data_7I6C
# 
_entry.id   7I6C 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   7I6C         pdb_00007i6c 10.2210/pdb7i6c/pdb 
WWPDB D_1001408371 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I6C 
_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   2025-03-12 
_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 '(1R,5R)-3-{[2-(methylsulfanyl)phenyl]acetyl}-3-azabicyclo[3.1.0]hexane-1-carboxamide' 290.381   1   ?         ? 
? ? 
3 non-polymer syn 'ZINC ION'                                                                             65.409    2   ?         ? 
? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                   78.133    2   ?         ? 
? ? 
5 water       nat water                                                                                  18.015    276 ?         ? 
? ? 
# 
_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 '(1R,5R)-3-{[2-(methylsulfanyl)phenyl]acetyl}-3-azabicyclo[3.1.0]hexane-1-carboxamide' A1B40 
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 
A1B40 non-polymer         . '(1R,5R)-3-{[2-(methylsulfanyl)phenyl]acetyl}-3-azabicyclo[3.1.0]hexane-1-carboxamide' ? 
'C15 H18 N2 O2 S' 290.381 
ALA   'L-peptide linking' y ALANINE                                                                                ? 'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                                               ? 
'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                             ? 'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                        ? 'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                               ? 
'C3 H7 N O2 S'    121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                   ? 'C2 H6 O S' 
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                              ? 
'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                        ? 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                                                ? 'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                              ? 
'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                                                  ? 'H2 O' 18.015 
ILE   'L-peptide linking' y ISOLEUCINE                                                                             ? 'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                ? 'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                                                                 ? 
'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                                             ? 
'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                          ? 'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                                                                ? 'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                                                 ? 'C3 H7 N O3' 
105.093 
THR   'L-peptide linking' y THREONINE                                                                              ? 'C4 H9 N O3' 
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                             ? 
'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                                               ? 'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                                                 ? 'C5 H11 N O2' 
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                             ? 'Zn 2' 65.409 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 146 GLU GLU C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B40 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B40 
_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 A1B40 1   201 201 A1B40 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 1   DMS   DMS A . 
F 3 ZN    1   201 1   ZN    ZN  C . 
G 4 DMS   1   202 1   DMS   DMS C . 
H 5 HOH   1   301 265 HOH   HOH A . 
H 5 HOH   2   302 101 HOH   HOH A . 
H 5 HOH   3   303 238 HOH   HOH A . 
H 5 HOH   4   304 208 HOH   HOH A . 
H 5 HOH   5   305 82  HOH   HOH A . 
H 5 HOH   6   306 125 HOH   HOH A . 
H 5 HOH   7   307 59  HOH   HOH A . 
H 5 HOH   8   308 260 HOH   HOH A . 
H 5 HOH   9   309 236 HOH   HOH A . 
H 5 HOH   10  310 275 HOH   HOH A . 
H 5 HOH   11  311 112 HOH   HOH A . 
H 5 HOH   12  312 171 HOH   HOH A . 
H 5 HOH   13  313 26  HOH   HOH A . 
H 5 HOH   14  314 79  HOH   HOH A . 
H 5 HOH   15  315 183 HOH   HOH A . 
H 5 HOH   16  316 9   HOH   HOH A . 
H 5 HOH   17  317 43  HOH   HOH A . 
H 5 HOH   18  318 151 HOH   HOH A . 
H 5 HOH   19  319 138 HOH   HOH A . 
H 5 HOH   20  320 186 HOH   HOH A . 
H 5 HOH   21  321 41  HOH   HOH A . 
H 5 HOH   22  322 170 HOH   HOH A . 
H 5 HOH   23  323 142 HOH   HOH A . 
H 5 HOH   24  324 81  HOH   HOH A . 
H 5 HOH   25  325 69  HOH   HOH A . 
H 5 HOH   26  326 33  HOH   HOH A . 
H 5 HOH   27  327 122 HOH   HOH A . 
H 5 HOH   28  328 106 HOH   HOH A . 
H 5 HOH   29  329 257 HOH   HOH A . 
H 5 HOH   30  330 240 HOH   HOH A . 
H 5 HOH   31  331 168 HOH   HOH A . 
H 5 HOH   32  332 37  HOH   HOH A . 
H 5 HOH   33  333 243 HOH   HOH A . 
H 5 HOH   34  334 224 HOH   HOH A . 
H 5 HOH   35  335 4   HOH   HOH A . 
H 5 HOH   36  336 55  HOH   HOH A . 
H 5 HOH   37  337 166 HOH   HOH A . 
H 5 HOH   38  338 227 HOH   HOH A . 
H 5 HOH   39  339 116 HOH   HOH A . 
H 5 HOH   40  340 152 HOH   HOH A . 
H 5 HOH   41  341 156 HOH   HOH A . 
H 5 HOH   42  342 206 HOH   HOH A . 
H 5 HOH   43  343 8   HOH   HOH A . 
H 5 HOH   44  344 6   HOH   HOH A . 
H 5 HOH   45  345 121 HOH   HOH A . 
H 5 HOH   46  346 58  HOH   HOH A . 
H 5 HOH   47  347 196 HOH   HOH A . 
H 5 HOH   48  348 221 HOH   HOH A . 
H 5 HOH   49  349 167 HOH   HOH A . 
H 5 HOH   50  350 135 HOH   HOH A . 
H 5 HOH   51  351 252 HOH   HOH A . 
H 5 HOH   52  352 190 HOH   HOH A . 
H 5 HOH   53  353 195 HOH   HOH A . 
H 5 HOH   54  354 38  HOH   HOH A . 
H 5 HOH   55  355 78  HOH   HOH A . 
H 5 HOH   56  356 182 HOH   HOH A . 
H 5 HOH   57  357 102 HOH   HOH A . 
H 5 HOH   58  358 1   HOH   HOH A . 
H 5 HOH   59  359 60  HOH   HOH A . 
H 5 HOH   60  360 42  HOH   HOH A . 
H 5 HOH   61  361 50  HOH   HOH A . 
H 5 HOH   62  362 47  HOH   HOH A . 
H 5 HOH   63  363 86  HOH   HOH A . 
H 5 HOH   64  364 113 HOH   HOH A . 
H 5 HOH   65  365 87  HOH   HOH A . 
H 5 HOH   66  366 259 HOH   HOH A . 
H 5 HOH   67  367 222 HOH   HOH A . 
H 5 HOH   68  368 51  HOH   HOH A . 
H 5 HOH   69  369 13  HOH   HOH A . 
H 5 HOH   70  370 40  HOH   HOH A . 
H 5 HOH   71  371 159 HOH   HOH A . 
H 5 HOH   72  372 20  HOH   HOH A . 
H 5 HOH   73  373 64  HOH   HOH A . 
H 5 HOH   74  374 118 HOH   HOH A . 
H 5 HOH   75  375 211 HOH   HOH A . 
H 5 HOH   76  376 49  HOH   HOH A . 
H 5 HOH   77  377 230 HOH   HOH A . 
H 5 HOH   78  378 99  HOH   HOH A . 
H 5 HOH   79  379 62  HOH   HOH A . 
H 5 HOH   80  380 48  HOH   HOH A . 
H 5 HOH   81  381 165 HOH   HOH A . 
H 5 HOH   82  382 220 HOH   HOH A . 
H 5 HOH   83  383 148 HOH   HOH A . 
H 5 HOH   84  384 153 HOH   HOH A . 
H 5 HOH   85  385 254 HOH   HOH A . 
H 5 HOH   86  386 185 HOH   HOH A . 
H 5 HOH   87  387 251 HOH   HOH A . 
H 5 HOH   88  388 253 HOH   HOH A . 
H 5 HOH   89  389 76  HOH   HOH A . 
H 5 HOH   90  390 73  HOH   HOH A . 
H 5 HOH   91  391 126 HOH   HOH A . 
H 5 HOH   92  392 134 HOH   HOH A . 
H 5 HOH   93  393 164 HOH   HOH A . 
H 5 HOH   94  394 245 HOH   HOH A . 
H 5 HOH   95  395 3   HOH   HOH A . 
H 5 HOH   96  396 34  HOH   HOH A . 
H 5 HOH   97  397 212 HOH   HOH A . 
H 5 HOH   98  398 235 HOH   HOH A . 
H 5 HOH   99  399 117 HOH   HOH A . 
H 5 HOH   100 400 85  HOH   HOH A . 
H 5 HOH   101 401 145 HOH   HOH A . 
H 5 HOH   102 402 149 HOH   HOH A . 
H 5 HOH   103 403 192 HOH   HOH A . 
H 5 HOH   104 404 72  HOH   HOH A . 
H 5 HOH   105 405 231 HOH   HOH A . 
H 5 HOH   106 406 30  HOH   HOH A . 
H 5 HOH   107 407 114 HOH   HOH A . 
H 5 HOH   108 408 109 HOH   HOH A . 
H 5 HOH   109 409 225 HOH   HOH A . 
H 5 HOH   110 410 214 HOH   HOH A . 
H 5 HOH   111 411 39  HOH   HOH A . 
H 5 HOH   112 412 198 HOH   HOH A . 
H 5 HOH   113 413 262 HOH   HOH A . 
H 5 HOH   114 414 31  HOH   HOH A . 
H 5 HOH   115 415 84  HOH   HOH A . 
H 5 HOH   116 416 239 HOH   HOH A . 
H 5 HOH   117 417 19  HOH   HOH A . 
H 5 HOH   118 418 193 HOH   HOH A . 
H 5 HOH   119 419 56  HOH   HOH A . 
H 5 HOH   120 420 241 HOH   HOH A . 
H 5 HOH   121 421 105 HOH   HOH A . 
H 5 HOH   122 422 141 HOH   HOH A . 
H 5 HOH   123 423 202 HOH   HOH A . 
H 5 HOH   124 424 92  HOH   HOH A . 
H 5 HOH   125 425 140 HOH   HOH A . 
H 5 HOH   126 426 269 HOH   HOH A . 
H 5 HOH   127 427 169 HOH   HOH A . 
H 5 HOH   128 428 176 HOH   HOH A . 
H 5 HOH   129 429 160 HOH   HOH A . 
H 5 HOH   130 430 210 HOH   HOH A . 
H 5 HOH   131 431 261 HOH   HOH A . 
H 5 HOH   132 432 194 HOH   HOH A . 
H 5 HOH   133 433 279 HOH   HOH A . 
H 5 HOH   134 434 248 HOH   HOH A . 
H 5 HOH   135 435 146 HOH   HOH A . 
H 5 HOH   136 436 130 HOH   HOH A . 
H 5 HOH   137 437 174 HOH   HOH A . 
H 5 HOH   138 438 203 HOH   HOH A . 
H 5 HOH   139 439 277 HOH   HOH A . 
H 5 HOH   140 440 147 HOH   HOH A . 
H 5 HOH   141 441 143 HOH   HOH A . 
H 5 HOH   142 442 278 HOH   HOH A . 
I 5 HOH   1   301 150 HOH   HOH C . 
I 5 HOH   2   302 223 HOH   HOH C . 
I 5 HOH   3   303 270 HOH   HOH C . 
I 5 HOH   4   304 273 HOH   HOH C . 
I 5 HOH   5   305 213 HOH   HOH C . 
I 5 HOH   6   306 162 HOH   HOH C . 
I 5 HOH   7   307 88  HOH   HOH C . 
I 5 HOH   8   308 155 HOH   HOH C . 
I 5 HOH   9   309 16  HOH   HOH C . 
I 5 HOH   10  310 274 HOH   HOH C . 
I 5 HOH   11  311 132 HOH   HOH C . 
I 5 HOH   12  312 74  HOH   HOH C . 
I 5 HOH   13  313 180 HOH   HOH C . 
I 5 HOH   14  314 177 HOH   HOH C . 
I 5 HOH   15  315 119 HOH   HOH C . 
I 5 HOH   16  316 232 HOH   HOH C . 
I 5 HOH   17  317 52  HOH   HOH C . 
I 5 HOH   18  318 68  HOH   HOH C . 
I 5 HOH   19  319 80  HOH   HOH C . 
I 5 HOH   20  320 244 HOH   HOH C . 
I 5 HOH   21  321 67  HOH   HOH C . 
I 5 HOH   22  322 89  HOH   HOH C . 
I 5 HOH   23  323 61  HOH   HOH C . 
I 5 HOH   24  324 107 HOH   HOH C . 
I 5 HOH   25  325 104 HOH   HOH C . 
I 5 HOH   26  326 247 HOH   HOH C . 
I 5 HOH   27  327 154 HOH   HOH C . 
I 5 HOH   28  328 229 HOH   HOH C . 
I 5 HOH   29  329 115 HOH   HOH C . 
I 5 HOH   30  330 25  HOH   HOH C . 
I 5 HOH   31  331 204 HOH   HOH C . 
I 5 HOH   32  332 70  HOH   HOH C . 
I 5 HOH   33  333 136 HOH   HOH C . 
I 5 HOH   34  334 207 HOH   HOH C . 
I 5 HOH   35  335 10  HOH   HOH C . 
I 5 HOH   36  336 95  HOH   HOH C . 
I 5 HOH   37  337 94  HOH   HOH C . 
I 5 HOH   38  338 163 HOH   HOH C . 
I 5 HOH   39  339 12  HOH   HOH C . 
I 5 HOH   40  340 215 HOH   HOH C . 
I 5 HOH   41  341 137 HOH   HOH C . 
I 5 HOH   42  342 2   HOH   HOH C . 
I 5 HOH   43  343 175 HOH   HOH C . 
I 5 HOH   44  344 15  HOH   HOH C . 
I 5 HOH   45  345 256 HOH   HOH C . 
I 5 HOH   46  346 54  HOH   HOH C . 
I 5 HOH   47  347 124 HOH   HOH C . 
I 5 HOH   48  348 255 HOH   HOH C . 
I 5 HOH   49  349 97  HOH   HOH C . 
I 5 HOH   50  350 65  HOH   HOH C . 
I 5 HOH   51  351 14  HOH   HOH C . 
I 5 HOH   52  352 191 HOH   HOH C . 
I 5 HOH   53  353 35  HOH   HOH C . 
I 5 HOH   54  354 157 HOH   HOH C . 
I 5 HOH   55  355 181 HOH   HOH C . 
I 5 HOH   56  356 120 HOH   HOH C . 
I 5 HOH   57  357 158 HOH   HOH C . 
I 5 HOH   58  358 264 HOH   HOH C . 
I 5 HOH   59  359 27  HOH   HOH C . 
I 5 HOH   60  360 161 HOH   HOH C . 
I 5 HOH   61  361 96  HOH   HOH C . 
I 5 HOH   62  362 71  HOH   HOH C . 
I 5 HOH   63  363 90  HOH   HOH C . 
I 5 HOH   64  364 219 HOH   HOH C . 
I 5 HOH   65  365 246 HOH   HOH C . 
I 5 HOH   66  366 36  HOH   HOH C . 
I 5 HOH   67  367 18  HOH   HOH C . 
I 5 HOH   68  368 83  HOH   HOH C . 
I 5 HOH   69  369 98  HOH   HOH C . 
I 5 HOH   70  370 127 HOH   HOH C . 
I 5 HOH   71  371 11  HOH   HOH C . 
I 5 HOH   72  372 218 HOH   HOH C . 
I 5 HOH   73  373 57  HOH   HOH C . 
I 5 HOH   74  374 23  HOH   HOH C . 
I 5 HOH   75  375 249 HOH   HOH C . 
I 5 HOH   76  376 123 HOH   HOH C . 
I 5 HOH   77  377 187 HOH   HOH C . 
I 5 HOH   78  378 93  HOH   HOH C . 
I 5 HOH   79  379 128 HOH   HOH C . 
I 5 HOH   80  380 28  HOH   HOH C . 
I 5 HOH   81  381 7   HOH   HOH C . 
I 5 HOH   82  382 45  HOH   HOH C . 
I 5 HOH   83  383 53  HOH   HOH C . 
I 5 HOH   84  384 233 HOH   HOH C . 
I 5 HOH   85  385 108 HOH   HOH C . 
I 5 HOH   86  386 234 HOH   HOH C . 
I 5 HOH   87  387 226 HOH   HOH C . 
I 5 HOH   88  388 188 HOH   HOH C . 
I 5 HOH   89  389 110 HOH   HOH C . 
I 5 HOH   90  390 250 HOH   HOH C . 
I 5 HOH   91  391 32  HOH   HOH C . 
I 5 HOH   92  392 103 HOH   HOH C . 
I 5 HOH   93  393 29  HOH   HOH C . 
I 5 HOH   94  394 209 HOH   HOH C . 
I 5 HOH   95  395 100 HOH   HOH C . 
I 5 HOH   96  396 91  HOH   HOH C . 
I 5 HOH   97  397 129 HOH   HOH C . 
I 5 HOH   98  398 178 HOH   HOH C . 
I 5 HOH   99  399 63  HOH   HOH C . 
I 5 HOH   100 400 75  HOH   HOH C . 
I 5 HOH   101 401 228 HOH   HOH C . 
I 5 HOH   102 402 5   HOH   HOH C . 
I 5 HOH   103 403 46  HOH   HOH C . 
I 5 HOH   104 404 44  HOH   HOH C . 
I 5 HOH   105 405 66  HOH   HOH C . 
I 5 HOH   106 406 133 HOH   HOH C . 
I 5 HOH   107 407 21  HOH   HOH C . 
I 5 HOH   108 408 172 HOH   HOH C . 
I 5 HOH   109 409 24  HOH   HOH C . 
I 5 HOH   110 410 189 HOH   HOH C . 
I 5 HOH   111 411 17  HOH   HOH C . 
I 5 HOH   112 412 267 HOH   HOH C . 
I 5 HOH   113 413 144 HOH   HOH C . 
I 5 HOH   114 414 173 HOH   HOH C . 
I 5 HOH   115 415 139 HOH   HOH C . 
I 5 HOH   116 416 131 HOH   HOH C . 
I 5 HOH   117 417 266 HOH   HOH C . 
I 5 HOH   118 418 199 HOH   HOH C . 
I 5 HOH   119 419 217 HOH   HOH C . 
I 5 HOH   120 420 200 HOH   HOH C . 
I 5 HOH   121 421 205 HOH   HOH C . 
I 5 HOH   122 422 268 HOH   HOH C . 
I 5 HOH   123 423 237 HOH   HOH C . 
I 5 HOH   124 424 271 HOH   HOH C . 
I 5 HOH   125 425 184 HOH   HOH C . 
I 5 HOH   126 426 276 HOH   HOH C . 
I 5 HOH   127 427 111 HOH   HOH C . 
I 5 HOH   128 428 263 HOH   HOH C . 
I 5 HOH   129 429 216 HOH   HOH C . 
I 5 HOH   130 430 272 HOH   HOH C . 
I 5 HOH   131 431 242 HOH   HOH C . 
I 5 HOH   132 432 201 HOH   HOH C . 
I 5 HOH   133 433 197 HOH   HOH C . 
I 5 HOH   134 434 179 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           7I6C 
_cell.length_a           86.708 
_cell.length_b           57.731 
_cell.length_c           64.991 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.82 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I6C 
_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          7I6C 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.55 
_exptl_crystal.density_percent_sol   51.76 
_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   2025-01-30 
_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   0.92204 
_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        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I6C 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             37.74 
_reflns.d_resolution_high            1.39 
_reflns.number_obs                   62439 
_reflns.percent_possible_obs         96.4 
_reflns.pdbx_Rmerge_I_obs            0.151 
_reflns.pdbx_netI_over_sigmaI        4.5 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.164 
_reflns.pdbx_Rpim_I_all              0.064 
_reflns.pdbx_CC_half                 0.992 
_reflns.pdbx_number_measured_all     394881 
_reflns.pdbx_chi_squared             0.29 
_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                  1.39 
_reflns_shell.d_res_low                   1.41 
_reflns_shell.number_measured_all         11893 
_reflns_shell.number_unique_obs           2642 
_reflns_shell.Rmerge_I_obs                2.889 
_reflns_shell.pdbx_chi_squared            0.02 
_reflns_shell.pdbx_redundancy             4.5 
_reflns_shell.percent_possible_obs        82.4 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             3.276 
_reflns_shell.pdbx_Rpim_I_all             1.517 
_reflns_shell.pdbx_CC_half                0.277 
_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                                 7I6C 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     50102 
_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                             37.73 
_refine.ls_d_res_high                            1.407 
_refine.ls_percent_reflns_obs                    80.8 
_refine.ls_R_factor_obs                          0.2132 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2126 
_refine.ls_R_factor_R_free                       0.2247 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  2505 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.942 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_refine.B_iso_mean                               23.03 
_refine.aniso_B[1][1]                            -1.78060 
_refine.aniso_B[2][2]                            -3.07410 
_refine.aniso_B[3][3]                            4.85480 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -3.34090 
_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             0.080 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.075 
_refine.pdbx_overall_SU_R_Blow_DPI               0.083 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.078 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I6C 
_refine_analyze.Luzzati_coordinate_error_obs    0.23 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             276 
_refine_hist.number_atoms_total               2472 
_refine_hist.d_res_high                       1.407 
_refine_hist.d_res_low                        37.73 
# 
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  2275 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.95  ? 2.00  3105 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  765  '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  408  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2275 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.80  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.28 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  282  '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  1866 '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                       1.41 
_refine_ls_shell.d_res_low                        1.48 
_refine_ls_shell.number_reflns_R_work             942 
_refine_ls_shell.R_factor_R_work                  0.3967 
_refine_ls_shell.percent_reflns_obs               10.82 
_refine_ls_shell.R_factor_R_free                  0.4352 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            6.08 
_refine_ls_shell.number_reflns_R_free             61 
_refine_ls_shell.number_reflns_all                1003 
_refine_ls_shell.R_factor_all                     0.3990 
# 
_struct.entry_id                  7I6C 
_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-0037612-001 (A71EV2A-x4947)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I6C 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I6C A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I6C C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,H 
2 1 B,F,G,I   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.437 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.358 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.110 ? ? 
# 
_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_555 109.2 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 105.6 ? 
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_555 115.6 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 107.4 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 104.2 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 114.6 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 110.8 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 108.6 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.9 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 107.0 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 99.4  ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 112.4 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I6C 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN C 14 ? ? -99.75  38.86   
2 1 CYS C 56 ? ? -170.09 -178.76 
# 
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 14.9113 8.2339   14.3745 -0.0590 -0.0292 0.0355 0.0144 -0.0211 0.0002 1.2141 0.6392 0.6127 0.6728  
-0.1081 -0.0897 -0.0289 0.0190 0.0798 0.0109 0.0482 0.0044 0.0335 -0.0253 -0.0192 
'X-RAY DIFFRACTION' 2 ? refined 25.8046 -20.4180 17.7542 -0.0599 -0.0236 0.0365 0.0040 -0.0178 0.0135 0.7435 0.8582 0.3645 -0.1299 
0.0786  -0.0842 0.0018  0.0012 0.1050 0.0053 0.0467 0.0465 0.0394 0.0287  -0.0485 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B40 N1   N  N N 1   
A1B40 C4   C  Y N 2   
A1B40 C5   C  Y N 3   
A1B40 C6   C  Y N 4   
A1B40 C7   C  N N 5   
A1B40 C8   C  N N 6   
A1B40 C10  C  N R 7   
A1B40 C13  C  N N 8   
A1B40 O1   O  N N 9   
A1B40 C12  C  N R 10  
A1B40 C11  C  N N 11  
A1B40 C9   C  N N 12  
A1B40 C14  C  N N 13  
A1B40 N    N  N N 14  
A1B40 O    O  N N 15  
A1B40 C1   C  Y N 16  
A1B40 S    S  N N 17  
A1B40 C    C  N N 18  
A1B40 C3   C  Y N 19  
A1B40 C2   C  Y N 20  
A1B40 H15  H  N N 21  
A1B40 H14  H  N N 22  
A1B40 H6   H  N N 23  
A1B40 H7   H  N N 24  
A1B40 H8   H  N N 25  
A1B40 H9   H  N N 26  
A1B40 H    H  N N 27  
A1B40 H12  H  N N 28  
A1B40 H13  H  N N 29  
A1B40 H10  H  N N 30  
A1B40 H11  H  N N 31  
A1B40 H16  H  N N 32  
A1B40 H17  H  N N 33  
A1B40 H2   H  N N 34  
A1B40 H1   H  N N 35  
A1B40 H3   H  N N 36  
A1B40 H5   H  N N 37  
A1B40 H4   H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
DMS   S    S  N N 126 
DMS   O    O  N N 127 
DMS   C1   C  N N 128 
DMS   C2   C  N N 129 
DMS   H11  H  N N 130 
DMS   H12  H  N N 131 
DMS   H13  H  N N 132 
DMS   H21  H  N N 133 
DMS   H22  H  N N 134 
DMS   H23  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
THR   N    N  N N 352 
THR   CA   C  N S 353 
THR   C    C  N N 354 
THR   O    O  N N 355 
THR   CB   C  N R 356 
THR   OG1  O  N N 357 
THR   CG2  C  N N 358 
THR   OXT  O  N N 359 
THR   H    H  N N 360 
THR   H2   H  N N 361 
THR   HA   H  N N 362 
THR   HB   H  N N 363 
THR   HG1  H  N N 364 
THR   HG21 H  N N 365 
THR   HG22 H  N N 366 
THR   HG23 H  N N 367 
THR   HXT  H  N N 368 
TRP   N    N  N N 369 
TRP   CA   C  N S 370 
TRP   C    C  N N 371 
TRP   O    O  N N 372 
TRP   CB   C  N N 373 
TRP   CG   C  Y N 374 
TRP   CD1  C  Y N 375 
TRP   CD2  C  Y N 376 
TRP   NE1  N  Y N 377 
TRP   CE2  C  Y N 378 
TRP   CE3  C  Y N 379 
TRP   CZ2  C  Y N 380 
TRP   CZ3  C  Y N 381 
TRP   CH2  C  Y N 382 
TRP   OXT  O  N N 383 
TRP   H    H  N N 384 
TRP   H2   H  N N 385 
TRP   HA   H  N N 386 
TRP   HB2  H  N N 387 
TRP   HB3  H  N N 388 
TRP   HD1  H  N N 389 
TRP   HE1  H  N N 390 
TRP   HE3  H  N N 391 
TRP   HZ2  H  N N 392 
TRP   HZ3  H  N N 393 
TRP   HH2  H  N N 394 
TRP   HXT  H  N N 395 
TYR   N    N  N N 396 
TYR   CA   C  N S 397 
TYR   C    C  N N 398 
TYR   O    O  N N 399 
TYR   CB   C  N N 400 
TYR   CG   C  Y N 401 
TYR   CD1  C  Y N 402 
TYR   CD2  C  Y N 403 
TYR   CE1  C  Y N 404 
TYR   CE2  C  Y N 405 
TYR   CZ   C  Y N 406 
TYR   OH   O  N N 407 
TYR   OXT  O  N N 408 
TYR   H    H  N N 409 
TYR   H2   H  N N 410 
TYR   HA   H  N N 411 
TYR   HB2  H  N N 412 
TYR   HB3  H  N N 413 
TYR   HD1  H  N N 414 
TYR   HD2  H  N N 415 
TYR   HE1  H  N N 416 
TYR   HE2  H  N N 417 
TYR   HH   H  N N 418 
TYR   HXT  H  N N 419 
VAL   N    N  N N 420 
VAL   CA   C  N S 421 
VAL   C    C  N N 422 
VAL   O    O  N N 423 
VAL   CB   C  N N 424 
VAL   CG1  C  N N 425 
VAL   CG2  C  N N 426 
VAL   OXT  O  N N 427 
VAL   H    H  N N 428 
VAL   H2   H  N N 429 
VAL   HA   H  N N 430 
VAL   HB   H  N N 431 
VAL   HG11 H  N N 432 
VAL   HG12 H  N N 433 
VAL   HG13 H  N N 434 
VAL   HG21 H  N N 435 
VAL   HG22 H  N N 436 
VAL   HG23 H  N N 437 
VAL   HXT  H  N N 438 
ZN    ZN   ZN N N 439 
# 
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 
A1B40 C   S    sing N N 1   
A1B40 S   C1   sing N N 2   
A1B40 C1  C2   doub Y N 3   
A1B40 C2  C3   sing Y N 4   
A1B40 C3  C4   doub Y N 5   
A1B40 C4  C5   sing Y N 6   
A1B40 C5  C6   doub Y N 7   
A1B40 C1  C6   sing Y N 8   
A1B40 C6  C7   sing N N 9   
A1B40 C7  C8   sing N N 10  
A1B40 O   C8   doub N N 11  
A1B40 C8  N    sing N N 12  
A1B40 N   C9   sing N N 13  
A1B40 C9  C10  sing N N 14  
A1B40 C10 C11  sing N N 15  
A1B40 C11 C12  sing N N 16  
A1B40 C10 C12  sing N N 17  
A1B40 C12 C13  sing N N 18  
A1B40 N1  C13  sing N N 19  
A1B40 C13 O1   doub N N 20  
A1B40 C14 C12  sing N N 21  
A1B40 N   C14  sing N N 22  
A1B40 N1  H15  sing N N 23  
A1B40 N1  H14  sing N N 24  
A1B40 C4  H6   sing N N 25  
A1B40 C5  H7   sing N N 26  
A1B40 C7  H8   sing N N 27  
A1B40 C7  H9   sing N N 28  
A1B40 C10 H    sing N N 29  
A1B40 C11 H12  sing N N 30  
A1B40 C11 H13  sing N N 31  
A1B40 C9  H10  sing N N 32  
A1B40 C9  H11  sing N N 33  
A1B40 C14 H16  sing N N 34  
A1B40 C14 H17  sing N N 35  
A1B40 C   H2   sing N N 36  
A1B40 C   H1   sing N N 37  
A1B40 C   H3   sing N N 38  
A1B40 C3  H5   sing N N 39  
A1B40 C2  H4   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_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                    7I6C 
_atom_sites.fract_transf_matrix[1][1]   0.011533 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000973 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017322 
