.1806 0.2372 0.0048  -0.0091 -0.0020 20  ARG   C NE  
1185 C CZ  . ARG   B 14  ? 0.2268 0.1959 0.2607 0.0039  -0.0115 -0.0008 20  ARG   C CZ  
1186 N NH1 . ARG   B 14  ? 0.2336 0.1976 0.2640 0.0007  -0.0120 0.0032  20  ARG   C NH1 
1187 N NH2 . ARG   B 14  ? 0.2171 0.1835 0.2548 0.0068  -0.0132 -0.0034 20  ARG   C NH2 
1188 N N   . HIS   B 15  ? 0.2028 0.1744 0.2139 -0.0047 -0.0088 0.0121  21  HIS   C N   
1189 C CA  . HIS   B 15  ? 0.2162 0.1793 0.2215 -0.0055 -0.0109 0.0153  21  HIS   C CA  
1190 C C   . HIS   B 15  ? 0.2168 0.1777 0.2183 -0.0042 -0.0148 0.0171  21  HIS   C C   
1191 O O   . HIS   B 15  ? 0.2431 0.1964 0.2390 -0.0038 -0.0176 0.0197  21  HIS   C O   
1192 C CB  . HIS   B 15  ? 0.2205 0.1800 0.2199 -0.0084 -0.0072 0.0169  21  HIS   C CB  
1193 C CG  . HIS   B 15  ? 0.2327 0.1942 0.2263 -0.0095 -0.0050 0.0174  21  HIS   C CG  
1194 N ND1 . HIS   B 15  ? 0.2209 0.1897 0.2180 -0.0099 -0.0025 0.0148  21  HIS   C ND1 
1195 C CD2 . HIS   B 15  ? 0.2534 0.2097 0.2375 -0.0098 -0.0052 0.0200  21  HIS   C CD2 
1196 C CE1 . HIS   B 15  ? 0.2364 0.2046 0.2270 -0.0106 -0.0011 0.0157  21  HIS   C CE1 
1197 N NE2 . HIS   B 15  ? 0.2680 0.2288 0.2502 -0.0105 -0.0025 0.0187  21  HIS   C NE2 
1198 N N   . LEU   B 16  ? 0.2026 0.1695 0.2068 -0.0036 -0.0153 0.0158  22  LEU   C N   
1199 C CA  . LEU   B 16  ? 0.2144 0.1795 0.2171 -0.0025 -0.0200 0.0168  22  LEU   C CA  
1200 C C   . LEU   B 16  ? 0.2250 0.1953 0.2390 -0.0004 -0.0227 0.0155  22  LEU   C C   
1201 O O   . LEU   B 16  ? 0.2327 0.2030 0.2489 0.0005  -0.0271 0.0157  22  LEU   C O   
1202 C CB  . LEU   B 16  ? 0.2190 0.1863 0.2175 -0.0037 -0.0188 0.0163  22  LEU   C CB  
1203 C CG  . LEU   B 16  ? 0.2488 0.2115 0.2365 -0.0053 -0.0157 0.0175  22  LEU   C CG  
1204 C CD1 . LEU   B 16  ? 0.2712 0.2359 0.2552 -0.0058 -0.0150 0.0165  22  LEU   C CD1 
1205 C CD2 . LEU   B 16  ? 0.2553 0.2078 0.2327 -0.0047 -0.0185 0.0204  22  LEU   C CD2 
1206 N N   . ALA   B 17  ? 0.2079 0.1824 0.2294 0.0008  -0.0203 0.0140  23  ALA   C N   
1207 C CA  . ALA   B 17  ? 0.2169 0.1968 0.2496 0.0031  -0.0216 0.0128  23  ALA   C CA  
1208 C C   . ALA   B 17  ? 0.2140 0.1895 0.2490 0.0050  -0.0278 0.0139  23  ALA   C C   
1209 O O   . ALA   B 17  ? 0.2233 0.1912 0.2521 0.0053  -0.0300 0.0153  23  ALA   C O   
1210 C CB  . ALA   B 17  ? 0.2113 0.1948 0.2491 0.0047  -0.0179 0.0108  23  ALA   C CB  
1211 N N   . THR   B 18  ? 0.2140 0.1946 0.2591 0.0064  -0.0304 0.0134  24  THR   C N   
1212 C CA  . THR   B 18  ? 0.2215 0.1990 0.2711 0.0086  -0.0374 0.0139  24  THR   C CA  
1213 C C   . THR   B 18  ? 0.2341 0.2143 0.2938 0.0118  -0.0372 0.0127  24  THR   C C   
1214 O O   . THR   B 18  ? 0.2240 0.2091 0.2875 0.0123  -0.0314 0.0112  24  THR   C O   
1215 C CB  . THR   B 18  ? 0.2439 0.2261 0.3018 0.0084  -0.0410 0.0135  24  THR   C CB  
1216 O OG1 . THR   B 18  ? 0.2551 0.2474 0.3267 0.0087  -0.0362 0.0123  24  THR   C OG1 
1217 C CG2 . THR   B 18  ? 0.2351 0.2144 0.2833 0.0058  -0.0415 0.0140  24  THR   C CG2 
1218 N N   . HIS   B 19  ? 0.2367 0.2138 0.3011 0.0144  -0.0438 0.0130  25  HIS   C N   
1219 C CA  . HIS   B 19  ? 0.2356 0.2159 0.3113 0.0180  -0.0438 0.0115  25  HIS   C CA  
1220 C C   . HIS   B 19  ? 0.2219 0.2144 0.3122 0.0187  -0.0387 0.0097  25  HIS   C C   
1221 O O   . HIS   B 19  ? 0.2220 0.2186 0.3176 0.0208  -0.0338 0.0081  25  HIS   C O   
1222 C CB  . HIS   B 19  ? 0.2768 0.2532 0.3573 0.0210  -0.0527 0.0120  25  HIS   C CB  
1223 C CG  . HIS   B 19  ? 0.3905 0.3541 0.4566 0.0213  -0.0575 0.0143  25  HIS   C CG  
1224 N ND1 . HIS   B 19  ? 0.4453 0.4023 0.5044 0.0216  -0.0548 0.0150  25  HIS   C ND1 
1225 C CD2 . HIS   B 19  ? 0.4418 0.3975 0.4996 0.0218  -0.0649 0.0162  25  HIS   C CD2 
1226 C CE1 . HIS   B 19  ? 0.4695 0.4150 0.5167 0.0219  -0.0599 0.0179  25  HIS   C CE1 
1227 N NE2 . HIS   B 19  ? 0.4740 0.4181 0.5188 0.0223  -0.0660 0.0187  25  HIS   C NE2 
1228 N N   . ASN   B 20  ? 0.2164 0.2139 0.3122 0.0168  -0.0395 0.0101  26  ASN   C N   
1229 C CA  . ASN   B 20  ? 0.2123 0.2208 0.3222 0.0170  -0.0339 0.0093  26  ASN   C CA  
1230 C C   . ASN   B 20  ? 0.2046 0.2157 0.3083 0.0161  -0.0252 0.0091  26  ASN   C C   
1231 O O   . ASN   B 20  ? 0.1981 0.2160 0.3098 0.0181  -0.0192 0.0082  26  ASN   C O   
1232 C CB  . ASN   B 20  ? 0.2366 0.2488 0.3540 0.0147  -0.0368 0.0100  26  ASN   C CB  
1233 C CG  . ASN   B 20  ? 0.3311 0.3543 0.4658 0.0149  -0.0312 0.0098  26  ASN   C CG  
1234 O OD1 . ASN   B 20  ? 0.3572 0.3862 0.5071 0.0178  -0.0316 0.0090  26  ASN   C OD1 
1235 N ND2 . ASN   B 20  ? 0.3417 0.3680 0.4747 0.0121  -0.0256 0.0109  26  ASN   C ND2 
1236 N N   . ASP   B 21  ? 0.2008 0.2065 0.2899 0.0132  -0.0242 0.0098  27  ASP   C N   
1237 C CA  . ASP   B 21  ? 0.1969 0.2046 0.2798 0.0128  -0.0170 0.0091  27  ASP   C CA  
1238 C C   . ASP   B 21  ? 0.1933 0.2002 0.2757 0.0160  -0.0145 0.0071  27  ASP   C C   
1239 O O   . ASP   B 21  ? 0.2065 0.2185 0.2912 0.0179  -0.0086 0.0058  27  ASP   C O   
1240 C CB  . ASP   B 21  ? 0.1957 0.1975 0.2644 0.0096  -0.0172 0.0098  27  ASP   C CB  
1241 C CG  . ASP   B 21  ? 0.2222 0.2249 0.2896 0.0068  -0.0181 0.0111  27  ASP   C CG  
1242 O OD1 . ASP   B 21  ? 0.2286 0.2378 0.3044 0.0066  -0.0151 0.0115  27  ASP   C OD1 
1243 O OD2 . ASP   B 21  ? 0.2149 0.2115 0.2727 0.0049  -0.0213 0.0119  27  ASP   C OD2 
1244 N N   . TRP   B 22  ? 0.1978 0.1977 0.2766 0.0169  -0.0191 0.0068  28  TRP   C N   
1245 C CA  . TRP   B 22  ? 0.2137 0.2117 0.2924 0.0200  -0.0176 0.0045  28  TRP   C CA  
1246 C C   . TRP   B 22  ? 0.2253 0.2297 0.3171 0.0244  -0.0160 0.0029  28  TRP   C C   
1247 O O   . TRP   B 22  ? 0.2376 0.2437 0.3295 0.0274  -0.0117 0.0003  28  TRP   C O   
1248 C CB  . TRP   B 22  ? 0.2180 0.2058 0.2899 0.0195  -0.0229 0.0052  28  TRP   C CB  
1249 C CG  . TRP   B 22  ? 0.2000 0.1823 0.2600 0.0161  -0.0216 0.0057  28  TRP   C CG  
1250 C CD1 . TRP   B 22  ? 0.2172 0.1945 0.2688 0.0127  -0.0235 0.0083  28  TRP   C CD1 
1251 C CD2 . TRP   B 22  ? 0.2025 0.1835 0.2585 0.0162  -0.0182 0.0033  28  TRP   C CD2 
1252 N NE1 . TRP   B 22  ? 0.2225 0.1968 0.2666 0.0103  -0.0207 0.0079  28  TRP   C NE1 
1253 C CE2 . TRP   B 22  ? 0.2153 0.1914 0.2624 0.0123  -0.0180 0.0047  28  TRP   C CE2 
1254 C CE3 . TRP   B 22  ? 0.2158 0.1992 0.2751 0.0196  -0.0154 -0.0003 28  TRP   C CE3 
1255 C CZ2 . TRP   B 22  ? 0.2247 0.1991 0.2680 0.0112  -0.0157 0.0026  28  TRP   C CZ2 
1256 C CZ3 . TRP   B 22  ? 0.2258 0.2065 0.2795 0.0188  -0.0137 -0.0027 28  TRP   C CZ3 
1257 C CH2 . TRP   B 22  ? 0.2202 0.1968 0.2670 0.0144  -0.0140 -0.0012 28  TRP   C CH2 
1258 N N   . ALA   B 23  ? 0.2081 0.2163 0.3110 0.0250  -0.0191 0.0040  29  ALA   C N   
1259 C CA  . ALA   B 23  ? 0.2122 0.2277 0.3298 0.0292  -0.0171 0.0026  29  ALA   C CA  
1260 C C   . ALA   B 23  ? 0.2226 0.2473 0.3450 0.0297  -0.0082 0.0024  29  ALA   C C   
1261 O O   . ALA   B 23  ? 0.2376 0.2687 0.3706 0.0336  -0.0041 0.0012  29  ALA   C O   
1262 C CB  . ALA   B 23  ? 0.1980 0.2157 0.3280 0.0294  -0.0235 0.0037  29  ALA   C CB  
1263 N N   . ASN   B 24  ? 0.1997 0.2254 0.3158 0.0259  -0.0055 0.0042  30  ASN   C N   
1264 C CA  . ASN   B 24  ? 0.1819 0.2148 0.3007 0.0262  0.0027  0.0050  30  ASN   C CA  
1265 C C   . ASN   B 24  ? 0.1926 0.2216 0.2953 0.0255  0.0064  0.0042  30  ASN   C C   
1266 O O   . ASN   B 24  ? 0.1855 0.2168 0.2848 0.0237  0.0106  0.0058  30  ASN   C O   
1267 C CB  . ASN   B 24  ? 0.1905 0.2275 0.3174 0.0226  0.0021  0.0078  30  ASN   C CB  
1268 C CG  . ASN   B 24  ? 0.2275 0.2698 0.3729 0.0239  -0.0012 0.0079  30  ASN   C CG  
1269 O OD1 . ASN   B 24  ? 0.2114 0.2612 0.3694 0.0268  0.0042  0.0076  30  ASN   C OD1 
1270 N ND2 . ASN   B 24  ? 0.2482 0.2861 0.3949 0.0222  -0.0104 0.0080  30  ASN   C ND2 
1271 N N   . LEU   B 25  ? 0.1996 0.2226 0.2936 0.0270  0.0044  0.0017  31  LEU   C N   
1272 C CA  . LEU   B 25  ? 0.1967 0.2157 0.2770 0.0263  0.0061  0.0004  31  LEU   C CA  
1273 C C   . LEU   B 25  ? 0.2151 0.2383 0.2920 0.0295  0.0135  -0.0008 31  LEU   C C   
1274 O O   . LEU   B 25  ? 0.2407 0.2668 0.3218 0.0341  0.0172  -0.0025 31  LEU   C O   
1275 C CB  . LEU   B 25  ? 0.2061 0.2178 0.2812 0.0275  0.0021  -0.0024 31  LEU   C CB  
1276 C CG  . LEU   B 25  ? 0.2170 0.2244 0.2802 0.0267  0.0027  -0.0046 31  LEU   C CG  
1277 C CD1 . LEU   B 25  ? 0.2308 0.2362 0.2880 0.0216  0.0009  -0.0022 31  LEU   C CD1 
1278 C CD2 . LEU   B 25  ? 0.2183 0.2188 0.2794 0.0280  -0.0011 -0.0075 31  LEU   C CD2 
1279 N N   . VAL   B 26  ? 0.1957 0.2184 0.2636 0.0276  0.0158  0.0001  32  VAL   C N   
1280 C CA  . VAL   B 26  ? 0.2098 0.2345 0.2706 0.0309  0.0220  -0.0009 32  VAL   C CA  
1281 C C   . VAL   B 26  ? 0.2313 0.2502 0.2799 0.0317  0.0194  -0.0046 32  VAL   C C   
1282 O O   . VAL   B 26  ? 0.2463 0.2641 0.2892 0.0364  0.0215  -0.0080 32  VAL   C O   
1283 C CB  . VAL   B 26  ? 0.2286 0.2565 0.2885 0.0286  0.0259  0.0029  32  VAL   C CB  
1284 C CG1 . VAL   B 26  ? 0.2382 0.2662 0.2874 0.0322  0.0316  0.0022  32  VAL   C CG1 
1285 C CG2 . VAL   B 26  ? 0.2331 0.2670 0.3073 0.0276  0.0285  0.0063  32  VAL   C CG2 
1286 N N   . TRP   B 27  ? 0.2081 0.2231 0.2528 0.0272  0.0147  -0.0042 33  TRP   C N   
1287 C CA  . TRP   B 27  ? 0.2061 0.2165 0.2418 0.0271  0.0122  -0.0074 33  TRP   C CA  
1288 C C   . TRP   B 27  ? 0.2018 0.2085 0.2376 0.0219  0.0073  -0.0062 33  TRP   C C   
1289 O O   . TRP   B 27  ? 0.2051 0.2130 0.2433 0.0186  0.0069  -0.0028 33  TRP   C O   
1290 C CB  . TRP   B 27  ? 0.2235 0.2356 0.2505 0.0285  0.0155  -0.0076 33  TRP   C CB  
1291 C CG  . TRP   B 27  ? 0.2311 0.2395 0.2505 0.0277  0.0121  -0.0108 33  TRP   C CG  
1292 C CD1 . TRP   B 27  ? 0.2601 0.2655 0.2741 0.0311  0.0104  -0.0157 33  TRP   C CD1 
1293 C CD2 . TRP   B 27  ? 0.2144 0.2221 0.2315 0.0234  0.0101  -0.0094 33  TRP   C CD2 
1294 N NE1 . TRP   B 27  ? 0.2638 0.2671 0.2740 0.0287  0.0069  -0.0175 33  TRP   C NE1 
1295 C CE2 . TRP   B 27  ? 0.2410 0.2460 0.2530 0.0242  0.0072  -0.0136 33  TRP   C CE2 
1296 C CE3 . TRP   B 27  ? 0.2166 0.2256 0.2359 0.0193  0.0102  -0.0055 33  TRP   C CE3 
1297 C CZ2 . TRP   B 27  ? 0.2286 0.2333 0.2388 0.0210  0.0051  -0.0136 33  TRP   C CZ2 
1298 C CZ3 . TRP   B 27  ? 0.2265 0.2346 0.2424 0.0165  0.0084  -0.0056 33  TRP   C CZ3 
1299 C CH2 . TRP   B 27  ? 0.2199 0.2261 0.2318 0.0173  0.0061  -0.0095 33  TRP   C CH2 
1300 N N   . GLU   B 28  ? 0.1968 0.1985 0.2299 0.0213  0.0039  -0.0091 34  GLU   C N   
1301 C CA  . GLU   B 28  ? 0.2009 0.1989 0.2333 0.0164  0.0006  -0.0077 34  GLU   C CA  
1302 C C   . GLU   B 28  ? 0.2137 0.2085 0.2423 0.0160  -0.0011 -0.0112 34  GLU   C C   
1303 O O   . GLU   B 28  ? 0.2155 0.2089 0.2434 0.0194  -0.0017 -0.0152 34  GLU   C O   
1304 C CB  . GLU   B 28  ? 0.2095 0.2035 0.2466 0.0147  -0.0025 -0.0055 34  GLU   C CB  
1305 C CG  . GLU   B 28  ? 0.2335 0.2241 0.2741 0.0179  -0.0043 -0.0081 34  GLU   C CG  
1306 C CD  . GLU   B 28  ? 0.2774 0.2620 0.3161 0.0172  -0.0068 -0.0111 34  GLU   C CD  
1307 O OE1 . GLU   B 28  ? 0.3003 0.2828 0.3405 0.0208  -0.0077 -0.0148 34  GLU   C OE1 
1308 O OE2 . GLU   B 28  ? 0.2430 0.2247 0.2796 0.0130  -0.0079 -0.0099 34  GLU   C OE2 
1309 N N   . ASP   B 29  ? 0.2092 0.2029 0.2363 0.0119  -0.0021 -0.0100 35  ASP   C N   
1310 C CA  . ASP   B 29  ? 0.2072 0.1987 0.2334 0.0108  -0.0039 -0.0134 35  ASP   C CA  
1311 C C   . ASP   B 29  ? 0.1945 0.1829 0.2224 0.0056  -0.0048 -0.0108 35  ASP   C C   