_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]   0.015441 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.549 8.332   24.847 1.00 18.89 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.807 8.384   24.084 1.00 19.70 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 18.943 7.135   23.187 1.00 19.35 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.222 6.137   23.389 1.00 19.15 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.001 8.482   25.041 1.00 22.21 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.102 7.272   25.766 1.00 25.06 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.855 7.195   22.217 1.00 19.36 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.094 6.075   21.307 1.00 19.24 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.570 6.537   19.944 1.00 18.74 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.280 7.664   19.530 1.00 18.87 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.281 5.666   19.221 1.00 17.70 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.804 6.029   17.912 1.00 17.41 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.831 4.812   16.980 1.00 17.30 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.716 3.665   17.455 1.00 17.45 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.219 6.581   18.080 1.00 17.33 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.954 5.055   15.661 1.00 16.60 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.145 3.973   14.686 1.00 16.58 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.627 4.037   14.308 1.00 17.21 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.126 5.147   14.028 1.00 17.67 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.275 4.165   13.410 1.00 17.45 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.766 4.236   13.745 1.00 18.43 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.527 3.053   12.410 1.00 17.73 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.893 4.803   12.542 1.00 18.73 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.340 2.878   14.271 1.00 17.13 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.735 2.902   13.853 1.00 17.87 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.856 2.062   12.555 1.00 18.71 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.813 0.835   12.601 1.00 19.12 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.657 2.354   14.973 1.00 17.49 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.671 3.252   16.198 1.00 17.42 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.511 4.359   16.266 1.00 17.88 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.831 3.003   17.283 1.00 18.00 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.513 5.205   17.380 1.00 18.61 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.819 3.850   18.401 1.00 18.40 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.668 4.947   18.444 1.00 19.83 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.662 5.798   19.542 1.00 22.24 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.987 2.730   11.405 1.00 18.42 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.085 2.039   10.116 1.00 19.19 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.296 2.584   9.400  1.00 20.04 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.488 3.807   9.368  1.00 20.16 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.782 2.209   9.274  1.00 19.76 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.366 3.682   9.160  1.00 20.18 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.942 1.573   7.894  1.00 20.07 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.205 1.695   8.945  1.00 20.58 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.440 2.142   8.310  1.00 20.58 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.228 3.060   9.240  1.00 19.98 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.293 2.786   10.442 1.00 19.93 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.739 4.184   8.735  1.00 18.82 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.401 5.163   9.592  1.00 19.31 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.439 6.349   9.890  1.00 19.64 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.876 7.504   10.004 1.00 20.19 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.723 5.648   9.026  1.00 20.88 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.792 4.577   9.109  1.00 25.45 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.574 4.507   10.068 1.00 26.68 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.834 3.717   8.123  1.00 25.38 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.153 6.034   10.103 1.00 18.64 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.170 7.070   10.425 1.00 18.17 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.487 6.766   11.764 1.00 17.99 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.234 5.591   12.078 1.00 17.90 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.069 7.122   9.331  1.00 18.61 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.561 7.562   7.968  1.00 20.25 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.171 8.802   7.789  1.00 21.89 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.394 6.754   6.854  1.00 20.67 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.641 9.203   6.541  1.00 22.44 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.830 7.159   5.596  1.00 21.59 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.436 8.393   5.439  1.00 22.85 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.876 8.793   4.196  1.00 25.90 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.100 7.831   12.497 1.00 17.36 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.319 7.739   13.735 1.00 17.05 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.069 8.615   13.486 1.00 17.10 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.220 9.801   13.168 1.00 16.99 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.128 8.267   14.954 1.00 17.33 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.296 8.648   16.211 1.00 18.91 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.182 9.004   17.431 1.00 20.39 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.645 10.095  18.270 1.00 21.37 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.995 9.912   19.419 1.00 24.93 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.722 8.686   19.846 1.00 24.17 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.540 10.958  20.107 1.00 23.30 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.848 8.013   13.555 1.00 16.43 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.575 8.742   13.309 1.00 16.30 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.896 8.952   14.652 1.00 17.00 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.613 7.988   15.373 1.00 16.98 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.619 7.951   12.359 1.00 16.17 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.393 8.802   11.966 1.00 16.09 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.366 7.468   11.114 1.00 17.04 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.632 10.214  15.008 1.00 16.02 ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.002 10.555  16.289 0.50 15.90 ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.035 10.556  16.297 0.50 16.76 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.871 11.549  16.076 1.00 16.30 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.782 12.189  15.002 1.00 17.19 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.027 11.178  17.283 0.50 15.55 ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.166 11.178  17.191 0.50 18.15 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 22.939 10.131  17.892 0.50 16.70 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.678 11.559  18.571 0.50 18.40 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.801 12.322  16.640 0.50 14.07 ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.351 10.237  17.323 0.50 19.48 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.000 11.734  17.118 1.00 15.52 ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 17.963 12.780  17.057 1.00 14.92 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.776 14.112  17.078 1.00 15.06 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.689 14.255  17.917 1.00 15.19 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.130 12.737  18.324 1.00 15.06 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.275 11.485  18.397 1.00 16.93 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.685 10.467  18.991 1.00 17.11 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.079 11.540  17.781 1.00 16.86 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.459 15.076  16.201 1.00 15.22 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.207 16.345  16.167 1.00 14.82 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.118 17.057  17.527 1.00 16.75 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.125 17.614  17.985 1.00 17.79 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.621 17.264  15.061 1.00 16.31 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.419 18.562  14.796 1.00 17.69 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.616 19.463  13.856 1.00 18.06 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.351 20.648  13.377 1.00 21.29 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.366 21.820  14.008 1.00 23.71 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.803 21.944  15.209 1.00 21.51 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 19.963 22.877  13.451 1.00 23.84 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 17.943 16.954  18.217 1.00 16.32 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 17.821 17.649  19.506 1.00 17.67 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.677 17.029  20.638 1.00 18.72 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 18.831 17.651  21.698 1.00 20.76 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.346 17.809  19.927 1.00 18.11 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.704 16.549  20.430 1.00 19.00 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.074 15.662  19.567 1.00 20.52 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.551 16.100  21.701 1.00 19.70 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.588 14.692  20.336 1.00 20.92 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.837 14.919  21.627 1.00 20.43 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.232 15.827  20.422 1.00 17.73 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.101 15.180  21.413 1.00 17.41 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.584 15.118  20.979 1.00 18.25 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.393 14.479  21.653 1.00 18.57 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.594 13.777  21.754 1.00 17.52 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.192 13.733  22.349 1.00 19.42 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.748 12.295  22.560 1.00 20.04 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.135 14.505  23.687 1.00 20.39 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 21.931 15.747  19.842 1.00 17.09 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.303 15.718  19.348 1.00 17.85 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.288 16.352  20.337 1.00 18.62 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 23.955 17.353  20.967 1.00 18.81 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.374 16.422  18.001 1.00 17.38 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.481 15.744  20.488 1.00 19.05 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.520 16.263  21.401 1.00 19.64 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.437 17.280  20.673 1.00 20.32 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.359 17.408  19.443 1.00 20.19 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.378 15.084  21.932 1.00 21.09 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.107 14.514  20.837 1.00 22.08 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.549 14.001  22.625 1.00 20.88 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.362 17.973  21.411 1.00 20.44 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.321 18.868  20.775 1.00 21.48 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.202 18.050  19.813 1.00 20.93 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.469 18.516  18.716 1.00 21.33 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.199 19.605  21.818 1.00 24.63 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.436 20.244  21.234 1.00 32.29 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.370 21.440  20.539 1.00 35.77 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.721 19.804  21.225 1.00 35.46 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.609 21.717  20.162 1.00 36.95 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.465 20.758  20.545 1.00 37.53 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.598 16.814  20.201 1.00 19.67 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.421 15.986  19.319 1.00 20.51 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.678 15.677  18.002 1.00 20.13 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.300 15.694  16.935 1.00 20.98 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.913 14.700  20.000 1.00 22.93 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.933 13.991  19.134 1.00 30.36 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.083 14.462  18.963 1.00 32.46 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.525 12.890  18.511 1.00 32.43 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.340 15.445  18.068 1.00 18.40 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.550 15.225  16.850 1.00 17.83 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.623 16.468  15.932 1.00 17.88 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.848 16.316  14.736 1.00 18.59 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.076 14.940  17.169 1.00 17.54 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.845 13.583  17.796 1.00 18.93 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.511 12.604  17.364 1.00 18.65 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 25.984 13.491  18.699 1.00 20.37 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.400 17.683  16.490 1.00 17.48 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.466 18.912  15.694 1.00 18.63 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.888 19.177  15.145 1.00 18.98 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.030 19.769  14.067 1.00 19.37 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 27.977 20.131  16.521 1.00 18.99 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.478 20.198  16.628 1.00 19.60 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.703 19.768  17.665 1.00 20.77 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.573 20.648  15.611 1.00 19.55 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.367 20.023  17.399 1.00 20.28 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.260 20.527  16.123 1.00 20.36 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.744 21.151  14.325 1.00 20.35 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.129 20.902  15.376 1.00 21.07 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.633 21.519  13.593 1.00 21.84 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.350 21.406  14.118 1.00 21.83 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.932 18.787  15.902 1.00 18.46 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.324 19.000  15.461 1.00 19.29 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.748 17.989  14.367 1.00 19.67 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.798 18.163  13.762 1.00 19.64 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.286 18.910  16.664 1.00 19.86 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.957 16.911  14.162 1.00 18.74 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.221 15.882  13.135 1.00 18.98 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.963 15.691  12.281 1.00 18.79 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.619 14.567  11.906 1.00 19.24 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.629 14.557  13.822 1.00 19.65 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.953 14.719  14.540 1.00 23.67 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.004 14.661  13.911 1.00 24.65 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 33.923 14.973  15.864 1.00 23.48 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.275 16.805  11.975 1.00 18.38 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 28.997 16.802  11.261 1.00 17.71 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.088 16.335  9.820  1.00 18.48 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.936 16.817  9.057  1.00 19.77 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.383 18.224  11.298 1.00 17.35 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.022 18.379  10.666 1.00 18.88 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 25.984 17.558  11.438 1.00 18.39 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.578 19.834  10.626 1.00 20.00 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.171 15.436  9.433  1.00 17.46 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.042 14.996  8.035  1.00 17.80 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.790 15.694  7.415  1.00 18.33 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.877 16.302  6.336  1.00 18.97 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.949 13.453  7.927  1.00 18.53 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.530 13.015  6.522  1.00 19.46 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.270 12.795  8.346  1.00 18.41 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.630 15.599  8.105  1.00 17.29 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.368 16.159  7.585  1.00 17.97 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.383 16.368  8.743  1.00 18.24 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.399 15.584  9.696  1.00 17.63 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.753 15.156  6.585  1.00 18.51 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.339 15.436  6.131  1.00 19.56 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.943 16.290  5.143  1.00 21.28 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.139 14.787  6.608  1.00 19.38 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.566 16.218  4.975  1.00 21.94 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.049 15.319  5.879  1.00 20.37 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.881 13.833  7.598  1.00 19.31 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.723 14.879  6.077  1.00 20.72 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.578 13.393  7.776  1.00 19.65 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.512 13.941  7.049  1.00 19.98 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.537 17.422  8.667  1.00 18.55 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.526 17.656  9.697  1.00 18.42 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.287 18.276  9.077  1.00 19.79 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.405 19.104  8.159  1.00 20.77 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.042 18.522  10.851 1.00 19.01 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.634 19.871  10.433 1.00 19.11 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.649 21.019  10.251 1.00 24.35 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 21.986 21.987  9.532  1.00 26.50 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.527 20.945  10.802 1.00 23.60 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.096 17.908  9.585  1.00 18.94 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.865 18.501  9.069  1.00 19.32 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.904 18.700  10.248 1.00 20.12 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.376 17.716  10.776 1.00 19.44 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.234 17.576  8.012  1.00 22.36 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.065 18.196  7.274  1.00 27.05 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.359 19.034  7.878  1.00 27.29 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.851 17.839  6.094  1.00 29.80 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.679 19.965  10.657 1.00 20.51 ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.779 20.274  11.769 0.50 20.72 ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.784 20.243  11.777 0.50 21.27 ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.342 19.828  11.481 1.00 20.83 ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.641 19.375  12.396 1.00 20.26 ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.796 21.769  12.077 0.50 21.42 ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 15.837 21.717  12.168 0.50 23.56 ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 14.852 22.112  13.077 0.50 22.17 ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.572 22.545  11.048 0.50 27.11 ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.884 19.965  10.208 1.00 20.04 ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.507 19.549  9.877  1.00 20.49 ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.276 18.028  10.051 1.00 20.05 ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.135 17.606  10.153 1.00 20.84 ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.097 20.001  8.474  1.00 22.78 ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.710 19.193  7.483  1.00 26.01 ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.353 17.205  10.067 1.00 18.63 ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.224 15.751  10.265 1.00 18.09 ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.681 15.289  11.688 1.00 17.64 ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.553 14.103  12.011 1.00 17.23 ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.070 14.997  9.210  1.00 18.45 ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.581 15.207  7.774  1.00 19.68 ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.496 14.492  6.795  1.00 20.07 ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.383 13.044  6.917  1.00 19.40 ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.565 12.194  5.905  1.00 21.83 ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.863 12.649  4.688  1.00 22.23 ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.423 10.881  6.094  1.00 19.49 ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.259 16.212  12.505 1.00 15.76 ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.837 15.876  13.811 1.00 15.66 ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 15.973 14.886  13.644 1.00 14.92 ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.184 14.040  14.526 1.00 15.50 ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.808 15.356  14.851 1.00 17.33 ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.398 15.152  16.247 1.00 18.18 ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.232 15.991  16.672 1.00 18.21 ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.022 14.154  16.915 1.00 18.31 ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.762 15.005  12.521 1.00 13.24 ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.883 14.074  12.341 1.00 13.24 ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.253 14.792  12.235 1.00 14.84 ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.349 15.883  11.660 1.00 15.85 ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.710 13.206  11.087 1.00 14.13 ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.611 12.119  11.111 1.00 16.38 ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.556 11.380  9.782  1.00 17.66 ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.842 11.124  12.235 1.00 15.78 ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.307 14.107  12.716 1.00 14.43 ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.679 14.601  12.600 1.00 14.97 ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.560 13.364  12.411 1.00 15.44 ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.337 12.335  13.065 1.00 16.07 ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.111 15.396  13.853 1.00 14.35 ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.542 16.039  13.774 1.00 17.01 ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.583 17.387  14.433 1.00 17.34 ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.622 15.100  14.397 1.00 16.87 ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.527 13.443  11.489 1.00 14.42 ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.446 12.342  11.243 1.00 14.95 ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.875 12.866  11.422 1.00 15.59 ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.215 13.883  10.815 1.00 16.11 ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.269 11.773  9.813  1.00 16.53 ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.331 10.708  9.543  1.00 18.17 ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.851 11.205  9.607  1.00 16.92 ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.711 12.158  12.228 1.00 14.64 ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.128 12.530  12.410 1.00 15.52 ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 29.040 11.364  11.957 1.00 17.00 ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.558 10.237  11.773 1.00 17.25 ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.418 12.904  13.861 1.00 17.38 ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.104 11.836  14.740 1.00 18.65 ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.350 11.634  11.763 1.00 17.46 ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.267 10.574  11.341 1.00 18.94 ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.902 9.851   12.556 1.00 20.59 ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.076 10.453  13.637 1.00 20.94 ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.362 11.168  10.457 1.00 20.95 ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.048 12.167  11.196 1.00 24.07 ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.300 8.578   12.364 1.00 20.66 ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.891 7.781   13.440 1.00 22.41 ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.219 7.159   13.007 1.00 25.17 ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.460 6.982   11.805 1.00 25.51 ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.928 6.647   13.887 1.00 23.67 ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.744 5.693   12.822 1.00 24.87 ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.589 7.183   14.369 1.00 22.19 ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 35.067 6.802   13.986 1.00 26.29 ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.337 6.168   13.663 1.00 27.96 ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.125 4.670   13.467 1.00 28.01 ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.656 4.100   12.512 1.00 28.78 ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.409 6.541   14.695 1.00 31.39 ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.975 6.082   15.976 1.00 33.70 ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.662 8.052   14.738 1.00 32.12 ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.335 4.035   14.339 1.00 27.76 ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 35.042 2.609   14.217 1.00 28.67 ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.840 2.356   13.301 1.00 28.65 ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.920 3.199   13.217 1.00 28.27 ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.748 2.011   15.590 1.00 29.61 ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.810 1.153   12.679 1.00 27.59 ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.711 0.745   11.806 1.00 27.23 ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.553 0.179   12.632 1.00 25.63 ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.787 -0.571  13.601 1.00 25.07 ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.185 -0.306  10.791 1.00 30.57 ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.886 0.309   9.578  1.00 36.47 ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.169 -0.729  8.529  1.00 43.91 ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.023 -1.610  8.713  1.00 43.91 ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.459 -0.642  7.406  1.00 47.03 ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.325 0.552   12.258 1.00 23.28 ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.130 0.105   12.956 1.00 22.54 ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.574 -1.196  12.424 1.00 21.89 ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.943 -1.634  11.336 1.00 21.85 ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.669 -1.828  13.209 1.00 21.57 ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 27.109 -3.128  12.832 1.00 22.74 ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.653 -3.116  12.403 1.00 21.77 ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 25.135 -4.184  12.030 1.00 22.48 ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.325 -4.126  13.958 1.00 24.96 ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 29.072 -4.472  14.273 1.00 29.96 ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.976 -1.952  12.479 1.00 19.39 ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.586 -1.879  12.052 1.00 19.28 ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.494 -1.863  10.511 1.00 20.15 ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.359 -1.306  9.836  1.00 20.11 ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.937 -0.609  12.632 1.00 19.47 ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.807 -0.656  14.146 1.00 21.43 ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.492 -1.767  14.683 1.00 19.86 ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.965 0.419   14.798 1.00 22.50 ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.422 -2.445  9.974  1.00 20.31 ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 22.128 -2.412  8.537  1.00 21.27 ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.818 -1.633  8.367  1.00 20.61 ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.891 -1.874  9.135  1.00 21.01 ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.942 -3.826  8.009  1.00 25.01 ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 23.240 -4.452  7.993  1.00 27.66 ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 21.346 -3.850  6.610  1.00 27.04 ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.723 -0.748  7.347  1.00 19.54 ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.502 0.027   7.126  1.00 18.42 ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.536 -0.767  6.241  1.00 19.11 ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.951 -1.329  5.200  1.00 18.92 ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.790 1.417   6.476  1.00 18.77 ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.884 2.203   7.253  1.00 19.39 ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.500 2.267   6.364  1.00 19.90 ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.563 2.443   8.738  1.00 19.90 ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.242 -0.754  6.599  1.00 18.55 ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.216 -1.411  5.804  1.00 19.46 ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.994 -0.594  4.511  1.00 20.96 ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.999 0.640   4.529  1.00 21.32 ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.903 -1.457  6.583  1.00 19.08 ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.783 -1.288  3.396  1.00 21.47 ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.469 -0.639  2.123  1.00 22.34 ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 14.200 -1.422  1.655  1.00 23.77 ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 14.285 -2.492  1.025  1.00 24.32 ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.663 -0.755  1.147  1.00 23.05 ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.981 -0.143  1.685  1.00 23.33 ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.980 1.375   1.869  1.00 21.78 ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.285 1.852   2.375  1.00 21.02 ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.465 3.018   2.997  1.00 23.93 ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.445 3.863   3.153  1.00 20.24 ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.665 3.355   3.461  1.00 22.38 ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 13.036 -0.927  2.065  1.00 23.04 ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.765 -1.646  1.913  1.00 23.84 ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.566 -0.702  2.133  1.00 24.95 ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.730 0.479   2.471  1.00 25.14 ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.735 -2.750  2.968  1.00 24.56 ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.604 -2.095  4.658  1.00 24.18 ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 9.334  -1.284  2.067  1.00 25.71 ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 8.132  -0.524  2.336  1.00 26.90 ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.353  -1.171  3.495  1.00 26.04 ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 6.132  -1.091  3.510  1.00 26.89 ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 7.233  -0.465  1.071  1.00 32.81 ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.838  -1.825  0.502  1.00 42.14 ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 7.140  -2.850  1.144  1.00 43.24 ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 6.233  -1.862  -0.601 1.00 47.36 ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 8.042  -1.798  4.468  1.00 24.50 ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.345  -2.408  5.612  1.00 22.54 ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.555  -1.386  6.401  1.00 21.20 ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 7.007  -0.252  6.567  1.00 22.32 ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.325  -3.136  6.528  1.00 21.01 ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.947  -4.713  5.874  1.00 22.99 ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.396  -1.798  6.920  1.00 19.08 ? 59  GLN   A N   1 
ATOM   411  C  CA  A GLN   A 1 53  ? 4.525  -0.967  7.765  0.50 18.80 ? 59  GLN   A CA  1 
ATOM   412  C  CA  B GLN   A 1 53  ? 4.664  -0.902  7.802  0.50 18.56 ? 59  GLN   A CA  1 
ATOM   413  C  C   . GLN   A 1 53  ? 4.292  -1.656  9.140  1.00 18.32 ? 59  GLN   A C   1 
ATOM   414  O  O   . GLN   A 1 53  ? 3.433  -1.228  9.917  1.00 18.63 ? 59  GLN   A O   1 
ATOM   415  C  CB  A GLN   A 1 53  ? 3.165  -0.639  7.091  0.50 19.82 ? 59  GLN   A CB  1 
ATOM   416  C  CB  B GLN   A 1 53  ? 3.527  -0.168  7.072  0.50 19.16 ? 59  GLN   A CB  1 
ATOM   417  C  CG  A GLN   A 1 53  ? 3.143  0.648   6.241  0.50 21.03 ? 59  GLN   A CG  1 
ATOM   418  C  CG  B GLN   A 1 53  ? 4.056  0.698   5.861  0.50 19.25 ? 59  GLN   A CG  1 
ATOM   419  C  CD  A GLN   A 1 53  ? 1.743  1.198   5.963  0.50 23.20 ? 59  GLN   A CD  1 
ATOM   420  C  CD  B GLN   A 1 53  ? 5.035  1.832   6.231  0.50 21.51 ? 59  GLN   A CD  1 
ATOM   421  O  OE1 A GLN   A 1 53  ? 1.167  1.009   4.888  0.50 23.59 ? 59  GLN   A OE1 1 
ATOM   422  O  OE1 B GLN   A 1 53  ? 5.999  2.188   5.517  0.50 20.24 ? 59  GLN   A OE1 1 
ATOM   423  N  NE2 A GLN   A 1 53  ? 1.173  1.932   6.910  0.50 21.96 ? 59  GLN   A NE2 1 
ATOM   424  N  NE2 B GLN   A 1 53  ? 4.814  2.439   7.361  0.50 22.29 ? 59  GLN   A NE2 1 
ATOM   425  N  N   . THR   A 1 54  ? 5.061  -2.741  9.444  1.00 17.59 ? 60  THR   A N   1 
ATOM   426  C  CA  . THR   A 1 54  ? 5.040  -3.480  10.704 1.00 18.15 ? 60  THR   A CA  1 
ATOM   427  C  C   . THR   A 1 54  ? 6.503  -3.733  11.112 1.00 17.86 ? 60  THR   A C   1 
ATOM   428  O  O   . THR   A 1 54  ? 7.378  -3.958  10.268 1.00 18.73 ? 60  THR   A O   1 
ATOM   429  C  CB  . THR   A 1 54  ? 4.200  -4.768  10.705 1.00 21.77 ? 60  THR   A CB  1 
ATOM   430  O  OG1 . THR   A 1 54  ? 4.823  -5.764  9.896  1.00 25.31 ? 60  THR   A OG1 1 
ATOM   431  C  CG2 . THR   A 1 54  ? 2.793  -4.538  10.239 1.00 21.82 ? 60  THR   A CG2 1 
ATOM   432  N  N   . GLY   A 1 55  ? 6.763  -3.617  12.396 1.00 16.96 ? 61  GLY   A N   1 
ATOM   433  C  CA  . GLY   A 1 55  ? 8.116  -3.821  12.904 1.00 16.36 ? 61  GLY   A CA  1 
ATOM   434  C  C   . GLY   A 1 55  ? 8.129  -3.901  14.409 1.00 16.59 ? 61  GLY   A C   1 
ATOM   435  O  O   . GLY   A 1 55  ? 7.092  -4.175  15.019 1.00 16.98 ? 61  GLY   A O   1 
ATOM   436  N  N   . VAL   A 1 56  ? 9.306  -3.671  15.017 1.00 14.90 ? 62  VAL   A N   1 
ATOM   437  C  CA  . VAL   A 1 56  ? 9.460  -3.742  16.470 1.00 15.57 ? 62  VAL   A CA  1 
ATOM   438  C  C   . VAL   A 1 56  ? 10.299 -2.532  16.920 1.00 15.36 ? 62  VAL   A C   1 
ATOM   439  O  O   . VAL   A 1 56  ? 11.269 -2.209  16.251 1.00 14.99 ? 62  VAL   A O   1 
ATOM   440  C  CB  . VAL   A 1 56  ? 10.177 -5.076  16.814 1.00 17.40 ? 62  VAL   A CB  1 
ATOM   441  C  CG1 . VAL   A 1 56  ? 10.595 -5.115  18.275 1.00 18.63 ? 62  VAL   A CG1 1 
ATOM   442  C  CG2 . VAL   A 1 56  ? 9.295  -6.298  16.454 1.00 18.11 ? 62  VAL   A CG2 1 
ATOM   443  N  N   . TYR   A 1 57  ? 9.922  -1.835  18.018 1.00 14.26 ? 63  TYR   A N   1 
ATOM   444  C  CA  . TYR   A 1 57  ? 10.763 -0.713  18.480 1.00 14.83 ? 63  TYR   A CA  1 
ATOM   445  C  C   . TYR   A 1 57  ? 11.211 -0.914  19.930 1.00 15.28 ? 63  TYR   A C   1 
ATOM   446  O  O   . TYR   A 1 57  ? 10.515 -1.592  20.702 1.00 15.52 ? 63  TYR   A O   1 
ATOM   447  C  CB  . TYR   A 1 57  ? 10.054 0.656   18.326 1.00 15.04 ? 63  TYR   A CB  1 
ATOM   448  C  CG  . TYR   A 1 57  ? 9.039  0.998   19.408 1.00 16.31 ? 63  TYR   A CG  1 
ATOM   449  C  CD1 . TYR   A 1 57  ? 7.780  0.404   19.424 1.00 17.76 ? 63  TYR   A CD1 1 
ATOM   450  C  CD2 . TYR   A 1 57  ? 9.331  1.929   20.397 1.00 16.65 ? 63  TYR   A CD2 1 
ATOM   451  C  CE1 . TYR   A 1 57  ? 6.828  0.750   20.383 1.00 17.64 ? 63  TYR   A CE1 1 
ATOM   452  C  CE2 . TYR   A 1 57  ? 8.389  2.269   21.373 1.00 16.11 ? 63  TYR   A CE2 1 
ATOM   453  C  CZ  . TYR   A 1 57  ? 7.145  1.658   21.372 1.00 16.86 ? 63  TYR   A CZ  1 
ATOM   454  O  OH  . TYR   A 1 57  ? 6.204  1.963   22.343 1.00 18.37 ? 63  TYR   A OH  1 
ATOM   455  N  N   . TYR   A 1 58  ? 12.338 -0.268  20.309 1.00 15.24 ? 64  TYR   A N   1 
ATOM   456  C  CA  . TYR   A 1 58  ? 12.822 -0.349  21.678 1.00 15.72 ? 64  TYR   A CA  1 
ATOM   457  C  C   . TYR   A 1 58  ? 12.318 0.834   22.480 1.00 15.58 ? 64  TYR   A C   1 
ATOM   458  O  O   . TYR   A 1 58  ? 12.535 1.977   22.087 1.00 15.72 ? 64  TYR   A O   1 
ATOM   459  C  CB  . TYR   A 1 58  ? 14.361 -0.409  21.762 1.00 15.48 ? 64  TYR   A CB  1 
ATOM   460  C  CG  . TYR   A 1 58  ? 14.814 -0.526  23.192 1.00 16.42 ? 64  TYR   A CG  1 
ATOM   461  C  CD1 . TYR   A 1 58  ? 14.498 -1.642  23.946 1.00 17.38 ? 64  TYR   A CD1 1 
ATOM   462  C  CD2 . TYR   A 1 58  ? 15.571 0.476   23.788 1.00 17.02 ? 64  TYR   A CD2 1 
ATOM   463  C  CE1 . TYR   A 1 58  ? 14.892 -1.746  25.273 1.00 17.98 ? 64  TYR   A CE1 1 
ATOM   464  C  CE2 . TYR   A 1 58  ? 15.958 0.395   25.119 1.00 17.38 ? 64  TYR   A CE2 1 
ATOM   465  C  CZ  . TYR   A 1 58  ? 15.638 -0.731  25.850 1.00 18.55 ? 64  TYR   A CZ  1 
ATOM   466  O  OH  . TYR   A 1 58  ? 16.039 -0.826  27.158 1.00 19.23 ? 64  TYR   A OH  1 
ATOM   467  N  N   . CYS   A 1 59  ? 11.705 0.544   23.645 1.00 14.59 ? 65  CYS   A N   1 
ATOM   468  C  CA  . CYS   A 1 59  ? 11.140 1.537   24.569 1.00 14.84 ? 65  CYS   A CA  1 
ATOM   469  C  C   . CYS   A 1 59  ? 11.975 1.539   25.857 1.00 15.84 ? 65  CYS   A C   1 
ATOM   470  O  O   . CYS   A 1 59  ? 11.760 0.675   26.736 1.00 16.26 ? 65  CYS   A O   1 
ATOM   471  C  CB  . CYS   A 1 59  ? 9.675  1.201   24.850 1.00 15.30 ? 65  CYS   A CB  1 
ATOM   472  S  SG  . CYS   A 1 59  ? 8.877  2.326   26.029 1.00 18.70 ? 65  CYS   A SG  1 
ATOM   473  N  N   . SER   A 1 60  ? 12.924 2.499   26.003 1.00 16.38 ? 66  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 60  ? 13.767 2.523   27.213 1.00 17.17 ? 66  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 60  ? 12.984 2.683   28.536 1.00 17.70 ? 66  SER   A C   1 
ATOM   476  O  O   . SER   A 1 60  ? 13.364 2.080   29.561 1.00 18.31 ? 66  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 60  ? 14.878 3.576   27.102 1.00 19.51 ? 66  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 60  ? 14.385 4.900   27.207 1.00 21.98 ? 66  SER   A OG  1 
ATOM   479  N  N   . SER   A 1 61  ? 11.878 3.466   28.510 1.00 16.25 ? 67  SER   A N   1 
ATOM   480  C  CA  . SER   A 1 61  ? 11.034 3.697   29.687 1.00 15.89 ? 67  SER   A CA  1 
ATOM   481  C  C   . SER   A 1 61  ? 10.277 2.419   30.162 1.00 16.20 ? 67  SER   A C   1 
ATOM   482  O  O   . SER   A 1 61  ? 9.621  2.462   31.210 1.00 16.47 ? 67  SER   A O   1 
ATOM   483  C  CB  . SER   A 1 61  ? 10.052 4.850   29.468 1.00 17.10 ? 67  SER   A CB  1 
ATOM   484  O  OG  . SER   A 1 61  ? 9.066  4.526   28.505 1.00 18.87 ? 67  SER   A OG  1 
ATOM   485  N  N   . ARG   A 1 62  ? 10.356 1.306   29.392 1.00 15.66 ? 68  ARG   A N   1 
ATOM   486  C  CA  . ARG   A 1 62  ? 9.786  0.020   29.827 1.00 16.16 ? 68  ARG   A CA  1 
ATOM   487  C  C   . ARG   A 1 62  ? 10.845 -1.135  29.745 1.00 18.31 ? 68  ARG   A C   1 
ATOM   488  O  O   . ARG   A 1 62  ? 10.490 -2.294  30.024 1.00 19.22 ? 68  ARG   A O   1 
ATOM   489  C  CB  . ARG   A 1 62  ? 8.588  -0.377  28.945 1.00 17.21 ? 68  ARG   A CB  1 
ATOM   490  C  CG  . ARG   A 1 62  ? 7.395  0.567   29.078 1.00 18.47 ? 68  ARG   A CG  1 
ATOM   491  C  CD  . ARG   A 1 62  ? 6.592  0.273   30.326 1.00 19.39 ? 68  ARG   A CD  1 
ATOM   492  N  NE  . ARG   A 1 62  ? 5.442  1.172   30.456 1.00 18.52 ? 68  ARG   A NE  1 
ATOM   493  C  CZ  . ARG   A 1 62  ? 5.470  2.356   31.055 1.00 18.28 ? 68  ARG   A CZ  1 
ATOM   494  N  NH1 . ARG   A 1 62  ? 6.601  2.817   31.581 1.00 17.37 ? 68  ARG   A NH1 1 
ATOM   495  N  NH2 . ARG   A 1 62  ? 4.366  3.103   31.115 1.00 17.93 ? 68  ARG   A NH2 1 
ATOM   496  N  N   . ARG   A 1 63  ? 12.087 -0.840  29.259 1.00 18.04 ? 69  ARG   A N   1 
ATOM   497  C  CA  . ARG   A 1 63  ? 13.136 -1.858  29.033 1.00 19.57 ? 69  ARG   A CA  1 
ATOM   498  C  C   . ARG   A 1 63  ? 12.573 -3.018  28.181 1.00 20.75 ? 69  ARG   A C   1 
ATOM   499  O  O   . ARG   A 1 63  ? 12.760 -4.203  28.507 1.00 21.97 ? 69  ARG   A O   1 
ATOM   500  C  CB  . ARG   A 1 63  ? 13.654 -2.422  30.356 1.00 21.97 ? 69  ARG   A CB  1 
ATOM   501  C  CG  . ARG   A 1 63  ? 14.617 -1.516  31.012 1.00 24.57 ? 69  ARG   A CG  1 
ATOM   502  C  CD  . ARG   A 1 63  ? 15.553 -2.351  31.883 1.00 26.44 ? 69  ARG   A CD  1 
ATOM   503  N  NE  . ARG   A 1 63  ? 16.309 -1.416  32.699 1.00 27.63 ? 69  ARG   A NE  1 
ATOM   504  C  CZ  . ARG   A 1 63  ? 15.960 -1.030  33.920 1.00 26.30 ? 69  ARG   A CZ  1 
ATOM   505  N  NH1 . ARG   A 1 63  ? 14.896 -1.566  34.517 1.00 26.43 ? 69  ARG   A NH1 1 
ATOM   506  N  NH2 . ARG   A 1 63  ? 16.678 -0.116  34.562 1.00 24.83 ? 69  ARG   A NH2 1 
ATOM   507  N  N   . LYS   A 1 64  ? 11.800 -2.672  27.140 1.00 18.93 ? 70  LYS   A N   1 
ATOM   508  C  CA  . LYS   A 1 64  ? 11.140 -3.696  26.332 1.00 19.28 ? 70  LYS   A CA  1 
ATOM   509  C  C   . LYS   A 1 64  ? 11.065 -3.303  24.872 1.00 19.15 ? 70  LYS   A C   1 
ATOM   510  O  O   . LYS   A 1 64  ? 10.965 -2.112  24.560 1.00 19.33 ? 70  LYS   A O   1 
ATOM   511  C  CB  . LYS   A 1 64  ? 9.685  -3.884  26.825 1.00 22.89 ? 70  LYS   A CB  1 
ATOM   512  C  CG  . LYS   A 1 64  ? 9.535  -4.889  27.960 1.00 31.15 ? 70  LYS   A CG  1 
ATOM   513  C  CD  . LYS   A 1 64  ? 8.083  -5.143  28.301 1.00 39.45 ? 70  LYS   A CD  1 
ATOM   514  C  CE  . LYS   A 1 64  ? 7.936  -6.130  29.457 1.00 45.23 ? 70  LYS   A CE  1 
ATOM   515  N  NZ  . LYS   A 1 64  ? 8.645  -5.675  30.692 1.00 48.67 ? 70  LYS   A NZ  1 
ATOM   516  N  N   . HIS   A 1 65  ? 11.055 -4.319  23.983 1.00 18.74 ? 71  HIS   A N   1 
ATOM   517  C  CA  . HIS   A 1 65  ? 10.857 -4.170  22.537 1.00 18.23 ? 71  HIS   A CA  1 
ATOM   518  C  C   . HIS   A 1 65  ? 9.384  -4.520  22.262 1.00 18.23 ? 71  HIS   A C   1 
ATOM   519  O  O   . HIS   A 1 65  ? 8.904  -5.565  22.743 1.00 19.56 ? 71  HIS   A O   1 
ATOM   520  C  CB  . HIS   A 1 65  ? 11.760 -5.165  21.755 1.00 18.16 ? 71  HIS   A CB  1 
ATOM   521  C  CG  . HIS   A 1 65  ? 13.236 -4.903  21.921 1.00 19.94 ? 71  HIS   A CG  1 
ATOM   522  N  ND1 . HIS   A 1 65  ? 13.956 -4.150  20.995 1.00 22.73 ? 71  HIS   A ND1 1 
ATOM   523  C  CD2 . HIS   A 1 65  ? 14.069 -5.276  22.918 1.00 19.57 ? 71  HIS   A CD2 1 
ATOM   524  C  CE1 . HIS   A 1 65  ? 15.199 -4.106  21.454 1.00 21.70 ? 71  HIS   A CE1 1 
ATOM   525  N  NE2 . HIS   A 1 65  ? 15.312 -4.750  22.614 1.00 22.07 ? 71  HIS   A NE2 1 
ATOM   526  N  N   . TYR   A 1 66  ? 8.655  -3.651  21.544 1.00 16.09 ? 72  TYR   A N   1 
ATOM   527  C  CA  . TYR   A 1 66  ? 7.226  -3.908  21.270 1.00 16.59 ? 72  TYR   A CA  1 
ATOM   528  C  C   . TYR   A 1 66  ? 6.962  -4.023  19.783 1.00 15.29 ? 72  TYR   A C   1 
ATOM   529  O  O   . TYR   A 1 66  ? 7.455  -3.188  19.016 1.00 14.30 ? 72  TYR   A O   1 
ATOM   530  C  CB  . TYR   A 1 66  ? 6.353  -2.736  21.790 1.00 16.11 ? 72  TYR   A CB  1 
ATOM   531  C  CG  . TYR   A 1 66  ? 6.295  -2.561  23.294 1.00 16.89 ? 72  TYR   A CG  1 
ATOM   532  C  CD1 . TYR   A 1 66  ? 5.481  -3.374  24.080 1.00 18.29 ? 72  TYR   A CD1 1 
ATOM   533  C  CD2 . TYR   A 1 66  ? 7.013  -1.557  23.922 1.00 18.02 ? 72  TYR   A CD2 1 
ATOM   534  C  CE1 . TYR   A 1 66  ? 5.365  -3.177  25.453 1.00 19.49 ? 72  TYR   A CE1 1 
ATOM   535  C  CE2 . TYR   A 1 66  ? 6.891  -1.333  25.287 1.00 19.60 ? 72  TYR   A CE2 1 
ATOM   536  C  CZ  . TYR   A 1 66  ? 6.089  -2.167  26.059 1.00 20.96 ? 72  TYR   A CZ  1 
ATOM   537  O  OH  . TYR   A 1 66  ? 6.013  -1.990  27.419 1.00 22.15 ? 72  TYR   A OH  1 
ATOM   538  N  N   . PRO   A 1 67  ? 6.136  -4.992  19.351 1.00 15.30 ? 73  PRO   A N   1 
ATOM   539  C  CA  . PRO   A 1 67  ? 5.774  -5.025  17.919 1.00 15.56 ? 73  PRO   A CA  1 
ATOM   540  C  C   . PRO   A 1 67  ? 4.746  -3.907  17.643 1.00 17.61 ? 73  PRO   A C   1 
ATOM   541  O  O   . PRO   A 1 67  ? 3.847  -3.673  18.468 1.00 19.09 ? 73  PRO   A O   1 
ATOM   542  C  CB  . PRO   A 1 67  ? 5.114  -6.406  17.729 1.00 17.53 ? 73  PRO   A CB  1 
ATOM   543  C  CG  . PRO   A 1 67  ? 4.692  -6.849  19.096 1.00 18.20 ? 73  PRO   A CG  1 
ATOM   544  C  CD  . PRO   A 1 67  ? 5.467  -6.052  20.139 1.00 16.02 ? 73  PRO   A CD  1 
ATOM   545  N  N   . VAL   A 1 68  ? 4.843  -3.239  16.491 1.00 16.65 ? 74  VAL   A N   1 
ATOM   546  C  CA  . VAL   A 1 68  ? 3.897  -2.159  16.164 1.00 17.95 ? 74  VAL   A CA  1 
ATOM   547  C  C   . VAL   A 1 68  ? 3.604  -2.118  14.662 1.00 18.09 ? 74  VAL   A C   1 
ATOM   548  O  O   . VAL   A 1 68  ? 4.409  -2.576  13.842 1.00 16.96 ? 74  VAL   A O   1 
ATOM   549  C  CB  . VAL   A 1 68  ? 4.455  -0.770  16.564 1.00 20.21 ? 74  VAL   A CB  1 
ATOM   550  C  CG1 . VAL   A 1 68  ? 4.359  -0.516  18.065 1.00 21.60 ? 74  VAL   A CG1 1 
ATOM   551  C  CG2 . VAL   A 1 68  ? 5.881  -0.575  16.030 1.00 21.33 ? 74  VAL   A CG2 1 
ATOM   552  N  N   . SER   A 1 69  ? 2.431  -1.549  14.314 1.00 18.48 ? 75  SER   A N   1 
ATOM   553  C  CA  . SER   A 1 69  ? 2.036  -1.192  12.959 1.00 18.66 ? 75  SER   A CA  1 
ATOM   554  C  C   . SER   A 1 69  ? 2.278  0.307   12.909 1.00 17.26 ? 75  SER   A C   1 
ATOM   555  O  O   . SER   A 1 69  ? 1.850  1.018   13.851 1.00 17.10 ? 75  SER   A O   1 
ATOM   556  C  CB  . SER   A 1 69  ? 0.542  -1.425  12.741 1.00 21.94 ? 75  SER   A CB  1 
ATOM   557  O  OG  . SER   A 1 69  ? 0.250  -2.811  12.733 1.00 27.06 ? 75  SER   A OG  1 
ATOM   558  N  N   . PHE   A 1 70  ? 2.898  0.816   11.832 1.00 16.92 ? 76  PHE   A N   1 
ATOM   559  C  CA  . PHE   A 1 70  ? 3.186  2.242   11.752 1.00 16.51 ? 76  PHE   A CA  1 
ATOM   560  C  C   . PHE   A 1 70  ? 2.800  2.815   10.398 1.00 17.76 ? 76  PHE   A C   1 
ATOM   561  O  O   . PHE   A 1 70  ? 2.787  2.098   9.374  1.00 18.73 ? 76  PHE   A O   1 
ATOM   562  C  CB  . PHE   A 1 70  ? 4.660  2.539   12.135 1.00 15.95 ? 76  PHE   A CB  1 
ATOM   563  C  CG  . PHE   A 1 70  ? 5.688  1.733   11.354 1.00 15.41 ? 76  PHE   A CG  1 
ATOM   564  C  CD1 . PHE   A 1 70  ? 6.096  0.486   11.790 1.00 15.46 ? 76  PHE   A CD1 1 
ATOM   565  C  CD2 . PHE   A 1 70  ? 6.273  2.244   10.196 1.00 15.66 ? 76  PHE   A CD2 1 
ATOM   566  C  CE1 . PHE   A 1 70  ? 7.039  -0.260  11.059 1.00 16.66 ? 76  PHE   A CE1 1 
ATOM   567  C  CE2 . PHE   A 1 70  ? 7.219  1.490   9.463  1.00 16.53 ? 76  PHE   A CE2 1 
ATOM   568  C  CZ  . PHE   A 1 70  ? 7.611  0.260   9.924  1.00 16.12 ? 76  PHE   A CZ  1 
ATOM   569  N  N   . SER   A 1 71  ? 2.430  4.107   10.390 1.00 17.77 ? 77  SER   A N   1 
ATOM   570  C  CA  . SER   A 1 71  ? 1.999  4.801   9.173  1.00 18.72 ? 77  SER   A CA  1 
ATOM   571  C  C   . SER   A 1 71  ? 3.161  5.057   8.188  1.00 18.80 ? 77  SER   A C   1 
ATOM   572  O  O   . SER   A 1 71  ? 4.312  4.919   8.567  1.00 19.11 ? 77  SER   A O   1 
ATOM   573  C  CB  . SER   A 1 71  ? 1.306  6.124   9.525  1.00 20.06 ? 77  SER   A CB  1 
ATOM   574  O  OG  . SER   A 1 71  ? 2.225  7.088   10.033 1.00 21.41 ? 77  SER   A OG  1 
ATOM   575  N  N   . LYS   A 1 72  ? 2.852  5.442   6.941  1.00 19.00 ? 78  LYS   A N   1 
ATOM   576  C  CA  . LYS   A 1 72  ? 3.883  5.754   5.953  1.00 19.74 ? 78  LYS   A CA  1 
ATOM   577  C  C   . LYS   A 1 72  ? 4.531  7.106   6.284  1.00 19.87 ? 78  LYS   A C   1 
ATOM   578  O  O   . LYS   A 1 72  ? 3.869  7.994   6.816  1.00 19.79 ? 78  LYS   A O   1 
ATOM   579  C  CB  . LYS   A 1 72  ? 3.264  5.747   4.542  1.00 22.09 ? 78  LYS   A CB  1 
ATOM   580  C  CG  . LYS   A 1 72  ? 2.964  4.327   4.055  1.00 27.57 ? 78  LYS   A CG  1 
ATOM   581  C  CD  . LYS   A 1 72  ? 2.541  4.306   2.578  1.00 34.22 ? 78  LYS   A CD  1 
ATOM   582  C  CE  . LYS   A 1 72  ? 2.261  2.900   2.094  1.00 39.96 ? 78  LYS   A CE  1 
ATOM   583  N  NZ  . LYS   A 1 72  ? 2.326  2.798   0.605  1.00 42.98 ? 78  LYS   A NZ  1 
ATOM   584  N  N   . PRO   A 1 73  ? 5.815  7.307   5.936  1.00 20.70 ? 79  PRO   A N   1 
ATOM   585  C  CA  . PRO   A 1 73  ? 6.470  8.607   6.248  1.00 20.90 ? 79  PRO   A CA  1 
ATOM   586  C  C   . PRO   A 1 73  ? 5.683  9.807   5.694  1.00 21.57 ? 79  PRO   A C   1 
ATOM   587  O  O   . PRO   A 1 73  ? 5.305  9.807   4.530  1.00 21.41 ? 79  PRO   A O   1 
ATOM   588  C  CB  . PRO   A 1 73  ? 7.860  8.502   5.601  1.00 22.49 ? 79  PRO   A CB  1 
ATOM   589  C  CG  . PRO   A 1 73  ? 7.950  7.156   4.968  1.00 23.34 ? 79  PRO   A CG  1 
ATOM   590  C  CD  . PRO   A 1 73  ? 6.729  6.343   5.279  1.00 21.35 ? 79  PRO   A CD  1 
ATOM   591  N  N   . SER   A 1 74  ? 5.360  10.773  6.555  1.00 21.96 ? 80  SER   A N   1 
ATOM   592  C  CA  . SER   A 1 74  ? 4.520  11.905  6.157  1.00 23.35 ? 80  SER   A CA  1 
ATOM   593  C  C   . SER   A 1 74  ? 4.902  13.224  6.887  1.00 22.73 ? 80  SER   A C   1 
ATOM   594  O  O   . SER   A 1 74  ? 5.713  13.215  7.804  1.00 21.18 ? 80  SER   A O   1 
ATOM   595  C  CB  . SER   A 1 74  ? 3.052  11.589  6.467  1.00 26.92 ? 80  SER   A CB  1 
ATOM   596  O  OG  . SER   A 1 74  ? 2.687  10.221  6.367  1.00 31.62 ? 80  SER   A OG  1 
ATOM   597  N  N   . LEU   A 1 75  ? 4.246  14.347  6.494  1.00 23.45 ? 81  LEU   A N   1 
ATOM   598  C  CA  . LEU   A 1 75  ? 4.418  15.658  7.119  1.00 24.36 ? 81  LEU   A CA  1 
ATOM   599  C  C   . LEU   A 1 75  ? 3.328  15.738  8.224  1.00 25.21 ? 81  LEU   A C   1 
ATOM   600  O  O   . LEU   A 1 75  ? 2.125  15.757  7.913  1.00 26.07 ? 81  LEU   A O   1 
ATOM   601  C  CB  . LEU   A 1 75  ? 4.215  16.750  6.053  1.00 24.99 ? 81  LEU   A CB  1 
ATOM   602  C  CG  . LEU   A 1 75  ? 4.582  18.180  6.445  1.00 27.46 ? 81  LEU   A CG  1 
ATOM   603  C  CD1 . LEU   A 1 75  ? 6.074  18.322  6.673  1.00 27.09 ? 81  LEU   A CD1 1 
ATOM   604  C  CD2 . LEU   A 1 75  ? 4.117  19.180  5.368  1.00 28.62 ? 81  LEU   A CD2 1 
ATOM   605  N  N   . ILE   A 1 76  ? 3.733  15.690  9.503  1.00 24.73 ? 82  ILE   A N   1 
ATOM   606  C  CA  . ILE   A 1 76  ? 2.807  15.650  10.651 1.00 25.72 ? 82  ILE   A CA  1 
ATOM   607  C  C   . ILE   A 1 76  ? 3.031  16.862  11.573 1.00 25.59 ? 82  ILE   A C   1 
ATOM   608  O  O   . ILE   A 1 76  ? 4.182  17.212  11.858 1.00 24.29 ? 82  ILE   A O   1 
ATOM   609  C  CB  . ILE   A 1 76  ? 3.069  14.348  11.470 1.00 27.46 ? 82  ILE   A CB  1 
ATOM   610  C  CG1 . ILE   A 1 76  ? 2.871  13.042  10.610 1.00 29.93 ? 82  ILE   A CG1 1 
ATOM   611  C  CG2 . ILE   A 1 76  ? 2.266  14.310  12.793 1.00 28.18 ? 82  ILE   A CG2 1 
ATOM   612  C  CD1 . ILE   A 1 76  ? 1.499  12.683  10.305 1.00 33.11 ? 82  ILE   A CD1 1 
ATOM   613  N  N   . PHE   A 1 77  ? 1.947  17.484  12.074 1.00 25.55 ? 83  PHE   A N   1 
ATOM   614  C  CA  . PHE   A 1 77  ? 2.089  18.602  12.998 1.00 26.17 ? 83  PHE   A CA  1 
ATOM   615  C  C   . PHE   A 1 77  ? 2.491  18.064  14.382 1.00 26.44 ? 83  PHE   A C   1 
ATOM   616  O  O   . PHE   A 1 77  ? 1.875  17.126  14.892 1.00 26.71 ? 83  PHE   A O   1 
ATOM   617  C  CB  . PHE   A 1 77  ? 0.769  19.399  13.087 1.00 26.83 ? 83  PHE   A CB  1 
ATOM   618  C  CG  . PHE   A 1 77  ? 0.942  20.683  13.852 1.00 28.17 ? 83  PHE   A CG  1 
ATOM   619  C  CD1 . PHE   A 1 77  ? 1.580  21.768  13.278 1.00 29.66 ? 83  PHE   A CD1 1 
ATOM   620  C  CD2 . PHE   A 1 77  ? 0.483  20.800  15.150 1.00 29.08 ? 83  PHE   A CD2 1 
ATOM   621  C  CE1 . PHE   A 1 77  ? 1.754  22.946  13.991 1.00 30.73 ? 83  PHE   A CE1 1 
ATOM   622  C  CE2 . PHE   A 1 77  ? 0.657  21.980  15.861 1.00 29.35 ? 83  PHE   A CE2 1 
ATOM   623  C  CZ  . PHE   A 1 77  ? 1.268  23.050  15.269 1.00 30.05 ? 83  PHE   A CZ  1 
ATOM   624  N  N   . VAL   A 1 78  ? 3.575  18.625  14.954 1.00 25.62 ? 84  VAL   A N   1 
ATOM   625  C  CA  . VAL   A 1 78  ? 4.098  18.242  16.262 1.00 25.56 ? 84  VAL   A CA  1 
ATOM   626  C  C   . VAL   A 1 78  ? 4.017  19.448  17.216 1.00 25.74 ? 84  VAL   A C   1 
ATOM   627  O  O   . VAL   A 1 78  ? 4.483  20.532  16.866 1.00 25.41 ? 84  VAL   A O   1 
ATOM   628  C  CB  . VAL   A 1 78  ? 5.552  17.725  16.168 1.00 25.52 ? 84  VAL   A CB  1 
ATOM   629  C  CG1 . VAL   A 1 78  ? 6.085  17.332  17.555 1.00 26.07 ? 84  VAL   A CG1 1 
ATOM   630  C  CG2 . VAL   A 1 78  ? 5.632  16.548  15.178 1.00 25.16 ? 84  VAL   A CG2 1 
ATOM   631  N  N   . GLU   A 1 79  ? 3.469  19.230  18.425 1.00 26.41 ? 85  GLU   A N   1 
ATOM   632  C  CA  . GLU   A 1 79  ? 3.298  20.265  19.450 1.00 27.69 ? 85  GLU   A CA  1 
ATOM   633  C  C   . GLU   A 1 79  ? 4.636  20.822  19.935 1.00 27.54 ? 85  GLU   A C   1 
ATOM   634  O  O   . GLU   A 1 79  ? 5.660  20.143  19.843 1.00 27.70 ? 85  GLU   A O   1 
ATOM   635  C  CB  . GLU   A 1 79  ? 2.539  19.680  20.668 1.00 31.48 ? 85  GLU   A CB  1 
ATOM   636  C  CG  . GLU   A 1 79  ? 1.121  19.247  20.365 1.00 41.21 ? 85  GLU   A CG  1 
ATOM   637  C  CD  . GLU   A 1 79  ? 0.276  20.390  19.848 1.00 51.95 ? 85  GLU   A CD  1 
ATOM   638  O  OE1 . GLU   A 1 79  ? 0.217  21.445  20.521 1.00 54.41 ? 85  GLU   A OE1 1 
ATOM   639  O  OE2 . GLU   A 1 79  ? -0.299 20.242  18.748 1.00 55.38 ? 85  GLU   A OE2 1 
ATOM   640  N  N   . ALA   A 1 80  ? 4.594  22.041  20.531 1.00 27.74 ? 86  ALA   A N   1 
ATOM   641  C  CA  . ALA   A 1 80  ? 5.786  22.674  21.106 1.00 28.14 ? 86  ALA   A CA  1 
ATOM   642  C  C   . ALA   A 1 80  ? 6.326  21.809  22.233 1.00 28.01 ? 86  ALA   A C   1 
ATOM   643  O  O   . ALA   A 1 80  ? 5.555  21.176  22.981 1.00 28.42 ? 86  ALA   A O   1 
ATOM   644  C  CB  . ALA   A 1 80  ? 5.444  24.056  21.646 1.00 28.95 ? 86  ALA   A CB  1 
ATOM   645  N  N   . SER   A 1 81  ? 7.652  21.741  22.324 1.00 26.73 ? 87  SER   A N   1 
ATOM   646  C  CA  . SER   A 1 81  ? 8.360  21.004  23.364 1.00 26.48 ? 87  SER   A CA  1 
ATOM   647  C  C   . SER   A 1 81  ? 9.534  21.914  23.827 1.00 26.99 ? 87  SER   A C   1 
ATOM   648  O  O   . SER   A 1 81  ? 9.703  23.040  23.304 1.00 26.46 ? 87  SER   A O   1 
ATOM   649  C  CB  . SER   A 1 81  ? 8.913  19.703  22.781 1.00 26.68 ? 87  SER   A CB  1 
ATOM   650  O  OG  . SER   A 1 81  ? 9.854  20.022  21.769 1.00 26.77 ? 87  SER   A OG  1 
ATOM   651  N  N   . GLU   A 1 82  ? 10.365 21.424  24.769 1.00 27.69 ? 88  GLU   A N   1 
ATOM   652  C  CA  . GLU   A 1 82  ? 11.524 22.233  25.180 1.00 28.44 ? 88  GLU   A CA  1 
ATOM   653  C  C   . GLU   A 1 82  ? 12.590 22.333  24.049 1.00 26.76 ? 88  GLU   A C   1 
ATOM   654  O  O   . GLU   A 1 82  ? 13.487 23.175  24.128 1.00 25.77 ? 88  GLU   A O   1 
ATOM   655  C  CB  . GLU   A 1 82  ? 12.114 21.736  26.505 1.00 32.14 ? 88  GLU   A CB  1 
ATOM   656  C  CG  . GLU   A 1 82  ? 12.753 20.373  26.429 1.00 39.68 ? 88  GLU   A CG  1 
ATOM   657  C  CD  . GLU   A 1 82  ? 13.517 19.998  27.685 1.00 50.57 ? 88  GLU   A CD  1 
ATOM   658  O  OE1 . GLU   A 1 82  ? 12.988 19.192  28.484 1.00 51.85 ? 88  GLU   A OE1 1 
ATOM   659  O  OE2 . GLU   A 1 82  ? 14.642 20.518  27.875 1.00 54.77 ? 88  GLU   A OE2 1 
ATOM   660  N  N   . TYR   A 1 83  ? 12.468 21.502  22.977 1.00 26.08 ? 89  TYR   A N   1 
ATOM   661  C  CA  . TYR   A 1 83  ? 13.455 21.457  21.877 1.00 25.10 ? 89  TYR   A CA  1 
ATOM   662  C  C   . TYR   A 1 83  ? 13.066 22.135  20.580 1.00 24.22 ? 89  TYR   A C   1 
ATOM   663  O  O   . TYR   A 1 83  ? 13.957 22.527  19.832 1.00 23.08 ? 89  TYR   A O   1 
ATOM   664  C  CB  . TYR   A 1 83  ? 13.839 20.017  21.562 1.00 24.88 ? 89  TYR   A CB  1 
ATOM   665  C  CG  . TYR   A 1 83  ? 14.369 19.286  22.766 1.00 26.38 ? 89  TYR   A CG  1 
ATOM   666  C  CD1 . TYR   A 1 83  ? 15.655 19.519  23.232 1.00 27.79 ? 89  TYR   A CD1 1 
ATOM   667  C  CD2 . TYR   A 1 83  ? 13.588 18.352  23.439 1.00 28.25 ? 89  TYR   A CD2 1 
ATOM   668  C  CE1 . TYR   A 1 83  ? 16.161 18.834  24.332 1.00 29.28 ? 89  TYR   A CE1 1 
ATOM   669  C  CE2 . TYR   A 1 83  ? 14.075 17.674  24.553 1.00 29.53 ? 89  TYR   A CE2 1 
ATOM   670  C  CZ  . TYR   A 1 83  ? 15.357 17.930  25.005 1.00 30.93 ? 89  TYR   A CZ  1 
ATOM   671  O  OH  . TYR   A 1 83  ? 15.870 17.244  26.087 1.00 33.70 ? 89  TYR   A OH  1 
ATOM   672  N  N   . TYR   A 1 84  ? 11.755 22.244  20.280 1.00 23.67 ? 90  TYR   A N   1 
ATOM   673  C  CA  . TYR   A 1 84  ? 11.293 22.884  19.042 1.00 23.46 ? 90  TYR   A CA  1 
ATOM   674  C  C   . TYR   A 1 84  ? 9.957  23.610  19.322 1.00 24.95 ? 90  TYR   A C   1 
ATOM   675  O  O   . TYR   A 1 84  ? 9.132  23.084  20.073 1.00 25.07 ? 90  TYR   A O   1 
ATOM   676  C  CB  . TYR   A 1 84  ? 10.972 21.825  17.951 1.00 22.52 ? 90  TYR   A CB  1 
ATOM   677  C  CG  . TYR   A 1 84  ? 12.128 20.978  17.446 1.00 20.36 ? 90  TYR   A CG  1 
ATOM   678  C  CD1 . TYR   A 1 84  ? 13.021 21.469  16.498 1.00 20.40 ? 90  TYR   A CD1 1 
ATOM   679  C  CD2 . TYR   A 1 84  ? 12.324 19.688  17.913 1.00 20.10 ? 90  TYR   A CD2 1 
ATOM   680  C  CE1 . TYR   A 1 84  ? 14.072 20.679  16.016 1.00 19.54 ? 90  TYR   A CE1 1 
ATOM   681  C  CE2 . TYR   A 1 84  ? 13.378 18.899  17.456 1.00 19.48 ? 90  TYR   A CE2 1 