1312 O O   . ASP   B 29  ? 0.1951 0.1856 0.2210 0.0032  -0.0034 -0.0082 35  ASP   C O   
1313 C CB  . ASP   B 29  ? 0.2125 0.2080 0.2342 0.0128  -0.0029 -0.0158 35  ASP   C CB  
1314 C CG  . ASP   B 29  ? 0.2718 0.2659 0.2940 0.0123  -0.0057 -0.0201 35  ASP   C CG  
1315 O OD1 . ASP   B 29  ? 0.3029 0.2941 0.3298 0.0085  -0.0073 -0.0199 35  ASP   C OD1 
1316 O OD2 . ASP   B 29  ? 0.2708 0.2667 0.2887 0.0158  -0.0062 -0.0235 35  ASP   C OD2 
1317 N N   . SER   B 30  ? 0.1882 0.1709 0.2195 0.0041  -0.0069 -0.0111 36  SER   C N   
1318 C CA  A SER   B 30  ? 0.1934 0.1721 0.2257 -0.0005 -0.0069 -0.0080 36  SER   C CA  
1319 C CA  B SER   B 30  ? 0.1920 0.1709 0.2242 -0.0005 -0.0068 -0.0079 36  SER   C CA  
1320 C C   . SER   B 30  ? 0.2032 0.1847 0.2363 -0.0032 -0.0057 -0.0092 36  SER   C C   
1321 O O   . SER   B 30  ? 0.2180 0.1993 0.2498 -0.0064 -0.0038 -0.0059 36  SER   C O   
1322 C CB  A SER   B 30  ? 0.2196 0.1912 0.2558 -0.0012 -0.0091 -0.0085 36  SER   C CB  
1323 C CB  B SER   B 30  ? 0.2141 0.1856 0.2499 -0.0015 -0.0089 -0.0078 36  SER   C CB  
1324 O OG  A SER   B 30  ? 0.2596 0.2264 0.2964 -0.0057 -0.0082 -0.0049 36  SER   C OG  
1325 O OG  B SER   B 30  ? 0.2445 0.2151 0.2844 -0.0010 -0.0106 -0.0127 36  SER   C OG  
1326 N N   . SER   B 31  ? 0.1848 0.1689 0.2198 -0.0013 -0.0071 -0.0142 37  SER   C N   
1327 C CA  . SER   B 31  ? 0.1826 0.1698 0.2203 -0.0036 -0.0068 -0.0158 37  SER   C CA  
1328 C C   . SER   B 31  ? 0.2001 0.1924 0.2331 -0.0034 -0.0044 -0.0138 37  SER   C C   
1329 O O   . SER   B 31  ? 0.2227 0.2174 0.2581 -0.0058 -0.0034 -0.0138 37  SER   C O   
1330 C CB  . SER   B 31  ? 0.2324 0.2209 0.2728 -0.0011 -0.0101 -0.0221 37  SER   C CB  
1331 O OG  . SER   B 31  ? 0.2974 0.2896 0.3315 0.0038  -0.0105 -0.0244 37  SER   C OG  
1332 N N   . ARG   B 32  ? 0.1685 0.1626 0.1963 -0.0008 -0.0034 -0.0122 38  ARG   C N   
1333 C CA  . ARG   B 32  ? 0.1676 0.1657 0.1913 -0.0007 -0.0013 -0.0101 38  ARG   C CA  
1334 C C   . ARG   B 32  ? 0.1687 0.1650 0.1901 -0.0028 0.0003  -0.0053 38  ARG   C C   
1335 O O   . ARG   B 32  ? 0.1597 0.1583 0.1780 -0.0031 0.0017  -0.0036 38  ARG   C O   
1336 C CB  . ARG   B 32  ? 0.1748 0.1759 0.1943 0.0038  -0.0009 -0.0112 38  ARG   C CB  
1337 C CG  . ARG   B 32  ? 0.1830 0.1854 0.2018 0.0069  -0.0029 -0.0161 38  ARG   C CG  
1338 C CD  . ARG   B 32  ? 0.1853 0.1895 0.1979 0.0119  -0.0017 -0.0167 38  ARG   C CD  
1339 N NE  . ARG   B 32  ? 0.1746 0.1815 0.1836 0.0119  0.0005  -0.0139 38  ARG   C NE  
1340 C CZ  . ARG   B 32  ? 0.1831 0.1915 0.1861 0.0157  0.0015  -0.0143 38  ARG   C CZ  
1341 N NH1 . ARG   B 32  ? 0.2032 0.2107 0.2018 0.0203  0.0005  -0.0177 38  ARG   C NH1 
1342 N NH2 . ARG   B 32  ? 0.1933 0.2032 0.1937 0.0153  0.0034  -0.0114 38  ARG   C NH2 
1343 N N   . ASP   B 33  ? 0.1720 0.1637 0.1943 -0.0039 -0.0004 -0.0033 39  ASP   C N   
1344 C CA  . ASP   B 33  ? 0.1672 0.1564 0.1865 -0.0050 -0.0003 0.0008  39  ASP   C CA  
1345 C C   . ASP   B 33  ? 0.1692 0.1617 0.1874 -0.0027 -0.0002 0.0016  39  ASP   C C   
1346 O O   . ASP   B 33  ? 0.1683 0.1604 0.1839 -0.0036 -0.0002 0.0040  39  ASP   C O   
1347 C CB  . ASP   B 33  ? 0.1702 0.1580 0.1860 -0.0080 0.0015  0.0032  39  ASP   C CB  
1348 C CG  . ASP   B 33  ? 0.1901 0.1736 0.2010 -0.0087 0.0008  0.0069  39  ASP   C CG  
1349 O OD1 . ASP   B 33  ? 0.2023 0.1815 0.2135 -0.0081 -0.0014 0.0083  39  ASP   C OD1 
1350 O OD2 . ASP   B 33  ? 0.1793 0.1633 0.1857 -0.0094 0.0018  0.0082  39  ASP   C OD2 
1351 N N   . LEU   B 34  ? 0.1609 0.1561 0.1812 0.0005  -0.0002 -0.0005 40  LEU   C N   
1352 C CA  . LEU   B 34  ? 0.1602 0.1586 0.1811 0.0025  0.0008  0.0007  40  LEU   C CA  
1353 C C   . LEU   B 34  ? 0.1704 0.1687 0.1956 0.0049  0.0002  0.0007  40  LEU   C C   
1354 O O   . LEU   B 34  ? 0.1791 0.1758 0.2056 0.0067  -0.0005 -0.0018 40  LEU   C O   
1355 C CB  . LEU   B 34  ? 0.1684 0.1711 0.1872 0.0049  0.0031  -0.0009 40  LEU   C CB  
1356 C CG  . LEU   B 34  ? 0.1876 0.1916 0.2029 0.0035  0.0038  -0.0007 40  LEU   C CG  
1357 C CD1 . LEU   B 34  ? 0.2000 0.2071 0.2123 0.0068  0.0055  -0.0023 40  LEU   C CD1 
1358 C CD2 . LEU   B 34  ? 0.2045 0.2081 0.2194 0.0013  0.0039  0.0025  40  LEU   C CD2 
1359 N N   . LEU   B 35  ? 0.1558 0.1560 0.1841 0.0053  0.0003  0.0030  41  LEU   C N   
1360 C CA  . LEU   B 35  ? 0.1661 0.1678 0.2005 0.0080  0.0003  0.0029  41  LEU   C CA  
1361 C C   . LEU   B 35  ? 0.1659 0.1728 0.2042 0.0088  0.0029  0.0047  41  LEU   C C   
1362 O O   . LEU   B 35  ? 0.1698 0.1770 0.2073 0.0064  0.0024  0.0066  41  LEU   C O   
1363 C CB  . LEU   B 35  ? 0.1757 0.1732 0.2130 0.0072  -0.0037 0.0042  41  LEU   C CB  
1364 C CG  . LEU   B 35  ? 0.1653 0.1645 0.2105 0.0104  -0.0043 0.0038  41  LEU   C CG  
1365 C CD1 . LEU   B 35  ? 0.1729 0.1658 0.2186 0.0105  -0.0085 0.0038  41  LEU   C CD1 
1366 C CD2 . LEU   B 35  ? 0.1841 0.1875 0.2364 0.0102  -0.0047 0.0060  41  LEU   C CD2 
1367 N N   . VAL   B 36  ? 0.1664 0.1771 0.2086 0.0122  0.0061  0.0039  42  VAL   C N   
1368 C CA  . VAL   B 36  ? 0.1663 0.1821 0.2138 0.0130  0.0098  0.0061  42  VAL   C CA  
1369 C C   . VAL   B 36  ? 0.1633 0.1818 0.2212 0.0150  0.0099  0.0063  42  VAL   C C   
1370 O O   . VAL   B 36  ? 0.1680 0.1860 0.2265 0.0182  0.0104  0.0040  42  VAL   C O   
1371 C CB  . VAL   B 36  ? 0.1788 0.1969 0.2208 0.0158  0.0151  0.0055  42  VAL   C CB  
1372 C CG1 . VAL   B 36  ? 0.1863 0.2092 0.2346 0.0165  0.0200  0.0085  42  VAL   C CG1 
1373 C CG2 . VAL   B 36  ? 0.1785 0.1941 0.2114 0.0141  0.0142  0.0049  42  VAL   C CG2 
1374 N N   . SER   B 37  ? 0.1626 0.1838 0.2295 0.0133  0.0090  0.0087  43  SER   C N   
1375 C CA  . SER   B 37  ? 0.1657 0.1909 0.2453 0.0152  0.0089  0.0090  43  SER   C CA  
1376 C C   . SER   B 37  ? 0.1921 0.2239 0.2807 0.0154  0.0144  0.0115  43  SER   C C   
1377 O O   . SER   B 37  ? 0.1948 0.2267 0.2800 0.0132  0.0166  0.0134  43  SER   C O   
1378 C CB  . SER   B 37  ? 0.1820 0.2042 0.2662 0.0131  0.0015  0.0095  43  SER   C CB  
1379 O OG  . SER   B 37  ? 0.2068 0.2280 0.2907 0.0095  -0.0012 0.0113  43  SER   C OG  
1380 N N   . SER   B 38  ? 0.1969 0.2340 0.2981 0.0179  0.0169  0.0116  44  SER   C N   
1381 C CA  . SER   B 38  ? 0.2216 0.2654 0.3336 0.0179  0.0231  0.0143  44  SER   C CA  
1382 C C   . SER   B 38  ? 0.2383 0.2845 0.3645 0.0142  0.0184  0.0161  44  SER   C C   
1383 O O   . SER   B 38  ? 0.2448 0.2890 0.3753 0.0135  0.0108  0.0148  44  SER   C O   
1384 C CB  . SER   B 38  ? 0.2347 0.2839 0.3541 0.0227  0.0293  0.0136  44  SER   C CB  
1385 O OG  . SER   B 38  ? 0.2659 0.3159 0.3947 0.0241  0.0242  0.0116  44  SER   C OG  
1386 N N   . THR   B 39  ? 0.2439 0.2936 0.3769 0.0120  0.0227  0.0191  45  THR   C N   
1387 C CA  . THR   B 39  ? 0.2771 0.3290 0.4249 0.0083  0.0182  0.0205  45  THR   C CA  
1388 C C   . THR   B 39  ? 0.3101 0.3706 0.4765 0.0087  0.0255  0.0231  45  THR   C C   
1389 O O   . THR   B 39  ? 0.3082 0.3716 0.4720 0.0112  0.0351  0.0248  45  THR   C O   
1390 C CB  . THR   B 39  ? 0.2989 0.3460 0.4388 0.0043  0.0160  0.0218  45  THR   C CB  
1391 O OG1 . THR   B 39  ? 0.3224 0.3712 0.4601 0.0043  0.0247  0.0248  45  THR   C OG1 
1392 C CG2 . THR   B 39  ? 0.3138 0.3531 0.4351 0.0040  0.0110  0.0198  45  THR   C CG2 
1393 N N   . THR   B 40  ? 0.3313 0.3957 0.5164 0.0062  0.0210  0.0235  46  THR   C N   
1394 C CA  . THR   B 40  ? 0.3512 0.4244 0.5572 0.0056  0.0278  0.0263  46  THR   C CA  
1395 C C   . THR   B 40  ? 0.3650 0.4370 0.5732 0.0012  0.0308  0.0298  46  THR   C C   
1396 O O   . THR   B 40  ? 0.3858 0.4632 0.6042 0.0009  0.0404  0.0335  46  THR   C O   
1397 C CB  . THR   B 40  ? 0.3685 0.4471 0.5964 0.0053  0.0210  0.0245  46  THR   C CB  
1398 O OG1 . THR   B 40  ? 0.4007 0.4736 0.6269 0.0021  0.0091  0.0226  46  THR   C OG1 
1399 C CG2 . THR   B 40  ? 0.3743 0.4547 0.6023 0.0104  0.0198  0.0216  46  THR   C CG2 
1400 N N   . ALA   B 41  ? 0.3550 0.4199 0.5541 -0.0021 0.0229  0.0288  47  ALA   C N   
1401 C CA  . ALA   B 41  ? 0.3543 0.4167 0.5548 -0.0061 0.0242  0.0316  47  ALA   C CA  
1402 C C   . ALA   B 41  ? 0.3618 0.4187 0.5413 -0.0051 0.0304  0.0335  47  ALA   C C   
1403 O O   . ALA   B 41  ? 0.3664 0.4193 0.5281 -0.0025 0.0292  0.0312  47  ALA   C O   
1404 C CB  . ALA   B 41  ? 0.3587 0.4156 0.5594 -0.0094 0.0123  0.0290  47  ALA   C CB  
1405 N N   . GLN   B 42  ? 0.3528 0.4094 0.5352 -0.0073 0.0366  0.0375  48  GLN   C N   
1406 C CA  . GLN   B 42  ? 0.3681 0.4194 0.5316 -0.0060 0.0422  0.0397  48  GLN   C CA  
1407 C C   . GLN   B 42  ? 0.3600 0.4031 0.5097 -0.0080 0.0341  0.0373  48  GLN   C C   
1408 O O   . GLN   B 42  ? 0.3746 0.4156 0.5323 -0.0117 0.0279  0.0369  48  GLN   C O   
1409 C CB  . GLN   B 42  ? 0.4058 0.4588 0.5783 -0.0076 0.0518  0.0455  48  GLN   C CB  
1410 C CG  . GLN   B 42  ? 0.4930 0.5395 0.6468 -0.0063 0.0569  0.0483  48  GLN   C CG  
1411 C CD  . GLN   B 42  ? 0.5998 0.6467 0.7382 -0.0007 0.0646  0.0489  48  GLN   C CD  
1412 O OE1 . GLN   B 42  ? 0.6270 0.6795 0.7699 0.0024  0.0684  0.0480  48  GLN   C OE1 
1413 N NE2 . GLN   B 42  ? 0.6324 0.6729 0.7521 0.0012  0.0667  0.0502  48  GLN   C NE2 
1414 N N   . GLY   B 43  ? 0.3264 0.3653 0.4560 -0.0052 0.0340  0.0355  49  GLY   C N   
1415 C CA  . GLY   B 43  ? 0.3151 0.3470 0.4309 -0.0063 0.0277  0.0334  49  GLY   C CA  
1416 C C   . GLY   B 43  ? 0.3027 0.3308 0.4107 -0.0066 0.0325  0.0365  49  GLY   C C   
1417 O O   . GLY   B 43  ? 0.3116 0.3411 0.4157 -0.0040 0.0408  0.0395  49  GLY   C O   
1418 N N   . CYS   B 44  ? 0.2850 0.3077 0.3896 -0.0091 0.0274  0.0358  50  CYS   C N   
1419 C CA  . CYS   B 44  ? 0.2843 0.3026 0.3826 -0.0093 0.0313  0.0389  50  CYS   C CA  
1420 C C   . CYS   B 44  ? 0.2737 0.2864 0.3538 -0.0076 0.0283  0.0365  50  CYS   C C   
1421 O O   . CYS   B 44  ? 0.2874 0.2954 0.3631 -0.0080 0.0294  0.0385  50  CYS   C O   
1422 C CB  . CYS   B 44  ? 0.3013 0.3177 0.4135 -0.0135 0.0295  0.0410  50  CYS   C CB  
1423 S SG  . CYS   B 44  ? 0.3819 0.4058 0.5189 -0.0158 0.0344  0.0446  50  CYS   C SG  
1424 N N   . ASP   B 45  ? 0.2313 0.2443 0.3021 -0.0058 0.0247  0.0325  51  ASP   C N   
1425 C CA  . ASP   B 45  ? 0.2259 0.2347 0.2814 -0.0042 0.0227  0.0304  51  ASP   C CA  
1426 C C   . ASP   B 45  ? 0.2503 0.2590 0.2963 -0.0005 0.0289  0.0323  51  ASP   C C   
1427 O O   . ASP   B 45  ? 0.2829 0.2951 0.3298 0.0018  0.0338  0.0336  51  ASP   C O   
1428 C CB  . ASP   B 45  ? 0.2472 0.2563 0.2968 -0.0037 0.0177  0.0260  51  ASP   C CB  
1429 C CG  . ASP   B 45  ? 0.3167 0.3240 0.3711 -0.0065 0.0109  0.0238  51  ASP   C CG  
1430 O OD1 . ASP   B 45  ? 0.3349 0.3396 0.3949 -0.0087 0.0087  0.0246  51  ASP   C OD1 
1431 O OD2 . ASP   B 45  ? 0.3006 0.3083 0.3528 -0.0062 0.0076  0.0213  51  ASP   C OD2 
1432 N N   . THR   B 46  ? 0.2397 0.2441 0.2759 0.0007  0.0284  0.0323  52  THR   C N   
1433 C CA  . THR   B 46  ? 0.2563 0.2595 0.2813 0.0049  0.0328  0.0337  52  THR   C CA  
1434 C C   . THR   B 46  ? 0.2383 0.2417 0.2531 0.0071  0.0289  0.0289  52  THR   C C   
1435 O O   . THR   B 46  ? 0.2410 0.2427 0.2543 0.0056  0.0242  0.0263  52  THR   C O   
1436 C CB  . THR   B 46  ? 0.3326 0.3303 0.3536 0.0051  0.0340  0.0368  52  THR   C CB  
1437 O OG1 . THR   B 46  ? 0.3663 0.3635 0.3979 0.0028  0.0384  0.0418  52  THR   C OG1 
1438 C CG2 . THR   B 46  ? 0.3491 0.3444 0.3561 0.0101  0.0366  0.0375  52  THR   C CG2 
1439 N N   . ILE   B 47  ? 0.2247 0.2301 0.2334 0.0106  0.0310  0.0276  53  ILE   C N   