ATOM   682  C  CZ  . TYR   A 1 84  ? 14.252 19.395  16.505 1.00 19.51 ? 90  TYR   A CZ  1 
ATOM   683  O  OH  . TYR   A 1 84  ? 15.294 18.581  16.072 1.00 18.34 ? 90  TYR   A OH  1 
ATOM   684  N  N   . PRO   A 1 85  ? 9.657  24.695  18.602 1.00 25.98 ? 91  PRO   A N   1 
ATOM   685  C  CA  . PRO   A 1 85  ? 8.295  25.268  18.688 1.00 27.66 ? 91  PRO   A CA  1 
ATOM   686  C  C   . PRO   A 1 85  ? 7.290  24.332  17.962 1.00 28.81 ? 91  PRO   A C   1 
ATOM   687  O  O   . PRO   A 1 85  ? 7.701  23.328  17.339 1.00 29.01 ? 91  PRO   A O   1 
ATOM   688  C  CB  . PRO   A 1 85  ? 8.433  26.601  17.937 1.00 28.15 ? 91  PRO   A CB  1 
ATOM   689  C  CG  . PRO   A 1 85  ? 9.493  26.346  16.930 1.00 27.92 ? 91  PRO   A CG  1 
ATOM   690  C  CD  . PRO   A 1 85  ? 10.478 25.387  17.581 1.00 25.58 ? 91  PRO   A CD  1 
ATOM   691  N  N   . ALA   A 1 86  ? 5.982  24.644  18.009 1.00 29.04 ? 92  ALA   A N   1 
ATOM   692  C  CA  . ALA   A 1 86  ? 4.976  23.823  17.306 1.00 29.29 ? 92  ALA   A CA  1 
ATOM   693  C  C   . ALA   A 1 86  ? 5.232  23.993  15.803 1.00 28.93 ? 92  ALA   A C   1 
ATOM   694  O  O   . ALA   A 1 86  ? 5.458  25.114  15.345 1.00 29.88 ? 92  ALA   A O   1 
ATOM   695  C  CB  . ALA   A 1 86  ? 3.571  24.311  17.663 1.00 29.80 ? 92  ALA   A CB  1 
ATOM   696  N  N   . ARG   A 1 87  ? 5.369  22.884  15.067 1.00 27.76 ? 93  ARG   A N   1 
ATOM   697  C  CA  . ARG   A 1 87  ? 5.727  22.954  13.648 1.00 26.28 ? 93  ARG   A CA  1 
ATOM   698  C  C   . ARG   A 1 87  ? 5.340  21.628  12.962 1.00 25.71 ? 93  ARG   A C   1 
ATOM   699  O  O   . ARG   A 1 87  ? 4.904  20.680  13.623 1.00 26.02 ? 93  ARG   A O   1 
ATOM   700  C  CB  . ARG   A 1 87  ? 7.271  23.199  13.509 1.00 26.41 ? 93  ARG   A CB  1 
ATOM   701  C  CG  . ARG   A 1 87  ? 8.136  21.897  13.578 1.00 25.77 ? 93  ARG   A CG  1 
ATOM   702  C  CD  . ARG   A 1 87  ? 9.481  22.016  14.288 1.00 24.65 ? 93  ARG   A CD  1 
ATOM   703  N  NE  . ARG   A 1 87  ? 10.402 20.908  13.969 1.00 23.50 ? 93  ARG   A NE  1 
ATOM   704  C  CZ  . ARG   A 1 87  ? 10.310 19.675  14.473 1.00 23.47 ? 93  ARG   A CZ  1 
ATOM   705  N  NH1 . ARG   A 1 87  ? 9.355  19.377  15.355 1.00 21.82 ? 93  ARG   A NH1 1 
ATOM   706  N  NH2 . ARG   A 1 87  ? 11.209 18.747  14.146 1.00 21.72 ? 93  ARG   A NH2 1 
ATOM   707  N  N   . TYR   A 1 88  ? 5.554  21.550  11.644 1.00 24.96 ? 94  TYR   A N   1 
ATOM   708  C  CA  . TYR   A 1 88  ? 5.366  20.322  10.917 1.00 24.85 ? 94  TYR   A CA  1 
ATOM   709  C  C   . TYR   A 1 88  ? 6.719  19.620  10.836 1.00 23.19 ? 94  TYR   A C   1 
ATOM   710  O  O   . TYR   A 1 88  ? 7.708  20.247  10.453 1.00 23.76 ? 94  TYR   A O   1 
ATOM   711  C  CB  . TYR   A 1 88  ? 4.880  20.621  9.507  1.00 25.94 ? 94  TYR   A CB  1 
ATOM   712  C  CG  . TYR   A 1 88  ? 3.408  20.956  9.478  1.00 27.56 ? 94  TYR   A CG  1 
ATOM   713  C  CD1 . TYR   A 1 88  ? 2.447  19.954  9.436  1.00 28.89 ? 94  TYR   A CD1 1 
ATOM   714  C  CD2 . TYR   A 1 88  ? 2.972  22.267  9.578  1.00 29.14 ? 94  TYR   A CD2 1 
ATOM   715  C  CE1 . TYR   A 1 88  ? 1.087  20.251  9.460  1.00 30.41 ? 94  TYR   A CE1 1 
ATOM   716  C  CE2 . TYR   A 1 88  ? 1.615  22.576  9.619  1.00 30.59 ? 94  TYR   A CE2 1 
ATOM   717  C  CZ  . TYR   A 1 88  ? 0.676  21.564  9.554  1.00 31.55 ? 94  TYR   A CZ  1 
ATOM   718  O  OH  . TYR   A 1 88  ? -0.664 21.852  9.590  1.00 34.53 ? 94  TYR   A OH  1 
ATOM   719  N  N   . GLN   A 1 89  ? 6.757  18.330  11.166 1.00 20.92 ? 95  GLN   A N   1 
ATOM   720  C  CA  . GLN   A 1 89  ? 7.966  17.509  11.047 1.00 18.96 ? 95  GLN   A CA  1 
ATOM   721  C  C   . GLN   A 1 89  ? 7.750  16.575  9.838  1.00 19.17 ? 95  GLN   A C   1 
ATOM   722  O  O   . GLN   A 1 89  ? 6.683  15.942  9.723  1.00 19.39 ? 95  GLN   A O   1 
ATOM   723  C  CB  . GLN   A 1 89  ? 8.250  16.711  12.340 1.00 18.08 ? 95  GLN   A CB  1 
ATOM   724  C  CG  . GLN   A 1 89  ? 9.435  15.769  12.241 1.00 17.10 ? 95  GLN   A CG  1 
ATOM   725  C  CD  . GLN   A 1 89  ? 9.965  15.319  13.603 1.00 18.10 ? 95  GLN   A CD  1 
ATOM   726  O  OE1 . GLN   A 1 89  ? 9.978  16.077  14.577 1.00 20.00 ? 95  GLN   A OE1 1 
ATOM   727  N  NE2 . GLN   A 1 89  ? 10.447 14.084  13.673 1.00 16.09 ? 95  GLN   A NE2 1 
ATOM   728  N  N   . SER   A 1 90  ? 8.746  16.494  8.937  1.00 18.55 ? 96  SER   A N   1 
ATOM   729  C  CA  . SER   A 1 90  ? 8.623  15.658  7.751  1.00 18.97 ? 96  SER   A CA  1 
ATOM   730  C  C   . SER   A 1 90  ? 9.262  14.259  7.954  1.00 18.64 ? 96  SER   A C   1 
ATOM   731  O  O   . SER   A 1 90  ? 10.018 14.051  8.908  1.00 17.88 ? 96  SER   A O   1 
ATOM   732  C  CB  . SER   A 1 90  ? 9.263  16.362  6.552  1.00 21.69 ? 96  SER   A CB  1 
ATOM   733  O  OG  . SER   A 1 90  ? 10.656 16.563  6.784  1.00 24.21 ? 96  SER   A OG  1 
ATOM   734  N  N   . HIS   A 1 91  ? 8.871  13.294  7.076  1.00 18.01 ? 97  HIS   A N   1 
ATOM   735  C  CA  . HIS   A 1 91  ? 9.391  11.926  7.080  1.00 18.39 ? 97  HIS   A CA  1 
ATOM   736  C  C   . HIS   A 1 91  ? 9.096  11.225  8.445  1.00 18.07 ? 97  HIS   A C   1 
ATOM   737  O  O   . HIS   A 1 91  ? 9.898  10.397  8.893  1.00 17.41 ? 97  HIS   A O   1 
ATOM   738  C  CB  . HIS   A 1 91  ? 10.914 11.895  6.693  1.00 19.37 ? 97  HIS   A CB  1 
ATOM   739  C  CG  . HIS   A 1 91  ? 11.212 12.469  5.321  1.00 22.63 ? 97  HIS   A CG  1 
ATOM   740  N  ND1 . HIS   A 1 91  ? 11.325 11.655  4.201  1.00 24.53 ? 97  HIS   A ND1 1 
ATOM   741  C  CD2 . HIS   A 1 91  ? 11.416 13.752  4.938  1.00 24.08 ? 97  HIS   A CD2 1 
ATOM   742  C  CE1 . HIS   A 1 91  ? 11.580 12.466  3.183  1.00 24.39 ? 97  HIS   A CE1 1 
ATOM   743  N  NE2 . HIS   A 1 91  ? 11.650 13.731  3.576  1.00 24.72 ? 97  HIS   A NE2 1 
ATOM   744  N  N   . LEU   A 1 92  ? 7.956  11.577  9.078  1.00 17.26 ? 98  LEU   A N   1 
ATOM   745  C  CA  . LEU   A 1 92  ? 7.576  11.022  10.381 1.00 17.52 ? 98  LEU   A CA  1 
ATOM   746  C  C   . LEU   A 1 92  ? 6.512  9.903   10.217 1.00 17.05 ? 98  LEU   A C   1 
ATOM   747  O  O   . LEU   A 1 92  ? 5.610  10.037  9.388  1.00 17.75 ? 98  LEU   A O   1 
ATOM   748  C  CB  . LEU   A 1 92  ? 7.004  12.164  11.267 1.00 17.85 ? 98  LEU   A CB  1 
ATOM   749  C  CG  . LEU   A 1 92  ? 6.696  11.812  12.745 1.00 19.42 ? 98  LEU   A CG  1 
ATOM   750  C  CD1 . LEU   A 1 92  ? 7.938  11.314  13.468 1.00 18.13 ? 98  LEU   A CD1 1 
ATOM   751  C  CD2 . LEU   A 1 92  ? 6.081  13.028  13.487 1.00 20.19 ? 98  LEU   A CD2 1 
ATOM   752  N  N   . MET   A 1 93  ? 6.622  8.818   11.016 1.00 16.40 ? 99  MET   A N   1 
ATOM   753  C  CA  . MET   A 1 93  ? 5.648  7.697   10.953 1.00 16.86 ? 99  MET   A CA  1 
ATOM   754  C  C   . MET   A 1 93  ? 5.084  7.513   12.366 1.00 17.34 ? 99  MET   A C   1 
ATOM   755  O  O   . MET   A 1 93  ? 5.863  7.543   13.324 1.00 17.19 ? 99  MET   A O   1 
ATOM   756  C  CB  . MET   A 1 93  ? 6.384  6.415   10.522 1.00 18.15 ? 99  MET   A CB  1 
ATOM   757  C  CG  . MET   A 1 93  ? 7.087  6.545   9.164  1.00 20.17 ? 99  MET   A CG  1 
ATOM   758  S  SD  . MET   A 1 93  ? 8.200  5.147   8.736  1.00 21.52 ? 99  MET   A SD  1 
ATOM   759  C  CE  . MET   A 1 93  ? 9.392  5.250   10.093 1.00 21.52 ? 99  MET   A CE  1 
ATOM   760  N  N   . LEU   A 1 94  ? 3.770  7.369   12.511 1.00 16.10 ? 100 LEU   A N   1 
ATOM   761  C  CA  . LEU   A 1 94  ? 3.163  7.212   13.830 1.00 17.29 ? 100 LEU   A CA  1 
ATOM   762  C  C   . LEU   A 1 94  ? 2.660  5.793   14.079 1.00 17.74 ? 100 LEU   A C   1 
ATOM   763  O  O   . LEU   A 1 94  ? 2.219  5.100   13.153 1.00 17.83 ? 100 LEU   A O   1 
ATOM   764  C  CB  . LEU   A 1 94  ? 1.936  8.172   14.006 1.00 18.56 ? 100 LEU   A CB  1 
ATOM   765  C  CG  . LEU   A 1 94  ? 2.165  9.658   13.918 1.00 22.28 ? 100 LEU   A CG  1 
ATOM   766  C  CD1 . LEU   A 1 94  ? 0.868  10.452  14.249 1.00 23.97 ? 100 LEU   A CD1 1 
ATOM   767  C  CD2 . LEU   A 1 94  ? 3.256  10.122  14.878 1.00 23.32 ? 100 LEU   A CD2 1 
ATOM   768  N  N   . ALA   A 1 95  ? 2.625  5.423   15.356 1.00 16.76 ? 101 ALA   A N   1 
ATOM   769  C  CA  . ALA   A 1 95  ? 2.132  4.124   15.808 1.00 17.88 ? 101 ALA   A CA  1 
ATOM   770  C  C   . ALA   A 1 95  ? 1.512  4.279   17.214 1.00 17.82 ? 101 ALA   A C   1 
ATOM   771  O  O   . ALA   A 1 95  ? 1.797  5.248   17.929 1.00 17.50 ? 101 ALA   A O   1 
ATOM   772  C  CB  . ALA   A 1 95  ? 3.310  3.137   15.884 1.00 18.03 ? 101 ALA   A CB  1 
ATOM   773  N  N   . VAL   A 1 96  ? 0.713  3.289   17.632 1.00 16.76 ? 102 VAL   A N   1 
ATOM   774  C  CA  . VAL   A 1 96  ? 0.211  3.256   18.992 1.00 16.46 ? 102 VAL   A CA  1 
ATOM   775  C  C   . VAL   A 1 96  ? 1.254  2.481   19.816 1.00 17.86 ? 102 VAL   A C   1 
ATOM   776  O  O   . VAL   A 1 96  ? 1.593  1.358   19.471 1.00 18.11 ? 102 VAL   A O   1 
ATOM   777  C  CB  . VAL   A 1 96  ? -1.153 2.536   19.013 1.00 16.68 ? 102 VAL   A CB  1 
ATOM   778  C  CG1 . VAL   A 1 96  ? -1.600 2.277   20.451 1.00 17.27 ? 102 VAL   A CG1 1 
ATOM   779  C  CG2 . VAL   A 1 96  ? -2.183 3.378   18.233 1.00 17.65 ? 102 VAL   A CG2 1 
ATOM   780  N  N   . GLY   A 1 97  ? 1.754  3.092   20.871 1.00 18.18 ? 103 GLY   A N   1 
ATOM   781  C  CA  . GLY   A 1 97  ? 2.768  2.489   21.735 1.00 18.20 ? 103 GLY   A CA  1 
ATOM   782  C  C   . GLY   A 1 97  ? 3.219  3.488   22.785 1.00 18.42 ? 103 GLY   A C   1 
ATOM   783  O  O   . GLY   A 1 97  ? 3.005  4.705   22.631 1.00 19.01 ? 103 GLY   A O   1 
ATOM   784  N  N   . HIS   A 1 98  ? 3.721  2.978   23.907 1.00 17.75 ? 104 HIS   A N   1 
ATOM   785  C  CA  . HIS   A 1 98  ? 4.163  3.840   24.977 1.00 17.55 ? 104 HIS   A CA  1 
ATOM   786  C  C   . HIS   A 1 98  ? 5.420  4.600   24.582 1.00 17.84 ? 104 HIS   A C   1 
ATOM   787  O  O   . HIS   A 1 98  ? 6.365  4.010   24.031 1.00 18.31 ? 104 HIS   A O   1 
ATOM   788  C  CB  . HIS   A 1 98  ? 4.425  3.028   26.279 1.00 17.49 ? 104 HIS   A CB  1 
ATOM   789  C  CG  . HIS   A 1 98  ? 4.804  3.910   27.433 1.00 19.22 ? 104 HIS   A CG  1 
ATOM   790  N  ND1 . HIS   A 1 98  ? 3.881  4.777   28.000 1.00 20.40 ? 104 HIS   A ND1 1 
ATOM   791  C  CD2 . HIS   A 1 98  ? 6.014  4.114   28.021 1.00 19.25 ? 104 HIS   A CD2 1 
ATOM   792  C  CE1 . HIS   A 1 98  ? 4.551  5.462   28.929 1.00 20.64 ? 104 HIS   A CE1 1 
ATOM   793  N  NE2 . HIS   A 1 98  ? 5.829  5.085   29.000 1.00 19.96 ? 104 HIS   A NE2 1 
ATOM   794  N  N   . SER   A 1 99  ? 5.487  5.869   24.952 1.00 17.59 ? 105 SER   A N   1 
ATOM   795  C  CA  . SER   A 1 99  ? 6.705  6.655   24.789 1.00 17.19 ? 105 SER   A CA  1 
ATOM   796  C  C   . SER   A 1 99  ? 6.704  7.836   25.767 1.00 18.70 ? 105 SER   A C   1 
ATOM   797  O  O   . SER   A 1 99  ? 5.623  8.371   26.089 1.00 19.90 ? 105 SER   A O   1 
ATOM   798  C  CB  . SER   A 1 99  ? 6.948  7.098   23.342 1.00 18.59 ? 105 SER   A CB  1 
ATOM   799  O  OG  . SER   A 1 99  ? 5.986  8.059   22.928 1.00 19.94 ? 105 SER   A OG  1 
ATOM   800  N  N   . GLU   A 1 100 ? 7.915  8.202   26.260 1.00 18.32 ? 106 GLU   A N   1 
ATOM   801  C  CA  . GLU   A 1 100 ? 8.237  9.343   27.147 1.00 19.72 ? 106 GLU   A CA  1 
ATOM   802  C  C   . GLU   A 1 100 ? 9.404  10.136  26.489 1.00 20.16 ? 106 GLU   A C   1 
ATOM   803  O  O   . GLU   A 1 100 ? 10.095 9.573   25.631 1.00 19.52 ? 106 GLU   A O   1 
ATOM   804  C  CB  . GLU   A 1 100 ? 8.629  8.864   28.563 1.00 22.01 ? 106 GLU   A CB  1 
ATOM   805  C  CG  . GLU   A 1 100 ? 7.491  8.165   29.264 1.00 22.32 ? 106 GLU   A CG  1 
ATOM   806  C  CD  . GLU   A 1 100 ? 7.786  7.497   30.600 1.00 23.82 ? 106 GLU   A CD  1 
ATOM   807  O  OE1 . GLU   A 1 100 ? 8.623  8.024   31.372 1.00 25.81 ? 106 GLU   A OE1 1 
ATOM   808  O  OE2 . GLU   A 1 100 ? 7.121  6.481   30.902 1.00 22.61 ? 106 GLU   A OE2 1 
ATOM   809  N  N   . PRO   A 1 101 ? 9.667  11.411  26.857 1.00 21.10 ? 107 PRO   A N   1 
ATOM   810  C  CA  . PRO   A 1 101 ? 10.715 12.184  26.127 1.00 21.91 ? 107 PRO   A CA  1 
ATOM   811  C  C   . PRO   A 1 101 ? 12.065 11.468  25.937 1.00 20.70 ? 107 PRO   A C   1 
ATOM   812  O  O   . PRO   A 1 101 ? 12.617 11.457  24.824 1.00 21.22 ? 107 PRO   A O   1 
ATOM   813  C  CB  . PRO   A 1 101 ? 10.841 13.475  26.952 1.00 23.33 ? 107 PRO   A CB  1 
ATOM   814  C  CG  . PRO   A 1 101 ? 9.484  13.654  27.578 1.00 23.78 ? 107 PRO   A CG  1 
ATOM   815  C  CD  . PRO   A 1 101 ? 8.915  12.268  27.808 1.00 21.63 ? 107 PRO   A CD  1 
ATOM   816  N  N   . GLY   A 1 102 ? 12.559 10.841  27.003 1.00 18.74 ? 108 GLY   A N   1 
ATOM   817  C  CA  . GLY   A 1 102 ? 13.832 10.111  27.033 1.00 18.01 ? 108 GLY   A CA  1 
ATOM   818  C  C   . GLY   A 1 102 ? 13.880 8.861   26.175 1.00 16.03 ? 108 GLY   A C   1 
ATOM   819  O  O   . GLY   A 1 102 ? 14.952 8.253   26.030 1.00 17.33 ? 108 GLY   A O   1 
ATOM   820  N  N   . ASP   A 1 103 ? 12.717 8.400   25.661 1.00 14.69 ? 109 ASP   A N   1 
ATOM   821  C  CA  . ASP   A 1 103 ? 12.673 7.242   24.743 1.00 15.61 ? 109 ASP   A CA  1 
ATOM   822  C  C   . ASP   A 1 103 ? 13.248 7.578   23.341 1.00 16.73 ? 109 ASP   A C   1 
ATOM   823  O  O   . ASP   A 1 103 ? 13.561 6.668   22.555 1.00 16.41 ? 109 ASP   A O   1 
ATOM   824  C  CB  . ASP   A 1 103 ? 11.235 6.672   24.621 1.00 15.96 ? 109 ASP   A CB  1 
ATOM   825  C  CG  . ASP   A 1 103 ? 10.845 5.918   25.878 1.00 16.91 ? 109 ASP   A CG  1 
ATOM   826  O  OD1 . ASP   A 1 103 ? 11.736 5.250   26.467 1.00 17.33 ? 109 ASP   A OD1 1 
ATOM   827  O  OD2 . ASP   A 1 103 ? 9.650  5.995   26.280 1.00 19.32 ? 109 ASP   A OD2 1 
ATOM   828  N  N   . CYS   A 1 104 ? 13.427 8.883   23.021 1.00 16.83 ? 110 CYS   A N   1 
ATOM   829  C  CA  . CYS   A 1 104 ? 13.979 9.295   21.719 1.00 17.18 ? 110 CYS   A CA  1 
ATOM   830  C  C   . CYS   A 1 104 ? 15.327 8.596   21.470 1.00 16.34 ? 110 CYS   A C   1 
ATOM   831  O  O   . CYS   A 1 104 ? 16.112 8.448   22.413 1.00 15.33 ? 110 CYS   A O   1 
ATOM   832  C  CB  . CYS   A 1 104 ? 14.109 10.805  21.637 1.00 18.85 ? 110 CYS   A CB  1 
ATOM   833  S  SG  . CYS   A 1 104 ? 12.522 11.666  21.420 1.00 19.16 ? 110 CYS   A SG  1 
ATOM   834  N  N   . GLY   A 1 105 ? 15.523 8.090   20.258 1.00 16.64 ? 111 GLY   A N   1 
ATOM   835  C  CA  . GLY   A 1 105 ? 16.743 7.358   19.925 1.00 16.60 ? 111 GLY   A CA  1 
ATOM   836  C  C   . GLY   A 1 105 ? 16.581 5.854   19.843 1.00 16.76 ? 111 GLY   A C   1 
ATOM   837  O  O   . GLY   A 1 105 ? 17.434 5.159   19.282 1.00 17.08 ? 111 GLY   A O   1 
ATOM   838  N  N   . GLY   A 1 106 ? 15.504 5.325   20.423 1.00 16.87 ? 112 GLY   A N   1 
ATOM   839  C  CA  . GLY   A 1 106 ? 15.259 3.892   20.370 1.00 16.62 ? 112 GLY   A CA  1 
ATOM   840  C  C   . GLY   A 1 106 ? 15.029 3.456   18.932 1.00 15.05 ? 112 GLY   A C   1 
ATOM   841  O  O   . GLY   A 1 106 ? 14.384 4.175   18.177 1.00 15.01 ? 112 GLY   A O   1 
ATOM   842  N  N   . ILE   A 1 107 ? 15.616 2.328   18.524 1.00 14.24 ? 113 ILE   A N   1 
ATOM   843  C  CA  . ILE   A 1 107 ? 15.472 1.873   17.136 1.00 14.13 ? 113 ILE   A CA  1 
ATOM   844  C  C   . ILE   A 1 107 ? 14.143 1.176   16.842 1.00 14.83 ? 113 ILE   A C   1 
ATOM   845  O  O   . ILE   A 1 107 ? 13.704 0.338   17.632 1.00 14.63 ? 113 ILE   A O   1 
ATOM   846  C  CB  . ILE   A 1 107 ? 16.655 0.908   16.817 1.00 14.87 ? 113 ILE   A CB  1 
ATOM   847  C  CG1 . ILE   A 1 107 ? 17.942 1.712   16.589 1.00 15.06 ? 113 ILE   A CG1 1 
ATOM   848  C  CG2 . ILE   A 1 107 ? 16.378 -0.048  15.630 1.00 15.88 ? 113 ILE   A CG2 1 
ATOM   849  C  CD1 . ILE   A 1 107 ? 19.190 0.852   16.450 1.00 16.84 ? 113 ILE   A CD1 1 
ATOM   850  N  N   . LEU   A 1 108 ? 13.575 1.453   15.652 1.00 13.97 ? 114 LEU   A N   1 
ATOM   851  C  CA  . LEU   A 1 108 ? 12.445 0.716   15.072 1.00 13.92 ? 114 LEU   A CA  1 
ATOM   852  C  C   . LEU   A 1 108 ? 13.090 -0.159  13.950 1.00 14.60 ? 114 LEU   A C   1 
ATOM   853  O  O   . LEU   A 1 108 ? 13.872 0.378   13.141 1.00 15.37 ? 114 LEU   A O   1 
ATOM   854  C  CB  . LEU   A 1 108 ? 11.433 1.687   14.423 1.00 15.01 ? 114 LEU   A CB  1 
ATOM   855  C  CG  . LEU   A 1 108 ? 10.357 1.049   13.529 1.00 17.55 ? 114 LEU   A CG  1 
ATOM   856  C  CD1 . LEU   A 1 108 ? 9.353  0.267   14.370 1.00 17.23 ? 114 LEU   A CD1 1 
ATOM   857  C  CD2 . LEU   A 1 108 ? 9.622  2.129   12.714 1.00 18.80 ? 114 LEU   A CD2 1 
ATOM   858  N  N   . ARG   A 1 109 ? 12.730 -1.447  13.856 1.00 14.11 ? 115 ARG   A N   1 
ATOM   859  C  CA  . ARG   A 1 109 ? 13.321 -2.311  12.834 1.00 13.79 ? 115 ARG   A CA  1 
ATOM   860  C  C   . ARG   A 1 109 ? 12.283 -3.287  12.275 1.00 16.02 ? 115 ARG   A C   1 
ATOM   861  O  O   . ARG   A 1 109 ? 11.273 -3.555  12.907 1.00 16.65 ? 115 ARG   A O   1 
ATOM   862  C  CB  . ARG   A 1 109 ? 14.492 -3.091  13.450 1.00 14.40 ? 115 ARG   A CB  1 
ATOM   863  C  CG  . ARG   A 1 109 ? 14.083 -4.045  14.585 1.00 16.22 ? 115 ARG   A CG  1 
ATOM   864  C  CD  . ARG   A 1 109 ? 15.315 -4.785  15.152 1.00 18.64 ? 115 ARG   A CD  1 
ATOM   865  N  NE  . ARG   A 1 109 ? 16.121 -3.919  16.022 1.00 21.67 ? 115 ARG   A NE  1 
ATOM   866  C  CZ  . ARG   A 1 109 ? 17.427 -3.701  15.876 1.00 22.21 ? 115 ARG   A CZ  1 
ATOM   867  N  NH1 . ARG   A 1 109 ? 18.095 -4.269  14.873 1.00 20.63 ? 115 ARG   A NH1 1 
ATOM   868  N  NH2 . ARG   A 1 109 ? 18.067 -2.868  16.700 1.00 20.82 ? 115 ARG   A NH2 1 
ATOM   869  N  N   . CYS   A 1 110 ? 12.562 -3.852  11.101 1.00 16.86 ? 116 CYS   A N   1 
ATOM   870  C  CA  . CYS   A 1 110 ? 11.707 -4.857  10.464 1.00 18.55 ? 116 CYS   A CA  1 
ATOM   871  C  C   . CYS   A 1 110 ? 12.649 -6.062  10.060 1.00 21.94 ? 116 CYS   A C   1 
ATOM   872  O  O   . CYS   A 1 110 ? 13.828 -6.078  10.440 1.00 22.20 ? 116 CYS   A O   1 
ATOM   873  C  CB  . CYS   A 1 110 ? 11.058 -4.235  9.236  1.00 20.49 ? 116 CYS   A CB  1 
ATOM   874  S  SG  . CYS   A 1 110 ? 12.276 -3.741  7.982  1.00 21.96 ? 116 CYS   A SG  1 
ATOM   875  N  N   . GLN   A 1 111 ? 12.153 -7.023  9.245  1.00 24.07 ? 117 GLN   A N   1 
ATOM   876  C  CA  . GLN   A 1 111 ? 12.984 -8.155  8.812  1.00 26.59 ? 117 GLN   A CA  1 
ATOM   877  C  C   . GLN   A 1 111 ? 14.213 -7.711  7.969  1.00 27.41 ? 117 GLN   A C   1 
ATOM   878  O  O   . GLN   A 1 111 ? 15.200 -8.444  7.883  1.00 29.39 ? 117 GLN   A O   1 
ATOM   879  C  CB  . GLN   A 1 111 ? 12.128 -9.176  8.017  1.00 29.95 ? 117 GLN   A CB  1 
ATOM   880  C  CG  . GLN   A 1 111 ? 11.586 -8.618  6.701  1.00 35.46 ? 117 GLN   A CG  1 
ATOM   881  C  CD  . GLN   A 1 111 ? 10.668 -9.561  5.950  1.00 43.34 ? 117 GLN   A CD  1 
ATOM   882  O  OE1 . GLN   A 1 111 ? 9.435  -9.415  5.966  1.00 43.93 ? 117 GLN   A OE1 1 
ATOM   883  N  NE2 . GLN   A 1 111 ? 11.247 -10.527 5.241  1.00 45.04 ? 117 GLN   A NE2 1 
ATOM   884  N  N   . HIS   A 1 112 ? 14.140 -6.522  7.349  1.00 25.31 ? 118 HIS   A N   1 
ATOM   885  C  CA  . HIS   A 1 112 ? 15.209 -6.031  6.480  1.00 24.14 ? 118 HIS   A CA  1 
ATOM   886  C  C   . HIS   A 1 112 ? 16.305 -5.220  7.193  1.00 23.85 ? 118 HIS   A C   1 
ATOM   887  O  O   . HIS   A 1 112 ? 17.361 -4.975  6.599  1.00 25.40 ? 118 HIS   A O   1 
ATOM   888  C  CB  . HIS   A 1 112 ? 14.617 -5.198  5.319  1.00 24.37 ? 118 HIS   A CB  1 
ATOM   889  C  CG  . HIS   A 1 112 ? 13.513 -5.900  4.580  1.00 26.53 ? 118 HIS   A CG  1 
ATOM   890  N  ND1 . HIS   A 1 112 ? 12.180 -5.582  4.799  1.00 28.38 ? 118 HIS   A ND1 1 
ATOM   891  C  CD2 . HIS   A 1 112 ? 13.578 -6.900  3.662  1.00 27.85 ? 118 HIS   A CD2 1 
ATOM   892  C  CE1 . HIS   A 1 112 ? 11.477 -6.359  3.987  1.00 29.25 ? 118 HIS   A CE1 1 
ATOM   893  N  NE2 . HIS   A 1 112 ? 12.273 -7.192  3.298  1.00 28.99 ? 118 HIS   A NE2 1 
ATOM   894  N  N   . GLY   A 1 113 ? 16.043 -4.762  8.423  1.00 21.59 ? 119 GLY   A N   1 
ATOM   895  C  CA  . GLY   A 1 113 ? 17.031 -3.955  9.130  1.00 20.01 ? 119 GLY   A CA  1 
ATOM   896  C  C   . GLY   A 1 113 ? 16.404 -2.775  9.870  1.00 18.68 ? 119 GLY   A C   1 
ATOM   897  O  O   . GLY   A 1 113 ? 15.222 -2.819  10.239 1.00 18.27 ? 119 GLY   A O   1 
ATOM   898  N  N   . VAL   A 1 114 ? 17.218 -1.726  10.126 1.00 16.63 ? 120 VAL   A N   1 
ATOM   899  C  CA  . VAL   A 1 114 ? 16.769 -0.542  10.848 1.00 16.06 ? 120 VAL   A CA  1 
ATOM   900  C  C   . VAL   A 1 114 ? 15.896 0.349   9.950  1.00 15.30 ? 120 VAL   A C   1 
ATOM   901  O  O   . VAL   A 1 114 ? 16.337 0.759   8.874  1.00 15.59 ? 120 VAL   A O   1 
ATOM   902  C  CB  . VAL   A 1 114 ? 17.978 0.275   11.400 1.00 16.27 ? 120 VAL   A CB  1 
ATOM   903  C  CG1 . VAL   A 1 114 ? 17.503 1.554   12.083 1.00 16.53 ? 120 VAL   A CG1 1 
ATOM   904  C  CG2 . VAL   A 1 114 ? 18.784 -0.572  12.380 1.00 16.53 ? 120 VAL   A CG2 1 
ATOM   905  N  N   . VAL   A 1 115 ? 14.731 0.734   10.438 1.00 14.49 ? 121 VAL   A N   1 
ATOM   906  C  CA  . VAL   A 1 115 ? 13.772 1.580   9.712  1.00 15.56 ? 121 VAL   A CA  1 
ATOM   907  C  C   . VAL   A 1 115 ? 13.891 3.041   10.117 1.00 16.39 ? 121 VAL   A C   1 
ATOM   908  O  O   . VAL   A 1 115 ? 13.773 3.944   9.283  1.00 17.95 ? 121 VAL   A O   1 
ATOM   909  C  CB  . VAL   A 1 115 ? 12.303 1.058   9.964  1.00 16.71 ? 121 VAL   A CB  1 
ATOM   910  C  CG1 . VAL   A 1 115 ? 11.246 2.002   9.367  1.00 16.56 ? 121 VAL   A CG1 1 
ATOM   911  C  CG2 . VAL   A 1 115 ? 12.132 -0.349  9.438  1.00 17.09 ? 121 VAL   A CG2 1 
ATOM   912  N  N   . GLY   A 1 116 ? 14.086 3.281   11.412 1.00 16.17 ? 122 GLY   A N   1 
ATOM   913  C  CA  . GLY   A 1 116 ? 14.166 4.644   11.931 1.00 15.93 ? 122 GLY   A CA  1 
ATOM   914  C  C   . GLY   A 1 116 ? 14.383 4.705   13.431 1.00 15.99 ? 122 GLY   A C   1 
ATOM   915  O  O   . GLY   A 1 116 ? 14.741 3.682   14.035 1.00 16.49 ? 122 GLY   A O   1 
ATOM   916  N  N   . ILE   A 1 117 ? 14.198 5.903   14.059 1.00 14.81 ? 123 ILE   A N   1 
ATOM   917  C  CA  . ILE   A 1 117 ? 14.411 6.058   15.502 1.00 13.91 ? 123 ILE   A CA  1 
ATOM   918  C  C   . ILE   A 1 117 ? 13.280 6.840   16.131 1.00 13.58 ? 123 ILE   A C   1 
ATOM   919  O  O   . ILE   A 1 117 ? 12.714 7.729   15.483 1.00 13.76 ? 123 ILE   A O   1 
ATOM   920  C  CB  . ILE   A 1 117 ? 15.750 6.771   15.872 1.00 14.71 ? 123 ILE   A CB  1 
ATOM   921  C  CG1 . ILE   A 1 117 ? 15.894 8.108   15.141 1.00 14.62 ? 123 ILE   A CG1 1 
ATOM   922  C  CG2 . ILE   A 1 117 ? 16.976 5.852   15.657 1.00 15.66 ? 123 ILE   A CG2 1 
ATOM   923  C  CD1 . ILE   A 1 117 ? 17.228 8.927   15.673 1.00 16.26 ? 123 ILE   A CD1 1 
ATOM   924  N  N   . VAL   A 1 118 ? 12.963 6.550   17.404 1.00 13.00 ? 124 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 118 ? 11.904 7.312   18.119 1.00 13.34 ? 124 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 118 ? 12.230 8.823   18.081 1.00 13.61 ? 124 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 118 ? 13.385 9.190   18.335 1.00 13.39 ? 124 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 118 ? 11.752 6.809   19.587 1.00 14.87 ? 124 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 118 ? 10.746 7.665   20.376 1.00 15.76 ? 124 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 118 ? 11.359 5.328   19.611 1.00 14.86 ? 124 VAL   A CG2 1 
ATOM   931  N  N   . SER   A 1 119 ? 11.227 9.691   17.761 1.00 14.42 ? 125 SER   A N   1 
ATOM   932  C  CA  . SER   A 1 119 ? 11.460 11.134  17.682 1.00 15.17 ? 125 SER   A CA  1 
ATOM   933  C  C   . SER   A 1 119 ? 10.336 11.925  18.360 1.00 15.92 ? 125 SER   A C   1 
ATOM   934  O  O   . SER   A 1 119 ? 10.576 13.030  18.803 1.00 16.11 ? 125 SER   A O   1 
ATOM   935  C  CB  . SER   A 1 119 ? 11.602 11.581  16.227 1.00 17.19 ? 125 SER   A CB  1 
ATOM   936  O  OG  . SER   A 1 119 ? 11.736 12.984  16.015 1.00 17.77 ? 125 SER   A OG  1 
ATOM   937  N  N   . THR   A 1 120 ? 9.092  11.380  18.398 1.00 14.30 ? 126 THR   A N   1 
ATOM   938  C  CA  . THR   A 1 120 ? 7.966  12.119  19.004 1.00 15.48 ? 126 THR   A CA  1 
ATOM   939  C  C   . THR   A 1 120 ? 7.060  11.133  19.834 1.00 17.86 ? 126 THR   A C   1 
ATOM   940  O  O   . THR   A 1 120 ? 7.254  9.908   19.745 1.00 17.58 ? 126 THR   A O   1 
ATOM   941  C  CB  . THR   A 1 120 ? 7.090  12.825  17.920 1.00 17.00 ? 126 THR   A CB  1 
ATOM   942  O  OG1 . THR   A 1 120 ? 6.233  11.866  17.278 1.00 16.91 ? 126 THR   A OG1 1 
ATOM   943  C  CG2 . THR   A 1 120 ? 7.879  13.629  16.899 1.00 16.01 ? 126 THR   A CG2 1 
ATOM   944  N  N   . GLY   A 1 121 ? 6.012  11.640  20.493 1.00 19.19 ? 127 GLY   A N   1 
ATOM   945  C  CA  . GLY   A 1 121 ? 5.084  10.747  21.181 1.00 20.18 ? 127 GLY   A CA  1 
ATOM   946  C  C   . GLY   A 1 121 ? 4.163  11.481  22.124 1.00 21.49 ? 127 GLY   A C   1 
ATOM   947  O  O   . GLY   A 1 121 ? 4.190  12.713  22.197 1.00 21.68 ? 127 GLY   A O   1 
ATOM   948  N  N   . GLY   A 1 122 ? 3.451  10.708  22.921 1.00 21.91 ? 128 GLY   A N   1 
ATOM   949  C  CA  . GLY   A 1 122 ? 2.563  11.258  23.934 1.00 22.66 ? 128 GLY   A CA  1 
ATOM   950  C  C   . GLY   A 1 122 ? 1.219  10.564  23.907 1.00 23.60 ? 128 GLY   A C   1 
ATOM   951  O  O   . GLY   A 1 122 ? 0.776  10.127  22.843 1.00 24.18 ? 128 GLY   A O   1 
ATOM   952  N  N   . ASN   A 1 123 ? 0.569  10.432  25.086 1.00 23.18 ? 129 ASN   A N   1 
ATOM   953  C  CA  . ASN   A 1 123 ? -0.760 9.848   25.222 1.00 22.95 ? 129 ASN   A CA  1 
ATOM   954  C  C   . ASN   A 1 123 ? -0.974 8.507   24.488 1.00 21.30 ? 129 ASN   A C   1 
ATOM   955  O  O   . ASN   A 1 123 ? -2.032 8.302   23.879 1.00 21.72 ? 129 ASN   A O   1 
ATOM   956  C  CB  . ASN   A 1 123 ? -1.794 10.879  24.761 1.00 26.00 ? 129 ASN   A CB  1 
ATOM   957  C  CG  . ASN   A 1 123 ? -1.787 12.126  25.597 1.00 31.17 ? 129 ASN   A CG  1 
ATOM   958  O  OD1 . ASN   A 1 123 ? -2.024 12.052  26.808 1.00 32.67 ? 129 ASN   A OD1 1 
ATOM   959  N  ND2 . ASN   A 1 123 ? -1.479 13.279  24.965 1.00 31.68 ? 129 ASN   A ND2 1 
ATOM   960  N  N   . GLY   A 1 124 ? -0.008 7.592   24.590 1.00 19.34 ? 130 GLY   A N   1 
ATOM   961  C  CA  . GLY   A 1 124 ? -0.140 6.293   23.942 1.00 19.40 ? 130 GLY   A CA  1 
ATOM   962  C  C   . GLY   A 1 124 ? 0.237  6.251   22.479 1.00 18.99 ? 130 GLY   A C   1 
ATOM   963  O  O   . GLY   A 1 124 ? -0.008 5.239   21.817 1.00 19.74 ? 130 GLY   A O   1 
ATOM   964  N  N   . LEU   A 1 125 ? 0.869  7.318   21.972 1.00 17.76 ? 131 LEU   A N   1 
ATOM   965  C  CA  . LEU   A 1 125 ? 1.379  7.361   20.596 1.00 18.62 ? 131 LEU   A CA  1 
ATOM   966  C  C   . LEU   A 1 125 ? 2.912  7.424   20.637 1.00 17.93 ? 131 LEU   A C   1 
ATOM   967  O  O   . LEU   A 1 125 ? 3.506  7.903   21.623 1.00 17.80 ? 131 LEU   A O   1 
ATOM   968  C  CB  . LEU   A 1 125 ? 0.874  8.616   19.863 1.00 19.58 ? 131 LEU   A CB  1 
ATOM   969  C  CG  . LEU   A 1 125 ? -0.609 8.616   19.490 1.00 21.66 ? 131 LEU   A CG  1 
ATOM   970  C  CD1 . LEU   A 1 125 ? -1.017 9.983   19.007 1.00 23.27 ? 131 LEU   A CD1 1 
ATOM   971  C  CD2 . LEU   A 1 125 ? -0.919 7.568   18.399 1.00 21.54 ? 131 LEU   A CD2 1 
ATOM   972  N  N   . VAL   A 1 126 ? 3.549  6.940   19.572 1.00 15.71 ? 132 VAL   A N   1 
ATOM   973  C  CA  . VAL   A 1 126 ? 5.007  7.036   19.429 1.00 16.00 ? 132 VAL   A CA  1 
ATOM   974  C  C   . VAL   A 1 126 ? 5.273  7.319   17.922 1.00 14.97 ? 132 VAL   A C   1 
ATOM   975  O  O   . VAL   A 1 126 ? 4.593  6.714   17.071 1.00 15.80 ? 132 VAL   A O   1 
ATOM   976  C  CB  . VAL   A 1 126 ? 5.741  5.755   19.936 1.00 17.12 ? 132 VAL   A CB  1 
ATOM   977  C  CG1 . VAL   A 1 126 ? 5.291  4.518   19.160 1.00 17.55 ? 132 VAL   A CG1 1 
ATOM   978  C  CG2 . VAL   A 1 126 ? 7.270  5.931   19.856 1.00 17.20 ? 132 VAL   A CG2 1 
ATOM   979  N  N   . GLY   A 1 127 ? 6.133  8.316   17.620 1.00 14.88 ? 133 GLY   A N   1 
ATOM   980  C  CA  . GLY   A 1 127 ? 6.483  8.720   16.260 1.00 15.02 ? 133 GLY   A CA  1 
ATOM   981  C  C   . GLY   A 1 127 ? 7.945  8.416   15.953 1.00 15.65 ? 133 GLY   A C   1 
ATOM   982  O  O   . GLY   A 1 127 ? 8.817  8.587   16.825 1.00 15.27 ? 133 GLY   A O   1 
ATOM   983  N  N   . PHE   A 1 128 ? 8.237  7.925   14.726 1.00 15.07 ? 134 PHE   A N   1 
ATOM   984  C  CA  . PHE   A 1 128 ? 9.605  7.535   14.352 1.00 15.27 ? 134 PHE   A CA  1 
ATOM   985  C  C   . PHE   A 1 128 ? 10.083 8.357   13.152 1.00 15.58 ? 134 PHE   A C   1 
ATOM   986  O  O   . PHE   A 1 128 ? 9.337  8.535   12.171 1.00 15.58 ? 134 PHE   A O   1 
ATOM   987  C  CB  . PHE   A 1 128 ? 9.607  6.049   13.945 1.00 15.54 ? 134 PHE   A CB  1 
ATOM   988  C  CG  . PHE   A 1 128 ? 8.974  5.112   14.975 1.00 15.61 ? 134 PHE   A CG  1 
ATOM   989  C  CD1 . PHE   A 1 128 ? 9.723  4.602   16.031 1.00 15.95 ? 134 PHE   A CD1 1 
ATOM   990  C  CD2 . PHE   A 1 128 ? 7.658  4.699   14.847 1.00 15.84 ? 134 PHE   A CD2 1 
ATOM   991  C  CE1 . PHE   A 1 128 ? 9.140  3.755   16.985 1.00 16.61 ? 134 PHE   A CE1 1 
ATOM   992  C  CE2 . PHE   A 1 128 ? 7.090  3.815   15.776 1.00 16.68 ? 134 PHE   A CE2 1 
ATOM   993  C  CZ  . PHE   A 1 128 ? 7.835  3.359   16.846 1.00 16.36 ? 134 PHE   A CZ  1 
ATOM   994  N  N   . ALA   A 1 129 ? 11.316 8.847   13.224 1.00 14.56 ? 135 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 129 ? 11.923 9.550   12.081 1.00 15.32 ? 135 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 129 ? 12.455 8.472   11.125 1.00 15.67 ? 135 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 129 ? 13.348 7.696   11.507 1.00 15.05 ? 135 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 129 ? 13.072 10.446  12.560 1.00 15.13 ? 135 ALA   A CB  1 
ATOM   999  N  N   . ASP   A 1 130 ? 11.893 8.392   9.898  1.00 15.96 ? 136 ASP   A N   1 
ATOM   1000 C  CA  . ASP   A 1 130 ? 12.324 7.373   8.935  1.00 16.48 ? 136 ASP   A CA  1 
ATOM   1001 C  C   . ASP   A 1 130 ? 13.747 7.682   8.422  1.00 16.21 ? 136 ASP   A C   1 
ATOM   1002 O  O   . ASP   A 1 130 ? 14.115 8.863   8.276  1.00 17.01 ? 136 ASP   A O   1 
ATOM   1003 C  CB  . ASP   A 1 130 ? 11.359 7.416   7.729  1.00 18.09 ? 136 ASP   A CB  1 
ATOM   1004 C  CG  . ASP   A 1 130 ? 11.599 6.385   6.638  1.00 24.84 ? 136 ASP   A CG  1 
ATOM   1005 O  OD1 . ASP   A 1 130 ? 11.820 5.200   6.973  1.00 22.77 ? 136 ASP   A OD1 1 
ATOM   1006 O  OD2 . ASP   A 1 130 ? 11.562 6.765   5.437  1.00 30.52 ? 136 ASP   A OD2 1 
ATOM   1007 N  N   . VAL   A 1 131 ? 14.544 6.623   8.140  1.00 14.83 ? 137 VAL   A N   1 
ATOM   1008 C  CA  . VAL   A 1 131 ? 15.871 6.820   7.536  1.00 15.36 ? 137 VAL   A CA  1 
ATOM   1009 C  C   . VAL   A 1 131 ? 16.027 5.990   6.230  1.00 16.16 ? 137 VAL   A C   1 
ATOM   1010 O  O   . VAL   A 1 131 ? 17.094 6.052   5.631  1.00 16.59 ? 137 VAL   A O   1 
ATOM   1011 C  CB  . VAL   A 1 131 ? 17.049 6.493   8.503  1.00 15.57 ? 137 VAL   A CB  1 
ATOM   1012 C  CG1 . VAL   A 1 131 ? 17.030 7.420   9.738  1.00 16.23 ? 137 VAL   A CG1 1 
ATOM   1013 C  CG2 . VAL   A 1 131 ? 17.055 5.010   8.900  1.00 15.77 ? 137 VAL   A CG2 1 
ATOM   1014 N  N   . ARG   A 1 132 ? 14.986 5.196   5.815  1.00 16.16 ? 138 ARG   A N   1 
ATOM   1015 C  CA  . ARG   A 1 132 ? 15.082 4.315   4.647  1.00 15.98 ? 138 ARG   A CA  1 
ATOM   1016 C  C   . ARG   A 1 132 ? 15.356 5.034   3.315  1.00 16.78 ? 138 ARG   A C   1 
ATOM   1017 O  O   . ARG   A 1 132 ? 15.800 4.391   2.367  1.00 17.11 ? 138 ARG   A O   1 
ATOM   1018 C  CB  . ARG   A 1 132 ? 13.832 3.415   4.534  1.00 16.08 ? 138 ARG   A CB  1 
ATOM   1019 C  CG  . ARG   A 1 132 ? 13.648 2.510   5.760  1.00 15.57 ? 138 ARG   A CG  1 
ATOM   1020 C  CD  . ARG   A 1 132 ? 12.340 1.718   5.631  1.00 17.16 ? 138 ARG   A CD  1 
ATOM   1021 N  NE  . ARG   A 1 132 ? 11.170 2.587   5.841  1.00 18.46 ? 138 ARG   A NE  1 
ATOM   1022 C  CZ  . ARG   A 1 132 ? 9.916  2.134   5.889  1.00 20.98 ? 138 ARG   A CZ  1 
ATOM   1023 N  NH1 . ARG   A 1 132 ? 9.650  0.860   5.589  1.00 18.94 ? 138 ARG   A NH1 1 
ATOM   1024 N  NH2 . ARG   A 1 132 ? 8.912  2.963   6.180  1.00 19.56 ? 138 ARG   A NH2 1 
ATOM   1025 N  N   . ASP   A 1 133 ? 15.018 6.324   3.215  1.00 16.23 ? 139 ASP   A N   1 
ATOM   1026 C  CA  . ASP   A 1 133 ? 15.282 7.087   1.964  1.00 16.76 ? 139 ASP   A CA  1 
ATOM   1027 C  C   . ASP   A 1 133 ? 16.725 7.658   1.889  1.00 17.36 ? 139 ASP   A C   1 
ATOM   1028 O  O   . ASP   A 1 133 ? 17.113 8.230   0.844  1.00 18.69 ? 139 ASP   A O   1 
ATOM   1029 C  CB  . ASP   A 1 133 ? 14.274 8.251   1.842  1.00 19.12 ? 139 ASP   A CB  1 
ATOM   1030 C  CG  . ASP   A 1 133 ? 14.472 9.278   2.955  1.00 24.56 ? 139 ASP   A CG  1 
ATOM   1031 O  OD1 . ASP   A 1 133 ? 14.557 8.867   4.131  1.00 25.42 ? 139 ASP   A OD1 1 
ATOM   1032 O  OD2 . ASP   A 1 133 ? 14.595 10.485  2.639  1.00 25.99 ? 139 ASP   A OD2 1 
ATOM   1033 N  N   . LEU   A 1 134 ? 17.516 7.539   2.992  1.00 16.83 ? 140 LEU   A N   1 
ATOM   1034 C  CA  . LEU   A 1 134 ? 18.874 8.109   3.048  1.00 16.28 ? 140 LEU   A CA  1 
ATOM   1035 C  C   . LEU   A 1 134 ? 19.851 7.056   2.509  1.00 17.17 ? 140 LEU   A C   1 
ATOM   1036 O  O   . LEU   A 1 134 ? 20.566 6.395   3.272  1.00 16.70 ? 140 LEU   A O   1 
ATOM   1037 C  CB  . LEU   A 1 134 ? 19.214 8.497   4.497  1.00 16.89 ? 140 LEU   A CB  1 
ATOM   1038 C  CG  . LEU   A 1 134 ? 18.262 9.556   5.123  1.00 17.95 ? 140 LEU   A CG  1 
ATOM   1039 C  CD1 . LEU   A 1 134 ? 18.695 9.881   6.550  1.00 18.23 ? 140 LEU   A CD1 1 
ATOM   1040 C  CD2 . LEU   A 1 134 ? 18.269 10.865  4.302  1.00 19.26 ? 140 LEU   A CD2 1 
ATOM   1041 N  N   . LEU   A 1 135 ? 19.845 6.889   1.187  1.00 17.51 ? 141 LEU   A N   1 
ATOM   1042 C  CA  . LEU   A 1 135 ? 20.632 5.834   0.529  1.00 19.44 ? 141 LEU   A CA  1 
ATOM   1043 C  C   . LEU   A 1 135 ? 22.127 5.968   0.740  1.00 19.80 ? 141 LEU   A C   1 
ATOM   1044 O  O   . LEU   A 1 135 ? 22.834 4.950   0.750  1.00 20.60 ? 141 LEU   A O   1 
ATOM   1045 C  CB  . LEU   A 1 135 ? 20.295 5.718   -0.971 1.00 20.10 ? 141 LEU   A CB  1 
ATOM   1046 C  CG  . LEU   A 1 135 ? 18.785 5.643   -1.298 1.00 22.00 ? 141 LEU   A CG  1 
ATOM   1047 C  CD1 . LEU   A 1 135 ? 18.572 5.493   -2.791 1.00 23.18 ? 141 LEU   A CD1 1 
ATOM   1048 C  CD2 . LEU   A 1 135 ? 18.065 4.537   -0.508 1.00 22.45 ? 141 LEU   A CD2 1 
ATOM   1049 N  N   . TRP   A 1 136 ? 22.609 7.219   0.919  1.00 19.57 ? 142 TRP   A N   1 
ATOM   1050 C  CA  . TRP   A 1 136 ? 24.032 7.496   1.112  1.00 19.40 ? 142 TRP   A CA  1 
ATOM   1051 C  C   . TRP   A 1 136 ? 24.605 6.896   2.409  1.00 19.68 ? 142 TRP   A C   1 
ATOM   1052 O  O   . TRP   A 1 136 ? 25.831 6.757   2.529  1.00 19.21 ? 142 TRP   A O   1 
ATOM   1053 C  CB  . TRP   A 1 136 ? 24.324 9.002   1.016  1.00 19.18 ? 142 TRP   A CB  1 
ATOM   1054 C  CG  . TRP   A 1 136 ? 23.468 9.838   1.922  1.00 18.99 ? 142 TRP   A CG  1 
ATOM   1055 C  CD1 . TRP   A 1 136 ? 22.314 10.496  1.595  1.00 19.67 ? 142 TRP   A CD1 1 
ATOM   1056 C  CD2 . TRP   A 1 136 ? 23.758 10.182  3.279  1.00 19.02 ? 142 TRP   A CD2 1 
ATOM   1057 N  NE1 . TRP   A 1 136 ? 21.871 11.231  2.668  1.00 20.01 ? 142 TRP   A NE1 1 
ATOM   1058 C  CE2 . TRP   A 1 136 ? 22.736 11.047  3.720  1.00 19.88 ? 142 TRP   A CE2 1 
ATOM   1059 C  CE3 . TRP   A 1 136 ? 24.804 9.863   4.159  1.00 19.91 ? 142 TRP   A CE3 1 
ATOM   1060 C  CZ2 . TRP   A 1 136 ? 22.711 11.560  5.020  1.00 20.05 ? 142 TRP   A CZ2 1 
ATOM   1061 C  CZ3 . TRP   A 1 136 ? 24.803 10.413  5.425  1.00 20.30 ? 142 TRP   A CZ3 1 
ATOM   1062 C  CH2 . TRP   A 1 136 ? 23.765 11.246  5.845  1.00 19.95 ? 142 TRP   A CH2 1 
ATOM   1063 N  N   . LEU   A 1 137 ? 23.720 6.490   3.365  1.00 18.76 ? 143 LEU   A N   1 
ATOM   1064 C  CA  . LEU   A 1 137 ? 24.217 5.848   4.592  1.00 20.31 ? 143 LEU   A CA  1 
ATOM   1065 C  C   . LEU   A 1 137 ? 24.928 4.511   4.280  1.00 22.55 ? 143 LEU   A C   1 
ATOM   1066 O  O   . LEU   A 1 137 ? 25.730 4.069   5.094  1.00 21.94 ? 143 LEU   A O   1 
ATOM   1067 C  CB  . LEU   A 1 137 ? 23.075 5.577   5.585  1.00 19.30 ? 143 LEU   A CB  1 
ATOM   1068 C  CG  . LEU   A 1 137 ? 22.449 6.813   6.259  1.00 19.74 ? 143 LEU   A CG  1 
ATOM   1069 C  CD1 . LEU   A 1 137 ? 21.219 6.419   7.083  1.00 20.13 ? 143 LEU   A CD1 1 
ATOM   1070 C  CD2 . LEU   A 1 137 ? 23.484 7.525   7.189  1.00 19.36 ? 143 LEU   A CD2 1 
ATOM   1071 N  N   . ASP   A 1 138 ? 24.606 3.866   3.138  1.00 25.36 ? 144 ASP   A N   1 
ATOM   1072 C  CA  . ASP   A 1 138 ? 25.175 2.562   2.757  1.00 29.38 ? 144 ASP   A CA  1 
ATOM   1073 C  C   . ASP   A 1 138 ? 26.536 2.655   2.066  1.00 33.71 ? 144 ASP   A C   1 
ATOM   1074 O  O   . ASP   A 1 138 ? 27.067 1.617   1.678  1.00 33.81 ? 144 ASP   A O   1 
ATOM   1075 C  CB  . ASP   A 1 138 ? 24.222 1.816   1.794  1.00 31.30 ? 144 ASP   A CB  1 
ATOM   1076 C  CG  . ASP   A 1 138 ? 22.866 1.452   2.364  1.00 38.06 ? 144 ASP   A CG  1 
ATOM   1077 O  OD1 . ASP   A 1 138 ? 22.717 1.480   3.598  1.00 38.76 ? 144 ASP   A OD1 1 
ATOM   1078 O  OD2 . ASP   A 1 138 ? 21.955 1.125   1.573  1.00 42.50 ? 144 ASP   A OD2 1 
ATOM   1079 N  N   . GLU   A 1 139 ? 27.087 3.868   1.863  1.00 36.59 ? 145 GLU   A N   1 
ATOM   1080 C  CA  . GLU   A 1 139 ? 28.361 4.002   1.137  1.00 39.94 ? 145 GLU   A CA  1 
ATOM   1081 C  C   . GLU   A 1 139 ? 29.259 5.148   1.690  1.00 42.79 ? 145 GLU   A C   1 
ATOM   1082 O  O   . GLU   A 1 139 ? 28.831 5.877   2.583  1.00 42.75 ? 145 GLU   A O   1 
ATOM   1083 C  CB  . GLU   A 1 139 ? 28.031 4.269   -0.346 1.00 42.86 ? 145 GLU   A CB  1 
ATOM   1084 C  CG  . GLU   A 1 139 ? 27.412 5.643   -0.548 1.00 48.77 ? 145 GLU   A CG  1 
ATOM   1085 C  CD  . GLU   A 1 139 ? 26.534 5.830   -1.768 1.00 56.86 ? 145 GLU   A CD  1 
ATOM   1086 O  OE1 . GLU   A 1 139 ? 26.207 7.000   -2.085 1.00 57.00 ? 145 GLU   A OE1 1 
ATOM   1087 O  OE2 . GLU   A 1 139 ? 26.165 4.814   -2.401 1.00 60.08 ? 145 GLU   A OE2 1 
ATOM   1088 N  N   . GLU   A 1 140 ? 30.472 5.338   1.103  1.00 45.13 ? 146 GLU   A N   1 
ATOM   1089 C  CA  . GLU   A 1 140 ? 31.427 6.428   1.380  1.00 47.63 ? 146 GLU   A CA  1 
ATOM   1090 C  C   . GLU   A 1 140 ? 31.478 6.844   2.854  1.00 49.42 ? 146 GLU   A C   1 
ATOM   1091 O  O   . GLU   A 1 140 ? 32.477 7.401   3.312  1.00 50.50 ? 146 GLU   A O   1 
ATOM   1092 C  CB  . GLU   A 1 140 ? 31.122 7.625   0.434  1.00 51.16 ? 146 GLU   A CB  1 
ATOM   1093 C  CG  . GLU   A 1 140 ? 31.279 9.050   0.965  1.00 58.22 ? 146 GLU   A CG  1 
ATOM   1094 C  CD  . GLU   A 1 140 ? 32.669 9.659   0.913  1.00 66.55 ? 146 GLU   A CD  1 
ATOM   1095 O  OE1 . GLU   A 1 140 ? 32.761 10.905  0.826  1.00 68.85 ? 146 GLU   A OE1 1 
ATOM   1096 O  OE2 . GLU   A 1 140 ? 33.666 8.901   0.963  1.00 68.46 ? 146 GLU   A OE2 1 
ATOM   1097 N  N   . SER   B 1 1   ? 21.760 -21.352 7.653  1.00 23.27 ? 7   SER   C N   1 
ATOM   1098 C  CA  . SER   B 1 1   ? 20.617 -21.252 8.561  1.00 23.77 ? 7   SER   C CA  1 
ATOM   1099 C  C   . SER   B 1 1   ? 20.629 -22.390 9.612  1.00 22.95 ? 7   SER   C C   1 
ATOM   1100 O  O   . SER   B 1 1   ? 21.317 -23.409 9.413  1.00 22.77 ? 7   SER   C O   1 
ATOM   1101 C  CB  . SER   B 1 1   ? 19.317 -21.305 7.760  1.00 26.62 ? 7   SER   C CB  1 
ATOM   1102 O  OG  . SER   B 1 1   ? 19.155 -22.602 7.196  1.00 30.16 ? 7   SER   C OG  1 
ATOM   1103 N  N   . GLY   B 1 2   ? 19.870 -22.203 10.707 1.00 22.21 ? 8   GLY   C N   1 
ATOM   1104 C  CA  . GLY   B 1 2   ? 19.761 -23.188 11.784 1.00 21.78 ? 8   GLY   C CA  1 
ATOM   1105 C  C   . GLY   B 1 2   ? 19.469 -22.529 13.130 1.00 20.77 ? 8   GLY   C C   1 
ATOM   1106 O  O   . GLY   B 1 2   ? 19.833 -21.371 13.366 1.00 20.98 ? 8   GLY   C O   1 
ATOM   1107 N  N   . ALA   B 1 3   ? 18.827 -23.275 14.035 1.00 19.23 ? 9   ALA   C N   1 
ATOM   1108 C  CA  . ALA   B 1 3   ? 18.497 -22.770 15.362 1.00 18.99 ? 9   ALA   C CA  1 
ATOM   1109 C  C   . ALA   B 1 3   ? 18.605 -23.888 16.422 1.00 18.14 ? 9   ALA   C C   1 
ATOM   1110 O  O   . ALA   B 1 3   ? 18.644 -25.072 16.064 1.00 19.14 ? 9   ALA   C O   1 
ATOM   1111 C  CB  . ALA   B 1 3   ? 17.059 -22.214 15.357 1.00 19.05 ? 9   ALA   C CB  1 
ATOM   1112 N  N   . ILE   B 1 4   ? 18.659 -23.510 17.709 1.00 17.29 ? 10  ILE   C N   1 
ATOM   1113 C  CA  . ILE   B 1 4   ? 18.603 -24.484 18.813 1.00 17.30 ? 10  ILE   C CA  1 
ATOM   1114 C  C   . ILE   B 1 4   ? 17.198 -24.329 19.421 1.00 18.15 ? 10  ILE   C C   1 
ATOM   1115 O  O   . ILE   B 1 4   ? 16.753 -23.183 19.646 1.00 19.04 ? 10  ILE   C O   1 
ATOM   1116 C  CB  . ILE   B 1 4   ? 19.660 -24.177 19.904 1.00 17.54 ? 10  ILE   C CB  1 
ATOM   1117 C  CG1 . ILE   B 1 4   ? 21.118 -24.155 19.314 1.00 17.78 ? 10  ILE   C CG1 1 
ATOM   1118 C  CG2 . ILE   B 1 4   ? 19.551 -25.181 21.051 1.00 18.14 ? 10  ILE   C CG2 1 
ATOM   1119 C  CD1 . ILE   B 1 4   ? 22.153 -23.500 20.317 1.00 18.39 ? 10  ILE   C CD1 1 
ATOM   1120 N  N   . TYR   B 1 5   ? 16.500 -25.451 19.720 1.00 18.04 ? 11  TYR   C N   1 
ATOM   1121 C  CA  . TYR   B 1 5   ? 15.180 -25.367 20.338 1.00 19.05 ? 11  TYR   C CA  1 
ATOM   1122 C  C   . TYR   B 1 5   ? 15.241 -26.048 21.719 1.00 19.98 ? 11  TYR   C C   1 
ATOM   1123 O  O   . TYR   B 1 5   ? 15.291 -27.268 21.803 1.00 20.47 ? 11  TYR   C O   1 
ATOM   1124 C  CB  . TYR   B 1 5   ? 14.102 -26.009 19.428 1.00 18.45 ? 11  TYR   C CB  1 
ATOM   1125 C  CG  . TYR   B 1 5   ? 13.917 -25.243 18.131 1.00 18.50 ? 11  TYR   C CG  1 
ATOM   1126 C  CD1 . TYR   B 1 5   ? 13.072 -24.139 18.065 1.00 19.15 ? 11  TYR   C CD1 1 
ATOM   1127 C  CD2 . TYR   B 1 5   ? 14.589 -25.619 16.974 1.00 18.69 ? 11  TYR   C CD2 1 
ATOM   1128 C  CE1 . TYR   B 1 5   ? 12.906 -23.428 16.882 1.00 19.81 ? 11  TYR   C CE1 1 
ATOM   1129 C  CE2 . TYR   B 1 5   ? 14.437 -24.913 15.789 1.00 20.21 ? 11  TYR   C CE2 1 
ATOM   1130 C  CZ  . TYR   B 1 5   ? 13.588 -23.822 15.741 1.00 21.39 ? 11  TYR   C CZ  1 
ATOM   1131 O  OH  . TYR   B 1 5   ? 13.488 -23.101 14.566 1.00 23.90 ? 11  TYR   C OH  1 
ATOM   1132 N  N   . VAL   B 1 6   ? 15.265 -25.257 22.805 1.00 18.67 ? 12  VAL   C N   1 
ATOM   1133 C  CA  . VAL   B 1 6   ? 15.332 -25.823 24.159 1.00 18.42 ? 12  VAL   C CA  1 
ATOM   1134 C  C   . VAL   B 1 6   ? 14.225 -25.188 25.002 1.00 18.74 ? 12  VAL   C C   1 
ATOM   1135 O  O   . VAL   B 1 6   ? 14.046 -23.985 24.939 1.00 18.48 ? 12  VAL   C O   1 
ATOM   1136 C  CB  . VAL   B 1 6   ? 16.735 -25.621 24.775 1.00 19.79 ? 12  VAL   C CB  1 
ATOM   1137 C  CG1 . VAL   B 1 6   ? 17.177 -24.151 24.671 1.00 19.64 ? 12  VAL   C CG1 1 
ATOM   1138 C  CG2 . VAL   B 1 6   ? 16.779 -26.153 26.216 1.00 20.60 ? 12  VAL   C CG2 1 
ATOM   1139 N  N   . GLY   B 1 7   ? 13.392 -25.997 25.692 1.00 19.24 ? 13  GLY   C N   1 
ATOM   1140 C  CA  . GLY   B 1 7   ? 12.266 -25.448 26.451 1.00 19.57 ? 13  GLY   C CA  1 
ATOM   1141 C  C   . GLY   B 1 7   ? 11.355 -24.609 25.564 1.00 20.15 ? 13  GLY   C C   1 
ATOM   1142 O  O   . GLY   B 1 7   ? 11.108 -24.988 24.407 1.00 20.75 ? 13  GLY   C O   1 
ATOM   1143 N  N   . ASN   B 1 8   ? 10.931 -23.427 26.033 1.00 19.72 ? 14  ASN   C N   1 
ATOM   1144 C  CA  . ASN   B 1 8   ? 10.156 -22.528 25.179 1.00 20.11 ? 14  ASN   C CA  1 
ATOM   1145 C  C   . ASN   B 1 8   ? 11.085 -21.427 24.605 1.00 18.80 ? 14  ASN   C C   1 
ATOM   1146 O  O   . ASN   B 1 8   ? 10.650 -20.283 24.436 1.00 18.99 ? 14  ASN   C O   1 
ATOM   1147 C  CB  . ASN   B 1 8   ? 8.935  -21.938 25.882 1.00 23.17 ? 14  ASN   C CB  1 
ATOM   1148 C  CG  . ASN   B 1 8   ? 7.859  -22.990 26.075 1.00 28.69 ? 14  ASN   C CG  1 
ATOM   1149 O  OD1 . ASN   B 1 8   ? 6.946  -23.145 25.251 1.00 31.18 ? 14  ASN   C OD1 1 
ATOM   1150 N  ND2 . ASN   B 1 8   ? 7.976  -23.746 27.143 1.00 29.59 ? 14  ASN   C ND2 1 
ATOM   1151 N  N   . TYR   B 1 9   ? 12.313 -21.801 24.244 1.00 17.52 ? 15  TYR   C N   1 
ATOM   1152 C  CA  . TYR   B 1 9   ? 13.254 -20.829 23.657 1.00 18.13 ? 15  TYR   C CA  1 
ATOM   1153 C  C   . TYR   B 1 9   ? 13.739 -21.288 22.264 1.00 18.39 ? 15  TYR   C C   1 
ATOM   1154 O  O   . TYR   B 1 9   ? 13.948 -22.481 22.054 1.00 18.70 ? 15  TYR   C O   1 
ATOM   1155 C  CB  . TYR   B 1 9   ? 14.500 -20.682 24.567 1.00 18.65 ? 15  TYR   C CB  1 
ATOM   1156 C  CG  . TYR   B 1 9   ? 14.212 -20.119 25.949 1.00 19.92 ? 15  TYR   C CG  1 
ATOM   1157 C  CD1 . TYR   B 1 9   ? 13.652 -18.860 26.104 1.00 21.70 ? 15  TYR   C CD1 1 
ATOM   1158 C  CD2 . TYR   B 1 9   ? 14.561 -20.824 27.100 1.00 21.04 ? 15  TYR   C CD2 1 
ATOM   1159 C  CE1 . TYR   B 1 9   ? 13.371 -18.343 27.372 1.00 23.19 ? 15  TYR   C CE1 1 
ATOM   1160 C  CE2 . TYR   B 1 9   ? 14.310 -20.307 28.372 1.00 22.68 ? 15  TYR   C CE2 1 
ATOM   1161 C  CZ  . TYR   B 1 9   ? 13.737 -19.054 28.504 1.00 25.33 ? 15  TYR   C CZ  1 
ATOM   1162 O  OH  . TYR   B 1 9   ? 13.499 -18.530 29.762 1.00 28.74 ? 15  TYR   C OH  1 
ATOM   1163 N  N   . ARG   B 1 10  ? 14.011 -20.326 21.362 1.00 16.98 ? 16  ARG   C N   1 
ATOM   1164 C  CA  . ARG   B 1 10  ? 14.612 -20.553 20.037 1.00 16.52 ? 16  ARG   C CA  1 
ATOM   1165 C  C   . ARG   B 1 10  ? 15.882 -19.683 19.990 1.00 16.41 ? 16  ARG   C C   1 
ATOM   1166 O  O   . ARG   B 1 10  ? 15.784 -18.478 20.222 1.00 15.68 ? 16  ARG   C O   1 
ATOM   1167 C  CB  . ARG   B 1 10  ? 13.634 -20.155 18.896 1.00 18.37 ? 16  ARG   C CB  1 
ATOM   1168 C  CG  . ARG   B 1 10  ? 14.271 -19.924 17.494 1.00 18.87 ? 16  ARG   C CG  1 
ATOM   1169 C  CD  . ARG   B 1 10  ? 13.211 -19.689 16.389 1.00 19.75 ? 16  ARG   C CD  1 
ATOM   1170 N  NE  . ARG   B 1 10  ? 13.617 -18.700 15.369 1.00 22.32 ? 16  ARG   C NE  1 
ATOM   1171 C  CZ  . ARG   B 1 10  ? 14.086 -19.007 14.159 1.00 24.29 ? 16  ARG   C CZ  1 
ATOM   1172 N  NH1 . ARG   B 1 10  ? 14.316 -20.273 13.830 1.00 22.20 ? 16  ARG   C NH1 1 
ATOM   1173 N  NH2 . ARG   B 1 10  ? 14.418 -18.041 13.301 1.00 24.06 ? 16  ARG   C NH2 1 
ATOM   1174 N  N   . VAL   B 1 11  ? 17.070 -20.304 19.794 1.00 16.26 ? 17  VAL   C N   1 
ATOM   1175 C  CA  . VAL   B 1 11  ? 18.363 -19.578 19.744 1.00 16.39 ? 17  VAL   C CA  1 
ATOM   1176 C  C   . VAL   B 1 11  ? 18.826 -19.526 18.297 1.00 17.44 ? 17  VAL   C C   1 
ATOM   1177 O  O   . VAL   B 1 11  ? 18.979 -20.577 17.656 1.00 17.27 ? 17  VAL   C O   1 
ATOM   1178 C  CB  . VAL   B 1 11  ? 19.447 -20.283 20.614 1.00 17.09 ? 17  VAL   C CB  1 
ATOM   1179 C  CG1 . VAL   B 1 11  ? 20.723 -19.418 20.693 1.00 17.95 ? 17  VAL   C CG1 1 
ATOM   1180 C  CG2 . VAL   B 1 11  ? 18.900 -20.645 22.008 1.00 17.06 ? 17  VAL   C CG2 1 
ATOM   1181 N  N   . VAL   B 1 12  ? 19.058 -18.309 17.765 1.00 16.86 ? 18  VAL   C N   1 
ATOM   1182 C  CA  A VAL   B 1 12  ? 19.490 -18.126 16.372 0.50 15.92 ? 18  VAL   C CA  1 
ATOM   1183 C  CA  B VAL   B 1 12  ? 19.457 -18.125 16.369 0.50 16.75 ? 18  VAL   C CA  1 
ATOM   1184 C  C   . VAL   B 1 12  ? 20.630 -17.117 16.292 1.00 16.55 ? 18  VAL   C C   1 
ATOM   1185 O  O   . VAL   B 1 12  ? 20.845 -16.339 17.246 1.00 16.71 ? 18  VAL   C O   1 
ATOM   1186 C  CB  A VAL   B 1 12  ? 18.328 -17.598 15.488 0.50 15.79 ? 18  VAL   C CB  1 
ATOM   1187 C  CB  B VAL   B 1 12  ? 18.205 -17.587 15.598 0.50 18.29 ? 18  VAL   C CB  1 
ATOM   1188 C  CG1 A VAL   B 1 12  ? 17.338 -18.700 15.143 0.50 16.41 ? 18  VAL   C CG1 1 
ATOM   1189 C  CG1 B VAL   B 1 12  ? 18.480 -17.364 14.122 0.50 18.17 ? 18  VAL   C CG1 1 
ATOM   1190 C  CG2 A VAL   B 1 12  ? 17.656 -16.378 16.120 0.50 14.39 ? 18  VAL   C CG2 1 
ATOM   1191 C  CG2 B VAL   B 1 12  ? 17.022 -18.532 15.749 0.50 19.55 ? 18  VAL   C CG2 1 
ATOM   1192 N  N   . ASN   B 1 13  ? 21.348 -17.070 15.127 1.00 15.91 ? 19  ASN   C N   1 
ATOM   1193 C  CA  . ASN   B 1 13  ? 22.369 -16.038 14.904 1.00 15.79 ? 19  ASN   C CA  1 
ATOM   1194 C  C   . ASN   B 1 13  ? 21.554 -14.688 14.850 1.00 16.35 ? 19  ASN   C C   1 
ATOM   1195 O  O   . ASN   B 1 13  ? 20.540 -14.628 14.162 1.00 16.85 ? 19  ASN   C O   1 
ATOM   1196 C  CB  . ASN   B 1 13  ? 23.017 -16.231 13.534 1.00 16.77 ? 19  ASN   C CB  1 
ATOM   1197 C  CG  . ASN   B 1 13  ? 23.852 -17.504 13.478 1.00 18.74 ? 19  ASN   C CG  1 
ATOM   1198 O  OD1 . ASN   B 1 13  ? 23.367 -18.579 13.047 1.00 19.30 ? 19  ASN   C OD1 1 
ATOM   1199 N  ND2 . ASN   B 1 13  ? 25.113 -17.399 13.913 1.00 17.59 ? 19  ASN   C ND2 1 
ATOM   1200 N  N   . ARG   B 1 14  ? 21.991 -13.634 15.563 1.00 16.98 ? 20  ARG   C N   1 
ATOM   1201 C  CA  . ARG   B 1 14  ? 21.251 -12.359 15.583 1.00 16.22 ? 20  ARG   C CA  1 
ATOM   1202 C  C   . ARG   B 1 14  ? 21.129 -11.798 14.149 1.00 16.60 ? 20  ARG   C C   1 
ATOM   1203 O  O   . ARG   B 1 14  ? 20.081 -11.236 13.795 1.00 16.93 ? 20  ARG   C O   1 
ATOM   1204 C  CB  . ARG   B 1 14  ? 21.983 -11.333 16.472 1.00 17.19 ? 20  ARG   C CB  1 
ATOM   1205 C  CG  . ARG   B 1 14  ? 21.214 -10.013 16.734 1.00 18.65 ? 20  ARG   C CG  1 
ATOM   1206 C  CD  . ARG   B 1 14  ? 22.122 -9.019  17.459 1.00 19.66 ? 20  ARG   C CD  1 
ATOM   1207 N  NE  . ARG   B 1 14  ? 21.473 -7.783  17.942 1.00 19.93 ? 20  ARG   C NE  1 
ATOM   1208 C  CZ  . ARG   B 1 14  ? 21.346 -6.670  17.217 1.00 20.81 ? 20  ARG   C CZ  1 
ATOM   1209 N  NH1 . ARG   B 1 14  ? 21.709 -6.657  15.937 1.00 19.45 ? 20  ARG   C NH1 1 
ATOM   1210 N  NH2 . ARG   B 1 14  ? 20.841 -5.563  17.764 1.00 20.00 ? 20  ARG   C NH2 1 
ATOM   1211 N  N   . HIS   B 1 15  ? 22.184 -12.003 13.295 1.00 16.72 ? 21  HIS   C N   1 
ATOM   1212 C  CA  . HIS   B 1 15  ? 22.104 -11.454 11.918 1.00 16.85 ? 21  HIS   C CA  1 
ATOM   1213 C  C   . HIS   B 1 15  ? 21.088 -12.191 11.016 1.00 17.86 ? 21  HIS   C C   1 
ATOM   1214 O  O   . HIS   B 1 15  ? 20.765 -11.689 9.935  1.00 19.23 ? 21  HIS   C O   1 
ATOM   1215 C  CB  . HIS   B 1 15  ? 23.488 -11.362 11.239 1.00 17.30 ? 21  HIS   C CB  1 
ATOM   1216 C  CG  . HIS   B 1 15  ? 24.051 -12.673 10.798 1.00 18.56 ? 21  HIS   C CG  1 
ATOM   1217 N  ND1 . HIS   B 1 15  ? 24.817 -13.462 11.654 1.00 20.20 ? 21  HIS   C ND1 1 
ATOM   1218 C  CD2 . HIS   B 1 15  ? 24.014 -13.260 9.576  1.00 20.17 ? 21  HIS   C CD2 1 
ATOM   1219 C  CE1 . HIS   B 1 15  ? 25.182 -14.520 10.939 1.00 21.29 ? 21  HIS   C CE1 1 
ATOM   1220 N  NE2 . HIS   B 1 15  ? 24.730 -14.441 9.682  1.00 21.60 ? 21  HIS   C NE2 1 
ATOM   1221 N  N   . LEU   B 1 16  ? 20.573 -13.354 11.466 1.00 17.13 ? 22  LEU   C N   1 
ATOM   1222 C  CA  . LEU   B 1 16  ? 19.549 -14.085 10.706 1.00 17.95 ? 22  LEU   C CA  1 
ATOM   1223 C  C   . LEU   B 1 16  ? 18.157 -14.055 11.376 1.00 18.67 ? 22  LEU   C C   1 
ATOM   1224 O  O   . LEU   B 1 16  ? 17.254 -14.764 10.933 1.00 19.31 ? 22  LEU   C O   1 
ATOM   1225 C  CB  . LEU   B 1 16  ? 20.003 -15.525 10.463 1.00 18.85 ? 22  LEU   C CB  1 
ATOM   1226 C  CG  . LEU   B 1 16  ? 21.287 -15.675 9.652  1.00 20.36 ? 22  LEU   C CG  1 
ATOM   1227 C  CD1 . LEU   B 1 16  ? 21.702 -17.151 9.562  1.00 21.24 ? 22  LEU   C CD1 1 
ATOM   1228 C  CD2 . LEU   B 1 16  ? 21.132 -15.053 8.242  1.00 21.06 ? 22  LEU   C CD2 1 
ATOM   1229 N  N   . ALA   B 1 17  ? 17.991 -13.290 12.473 1.00 18.66 ? 23  ALA   C N   1 
ATOM   1230 C  CA  . ALA   B 1 17  ? 16.716 -13.242 13.194 1.00 19.54 ? 23  ALA   C CA  1 
ATOM   1231 C  C   . ALA   B 1 17  ? 15.582 -12.700 12.320 1.00 20.49 ? 23  ALA   C C   1 
ATOM   1232 O  O   . ALA   B 1 17  ? 15.816 -11.789 11.517 1.00 20.75 ? 23  ALA   C O   1 
ATOM   1233 C  CB  . ALA   B 1 17  ? 16.858 -12.408 14.454 1.00 20.08 ? 23  ALA   C CB  1 
ATOM   1234 N  N   . THR   B 1 18  ? 14.378 -13.304 12.435 1.00 20.17 ? 24  THR   C N   1 
ATOM   1235 C  CA  . THR   B 1 18  ? 13.205 -12.873 11.651 1.00 20.80 ? 24  THR   C CA  1 
ATOM   1236 C  C   . THR   B 1 18  ? 12.403 -11.770 12.410 1.00 22.49 ? 24  THR   C C   1 
ATOM   1237 O  O   . THR   B 1 18  ? 12.663 -11.509 13.589 1.00 23.05 ? 24  THR   C O   1 
ATOM   1238 C  CB  . THR   B 1 18  ? 12.279 -14.106 11.386 1.00 21.68 ? 24  THR   C CB  1 
ATOM   1239 O  OG1 . THR   B 1 18  ? 11.754 -14.548 12.627 1.00 22.67 ? 24  THR   C OG1 1 
ATOM   1240 C  CG2 . THR   B 1 18  ? 13.003 -15.269 10.687 1.00 22.04 ? 24  THR   C CG2 1 
ATOM   1241 N  N   . HIS   B 1 19  ? 11.365 -11.165 11.760 1.00 23.07 ? 25  HIS   C N   1 
ATOM   1242 C  CA  . HIS   B 1 19  ? 10.499 -10.205 12.455 1.00 24.36 ? 25  HIS   C CA  1 
ATOM   1243 C  C   . HIS   B 1 19  ? 9.791  -10.938 13.614 1.00 23.25 ? 25  HIS   C C   1 
ATOM   1244 O  O   . HIS   B 1 19  ? 9.696  -10.365 14.692 1.00 24.43 ? 25  HIS   C O   1 
ATOM   1245 C  CB  . HIS   B 1 19  ? 9.449  -9.590  11.496 1.00 27.25 ? 25  HIS   C CB  1 
ATOM   1246 C  CG  . HIS   B 1 19  ? 8.300  -8.909  12.195 1.00 32.54 ? 25  HIS   C CG  1 
ATOM   1247 N  ND1 . HIS   B 1 19  ? 8.438  -7.652  12.756 1.00 35.49 ? 25  HIS   C ND1 1 
ATOM   1248 C  CD2 . HIS   B 1 19  ? 7.045  -9.358  12.435 1.00 34.86 ? 25  HIS   C CD2 1 
ATOM   1249 C  CE1 . HIS   B 1 19  ? 7.253  -7.351  13.273 1.00 36.67 ? 25  HIS   C CE1 1 
ATOM   1250 N  NE2 . HIS   B 1 19  ? 6.382  -8.353  13.115 1.00 36.34 ? 25  HIS   C NE2 1 
ATOM   1251 N  N   . ASN   B 1 20  ? 9.358  -12.195 13.417 1.00 22.25 ? 26  ASN   C N   1 
ATOM   1252 C  CA  . ASN   B 1 20  ? 8.702  -12.940 14.502 1.00 22.95 ? 26  ASN   C CA  1 
ATOM   1253 C  C   . ASN   B 1 20  ? 9.647  -13.115 15.711 1.00 22.02 ? 26  ASN   C C   1 
ATOM   1254 O  O   . ASN   B 1 20  ? 9.208  -13.003 16.860 1.00 22.22 ? 26  ASN   C O   1 
ATOM   1255 C  CB  . ASN   B 1 20  ? 8.138  -14.287 14.041 1.00 25.79 ? 26  ASN   C CB  1 
ATOM   1256 C  CG  . ASN   B 1 20  ? 7.290  -14.924 15.125 1.00 32.34 ? 26  ASN   C CG  1 
ATOM   1257 O  OD1 . ASN   B 1 20  ? 6.179  -14.472 15.419 1.00 34.23 ? 26  ASN   C OD1 1 
ATOM   1258 N  ND2 . ASN   B 1 20  ? 7.812  -15.961 15.777 1.00 33.77 ? 26  ASN   C ND2 1 
ATOM   1259 N  N   . ASP   B 1 21  ? 10.966 -13.344 15.456 1.00 20.92 ? 27  ASP   C N   1 
ATOM   1260 C  CA  . ASP   B 1 21  ? 11.931 -13.441 16.554 1.00 20.40 ? 27  ASP   C CA  1 
ATOM   1261 C  C   . ASP   B 1 21  ? 11.982 -12.109 17.340 1.00 20.80 ? 27  ASP   C C   1 
ATOM   1262 O  O   . ASP   B 1 21  ? 11.942 -12.128 18.566 1.00 21.00 ? 27  ASP   C O   1 
ATOM   1263 C  CB  . ASP   B 1 21  ? 13.347 -13.761 16.022 1.00 20.26 ? 27  ASP   C CB  1 
ATOM   1264 C  CG  . ASP   B 1 21  ? 13.512 -15.174 15.528 1.00 20.28 ? 27  ASP   C CG  1 
ATOM   1265 O  OD1 . ASP   B 1 21  ? 12.948 -16.088 16.161 1.00 19.80 ? 27  ASP   C OD1 1 
ATOM   1266 O  OD2 . ASP   B 1 21  ? 14.218 -15.365 14.517 1.00 21.01 ? 27  ASP   C OD2 1 
ATOM   1267 N  N   . TRP   B 1 22  ? 12.086 -10.966 16.638 1.00 20.75 ? 28  TRP   C N   1 
ATOM   1268 C  CA  . TRP   B 1 22  ? 12.120 -9.664  17.312 1.00 20.93 ? 28  TRP   C CA  1 
ATOM   1269 C  C   . TRP   B 1 22  ? 10.794 -9.342  18.043 1.00 20.58 ? 28  TRP   C C   1 
ATOM   1270 O  O   . TRP   B 1 22  ? 10.812 -8.691  19.088 1.00 20.16 ? 28  TRP   C O   1 
ATOM   1271 C  CB  . TRP   B 1 22  ? 12.482 -8.548  16.314 1.00 21.01 ? 28  TRP   C CB  1 
ATOM   1272 C  CG  . TRP   B 1 22  ? 13.948 -8.504  16.000 1.00 21.27 ? 28  TRP   C CG  1 
ATOM   1273 C  CD1 . TRP   B 1 22  ? 14.578 -9.055  14.919 1.00 22.20 ? 28  TRP   C CD1 1 
ATOM   1274 C  CD2 . TRP   B 1 22  ? 14.979 -7.939  16.822 1.00 20.92 ? 28  TRP   C CD2 1 
ATOM   1275 N  NE1 . TRP   B 1 22  ? 15.933 -8.801  14.983 1.00 22.51 ? 28  TRP   C NE1 1 
ATOM   1276 C  CE2 . TRP   B 1 22  ? 16.207 -8.146  16.156 1.00 22.28 ? 28  TRP   C CE2 1 
ATOM   1277 C  CE3 . TRP   B 1 22  ? 14.982 -7.265  18.047 1.00 21.57 ? 28  TRP   C CE3 1 
ATOM   1278 C  CZ2 . TRP   B 1 22  ? 17.411 -7.673  16.655 1.00 22.87 ? 28  TRP   C CZ2 1 
ATOM   1279 C  CZ3 . TRP   B 1 22  ? 16.191 -6.811  18.554 1.00 23.24 ? 28  TRP   C CZ3 1 
ATOM   1280 C  CH2 . TRP   B 1 22  ? 17.385 -7.006  17.848 1.00 23.16 ? 28  TRP   C CH2 1 
ATOM   1281 N  N   . ALA   B 1 23  ? 9.647  -9.785  17.483 1.00 20.44 ? 29  ALA   C N   1 
ATOM   1282 C  CA  . ALA   B 1 23  ? 8.324  -9.548  18.107 1.00 21.51 ? 29  ALA   C CA  1 
ATOM   1283 C  C   . ALA   B 1 23  ? 8.099  -10.436 19.360 1.00 22.62 ? 29  ALA   C C   1 
ATOM   1284 O  O   . ALA   B 1 23  ? 7.154  -10.205 20.122 1.00 23.10 ? 29  ALA   C O   1 
ATOM   1285 C  CB  . ALA   B 1 23  ? 7.201  -9.786  17.099 1.00 21.79 ? 29  ALA   C CB  1 
ATOM   1286 N  N   . ASN   B 1 24  ? 8.941  -11.475 19.548 1.00 22.24 ? 30  ASN   C N   1 
ATOM   1287 C  CA  . ASN   B 1 24  ? 8.849  -12.361 20.707 1.00 22.23 ? 30  ASN   C CA  1 
ATOM   1288 C  C   . ASN   B 1 24  ? 10.234 -12.446 21.381 1.00 21.82 ? 30  ASN   C C   1 
ATOM   1289 O  O   . ASN   B 1 24  ? 10.658 -13.519 21.809 1.00 21.55 ? 30  ASN   C O   1 
ATOM   1290 C  CB  . ASN   B 1 24  ? 8.368  -13.737 20.242 1.00 23.28 ? 30  ASN   C CB  1 
ATOM   1291 C  CG  . ASN   B 1 24  ? 6.951  -13.707 19.718 1.00 25.90 ? 30  ASN   C CG  1 
ATOM   1292 O  OD1 . ASN   B 1 24  ? 5.991  -13.735 20.495 1.00 26.59 ? 30  ASN   C OD1 1 
ATOM   1293 N  ND2 . ASN   B 1 24  ? 6.794  -13.630 18.403 1.00 26.42 ? 30  ASN   C ND2 1 
ATOM   1294 N  N   . LEU   B 1 25  ? 10.955 -11.311 21.445 1.00 22.00 ? 31  LEU   C N   1 
ATOM   1295 C  CA  . LEU   B 1 25  ? 12.323 -11.256 21.963 1.00 21.35 ? 31  LEU   C CA  1 
ATOM   1296 C  C   . LEU   B 1 25  ? 12.450 -11.573 23.446 1.00 21.57 ? 31  LEU   C C   1 
ATOM   1297 O  O   . LEU   B 1 25  ? 11.706 -11.010 24.259 1.00 22.45 ? 31  LEU   C O   1 
ATOM   1298 C  CB  . LEU   B 1 25  ? 12.920 -9.866  21.677 1.00 20.48 ? 31  LEU   C CB  1 
ATOM   1299 C  CG  . LEU   B 1 25  ? 14.365 -9.676  22.083 1.00 20.94 ? 31  LEU   C CG  1 
ATOM   1300 C  CD1 . LEU   B 1 25  ? 15.270 -10.585 21.249 1.00 20.94 ? 31  LEU   C CD1 1 