1440 C CA  . ILE   B 47  ? 0.2146 0.2203 0.2154 0.0125  0.0273  0.0230  53  ILE   C CA  
1441 C C   . ILE   B 47  ? 0.2090 0.2115 0.1991 0.0160  0.0272  0.0229  53  ILE   C C   
1442 O O   . ILE   B 47  ? 0.2139 0.2144 0.1985 0.0192  0.0314  0.0261  53  ILE   C O   
1443 C CB  . ILE   B 47  ? 0.2357 0.2443 0.2351 0.0150  0.0285  0.0208  53  ILE   C CB  
1444 C CG1 . ILE   B 47  ? 0.2623 0.2741 0.2726 0.0125  0.0290  0.0213  53  ILE   C CG1 
1445 C CG2 . ILE   B 47  ? 0.2331 0.2418 0.2268 0.0162  0.0240  0.0158  53  ILE   C CG2 
1446 C CD1 . ILE   B 47  ? 0.2797 0.2912 0.2954 0.0084  0.0235  0.0193  53  ILE   C CD1 
1447 N N   . ALA   B 48  ? 0.1931 0.1948 0.1804 0.0156  0.0226  0.0196  54  ALA   C N   
1448 C CA  . ALA   B 48  ? 0.1968 0.1961 0.1751 0.0193  0.0213  0.0187  54  ALA   C CA  
1449 C C   . ALA   B 48  ? 0.1832 0.1834 0.1539 0.0238  0.0213  0.0163  54  ALA   C C   
1450 O O   . ALA   B 48  ? 0.1859 0.1890 0.1589 0.0234  0.0200  0.0131  54  ALA   C O   
1451 C CB  . ALA   B 48  ? 0.1881 0.1879 0.1677 0.0177  0.0165  0.0150  54  ALA   C CB  
1452 N N   . ARG   B 49  ? 0.1900 0.1868 0.1509 0.0285  0.0222  0.0177  55  ARG   C N   
1453 C CA  . ARG   B 49  ? 0.1911 0.1874 0.1422 0.0340  0.0212  0.0149  55  ARG   C CA  
1454 C C   . ARG   B 49  ? 0.1988 0.1927 0.1436 0.0370  0.0167  0.0129  55  ARG   C C   
1455 O O   . ARG   B 49  ? 0.2220 0.2112 0.1590 0.0402  0.0181  0.0164  55  ARG   C O   
1456 C CB  . ARG   B 49  ? 0.1881 0.1818 0.1317 0.0377  0.0273  0.0190  55  ARG   C CB  
1457 C CG  . ARG   B 49  ? 0.2143 0.2112 0.1670 0.0345  0.0322  0.0213  55  ARG   C CG  
1458 C CD  . ARG   B 49  ? 0.2303 0.2314 0.1879 0.0335  0.0295  0.0162  55  ARG   C CD  
1459 N NE  . ARG   B 49  ? 0.2290 0.2330 0.1954 0.0312  0.0341  0.0186  55  ARG   C NE  
1460 C CZ  . ARG   B 49  ? 0.2397 0.2470 0.2136 0.0290  0.0322  0.0156  55  ARG   C CZ  
1461 N NH1 . ARG   B 49  ? 0.2154 0.2233 0.1889 0.0285  0.0266  0.0106  55  ARG   C NH1 
1462 N NH2 . ARG   B 49  ? 0.2612 0.2712 0.2438 0.0273  0.0360  0.0179  55  ARG   C NH2 
1463 N N   . CYS   B 50  ? 0.1937 0.1909 0.1429 0.0358  0.0113  0.0076  56  CYS   C N   
1464 C CA  . CYS   B 50  ? 0.2032 0.1998 0.1508 0.0378  0.0067  0.0053  56  CYS   C CA  
1465 C C   . CYS   B 50  ? 0.2094 0.2108 0.1635 0.0366  0.0016  -0.0010 56  CYS   C C   
1466 O O   . CYS   B 50  ? 0.1972 0.2017 0.1570 0.0338  0.0018  -0.0031 56  CYS   C O   
1467 C CB  . CYS   B 50  ? 0.1950 0.1900 0.1474 0.0345  0.0080  0.0085  56  CYS   C CB  
1468 S SG  . CYS   B 50  ? 0.1925 0.1919 0.1578 0.0275  0.0078  0.0069  56  CYS   C SG  
1469 N N   . ASP   B 51  ? 0.2057 0.2077 0.1603 0.0386  -0.0029 -0.0038 57  ASP   C N   
1470 C CA  . ASP   B 51  ? 0.2105 0.2178 0.1740 0.0370  -0.0070 -0.0092 57  ASP   C CA  
1471 C C   . ASP   B 51  ? 0.2200 0.2292 0.1910 0.0340  -0.0068 -0.0091 57  ASP   C C   
1472 O O   . ASP   B 51  ? 0.2080 0.2211 0.1852 0.0343  -0.0101 -0.0132 57  ASP   C O   
1473 C CB  . ASP   B 51  ? 0.2453 0.2531 0.2052 0.0424  -0.0130 -0.0141 57  ASP   C CB  
1474 C CG  . ASP   B 51  ? 0.3065 0.3111 0.2597 0.0474  -0.0157 -0.0133 57  ASP   C CG  
1475 O OD1 . ASP   B 51  ? 0.3120 0.3133 0.2629 0.0467  -0.0125 -0.0086 57  ASP   C OD1 
1476 O OD2 . ASP   B 51  ? 0.3837 0.3887 0.3344 0.0522  -0.0218 -0.0177 57  ASP   C OD2 
1477 N N   . CYS   B 52  ? 0.2008 0.2075 0.1720 0.0311  -0.0029 -0.0048 58  CYS   C N   
1478 C CA  . CYS   B 52  ? 0.1931 0.2006 0.1699 0.0286  -0.0026 -0.0049 58  CYS   C CA  
1479 C C   . CYS   B 52  ? 0.1724 0.1854 0.1582 0.0252  -0.0029 -0.0086 58  CYS   C C   
1480 O O   . CYS   B 52  ? 0.1711 0.1859 0.1596 0.0226  -0.0020 -0.0091 58  CYS   C O   
1481 C CB  . CYS   B 52  ? 0.1867 0.1904 0.1629 0.0255  0.0011  -0.0004 58  CYS   C CB  
1482 S SG  . CYS   B 52  ? 0.2130 0.2096 0.1814 0.0288  0.0021  0.0045  58  CYS   C SG  
1483 N N   . GLN   B 53  ? 0.1595 0.1748 0.1501 0.0252  -0.0038 -0.0106 59  GLN   C N   
1484 C CA  . GLN   B 53  ? 0.1548 0.1748 0.1540 0.0219  -0.0026 -0.0132 59  GLN   C CA  
1485 C C   . GLN   B 53  ? 0.1628 0.1813 0.1626 0.0202  -0.0001 -0.0120 59  GLN   C C   
1486 O O   . GLN   B 53  ? 0.1664 0.1886 0.1724 0.0186  0.0013  -0.0142 59  GLN   C O   
1487 C CB  . GLN   B 53  ? 0.1647 0.1905 0.1715 0.0238  -0.0057 -0.0181 59  GLN   C CB  
1488 C CG  . GLN   B 53  ? 0.1664 0.1941 0.1746 0.0242  -0.0084 -0.0204 59  GLN   C CG  
1489 C CD  . GLN   B 53  ? 0.2043 0.2380 0.2221 0.0257  -0.0123 -0.0256 59  GLN   C CD  
1490 O OE1 . GLN   B 53  ? 0.2228 0.2565 0.2385 0.0304  -0.0174 -0.0282 59  GLN   C OE1 
1491 N NE2 . GLN   B 53  ? 0.1855 0.2240 0.2141 0.0219  -0.0097 -0.0270 59  GLN   C NE2 
1492 N N   . THR   B 54  ? 0.1660 0.1788 0.1598 0.0206  0.0006  -0.0087 60  THR   C N   
1493 C CA  . THR   B 54  ? 0.1694 0.1795 0.1629 0.0189  0.0024  -0.0079 60  THR   C CA  
1494 C C   . THR   B 54  ? 0.1701 0.1751 0.1596 0.0165  0.0035  -0.0041 60  THR   C C   
1495 O O   . THR   B 54  ? 0.1885 0.1913 0.1751 0.0174  0.0032  -0.0015 60  THR   C O   
1496 C CB  . THR   B 54  ? 0.2325 0.2406 0.2250 0.0224  0.0010  -0.0088 60  THR   C CB  
1497 O OG1 . THR   B 54  ? 0.2826 0.2859 0.2696 0.0251  -0.0006 -0.0061 60  THR   C OG1 
1498 C CG2 . THR   B 54  ? 0.2405 0.2543 0.2386 0.0252  -0.0004 -0.0129 60  THR   C CG2 
1499 N N   . GLY   B 55  ? 0.1586 0.1617 0.1483 0.0137  0.0048  -0.0038 61  GLY   C N   
1500 C CA  . GLY   B 55  ? 0.1634 0.1620 0.1512 0.0113  0.0049  -0.0007 61  GLY   C CA  
1501 C C   . GLY   B 55  ? 0.1549 0.1511 0.1417 0.0091  0.0052  -0.0015 61  GLY   C C   
1502 O O   . GLY   B 55  ? 0.1895 0.1865 0.1757 0.0100  0.0058  -0.0040 61  GLY   C O   
1503 N N   . VAL   B 56  ? 0.1513 0.1441 0.1377 0.0067  0.0045  0.0006  62  VAL   C N   
1504 C CA  . VAL   B 56  ? 0.1607 0.1499 0.1446 0.0051  0.0036  -0.0002 62  VAL   C CA  
1505 C C   . VAL   B 56  ? 0.1726 0.1623 0.1573 0.0025  0.0034  0.0011  62  VAL   C C   
1506 O O   . VAL   B 56  ? 0.1645 0.1549 0.1526 0.0016  0.0030  0.0033  62  VAL   C O   
1507 C CB  . VAL   B 56  ? 0.1763 0.1593 0.1597 0.0052  0.0011  0.0005  62  VAL   C CB  
1508 C CG1 . VAL   B 56  ? 0.1989 0.1770 0.1787 0.0040  -0.0012 -0.0009 62  VAL   C CG1 
1509 C CG2 . VAL   B 56  ? 0.1883 0.1698 0.1706 0.0082  0.0010  -0.0007 62  VAL   C CG2 
1510 N N   . TYR   B 57  ? 0.1744 0.1633 0.1556 0.0016  0.0039  -0.0001 63  TYR   C N   
1511 C CA  . TYR   B 57  ? 0.1604 0.1485 0.1417 -0.0006 0.0030  0.0014  63  TYR   C CA  
1512 C C   . TYR   B 57  ? 0.1785 0.1605 0.1544 -0.0011 0.0003  0.0010  63  TYR   C C   
1513 O O   . TYR   B 57  ? 0.1782 0.1570 0.1486 0.0003  0.0002  -0.0009 63  TYR   C O   
1514 C CB  . TYR   B 57  ? 0.1682 0.1600 0.1501 -0.0014 0.0057  0.0013  63  TYR   C CB  
1515 C CG  . TYR   B 57  ? 0.1759 0.1663 0.1525 -0.0013 0.0080  0.0001  63  TYR   C CG  
1516 C CD1 . TYR   B 57  ? 0.1906 0.1834 0.1673 0.0003  0.0106  -0.0019 63  TYR   C CD1 
1517 C CD2 . TYR   B 57  ? 0.1751 0.1620 0.1472 -0.0026 0.0080  0.0013  63  TYR   C CD2 
1518 C CE1 . TYR   B 57  ? 0.2090 0.2012 0.1817 0.0004  0.0141  -0.0027 63  TYR   C CE1 
1519 C CE2 . TYR   B 57  ? 0.1946 0.1798 0.1610 -0.0024 0.0113  0.0009  63  TYR   C CE2 
1520 C CZ  . TYR   B 57  ? 0.2132 0.2013 0.1801 -0.0009 0.0147  -0.0011 63  TYR   C CZ  
1521 O OH  . TYR   B 57  ? 0.2410 0.2280 0.2030 -0.0005 0.0192  -0.0012 63  TYR   C OH  
1522 N N   . TYR   B 58  ? 0.1823 0.1628 0.1596 -0.0026 -0.0023 0.0025  64  TYR   C N   
1523 C CA  . TYR   B 58  ? 0.1825 0.1568 0.1542 -0.0027 -0.0060 0.0018  64  TYR   C CA  
1524 C C   . TYR   B 58  ? 0.1911 0.1640 0.1559 -0.0027 -0.0044 0.0021  64  TYR   C C   
1525 O O   . TYR   B 58  ? 0.1890 0.1644 0.1566 -0.0039 -0.0031 0.0038  64  TYR   C O   
1526 C CB  . TYR   B 58  ? 0.1968 0.1698 0.1746 -0.0040 -0.0106 0.0030  64  TYR   C CB  
1527 C CG  . TYR   B 58  ? 0.2279 0.1941 0.1998 -0.0037 -0.0158 0.0017  64  TYR   C CG  
1528 C CD1 . TYR   B 58  ? 0.2431 0.2038 0.2096 -0.0024 -0.0185 -0.0008 64  TYR   C CD1 
1529 C CD2 . TYR   B 58  ? 0.2590 0.2234 0.2292 -0.0041 -0.0185 0.0027  64  TYR   C CD2 
1530 C CE1 . TYR   B 58  ? 0.2738 0.2273 0.2329 -0.0013 -0.0241 -0.0026 64  TYR   C CE1 
1531 C CE2 . TYR   B 58  ? 0.2664 0.2237 0.2295 -0.0030 -0.0242 0.0012  64  TYR   C CE2 
1532 C CZ  . TYR   B 58  ? 0.2816 0.2335 0.2389 -0.0016 -0.0271 -0.0015 64  TYR   C CZ  
1533 O OH  . TYR   B 58  ? 0.3178 0.2618 0.2664 0.0000  -0.0335 -0.0036 64  TYR   C OH  
1534 N N   . CYS   B 59  ? 0.2002 0.1678 0.1549 -0.0012 -0.0045 0.0006  65  CYS   C N   
1535 C CA  . CYS   B 59  ? 0.2017 0.1664 0.1478 -0.0010 -0.0022 0.0015  65  CYS   C CA  
1536 C C   . CYS   B 59  ? 0.2232 0.1794 0.1601 0.0001  -0.0078 0.0012  65  CYS   C C   
1537 O O   . CYS   B 59  ? 0.2466 0.1973 0.1753 0.0022  -0.0099 -0.0011 65  CYS   C O   
1538 C CB  . CYS   B 59  ? 0.2130 0.1785 0.1541 0.0005  0.0034  0.0002  65  CYS   C CB  
1539 S SG  . CYS   B 59  ? 0.2509 0.2116 0.1797 0.0011  0.0078  0.0018  65  CYS   C SG  
1540 N N   . SER   B 60  ? 0.2312 0.1862 0.1695 -0.0010 -0.0106 0.0033  66  SER   C N   
1541 C CA  . SER   B 60  ? 0.2709 0.2181 0.2016 0.0004  -0.0173 0.0028  66  SER   C CA  
1542 C C   . SER   B 60  ? 0.2868 0.2262 0.2007 0.0029  -0.0160 0.0025  66  SER   C C   
1543 O O   . SER   B 60  ? 0.3028 0.2349 0.2076 0.0052  -0.0216 0.0003  66  SER   C O   
1544 C CB  . SER   B 60  ? 0.3348 0.2827 0.2714 -0.0008 -0.0207 0.0050  66  SER   C CB  
1545 O OG  . SER   B 60  ? 0.4451 0.3937 0.3793 -0.0015 -0.0161 0.0077  66  SER   C OG  
1546 N N   . SER   B 61  ? 0.2720 0.2128 0.1815 0.0027  -0.0085 0.0044  67  SER   C N   
1547 C CA  . SER   B 61  ? 0.2875 0.2208 0.1801 0.0052  -0.0055 0.0049  67  SER   C CA  
1548 C C   . SER   B 61  ? 0.3024 0.2336 0.1876 0.0079  -0.0038 0.0015  67  SER   C C   
1549 O O   . SER   B 61  ? 0.3181 0.2422 0.1875 0.0109  -0.0013 0.0015  67  SER   C O   
1550 C CB  . SER   B 61  ? 0.2846 0.2200 0.1765 0.0038  0.0027  0.0084  67  SER   C CB  
1551 O OG  . SER   B 61  ? 0.2783 0.2225 0.1804 0.0023  0.0089  0.0076  67  SER   C OG  
1552 N N   . ARG   B 62  ? 0.2740 0.2100 0.1690 0.0074  -0.0052 -0.0013 68  ARG   C N   
1553 C CA  . ARG   B 62  ? 0.2733 0.2065 0.1624 0.0103  -0.0052 -0.0050 68  ARG   C CA  
1554 C C   . ARG   B 62  ? 0.2796 0.2103 0.1737 0.0104  -0.0140 -0.0080 68  ARG   C C   
1555 O O   . ARG   B 62  ? 0.2984 0.2259 0.1888 0.0127  -0.0152 -0.0116 68  ARG   C O   
1556 C CB  . ARG   B 62  ? 0.2851 0.2264 0.1821 0.0099  0.0021  -0.0056 68  ARG   C CB  
1557 C CG  . ARG   B 62  ? 0.3076 0.2519 0.2018 0.0096  0.0111  -0.0032 68  ARG   C CG  
1558 C CD  . ARG   B 62  ? 0.3245 0.2616 0.2017 0.0135  0.0148  -0.0043 68  ARG   C CD  
1559 N NE  . ARG   B 62  ? 0.3646 0.3050 0.2407 0.0129  0.0245  -0.0015 68  ARG   C NE  
1560 C CZ  . ARG   B 62  ? 0.3919 0.3283 0.2608 0.0121  0.0273  0.0025  68  ARG   C CZ  
1561 N NH1 . ARG   B 62  ? 0.3919 0.3210 0.2534 0.0121  0.0205  0.0039  68  ARG   C NH1 
1562 N NH2 . ARG   B 62  ? 0.3881 0.3275 0.2576 0.0113  0.0369  0.0052  68  ARG   C NH2 
1563 N N   . ARG   B 63  ? 0.2829 0.2152 0.1867 0.0080  -0.0195 -0.0066 69  ARG   C N   
1564 C CA  . ARG   B 63  ? 0.3031 0.2345 0.2159 0.0071  -0.0269 -0.0088 69  ARG   C CA  
1565 C C   . ARG   B 63  ? 0.3176 0.2530 0.2381 0.0069  -0.0243 -0.0103 69  ARG   C C   
1566 O O   . ARG   B 63  ? 0.3343 0.2651 0.2545 0.0080  -0.0288 -0.0134 69  ARG   C O   