ATOM   1301 C  CD2 . LEU   B 1 25  ? 14.796 -8.215  21.930 1.00 21.55 ? 31  LEU   C CD2 1 
ATOM   1302 N  N   . VAL   B 1 26  ? 13.418 -12.440 23.797 1.00 20.15 ? 32  VAL   C N   1 
ATOM   1303 C  CA  . VAL   B 1 26  ? 13.761 -12.736 25.185 1.00 20.58 ? 32  VAL   C CA  1 
ATOM   1304 C  C   . VAL   B 1 26  ? 15.102 -12.014 25.530 1.00 21.49 ? 32  VAL   C C   1 
ATOM   1305 O  O   . VAL   B 1 26  ? 15.188 -11.280 26.525 1.00 22.04 ? 32  VAL   C O   1 
ATOM   1306 C  CB  . VAL   B 1 26  ? 13.876 -14.260 25.432 1.00 21.66 ? 32  VAL   C CB  1 
ATOM   1307 C  CG1 . VAL   B 1 26  ? 14.507 -14.568 26.793 1.00 22.59 ? 32  VAL   C CG1 1 
ATOM   1308 C  CG2 . VAL   B 1 26  ? 12.517 -14.949 25.292 1.00 21.58 ? 32  VAL   C CG2 1 
ATOM   1309 N  N   . TRP   B 1 27  ? 16.141 -12.196 24.679 1.00 20.86 ? 33  TRP   C N   1 
ATOM   1310 C  CA  . TRP   B 1 27  ? 17.457 -11.603 24.936 1.00 21.01 ? 33  TRP   C CA  1 
ATOM   1311 C  C   . TRP   B 1 27  ? 18.259 -11.544 23.612 1.00 20.68 ? 33  TRP   C C   1 
ATOM   1312 O  O   . TRP   B 1 27  ? 18.094 -12.432 22.766 1.00 20.73 ? 33  TRP   C O   1 
ATOM   1313 C  CB  . TRP   B 1 27  ? 18.208 -12.491 25.959 1.00 21.40 ? 33  TRP   C CB  1 
ATOM   1314 C  CG  . TRP   B 1 27  ? 19.682 -12.206 26.137 1.00 21.93 ? 33  TRP   C CG  1 
ATOM   1315 C  CD1 . TRP   B 1 27  ? 20.244 -11.267 26.957 1.00 22.98 ? 33  TRP   C CD1 1 
ATOM   1316 C  CD2 . TRP   B 1 27  ? 20.781 -12.919 25.529 1.00 21.28 ? 33  TRP   C CD2 1 
ATOM   1317 N  NE1 . TRP   B 1 27  ? 21.627 -11.340 26.890 1.00 23.28 ? 33  TRP   C NE1 1 
ATOM   1318 C  CE2 . TRP   B 1 27  ? 21.979 -12.334 26.007 1.00 22.33 ? 33  TRP   C CE2 1 
ATOM   1319 C  CE3 . TRP   B 1 27  ? 20.866 -13.971 24.603 1.00 21.56 ? 33  TRP   C CE3 1 
ATOM   1320 C  CZ2 . TRP   B 1 27  ? 23.238 -12.807 25.633 1.00 22.37 ? 33  TRP   C CZ2 1 
ATOM   1321 C  CZ3 . TRP   B 1 27  ? 22.119 -14.444 24.249 1.00 22.66 ? 33  TRP   C CZ3 1 
ATOM   1322 C  CH2 . TRP   B 1 27  ? 23.280 -13.835 24.726 1.00 22.78 ? 33  TRP   C CH2 1 
ATOM   1323 N  N   . GLU   B 1 28  ? 19.104 -10.510 23.432 1.00 19.01 ? 34  GLU   C N   1 
ATOM   1324 C  CA  . GLU   B 1 28  ? 19.935 -10.408 22.236 1.00 19.25 ? 34  GLU   C CA  1 
ATOM   1325 C  C   . GLU   B 1 28  ? 21.255 -9.735  22.578 1.00 20.14 ? 34  GLU   C C   1 
ATOM   1326 O  O   . GLU   B 1 28  ? 21.283 -8.825  23.414 1.00 19.82 ? 34  GLU   C O   1 
ATOM   1327 C  CB  . GLU   B 1 28  ? 19.232 -9.658  21.086 1.00 20.37 ? 34  GLU   C CB  1 
ATOM   1328 C  CG  . GLU   B 1 28  ? 18.705 -8.270  21.452 1.00 22.01 ? 34  GLU   C CG  1 
ATOM   1329 C  CD  . GLU   B 1 28  ? 19.713 -7.137  21.357 1.00 23.63 ? 34  GLU   C CD  1 
ATOM   1330 O  OE1 . GLU   B 1 28  ? 19.513 -6.092  22.016 1.00 24.76 ? 34  GLU   C OE1 1 
ATOM   1331 O  OE2 . GLU   B 1 28  ? 20.707 -7.295  20.618 1.00 22.33 ? 34  GLU   C OE2 1 
ATOM   1332 N  N   . ASP   B 1 29  ? 22.345 -10.155 21.914 1.00 19.71 ? 35  ASP   C N   1 
ATOM   1333 C  CA  . ASP   B 1 29  ? 23.639 -9.522  22.139 1.00 19.97 ? 35  ASP   C CA  1 
ATOM   1334 C  C   . ASP   B 1 29  ? 24.397 -9.455  20.803 1.00 19.72 ? 35  ASP   C C   1 
ATOM   1335 O  O   . ASP   B 1 29  ? 24.828 -10.491 20.298 1.00 20.29 ? 35  ASP   C O   1 
ATOM   1336 C  CB  . ASP   B 1 29  ? 24.436 -10.330 23.174 1.00 21.61 ? 35  ASP   C CB  1 
ATOM   1337 C  CG  . ASP   B 1 29  ? 25.712 -9.639  23.634 1.00 27.15 ? 35  ASP   C CG  1 
ATOM   1338 O  OD1 . ASP   B 1 29  ? 26.324 -8.904  22.822 1.00 27.79 ? 35  ASP   C OD1 1 
ATOM   1339 O  OD2 . ASP   B 1 29  ? 26.104 -9.841  24.794 1.00 28.41 ? 35  ASP   C OD2 1 
ATOM   1340 N  N   . SER   B 1 30  ? 24.548 -8.246  20.230 1.00 19.50 ? 36  SER   C N   1 
ATOM   1341 C  CA  A SER   B 1 30  ? 25.251 -8.051  18.960 0.50 19.91 ? 36  SER   C CA  1 
ATOM   1342 C  CA  B SER   B 1 30  ? 25.245 -8.083  18.956 0.50 19.95 ? 36  SER   C CA  1 
ATOM   1343 C  C   . SER   B 1 30  ? 26.712 -8.498  19.041 1.00 19.71 ? 36  SER   C C   1 
ATOM   1344 O  O   . SER   B 1 30  ? 27.237 -9.071  18.064 1.00 19.74 ? 36  SER   C O   1 
ATOM   1345 C  CB  A SER   B 1 30  ? 25.190 -6.584  18.533 0.50 21.19 ? 36  SER   C CB  1 
ATOM   1346 C  CB  B SER   B 1 30  ? 25.134 -6.646  18.451 0.50 21.36 ? 36  SER   C CB  1 
ATOM   1347 O  OG  A SER   B 1 30  ? 25.989 -6.331  17.388 0.50 21.63 ? 36  SER   C OG  1 
ATOM   1348 O  OG  B SER   B 1 30  ? 25.550 -5.720  19.440 0.50 21.82 ? 36  SER   C OG  1 
ATOM   1349 N  N   . SER   B 1 31  ? 27.384 -8.232  20.194 1.00 19.54 ? 37  SER   C N   1 
ATOM   1350 C  CA  . SER   B 1 31  ? 28.803 -8.625  20.302 1.00 20.18 ? 37  SER   C CA  1 
ATOM   1351 C  C   . SER   B 1 31  ? 29.009 -10.144 20.234 1.00 18.62 ? 37  SER   C C   1 
ATOM   1352 O  O   . SER   B 1 31  ? 30.118 -10.584 19.920 1.00 19.97 ? 37  SER   C O   1 
ATOM   1353 C  CB  . SER   B 1 31  ? 29.448 -8.035  21.549 1.00 24.30 ? 37  SER   C CB  1 
ATOM   1354 O  OG  . SER   B 1 31  ? 28.995 -8.702  22.715 1.00 29.86 ? 37  SER   C OG  1 
ATOM   1355 N  N   . ARG   B 1 32  ? 27.943 -10.957 20.521 1.00 16.81 ? 38  ARG   C N   1 
ATOM   1356 C  CA  . ARG   B 1 32  ? 28.046 -12.427 20.464 1.00 17.94 ? 38  ARG   C CA  1 
ATOM   1357 C  C   . ARG   B 1 32  ? 27.385 -13.032 19.202 1.00 17.88 ? 38  ARG   C C   1 
ATOM   1358 O  O   . ARG   B 1 32  ? 27.443 -14.250 19.006 1.00 17.16 ? 38  ARG   C O   1 
ATOM   1359 C  CB  . ARG   B 1 32  ? 27.354 -13.057 21.714 1.00 20.27 ? 38  ARG   C CB  1 
ATOM   1360 C  CG  . ARG   B 1 32  ? 27.997 -12.673 23.034 1.00 23.03 ? 38  ARG   C CG  1 
ATOM   1361 C  CD  . ARG   B 1 32  ? 27.212 -13.267 24.210 1.00 23.42 ? 38  ARG   C CD  1 
ATOM   1362 N  NE  . ARG   B 1 32  ? 27.298 -14.731 24.259 1.00 21.93 ? 38  ARG   C NE  1 
ATOM   1363 C  CZ  . ARG   B 1 32  ? 27.263 -15.449 25.388 1.00 21.48 ? 38  ARG   C CZ  1 
ATOM   1364 N  NH1 . ARG   B 1 32  ? 27.126 -14.845 26.568 1.00 20.09 ? 38  ARG   C NH1 1 
ATOM   1365 N  NH2 . ARG   B 1 32  ? 27.402 -16.764 25.347 1.00 18.94 ? 38  ARG   C NH2 1 
ATOM   1366 N  N   . ASP   B 1 33  ? 26.678 -12.194 18.403 1.00 16.97 ? 39  ASP   C N   1 
ATOM   1367 C  CA  . ASP   B 1 33  ? 25.910 -12.653 17.252 1.00 16.56 ? 39  ASP   C CA  1 
ATOM   1368 C  C   . ASP   B 1 33  ? 24.818 -13.612 17.714 1.00 16.15 ? 39  ASP   C C   1 
ATOM   1369 O  O   . ASP   B 1 33  ? 24.506 -14.558 16.975 1.00 15.75 ? 39  ASP   C O   1 
ATOM   1370 C  CB  . ASP   B 1 33  ? 26.778 -13.277 16.122 1.00 17.00 ? 39  ASP   C CB  1 
ATOM   1371 C  CG  . ASP   B 1 33  ? 25.985 -13.619 14.863 1.00 19.14 ? 39  ASP   C CG  1 
ATOM   1372 O  OD1 . ASP   B 1 33  ? 25.090 -12.829 14.498 1.00 20.55 ? 39  ASP   C OD1 1 
ATOM   1373 O  OD2 . ASP   B 1 33  ? 26.272 -14.673 14.238 1.00 16.89 ? 39  ASP   C OD2 1 
ATOM   1374 N  N   . LEU   B 1 34  ? 24.213 -13.366 18.925 1.00 15.47 ? 40  LEU   C N   1 
ATOM   1375 C  CA  . LEU   B 1 34  ? 23.112 -14.242 19.391 1.00 14.21 ? 40  LEU   C CA  1 
ATOM   1376 C  C   . LEU   B 1 34  ? 21.789 -13.504 19.632 1.00 15.23 ? 40  LEU   C C   1 
ATOM   1377 O  O   . LEU   B 1 34  ? 21.789 -12.363 20.101 1.00 16.37 ? 40  LEU   C O   1 
ATOM   1378 C  CB  . LEU   B 1 34  ? 23.471 -14.980 20.682 1.00 14.06 ? 40  LEU   C CB  1 
ATOM   1379 C  CG  . LEU   B 1 34  ? 24.552 -16.084 20.597 1.00 15.98 ? 40  LEU   C CG  1 
ATOM   1380 C  CD1 . LEU   B 1 34  ? 24.775 -16.686 21.986 1.00 15.80 ? 40  LEU   C CD1 1 
ATOM   1381 C  CD2 . LEU   B 1 34  ? 24.158 -17.196 19.622 1.00 16.40 ? 40  LEU   C CD2 1 
ATOM   1382 N  N   . LEU   B 1 35  ? 20.670 -14.219 19.409 1.00 14.89 ? 41  LEU   C N   1 
ATOM   1383 C  CA  . LEU   B 1 35  ? 19.348 -13.703 19.685 1.00 16.05 ? 41  LEU   C CA  1 
ATOM   1384 C  C   . LEU   B 1 35  ? 18.500 -14.912 20.151 1.00 16.52 ? 41  LEU   C C   1 
ATOM   1385 O  O   . LEU   B 1 35  ? 18.595 -15.996 19.568 1.00 18.17 ? 41  LEU   C O   1 
ATOM   1386 C  CB  . LEU   B 1 35  ? 18.717 -13.025 18.437 1.00 16.22 ? 41  LEU   C CB  1 
ATOM   1387 C  CG  . LEU   B 1 35  ? 17.330 -12.376 18.704 1.00 17.93 ? 41  LEU   C CG  1 
ATOM   1388 C  CD1 . LEU   B 1 35  ? 17.175 -11.072 17.939 1.00 20.02 ? 41  LEU   C CD1 1 
ATOM   1389 C  CD2 . LEU   B 1 35  ? 16.179 -13.348 18.372 1.00 18.11 ? 41  LEU   C CD2 1 
ATOM   1390 N  N   . VAL   B 1 36  ? 17.724 -14.736 21.219 1.00 16.10 ? 42  VAL   C N   1 
ATOM   1391 C  CA  . VAL   B 1 36  ? 16.837 -15.774 21.732 1.00 16.32 ? 42  VAL   C CA  1 
ATOM   1392 C  C   . VAL   B 1 36  ? 15.405 -15.233 21.726 1.00 17.39 ? 42  VAL   C C   1 
ATOM   1393 O  O   . VAL   B 1 36  ? 15.167 -14.150 22.276 1.00 17.96 ? 42  VAL   C O   1 
ATOM   1394 C  CB  . VAL   B 1 36  ? 17.233 -16.196 23.168 1.00 17.48 ? 42  VAL   C CB  1 
ATOM   1395 C  CG1 . VAL   B 1 36  ? 16.234 -17.214 23.722 1.00 17.42 ? 42  VAL   C CG1 1 
ATOM   1396 C  CG2 . VAL   B 1 36  ? 18.667 -16.763 23.197 1.00 17.54 ? 42  VAL   C CG2 1 
ATOM   1397 N  N   . SER   B 1 37  ? 14.453 -15.999 21.151 1.00 17.33 ? 43  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 37  ? 13.036 -15.617 21.145 1.00 17.94 ? 43  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 37  ? 12.207 -16.724 21.835 1.00 19.17 ? 43  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 37  ? 12.714 -17.836 22.053 1.00 18.69 ? 43  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 37  ? 12.531 -15.409 19.717 1.00 18.52 ? 43  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 37  ? 12.692 -16.571 18.918 1.00 20.01 ? 43  SER   C OG  1 
ATOM   1403 N  N   . SER   B 1 38  ? 10.956 -16.412 22.217 1.00 19.79 ? 44  SER   C N   1 
ATOM   1404 C  CA  . SER   B 1 38  ? 10.101 -17.394 22.875 1.00 21.13 ? 44  SER   C CA  1 
ATOM   1405 C  C   . SER   B 1 38  ? 9.279  -18.203 21.849 1.00 22.82 ? 44  SER   C C   1 
ATOM   1406 O  O   . SER   B 1 38  ? 8.975  -17.723 20.751 1.00 23.02 ? 44  SER   C O   1 
ATOM   1407 C  CB  . SER   B 1 38  ? 9.175  -16.696 23.872 1.00 23.85 ? 44  SER   C CB  1 
ATOM   1408 O  OG  . SER   B 1 38  ? 8.364  -15.762 23.183 1.00 26.45 ? 44  SER   C OG  1 
ATOM   1409 N  N   . THR   B 1 39  ? 8.883  -19.430 22.221 1.00 22.78 ? 45  THR   C N   1 
ATOM   1410 C  CA  . THR   B 1 39  ? 8.128  -20.302 21.323 1.00 23.41 ? 45  THR   C CA  1 
ATOM   1411 C  C   . THR   B 1 39  ? 6.858  -20.826 22.013 1.00 26.19 ? 45  THR   C C   1 
ATOM   1412 O  O   . THR   B 1 39  ? 6.786  -20.856 23.238 1.00 26.04 ? 45  THR   C O   1 
ATOM   1413 C  CB  . THR   B 1 39  ? 8.992  -21.512 20.871 1.00 24.01 ? 45  THR   C CB  1 
ATOM   1414 O  OG1 . THR   B 1 39  ? 9.309  -22.333 22.004 1.00 24.35 ? 45  THR   C OG1 1 
ATOM   1415 C  CG2 . THR   B 1 39  ? 10.272 -21.086 20.138 1.00 24.26 ? 45  THR   C CG2 1 
ATOM   1416 N  N   . THR   B 1 40  ? 5.877  -21.265 21.216 1.00 28.12 ? 46  THR   C N   1 
ATOM   1417 C  CA  . THR   B 1 40  ? 4.642  -21.812 21.785 1.00 30.31 ? 46  THR   C CA  1 
ATOM   1418 C  C   . THR   B 1 40  ? 4.854  -23.281 22.122 1.00 30.22 ? 46  THR   C C   1 
ATOM   1419 O  O   . THR   B 1 40  ? 4.463  -23.725 23.198 1.00 31.57 ? 46  THR   C O   1 
ATOM   1420 C  CB  . THR   B 1 40  ? 3.449  -21.520 20.860 1.00 34.14 ? 46  THR   C CB  1 
ATOM   1421 O  OG1 . THR   B 1 40  ? 3.690  -22.163 19.609 1.00 37.08 ? 46  THR   C OG1 1 
ATOM   1422 C  CG2 . THR   B 1 40  ? 3.267  -20.021 20.604 1.00 34.76 ? 46  THR   C CG2 1 
ATOM   1423 N  N   . ALA   B 1 41  ? 5.487  -24.039 21.215 1.00 28.60 ? 47  ALA   C N   1 
ATOM   1424 C  CA  . ALA   B 1 41  ? 5.768  -25.451 21.469 1.00 28.05 ? 47  ALA   C CA  1 
ATOM   1425 C  C   . ALA   B 1 41  ? 7.109  -25.635 22.203 1.00 26.99 ? 47  ALA   C C   1 
ATOM   1426 O  O   . ALA   B 1 41  ? 8.027  -24.803 22.070 1.00 26.09 ? 47  ALA   C O   1 
ATOM   1427 C  CB  . ALA   B 1 41  ? 5.797  -26.222 20.152 1.00 28.39 ? 47  ALA   C CB  1 
ATOM   1428 N  N   . GLN   B 1 42  ? 7.249  -26.758 22.917 1.00 26.53 ? 48  GLN   C N   1 
ATOM   1429 C  CA  . GLN   B 1 42  ? 8.487  -27.074 23.626 1.00 27.19 ? 48  GLN   C CA  1 
ATOM   1430 C  C   . GLN   B 1 42  ? 9.517  -27.713 22.670 1.00 26.65 ? 48  GLN   C C   1 
ATOM   1431 O  O   . GLN   B 1 42  ? 9.137  -28.523 21.817 1.00 27.18 ? 48  GLN   C O   1 
ATOM   1432 C  CB  . GLN   B 1 42  ? 8.193  -28.032 24.800 1.00 30.63 ? 48  GLN   C CB  1 
ATOM   1433 C  CG  . GLN   B 1 42  ? 7.702  -27.317 26.054 1.00 38.12 ? 48  GLN   C CG  1 
ATOM   1434 C  CD  . GLN   B 1 42  ? 7.675  -28.284 27.218 1.00 47.88 ? 48  GLN   C CD  1 
ATOM   1435 O  OE1 . GLN   B 1 42  ? 6.918  -29.267 27.234 1.00 50.94 ? 48  GLN   C OE1 1 
ATOM   1436 N  NE2 . GLN   B 1 42  ? 8.531  -28.052 28.205 1.00 49.31 ? 48  GLN   C NE2 1 
ATOM   1437 N  N   . GLY   B 1 43  ? 10.791 -27.346 22.825 1.00 24.61 ? 49  GLY   C N   1 
ATOM   1438 C  CA  . GLY   B 1 43  ? 11.879 -27.900 22.030 1.00 23.65 ? 49  GLY   C CA  1 
ATOM   1439 C  C   . GLY   B 1 43  ? 12.510 -29.134 22.666 1.00 23.16 ? 49  GLY   C C   1 
ATOM   1440 O  O   . GLY   B 1 43  ? 12.278 -29.421 23.852 1.00 23.89 ? 49  GLY   C O   1 
ATOM   1441 N  N   . CYS   B 1 44  ? 13.290 -29.881 21.891 1.00 21.84 ? 50  CYS   C N   1 
ATOM   1442 C  CA  . CYS   B 1 44  ? 13.860 -31.129 22.403 1.00 22.94 ? 50  CYS   C CA  1 
ATOM   1443 C  C   . CYS   B 1 44  ? 15.375 -31.144 22.511 1.00 22.63 ? 50  CYS   C C   1 
ATOM   1444 O  O   . CYS   B 1 44  ? 15.921 -32.175 22.895 1.00 23.38 ? 50  CYS   C O   1 
ATOM   1445 C  CB  . CYS   B 1 44  ? 13.350 -32.302 21.573 1.00 24.58 ? 50  CYS   C CB  1 
ATOM   1446 S  SG  . CYS   B 1 44  ? 11.535 -32.407 21.542 1.00 30.77 ? 50  CYS   C SG  1 
ATOM   1447 N  N   . ASP   B 1 45  ? 16.055 -30.039 22.171 1.00 20.68 ? 51  ASP   C N   1 
ATOM   1448 C  CA  . ASP   B 1 45  ? 17.504 -29.983 22.301 1.00 19.93 ? 51  ASP   C CA  1 
ATOM   1449 C  C   . ASP   B 1 45  ? 17.892 -29.802 23.780 1.00 20.03 ? 51  ASP   C C   1 
ATOM   1450 O  O   . ASP   B 1 45  ? 17.163 -29.169 24.560 1.00 20.26 ? 51  ASP   C O   1 
ATOM   1451 C  CB  . ASP   B 1 45  ? 18.084 -28.812 21.475 1.00 20.92 ? 51  ASP   C CB  1 
ATOM   1452 C  CG  . ASP   B 1 45  ? 17.948 -29.002 19.970 1.00 25.68 ? 51  ASP   C CG  1 
ATOM   1453 O  OD1 . ASP   B 1 45  ? 18.027 -30.163 19.507 1.00 25.88 ? 51  ASP   C OD1 1 
ATOM   1454 O  OD2 . ASP   B 1 45  ? 17.767 -27.980 19.252 1.00 25.76 ? 51  ASP   C OD2 1 
ATOM   1455 N  N   . THR   B 1 46  ? 19.042 -30.373 24.154 1.00 19.10 ? 52  THR   C N   1 
ATOM   1456 C  CA  . THR   B 1 46  ? 19.598 -30.220 25.489 1.00 19.35 ? 52  THR   C CA  1 
ATOM   1457 C  C   . THR   B 1 46  ? 20.899 -29.411 25.338 1.00 18.56 ? 52  THR   C C   1 
ATOM   1458 O  O   . THR   B 1 46  ? 21.715 -29.744 24.481 1.00 17.61 ? 52  THR   C O   1 
ATOM   1459 C  CB  . THR   B 1 46  ? 19.952 -31.585 26.068 1.00 21.94 ? 52  THR   C CB  1 
ATOM   1460 O  OG1 . THR   B 1 46  ? 18.757 -32.346 26.270 1.00 23.75 ? 52  THR   C OG1 1 
ATOM   1461 C  CG2 . THR   B 1 46  ? 20.731 -31.465 27.383 1.00 23.42 ? 52  THR   C CG2 1 
ATOM   1462 N  N   . ILE   B 1 47  ? 21.109 -28.406 26.190 1.00 17.45 ? 53  ILE   C N   1 
ATOM   1463 C  CA  . ILE   B 1 47  ? 22.335 -27.601 26.138 1.00 17.16 ? 53  ILE   C CA  1 
ATOM   1464 C  C   . ILE   B 1 47  ? 23.427 -28.294 26.947 1.00 17.01 ? 53  ILE   C C   1 
ATOM   1465 O  O   . ILE   B 1 47  ? 23.173 -28.748 28.076 1.00 17.54 ? 53  ILE   C O   1 
ATOM   1466 C  CB  . ILE   B 1 47  ? 22.113 -26.180 26.709 1.00 17.12 ? 53  ILE   C CB  1 
ATOM   1467 C  CG1 . ILE   B 1 47  ? 20.903 -25.467 26.063 1.00 18.02 ? 53  ILE   C CG1 1 
ATOM   1468 C  CG2 . ILE   B 1 47  ? 23.381 -25.326 26.555 1.00 17.91 ? 53  ILE   C CG2 1 
ATOM   1469 C  CD1 . ILE   B 1 47  ? 20.997 -25.378 24.507 1.00 19.32 ? 53  ILE   C CD1 1 
ATOM   1470 N  N   . ALA   B 1 48  ? 24.655 -28.321 26.412 1.00 17.12 ? 54  ALA   C N   1 
ATOM   1471 C  CA  . ALA   B 1 48  ? 25.768 -28.904 27.143 1.00 16.56 ? 54  ALA   C CA  1 
ATOM   1472 C  C   . ALA   B 1 48  ? 26.139 -27.994 28.316 1.00 16.70 ? 54  ALA   C C   1 
ATOM   1473 O  O   . ALA   B 1 48  ? 26.117 -26.775 28.158 1.00 18.08 ? 54  ALA   C O   1 
ATOM   1474 C  CB  . ALA   B 1 48  ? 26.970 -29.022 26.219 1.00 16.08 ? 54  ALA   C CB  1 
ATOM   1475 N  N   . ARG   B 1 49  ? 26.512 -28.577 29.471 1.00 15.67 ? 55  ARG   C N   1 
ATOM   1476 C  CA  . ARG   B 1 49  ? 26.978 -27.799 30.598 1.00 16.24 ? 55  ARG   C CA  1 
ATOM   1477 C  C   . ARG   B 1 49  ? 28.316 -28.475 30.981 1.00 16.51 ? 55  ARG   C C   1 
ATOM   1478 O  O   . ARG   B 1 49  ? 28.333 -29.491 31.690 1.00 17.01 ? 55  ARG   C O   1 
ATOM   1479 C  CB  . ARG   B 1 49  ? 25.954 -27.848 31.730 1.00 16.32 ? 55  ARG   C CB  1 
ATOM   1480 C  CG  . ARG   B 1 49  ? 24.576 -27.294 31.334 1.00 17.18 ? 55  ARG   C CG  1 
ATOM   1481 C  CD  . ARG   B 1 49  ? 24.559 -25.801 31.009 1.00 18.33 ? 55  ARG   C CD  1 
ATOM   1482 N  NE  . ARG   B 1 49  ? 23.204 -25.364 30.645 1.00 18.29 ? 55  ARG   C NE  1 
ATOM   1483 C  CZ  . ARG   B 1 49  ? 22.934 -24.263 29.947 1.00 21.59 ? 55  ARG   C CZ  1 
ATOM   1484 N  NH1 . ARG   B 1 49  ? 23.917 -23.450 29.564 1.00 18.84 ? 55  ARG   C NH1 1 
ATOM   1485 N  NH2 . ARG   B 1 49  ? 21.683 -23.961 29.635 1.00 21.15 ? 55  ARG   C NH2 1 
ATOM   1486 N  N   . CYS   B 1 50  ? 29.415 -27.953 30.426 1.00 16.51 ? 56  CYS   C N   1 
ATOM   1487 C  CA  . CYS   B 1 50  ? 30.723 -28.608 30.499 1.00 16.23 ? 56  CYS   C CA  1 
ATOM   1488 C  C   . CYS   B 1 50  ? 31.826 -27.642 29.984 1.00 17.68 ? 56  CYS   C C   1 
ATOM   1489 O  O   . CYS   B 1 50  ? 31.523 -26.542 29.487 1.00 16.81 ? 56  CYS   C O   1 
ATOM   1490 C  CB  . CYS   B 1 50  ? 30.655 -29.814 29.568 1.00 17.39 ? 56  CYS   C CB  1 
ATOM   1491 S  SG  . CYS   B 1 50  ? 30.487 -29.319 27.829 1.00 18.88 ? 56  CYS   C SG  1 
ATOM   1492 N  N   . ASP   B 1 51  ? 33.086 -28.139 29.975 1.00 17.32 ? 57  ASP   C N   1 
ATOM   1493 C  CA  . ASP   B 1 51  ? 34.192 -27.377 29.420 1.00 18.11 ? 57  ASP   C CA  1 
ATOM   1494 C  C   . ASP   B 1 51  ? 34.857 -28.212 28.278 1.00 18.37 ? 57  ASP   C C   1 
ATOM   1495 O  O   . ASP   B 1 51  ? 36.064 -28.131 28.082 1.00 19.91 ? 57  ASP   C O   1 
ATOM   1496 C  CB  . ASP   B 1 51  ? 35.232 -27.032 30.495 1.00 20.92 ? 57  ASP   C CB  1 
ATOM   1497 C  CG  . ASP   B 1 51  ? 35.820 -28.219 31.218 1.00 24.49 ? 57  ASP   C CG  1 
ATOM   1498 O  OD1 . ASP   B 1 51  ? 35.481 -29.374 30.853 1.00 24.01 ? 57  ASP   C OD1 1 
ATOM   1499 O  OD2 . ASP   B 1 51  ? 36.655 -27.999 32.125 1.00 29.82 ? 57  ASP   C OD2 1 
ATOM   1500 N  N   . CYS   B 1 52  ? 34.073 -29.010 27.530 1.00 17.42 ? 58  CYS   C N   1 
ATOM   1501 C  CA  . CYS   B 1 52  ? 34.613 -29.822 26.430 1.00 15.89 ? 58  CYS   C CA  1 
ATOM   1502 C  C   . CYS   B 1 52  ? 35.315 -28.960 25.402 1.00 16.06 ? 58  CYS   C C   1 
ATOM   1503 O  O   . CYS   B 1 52  ? 34.870 -27.839 25.128 1.00 16.60 ? 58  CYS   C O   1 
ATOM   1504 C  CB  . CYS   B 1 52  ? 33.513 -30.639 25.745 1.00 16.13 ? 58  CYS   C CB  1 
ATOM   1505 S  SG  . CYS   B 1 52  ? 33.000 -32.113 26.649 1.00 18.13 ? 58  CYS   C SG  1 
ATOM   1506 N  N   . GLN   B 1 53  ? 36.362 -29.522 24.793 1.00 14.91 ? 59  GLN   C N   1 
ATOM   1507 C  CA  . GLN   B 1 53  ? 37.023 -28.859 23.676 1.00 16.05 ? 59  GLN   C CA  1 
ATOM   1508 C  C   . GLN   B 1 53  ? 37.058 -29.752 22.439 1.00 16.33 ? 59  GLN   C C   1 
ATOM   1509 O  O   . GLN   B 1 53  ? 37.800 -29.453 21.511 1.00 15.96 ? 59  GLN   C O   1 
ATOM   1510 C  CB  . GLN   B 1 53  ? 38.438 -28.371 24.002 1.00 17.83 ? 59  GLN   C CB  1 
ATOM   1511 C  CG  . GLN   B 1 53  ? 38.437 -27.141 24.902 1.00 19.94 ? 59  GLN   C CG  1 
ATOM   1512 C  CD  . GLN   B 1 53  ? 39.835 -26.614 25.084 1.00 24.17 ? 59  GLN   C CD  1 
ATOM   1513 O  OE1 . GLN   B 1 53  ? 40.405 -26.684 26.189 1.00 25.88 ? 59  GLN   C OE1 1 
ATOM   1514 N  NE2 . GLN   B 1 53  ? 40.418 -26.081 24.011 1.00 20.92 ? 59  GLN   C NE2 1 
ATOM   1515 N  N   . THR   B 1 54  ? 36.264 -30.846 22.410 1.00 16.20 ? 60  THR   C N   1 
ATOM   1516 C  CA  . THR   B 1 54  ? 36.121 -31.715 21.243 1.00 17.48 ? 60  THR   C CA  1 
ATOM   1517 C  C   . THR   B 1 54  ? 34.642 -31.988 21.034 1.00 17.35 ? 60  THR   C C   1 
ATOM   1518 O  O   . THR   B 1 54  ? 33.886 -32.077 22.008 1.00 17.49 ? 60  THR   C O   1 
ATOM   1519 C  CB  . THR   B 1 54  ? 36.930 -33.017 21.322 1.00 20.62 ? 60  THR   C CB  1 
ATOM   1520 O  OG1 . THR   B 1 54  ? 36.367 -33.860 22.329 1.00 21.32 ? 60  THR   C OG1 1 
ATOM   1521 C  CG2 . THR   B 1 54  ? 38.408 -32.767 21.597 1.00 21.75 ? 60  THR   C CG2 1 
ATOM   1522 N  N   . GLY   B 1 55  ? 34.241 -32.056 19.766 1.00 16.73 ? 61  GLY   C N   1 
ATOM   1523 C  CA  . GLY   B 1 55  ? 32.847 -32.286 19.420 1.00 17.00 ? 61  GLY   C CA  1 
ATOM   1524 C  C   . GLY   B 1 55  ? 32.690 -32.535 17.937 1.00 16.83 ? 61  GLY   C C   1 
ATOM   1525 O  O   . GLY   B 1 55  ? 33.676 -32.850 17.250 1.00 16.33 ? 61  GLY   C O   1 
ATOM   1526 N  N   . VAL   B 1 56  ? 31.459 -32.385 17.438 1.00 15.26 ? 62  VAL   C N   1 
ATOM   1527 C  CA  . VAL   B 1 56  ? 31.156 -32.589 16.021 1.00 14.63 ? 62  VAL   C CA  1 
ATOM   1528 C  C   . VAL   B 1 56  ? 30.242 -31.418 15.563 1.00 14.82 ? 62  VAL   C C   1 
ATOM   1529 O  O   . VAL   B 1 56  ? 29.319 -31.056 16.306 1.00 16.10 ? 62  VAL   C O   1 
ATOM   1530 C  CB  . VAL   B 1 56  ? 30.417 -33.947 15.870 1.00 15.83 ? 62  VAL   C CB  1 
ATOM   1531 C  CG1 . VAL   B 1 56  ? 29.873 -34.133 14.454 1.00 16.40 ? 62  VAL   C CG1 1 
ATOM   1532 C  CG2 . VAL   B 1 56  ? 31.331 -35.123 16.261 1.00 16.65 ? 62  VAL   C CG2 1 
ATOM   1533 N  N   . TYR   B 1 57  ? 30.484 -30.835 14.366 1.00 14.56 ? 63  TYR   C N   1 
ATOM   1534 C  CA  . TYR   B 1 57  ? 29.593 -29.745 13.906 1.00 15.33 ? 63  TYR   C CA  1 
ATOM   1535 C  C   . TYR   B 1 57  ? 29.011 -30.067 12.539 1.00 15.49 ? 63  TYR   C C   1 
ATOM   1536 O  O   . TYR   B 1 57  ? 29.648 -30.789 11.764 1.00 16.04 ? 63  TYR   C O   1 
ATOM   1537 C  CB  . TYR   B 1 57  ? 30.287 -28.364 13.872 1.00 16.69 ? 63  TYR   C CB  1 
ATOM   1538 C  CG  . TYR   B 1 57  ? 31.164 -28.082 12.665 1.00 17.10 ? 63  TYR   C CG  1 
ATOM   1539 C  CD1 . TYR   B 1 57  ? 32.440 -28.621 12.565 1.00 17.43 ? 63  TYR   C CD1 1 
ATOM   1540 C  CD2 . TYR   B 1 57  ? 30.728 -27.237 11.642 1.00 17.09 ? 63  TYR   C CD2 1 
ATOM   1541 C  CE1 . TYR   B 1 57  ? 33.277 -28.307 11.486 1.00 18.09 ? 63  TYR   C CE1 1 
ATOM   1542 C  CE2 . TYR   B 1 57  ? 31.550 -26.920 10.559 1.00 17.39 ? 63  TYR   C CE2 1 
ATOM   1543 C  CZ  . TYR   B 1 57  ? 32.812 -27.488 10.464 1.00 18.75 ? 63  TYR   C CZ  1 
ATOM   1544 O  OH  . TYR   B 1 57  ? 33.619 -27.127 9.402  1.00 20.16 ? 63  TYR   C OH  1 
ATOM   1545 N  N   . TYR   B 1 58  ? 27.831 -29.482 12.230 1.00 15.27 ? 64  TYR   C N   1 
ATOM   1546 C  CA  . TYR   B 1 58  ? 27.206 -29.702 10.936 1.00 16.50 ? 64  TYR   C CA  1 
ATOM   1547 C  C   . TYR   B 1 58  ? 27.583 -28.568 9.989  1.00 16.28 ? 64  TYR   C C   1 
ATOM   1548 O  O   . TYR   B 1 58  ? 27.375 -27.393 10.320 1.00 15.66 ? 64  TYR   C O   1 
ATOM   1549 C  CB  . TYR   B 1 58  ? 25.676 -29.809 11.016 1.00 17.11 ? 64  TYR   C CB  1 
ATOM   1550 C  CG  . TYR   B 1 58  ? 25.083 -30.081 9.644  1.00 18.23 ? 64  TYR   C CG  1 
ATOM   1551 C  CD1 . TYR   B 1 58  ? 25.411 -31.235 8.935  1.00 18.45 ? 64  TYR   C CD1 1 
ATOM   1552 C  CD2 . TYR   B 1 58  ? 24.208 -29.180 9.052  1.00 18.72 ? 64  TYR   C CD2 1 
ATOM   1553 C  CE1 . TYR   B 1 58  ? 24.892 -31.477 7.662  1.00 18.57 ? 64  TYR   C CE1 1 
ATOM   1554 C  CE2 . TYR   B 1 58  ? 23.668 -29.422 7.791  1.00 19.20 ? 64  TYR   C CE2 1 
ATOM   1555 C  CZ  . TYR   B 1 58  ? 24.018 -30.569 7.096  1.00 19.66 ? 64  TYR   C CZ  1 
ATOM   1556 O  OH  . TYR   B 1 58  ? 23.504 -30.804 5.839  1.00 21.62 ? 64  TYR   C OH  1 
ATOM   1557 N  N   . CYS   B 1 59  ? 28.094 -28.946 8.795  1.00 15.73 ? 65  CYS   C N   1 
ATOM   1558 C  CA  . CYS   B 1 59  ? 28.503 -28.004 7.750  1.00 16.48 ? 65  CYS   C CA  1 
ATOM   1559 C  C   . CYS   B 1 59  ? 27.537 -28.177 6.553  1.00 17.16 ? 65  CYS   C C   1 
ATOM   1560 O  O   . CYS   B 1 59  ? 27.731 -29.102 5.746  1.00 16.95 ? 65  CYS   C O   1 
ATOM   1561 C  CB  . CYS   B 1 59  ? 29.945 -28.279 7.340  1.00 17.04 ? 65  CYS   C CB  1 
ATOM   1562 S  SG  . CYS   B 1 59  ? 30.527 -27.208 6.000  1.00 19.78 ? 65  CYS   C SG  1 
ATOM   1563 N  N   . SER   B 1 60  ? 26.505 -27.296 6.426  1.00 17.32 ? 66  SER   C N   1 
ATOM   1564 C  CA  A SER   B 1 60  ? 25.541 -27.467 5.338  0.50 18.20 ? 66  SER   C CA  1 
ATOM   1565 C  CA  B SER   B 1 60  ? 25.542 -27.450 5.339  0.50 17.78 ? 66  SER   C CA  1 
ATOM   1566 C  C   . SER   B 1 60  ? 26.166 -27.365 3.943  1.00 18.15 ? 66  SER   C C   1 
ATOM   1567 O  O   . SER   B 1 60  ? 25.722 -28.056 3.009  1.00 18.68 ? 66  SER   C O   1 
ATOM   1568 C  CB  A SER   B 1 60  ? 24.375 -26.492 5.469  0.50 20.18 ? 66  SER   C CB  1 
ATOM   1569 C  CB  B SER   B 1 60  ? 24.417 -26.426 5.453  0.50 18.55 ? 66  SER   C CB  1 
ATOM   1570 O  OG  A SER   B 1 60  ? 24.835 -25.156 5.381  0.50 22.58 ? 66  SER   C OG  1 
ATOM   1571 O  OG  B SER   B 1 60  ? 23.462 -26.660 4.434  0.50 18.83 ? 66  SER   C OG  1 
ATOM   1572 N  N   . SER   B 1 61  ? 27.187 -26.523 3.780  1.00 18.70 ? 67  SER   C N   1 
ATOM   1573 C  CA  . SER   B 1 61  ? 27.838 -26.350 2.472  1.00 19.26 ? 67  SER   C CA  1 
ATOM   1574 C  C   . SER   B 1 61  ? 28.638 -27.603 2.006  1.00 20.29 ? 67  SER   C C   1 
ATOM   1575 O  O   . SER   B 1 61  ? 29.125 -27.638 0.872  1.00 21.68 ? 67  SER   C O   1 
ATOM   1576 C  CB  . SER   B 1 61  ? 28.719 -25.099 2.458  1.00 19.94 ? 67  SER   C CB  1 
ATOM   1577 O  OG  . SER   B 1 61  ? 29.821 -25.247 3.336  1.00 22.89 ? 67  SER   C OG  1 
ATOM   1578 N  N   . ARG   B 1 62  ? 28.789 -28.618 2.886  1.00 19.44 ? 68  ARG   C N   1 
ATOM   1579 C  CA  . ARG   B 1 62  ? 29.422 -29.882 2.498  1.00 19.89 ? 68  ARG   C CA  1 
ATOM   1580 C  C   . ARG   B 1 62  ? 28.472 -31.098 2.762  1.00 20.32 ? 68  ARG   C C   1 
ATOM   1581 O  O   . ARG   B 1 62  ? 28.898 -32.246 2.540  1.00 20.23 ? 68  ARG   C O   1 
ATOM   1582 C  CB  . ARG   B 1 62  ? 30.721 -30.110 3.291  1.00 21.38 ? 68  ARG   C CB  1 
ATOM   1583 C  CG  . ARG   B 1 62  ? 31.806 -29.065 3.004  1.00 25.24 ? 68  ARG   C CG  1 
ATOM   1584 C  CD  . ARG   B 1 62  ? 32.520 -29.329 1.708  1.00 27.27 ? 68  ARG   C CD  1 
ATOM   1585 N  NE  . ARG   B 1 62  ? 33.545 -28.311 1.464  1.00 29.60 ? 68  ARG   C NE  1 
ATOM   1586 C  CZ  . ARG   B 1 62  ? 33.344 -27.182 0.793  1.00 33.53 ? 68  ARG   C CZ  1 
ATOM   1587 N  NH1 . ARG   B 1 62  ? 32.142 -26.901 0.294  1.00 35.97 ? 68  ARG   C NH1 1 
ATOM   1588 N  NH2 . ARG   B 1 62  ? 34.343 -26.324 0.608  1.00 31.86 ? 68  ARG   C NH2 1 
ATOM   1589 N  N   . ARG   B 1 63  ? 27.258 -30.853 3.344  1.00 19.30 ? 69  ARG   C N   1 
ATOM   1590 C  CA  . ARG   B 1 63  ? 26.291 -31.889 3.746  1.00 20.01 ? 69  ARG   C CA  1 
ATOM   1591 C  C   . ARG   B 1 63  ? 26.992 -32.921 4.641  1.00 20.23 ? 69  ARG   C C   1 
ATOM   1592 O  O   . ARG   B 1 63  ? 26.818 -34.131 4.452  1.00 21.13 ? 69  ARG   C O   1 
ATOM   1593 C  CB  . ARG   B 1 63  ? 25.678 -32.591 2.518  1.00 21.57 ? 69  ARG   C CB  1 
ATOM   1594 C  CG  . ARG   B 1 63  ? 24.753 -31.756 1.688  1.00 25.21 ? 69  ARG   C CG  1 
ATOM   1595 C  CD  . ARG   B 1 63  ? 23.470 -31.415 2.379  1.00 30.80 ? 69  ARG   C CD  1 
ATOM   1596 N  NE  . ARG   B 1 63  ? 22.470 -30.995 1.397  1.00 34.27 ? 69  ARG   C NE  1 
ATOM   1597 C  CZ  . ARG   B 1 63  ? 22.298 -29.740 0.998  1.00 33.87 ? 69  ARG   C CZ  1 
ATOM   1598 N  NH1 . ARG   B 1 63  ? 23.064 -28.765 1.488  1.00 31.75 ? 69  ARG   C NH1 1 
ATOM   1599 N  NH2 . ARG   B 1 63  ? 21.365 -29.447 0.103  1.00 31.87 ? 69  ARG   C NH2 1 
ATOM   1600 N  N   . LYS   B 1 64  ? 27.828 -32.446 5.560  1.00 18.72 ? 70  LYS   C N   1 
ATOM   1601 C  CA  . LYS   B 1 64  ? 28.624 -33.360 6.383  1.00 19.71 ? 70  LYS   C CA  1 
ATOM   1602 C  C   . LYS   B 1 64  ? 28.801 -32.842 7.798  1.00 18.75 ? 70  LYS   C C   1 
ATOM   1603 O  O   . LYS   B 1 64  ? 28.870 -31.628 8.005  1.00 18.42 ? 70  LYS   C O   1 
ATOM   1604 C  CB  . LYS   B 1 64  ? 30.040 -33.497 5.780  1.00 24.41 ? 70  LYS   C CB  1 
ATOM   1605 C  CG  . LYS   B 1 64  ? 30.170 -34.573 4.718  1.00 33.71 ? 70  LYS   C CG  1 
ATOM   1606 C  CD  . LYS   B 1 64  ? 31.612 -34.747 4.274  1.00 42.42 ? 70  LYS   C CD  1 
ATOM   1607 C  CE  . LYS   B 1 64  ? 31.742 -35.834 3.231  1.00 48.64 ? 70  LYS   C CE  1 
ATOM   1608 N  NZ  . LYS   B 1 64  ? 30.895 -35.565 2.036  1.00 52.60 ? 70  LYS   C NZ  1 
ATOM   1609 N  N   . HIS   B 1 65  ? 28.917 -33.793 8.753  1.00 18.06 ? 71  HIS   C N   1 
ATOM   1610 C  CA  . HIS   B 1 65  ? 29.229 -33.527 10.155 1.00 17.85 ? 71  HIS   C CA  1 