1567 C CB  . ARG   B 63  ? 0.3447 0.2657 0.2465 0.0099  -0.0352 -0.0121 69  ARG   C CB  
1568 C CG  . ARG   B 63  ? 0.4114 0.3286 0.3093 0.0100  -0.0405 -0.0106 69  ARG   C CG  
1569 C CD  . ARG   B 63  ? 0.5076 0.4149 0.3971 0.0128  -0.0505 -0.0146 69  ARG   C CD  
1570 N NE  . ARG   B 63  ? 0.5968 0.4976 0.4748 0.0148  -0.0550 -0.0136 69  ARG   C NE  
1571 C CZ  . ARG   B 63  ? 0.6839 0.5740 0.5417 0.0194  -0.0582 -0.0158 69  ARG   C CZ  
1572 N NH1 . ARG   B 63  ? 0.7016 0.5867 0.5487 0.0223  -0.0570 -0.0195 69  ARG   C NH1 
1573 N NH2 . ARG   B 63  ? 0.6986 0.5824 0.5456 0.0214  -0.0624 -0.0142 69  ARG   C NH2 
1574 N N   . LYS   B 64  ? 0.2905 0.2338 0.2172 0.0057  -0.0171 -0.0083 70  LYS   C N   
1575 C CA  . LYS   B 64  ? 0.2862 0.2325 0.2182 0.0063  -0.0145 -0.0098 70  LYS   C CA  
1576 C C   . LYS   B 64  ? 0.2529 0.2081 0.1967 0.0041  -0.0105 -0.0071 70  LYS   C C   
1577 O O   . LYS   B 64  ? 0.2414 0.2008 0.1869 0.0027  -0.0075 -0.0048 70  LYS   C O   
1578 C CB  . LYS   B 64  ? 0.3517 0.2976 0.2743 0.0093  -0.0087 -0.0116 70  LYS   C CB  
1579 C CG  . LYS   B 64  ? 0.4949 0.4323 0.4056 0.0129  -0.0113 -0.0156 70  LYS   C CG  
1580 C CD  . LYS   B 64  ? 0.5918 0.5313 0.4968 0.0157  -0.0038 -0.0170 70  LYS   C CD  
1581 C CE  . LYS   B 64  ? 0.6824 0.6146 0.5773 0.0200  -0.0053 -0.0216 70  LYS   C CE  
1582 N NZ  . LYS   B 64  ? 0.7331 0.6570 0.6108 0.0229  -0.0059 -0.0228 70  LYS   C NZ  
1583 N N   . HIS   B 65  ? 0.2279 0.1852 0.1786 0.0042  -0.0104 -0.0076 71  HIS   C N   
1584 C CA  . HIS   B 65  ? 0.2139 0.1787 0.1731 0.0034  -0.0065 -0.0056 71  HIS   C CA  
1585 C C   . HIS   B 65  ? 0.2348 0.2024 0.1916 0.0057  -0.0018 -0.0073 71  HIS   C C   
1586 O O   . HIS   B 65  ? 0.2687 0.2323 0.2205 0.0082  -0.0023 -0.0101 71  HIS   C O   
1587 C CB  . HIS   B 65  ? 0.2100 0.1745 0.1775 0.0026  -0.0089 -0.0045 71  HIS   C CB  
1588 C CG  . HIS   B 65  ? 0.2264 0.1898 0.1998 0.0001  -0.0128 -0.0027 71  HIS   C CG  
1589 N ND1 . HIS   B 65  ? 0.2485 0.2172 0.2294 -0.0017 -0.0111 0.0004  71  HIS   C ND1 
1590 C CD2 . HIS   B 65  ? 0.2352 0.1927 0.2085 -0.0006 -0.0184 -0.0038 71  HIS   C CD2 
1591 C CE1 . HIS   B 65  ? 0.2416 0.2082 0.2278 -0.0035 -0.0152 0.0012  71  HIS   C CE1 
1592 N NE2 . HIS   B 65  ? 0.2729 0.2329 0.2553 -0.0030 -0.0200 -0.0013 71  HIS   C NE2 
1593 N N   . TYR   B 66  ? 0.2036 0.1782 0.1650 0.0051  0.0023  -0.0062 72  TYR   C N   
1594 C CA  . TYR   B 66  ? 0.1927 0.1714 0.1547 0.0073  0.0064  -0.0080 72  TYR   C CA  
1595 C C   . TYR   B 66  ? 0.1893 0.1739 0.1597 0.0075  0.0070  -0.0073 72  TYR   C C   
1596 O O   . TYR   B 66  ? 0.1919 0.1798 0.1666 0.0057  0.0069  -0.0052 72  TYR   C O   
1597 C CB  . TYR   B 66  ? 0.2125 0.1944 0.1726 0.0065  0.0110  -0.0077 72  TYR   C CB  
1598 C CG  . TYR   B 66  ? 0.2421 0.2181 0.1915 0.0073  0.0119  -0.0083 72  TYR   C CG  
1599 C CD1 . TYR   B 66  ? 0.2608 0.2341 0.2040 0.0104  0.0139  -0.0111 72  TYR   C CD1 
1600 C CD2 . TYR   B 66  ? 0.2549 0.2276 0.1995 0.0055  0.0111  -0.0062 72  TYR   C CD2 
1601 C CE1 . TYR   B 66  ? 0.2822 0.2493 0.2134 0.0118  0.0151  -0.0117 72  TYR   C CE1 
1602 C CE2 . TYR   B 66  ? 0.2750 0.2412 0.2077 0.0068  0.0117  -0.0066 72  TYR   C CE2 
1603 C CZ  . TYR   B 66  ? 0.3052 0.2686 0.2307 0.0100  0.0141  -0.0093 72  TYR   C CZ  
1604 O OH  . TYR   B 66  ? 0.3393 0.2955 0.2508 0.0120  0.0151  -0.0096 72  TYR   C OH  
1605 N N   . PRO   B 67  ? 0.1810 0.1666 0.1529 0.0103  0.0074  -0.0092 73  PRO   C N   
1606 C CA  . PRO   B 67  ? 0.1842 0.1748 0.1623 0.0113  0.0076  -0.0088 73  PRO   C CA  
1607 C C   . PRO   B 67  ? 0.1995 0.1975 0.1820 0.0113  0.0110  -0.0100 73  PRO   C C   
1608 O O   . PRO   B 67  ? 0.2184 0.2176 0.1997 0.0119  0.0141  -0.0118 73  PRO   C O   
1609 C CB  . PRO   B 67  ? 0.1885 0.1764 0.1661 0.0147  0.0062  -0.0105 73  PRO   C CB  
1610 C CG  . PRO   B 67  ? 0.2039 0.1886 0.1762 0.0159  0.0075  -0.0132 73  PRO   C CG  
1611 C CD  . PRO   B 67  ? 0.1931 0.1744 0.1602 0.0131  0.0073  -0.0120 73  PRO   C CD  
1612 N N   . VAL   B 68  ? 0.1854 0.1880 0.1729 0.0105  0.0106  -0.0090 74  VAL   C N   
1613 C CA  . VAL   B 68  ? 0.1862 0.1957 0.1798 0.0100  0.0130  -0.0105 74  VAL   C CA  
1614 C C   . VAL   B 68  ? 0.1660 0.1797 0.1649 0.0119  0.0108  -0.0114 74  VAL   C C   
1615 O O   . VAL   B 68  ? 0.1833 0.1947 0.1800 0.0126  0.0082  -0.0097 74  VAL   C O   
1616 C CB  . VAL   B 68  ? 0.2222 0.2320 0.2159 0.0064  0.0143  -0.0087 74  VAL   C CB  
1617 C CG1 . VAL   B 68  ? 0.2683 0.2747 0.2567 0.0050  0.0173  -0.0081 74  VAL   C CG1 
1618 C CG2 . VAL   B 68  ? 0.2264 0.2334 0.2184 0.0053  0.0115  -0.0062 74  VAL   C CG2 
1619 N N   . SER   B 69  ? 0.1595 0.1796 0.1657 0.0128  0.0119  -0.0141 75  SER   C N   
1620 C CA  . SER   B 69  ? 0.1585 0.1831 0.1702 0.0141  0.0091  -0.0155 75  SER   C CA  
1621 C C   . SER   B 69  ? 0.1528 0.1793 0.1677 0.0104  0.0103  -0.0148 75  SER   C C   
1622 O O   . SER   B 69  ? 0.1754 0.2023 0.1917 0.0075  0.0140  -0.0143 75  SER   C O   
1623 C CB  . SER   B 69  ? 0.1899 0.2210 0.2103 0.0166  0.0090  -0.0193 75  SER   C CB  
1624 O OG  . SER   B 69  ? 0.2564 0.2851 0.2739 0.0203  0.0077  -0.0199 75  SER   C OG  
1625 N N   . PHE   B 70  ? 0.1478 0.1749 0.1632 0.0108  0.0074  -0.0149 76  PHE   C N   
1626 C CA  . PHE   B 70  ? 0.1508 0.1789 0.1693 0.0077  0.0079  -0.0147 76  PHE   C CA  
1627 C C   . PHE   B 70  ? 0.1528 0.1847 0.1767 0.0094  0.0043  -0.0177 76  PHE   C C   
1628 O O   . PHE   B 70  ? 0.1680 0.2001 0.1899 0.0133  0.0008  -0.0191 76  PHE   C O   
1629 C CB  . PHE   B 70  ? 0.1549 0.1776 0.1664 0.0059  0.0083  -0.0112 76  PHE   C CB  
1630 C CG  . PHE   B 70  ? 0.1576 0.1770 0.1629 0.0084  0.0061  -0.0096 76  PHE   C CG  
1631 C CD1 . PHE   B 70  ? 0.1662 0.1819 0.1666 0.0093  0.0064  -0.0076 76  PHE   C CD1 
1632 C CD2 . PHE   B 70  ? 0.1671 0.1868 0.1716 0.0098  0.0040  -0.0099 76  PHE   C CD2 
1633 C CE1 . PHE   B 70  ? 0.1746 0.1870 0.1705 0.0111  0.0052  -0.0054 76  PHE   C CE1 
1634 C CE2 . PHE   B 70  ? 0.1612 0.1778 0.1597 0.0122  0.0033  -0.0078 76  PHE   C CE2 
1635 C CZ  . PHE   B 70  ? 0.1620 0.1751 0.1568 0.0126  0.0041  -0.0052 76  PHE   C CZ  
1636 N N   . SER   B 71  ? 0.1359 0.1699 0.1663 0.0068  0.0045  -0.0189 77  SER   C N   
1637 C CA  . SER   B 71  ? 0.1498 0.1873 0.1865 0.0083  0.0003  -0.0227 77  SER   C CA  
1638 C C   . SER   B 71  ? 0.1720 0.2059 0.2011 0.0107  -0.0031 -0.0225 77  SER   C C   
1639 O O   . SER   B 71  ? 0.1839 0.2132 0.2042 0.0108  -0.0016 -0.0191 77  SER   C O   
1640 C CB  . SER   B 71  ? 0.1559 0.1962 0.2031 0.0042  0.0019  -0.0240 77  SER   C CB  
1641 O OG  . SER   B 71  ? 0.1804 0.2162 0.2235 0.0014  0.0036  -0.0212 77  SER   C OG  
1642 N N   . LYS   B 72  ? 0.1769 0.2128 0.2096 0.0128  -0.0077 -0.0265 78  LYS   C N   
1643 C CA  . LYS   B 72  ? 0.1880 0.2202 0.2129 0.0155  -0.0104 -0.0268 78  LYS   C CA  
1644 C C   . LYS   B 72  ? 0.1856 0.2158 0.2125 0.0118  -0.0086 -0.0259 78  LYS   C C   
1645 O O   . LYS   B 72  ? 0.2192 0.2517 0.2557 0.0078  -0.0073 -0.0267 78  LYS   C O   
1646 C CB  . LYS   B 72  ? 0.2370 0.2713 0.2644 0.0196  -0.0168 -0.0322 78  LYS   C CB  
1647 C CG  . LYS   B 72  ? 0.3154 0.3509 0.3400 0.0239  -0.0191 -0.0328 78  LYS   C CG  
1648 C CD  . LYS   B 72  ? 0.4631 0.4970 0.4815 0.0302  -0.0258 -0.0364 78  LYS   C CD  
1649 C CE  . LYS   B 72  ? 0.5671 0.5987 0.5767 0.0350  -0.0268 -0.0346 78  LYS   C CE  
1650 N NZ  . LYS   B 72  ? 0.6365 0.6618 0.6305 0.0405  -0.0288 -0.0334 78  LYS   C NZ  
1651 N N   . PRO   B 73  ? 0.1816 0.2078 0.2003 0.0132  -0.0084 -0.0242 79  PRO   C N   
1652 C CA  . PRO   B 73  ? 0.1850 0.2091 0.2059 0.0103  -0.0072 -0.0236 79  PRO   C CA  
1653 C C   . PRO   B 73  ? 0.2065 0.2322 0.2362 0.0095  -0.0109 -0.0284 79  PRO   C C   
1654 O O   . PRO   B 73  ? 0.2222 0.2488 0.2517 0.0132  -0.0158 -0.0329 79  PRO   C O   
1655 C CB  . PRO   B 73  ? 0.2120 0.2324 0.2232 0.0135  -0.0071 -0.0221 79  PRO   C CB  
1656 C CG  . PRO   B 73  ? 0.2367 0.2566 0.2403 0.0165  -0.0060 -0.0197 79  PRO   C CG  
1657 C CD  . PRO   B 73  ? 0.1951 0.2182 0.2025 0.0176  -0.0086 -0.0224 79  PRO   C CD  
1658 N N   . SER   B 74  ? 0.1973 0.2228 0.2347 0.0047  -0.0087 -0.0275 80  SER   C N   
1659 C CA  . SER   B 74  ? 0.2133 0.2402 0.2616 0.0030  -0.0118 -0.0318 80  SER   C CA  
1660 C C   . SER   B 74  ? 0.2008 0.2244 0.2539 -0.0016 -0.0093 -0.0297 80  SER   C C   
1661 O O   . SER   B 74  ? 0.1824 0.2027 0.2295 -0.0030 -0.0055 -0.0250 80  SER   C O   
1662 C CB  . SER   B 74  ? 0.2909 0.3236 0.3497 0.0020  -0.0125 -0.0341 80  SER   C CB  
1663 O OG  . SER   B 74  ? 0.3653 0.3992 0.4287 -0.0025 -0.0066 -0.0303 80  SER   C OG  
1664 N N   . LEU   B 75  ? 0.2060 0.2298 0.2696 -0.0034 -0.0122 -0.0334 81  LEU   C N   
1665 C CA  . LEU   B 75  ? 0.2246 0.2445 0.2940 -0.0078 -0.0104 -0.0317 81  LEU   C CA  
1666 C C   . LEU   B 75  ? 0.2260 0.2485 0.3047 -0.0129 -0.0053 -0.0287 81  LEU   C C   
1667 O O   . LEU   B 75  ? 0.2354 0.2630 0.3259 -0.0140 -0.0065 -0.0319 81  LEU   C O   
1668 C CB  . LEU   B 75  ? 0.2531 0.2718 0.3311 -0.0074 -0.0162 -0.0376 81  LEU   C CB  
1669 C CG  . LEU   B 75  ? 0.3230 0.3356 0.3967 -0.0055 -0.0193 -0.0395 81  LEU   C CG  
1670 C CD1 . LEU   B 75  ? 0.3429 0.3542 0.4297 -0.0075 -0.0241 -0.0447 81  LEU   C CD1 
1671 C CD2 . LEU   B 75  ? 0.3385 0.3461 0.4074 -0.0077 -0.0150 -0.0340 81  LEU   C CD2 
1672 N N   . ILE   B 76  ? 0.2081 0.2270 0.2821 -0.0157 0.0002  -0.0230 82  ILE   C N   
1673 C CA  . ILE   B 76  ? 0.2349 0.2550 0.3138 -0.0198 0.0063  -0.0192 82  ILE   C CA  
1674 C C   . ILE   B 76  ? 0.2529 0.2664 0.3325 -0.0237 0.0095  -0.0150 82  ILE   C C   
1675 O O   . ILE   B 76  ? 0.2400 0.2477 0.3103 -0.0227 0.0087  -0.0127 82  ILE   C O   
1676 C CB  . ILE   B 76  ? 0.2663 0.2873 0.3342 -0.0179 0.0096  -0.0160 82  ILE   C CB  
1677 C CG1 . ILE   B 76  ? 0.2979 0.3248 0.3657 -0.0140 0.0064  -0.0199 82  ILE   C CG1 
1678 C CG2 . ILE   B 76  ? 0.2853 0.3059 0.3539 -0.0213 0.0165  -0.0116 82  ILE   C CG2 
1679 C CD1 . ILE   B 76  ? 0.3412 0.3688 0.3999 -0.0119 0.0084  -0.0177 82  ILE   C CD1 
1680 N N   . PHE   B 77  ? 0.2587 0.2727 0.3495 -0.0281 0.0133  -0.0138 83  PHE   C N   
1681 C CA  . PHE   B 77  ? 0.2791 0.2857 0.3702 -0.0319 0.0167  -0.0092 83  PHE   C CA  
1682 C C   . PHE   B 77  ? 0.2962 0.2981 0.3734 -0.0318 0.0218  -0.0029 83  PHE   C C   
1683 O O   . PHE   B 77  ? 0.3083 0.3135 0.3818 -0.0314 0.0259  -0.0013 83  PHE   C O   
1684 C CB  . PHE   B 77  ? 0.2897 0.2982 0.3973 -0.0369 0.0206  -0.0089 83  PHE   C CB  
1685 C CG  . PHE   B 77  ? 0.3165 0.3163 0.4249 -0.0410 0.0244  -0.0036 83  PHE   C CG  
1686 C CD1 . PHE   B 77  ? 0.3419 0.3355 0.4534 -0.0416 0.0196  -0.0051 83  PHE   C CD1 
1687 C CD2 . PHE   B 77  ? 0.3466 0.3432 0.4501 -0.0434 0.0326  0.0030  83  PHE   C CD2 
1688 C CE1 . PHE   B 77  ? 0.3696 0.3540 0.4810 -0.0450 0.0229  0.0002  83  PHE   C CE1 
1689 C CE2 . PHE   B 77  ? 0.3646 0.3519 0.4671 -0.0468 0.0362  0.0085  83  PHE   C CE2 
1690 C CZ  . PHE   B 77  ? 0.3716 0.3528 0.4784 -0.0477 0.0312  0.0072  83  PHE   C CZ  
1691 N N   . VAL   B 78  ? 0.2897 0.2833 0.3587 -0.0317 0.0209  0.0003  84  VAL   C N   
1692 C CA  . VAL   B 78  ? 0.2936 0.2815 0.3489 -0.0313 0.0243  0.0060  84  VAL   C CA  
1693 C C   . VAL   B 78  ? 0.3010 0.2799 0.3562 -0.0345 0.0270  0.0109  84  VAL   C C   
1694 O O   . VAL   B 78  ? 0.2935 0.2679 0.3526 -0.0349 0.0233  0.0099  84  VAL   C O   
1695 C CB  . VAL   B 78  ? 0.2888 0.2753 0.3330 -0.0271 0.0195  0.0053  84  VAL   C CB  
1696 C CG1 . VAL   B 78  ? 0.2945 0.2745 0.3254 -0.0266 0.0217  0.0106  84  VAL   C CG1 
1697 C CG2 . VAL   B 78  ? 0.2718 0.2661 0.3156 -0.0241 0.0175  0.0013  84  VAL   C CG2 
1698 N N   . GLU   B 79  ? 0.3271 0.3024 0.3765 -0.0363 0.0336  0.0162  85  GLU   C N   
1699 C CA  . GLU   B 79  ? 0.3488 0.3144 0.3955 -0.0390 0.0372  0.0221  85  GLU   C CA  
1700 C C   . GLU   B 79  ? 0.3409 0.2975 0.3771 -0.0368 0.0325  0.0243  85  GLU   C C   
1701 O O   . GLU   B 79  ? 0.3234 0.2810 0.3507 -0.0331 0.0283  0.0229  85  GLU   C O   
1702 C CB  . GLU   B 79  ? 0.4244 0.3875 0.4619 -0.0397 0.0452  0.0275  85  GLU   C CB  
1703 C CG  . GLU   B 79  ? 0.5458 0.5185 0.5920 -0.0409 0.0505  0.0254  85  GLU   C CG  
1704 C CD  . GLU   B 79  ? 0.7055 0.6833 0.7424 -0.0370 0.0497  0.0232  85  GLU   C CD  
1705 O OE1 . GLU   B 79  ? 0.7371 0.7164 0.7695 -0.0339 0.0428  0.0199  85  GLU   C OE1 
1706 O OE2 . GLU   B 79  ? 0.7604 0.7408 0.7952 -0.0371 0.0563  0.0247  85  GLU   C OE2 
1707 N N   . ALA   B 80  ? 0.3405 0.2879 0.3782 -0.0391 0.0332  0.0280  86  ALA   C N   
1708 C CA  . ALA   B 80  ? 0.3420 0.2804 0.3702 -0.0366 0.0285  0.0302  86  ALA   C CA  
1709 C C   . ALA   B 80  ? 0.3413 0.2755 0.3519 -0.0338 0.0293  0.0343  86  ALA   C C   
1710 O O   . ALA   B 80  ? 0.3537 0.2875 0.3579 -0.0346 0.0354  0.0375  86  ALA   C O   
1711 C CB  . ALA   B 80  ? 0.3510 0.2789 0.3826 -0.0396 0.0302  0.0346  86  ALA   C CB  
1712 N N   . SER   B 81  ? 0.3132 0.2446 0.3168 -0.0301 0.0230  0.0336  87  SER   C N   
1713 C CA  . SER   B 81  ? 0.3074 0.2335 0.2953 -0.0270 0.0216  0.0368  87  SER   C CA  
1714 C C   . SER   B 81  ? 0.3212 0.2385 0.3058 -0.0249 0.0158  0.0385  87  SER   C C   
1715 O O   . SER   B 81  ? 0.3225 0.2382 0.3169 -0.0259 0.0138  0.0372  87  SER   C O   
1716 C CB  . SER   B 81  ? 0.2923 0.2271 0.2782 -0.0242 0.0185  0.0326  87  SER   C CB  
1717 O OG  . SER   B 81  ? 0.2782 0.2177 0.2721 -0.0225 0.0130  0.0280  87  SER   C OG  
1718 N N   . GLU   B 82  ? 0.3348 0.2464 0.3064 -0.0216 0.0124  0.0411  88  GLU   C N   
1719 C CA  . GLU   B 82  ? 0.3563 0.2609 0.3257 -0.0189 0.0060  0.0421  88  GLU   C CA  
1720 C C   . GLU   B 82  ? 0.3478 0.2607 0.3287 -0.0170 0.0008  0.0362  88  GLU   C C   
1721 O O   . GLU   B 82  ? 0.3673 0.2761 0.3516 -0.0152 -0.0036 0.0358  88  GLU   C O   
1722 C CB  . GLU   B 82  ? 0.4351 0.3342 0.3899 -0.0151 0.0019  0.0446  88  GLU   C CB  
1723 C CG  . GLU   B 82  ? 0.5543 0.4420 0.4932 -0.0151 0.0055  0.0510  88  GLU   C CG  
1724 C CD  . GLU   B 82  ? 0.6988 0.5839 0.6242 -0.0110 0.0003  0.0511  88  GLU   C CD  
1725 O OE1 . GLU   B 82  ? 0.7511 0.6441 0.6761 -0.0106 0.0009  0.0479  88  GLU   C OE1 
1726 O OE2 . GLU   B 82  ? 0.7082 0.5838 0.6248 -0.0078 -0.0052 0.0539  88  GLU   C OE2 
1727 N N   . TYR   B 83  ? 0.3230 0.2469 0.3089 -0.0170 0.0015  0.0317  89  TYR   C N   
1728 C CA  . TYR   B 83  ? 0.3141 0.2458 0.3085 -0.0148 -0.0024 0.0266  89  TYR   C CA  
1729 C C   . TYR   B 83  ? 0.3076 0.2435 0.3138 -0.0161 -0.0015 0.0226  89  TYR   C C   
1730 O O   . TYR   B 83  ? 0.3344 0.2733 0.3465 -0.0136 -0.0050 0.0190  89  TYR   C O   
1731 C CB  . TYR   B 83  ? 0.3062 0.2464 0.2990 -0.0138 -0.0021 0.0242  89  TYR   C CB  
1732 C CG  . TYR   B 83  ? 0.3282 0.2646 0.3097 -0.0123 -0.0037 0.0270  89  TYR   C CG  
1733 C CD1 . TYR   B 83  ? 0.3548 0.2888 0.3344 -0.0092 -0.0096 0.0273  89  TYR   C CD1 
1734 C CD2 . TYR   B 83  ? 0.3437 0.2791 0.3171 -0.0136 0.0002  0.0289  89  TYR   C CD2 
1735 C CE1 . TYR   B 83  ? 0.3827 0.3130 0.3524 -0.0076 -0.0124 0.0292  89  TYR   C CE1 
1736 C CE2 . TYR   B 83  ? 0.3767 0.3077 0.3385 -0.0117 -0.0020 0.0308  89  TYR   C CE2 
1737 C CZ  . TYR   B 83  ? 0.4050 0.3334 0.3650 -0.0087 -0.0088 0.0308  89  TYR   C CZ  
1738 O OH  . TYR   B 83  ? 0.4623 0.3864 0.4115 -0.0066 -0.0122 0.0318  89  TYR   C OH  
1739 N N   . TYR   B 84  ? 0.2858 0.2224 0.2957 -0.0197 0.0030  0.0227  90  TYR   C N   
1740 C CA  . TYR   B 84  ? 0.2910 0.2321 0.3125 -0.0209 0.0029  0.0181  90  TYR   C CA  
1741 C C   . TYR   B 84  ? 0.3175 0.2541 0.3444 -0.0252 0.0067  0.0202  90  TYR   C C   
1742 O O   . TYR   B 84  ? 0.3136 0.2483 0.3364 -0.0279 0.0117  0.0243  90  TYR   C O   
1743 C CB  . TYR   B 84  ? 0.2688 0.2208 0.2936 -0.0207 0.0043  0.0139  90  TYR   C CB  
1744 C CG  . TYR   B 84  ? 0.2492 0.2068 0.2711 -0.0169 0.0014  0.0114  90  TYR   C CG  
1745 C CD1 . TYR   B 84  ? 0.2475 0.2084 0.2628 -0.0162 0.0026  0.0128  90  TYR   C CD1 
1746 C CD2 . TYR   B 84  ? 0.2409 0.2005 0.2671 -0.0139 -0.0021 0.0077  90  TYR   C CD2 
1747 C CE1 . TYR   B 84  ? 0.2398 0.2057 0.2538 -0.0132 0.0004  0.0109  90  TYR   C CE1 
1748 C CE2 . TYR   B 84  ? 0.2329 0.1980 0.2572 -0.0106 -0.0035 0.0059  90  TYR   C CE2 
1749 C CZ  . TYR   B 84  ? 0.2248 0.1931 0.2438 -0.0106 -0.0023 0.0077  90  TYR   C CZ  
1750 O OH  . TYR   B 84  ? 0.2196 0.1927 0.2381 -0.0078 -0.0035 0.0066  90  TYR   C OH  
1751 N N   . PRO   B 85  ? 0.3274 0.2632 0.3648 -0.0262 0.0047  0.0167  91  PRO   C N   
1752 C CA  . PRO   B 85  ? 0.3166 0.2502 0.3627 -0.0309 0.0083  0.0177  91  PRO   C CA  
1753 C C   . PRO   B 85  ? 0.3034 0.2470 0.3546 -0.0327 0.0117  0.0152  91  PRO   C C   
1754 O O   . PRO   B 85  ? 0.2961 0.2477 0.3451 -0.0300 0.0101  0.0115  91  PRO   C O   
1755 C CB  . PRO   B 85  ? 0.3265 0.2581 0.3832 -0.0305 0.0035  0.0127  91  PRO   C CB  
1756 C CG  . PRO   B 85  ? 0.3419 0.2802 0.3963 -0.0254 -0.0011 0.0072  91  PRO   C CG  
1757 C CD  . PRO   B 85  ? 0.3248 0.2628 0.3672 -0.0228 -0.0007 0.0110  91  PRO   C CD  
1758 N N   . ALA   B 86  ? 0.2970 0.2403 0.3565 -0.0373 0.0164  0.0169  92  ALA   C N   
1759 C CA  . ALA   B 86  ? 0.2956 0.2488 0.3635 -0.0391 0.0191  0.0137  92  ALA   C CA  
1760 C C   . ALA   B 86  ? 0.2926 0.2524 0.3692 -0.0368 0.0127  0.0055  92  ALA   C C   
1761 O O   . ALA   B 86  ? 0.2905 0.2458 0.3727 -0.0366 0.0083  0.0029  92  ALA   C O   
1762 C CB  . ALA   B 86  ? 0.3093 0.2606 0.3885 -0.0446 0.0248  0.0166  92  ALA   C CB  
1763 N N   . ARG   B 87  ? 0.2802 0.2491 0.3553 -0.0342 0.0115  0.0017  93  ARG   C N   
1764 C CA  . ARG   B 87  ? 0.2655 0.2393 0.3446 -0.0309 0.0054  -0.0055 93  ARG   C CA  
1765 C C   . ARG   B 87  ? 0.2583 0.2419 0.3374 -0.0290 0.0054  -0.0087 93  ARG   C C   
1766 O O   . ARG   B 87  ? 0.2681 0.2548 0.3436 -0.0300 0.0101  -0.0055 93  ARG   C O   
1767 C CB  . ARG   B 87  ? 0.2771 0.2474 0.3460 -0.0264 0.0016  -0.0059 93  ARG   C CB  
1768 C CG  . ARG   B 87  ? 0.2391 0.2127 0.2961 -0.0237 0.0034  -0.0032 93  ARG   C CG  
1769 C CD  . ARG   B 87  ? 0.2475 0.2164 0.2957 -0.0208 0.0016  -0.0010 93  ARG   C CD  
1770 N NE  . ARG   B 87  ? 0.2440 0.2180 0.2853 -0.0170 0.0007  -0.0019 93  ARG   C NE  
1771 C CZ  . ARG   B 87  ? 0.2644 0.2415 0.2997 -0.0170 0.0031  0.0005  93  ARG   C CZ  
1772 N NH1 . ARG   B 87  ? 0.2377 0.2187 0.2683 -0.0138 0.0020  -0.0003 93  ARG   C NH1 
1773 N NH2 . ARG   B 87  ? 0.2503 0.2262 0.2844 -0.0201 0.0071  0.0039  93  ARG   C NH2 
1774 N N   . TYR   B 88  ? 0.2625 0.2503 0.3444 -0.0258 0.0000  -0.0152 94  TYR   C N   
1775 C CA  . TYR   B 88  ? 0.2709 0.2666 0.3505 -0.0230 -0.0007 -0.0180 94  TYR   C CA  
1776 C C   . TYR   B 88  ? 0.2414 0.2366 0.3075 -0.0185 -0.0017 -0.0170 94  TYR   C C   
1777 O O   . TYR   B 88  ? 0.2443 0.2362 0.3072 -0.0157 -0.0050 -0.0188 94  TYR   C O   
1778 C CB  . TYR   B 88  ? 0.2905 0.2903 0.3786 -0.0212 -0.0064 -0.0253 94  TYR   C CB  
1779 C CG  . TYR   B 88  ? 0.3379 0.3404 0.4420 -0.0257 -0.0056 -0.0268 94  TYR   C CG  
1780 C CD1 . TYR   B 88  ? 0.3644 0.3742 0.4739 -0.0269 -0.0027 -0.0266 94  TYR   C CD1 
1781 C CD2 . TYR   B 88  ? 0.3731 0.3707 0.4880 -0.0291 -0.0073 -0.0280 94  TYR   C CD2 
1782 C CE1 . TYR   B 88  ? 0.3930 0.4063 0.5194 -0.0313 -0.0012 -0.0278 94  TYR   C CE1 
1783 C CE2 . TYR   B 88  ? 0.3944 0.3949 0.5265 -0.0338 -0.0061 -0.0291 94  TYR   C CE2 
1784 C CZ  . TYR   B 88  ? 0.4145 0.4232 0.5525 -0.0351 -0.0026 -0.0287 94  TYR   C CZ  
1785 O OH  . TYR   B 88  ? 0.4684 0.4810 0.6251 -0.0398 -0.0006 -0.0295 94  TYR   C OH  
1786 N N   . GLN   B 89  ? 0.1989 0.1973 0.2582 -0.0178 0.0014  -0.0142 95  GLN   C N   
1787 C CA  . GLN   B 89  ? 0.1969 0.1957 0.2456 -0.0139 0.0006  -0.0133 95  GLN   C CA  
1788 C C   . GLN   B 89  ? 0.1950 0.1994 0.2429 -0.0102 -0.0020 -0.0177 95  GLN   C C   
1789 O O   . GLN   B 89  ? 0.2049 0.2140 0.2568 -0.0109 -0.0014 -0.0189 95  GLN   C O   
1790 C CB  . GLN   B 89  ? 0.1906 0.1884 0.2319 -0.0149 0.0045  -0.0081 95  GLN   C CB  
1791 C CG  . GLN   B 89  ? 0.1830 0.1816 0.2156 -0.0113 0.0035  -0.0073 95  GLN   C CG  
1792 C CD  . GLN   B 89  ? 0.1886 0.1840 0.2144 -0.0122 0.0056  -0.0025 95  GLN   C CD  
1793 O OE1 . GLN   B 89  ? 0.1971 0.1873 0.2220 -0.0144 0.0067  0.0006  95  GLN   C OE1 
1794 N NE2 . GLN   B 89  ? 0.1856 0.1835 0.2063 -0.0104 0.0059  -0.0018 95  GLN   C NE2 
1795 N N   . SER   B 90  ? 0.1877 0.1916 0.2303 -0.0061 -0.0047 -0.0198 96  SER   C N   
1796 C CA  . SER   B 90  ? 0.1787 0.1864 0.2182 -0.0019 -0.0072 -0.0235 96  SER   C CA  
1797 C C   . SER   B 90  ? 0.1757 0.1854 0.2065 0.0002  -0.0048 -0.0203 96  SER   C C   
1798 O O   . SER   B 90  ? 0.1809 0.1887 0.2081 -0.0010 -0.0020 -0.0160 96  SER   C O   
1799 C CB  . SER   B 90  ? 0.1981 0.2035 0.2353 0.0021  -0.0111 -0.0278 96  SER   C CB  
1800 O OG  . SER   B 90  ? 0.2221 0.2246 0.2536 0.0036  -0.0094 -0.0251 96  SER   C OG  
1801 N N   . HIS   B 91  ? 0.1688 0.1817 0.1965 0.0036  -0.0064 -0.0227 97  HIS   C N   
1802 C CA  . HIS   B 91  ? 0.1690 0.1831 0.1890 0.0060  -0.0045 -0.0201 97  HIS   C CA  
1803 C C   . HIS   B 91  ? 0.1716 0.1863 0.1922 0.0025  -0.0011 -0.0160 97  HIS   C C   
1804 O O   . HIS   B 91  ? 0.1777 0.1914 0.1930 0.0031  0.0009  -0.0126 97  HIS   C O   
1805 C CB  . HIS   B 91  ? 0.1746 0.1862 0.1881 0.0087  -0.0034 -0.0184 97  HIS   C CB  
1806 C CG  . HIS   B 91  ? 0.1850 0.1955 0.1953 0.0132  -0.0062 -0.0225 97  HIS   C CG  
1807 N ND1 . HIS   B 91  ? 0.2245 0.2357 0.2271 0.0181  -0.0068 -0.0237 97  HIS   C ND1 
1808 C CD2 . HIS   B 91  ? 0.2097 0.2179 0.2229 0.0136  -0.0085 -0.0257 97  HIS   C CD2 
1809 C CE1 . HIS   B 91  ? 0.2240 0.2331 0.2237 0.0218  -0.0094 -0.0278 97  HIS   C CE1 
1810 N NE2 . HIS   B 91  ? 0.2329 0.2403 0.2395 0.0192  -0.0109 -0.0296 97  HIS   C NE2 
1811 N N   . LEU   B 92  ? 0.1688 0.1850 0.1962 -0.0008 -0.0003 -0.0164 98  LEU   C N   
1812 C CA  . LEU   B 92  ? 0.1721 0.1881 0.1991 -0.0036 0.0032  -0.0130 98  LEU   C CA  
1813 C C   . LEU   B 92  ? 0.1768 0.1971 0.2052 -0.0025 0.0035  -0.0144 98  LEU   C C   
1814 O O   . LEU   B 92  ? 0.1700 0.1937 0.2046 -0.0017 0.0012  -0.0181 98  LEU   C O   
1815 C CB  . LEU   B 92  ? 0.1760 0.1901 0.2087 -0.0079 0.0052  -0.0117 98  LEU   C CB  
1816 C CG  . LEU   B 92  ? 0.2074 0.2200 0.2375 -0.0104 0.0094  -0.0079 98  LEU   C CG  
1817 C CD1 . LEU   B 92  ? 0.2028 0.2110 0.2240 -0.0098 0.0096  -0.0044 98  LEU   C CD1 
1818 C CD2 . LEU   B 92  ? 0.2371 0.2471 0.2726 -0.0144 0.0119  -0.0064 98  LEU   C CD2 
1819 N N   . MET   B 93  ? 0.1623 0.1820 0.1855 -0.0023 0.0056  -0.0117 99  MET   C N   
1820 C CA  . MET   B 93  ? 0.1604 0.1835 0.1846 -0.0009 0.0060  -0.0129 99  MET   C CA  
1821 C C   . MET   B 93  ? 0.1657 0.1884 0.1904 -0.0036 0.0100  -0.0109 99  MET   C C   