ATOM   1611 C  C   . HIS   B 1 65  ? 30.724 -33.809 10.303 1.00 19.26 ? 71  HIS   C C   1 
ATOM   1612 O  O   . HIS   B 1 65  ? 31.195 -34.881 9.869  1.00 20.71 ? 71  HIS   C O   1 
ATOM   1613 C  CB  . HIS   B 1 65  ? 28.431 -34.477 11.099 1.00 17.64 ? 71  HIS   C CB  1 
ATOM   1614 C  CG  . HIS   B 1 65  ? 26.949 -34.273 11.043 1.00 18.00 ? 71  HIS   C CG  1 
ATOM   1615 N  ND1 . HIS   B 1 65  ? 26.283 -33.453 11.953 1.00 20.41 ? 71  HIS   C ND1 1 
ATOM   1616 C  CD2 . HIS   B 1 65  ? 26.051 -34.759 10.160 1.00 19.15 ? 71  HIS   C CD2 1 
ATOM   1617 C  CE1 . HIS   B 1 65  ? 25.001 -33.496 11.614 1.00 19.64 ? 71  HIS   C CE1 1 
ATOM   1618 N  NE2 . HIS   B 1 65  ? 24.812 -34.249 10.525 1.00 20.61 ? 71  HIS   C NE2 1 
ATOM   1619 N  N   . TYR   B 1 66  ? 31.487 -32.859 10.880 1.00 18.00 ? 72  TYR   C N   1 
ATOM   1620 C  CA  . TYR   B 1 66  ? 32.925 -33.073 11.015 1.00 18.30 ? 72  TYR   C CA  1 
ATOM   1621 C  C   . TYR   B 1 66  ? 33.316 -33.113 12.485 1.00 16.96 ? 72  TYR   C C   1 
ATOM   1622 O  O   . TYR   B 1 66  ? 32.901 -32.226 13.243 1.00 16.34 ? 72  TYR   C O   1 
ATOM   1623 C  CB  . TYR   B 1 66  ? 33.703 -31.894 10.371 1.00 19.09 ? 72  TYR   C CB  1 
ATOM   1624 C  CG  . TYR   B 1 66  ? 33.636 -31.796 8.859  1.00 20.11 ? 72  TYR   C CG  1 
ATOM   1625 C  CD1 . TYR   B 1 66  ? 34.447 -32.578 8.060  1.00 20.82 ? 72  TYR   C CD1 1 
ATOM   1626 C  CD2 . TYR   B 1 66  ? 32.829 -30.851 8.237  1.00 21.59 ? 72  TYR   C CD2 1 
ATOM   1627 C  CE1 . TYR   B 1 66  ? 34.444 -32.439 6.673  1.00 21.44 ? 72  TYR   C CE1 1 
ATOM   1628 C  CE2 . TYR   B 1 66  ? 32.811 -30.705 6.855  1.00 22.21 ? 72  TYR   C CE2 1 
ATOM   1629 C  CZ  . TYR   B 1 66  ? 33.621 -31.504 6.071  1.00 22.80 ? 72  TYR   C CZ  1 
ATOM   1630 O  OH  . TYR   B 1 66  ? 33.578 -31.367 4.697  1.00 24.34 ? 72  TYR   C OH  1 
ATOM   1631 N  N   . PRO   B 1 67  ? 34.145 -34.087 12.900 1.00 16.78 ? 73  PRO   C N   1 
ATOM   1632 C  CA  . PRO   B 1 67  ? 34.659 -34.030 14.289 1.00 16.99 ? 73  PRO   C CA  1 
ATOM   1633 C  C   . PRO   B 1 67  ? 35.737 -32.935 14.366 1.00 17.61 ? 73  PRO   C C   1 
ATOM   1634 O  O   . PRO   B 1 67  ? 36.549 -32.809 13.430 1.00 18.28 ? 73  PRO   C O   1 
ATOM   1635 C  CB  . PRO   B 1 67  ? 35.283 -35.411 14.514 1.00 19.20 ? 73  PRO   C CB  1 
ATOM   1636 C  CG  . PRO   B 1 67  ? 35.523 -35.985 13.140 1.00 19.88 ? 73  PRO   C CG  1 
ATOM   1637 C  CD  . PRO   B 1 67  ? 34.724 -35.203 12.110 1.00 17.58 ? 73  PRO   C CD  1 
ATOM   1638 N  N   . VAL   B 1 68  ? 35.742 -32.132 15.435 1.00 16.79 ? 74  VAL   C N   1 
ATOM   1639 C  CA  . VAL   B 1 68  ? 36.712 -31.038 15.536 1.00 17.26 ? 74  VAL   C CA  1 
ATOM   1640 C  C   . VAL   B 1 68  ? 37.127 -30.849 17.007 1.00 15.83 ? 74  VAL   C C   1 
ATOM   1641 O  O   . VAL   B 1 68  ? 36.387 -31.204 17.952 1.00 15.96 ? 74  VAL   C O   1 
ATOM   1642 C  CB  . VAL   B 1 68  ? 36.089 -29.670 15.057 1.00 19.24 ? 74  VAL   C CB  1 
ATOM   1643 C  CG1 . VAL   B 1 68  ? 36.030 -29.530 13.531 1.00 20.82 ? 74  VAL   C CG1 1 
ATOM   1644 C  CG2 . VAL   B 1 68  ? 34.726 -29.400 15.711 1.00 19.21 ? 74  VAL   C CG2 1 
ATOM   1645 N  N   . SER   B 1 69  ? 38.330 -30.252 17.174 1.00 15.48 ? 75  SER   C N   1 
ATOM   1646 C  CA  . SER   B 1 69  ? 38.831 -29.701 18.432 1.00 16.08 ? 75  SER   C CA  1 
ATOM   1647 C  C   . SER   B 1 69  ? 38.529 -28.200 18.324 1.00 15.61 ? 75  SER   C C   1 
ATOM   1648 O  O   . SER   B 1 69  ? 38.713 -27.594 17.253 1.00 16.02 ? 75  SER   C O   1 
ATOM   1649 C  CB  . SER   B 1 69  ? 40.346 -29.878 18.535 1.00 18.73 ? 75  SER   C CB  1 
ATOM   1650 O  OG  . SER   B 1 69  ? 40.674 -31.245 18.732 1.00 23.73 ? 75  SER   C OG  1 
ATOM   1651 N  N   . PHE   B 1 70  ? 38.043 -27.579 19.414 1.00 15.64 ? 76  PHE   C N   1 
ATOM   1652 C  CA  . PHE   B 1 70  ? 37.728 -26.148 19.360 1.00 16.28 ? 76  PHE   C CA  1 
ATOM   1653 C  C   . PHE   B 1 70  ? 38.248 -25.411 20.593 1.00 17.20 ? 76  PHE   C C   1 
ATOM   1654 O  O   . PHE   B 1 70  ? 38.415 -26.025 21.659 1.00 18.67 ? 76  PHE   C O   1 
ATOM   1655 C  CB  . PHE   B 1 70  ? 36.242 -25.894 19.104 1.00 15.96 ? 76  PHE   C CB  1 
ATOM   1656 C  CG  . PHE   B 1 70  ? 35.343 -26.604 20.093 1.00 15.53 ? 76  PHE   C CG  1 
ATOM   1657 C  CD1 . PHE   B 1 70  ? 34.897 -27.894 19.847 1.00 15.72 ? 76  PHE   C CD1 1 
ATOM   1658 C  CD2 . PHE   B 1 70  ? 34.882 -25.951 21.222 1.00 15.35 ? 76  PHE   C CD2 1 
ATOM   1659 C  CE1 . PHE   B 1 70  ? 34.085 -28.557 20.772 1.00 16.13 ? 76  PHE   C CE1 1 
ATOM   1660 C  CE2 . PHE   B 1 70  ? 34.054 -26.602 22.142 1.00 15.46 ? 76  PHE   C CE2 1 
ATOM   1661 C  CZ  . PHE   B 1 70  ? 33.638 -27.888 21.906 1.00 15.57 ? 76  PHE   C CZ  1 
ATOM   1662 N  N   . SER   B 1 71  ? 38.568 -24.119 20.429 1.00 16.11 ? 77  SER   C N   1 
ATOM   1663 C  CA  . SER   B 1 71  ? 39.180 -23.318 21.495 1.00 16.66 ? 77  SER   C CA  1 
ATOM   1664 C  C   . SER   B 1 71  ? 38.194 -22.930 22.612 1.00 17.90 ? 77  SER   C C   1 
ATOM   1665 O  O   . SER   B 1 71  ? 37.001 -23.191 22.491 1.00 18.88 ? 77  SER   C O   1 
ATOM   1666 C  CB  . SER   B 1 71  ? 39.844 -22.076 20.897 1.00 17.37 ? 77  SER   C CB  1 
ATOM   1667 O  OG  . SER   B 1 71  ? 38.885 -21.147 20.418 1.00 19.32 ? 77  SER   C OG  1 
ATOM   1668 N  N   . LYS   B 1 72  ? 38.685 -22.294 23.700 1.00 17.44 ? 78  LYS   C N   1 
ATOM   1669 C  CA  . LYS   B 1 72  ? 37.806 -21.874 24.802 1.00 18.42 ? 78  LYS   C CA  1 
ATOM   1670 C  C   . LYS   B 1 72  ? 37.091 -20.566 24.400 1.00 18.79 ? 78  LYS   C C   1 
ATOM   1671 O  O   . LYS   B 1 72  ? 37.660 -19.737 23.686 1.00 19.68 ? 78  LYS   C O   1 
ATOM   1672 C  CB  . LYS   B 1 72  ? 38.643 -21.638 26.077 1.00 22.47 ? 78  LYS   C CB  1 
ATOM   1673 C  CG  . LYS   B 1 72  ? 39.311 -22.893 26.633 1.00 27.58 ? 78  LYS   C CG  1 
ATOM   1674 C  CD  . LYS   B 1 72  ? 39.788 -22.652 28.073 1.00 37.07 ? 78  LYS   C CD  1 
ATOM   1675 C  CE  . LYS   B 1 72  ? 40.497 -23.855 28.651 1.00 44.32 ? 78  LYS   C CE  1 
ATOM   1676 N  NZ  . LYS   B 1 72  ? 40.669 -23.734 30.130 1.00 48.25 ? 78  LYS   C NZ  1 
ATOM   1677 N  N   . PRO   B 1 73  ? 35.860 -20.335 24.879 1.00 18.38 ? 79  PRO   C N   1 
ATOM   1678 C  CA  . PRO   B 1 73  ? 35.132 -19.088 24.482 1.00 18.43 ? 79  PRO   C CA  1 
ATOM   1679 C  C   . PRO   B 1 73  ? 35.918 -17.828 24.839 1.00 19.29 ? 79  PRO   C C   1 
ATOM   1680 O  O   . PRO   B 1 73  ? 36.369 -17.681 25.976 1.00 20.03 ? 79  PRO   C O   1 
ATOM   1681 C  CB  . PRO   B 1 73  ? 33.822 -19.128 25.272 1.00 19.81 ? 79  PRO   C CB  1 
ATOM   1682 C  CG  . PRO   B 1 73  ? 33.821 -20.396 26.045 1.00 20.42 ? 79  PRO   C CG  1 
ATOM   1683 C  CD  . PRO   B 1 73  ? 35.072 -21.219 25.764 1.00 18.20 ? 79  PRO   C CD  1 
ATOM   1684 N  N   . SER   B 1 74  ? 36.153 -16.955 23.862 1.00 19.15 ? 80  SER   C N   1 
ATOM   1685 C  CA  . SER   B 1 74  ? 37.007 -15.767 24.078 1.00 20.59 ? 80  SER   C CA  1 
ATOM   1686 C  C   . SER   B 1 74  ? 36.594 -14.562 23.188 1.00 20.28 ? 80  SER   C C   1 
ATOM   1687 O  O   . SER   B 1 74  ? 35.707 -14.703 22.336 1.00 19.19 ? 80  SER   C O   1 
ATOM   1688 C  CB  . SER   B 1 74  ? 38.463 -16.111 23.746 1.00 24.86 ? 80  SER   C CB  1 
ATOM   1689 O  OG  . SER   B 1 74  ? 38.828 -17.468 23.919 1.00 31.95 ? 80  SER   C OG  1 
ATOM   1690 N  N   . LEU   B 1 75  ? 37.285 -13.399 23.349 1.00 20.69 ? 81  LEU   C N   1 
ATOM   1691 C  CA  . LEU   B 1 75  ? 37.072 -12.201 22.526 1.00 22.52 ? 81  LEU   C CA  1 
ATOM   1692 C  C   . LEU   B 1 75  ? 38.061 -12.327 21.345 1.00 22.62 ? 81  LEU   C C   1 
ATOM   1693 O  O   . LEU   B 1 75  ? 39.285 -12.288 21.559 1.00 22.80 ? 81  LEU   C O   1 
ATOM   1694 C  CB  . LEU   B 1 75  ? 37.394 -10.930 23.348 1.00 24.15 ? 81  LEU   C CB  1 
ATOM   1695 C  CG  . LEU   B 1 75  ? 37.001 -9.567  22.738 1.00 26.86 ? 81  LEU   C CG  1 
ATOM   1696 C  CD1 . LEU   B 1 75  ? 35.505 -9.427  22.597 1.00 26.90 ? 81  LEU   C CD1 1 
ATOM   1697 C  CD2 . LEU   B 1 75  ? 37.575 -8.405  23.572 1.00 28.66 ? 81  LEU   C CD2 1 
ATOM   1698 N  N   . ILE   B 1 76  ? 37.542 -12.569 20.130 1.00 21.92 ? 82  ILE   C N   1 
ATOM   1699 C  CA  . ILE   B 1 76  ? 38.373 -12.827 18.949 1.00 22.21 ? 82  ILE   C CA  1 
ATOM   1700 C  C   . ILE   B 1 76  ? 38.107 -11.772 17.870 1.00 22.26 ? 82  ILE   C C   1 
ATOM   1701 O  O   . ILE   B 1 76  ? 36.939 -11.450 17.594 1.00 21.42 ? 82  ILE   C O   1 
ATOM   1702 C  CB  . ILE   B 1 76  ? 38.013 -14.239 18.372 1.00 23.46 ? 82  ILE   C CB  1 
ATOM   1703 C  CG1 . ILE   B 1 76  ? 38.259 -15.401 19.367 1.00 25.38 ? 82  ILE   C CG1 1 
ATOM   1704 C  CG2 . ILE   B 1 76  ? 38.705 -14.520 17.021 1.00 24.67 ? 82  ILE   C CG2 1 
ATOM   1705 C  CD1 . ILE   B 1 76  ? 39.644 -15.754 19.601 1.00 27.98 ? 82  ILE   C CD1 1 
ATOM   1706 N  N   . PHE   B 1 77  ? 39.188 -11.271 17.226 1.00 22.19 ? 83  PHE   C N   1 
ATOM   1707 C  CA  . PHE   B 1 77  ? 39.022 -10.339 16.124 1.00 23.67 ? 83  PHE   C CA  1 
ATOM   1708 C  C   . PHE   B 1 77  ? 38.571 -11.161 14.890 1.00 24.34 ? 83  PHE   C C   1 
ATOM   1709 O  O   . PHE   B 1 77  ? 39.223 -12.164 14.521 1.00 25.46 ? 83  PHE   C O   1 
ATOM   1710 C  CB  . PHE   B 1 77  ? 40.329 -9.575  15.829 1.00 23.99 ? 83  PHE   C CB  1 
ATOM   1711 C  CG  . PHE   B 1 77  ? 40.106 -8.471  14.816 1.00 24.98 ? 83  PHE   C CG  1 
ATOM   1712 C  CD1 . PHE   B 1 77  ? 39.481 -7.290  15.183 1.00 26.50 ? 83  PHE   C CD1 1 
ATOM   1713 C  CD2 . PHE   B 1 77  ? 40.487 -8.633  13.489 1.00 25.61 ? 83  PHE   C CD2 1 
ATOM   1714 C  CE1 . PHE   B 1 77  ? 39.247 -6.290  14.242 1.00 27.53 ? 83  PHE   C CE1 1 
ATOM   1715 C  CE2 . PHE   B 1 77  ? 40.267 -7.627  12.557 1.00 26.47 ? 83  PHE   C CE2 1 
ATOM   1716 C  CZ  . PHE   B 1 77  ? 39.659 -6.463  12.939 1.00 27.16 ? 83  PHE   C CZ  1 
ATOM   1717 N  N   . VAL   B 1 78  ? 37.464 -10.738 14.257 1.00 22.41 ? 84  VAL   C N   1 
ATOM   1718 C  CA  . VAL   B 1 78  ? 36.911 -11.418 13.089 1.00 22.00 ? 84  VAL   C CA  1 
ATOM   1719 C  C   . VAL   B 1 78  ? 37.012 -10.494 11.877 1.00 21.60 ? 84  VAL   C C   1 
ATOM   1720 O  O   . VAL   B 1 78  ? 36.552 -9.355  11.984 1.00 21.61 ? 84  VAL   C O   1 
ATOM   1721 C  CB  . VAL   B 1 78  ? 35.411 -11.716 13.361 1.00 22.56 ? 84  VAL   C CB  1 
ATOM   1722 C  CG1 . VAL   B 1 78  ? 34.795 -12.421 12.165 1.00 23.45 ? 84  VAL   C CG1 1 
ATOM   1723 C  CG2 . VAL   B 1 78  ? 35.222 -12.554 14.615 1.00 22.66 ? 84  VAL   C CG2 1 
ATOM   1724 N  N   . GLU   B 1 79  ? 37.514 -10.990 10.711 1.00 21.03 ? 85  GLU   C N   1 
ATOM   1725 C  CA  . GLU   B 1 79  ? 37.567 -10.191 9.468  1.00 21.34 ? 85  GLU   C CA  1 
ATOM   1726 C  C   . GLU   B 1 79  ? 36.157 -9.859  8.948  1.00 20.99 ? 85  GLU   C C   1 
ATOM   1727 O  O   . GLU   B 1 79  ? 35.181 -10.538 9.310  1.00 20.03 ? 85  GLU   C O   1 
ATOM   1728 C  CB  . GLU   B 1 79  ? 38.325 -10.964 8.371  1.00 24.75 ? 85  GLU   C CB  1 
ATOM   1729 C  CG  . GLU   B 1 79  ? 39.791 -11.189 8.707  1.00 29.89 ? 85  GLU   C CG  1 
ATOM   1730 C  CD  . GLU   B 1 79  ? 40.560 -9.896  8.908  1.00 39.74 ? 85  GLU   C CD  1 
ATOM   1731 O  OE1 . GLU   B 1 79  ? 40.472 -9.006  8.029  1.00 42.14 ? 85  GLU   C OE1 1 
ATOM   1732 O  OE2 . GLU   B 1 79  ? 41.207 -9.749  9.970  1.00 42.68 ? 85  GLU   C OE2 1 
ATOM   1733 N  N   . ALA   B 1 80  ? 36.043 -8.855  8.072  1.00 21.80 ? 86  ALA   C N   1 
ATOM   1734 C  CA  . ALA   B 1 80  ? 34.755 -8.469  7.505  1.00 22.98 ? 86  ALA   C CA  1 
ATOM   1735 C  C   . ALA   B 1 80  ? 34.074 -9.660  6.783  1.00 24.54 ? 86  ALA   C C   1 
ATOM   1736 O  O   . ALA   B 1 80  ? 34.741 -10.507 6.182  1.00 24.33 ? 86  ALA   C O   1 
ATOM   1737 C  CB  . ALA   B 1 80  ? 34.941 -7.293  6.547  1.00 23.32 ? 86  ALA   C CB  1 
ATOM   1738 N  N   . SER   B 1 81  ? 32.770 -9.769  6.962  1.00 25.37 ? 87  SER   C N   1 
ATOM   1739 C  CA  . SER   B 1 81  ? 31.966 -10.804 6.314  1.00 26.74 ? 87  SER   C CA  1 
ATOM   1740 C  C   . SER   B 1 81  ? 30.842 -10.103 5.535  1.00 27.84 ? 87  SER   C C   1 
ATOM   1741 O  O   . SER   B 1 81  ? 30.732 -8.866  5.601  1.00 28.45 ? 87  SER   C O   1 
ATOM   1742 C  CB  . SER   B 1 81  ? 31.379 -11.759 7.363  1.00 28.02 ? 87  SER   C CB  1 
ATOM   1743 O  OG  . SER   B 1 81  ? 30.352 -11.114 8.107  1.00 29.98 ? 87  SER   C OG  1 
ATOM   1744 N  N   . GLU   B 1 82  ? 29.965 -10.870 4.835  1.00 28.41 ? 88  GLU   C N   1 
ATOM   1745 C  CA  . GLU   B 1 82  ? 28.852 -10.219 4.132  1.00 28.98 ? 88  GLU   C CA  1 
ATOM   1746 C  C   . GLU   B 1 82  ? 27.818 -9.599  5.099  1.00 28.84 ? 88  GLU   C C   1 
ATOM   1747 O  O   . GLU   B 1 82  ? 27.035 -8.744  4.682  1.00 29.17 ? 88  GLU   C O   1 
ATOM   1748 C  CB  . GLU   B 1 82  ? 28.187 -11.155 3.103  1.00 32.46 ? 88  GLU   C CB  1 
ATOM   1749 C  CG  . GLU   B 1 82  ? 27.568 -12.414 3.688  1.00 38.57 ? 88  GLU   C CG  1 
ATOM   1750 C  CD  . GLU   B 1 82  ? 26.912 -13.321 2.660  1.00 45.34 ? 88  GLU   C CD  1 
ATOM   1751 O  OE1 . GLU   B 1 82  ? 27.526 -13.544 1.591  1.00 45.57 ? 88  GLU   C OE1 1 
ATOM   1752 O  OE2 . GLU   B 1 82  ? 25.792 -13.819 2.927  1.00 48.66 ? 88  GLU   C OE2 1 
ATOM   1753 N  N   . TYR   B 1 83  ? 27.857 -9.972  6.406  1.00 27.41 ? 89  TYR   C N   1 
ATOM   1754 C  CA  . TYR   B 1 83  ? 26.858 -9.500  7.377  1.00 26.61 ? 89  TYR   C CA  1 
ATOM   1755 C  C   . TYR   B 1 83  ? 27.415 -8.584  8.521  1.00 25.65 ? 89  TYR   C C   1 
ATOM   1756 O  O   . TYR   B 1 83  ? 26.617 -7.893  9.172  1.00 26.37 ? 89  TYR   C O   1 
ATOM   1757 C  CB  . TYR   B 1 83  ? 26.049 -10.707 7.950  1.00 26.18 ? 89  TYR   C CB  1 
ATOM   1758 C  CG  . TYR   B 1 83  ? 26.897 -11.926 8.299  1.00 26.68 ? 89  TYR   C CG  1 
ATOM   1759 C  CD1 . TYR   B 1 83  ? 27.210 -12.885 7.340  1.00 27.19 ? 89  TYR   C CD1 1 
ATOM   1760 C  CD2 . TYR   B 1 83  ? 27.374 -12.119 9.587  1.00 27.40 ? 89  TYR   C CD2 1 
ATOM   1761 C  CE1 . TYR   B 1 83  ? 28.004 -13.988 7.653  1.00 27.33 ? 89  TYR   C CE1 1 
ATOM   1762 C  CE2 . TYR   B 1 83  ? 28.154 -13.217 9.914  1.00 28.14 ? 89  TYR   C CE2 1 
ATOM   1763 C  CZ  . TYR   B 1 83  ? 28.460 -14.159 8.949  1.00 28.85 ? 89  TYR   C CZ  1 
ATOM   1764 O  OH  . TYR   B 1 83  ? 29.223 -15.262 9.297  1.00 29.17 ? 89  TYR   C OH  1 
ATOM   1765 N  N   . TYR   B 1 84  ? 28.754 -8.542  8.759  1.00 23.07 ? 90  TYR   C N   1 
ATOM   1766 C  CA  . TYR   B 1 84  ? 29.322 -7.636  9.782  1.00 21.22 ? 90  TYR   C CA  1 
ATOM   1767 C  C   . TYR   B 1 84  ? 30.650 -7.032  9.250  1.00 21.31 ? 90  TYR   C C   1 
ATOM   1768 O  O   . TYR   B 1 84  ? 31.375 -7.712  8.499  1.00 21.02 ? 90  TYR   C O   1 
ATOM   1769 C  CB  . TYR   B 1 84  ? 29.683 -8.399  11.097 1.00 20.07 ? 90  TYR   C CB  1 
ATOM   1770 C  CG  . TYR   B 1 84  ? 28.501 -8.850  11.946 1.00 19.39 ? 90  TYR   C CG  1 
ATOM   1771 C  CD1 . TYR   B 1 84  ? 27.603 -7.926  12.479 1.00 20.00 ? 90  TYR   C CD1 1 
ATOM   1772 C  CD2 . TYR   B 1 84  ? 28.332 -10.182 12.281 1.00 19.51 ? 90  TYR   C CD2 1 
ATOM   1773 C  CE1 . TYR   B 1 84  ? 26.540 -8.331  13.296 1.00 20.22 ? 90  TYR   C CE1 1 
ATOM   1774 C  CE2 . TYR   B 1 84  ? 27.239 -10.609 13.038 1.00 19.37 ? 90  TYR   C CE2 1 
ATOM   1775 C  CZ  . TYR   B 1 84  ? 26.374 -9.676  13.592 1.00 20.56 ? 90  TYR   C CZ  1 
ATOM   1776 O  OH  . TYR   B 1 84  ? 25.316 -10.102 14.378 1.00 19.47 ? 90  TYR   C OH  1 
ATOM   1777 N  N   . PRO   B 1 85  ? 31.053 -5.841  9.731  1.00 21.60 ? 91  PRO   C N   1 
ATOM   1778 C  CA  . PRO   B 1 85  ? 32.407 -5.344  9.388  1.00 22.13 ? 91  PRO   C CA  1 
ATOM   1779 C  C   . PRO   B 1 85  ? 33.479 -6.089  10.224 1.00 22.01 ? 91  PRO   C C   1 
ATOM   1780 O  O   . PRO   B 1 85  ? 33.135 -6.945  11.071 1.00 21.23 ? 91  PRO   C O   1 
ATOM   1781 C  CB  . PRO   B 1 85  ? 32.340 -3.865  9.798  1.00 23.37 ? 91  PRO   C CB  1 
ATOM   1782 C  CG  . PRO   B 1 85  ? 31.382 -3.868  10.993 1.00 23.75 ? 91  PRO   C CG  1 
ATOM   1783 C  CD  . PRO   B 1 85  ? 30.349 -4.932  10.678 1.00 21.82 ? 91  PRO   C CD  1 
ATOM   1784 N  N   . ALA   B 1 86  ? 34.784 -5.771  10.007 1.00 21.86 ? 92  ALA   C N   1 
ATOM   1785 C  CA  . ALA   B 1 86  ? 35.871 -6.359  10.821 1.00 22.58 ? 92  ALA   C CA  1 
ATOM   1786 C  C   . ALA   B 1 86  ? 35.689 -5.843  12.269 1.00 23.29 ? 92  ALA   C C   1 
ATOM   1787 O  O   . ALA   B 1 86  ? 35.482 -4.645  12.446 1.00 23.78 ? 92  ALA   C O   1 
ATOM   1788 C  CB  . ALA   B 1 86  ? 37.224 -5.908  10.280 1.00 22.31 ? 92  ALA   C CB  1 
ATOM   1789 N  N   . ARG   B 1 87  ? 35.650 -6.744  13.280 1.00 22.83 ? 93  ARG   C N   1 
ATOM   1790 C  CA  . ARG   B 1 87  ? 35.393 -6.319  14.663 1.00 23.23 ? 93  ARG   C CA  1 
ATOM   1791 C  C   . ARG   B 1 87  ? 35.723 -7.454  15.652 1.00 23.51 ? 93  ARG   C C   1 
ATOM   1792 O  O   . ARG   B 1 87  ? 35.994 -8.579  15.226 1.00 23.53 ? 93  ARG   C O   1 
ATOM   1793 C  CB  . ARG   B 1 87  ? 33.889 -5.948  14.818 1.00 23.86 ? 93  ARG   C CB  1 
ATOM   1794 C  CG  . ARG   B 1 87  ? 32.992 -7.171  14.569 1.00 25.19 ? 93  ARG   C CG  1 
ATOM   1795 C  CD  . ARG   B 1 87  ? 31.527 -6.987  14.945 1.00 26.02 ? 93  ARG   C CD  1 
ATOM   1796 N  NE  . ARG   B 1 87  ? 30.842 -8.280  15.031 1.00 26.64 ? 93  ARG   C NE  1 
ATOM   1797 C  CZ  . ARG   B 1 87  ? 29.723 -8.495  15.718 1.00 27.90 ? 93  ARG   C CZ  1 
ATOM   1798 N  NH1 . ARG   B 1 87  ? 29.145 -7.503  16.392 1.00 26.34 ? 93  ARG   C NH1 1 
ATOM   1799 N  NH2 . ARG   B 1 87  ? 29.191 -9.710  15.766 1.00 26.35 ? 93  ARG   C NH2 1 
ATOM   1800 N  N   . TYR   B 1 88  ? 35.637 -7.176  16.976 1.00 23.29 ? 94  TYR   C N   1 
ATOM   1801 C  CA  . TYR   B 1 88  ? 35.826 -8.227  17.971 1.00 24.33 ? 94  TYR   C CA  1 
ATOM   1802 C  C   . TYR   B 1 88  ? 34.476 -8.855  18.282 1.00 22.65 ? 94  TYR   C C   1 
ATOM   1803 O  O   . TYR   B 1 88  ? 33.492 -8.140  18.519 1.00 23.06 ? 94  TYR   C O   1 
ATOM   1804 C  CB  . TYR   B 1 88  ? 36.392 -7.670  19.295 1.00 26.31 ? 94  TYR   C CB  1 
ATOM   1805 C  CG  . TYR   B 1 88  ? 37.856 -7.343  19.176 1.00 29.35 ? 94  TYR   C CG  1 
ATOM   1806 C  CD1 . TYR   B 1 88  ? 38.822 -8.323  19.349 1.00 31.25 ? 94  TYR   C CD1 1 
ATOM   1807 C  CD2 . TYR   B 1 88  ? 38.271 -6.075  18.801 1.00 31.39 ? 94  TYR   C CD2 1 
ATOM   1808 C  CE1 . TYR   B 1 88  ? 40.170 -8.032  19.197 1.00 32.75 ? 94  TYR   C CE1 1 
ATOM   1809 C  CE2 . TYR   B 1 88  ? 39.608 -5.773  18.641 1.00 32.87 ? 94  TYR   C CE2 1 
ATOM   1810 C  CZ  . TYR   B 1 88  ? 40.558 -6.748  18.846 1.00 34.31 ? 94  TYR   C CZ  1 
ATOM   1811 O  OH  . TYR   B 1 88  ? 41.869 -6.372  18.682 1.00 37.05 ? 94  TYR   C OH  1 
ATOM   1812 N  N   . GLN   B 1 89  ? 34.415 -10.178 18.280 1.00 20.57 ? 95  GLN   C N   1 
ATOM   1813 C  CA  . GLN   B 1 89  ? 33.190 -10.879 18.683 1.00 19.28 ? 95  GLN   C CA  1 
ATOM   1814 C  C   . GLN   B 1 89  ? 33.520 -11.640 19.986 1.00 19.07 ? 95  GLN   C C   1 
ATOM   1815 O  O   . GLN   B 1 89  ? 34.597 -12.261 20.083 1.00 18.89 ? 95  GLN   C O   1 
ATOM   1816 C  CB  . GLN   B 1 89  ? 32.741 -11.843 17.567 1.00 19.69 ? 95  GLN   C CB  1 
ATOM   1817 C  CG  . GLN   B 1 89  ? 31.511 -12.669 17.929 1.00 20.53 ? 95  GLN   C CG  1 
ATOM   1818 C  CD  . GLN   B 1 89  ? 30.802 -13.244 16.715 1.00 20.98 ? 95  GLN   C CD  1 
ATOM   1819 O  OE1 . GLN   B 1 89  ? 30.711 -12.609 15.642 1.00 22.32 ? 95  GLN   C OE1 1 
ATOM   1820 N  NE2 . GLN   B 1 89  ? 30.275 -14.444 16.874 1.00 20.40 ? 95  GLN   C NE2 1 
ATOM   1821 N  N   . SER   B 1 90  ? 32.635 -11.561 20.989 1.00 17.83 ? 96  SER   C N   1 
ATOM   1822 C  CA  . SER   B 1 90  ? 32.882 -12.223 22.282 1.00 18.32 ? 96  SER   C CA  1 
ATOM   1823 C  C   . SER   B 1 90  ? 32.214 -13.628 22.374 1.00 17.56 ? 96  SER   C C   1 
ATOM   1824 O  O   . SER   B 1 90  ? 31.360 -13.946 21.556 1.00 16.78 ? 96  SER   C O   1 
ATOM   1825 C  CB  . SER   B 1 90  ? 32.412 -11.349 23.451 1.00 20.24 ? 96  SER   C CB  1 
ATOM   1826 O  OG  . SER   B 1 90  ? 31.008 -11.203 23.400 1.00 22.71 ? 96  SER   C OG  1 
ATOM   1827 N  N   . HIS   B 1 91  ? 32.676 -14.468 23.331 1.00 16.94 ? 97  HIS   C N   1 
ATOM   1828 C  CA  . HIS   B 1 91  ? 32.173 -15.824 23.573 1.00 17.36 ? 97  HIS   C CA  1 
ATOM   1829 C  C   . HIS   B 1 91  ? 32.279 -16.694 22.281 1.00 16.29 ? 97  HIS   C C   1 
ATOM   1830 O  O   . HIS   B 1 91  ? 31.411 -17.539 22.027 1.00 16.96 ? 97  HIS   C O   1 
ATOM   1831 C  CB  . HIS   B 1 91  ? 30.742 -15.794 24.169 1.00 18.79 ? 97  HIS   C CB  1 
ATOM   1832 C  CG  . HIS   B 1 91  ? 30.636 -15.043 25.485 1.00 22.37 ? 97  HIS   C CG  1 
ATOM   1833 N  ND1 . HIS   B 1 91  ? 30.669 -15.710 26.711 1.00 24.17 ? 97  HIS   C ND1 1 
ATOM   1834 C  CD2 . HIS   B 1 91  ? 30.491 -13.710 25.723 1.00 23.29 ? 97  HIS   C CD2 1 
ATOM   1835 C  CE1 . HIS   B 1 91  ? 30.533 -14.771 27.642 1.00 23.96 ? 97  HIS   C CE1 1 
ATOM   1836 N  NE2 . HIS   B 1 91  ? 30.424 -13.553 27.098 1.00 24.45 ? 97  HIS   C NE2 1 
ATOM   1837 N  N   . LEU   B 1 92  ? 33.347 -16.451 21.483 1.00 15.25 ? 98  LEU   C N   1 
ATOM   1838 C  CA  . LEU   B 1 92  ? 33.568 -17.172 20.235 1.00 16.15 ? 98  LEU   C CA  1 
ATOM   1839 C  C   . LEU   B 1 92  ? 34.642 -18.269 20.429 1.00 16.28 ? 98  LEU   C C   1 
ATOM   1840 O  O   . LEU   B 1 92  ? 35.616 -18.059 21.163 1.00 16.87 ? 98  LEU   C O   1 
ATOM   1841 C  CB  . LEU   B 1 92  ? 34.032 -16.165 19.131 1.00 16.34 ? 98  LEU   C CB  1 
ATOM   1842 C  CG  . LEU   B 1 92  ? 34.140 -16.700 17.693 1.00 18.20 ? 98  LEU   C CG  1 
ATOM   1843 C  CD1 . LEU   B 1 92  ? 32.784 -17.211 17.190 1.00 19.51 ? 98  LEU   C CD1 1 
ATOM   1844 C  CD2 . LEU   B 1 92  ? 34.713 -15.635 16.711 1.00 17.14 ? 98  LEU   C CD2 1 
ATOM   1845 N  N   . MET   B 1 93  ? 34.452 -19.431 19.765 1.00 14.92 ? 99  MET   C N   1 
ATOM   1846 C  CA  . MET   B 1 93  ? 35.420 -20.546 19.839 1.00 15.28 ? 99  MET   C CA  1 
ATOM   1847 C  C   . MET   B 1 93  ? 35.803 -20.898 18.386 1.00 15.86 ? 99  MET   C C   1 
ATOM   1848 O  O   . MET   B 1 93  ? 34.912 -20.970 17.529 1.00 16.36 ? 99  MET   C O   1 
ATOM   1849 C  CB  . MET   B 1 93  ? 34.746 -21.776 20.508 1.00 16.39 ? 99  MET   C CB  1 
ATOM   1850 C  CG  . MET   B 1 93  ? 34.231 -21.473 21.899 1.00 18.00 ? 99  MET   C CG  1 
ATOM   1851 S  SD  . MET   B 1 93  ? 33.189 -22.814 22.539 1.00 19.75 ? 99  MET   C SD  1 
ATOM   1852 C  CE  . MET   B 1 93  ? 31.834 -22.840 21.340 1.00 19.64 ? 99  MET   C CE  1 
ATOM   1853 N  N   . LEU   B 1 94  ? 37.081 -21.132 18.099 1.00 14.70 ? 100 LEU   C N   1 
ATOM   1854 C  CA  . LEU   B 1 94  ? 37.500 -21.458 16.736 1.00 16.04 ? 100 LEU   C CA  1 
ATOM   1855 C  C   . LEU   B 1 94  ? 37.932 -22.907 16.598 1.00 16.16 ? 100 LEU   C C   1 
ATOM   1856 O  O   . LEU   B 1 94  ? 38.476 -23.502 17.527 1.00 16.81 ? 100 LEU   C O   1 
ATOM   1857 C  CB  . LEU   B 1 94  ? 38.723 -20.595 16.285 1.00 16.74 ? 100 LEU   C CB  1 
ATOM   1858 C  CG  . LEU   B 1 94  ? 38.571 -19.095 16.257 1.00 18.74 ? 100 LEU   C CG  1 
ATOM   1859 C  CD1 . LEU   B 1 94  ? 39.902 -18.422 15.773 1.00 20.21 ? 100 LEU   C CD1 1 
ATOM   1860 C  CD2 . LEU   B 1 94  ? 37.387 -18.672 15.374 1.00 19.97 ? 100 LEU   C CD2 1 
ATOM   1861 N  N   . ALA   B 1 95  ? 37.737 -23.459 15.370 1.00 15.35 ? 101 ALA   C N   1 
ATOM   1862 C  CA  . ALA   B 1 95  ? 38.228 -24.782 15.009 1.00 16.43 ? 101 ALA   C CA  1 
ATOM   1863 C  C   . ALA   B 1 95  ? 38.833 -24.683 13.595 1.00 16.35 ? 101 ALA   C C   1 
ATOM   1864 O  O   . ALA   B 1 95  ? 38.522 -23.742 12.864 1.00 16.99 ? 101 ALA   C O   1 
ATOM   1865 C  CB  . ALA   B 1 95  ? 37.080 -25.802 15.002 1.00 16.25 ? 101 ALA   C CB  1 
ATOM   1866 N  N   . VAL   B 1 96  ? 39.681 -25.646 13.200 1.00 15.72 ? 102 VAL   C N   1 
ATOM   1867 C  CA  . VAL   B 1 96  ? 40.189 -25.693 11.842 1.00 16.89 ? 102 VAL   C CA  1 
ATOM   1868 C  C   . VAL   B 1 96  ? 39.102 -26.443 11.040 1.00 17.56 ? 102 VAL   C C   1 
ATOM   1869 O  O   . VAL   B 1 96  ? 38.772 -27.601 11.349 1.00 17.47 ? 102 VAL   C O   1 
ATOM   1870 C  CB  . VAL   B 1 96  ? 41.543 -26.431 11.789 1.00 18.10 ? 102 VAL   C CB  1 
ATOM   1871 C  CG1 . VAL   B 1 96  ? 41.974 -26.620 10.338 1.00 19.23 ? 102 VAL   C CG1 1 
ATOM   1872 C  CG2 . VAL   B 1 96  ? 42.589 -25.642 12.574 1.00 18.58 ? 102 VAL   C CG2 1 
ATOM   1873 N  N   . GLY   B 1 97  ? 38.479 -25.738 10.102 1.00 18.55 ? 103 GLY   C N   1 
ATOM   1874 C  CA  . GLY   B 1 97  ? 37.396 -26.331 9.327  1.00 19.22 ? 103 GLY   C CA  1 
ATOM   1875 C  C   . GLY   B 1 97  ? 36.736 -25.375 8.353  1.00 19.82 ? 103 GLY   C C   1 
ATOM   1876 O  O   . GLY   B 1 97  ? 37.027 -24.169 8.362  1.00 20.61 ? 103 GLY   C O   1 
ATOM   1877 N  N   . HIS   B 1 98  ? 35.834 -25.918 7.513  1.00 18.62 ? 104 HIS   C N   1 
ATOM   1878 C  CA  . HIS   B 1 98  ? 35.149 -25.148 6.483  1.00 19.33 ? 104 HIS   C CA  1 
ATOM   1879 C  C   . HIS   B 1 98  ? 33.871 -24.445 7.010  1.00 19.17 ? 104 HIS   C C   1 
ATOM   1880 O  O   . HIS   B 1 98  ? 33.068 -25.069 7.714  1.00 19.00 ? 104 HIS   C O   1 
ATOM   1881 C  CB  . HIS   B 1 98  ? 34.768 -26.060 5.309  1.00 21.16 ? 104 HIS   C CB  1 
ATOM   1882 C  CG  . HIS   B 1 98  ? 34.187 -25.287 4.164  1.00 25.95 ? 104 HIS   C CG  1 
ATOM   1883 N  ND1 . HIS   B 1 98  ? 34.939 -24.339 3.463  1.00 28.59 ? 104 HIS   C ND1 1 
ATOM   1884 C  CD2 . HIS   B 1 98  ? 32.926 -25.300 3.669  1.00 28.08 ? 104 HIS   C CD2 1 
ATOM   1885 C  CE1 . HIS   B 1 98  ? 34.116 -23.814 2.560  1.00 29.98 ? 104 HIS   C CE1 1 
ATOM   1886 N  NE2 . HIS   B 1 98  ? 32.894 -24.376 2.629  1.00 29.73 ? 104 HIS   C NE2 1 
ATOM   1887 N  N   . SER   B 1 99  ? 33.664 -23.184 6.589  1.00 19.52 ? 105 SER   C N   1 
ATOM   1888 C  CA  . SER   B 1 99  ? 32.481 -22.392 6.986  1.00 20.02 ? 105 SER   C CA  1 
ATOM   1889 C  C   . SER   B 1 99  ? 32.203 -21.251 5.975  1.00 21.38 ? 105 SER   C C   1 
ATOM   1890 O  O   . SER   B 1 99  ? 33.020 -20.328 5.867  1.00 22.59 ? 105 SER   C O   1 
ATOM   1891 C  CB  . SER   B 1 99  ? 32.706 -21.799 8.376  1.00 20.59 ? 105 SER   C CB  1 
ATOM   1892 O  OG  . SER   B 1 99  ? 31.671 -20.925 8.808  1.00 24.29 ? 105 SER   C OG  1 
ATOM   1893 N  N   . GLU   B 1 100 ? 31.065 -21.339 5.246  1.00 20.49 ? 106 GLU   C N   1 
ATOM   1894 C  CA  . GLU   B 1 100 ? 30.571 -20.333 4.290  1.00 20.79 ? 106 GLU   C CA  1 
ATOM   1895 C  C   . GLU   B 1 100 ? 29.485 -19.498 5.035  1.00 20.19 ? 106 GLU   C C   1 
ATOM   1896 O  O   . GLU   B 1 100 ? 28.878 -19.994 6.018  1.00 19.52 ? 106 GLU   C O   1 
ATOM   1897 C  CB  . GLU   B 1 100 ? 29.814 -21.038 3.116  1.00 23.45 ? 106 GLU   C CB  1 
ATOM   1898 C  CG  . GLU   B 1 100 ? 30.587 -22.075 2.321  1.00 31.50 ? 106 GLU   C CG  1 
ATOM   1899 C  CD  . GLU   B 1 100 ? 31.474 -21.535 1.223  1.00 37.15 ? 106 GLU   C CD  1 
ATOM   1900 O  OE1 . GLU   B 1 100 ? 32.077 -22.355 0.498  1.00 37.83 ? 106 GLU   C OE1 1 
ATOM   1901 O  OE2 . GLU   B 1 100 ? 31.568 -20.295 1.086  1.00 38.71 ? 106 GLU   C OE2 1 
ATOM   1902 N  N   . PRO   B 1 101 ? 29.107 -18.310 4.518  1.00 20.16 ? 107 PRO   C N   1 
ATOM   1903 C  CA  . PRO   B 1 101 ? 28.013 -17.554 5.180  1.00 19.92 ? 107 PRO   C CA  1 
ATOM   1904 C  C   . PRO   B 1 101 ? 26.750 -18.388 5.465  1.00 19.85 ? 107 PRO   C C   1 
ATOM   1905 O  O   . PRO   B 1 101 ? 26.190 -18.289 6.555  1.00 20.82 ? 107 PRO   C O   1 
ATOM   1906 C  CB  . PRO   B 1 101 ? 27.726 -16.407 4.186  1.00 21.53 ? 107 PRO   C CB  1 
ATOM   1907 C  CG  . PRO   B 1 101 ? 29.047 -16.165 3.516  1.00 22.31 ? 107 PRO   C CG  1 
ATOM   1908 C  CD  . PRO   B 1 101 ? 29.701 -17.546 3.388  1.00 20.70 ? 107 PRO   C CD  1 
ATOM   1909 N  N   . GLY   B 1 102 ? 26.325 -19.236 4.521  1.00 18.14 ? 108 GLY   C N   1 
ATOM   1910 C  CA  . GLY   B 1 102 ? 25.103 -20.036 4.697  1.00 17.80 ? 108 GLY   C CA  1 
ATOM   1911 C  C   . GLY   B 1 102 ? 25.200 -21.145 5.732  1.00 18.28 ? 108 GLY   C C   1 
ATOM   1912 O  O   . GLY   B 1 102 ? 24.187 -21.770 6.095  1.00 18.95 ? 108 GLY   C O   1 
ATOM   1913 N  N   . ASP   B 1 103 ? 26.436 -21.454 6.176  1.00 17.10 ? 109 ASP   C N   1 
ATOM   1914 C  CA  . ASP   B 1 103 ? 26.635 -22.476 7.199  1.00 16.65 ? 109 ASP   C CA  1 
ATOM   1915 C  C   . ASP   B 1 103 ? 26.237 -21.977 8.609  1.00 17.05 ? 109 ASP   C C   1 
ATOM   1916 O  O   . ASP   B 1 103 ? 26.085 -22.803 9.515  1.00 16.27 ? 109 ASP   C O   1 
ATOM   1917 C  CB  . ASP   B 1 103 ? 28.113 -22.951 7.230  1.00 16.48 ? 109 ASP   C CB  1 
ATOM   1918 C  CG  . ASP   B 1 103 ? 28.436 -23.800 6.021  1.00 18.72 ? 109 ASP   C CG  1 
ATOM   1919 O  OD1 . ASP   B 1 103 ? 27.575 -24.573 5.601  1.00 19.21 ? 109 ASP   C OD1 1 
ATOM   1920 O  OD2 . ASP   B 1 103 ? 29.533 -23.662 5.478  1.00 20.19 ? 109 ASP   C OD2 1 