1822 O O   . MET   B 93  ? 0.1808 0.1992 0.1999 -0.0050 0.0117  -0.0077 99  MET   C O   
1823 C CB  . MET   B 93  ? 0.1618 0.1834 0.1782 0.0023  0.0050  -0.0117 99  MET   C CB  
1824 C CG  . MET   B 93  ? 0.2074 0.2288 0.2213 0.0055  0.0021  -0.0132 99  MET   C CG  
1825 S SD  . MET   B 93  ? 0.2368 0.2555 0.2419 0.0087  0.0024  -0.0104 99  MET   C SD  
1826 C CE  . MET   B 93  ? 0.1821 0.1971 0.1853 0.0054  0.0051  -0.0060 99  MET   C CE  
1827 N N   . LEU   B 94  ? 0.1596 0.1866 0.1911 -0.0040 0.0115  -0.0129 100 LEU   C N   
1828 C CA  . LEU   B 94  ? 0.1538 0.1804 0.1851 -0.0060 0.0163  -0.0110 100 LEU   C CA  
1829 C C   . LEU   B 94  ? 0.1586 0.1865 0.1867 -0.0034 0.0171  -0.0116 100 LEU   C C   
1830 O O   . LEU   B 94  ? 0.1479 0.1794 0.1790 -0.0005 0.0143  -0.0143 100 LEU   C O   
1831 C CB  . LEU   B 94  ? 0.1674 0.1980 0.2100 -0.0087 0.0195  -0.0122 100 LEU   C CB  
1832 C CG  . LEU   B 94  ? 0.1800 0.2085 0.2270 -0.0119 0.0193  -0.0114 100 LEU   C CG  
1833 C CD1 . LEU   B 94  ? 0.1958 0.2284 0.2558 -0.0150 0.0230  -0.0122 100 LEU   C CD1 
1834 C CD2 . LEU   B 94  ? 0.2100 0.2311 0.2471 -0.0135 0.0211  -0.0070 100 LEU   C CD2 
1835 N N   . ALA   B 95  ? 0.1574 0.1821 0.1794 -0.0041 0.0206  -0.0094 101 ALA   C N   
1836 C CA  . ALA   B 95  ? 0.1574 0.1828 0.1767 -0.0016 0.0218  -0.0103 101 ALA   C CA  
1837 C C   . ALA   B 95  ? 0.1619 0.1864 0.1798 -0.0031 0.0277  -0.0091 101 ALA   C C   
1838 O O   . ALA   B 95  ? 0.1714 0.1925 0.1867 -0.0059 0.0302  -0.0064 101 ALA   C O   
1839 C CB  . ALA   B 95  ? 0.1721 0.1920 0.1814 0.0002  0.0191  -0.0089 101 ALA   C CB  
1840 N N   . VAL   B 96  ? 0.1631 0.1900 0.1818 -0.0009 0.0301  -0.0108 102 VAL   C N   
1841 C CA  . VAL   B 96  ? 0.1780 0.2033 0.1926 -0.0012 0.0362  -0.0097 102 VAL   C CA  
1842 C C   . VAL   B 96  ? 0.2007 0.2176 0.2006 0.0002  0.0348  -0.0082 102 VAL   C C   
1843 O O   . VAL   B 96  ? 0.2177 0.2330 0.2141 0.0029  0.0314  -0.0097 102 VAL   C O   
1844 C CB  . VAL   B 96  ? 0.1887 0.2207 0.2113 0.0013  0.0394  -0.0129 102 VAL   C CB  
1845 C CG1 . VAL   B 96  ? 0.1973 0.2273 0.2145 0.0016  0.0468  -0.0117 102 VAL   C CG1 
1846 C CG2 . VAL   B 96  ? 0.1995 0.2402 0.2388 -0.0002 0.0396  -0.0149 102 VAL   C CG2 
1847 N N   . GLY   B 97  ? 0.2238 0.2349 0.2155 -0.0016 0.0370  -0.0052 103 GLY   C N   
1848 C CA  . GLY   B 97  ? 0.2508 0.2536 0.2290 -0.0002 0.0346  -0.0042 103 GLY   C CA  
1849 C C   . GLY   B 97  ? 0.2644 0.2609 0.2342 -0.0022 0.0362  -0.0008 103 GLY   C C   
1850 O O   . GLY   B 97  ? 0.2671 0.2650 0.2415 -0.0049 0.0391  0.0013  103 GLY   C O   
1851 N N   . HIS   B 98  ? 0.2571 0.2457 0.2143 -0.0007 0.0336  -0.0001 104 HIS   C N   
1852 C CA  . HIS   B 98  ? 0.2681 0.2492 0.2151 -0.0016 0.0339  0.0030  104 HIS   C CA  
1853 C C   . HIS   B 98  ? 0.2647 0.2435 0.2132 -0.0035 0.0281  0.0047  104 HIS   C C   
1854 O O   . HIS   B 98  ? 0.2629 0.2418 0.2134 -0.0029 0.0225  0.0034  104 HIS   C O   
1855 C CB  . HIS   B 98  ? 0.2744 0.2474 0.2062 0.0016  0.0328  0.0021  104 HIS   C CB  
1856 C CG  . HIS   B 98  ? 0.2870 0.2513 0.2061 0.0016  0.0327  0.0052  104 HIS   C CG  
1857 N ND1 . HIS   B 98  ? 0.3086 0.2716 0.2240 0.0007  0.0400  0.0084  104 HIS   C ND1 
1858 C CD2 . HIS   B 98  ? 0.2934 0.2503 0.2043 0.0021  0.0260  0.0060  104 HIS   C CD2 
1859 C CE1 . HIS   B 98  ? 0.3295 0.2834 0.2326 0.0011  0.0375  0.0111  104 HIS   C CE1 
1860 N NE2 . HIS   B 98  ? 0.3347 0.2850 0.2351 0.0021  0.0287  0.0095  104 HIS   C NE2 
1861 N N   . SER   B 99  ? 0.2672 0.2435 0.2146 -0.0055 0.0298  0.0079  105 SER   C N   
1862 C CA  . SER   B 99  ? 0.2941 0.2679 0.2429 -0.0070 0.0249  0.0097  105 SER   C CA  
1863 C C   . SER   B 99  ? 0.3221 0.2887 0.2623 -0.0077 0.0271  0.0134  105 SER   C C   
1864 O O   . SER   B 99  ? 0.3536 0.3213 0.2956 -0.0092 0.0336  0.0152  105 SER   C O   
1865 C CB  . SER   B 99  ? 0.3168 0.2979 0.2796 -0.0090 0.0246  0.0089  105 SER   C CB  
1866 O OG  . SER   B 99  ? 0.4025 0.3820 0.3678 -0.0099 0.0201  0.0100  105 SER   C OG  
1867 N N   . GLU   B 100 ? 0.2860 0.2453 0.2176 -0.0068 0.0218  0.0149  106 GLU   C N   
1868 C CA  . GLU   B 100 ? 0.3184 0.2696 0.2411 -0.0071 0.0227  0.0189  106 GLU   C CA  
1869 C C   . GLU   B 100 ? 0.3500 0.2990 0.2756 -0.0074 0.0155  0.0196  106 GLU   C C   
1870 O O   . GLU   B 100 ? 0.3544 0.3081 0.2879 -0.0073 0.0109  0.0171  106 GLU   C O   
1871 C CB  . GLU   B 100 ? 0.3666 0.3092 0.2716 -0.0043 0.0248  0.0201  106 GLU   C CB  
1872 C CG  . GLU   B 100 ? 0.4173 0.3564 0.3142 -0.0012 0.0186  0.0171  106 GLU   C CG  
1873 C CD  . GLU   B 100 ? 0.4558 0.3858 0.3338 0.0021  0.0210  0.0178  106 GLU   C CD  
1874 O OE1 . GLU   B 100 ? 0.5501 0.4711 0.4161 0.0034  0.0191  0.0209  106 GLU   C OE1 
1875 O OE2 . GLU   B 100 ? 0.4403 0.3719 0.3149 0.0039  0.0250  0.0155  106 GLU   C OE2 
1876 N N   . PRO   B 101 ? 0.3793 0.3228 0.3023 -0.0082 0.0154  0.0231  107 PRO   C N   
1877 C CA  . PRO   B 101 ? 0.3996 0.3436 0.3302 -0.0087 0.0095  0.0233  107 PRO   C CA  
1878 C C   . PRO   B 101 ? 0.3865 0.3319 0.3200 -0.0071 0.0017  0.0208  107 PRO   C C   
1879 O O   . PRO   B 101 ? 0.4073 0.3589 0.3530 -0.0079 -0.0005 0.0194  107 PRO   C O   
1880 C CB  . PRO   B 101 ? 0.4276 0.3622 0.3494 -0.0085 0.0095  0.0276  107 PRO   C CB  
1881 C CG  . PRO   B 101 ? 0.4267 0.3600 0.3449 -0.0101 0.0185  0.0301  107 PRO   C CG  
1882 C CD  . PRO   B 101 ? 0.3937 0.3314 0.3094 -0.0091 0.0217  0.0272  107 PRO   C CD  
1883 N N   . GLY   B 102 ? 0.3467 0.2860 0.2693 -0.0047 -0.0025 0.0204  108 GLY   C N   
1884 C CA  . GLY   B 102 ? 0.3318 0.2718 0.2574 -0.0033 -0.0100 0.0180  108 GLY   C CA  
1885 C C   . GLY   B 102 ? 0.2980 0.2464 0.2340 -0.0041 -0.0094 0.0149  108 GLY   C C   
1886 O O   . GLY   B 102 ? 0.2975 0.2476 0.2392 -0.0036 -0.0147 0.0132  108 GLY   C O   
1887 N N   . ASP   B 103 ? 0.2661 0.2198 0.2055 -0.0053 -0.0029 0.0143  109 ASP   C N   
1888 C CA  . ASP   B 103 ? 0.2365 0.1976 0.1848 -0.0057 -0.0022 0.0117  109 ASP   C CA  
1889 C C   . ASP   B 103 ? 0.2234 0.1912 0.1844 -0.0070 -0.0023 0.0116  109 ASP   C C   
1890 O O   . ASP   B 103 ? 0.2215 0.1944 0.1891 -0.0069 -0.0024 0.0100  109 ASP   C O   
1891 C CB  . ASP   B 103 ? 0.2399 0.2037 0.1863 -0.0058 0.0039  0.0106  109 ASP   C CB  
1892 C CG  . ASP   B 103 ? 0.2782 0.2362 0.2123 -0.0037 0.0040  0.0097  109 ASP   C CG  
1893 O OD1 . ASP   B 103 ? 0.2799 0.2334 0.2096 -0.0022 -0.0016 0.0086  109 ASP   C OD1 
1894 O OD2 . ASP   B 103 ? 0.2666 0.2243 0.1956 -0.0033 0.0099  0.0100  109 ASP   C OD2 
1895 N N   . CYS   B 104 ? 0.2192 0.1866 0.1832 -0.0079 -0.0019 0.0133  110 CYS   C N   
1896 C CA  . CYS   B 104 ? 0.2275 0.2009 0.2027 -0.0084 -0.0020 0.0126  110 CYS   C CA  
1897 C C   . CYS   B 104 ? 0.2167 0.1922 0.1974 -0.0075 -0.0060 0.0119  110 CYS   C C   
1898 O O   . CYS   B 104 ? 0.2304 0.2019 0.2085 -0.0068 -0.0105 0.0124  110 CYS   C O   
1899 C CB  . CYS   B 104 ? 0.2542 0.2257 0.2316 -0.0090 -0.0019 0.0141  110 CYS   C CB  
1900 S SG  . CYS   B 104 ? 0.2853 0.2572 0.2629 -0.0109 0.0039  0.0146  110 CYS   C SG  
1901 N N   . GLY   B 105 ? 0.1965 0.1782 0.1847 -0.0074 -0.0044 0.0107  111 GLY   C N   
1902 C CA  . GLY   B 105 ? 0.2031 0.1875 0.1980 -0.0068 -0.0068 0.0106  111 GLY   C CA  
1903 C C   . GLY   B 105 ? 0.2044 0.1896 0.1988 -0.0067 -0.0068 0.0098  111 GLY   C C   
1904 O O   . GLY   B 105 ? 0.2173 0.2054 0.2184 -0.0065 -0.0072 0.0100  111 GLY   C O   
1905 N N   . GLY   B 106 ? 0.1906 0.1732 0.1775 -0.0067 -0.0056 0.0089  112 GLY   C N   
1906 C CA  . GLY   B 106 ? 0.1785 0.1614 0.1648 -0.0063 -0.0054 0.0078  112 GLY   C CA  
1907 C C   . GLY   B 106 ? 0.1727 0.1612 0.1647 -0.0058 -0.0023 0.0077  112 GLY   C C   
1908 O O   . GLY   B 106 ? 0.1819 0.1734 0.1745 -0.0056 0.0005  0.0073  112 GLY   C O   
1909 N N   . ILE   B 107 ? 0.1717 0.1608 0.1675 -0.0056 -0.0030 0.0079  113 ILE   C N   
1910 C CA  . ILE   B 107 ? 0.1726 0.1657 0.1719 -0.0046 -0.0001 0.0083  113 ILE   C CA  
1911 C C   . ILE   B 107 ? 0.1669 0.1603 0.1623 -0.0034 0.0016  0.0069  113 ILE   C C   
1912 O O   . ILE   B 107 ? 0.1741 0.1642 0.1659 -0.0033 0.0004  0.0060  113 ILE   C O   
1913 C CB  . ILE   B 107 ? 0.2124 0.2059 0.2186 -0.0050 -0.0009 0.0102  113 ILE   C CB  
1914 C CG1 . ILE   B 107 ? 0.2450 0.2407 0.2574 -0.0054 -0.0012 0.0115  113 ILE   C CG1 
1915 C CG2 . ILE   B 107 ? 0.2325 0.2280 0.2397 -0.0035 0.0023  0.0113  113 ILE   C CG2 
1916 C CD1 . ILE   B 107 ? 0.2861 0.2831 0.3081 -0.0061 -0.0013 0.0136  113 ILE   C CD1 
1917 N N   . LEU   B 108 ? 0.1537 0.1509 0.1498 -0.0021 0.0040  0.0065  114 LEU   C N   
1918 C CA  . LEU   B 108 ? 0.1492 0.1476 0.1432 -0.0003 0.0052  0.0051  114 LEU   C CA  
1919 C C   . LEU   B 108 ? 0.1558 0.1545 0.1514 0.0013  0.0059  0.0068  114 LEU   C C   
1920 O O   . LEU   B 108 ? 0.1639 0.1646 0.1616 0.0018  0.0071  0.0081  114 LEU   C O   
1921 C CB  . LEU   B 108 ? 0.1525 0.1547 0.1468 0.0004  0.0066  0.0031  114 LEU   C CB  
1922 C CG  . LEU   B 108 ? 0.1725 0.1769 0.1662 0.0028  0.0071  0.0013  114 LEU   C CG  
1923 C CD1 . LEU   B 108 ? 0.1863 0.1890 0.1779 0.0031  0.0072  0.0001  114 LEU   C CD1 
1924 C CD2 . LEU   B 108 ? 0.1732 0.1818 0.1696 0.0033  0.0075  -0.0010 114 LEU   C CD2 
1925 N N   . ARG   B 109 ? 0.1575 0.1535 0.1517 0.0022  0.0055  0.0072  115 ARG   C N   
1926 C CA  . ARG   B 109 ? 0.1796 0.1745 0.1746 0.0036  0.0066  0.0097  115 ARG   C CA  
1927 C C   . ARG   B 109 ? 0.1841 0.1784 0.1753 0.0065  0.0066  0.0085  115 ARG   C C   
1928 O O   . ARG   B 109 ? 0.1883 0.1816 0.1780 0.0068  0.0054  0.0063  115 ARG   C O   
1929 C CB  . ARG   B 109 ? 0.2246 0.2153 0.2230 0.0017  0.0053  0.0116  115 ARG   C CB  
1930 C CG  . ARG   B 109 ? 0.3258 0.3172 0.3302 -0.0007 0.0051  0.0134  115 ARG   C CG  
1931 C CD  . ARG   B 109 ? 0.4205 0.4079 0.4303 -0.0028 0.0029  0.0147  115 ARG   C CD  
1932 N NE  . ARG   B 109 ? 0.5318 0.5193 0.5474 -0.0030 0.0058  0.0186  115 ARG   C NE  
1933 C CZ  . ARG   B 109 ? 0.5978 0.5882 0.6208 -0.0042 0.0075  0.0209  115 ARG   C CZ  
1934 N NH1 . ARG   B 109 ? 0.5978 0.5906 0.6239 -0.0054 0.0055  0.0194  115 ARG   C NH1 
1935 N NH2 . ARG   B 109 ? 0.6441 0.6345 0.6719 -0.0042 0.0114  0.0248  115 ARG   C NH2 
1936 N N   . CYS   B 110 ? 0.1799 0.1744 0.1693 0.0089  0.0079  0.0103  116 CYS   C N   
1937 C CA  . CYS   B 110 ? 0.1949 0.1876 0.1804 0.0123  0.0073  0.0099  116 CYS   C CA  
1938 C C   . CYS   B 110 ? 0.2228 0.2104 0.2077 0.0128  0.0086  0.0141  116 CYS   C C   
1939 O O   . CYS   B 110 ? 0.2130 0.1993 0.2020 0.0101  0.0100  0.0169  116 CYS   C O   
1940 C CB  . CYS   B 110 ? 0.1933 0.1894 0.1755 0.0156  0.0071  0.0081  116 CYS   C CB  
1941 S SG  . CYS   B 110 ? 0.1779 0.1738 0.1569 0.0174  0.0099  0.0114  116 CYS   C SG  
1942 N N   . GLN   B 111 ? 0.2431 0.2278 0.2234 0.0163  0.0082  0.0148  117 GLN   C N   
1943 C CA  . GLN   B 111 ? 0.2732 0.2520 0.2526 0.0168  0.0100  0.0195  117 GLN   C CA  
1944 C C   . GLN   B 111 ? 0.2744 0.2536 0.2532 0.0168  0.0141  0.0238  117 GLN   C C   
1945 O O   . GLN   B 111 ? 0.3069 0.2819 0.2877 0.0158  0.0169  0.0285  117 GLN   C O   
1946 C CB  . GLN   B 111 ? 0.3150 0.2898 0.2883 0.0212  0.0085  0.0196  117 GLN   C CB  
1947 C CG  . GLN   B 111 ? 0.3618 0.3387 0.3281 0.0258  0.0084  0.0191  117 GLN   C CG  
1948 C CD  . GLN   B 111 ? 0.4752 0.4481 0.4355 0.0307  0.0059  0.0188  117 GLN   C CD  
1949 O OE1 . GLN   B 111 ? 0.4943 0.4707 0.4542 0.0332  0.0024  0.0143  117 GLN   C OE1 
1950 N NE2 . GLN   B 111 ? 0.4905 0.4560 0.4467 0.0322  0.0076  0.0239  117 GLN   C NE2 
1951 N N   . HIS   B 112 ? 0.2474 0.2315 0.2244 0.0178  0.0150  0.0222  118 HIS   C N   
1952 C CA  . HIS   B 112 ? 0.2425 0.2272 0.2179 0.0188  0.0193  0.0256  118 HIS   C CA  
1953 C C   . HIS   B 112 ? 0.2551 0.2434 0.2392 0.0148  0.0211  0.0262  118 HIS   C C   
1954 O O   . HIS   B 112 ? 0.2774 0.2665 0.2624 0.0153  0.0254  0.0294  118 HIS   C O   
1955 C CB  . HIS   B 112 ? 0.2363 0.2233 0.2037 0.0233  0.0188  0.0233  118 HIS   C CB  
1956 C CG  . HIS   B 112 ? 0.2312 0.2150 0.1903 0.0278  0.0161  0.0222  118 HIS   C CG  
1957 N ND1 . HIS   B 112 ? 0.2196 0.2064 0.1787 0.0291  0.0114  0.0170  118 HIS   C ND1 
1958 C CD2 . HIS   B 112 ? 0.2569 0.2349 0.2082 0.0316  0.0176  0.0261  118 HIS   C CD2 
1959 C CE1 . HIS   B 112 ? 0.2646 0.2478 0.2167 0.0336  0.0093  0.0172  118 HIS   C CE1 
1960 N NE2 . HIS   B 112 ? 0.2800 0.2571 0.2262 0.0354  0.0127  0.0228  118 HIS   C NE2 
1961 N N   . GLY   B 113 ? 0.2258 0.2162 0.2158 0.0114  0.0179  0.0232  119 GLY   C N   
1962 C CA  . GLY   B 113 ? 0.2048 0.1981 0.2026 0.0081  0.0184  0.0233  119 GLY   C CA  
1963 C C   . GLY   B 113 ? 0.1824 0.1790 0.1807 0.0070  0.0153  0.0190  119 GLY   C C   
1964 O O   . GLY   B 113 ? 0.1765 0.1731 0.1713 0.0076  0.0127  0.0159  119 GLY   C O   
1965 N N   . VAL   B 114 ? 0.1777 0.1773 0.1806 0.0056  0.0159  0.0190  120 VAL   C N   
1966 C CA  . VAL   B 114 ? 0.1753 0.1771 0.1788 0.0044  0.0133  0.0156  120 VAL   C CA  
1967 C C   . VAL   B 114 ? 0.1723 0.1762 0.1704 0.0070  0.0132  0.0128  120 VAL   C C   
1968 O O   . VAL   B 114 ? 0.1787 0.1839 0.1745 0.0097  0.0155  0.0133  120 VAL   C O   
1969 C CB  . VAL   B 114 ? 0.1924 0.1961 0.2030 0.0025  0.0135  0.0166  120 VAL   C CB  
1970 C CG1 . VAL   B 114 ? 0.1978 0.2026 0.2078 0.0017  0.0110  0.0136  120 VAL   C CG1 
1971 C CG2 . VAL   B 114 ? 0.2014 0.2031 0.2190 -0.0004 0.0119  0.0184  120 VAL   C CG2 
1972 N N   . VAL   B 115 ? 0.1621 0.1665 0.1586 0.0064  0.0108  0.0097  121 VAL   C N   
1973 C CA  . VAL   B 115 ? 0.1627 0.1693 0.1566 0.0083  0.0100  0.0066  121 VAL   C CA  
1974 C C   . VAL   B 115 ? 0.1658 0.1740 0.1627 0.0066  0.0093  0.0050  121 VAL   C C   
1975 O O   . VAL   B 115 ? 0.1656 0.1753 0.1619 0.0082  0.0091  0.0031  121 VAL   C O   
1976 C CB  . VAL   B 115 ? 0.1663 0.1730 0.1587 0.0085  0.0083  0.0043  121 VAL   C CB  
1977 C CG1 . VAL   B 115 ? 0.1851 0.1949 0.1780 0.0096  0.0070  0.0006  121 VAL   C CG1 
1978 C CG2 . VAL   B 115 ? 0.1736 0.1782 0.1625 0.0109  0.0085  0.0056  121 VAL   C CG2 
1979 N N   . GLY   B 116 ? 0.1579 0.1648 0.1575 0.0035  0.0084  0.0056  122 GLY   C N   
1980 C CA  . GLY   B 116 ? 0.1778 0.1850 0.1795 0.0019  0.0076  0.0046  122 GLY   C CA  
1981 C C   . GLY   B 116 ? 0.1599 0.1644 0.1622 -0.0008 0.0063  0.0056  122 GLY   C C   
1982 O O   . GLY   B 116 ? 0.1664 0.1690 0.1681 -0.0014 0.0057  0.0069  122 GLY   C O   
1983 N N   . ILE   B 117 ? 0.1596 0.1632 0.1625 -0.0022 0.0056  0.0051  123 ILE   C N   
1984 C CA  . ILE   B 117 ? 0.1601 0.1599 0.1614 -0.0042 0.0041  0.0064  123 ILE   C CA  
1985 C C   . ILE   B 117 ? 0.1664 0.1648 0.1651 -0.0055 0.0048  0.0056  123 ILE   C C   
1986 O O   . ILE   B 117 ? 0.1670 0.1671 0.1678 -0.0055 0.0058  0.0043  123 ILE   C O   
1987 C CB  . ILE   B 117 ? 0.1755 0.1741 0.1801 -0.0045 0.0023  0.0078  123 ILE   C CB  
1988 C CG1 . ILE   B 117 ? 0.1913 0.1914 0.1986 -0.0037 0.0029  0.0069  123 ILE   C CG1 
1989 C CG2 . ILE   B 117 ? 0.1982 0.1980 0.2070 -0.0039 0.0017  0.0092  123 ILE   C CG2 
1990 C CD1 . ILE   B 117 ? 0.2122 0.2107 0.2232 -0.0037 0.0008  0.0082  123 ILE   C CD1 
1991 N N   . VAL   B 118 ? 0.1522 0.1467 0.1459 -0.0065 0.0044  0.0063  124 VAL   C N   
1992 C CA  . VAL   B 118 ? 0.1573 0.1499 0.1479 -0.0077 0.0064  0.0063  124 VAL   C CA  
1993 C C   . VAL   B 118 ? 0.1588 0.1497 0.1514 -0.0087 0.0060  0.0074  124 VAL   C C   
1994 O O   . VAL   B 118 ? 0.1694 0.1578 0.1620 -0.0085 0.0032  0.0087  124 VAL   C O   
1995 C CB  . VAL   B 118 ? 0.1702 0.1578 0.1531 -0.0079 0.0059  0.0073  124 VAL   C CB  
1996 C CG1 . VAL   B 118 ? 0.2039 0.1886 0.1825 -0.0090 0.0090  0.0083  124 VAL   C CG1 
1997 C CG2 . VAL   B 118 ? 0.1880 0.1766 0.1690 -0.0067 0.0062  0.0058  124 VAL   C CG2 
1998 N N   . SER   B 119 ? 0.1680 0.1600 0.1631 -0.0099 0.0083  0.0067  125 SER   C N   
1999 C CA  . SER   B 119 ? 0.1656 0.1554 0.1633 -0.0110 0.0081  0.0075  125 SER   C CA  
2000 C C   . SER   B 119 ? 0.1988 0.1856 0.1952 -0.0132 0.0113  0.0089  125 SER   C C   
2001 O O   . SER   B 119 ? 0.2032 0.1852 0.1987 -0.0142 0.0110  0.0110  125 SER   C O   
2002 C CB  . SER   B 119 ? 0.1719 0.1659 0.1765 -0.0100 0.0072  0.0050  125 SER   C CB  
2003 O OG  . SER   B 119 ? 0.1818 0.1731 0.1896 -0.0109 0.0066  0.0052  125 SER   C OG  
2004 N N   . THR   B 120 ? 0.1933 0.1831 0.1905 -0.0138 0.0147  0.0079  126 THR   C N   
2005 C CA  . THR   B 120 ? 0.2135 0.2013 0.2108 -0.0160 0.0192  0.0095  126 THR   C CA  
2006 C C   . THR   B 120 ? 0.2140 0.2024 0.2060 -0.0155 0.0227  0.0098  126 THR   C C   
2007 O O   . THR   B 120 ? 0.2131 0.2040 0.2032 -0.0135 0.0213  0.0080  126 THR   C O   
2008 C CB  . THR   B 120 ? 0.2380 0.2308 0.2470 -0.0177 0.0205  0.0072  126 THR   C CB  
2009 O OG1 . THR   B 120 ? 0.2520 0.2517 0.2656 -0.0166 0.0212  0.0040  126 THR   C OG1 
2010 C CG2 . THR   B 120 ? 0.2383 0.2313 0.2527 -0.0174 0.0166  0.0055  126 THR   C CG2 
2011 N N   . GLY   B 121 ? 0.2415 0.2270 0.2309 -0.0171 0.0278  0.0122  127 GLY   C N   
2012 C CA  . GLY   B 121 ? 0.2768 0.2627 0.2607 -0.0161 0.0320  0.0122  127 GLY   C CA  
2013 C C   . GLY   B 121 ? 0.3050 0.2893 0.2889 -0.0181 0.0392  0.0149  127 GLY   C C   
2014 O O   . GLY   B 121 ? 0.2981 0.2811 0.2878 -0.0207 0.0407  0.0167  127 GLY   C O   
2015 N N   . GLY   B 122 ? 0.3388 0.3223 0.3156 -0.0166 0.0437  0.0153  128 GLY   C N   
2016 C CA  . GLY   B 122 ? 0.3500 0.3322 0.3261 -0.0181 0.0522  0.0182  128 GLY   C CA  
2017 C C   . GLY   B 122 ? 0.3534 0.3453 0.3431 -0.0189 0.0571  0.0155  128 GLY   C C   
2018 O O   . GLY   B 122 ? 0.3342 0.3336 0.3351 -0.0187 0.0532  0.0115  128 GLY   C O   
2019 N N   . ASN   B 123 ? 0.3564 0.3482 0.3453 -0.0196 0.0661  0.0179  129 ASN   C N   
2020 C CA  . ASN   B 123 ? 0.3581 0.3600 0.3619 -0.0202 0.0713  0.0152  129 ASN   C CA  
2021 C C   . ASN   B 123 ? 0.3282 0.3361 0.3329 -0.0165 0.0678  0.0101  129 ASN   C C   
2022 O O   . ASN   B 123 ? 0.3382 0.3555 0.3579 -0.0166 0.0684  0.0067  129 ASN   C O   
2023 C CB  . ASN   B 123 ? 0.3881 0.3967 0.4118 -0.0240 0.0700  0.0138  129 ASN   C CB  
2024 C CG  . ASN   B 123 ? 0.4414 0.4497 0.4739 -0.0282 0.0780  0.0177  129 ASN   C CG  
2025 O OD1 . ASN   B 123 ? 0.4745 0.4762 0.4962 -0.0284 0.0853  0.0226  129 ASN   C OD1 
2026 N ND2 . ASN   B 123 ? 0.4342 0.4490 0.4863 -0.0315 0.0765  0.0155  129 ASN   C ND2 
2027 N N   . GLY   B 124 ? 0.2959 0.2979 0.2854 -0.0132 0.0637  0.0097  130 GLY   C N   
2028 C CA  . GLY   B 124 ? 0.2701 0.2760 0.2596 -0.0097 0.0602  0.0053  130 GLY   C CA  
2029 C C   . GLY   B 124 ? 0.2299 0.2408 0.2291 -0.0098 0.0525  0.0021  130 GLY   C C   
2030 O O   . GLY   B 124 ? 0.2315 0.2468 0.2339 -0.0072 0.0501  -0.0013 130 GLY   C O   
2031 N N   . LEU   B 125 ? 0.2214 0.2310 0.2241 -0.0122 0.0486  0.0033  131 LEU   C N   
2032 C CA  . LEU   B 125 ? 0.2103 0.2236 0.2198 -0.0118 0.0417  0.0006  131 LEU   C CA  
2033 C C   . LEU   B 125 ? 0.2288 0.2351 0.2284 -0.0115 0.0362  0.0023  131 LEU   C C   
2034 O O   . LEU   B 125 ? 0.2689 0.2685 0.2602 -0.0126 0.0373  0.0056  131 LEU   C O   
2035 C CB  . LEU   B 125 ? 0.2272 0.2455 0.2510 -0.0146 0.0417  -0.0003 131 LEU   C CB  
2036 C CG  . LEU   B 125 ? 0.2581 0.2841 0.2954 -0.0157 0.0469  -0.0019 131 LEU   C CG  
2037 C CD1 . LEU   B 125 ? 0.2774 0.3060 0.3284 -0.0194 0.0466  -0.0021 131 LEU   C CD1 
2038 C CD2 . LEU   B 125 ? 0.2584 0.2915 0.3020 -0.0125 0.0442  -0.0064 131 LEU   C CD2 
2039 N N   . VAL   B 126 ? 0.1769 0.1851 0.1782 -0.0099 0.0306  0.0003  132 VAL   C N   
2040 C CA  . VAL   B 126 ? 0.1886 0.1920 0.1841 -0.0098 0.0259  0.0017  132 VAL   C CA  
2041 C C   . VAL   B 126 ? 0.1889 0.1966 0.1930 -0.0098 0.0224  -0.0002 132 VAL   C C   
2042 O O   . VAL   B 126 ? 0.1795 0.1925 0.1894 -0.0084 0.0215  -0.0030 132 VAL   C O   
2043 C CB  . VAL   B 126 ? 0.2023 0.2023 0.1895 -0.0075 0.0231  0.0015  132 VAL   C CB  
2044 C CG1 . VAL   B 126 ? 0.2407 0.2449 0.2308 -0.0051 0.0225  -0.0013 132 VAL   C CG1 
2045 C CG2 . VAL   B 126 ? 0.1992 0.1957 0.1838 -0.0075 0.0182  0.0028  132 VAL   C CG2 
2046 N N   . GLY   B 127 ? 0.1703 0.1750 0.1741 -0.0110 0.0203  0.0013  133 GLY   C N   
2047 C CA  . GLY   B 127 ? 0.1742 0.1820 0.1844 -0.0105 0.0171  -0.0007 133 GLY   C CA  
2048 C C   . GLY   B 127 ? 0.1647 0.1700 0.1704 -0.0090 0.0136  0.0002  133 GLY   C C   
2049 O O   . GLY   B 127 ? 0.1786 0.1791 0.1790 -0.0096 0.0130  0.0027  133 GLY   C O   
2050 N N   . PHE   B 128 ? 0.1476 0.1563 0.1555 -0.0068 0.0114  -0.0018 134 PHE   C N   
2051 C CA  . PHE   B 128 ? 0.1543 0.1615 0.1593 -0.0052 0.0092  -0.0008 134 PHE   C CA  
2052 C C   . PHE   B 128 ? 0.1481 0.1568 0.1564 -0.0040 0.0076  -0.0023 134 PHE   C C   
2053 O O   . PHE   B 128 ? 0.1679 0.1799 0.1795 -0.0028 0.0068  -0.0051 134 PHE   C O   
2054 C CB  . PHE   B 128 ? 0.1549 0.1636 0.1576 -0.0029 0.0087  -0.0012 134 PHE   C CB  
2055 C CG  . PHE   B 128 ? 0.1622 0.1695 0.1616 -0.0032 0.0099  -0.0007 134 PHE   C CG  
2056 C CD1 . PHE   B 128 ? 0.1606 0.1636 0.1554 -0.0038 0.0093  0.0012  134 PHE   C CD1 
2057 C CD2 . PHE   B 128 ? 0.1738 0.1841 0.1753 -0.0026 0.0114  -0.0028 134 PHE   C CD2 
2058 C CE1 . PHE   B 128 ? 0.1708 0.1716 0.1614 -0.0036 0.0100  0.0010  134 PHE   C CE1 
2059 C CE2 . PHE   B 128 ? 0.1871 0.1959 0.1851 -0.0022 0.0128  -0.0028 134 PHE   C CE2 
2060 C CZ  . PHE   B 128 ? 0.1791 0.1828 0.1709 -0.0026 0.0121  -0.0009 134 PHE   C CZ  
2061 N N   . ALA   B 129 ? 0.1460 0.1524 0.1535 -0.0039 0.0067  -0.0007 135 ALA   C N   
2062 C CA  . ALA   B 129 ? 0.1502 0.1575 0.1597 -0.0020 0.0055  -0.0022 135 ALA   C CA  
2063 C C   . ALA   B 129 ? 0.1561 0.1653 0.1629 0.0010  0.0056  -0.0022 135 ALA   C C   
2064 O O   . ALA   B 129 ? 0.1621 0.1705 0.1674 0.0012  0.0063  0.0003  135 ALA   C O   
2065 C CB  . ALA   B 129 ? 0.1635 0.1678 0.1737 -0.0027 0.0048  -0.0004 135 ALA   C CB  
2066 N N   . ASP   B 130 ? 0.1538 0.1653 0.1603 0.0037  0.0048  -0.0051 136 ASP   C N   
2067 C CA  . ASP   B 130 ? 0.1503 0.1625 0.1525 0.0071  0.0052  -0.0047 136 ASP   C CA  
2068 C C   . ASP   B 130 ? 0.1719 0.1833 0.1728 0.0089  0.0065  -0.0032 136 ASP   C C   
2069 O O   . ASP   B 130 ? 0.1661 0.1769 0.1690 0.0091  0.0059  -0.0046 136 ASP   C O   
2070 C CB  . ASP   B 130 ? 0.1668 0.1807 0.1677 0.0101  0.0031  -0.0086 136 ASP   C CB  
2071 C CG  . ASP   B 130 ? 0.2395 0.2531 0.2339 0.0142  0.0034  -0.0079 136 ASP   C CG  
2072 O OD1 . ASP   B 130 ? 0.2315 0.2445 0.2241 0.0139  0.0049  -0.0052 136 ASP   C OD1 
2073 O OD2 . ASP   B 130 ? 0.2811 0.2944 0.2716 0.0180  0.0022  -0.0101 136 ASP   C OD2 
2074 N N   . VAL   B 131 ? 0.1612 0.1724 0.1594 0.0104  0.0086  -0.0004 137 VAL   C N   
2075 C CA  . VAL   B 131 ? 0.1626 0.1739 0.1605 0.0126  0.0110  0.0011  137 VAL   C CA  
2076 C C   . VAL   B 131 ? 0.1857 0.1968 0.1769 0.0168  0.0131  0.0018  137 VAL   C C   
2077 O O   . VAL   B 131 ? 0.1905 0.2017 0.1804 0.0192  0.0163  0.0035  137 VAL   C O   
2078 C CB  . VAL   B 131 ? 0.1749 0.1862 0.1779 0.0102  0.0127  0.0049  137 VAL   C CB  
2079 C CG1 . VAL   B 131 ? 0.1845 0.1949 0.1921 0.0068  0.0102  0.0044  137 VAL   C CG1 
2080 C CG2 . VAL   B 131 ? 0.1878 0.1982 0.1902 0.0089  0.0135  0.0076  137 VAL   C CG2 
2081 N N   . ARG   B 132 ? 0.1728 0.1834 0.1595 0.0182  0.0114  0.0006  138 ARG   C N   
2082 C CA  . ARG   B 132 ? 0.1745 0.1835 0.1534 0.0224  0.0131  0.0020  138 ARG   C CA  
2083 C C   . ARG   B 132 ? 0.1938 0.2021 0.1659 0.0274  0.0134  -0.0003 138 ARG   C C   
2084 O O   . ARG   B 132 ? 0.2123 0.2186 0.1767 0.0314  0.0163  0.0019  138 ARG   C O   
2085 C CB  . ARG   B 132 ? 0.1734 0.1819 0.1496 0.0231  0.0103  0.0008  138 ARG   C CB  
2086 C CG  . ARG   B 132 ? 0.1865 0.1947 0.1672 0.0193  0.0107  0.0032  138 ARG   C CG  
2087 C CD  . ARG   B 132 ? 0.1849 0.1929 0.1635 0.0206  0.0079  0.0013  138 ARG   C CD  
2088 N NE  . ARG   B 132 ? 0.1618 0.1727 0.1444 0.0197  0.0047  -0.0032 138 ARG   C NE  
2089 C CZ  . ARG   B 132 ? 0.1875 0.1999 0.1718 0.0201  0.0022  -0.0057 138 ARG   C CZ  
2090 N NH1 . ARG   B 132 ? 0.1767 0.1872 0.1572 0.0224  0.0018  -0.0044 138 ARG   C NH1 
2091 N NH2 . ARG   B 132 ? 0.1920 0.2076 0.1824 0.0184  0.0001  -0.0094 138 ARG   C NH2 
2092 N N   . ASP   B 133 ? 0.1862 0.1953 0.1603 0.0276  0.0104  -0.0047 139 ASP   C N   
2093 C CA  . ASP   B 133 ? 0.2098 0.2175 0.1771 0.0327  0.0098  -0.0079 139 ASP   C CA  
2094 C C   . ASP   B 133 ? 0.2228 0.2306 0.1910 0.0337  0.0142  -0.0061 139 ASP   C C   
2095 O O   . ASP   B 133 ? 0.2488 0.2551 0.2098 0.0388  0.0150  -0.0083 139 ASP   C O   
2096 C CB  . ASP   B 133 ? 0.2247 0.2327 0.1950 0.0325  0.0043  -0.0139 139 ASP   C CB  
2097 C CG  . ASP   B 133 ? 0.2506 0.2598 0.2310 0.0277  0.0037  -0.0144 139 ASP   C CG  
2098 O OD1 . ASP   B 133 ? 0.2407 0.2512 0.2270 0.0231  0.0052  -0.0111 139 ASP   C OD1 
2099 O OD2 . ASP   B 133 ? 0.2564 0.2646 0.2381 0.0288  0.0013  -0.0184 139 ASP   C OD2 
2100 N N   . LEU   B 134 ? 0.2057 0.2154 0.1825 0.0296  0.0170  -0.0026 140 LEU   C N   
2101 C CA  . LEU   B 134 ? 0.2133 0.2240 0.1934 0.0305  0.0209  -0.0011 140 LEU   C CA  
2102 C C   . LEU   B 134 ? 0.2222 0.2330 0.1987 0.0330  0.0272  0.0036  140 LEU   C C   
2103 O O   . LEU   B 134 ? 0.2205 0.2331 0.2044 0.0298  0.0304  0.0080  140 LEU   C O   
2104 C CB  . LEU   B 134 ? 0.2097 0.2222 0.2013 0.0252  0.0200  0.0003  140 LEU   C CB  
2105 C CG  . LEU   B 134 ? 0.2290 0.2407 0.2239 0.0224  0.0147  -0.0033 140 LEU   C CG  
2106 C CD1 . LEU   B 134 ? 0.2425 0.2546 0.2459 0.0177  0.0138  -0.0011 140 LEU   C CD1 
2107 C CD2 . LEU   B 134 ? 0.2295 0.2397 0.2227 0.0254  0.0127  -0.0079 140 LEU   C CD2 
2108 N N   . LEU   B 135 ? 0.2173 0.2259 0.1821 0.0388  0.0291  0.0028  141 LEU   C N   
2109 C CA  . LEU   B 135 ? 0.2426 0.2501 0.2021 0.0414  0.0359  0.0081  141 LEU   C CA  
2110 C C   . LEU   B 135 ? 0.2597 0.2702 0.2265 0.0413  0.0426  0.0114  141 LEU   C C   
2111 O O   . LEU   B 135 ? 0.2755 0.2866 0.2447 0.0406  0.0486  0.0170  141 LEU   C O   
2112 C CB  . LEU   B 135 ? 0.2482 0.2515 0.1913 0.0484  0.0365  0.0067  141 LEU   C CB  
2113 C CG  . LEU   B 135 ? 0.2653 0.2659 0.2012 0.0498  0.0291  0.0024  141 LEU   C CG  
2114 C CD1 . LEU   B 135 ? 0.2989 0.2947 0.2177 0.0573  0.0297  0.0017  141 LEU   C CD1 
2115 C CD2 . LEU   B 135 ? 0.2623 0.2637 0.2043 0.0448  0.0263  0.0043  141 LEU   C CD2 
2116 N N   . TRP   B 136 ? 0.2556 0.2680 0.2269 0.0421  0.0417  0.0078  142 TRP   C N   
2117 C CA  . TRP   B 136 ? 0.2534 0.2694 0.2331 0.0426  0.0477  0.0102  142 TRP   C CA  
2118 C C   . TRP   B 136 ? 0.2548 0.2745 0.2502 0.0364  0.0483  0.0143  142 TRP   C C   
2119 O O   . TRP   B 136 ? 0.2583 0.2817 0.2628 0.0364  0.0539  0.0172  142 TRP   C O   
2120 C CB  . TRP   B 136 ? 0.2485 0.2649 0.2297 0.0451  0.0453  0.0049  142 TRP   C CB  
2121 C CG  . TRP   B 136 ? 0.2457 0.2615 0.2327 0.0409  0.0372  0.0010  142 TRP   C CG  
2122 C CD1 . TRP   B 136 ? 0.2471 0.2597 0.2279 0.0413  0.0309  -0.0038 142 TRP   C CD1 
2123 C CD2 . TRP   B 136 ? 0.2346 0.2529 0.2353 0.0357  0.0348  0.0021  142 TRP   C CD2 
2124 N NE1 . TRP   B 136 ? 0.2460 0.2587 0.2356 0.0366  0.0257  -0.0054 142 TRP   C NE1 
2125 C CE2 . TRP   B 136 ? 0.2350 0.2508 0.2357 0.0335  0.0278  -0.0019 142 TRP   C CE2 
2126 C CE3 . TRP   B 136 ? 0.2402 0.2624 0.2533 0.0331  0.0376  0.0058  142 TRP   C CE3 
2127 C CZ2 . TRP   B 136 ? 0.2523 0.2685 0.2626 0.0289  0.0241  -0.0016 142 TRP   C CZ2 
2128 C CZ3 . TRP   B 136 ? 0.2600 0.2828 0.2830 0.0290  0.0328  0.0052  142 TRP   C CZ3 
2129 C CH2 . TRP   B 136 ? 0.2540 0.2733 0.2744 0.0272  0.0264  0.0018  142 TRP   C CH2 
2130 N N   . LEU   B 137 ? 0.2462 0.2651 0.2453 0.0313  0.0427  0.0143  143 LEU   C N   
2131 C CA  . LEU   B 137 ? 0.2494 0.2709 0.2620 0.0259  0.0424  0.0176  143 LEU   C CA  
2132 C C   . LEU   B 137 ? 0.2980 0.3203 0.3135 0.0256  0.0491  0.0234  143 LEU   C C   
2133 O O   . LEU   B 137 ? 0.3087 0.3341 0.3377 0.0222  0.0503  0.0261  143 LEU   C O   
2134 C CB  . LEU   B 137 ? 0.2372 0.2564 0.2498 0.0215  0.0358  0.0164  143 LEU   C CB  
2135 C CG  . LEU   B 137 ? 0.2339 0.2525 0.2478 0.0199  0.0296  0.0121  143 LEU   C CG  
2136 C CD1 . LEU   B 137 ? 0.2314 0.2477 0.2433 0.0163  0.0248  0.0114  143 LEU   C CD1 
2137 C CD2 . LEU   B 137 ? 0.2269 0.2481 0.2528 0.0180  0.0286  0.0124  143 LEU   C CD2 
2138 N N   . ASP   B 138 ? 0.3271 0.3461 0.3304 0.0291  0.0527  0.0252  144 ASP   C N   
2139 C CA  . ASP   B 138 ? 0.3787 0.3966 0.3818 0.0292  0.0595  0.0313  144 ASP   C CA  
2140 C C   . ASP   B 138 ? 0.4241 0.4448 0.4297 0.0326  0.0687  0.0345  144 ASP   C C   
2141 O O   . ASP   B 138 ? 0.4421 0.4620 0.4490 0.0324  0.0755  0.0402  144 ASP   C O   
2142 C CB  . ASP   B 138 ? 0.4119 0.4239 0.3982 0.0328  0.0594  0.0318  144 ASP   C CB  
2143 C CG  . ASP   B 138 ? 0.4521 0.4612 0.4353 0.0302  0.0519  0.0298  144 ASP   C CG  
2144 O OD1 . ASP   B 138 ? 0.4522 0.4629 0.4461 0.0249  0.0480  0.0294  144 ASP   C OD1 
2145 O OD2 . ASP   B 138 ? 0.4922 0.4972 0.4617 0.0340  0.0499  0.0283  144 ASP   C OD2 
2146 N N   . GLU   B 139 ? 0.4372 0.4603 0.4419 0.0362  0.0697  0.0310  145 GLU   C N   
2147 C CA  . GLU   B 139 ? 0.4706 0.4967 0.4774 0.0401  0.0792  0.0335  145 GLU   C CA  
2148 C C   . GLU   B 139 ? 0.4914 0.5238 0.5144 0.0386  0.0783  0.0311  145 GLU   C C   
2149 O O   . GLU   B 139 ? 0.5152 0.5513 0.5427 0.0419  0.0858  0.0324  145 GLU   C O   
2150 C CB  . GLU   B 139 ? 0.5161 0.5380 0.5031 0.0480  0.0817  0.0309  145 GLU   C CB  
2151 C CG  . GLU   B 139 ? 0.5932 0.6142 0.5752 0.0500  0.0740  0.0232  145 GLU   C CG  
2152 C CD  . GLU   B 139 ? 0.7377 0.7527 0.6990 0.0564  0.0717  0.0193  145 GLU   C CD  
2153 O OE1 . GLU   B 139 ? 0.7534 0.7676 0.7098 0.0604  0.0691  0.0136  145 GLU   C OE1 
2154 O OE2 . GLU   B 139 ? 0.7873 0.7978 0.7373 0.0575  0.0720  0.0218  145 GLU   C OE2 
2155 N N1  . A1BOO C .   ? 0.3717 0.3707 0.4217 0.0092  0.0349  -0.0288 201 A1BOO A N1  
2156 C C4  . A1BOO C .   ? 0.3539 0.3465 0.3985 0.0072  0.0364  -0.0356 201 A1BOO A C4  
2157 C C5  . A1BOO C .   ? 0.4370 0.4387 0.4810 0.0081  0.0363  -0.0285 201 A1BOO A C5  
2158 C C6  . A1BOO C .   ? 0.5303 0.5277 0.5586 0.0044  0.0393  -0.0351 201 A1BOO A C6  
2159 C C7  . A1BOO C .   ? 0.6365 0.6382 0.6851 0.0067  0.0542  -0.0365 201 A1BOO A C7  
2160 C C8  . A1BOO C .   ? 0.6445 0.6483 0.6903 0.0052  0.0592  -0.0375 201 A1BOO A C8  
2161 C C10 . A1BOO C .   ? 0.6377 0.6513 0.7229 0.0121  0.0620  -0.0290 201 A1BOO A C10 
2162 C C13 . A1BOO C .   ? 0.5390 0.5386 0.5547 0.0027  0.0331  -0.0315 201 A1BOO A C13 
2163 C C15 . A1BOO C .   ? 0.5421 0.5445 0.5411 -0.0001 0.0297  -0.0269 201 A1BOO A C15 
2164 C C17 . A1BOO C .   ? 0.5441 0.5458 0.5494 0.0022  0.0217  -0.0244 201 A1BOO A C17 
2165 O O1  . A1BOO C .   ? 0.4174 0.4245 0.4662 0.0091  0.0345  -0.0228 201 A1BOO A O1  
2166 C C3  . A1BOO C .   ? 0.3388 0.3311 0.3785 0.0062  0.0294  -0.0338 201 A1BOO A C3  
2167 C C2  . A1BOO C .   ? 0.3119 0.3070 0.3631 0.0091  0.0264  -0.0269 201 A1BOO A C2  
2168 C C19 . A1BOO C .   ? 0.3191 0.3214 0.3811 0.0117  0.0312  -0.0218 201 A1BOO A C19 
2169 C C1  . A1BOO C .   ? 0.2876 0.2884 0.3424 0.0105  0.0253  -0.0204 201 A1BOO A C1  
2170 C C   . A1BOO C .   ? 0.2598 0.2631 0.3239 0.0120  0.0220  -0.0133 201 A1BOO A C   
2171 O O   . A1BOO C .   ? 0.2663 0.2719 0.3246 0.0107  0.0176  -0.0091 201 A1BOO A O   
2172 N N   . A1BOO C .   ? 0.2339 0.2362 0.3121 0.0141  0.0244  -0.0117 201 A1BOO A N   
2173 C C18 . A1BOO C .   ? 0.5397 0.5398 0.5533 0.0031  0.0263  -0.0280 201 A1BOO A C18 
2174 C C16 . A1BOO C .   ? 0.5418 0.5443 0.5399 0.0006  0.0233  -0.0237 201 A1BOO A C16 
2175 C C14 . A1BOO C .   ? 0.5392 0.5401 0.5471 0.0010  0.0350  -0.0310 201 A1BOO A C14 
2176 S S   . A1BOO C .   ? 0.6221 0.6164 0.6503 0.0027  0.0506  -0.0423 201 A1BOO A S   
2177 C C12 . A1BOO C .   ? 0.6424 0.6473 0.7105 0.0108  0.0533  -0.0317 201 A1BOO A C12 
2178 C C11 . A1BOO C .   ? 0.6393 0.6502 0.7255 0.0134  0.0569  -0.0276 201 A1BOO A C11 
2179 C C9  . A1BOO C .   ? 0.6426 0.6522 0.7069 0.0079  0.0636  -0.0342 201 A1BOO A C9  
2185 N N1  . A1BOO F .   ? 0.3286 0.2907 0.3143 -0.0206 0.0209  0.0219  201 A1BOO C N1  
2186 C C4  . A1BOO F .   ? 0.3124 0.2652 0.2903 -0.0198 0.0181  0.0254  201 A1BOO C C4  
2187 C C5  . A1BOO F .   ? 0.4011 0.3660 0.3830 -0.0204 0.0247  0.0216  201 A1BOO C C5  
2188 C C6  . A1BOO F .   ? 0.5098 0.4676 0.4764 -0.0185 0.0249  0.0245  201 A1BOO C C6  
2189 C C7  . A1BOO F .   ? 0.6392 0.5951 0.6095 -0.0235 0.0399  0.0296  201 A1BOO C C7  
2190 C C8  . A1BOO F .   ? 0.6444 0.6089 0.6209 -0.0235 0.0432  0.0264  201 A1BOO C C8  
2191 C C10 . A1BOO F .   ? 0.6501 0.6140 0.6403 -0.0296 0.0544  0.0310  201 A1BOO C C10 
2192 C C13 . A1BOO F .   ? 0.5095 0.4722 0.4739 -0.0163 0.0233  0.0213  201 A1BOO C C13 
2193 C C15 . A1BOO F .   ? 0.5084 0.4781 0.4749 -0.0131 0.0160  0.0161  201 A1BOO C C15 
2194 C C17 . A1BOO F .   ? 0.5080 0.4746 0.4645 -0.0135 0.0256  0.0182  201 A1BOO C C17 
2195 O O1  . A1BOO F .   ? 0.3481 0.3206 0.3378 -0.0209 0.0267  0.0185  201 A1BOO C O1  
2196 C C3  . A1BOO F .   ? 0.2976 0.2514 0.2762 -0.0171 0.0113  0.0234  201 A1BOO C C3  
2197 C C2  . A1BOO F .   ? 0.2822 0.2429 0.2732 -0.0172 0.0096  0.0195  201 A1BOO C C2  
2198 C C19 . A1BOO F .   ? 0.2764 0.2446 0.2744 -0.0210 0.0186  0.0180  201 A1BOO C C19 
2199 C C1  . A1BOO F .   ? 0.2553 0.2242 0.2527 -0.0182 0.0128  0.0163  201 A1BOO C C1  
2200 C C   . A1BOO F .   ? 0.2339 0.2080 0.2417 -0.0180 0.0109  0.0123  201 A1BOO C C   
2201 O O   . A1BOO F .   ? 0.2221 0.1941 0.2360 -0.0196 0.0111  0.0120  201 A1BOO C O   
2202 N N   . A1BOO F .   ? 0.2144 0.1947 0.2238 -0.0159 0.0092  0.0092  201 A1BOO C N   
2203 C C18 . A1BOO F .   ? 0.5083 0.4716 0.4669 -0.0156 0.0277  0.0212  201 A1BOO C C18 
2204 C C16 . A1BOO F .   ? 0.5049 0.4744 0.4656 -0.0124 0.0197  0.0158  201 A1BOO C C16 
2205 C C14 . A1BOO F .   ? 0.5100 0.4763 0.4783 -0.0148 0.0175  0.0186  201 A1BOO C C14 
2206 S S   . A1BOO F .   ? 0.6182 0.5673 0.5737 -0.0196 0.0323  0.0300  201 A1BOO C S   
2207 C C12 . A1BOO F .   ? 0.6546 0.6055 0.6283 -0.0264 0.0435  0.0334  201 A1BOO C C12 
2208 C C11 . A1BOO F .   ? 0.6561 0.6107 0.6396 -0.0296 0.0509  0.0343  201 A1BOO C C11 
2209 C C9  . A1BOO F .   ? 0.6450 0.6136 0.6312 -0.0263 0.0503  0.0270  201 A1BOO C C9  
# 