ATOM   1921 N  N   . CYS   B 1 104 ? 26.070 -20.637 8.806  1.00 16.41 ? 110 CYS   C N   1 
ATOM   1922 C  CA  . CYS   B 1 104 ? 25.680 -20.074 10.111 1.00 17.12 ? 110 CYS   C CA  1 
ATOM   1923 C  C   . CYS   B 1 104 ? 24.417 -20.761 10.632 1.00 16.69 ? 110 CYS   C C   1 
ATOM   1924 O  O   . CYS   B 1 104 ? 23.512 -21.016 9.838  1.00 17.68 ? 110 CYS   C O   1 
ATOM   1925 C  CB  . CYS   B 1 104 ? 25.487 -18.571 10.024 1.00 18.50 ? 110 CYS   C CB  1 
ATOM   1926 S  SG  . CYS   B 1 104 ? 27.025 -17.630 9.926  1.00 20.58 ? 110 CYS   C SG  1 
ATOM   1927 N  N   . GLY   B 1 105 ? 24.409 -21.125 11.901 1.00 15.60 ? 111 GLY   C N   1 
ATOM   1928 C  CA  . GLY   B 1 105 ? 23.267 -21.833 12.478 1.00 16.33 ? 111 GLY   C CA  1 
ATOM   1929 C  C   . GLY   B 1 105 ? 23.466 -23.333 12.678 1.00 16.17 ? 111 GLY   C C   1 
ATOM   1930 O  O   . GLY   B 1 105 ? 22.704 -23.970 13.416 1.00 16.48 ? 111 GLY   C O   1 
ATOM   1931 N  N   . GLY   B 1 106 ? 24.480 -23.906 12.016 1.00 15.68 ? 112 GLY   C N   1 
ATOM   1932 C  CA  . GLY   B 1 106 ? 24.805 -25.332 12.141 1.00 15.71 ? 112 GLY   C CA  1 
ATOM   1933 C  C   . GLY   B 1 106 ? 25.225 -25.627 13.573 1.00 15.03 ? 112 GLY   C C   1 
ATOM   1934 O  O   . GLY   B 1 106 ? 25.921 -24.812 14.189 1.00 15.86 ? 112 GLY   C O   1 
ATOM   1935 N  N   . ILE   B 1 107 ? 24.721 -26.717 14.149 1.00 13.99 ? 113 ILE   C N   1 
ATOM   1936 C  CA  . ILE   B 1 107 ? 25.015 -27.024 15.551 1.00 14.10 ? 113 ILE   C CA  1 
ATOM   1937 C  C   . ILE   B 1 107 ? 26.375 -27.704 15.752 1.00 14.64 ? 113 ILE   C C   1 
ATOM   1938 O  O   . ILE   B 1 107 ? 26.756 -28.605 14.987 1.00 13.70 ? 113 ILE   C O   1 
ATOM   1939 C  CB  . ILE   B 1 107 ? 23.853 -27.908 16.136 1.00 16.68 ? 113 ILE   C CB  1 
ATOM   1940 C  CG1 . ILE   B 1 107 ? 22.612 -27.021 16.516 1.00 18.50 ? 113 ILE   C CG1 1 
ATOM   1941 C  CG2 . ILE   B 1 107 ? 24.300 -28.791 17.336 1.00 17.14 ? 113 ILE   C CG2 1 
ATOM   1942 C  CD1 . ILE   B 1 107 ? 21.341 -27.820 16.875 1.00 21.32 ? 113 ILE   C CD1 1 
ATOM   1943 N  N   . LEU   B 1 108 ? 27.072 -27.301 16.838 1.00 13.78 ? 114 LEU   C N   1 
ATOM   1944 C  CA  . LEU   B 1 108 ? 28.284 -27.963 17.335 1.00 13.70 ? 114 LEU   C CA  1 
ATOM   1945 C  C   . LEU   B 1 108 ? 27.792 -28.731 18.619 1.00 14.19 ? 114 LEU   C C   1 
ATOM   1946 O  O   . LEU   B 1 108 ? 27.139 -28.133 19.484 1.00 13.93 ? 114 LEU   C O   1 
ATOM   1947 C  CB  . LEU   B 1 108 ? 29.345 -26.919 17.724 1.00 15.01 ? 114 LEU   C CB  1 
ATOM   1948 C  CG  . LEU   B 1 108 ? 30.535 -27.451 18.534 1.00 16.49 ? 114 LEU   C CG  1 
ATOM   1949 C  CD1 . LEU   B 1 108 ? 31.444 -28.347 17.666 1.00 17.70 ? 114 LEU   C CD1 1 
ATOM   1950 C  CD2 . LEU   B 1 108 ? 31.327 -26.293 19.140 1.00 17.09 ? 114 LEU   C CD2 1 
ATOM   1951 N  N   . ARG   B 1 109 ? 28.096 -30.042 18.708 1.00 14.14 ? 115 ARG   C N   1 
ATOM   1952 C  CA  . ARG   B 1 109 ? 27.648 -30.868 19.843 1.00 14.51 ? 115 ARG   C CA  1 
ATOM   1953 C  C   . ARG   B 1 109 ? 28.773 -31.748 20.417 1.00 15.33 ? 115 ARG   C C   1 
ATOM   1954 O  O   . ARG   B 1 109 ? 29.642 -32.209 19.665 1.00 16.23 ? 115 ARG   C O   1 
ATOM   1955 C  CB  . ARG   B 1 109 ? 26.493 -31.784 19.402 1.00 16.34 ? 115 ARG   C CB  1 
ATOM   1956 C  CG  . ARG   B 1 109 ? 26.851 -32.763 18.271 1.00 23.50 ? 115 ARG   C CG  1 
ATOM   1957 C  CD  . ARG   B 1 109 ? 25.702 -33.737 17.903 1.00 31.51 ? 115 ARG   C CD  1 
ATOM   1958 N  NE  . ARG   B 1 109 ? 24.399 -33.067 17.821 1.00 38.32 ? 115 ARG   C NE  1 
ATOM   1959 C  CZ  . ARG   B 1 109 ? 23.747 -32.816 16.692 1.00 43.73 ? 115 ARG   C CZ  1 
ATOM   1960 N  NH1 . ARG   B 1 109 ? 24.233 -33.232 15.531 1.00 43.95 ? 115 ARG   C NH1 1 
ATOM   1961 N  NH2 . ARG   B 1 109 ? 22.582 -32.178 16.718 1.00 45.39 ? 115 ARG   C NH2 1 
ATOM   1962 N  N   . CYS   B 1 110 ? 28.717 -32.008 21.753 1.00 15.65 ? 116 CYS   C N   1 
ATOM   1963 C  CA  . CYS   B 1 110 ? 29.672 -32.889 22.452 1.00 15.97 ? 116 CYS   C CA  1 
ATOM   1964 C  C   . CYS   B 1 110 ? 28.846 -34.014 23.137 1.00 17.36 ? 116 CYS   C C   1 
ATOM   1965 O  O   . CYS   B 1 110 ? 27.628 -34.086 22.911 1.00 19.01 ? 116 CYS   C O   1 
ATOM   1966 C  CB  . CYS   B 1 110 ? 30.462 -32.085 23.484 1.00 16.95 ? 116 CYS   C CB  1 
ATOM   1967 S  SG  . CYS   B 1 110 ? 29.406 -31.402 24.785 1.00 17.44 ? 116 CYS   C SG  1 
ATOM   1968 N  N   . GLN   B 1 111 ? 29.462 -34.856 23.992 1.00 17.54 ? 117 GLN   C N   1 
ATOM   1969 C  CA  . GLN   B 1 111 ? 28.705 -35.926 24.678 1.00 19.01 ? 117 GLN   C CA  1 
ATOM   1970 C  C   . GLN   B 1 111 ? 27.590 -35.378 25.607 1.00 20.09 ? 117 GLN   C C   1 
ATOM   1971 O  O   . GLN   B 1 111 ? 26.631 -36.090 25.930 1.00 21.36 ? 117 GLN   C O   1 
ATOM   1972 C  CB  . GLN   B 1 111 ? 29.667 -36.843 25.475 1.00 22.19 ? 117 GLN   C CB  1 
ATOM   1973 C  CG  . GLN   B 1 111 ? 30.343 -36.117 26.642 1.00 27.51 ? 117 GLN   C CG  1 
ATOM   1974 C  CD  . GLN   B 1 111 ? 31.348 -36.973 27.394 1.00 34.73 ? 117 GLN   C CD  1 
ATOM   1975 O  OE1 . GLN   B 1 111 ? 32.564 -36.839 27.207 1.00 36.31 ? 117 GLN   C OE1 1 
ATOM   1976 N  NE2 . GLN   B 1 111 ? 30.861 -37.835 28.291 1.00 34.66 ? 117 GLN   C NE2 1 
ATOM   1977 N  N   . HIS   B 1 112 ? 27.718 -34.124 26.040 1.00 18.81 ? 118 HIS   C N   1 
ATOM   1978 C  CA  . HIS   B 1 112 ? 26.755 -33.521 26.958 1.00 18.31 ? 118 HIS   C CA  1 
ATOM   1979 C  C   . HIS   B 1 112 ? 25.584 -32.811 26.274 1.00 19.35 ? 118 HIS   C C   1 
ATOM   1980 O  O   . HIS   B 1 112 ? 24.597 -32.502 26.956 1.00 20.72 ? 118 HIS   C O   1 
ATOM   1981 C  CB  . HIS   B 1 112 ? 27.475 -32.551 27.905 1.00 19.62 ? 118 HIS   C CB  1 
ATOM   1982 C  CG  . HIS   B 1 112 ? 28.677 -33.147 28.596 1.00 20.68 ? 118 HIS   C CG  1 
ATOM   1983 N  ND1 . HIS   B 1 112 ? 29.977 -32.863 28.168 1.00 21.39 ? 118 HIS   C ND1 1 
ATOM   1984 C  CD2 . HIS   B 1 112 ? 28.740 -33.977 29.675 1.00 20.69 ? 118 HIS   C CD2 1 
ATOM   1985 C  CE1 . HIS   B 1 112 ? 30.785 -33.521 28.990 1.00 22.02 ? 118 HIS   C CE1 1 
ATOM   1986 N  NE2 . HIS   B 1 112 ? 30.090 -34.221 29.911 1.00 21.21 ? 118 HIS   C NE2 1 
ATOM   1987 N  N   . GLY   B 1 113 ? 25.675 -32.520 24.965 1.00 17.90 ? 119 GLY   C N   1 
ATOM   1988 C  CA  . GLY   B 1 113 ? 24.584 -31.812 24.296 1.00 16.68 ? 119 GLY   C CA  1 
ATOM   1989 C  C   . GLY   B 1 113 ? 25.064 -30.737 23.342 1.00 15.42 ? 119 GLY   C C   1 
ATOM   1990 O  O   . GLY   B 1 113 ? 26.169 -30.843 22.802 1.00 15.17 ? 119 GLY   C O   1 
ATOM   1991 N  N   . VAL   B 1 114 ? 24.197 -29.731 23.070 1.00 13.53 ? 120 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 114 ? 24.523 -28.637 22.149 1.00 14.32 ? 120 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 114 ? 25.491 -27.647 22.822 1.00 14.43 ? 120 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 114 ? 25.175 -27.091 23.872 1.00 15.60 ? 120 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 114 ? 23.236 -27.882 21.709 1.00 15.15 ? 120 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 114 ? 23.606 -26.690 20.815 1.00 15.88 ? 120 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 114 ? 22.272 -28.825 20.978 1.00 15.93 ? 120 VAL   C CG2 1 
ATOM   1998 N  N   . VAL   B 1 115 ? 26.621 -27.366 22.159 1.00 14.36 ? 121 VAL   C N   1 
ATOM   1999 C  CA  . VAL   B 1 115 ? 27.643 -26.433 22.667 1.00 15.58 ? 121 VAL   C CA  1 
ATOM   2000 C  C   . VAL   B 1 115 ? 27.441 -25.024 22.143 1.00 16.59 ? 121 VAL   C C   1 
ATOM   2001 O  O   . VAL   B 1 115 ? 27.646 -24.027 22.860 1.00 17.67 ? 121 VAL   C O   1 
ATOM   2002 C  CB  . VAL   B 1 115 ? 29.053 -26.967 22.282 1.00 16.08 ? 121 VAL   C CB  1 
ATOM   2003 C  CG1 . VAL   B 1 115 ? 30.151 -25.946 22.611 1.00 15.59 ? 121 VAL   C CG1 1 
ATOM   2004 C  CG2 . VAL   B 1 115 ? 29.310 -28.320 22.938 1.00 17.15 ? 121 VAL   C CG2 1 
ATOM   2005 N  N   . GLY   B 1 116 ? 27.097 -24.934 20.867 1.00 15.73 ? 122 GLY   C N   1 
ATOM   2006 C  CA  . GLY   B 1 116 ? 26.886 -23.645 20.236 1.00 16.67 ? 122 GLY   C CA  1 
ATOM   2007 C  C   . GLY   B 1 116 ? 26.506 -23.773 18.776 1.00 16.19 ? 122 GLY   C C   1 
ATOM   2008 O  O   . GLY   B 1 116 ? 26.145 -24.869 18.335 1.00 16.14 ? 122 GLY   C O   1 
ATOM   2009 N  N   . ILE   B 1 117 ? 26.573 -22.645 18.014 1.00 14.65 ? 123 ILE   C N   1 
ATOM   2010 C  CA  . ILE   B 1 117 ? 26.193 -22.654 16.611 1.00 14.00 ? 123 ILE   C CA  1 
ATOM   2011 C  C   . ILE   B 1 117 ? 27.205 -21.916 15.757 1.00 14.06 ? 123 ILE   C C   1 
ATOM   2012 O  O   . ILE   B 1 117 ? 27.826 -20.948 16.213 1.00 14.56 ? 123 ILE   C O   1 
ATOM   2013 C  CB  . ILE   B 1 117 ? 24.802 -21.979 16.360 1.00 15.65 ? 123 ILE   C CB  1 
ATOM   2014 C  CG1 . ILE   B 1 117 ? 24.719 -20.557 16.962 1.00 16.83 ? 123 ILE   C CG1 1 
ATOM   2015 C  CG2 . ILE   B 1 117 ? 23.622 -22.867 16.843 1.00 15.92 ? 123 ILE   C CG2 1 
ATOM   2016 C  CD1 . ILE   B 1 117 ? 23.303 -19.785 16.544 1.00 17.98 ? 123 ILE   C CD1 1 
ATOM   2017 N  N   . VAL   B 1 118 ? 27.374 -22.345 14.497 1.00 13.87 ? 124 VAL   C N   1 
ATOM   2018 C  CA  . VAL   B 1 118 ? 28.300 -21.646 13.572 1.00 14.13 ? 124 VAL   C CA  1 
ATOM   2019 C  C   . VAL   B 1 118 ? 27.948 -20.142 13.476 1.00 14.97 ? 124 VAL   C C   1 
ATOM   2020 O  O   . VAL   B 1 118 ? 26.772 -19.797 13.359 1.00 14.81 ? 124 VAL   C O   1 
ATOM   2021 C  CB  . VAL   B 1 118 ? 28.287 -22.309 12.160 1.00 15.06 ? 124 VAL   C CB  1 
ATOM   2022 C  CG1 . VAL   B 1 118 ? 29.139 -21.525 11.149 1.00 16.72 ? 124 VAL   C CG1 1 
ATOM   2023 C  CG2 . VAL   B 1 118 ? 28.758 -23.756 12.240 1.00 15.22 ? 124 VAL   C CG2 1 
ATOM   2024 N  N   . SER   B 1 119 ? 28.975 -19.249 13.559 1.00 15.17 ? 125 SER   C N   1 
ATOM   2025 C  CA  . SER   B 1 119 ? 28.741 -17.819 13.483 1.00 15.73 ? 125 SER   C CA  1 
ATOM   2026 C  C   . SER   B 1 119 ? 29.751 -17.118 12.554 1.00 15.63 ? 125 SER   C C   1 
ATOM   2027 O  O   . SER   B 1 119 ? 29.433 -16.064 11.984 1.00 16.04 ? 125 SER   C O   1 
ATOM   2028 C  CB  . SER   B 1 119 ? 28.803 -17.203 14.885 1.00 17.65 ? 125 SER   C CB  1 
ATOM   2029 O  OG  . SER   B 1 119 ? 28.654 -15.783 14.897 1.00 19.55 ? 125 SER   C OG  1 
ATOM   2030 N  N   . THR   B 1 120 ? 30.975 -17.685 12.411 1.00 14.28 ? 126 THR   C N   1 
ATOM   2031 C  CA  . THR   B 1 120 ? 31.989 -17.040 11.572 1.00 15.80 ? 126 THR   C CA  1 
ATOM   2032 C  C   . THR   B 1 120 ? 32.733 -18.081 10.692 1.00 17.35 ? 126 THR   C C   1 
ATOM   2033 O  O   . THR   B 1 120 ? 32.683 -19.282 10.977 1.00 17.68 ? 126 THR   C O   1 
ATOM   2034 C  CB  . THR   B 1 120 ? 33.024 -16.245 12.453 1.00 17.11 ? 126 THR   C CB  1 
ATOM   2035 O  OG1 . THR   B 1 120 ? 33.973 -17.146 13.049 1.00 17.11 ? 126 THR   C OG1 1 
ATOM   2036 C  CG2 . THR   B 1 120 ? 32.393 -15.327 13.474 1.00 17.76 ? 126 THR   C CG2 1 
ATOM   2037 N  N   . GLY   B 1 121 ? 33.404 -17.580 9.652  1.00 19.20 ? 127 GLY   C N   1 
ATOM   2038 C  CA  . GLY   B 1 121 ? 34.197 -18.396 8.733  1.00 21.24 ? 127 GLY   C CA  1 
ATOM   2039 C  C   . GLY   B 1 121 ? 35.229 -17.562 7.990  1.00 24.39 ? 127 GLY   C C   1 
ATOM   2040 O  O   . GLY   B 1 121 ? 35.023 -16.381 7.750  1.00 24.10 ? 127 GLY   C O   1 
ATOM   2041 N  N   . GLY   B 1 122 ? 36.335 -18.179 7.618  1.00 27.09 ? 128 GLY   C N   1 
ATOM   2042 C  CA  . GLY   B 1 122 ? 37.404 -17.485 6.892  1.00 28.68 ? 128 GLY   C CA  1 
ATOM   2043 C  C   . GLY   B 1 122 ? 38.769 -18.026 7.242  1.00 28.98 ? 128 GLY   C C   1 
ATOM   2044 O  O   . GLY   B 1 122 ? 38.947 -18.542 8.344  1.00 29.34 ? 128 GLY   C O   1 
ATOM   2045 N  N   . ASN   B 1 123 ? 39.742 -17.922 6.311  1.00 28.80 ? 129 ASN   C N   1 
ATOM   2046 C  CA  . ASN   B 1 123 ? 41.103 -18.417 6.532  1.00 28.69 ? 129 ASN   C CA  1 
ATOM   2047 C  C   . ASN   B 1 123 ? 41.163 -19.879 6.974  1.00 27.20 ? 129 ASN   C C   1 
ATOM   2048 O  O   . ASN   B 1 123 ? 42.058 -20.253 7.732  1.00 27.65 ? 129 ASN   C O   1 
ATOM   2049 C  CB  . ASN   B 1 123 ? 41.867 -17.517 7.516  1.00 31.99 ? 129 ASN   C CB  1 
ATOM   2050 C  CG  . ASN   B 1 123 ? 42.475 -16.280 6.885  1.00 38.91 ? 129 ASN   C CG  1 
ATOM   2051 O  OD1 . ASN   B 1 123 ? 42.750 -16.205 5.673  1.00 40.05 ? 129 ASN   C OD1 1 
ATOM   2052 N  ND2 . ASN   B 1 123 ? 42.747 -15.279 7.705  1.00 41.20 ? 129 ASN   C ND2 1 
ATOM   2053 N  N   . GLY   B 1 124 ? 40.223 -20.700 6.498  1.00 25.14 ? 130 GLY   C N   1 
ATOM   2054 C  CA  . GLY   B 1 124 ? 40.213 -22.110 6.863  1.00 24.24 ? 130 GLY   C CA  1 
ATOM   2055 C  C   . GLY   B 1 124 ? 39.853 -22.359 8.318  1.00 22.70 ? 130 GLY   C C   1 
ATOM   2056 O  O   . GLY   B 1 124 ? 40.172 -23.413 8.870  1.00 22.66 ? 130 GLY   C O   1 
ATOM   2057 N  N   . LEU   B 1 125 ? 39.168 -21.384 8.962  1.00 20.79 ? 131 LEU   C N   1 
ATOM   2058 C  CA  . LEU   B 1 125 ? 38.762 -21.533 10.352 1.00 20.26 ? 131 LEU   C CA  1 
ATOM   2059 C  C   . LEU   B 1 125 ? 37.245 -21.374 10.445 1.00 19.71 ? 131 LEU   C C   1 
ATOM   2060 O  O   . LEU   B 1 125 ? 36.641 -20.670 9.630  1.00 20.56 ? 131 LEU   C O   1 
ATOM   2061 C  CB  . LEU   B 1 125 ? 39.406 -20.465 11.231 1.00 21.06 ? 131 LEU   C CB  1 
ATOM   2062 C  CG  . LEU   B 1 125 ? 40.920 -20.462 11.275 1.00 23.82 ? 131 LEU   C CG  1 
ATOM   2063 C  CD1 . LEU   B 1 125 ? 41.444 -19.103 11.743 1.00 25.59 ? 131 LEU   C CD1 1 
ATOM   2064 C  CD2 . LEU   B 1 125 ? 41.424 -21.582 12.133 1.00 23.82 ? 131 LEU   C CD2 1 
ATOM   2065 N  N   . VAL   B 1 126 ? 36.624 -22.122 11.354 1.00 17.07 ? 132 VAL   C N   1 
ATOM   2066 C  CA  . VAL   B 1 126 ? 35.203 -21.997 11.616 1.00 16.64 ? 132 VAL   C CA  1 
ATOM   2067 C  C   . VAL   B 1 126 ? 35.047 -21.484 13.061 1.00 15.71 ? 132 VAL   C C   1 
ATOM   2068 O  O   . VAL   B 1 126 ? 35.726 -21.970 13.981 1.00 16.29 ? 132 VAL   C O   1 
ATOM   2069 C  CB  . VAL   B 1 126 ? 34.406 -23.319 11.421 1.00 17.72 ? 132 VAL   C CB  1 
ATOM   2070 C  CG1 . VAL   B 1 126 ? 35.052 -24.480 12.153 1.00 18.74 ? 132 VAL   C CG1 1 
ATOM   2071 C  CG2 . VAL   B 1 126 ? 32.941 -23.154 11.850 1.00 17.48 ? 132 VAL   C CG2 1 
ATOM   2072 N  N   . GLY   B 1 127 ? 34.130 -20.533 13.256 1.00 13.99 ? 133 GLY   C N   1 
ATOM   2073 C  CA  . GLY   B 1 127 ? 33.912 -20.007 14.592 1.00 14.18 ? 133 GLY   C CA  1 
ATOM   2074 C  C   . GLY   B 1 127 ? 32.496 -20.311 15.073 1.00 15.37 ? 133 GLY   C C   1 
ATOM   2075 O  O   . GLY   B 1 127 ? 31.536 -20.215 14.299 1.00 15.87 ? 133 GLY   C O   1 
ATOM   2076 N  N   . PHE   B 1 128 ? 32.365 -20.670 16.366 1.00 14.14 ? 134 PHE   C N   1 
ATOM   2077 C  CA  . PHE   B 1 128 ? 31.069 -21.034 16.951 1.00 14.42 ? 134 PHE   C CA  1 
ATOM   2078 C  C   . PHE   B 1 128 ? 30.735 -20.092 18.115 1.00 14.99 ? 134 PHE   C C   1 
ATOM   2079 O  O   . PHE   B 1 128 ? 31.596 -19.832 18.970 1.00 15.21 ? 134 PHE   C O   1 
ATOM   2080 C  CB  . PHE   B 1 128 ? 31.135 -22.467 17.516 1.00 14.16 ? 134 PHE   C CB  1 
ATOM   2081 C  CG  . PHE   B 1 128 ? 31.657 -23.506 16.531 1.00 13.96 ? 134 PHE   C CG  1 
ATOM   2082 C  CD1 . PHE   B 1 128 ? 30.799 -24.132 15.645 1.00 14.30 ? 134 PHE   C CD1 1 
ATOM   2083 C  CD2 . PHE   B 1 128 ? 32.992 -23.904 16.558 1.00 14.72 ? 134 PHE   C CD2 1 
ATOM   2084 C  CE1 . PHE   B 1 128 ? 31.268 -25.085 14.757 1.00 15.60 ? 134 PHE   C CE1 1 
ATOM   2085 C  CE2 . PHE   B 1 128 ? 33.471 -24.881 15.672 1.00 16.05 ? 134 PHE   C CE2 1 
ATOM   2086 C  CZ  . PHE   B 1 128 ? 32.606 -25.460 14.777 1.00 15.85 ? 134 PHE   C CZ  1 
ATOM   2087 N  N   . ALA   B 1 129 ? 29.495 -19.603 18.144 1.00 13.86 ? 135 ALA   C N   1 
ATOM   2088 C  CA  . ALA   B 1 129 ? 29.039 -18.773 19.258 1.00 14.77 ? 135 ALA   C CA  1 
ATOM   2089 C  C   . ALA   B 1 129 ? 28.635 -19.741 20.392 1.00 15.61 ? 135 ALA   C C   1 
ATOM   2090 O  O   . ALA   B 1 129 ? 27.704 -20.557 20.227 1.00 15.27 ? 135 ALA   C O   1 
ATOM   2091 C  CB  . ALA   B 1 129 ? 27.831 -17.936 18.824 1.00 14.43 ? 135 ALA   C CB  1 
ATOM   2092 N  N   . ASP   B 1 130 ? 29.333 -19.661 21.530 1.00 15.59 ? 136 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 130 ? 29.050 -20.571 22.649 1.00 16.09 ? 136 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 130 ? 27.709 -20.220 23.298 1.00 16.55 ? 136 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 130 ? 27.359 -19.037 23.377 1.00 16.68 ? 136 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 130 ? 30.147 -20.382 23.705 1.00 17.90 ? 136 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 130 ? 30.087 -21.298 24.910 1.00 21.31 ? 136 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 130 ? 29.847 -22.512 24.731 1.00 20.40 ? 136 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 130 ? 30.270 -20.801 26.028 1.00 23.68 ? 136 ASP   C OD2 1 
ATOM   2100 N  N   . VAL   B 1 131 ? 26.986 -21.238 23.818 1.00 16.26 ? 137 VAL   C N   1 
ATOM   2101 C  CA  . VAL   B 1 131 ? 25.757 -20.977 24.595 1.00 15.70 ? 137 VAL   C CA  1 
ATOM   2102 C  C   . VAL   B 1 131 ? 25.814 -21.658 25.994 1.00 15.90 ? 137 VAL   C C   1 
ATOM   2103 O  O   . VAL   B 1 131 ? 24.855 -21.543 26.746 1.00 17.00 ? 137 VAL   C O   1 
ATOM   2104 C  CB  . VAL   B 1 131 ? 24.468 -21.407 23.850 1.00 16.70 ? 137 VAL   C CB  1 
ATOM   2105 C  CG1 . VAL   B 1 131 ? 24.305 -20.626 22.545 1.00 16.80 ? 137 VAL   C CG1 1 
ATOM   2106 C  CG2 . VAL   B 1 131 ? 24.447 -22.922 23.610 1.00 17.93 ? 137 VAL   C CG2 1 
ATOM   2107 N  N   . ARG   B 1 132 ? 26.907 -22.417 26.315 1.00 15.60 ? 138 ARG   C N   1 
ATOM   2108 C  CA  . ARG   B 1 132 ? 26.994 -23.170 27.581 1.00 14.57 ? 138 ARG   C CA  1 
ATOM   2109 C  C   . ARG   B 1 132 ? 26.941 -22.311 28.864 1.00 15.87 ? 138 ARG   C C   1 
ATOM   2110 O  O   . ARG   B 1 132 ? 26.675 -22.856 29.940 1.00 17.19 ? 138 ARG   C O   1 
ATOM   2111 C  CB  . ARG   B 1 132 ? 28.235 -24.066 27.603 1.00 14.03 ? 138 ARG   C CB  1 
ATOM   2112 C  CG  . ARG   B 1 132 ? 28.262 -25.058 26.444 1.00 14.80 ? 138 ARG   C CG  1 
ATOM   2113 C  CD  . ARG   B 1 132 ? 29.585 -25.830 26.457 1.00 16.26 ? 138 ARG   C CD  1 
ATOM   2114 N  NE  . ARG   B 1 132 ? 30.686 -24.973 25.979 1.00 15.51 ? 138 ARG   C NE  1 
ATOM   2115 C  CZ  . ARG   B 1 132 ? 31.939 -25.396 25.837 1.00 18.03 ? 138 ARG   C CZ  1 
ATOM   2116 N  NH1 . ARG   B 1 132 ? 32.289 -26.609 26.246 1.00 17.04 ? 138 ARG   C NH1 1 
ATOM   2117 N  NH2 . ARG   B 1 132 ? 32.873 -24.580 25.354 1.00 17.62 ? 138 ARG   C NH2 1 
ATOM   2118 N  N   . ASP   B 1 133 ? 27.274 -21.024 28.772 1.00 15.21 ? 139 ASP   C N   1 
ATOM   2119 C  CA  . ASP   B 1 133 ? 27.227 -20.115 29.940 1.00 16.22 ? 139 ASP   C CA  1 
ATOM   2120 C  C   . ASP   B 1 133 ? 25.813 -19.533 30.202 1.00 17.57 ? 139 ASP   C C   1 
ATOM   2121 O  O   . ASP   B 1 133 ? 25.590 -18.893 31.246 1.00 18.09 ? 139 ASP   C O   1 
ATOM   2122 C  CB  . ASP   B 1 133 ? 28.224 -18.933 29.768 1.00 17.86 ? 139 ASP   C CB  1 
ATOM   2123 C  CG  . ASP   B 1 133 ? 27.822 -18.029 28.604 1.00 22.68 ? 139 ASP   C CG  1 
ATOM   2124 O  OD1 . ASP   B 1 133 ? 27.527 -18.569 27.515 1.00 21.74 ? 139 ASP   C OD1 1 
ATOM   2125 O  OD2 . ASP   B 1 133 ? 27.756 -16.781 28.803 1.00 25.59 ? 139 ASP   C OD2 1 
ATOM   2126 N  N   . LEU   B 1 134 ? 24.859 -19.767 29.264 1.00 17.28 ? 140 LEU   C N   1 
ATOM   2127 C  CA  . LEU   B 1 134 ? 23.498 -19.206 29.376 1.00 17.17 ? 140 LEU   C CA  1 
ATOM   2128 C  C   . LEU   B 1 134 ? 22.640 -20.203 30.160 1.00 17.32 ? 140 LEU   C C   1 
ATOM   2129 O  O   . LEU   B 1 134 ? 21.801 -20.915 29.595 1.00 16.73 ? 140 LEU   C O   1 
ATOM   2130 C  CB  . LEU   B 1 134 ? 22.938 -18.967 27.961 1.00 17.43 ? 140 LEU   C CB  1 
ATOM   2131 C  CG  . LEU   B 1 134 ? 23.767 -17.989 27.074 1.00 19.38 ? 140 LEU   C CG  1 
ATOM   2132 C  CD1 . LEU   B 1 134 ? 23.137 -17.826 25.670 1.00 19.96 ? 140 LEU   C CD1 1 
ATOM   2133 C  CD2 . LEU   B 1 134 ? 23.898 -16.583 27.748 1.00 19.55 ? 140 LEU   C CD2 1 
ATOM   2134 N  N   . LEU   B 1 135 ? 22.870 -20.257 31.489 1.00 17.52 ? 141 LEU   C N   1 
ATOM   2135 C  CA  . LEU   B 1 135 ? 22.209 -21.253 32.342 1.00 18.87 ? 141 LEU   C CA  1 
ATOM   2136 C  C   . LEU   B 1 135 ? 20.693 -21.122 32.394 1.00 18.75 ? 141 LEU   C C   1 
ATOM   2137 O  O   . LEU   B 1 135 ? 20.002 -22.123 32.623 1.00 19.34 ? 141 LEU   C O   1 
ATOM   2138 C  CB  . LEU   B 1 135 ? 22.802 -21.282 33.766 1.00 19.56 ? 141 LEU   C CB  1 
ATOM   2139 C  CG  . LEU   B 1 135 ? 24.341 -21.319 33.850 1.00 20.78 ? 141 LEU   C CG  1 
ATOM   2140 C  CD1 . LEU   B 1 135 ? 24.830 -21.337 35.315 1.00 21.68 ? 141 LEU   C CD1 1 
ATOM   2141 C  CD2 . LEU   B 1 135 ? 24.936 -22.488 33.035 1.00 20.49 ? 141 LEU   C CD2 1 
ATOM   2142 N  N   . TRP   B 1 136 ? 20.186 -19.899 32.171 1.00 18.84 ? 142 TRP   C N   1 
ATOM   2143 C  CA  . TRP   B 1 136 ? 18.744 -19.609 32.187 1.00 19.78 ? 142 TRP   C CA  1 
ATOM   2144 C  C   . TRP   B 1 136 ? 17.970 -20.328 31.055 1.00 19.40 ? 142 TRP   C C   1 
ATOM   2145 O  O   . TRP   B 1 136 ? 16.744 -20.471 31.142 1.00 20.18 ? 142 TRP   C O   1 
ATOM   2146 C  CB  . TRP   B 1 136 ? 18.482 -18.099 32.173 1.00 20.18 ? 142 TRP   C CB  1 
ATOM   2147 C  CG  . TRP   B 1 136 ? 19.171 -17.353 31.074 1.00 20.20 ? 142 TRP   C CG  1 
ATOM   2148 C  CD1 . TRP   B 1 136 ? 20.360 -16.683 31.149 1.00 20.67 ? 142 TRP   C CD1 1 
ATOM   2149 C  CD2 . TRP   B 1 136 ? 18.673 -17.138 29.733 1.00 20.47 ? 142 TRP   C CD2 1 
ATOM   2150 N  NE1 . TRP   B 1 136 ? 20.633 -16.056 29.939 1.00 20.88 ? 142 TRP   C NE1 1 
ATOM   2151 C  CE2 . TRP   B 1 136 ? 19.614 -16.327 29.055 1.00 21.37 ? 142 TRP   C CE2 1 
ATOM   2152 C  CE3 . TRP   B 1 136 ? 17.510 -17.531 29.055 1.00 20.99 ? 142 TRP   C CE3 1 
ATOM   2153 C  CZ2 . TRP   B 1 136 ? 19.441 -15.930 27.718 1.00 21.98 ? 142 TRP   C CZ2 1 
ATOM   2154 C  CZ3 . TRP   B 1 136 ? 17.320 -17.098 27.751 1.00 22.04 ? 142 TRP   C CZ3 1 
ATOM   2155 C  CH2 . TRP   B 1 136 ? 18.276 -16.312 27.097 1.00 22.19 ? 142 TRP   C CH2 1 
ATOM   2156 N  N   . LEU   B 1 137 ? 18.686 -20.827 30.026 1.00 18.04 ? 143 LEU   C N   1 
ATOM   2157 C  CA  . LEU   B 1 137 ? 18.008 -21.582 28.950 1.00 18.82 ? 143 LEU   C CA  1 
ATOM   2158 C  C   . LEU   B 1 137 ? 17.371 -22.877 29.493 1.00 20.71 ? 143 LEU   C C   1 
ATOM   2159 O  O   . LEU   B 1 137 ? 16.458 -23.397 28.864 1.00 21.81 ? 143 LEU   C O   1 
ATOM   2160 C  CB  . LEU   B 1 137 ? 18.967 -21.948 27.805 1.00 18.67 ? 143 LEU   C CB  1 
ATOM   2161 C  CG  . LEU   B 1 137 ? 19.470 -20.793 26.924 1.00 19.14 ? 143 LEU   C CG  1 
ATOM   2162 C  CD1 . LEU   B 1 137 ? 20.553 -21.267 25.944 1.00 18.41 ? 143 LEU   C CD1 1 
ATOM   2163 C  CD2 . LEU   B 1 137 ? 18.330 -20.178 26.105 1.00 20.31 ? 143 LEU   C CD2 1 
ATOM   2164 N  N   . ASP   B 1 138 ? 17.886 -23.421 30.624 1.00 20.88 ? 144 ASP   C N   1 
ATOM   2165 C  CA  . ASP   B 1 138 ? 17.403 -24.674 31.208 1.00 22.60 ? 144 ASP   C CA  1 
ATOM   2166 C  C   . ASP   B 1 138 ? 16.161 -24.516 32.088 1.00 26.10 ? 144 ASP   C C   1 
ATOM   2167 O  O   . ASP   B 1 138 ? 15.712 -25.516 32.653 1.00 25.52 ? 144 ASP   C O   1 
ATOM   2168 C  CB  . ASP   B 1 138 ? 18.498 -25.333 32.068 1.00 22.78 ? 144 ASP   C CB  1 
ATOM   2169 C  CG  . ASP   B 1 138 ? 19.736 -25.773 31.304 1.00 25.08 ? 144 ASP   C CG  1 
ATOM   2170 O  OD1 . ASP   B 1 138 ? 19.680 -25.845 30.050 1.00 23.45 ? 144 ASP   C OD1 1 
ATOM   2171 O  OD2 . ASP   B 1 138 ? 20.763 -26.056 31.959 1.00 27.54 ? 144 ASP   C OD2 1 
ATOM   2172 N  N   . GLU   B 1 139 ? 15.634 -23.288 32.252 1.00 29.39 ? 145 GLU   C N   1 
ATOM   2173 C  CA  . GLU   B 1 139 ? 14.474 -23.085 33.137 1.00 33.95 ? 145 GLU   C CA  1 
ATOM   2174 C  C   . GLU   B 1 139 ? 13.490 -21.996 32.611 1.00 38.23 ? 145 GLU   C C   1 
ATOM   2175 O  O   . GLU   B 1 139 ? 13.776 -21.350 31.603 1.00 39.01 ? 145 GLU   C O   1 
ATOM   2176 C  CB  . GLU   B 1 139 ? 15.020 -22.670 34.521 1.00 36.99 ? 145 GLU   C CB  1 
ATOM   2177 C  CG  . GLU   B 1 139 ? 15.646 -21.283 34.492 1.00 43.39 ? 145 GLU   C CG  1 
ATOM   2178 C  CD  . GLU   B 1 139 ? 16.691 -20.981 35.547 1.00 52.71 ? 145 GLU   C CD  1 
ATOM   2179 O  OE1 . GLU   B 1 139 ? 17.051 -19.790 35.697 1.00 53.60 ? 145 GLU   C OE1 1 
ATOM   2180 O  OE2 . GLU   B 1 139 ? 17.150 -21.932 36.221 1.00 56.39 ? 145 GLU   C OE2 1 
ATOM   2181 N  N   . GLU   B 1 140 ? 12.372 -21.749 33.348 1.00 40.90 ? 146 GLU   C N   1 
ATOM   2182 C  CA  . GLU   B 1 140 ? 11.386 -20.674 33.107 1.00 43.26 ? 146 GLU   C CA  1 
ATOM   2183 C  C   . GLU   B 1 140 ? 11.122 -20.389 31.624 1.00 45.14 ? 146 GLU   C C   1 
ATOM   2184 O  O   . GLU   B 1 140 ? 10.056 -19.884 31.268 1.00 46.32 ? 146 GLU   C O   1 
ATOM   2185 C  CB  . GLU   B 1 140 ? 11.825 -19.395 33.882 1.00 46.35 ? 146 GLU   C CB  1 
ATOM   2186 C  CG  . GLU   B 1 140 ? 11.569 -18.025 33.255 1.00 53.10 ? 146 GLU   C CG  1 
ATOM   2187 C  CD  . GLU   B 1 140 ? 10.193 -17.408 33.445 1.00 60.56 ? 146 GLU   C CD  1 
ATOM   2188 O  OE1 . GLU   B 1 140 ? 10.091 -16.161 33.374 1.00 62.42 ? 146 GLU   C OE1 1 
ATOM   2189 O  OE2 . GLU   B 1 140 ? 9.216  -18.165 33.649 1.00 62.84 ? 146 GLU   C OE2 1 
HETATM 2190 N  N1  . A1B40 C 2 .   ? 10.786 15.626  17.332 1.00 22.56 ? 201 A1B40 A N1  1 
HETATM 2191 C  C4  . A1B40 C 2 .   ? 5.787  12.997  25.539 1.00 24.83 ? 201 A1B40 A C4  1 
HETATM 2192 C  C5  . A1B40 C 2 .   ? 6.631  13.966  25.022 1.00 25.28 ? 201 A1B40 A C5  1 
HETATM 2193 C  C6  . A1B40 C 2 .   ? 7.658  13.627  24.139 1.00 25.37 ? 201 A1B40 A C6  1 
HETATM 2194 C  C7  . A1B40 C 2 .   ? 8.679  14.675  23.747 1.00 26.36 ? 201 A1B40 A C7  1 
HETATM 2195 C  C8  . A1B40 C 2 .   ? 8.278  15.339  22.444 1.00 27.29 ? 201 A1B40 A C8  1 
HETATM 2196 C  C10 . A1B40 C 2 .   ? 11.334 15.728  20.413 1.00 25.34 ? 201 A1B40 A C10 1 
HETATM 2197 C  C13 . A1B40 C 2 .   ? 10.227 16.577  18.070 1.00 23.90 ? 201 A1B40 A C13 1 
HETATM 2198 O  O1  . A1B40 C 2 .   ? 9.630  17.526  17.570 1.00 24.07 ? 201 A1B40 A O1  1 
HETATM 2199 C  C12 . A1B40 C 2 .   ? 10.271 16.422  19.583 1.00 25.14 ? 201 A1B40 A C12 1 
HETATM 2200 C  C11 . A1B40 C 2 .   ? 11.260 17.230  20.387 1.00 25.61 ? 201 A1B40 A C11 1 
HETATM 2201 C  C9  . A1B40 C 2 .   ? 10.641 15.047  21.588 1.00 25.77 ? 201 A1B40 A C9  1 
HETATM 2202 C  C14 . A1B40 C 2 .   ? 8.925  16.188  20.262 1.00 25.36 ? 201 A1B40 A C14 1 
HETATM 2203 N  N   . A1B40 C 2 .   ? 9.250  15.508  21.516 1.00 26.25 ? 201 A1B40 A N   1 
HETATM 2204 O  O   . A1B40 C 2 .   ? 7.110  15.669  22.241 1.00 28.26 ? 201 A1B40 A O   1 
HETATM 2205 C  C1  . A1B40 C 2 .   ? 7.771  12.291  23.734 1.00 24.64 ? 201 A1B40 A C1  1 
HETATM 2206 S  S   . A1B40 C 2 .   ? 8.976  11.929  22.486 1.00 24.62 ? 201 A1B40 A S   1 
HETATM 2207 C  C   . A1B40 C 2 .   ? 9.079  10.135  22.529 1.00 24.95 ? 201 A1B40 A C   1 
HETATM 2208 C  C3  . A1B40 C 2 .   ? 5.940  11.678  25.170 1.00 24.62 ? 201 A1B40 A C3  1 
HETATM 2209 C  C2  . A1B40 C 2 .   ? 6.924  11.318  24.263 1.00 24.50 ? 201 A1B40 A C2  1 
HETATM 2210 ZN ZN  . ZN    D 3 .   ? 11.311 -4.120  5.864  1.00 22.78 2 202 ZN    A ZN  1 
HETATM 2211 S  S   . DMS   E 4 .   ? 19.000 -2.345  24.239 1.00 87.93 ? 203 DMS   A S   1 
HETATM 2212 O  O   . DMS   E 4 .   ? 18.905 -3.598  25.066 1.00 87.83 ? 203 DMS   A O   1 
HETATM 2213 C  C1  . DMS   E 4 .   ? 19.516 -0.985  25.326 1.00 87.83 ? 203 DMS   A C1  1 
HETATM 2214 C  C2  . DMS   E 4 .   ? 20.553 -2.420  23.303 1.00 87.94 ? 203 DMS   A C2  1 
HETATM 2215 ZN ZN  . ZN    F 3 .   ? 30.678 -31.428 26.789 1.00 18.87 2 201 ZN    C ZN  1 
HETATM 2216 S  S   . DMS   G 4 .   ? 20.963 -32.579 10.189 1.00 88.46 ? 202 DMS   C S   1 
HETATM 2217 O  O   . DMS   G 4 .   ? 21.032 -31.555 9.094  1.00 88.34 ? 202 DMS   C O   1 
HETATM 2218 C  C1  . DMS   G 4 .   ? 21.908 -31.939 11.600 1.00 88.46 ? 202 DMS   C C1  1 
HETATM 2219 C  C2  . DMS   G 4 .   ? 19.336 -32.387 10.974 1.00 88.59 ? 202 DMS   C C2  1 
HETATM 2220 O  O   . HOH   H 5 .   ? 11.307 8.774   4.234  1.00 24.65 ? 301 HOH   A O   1 
HETATM 2221 O  O   . HOH   H 5 .   ? 35.434 -3.869  7.922  1.00 30.10 ? 302 HOH   A O   1 
HETATM 2222 O  O   . HOH   H 5 .   ? 5.774  17.513  21.213 1.00 39.15 ? 303 HOH   A O   1 
HETATM 2223 O  O   . HOH   H 5 .   ? 6.470  2.810   3.103  1.00 32.27 ? 304 HOH   A O   1 
HETATM 2224 O  O   . HOH   H 5 .   ? 7.327  20.788  17.101 1.00 22.88 ? 305 HOH   A O   1 
HETATM 2225 O  O   . HOH   H 5 .   ? 1.978  23.351  20.651 1.00 36.22 ? 306 HOH   A O   1 
HETATM 2226 O  O   . HOH   H 5 .   ? 17.348 1.089   28.339 1.00 25.01 ? 307 HOH   A O   1 
HETATM 2227 O  O   . HOH   H 5 .   ? 35.056 16.745  19.770 1.00 42.31 ? 308 HOH   A O   1 
HETATM 2228 O  O   . HOH   H 5 .   ? -3.275 10.071  28.025 1.00 38.11 ? 309 HOH   A O   1 
HETATM 2229 O  O   . HOH   H 5 .   ? 17.899 -5.877  24.179 1.00 40.75 ? 310 HOH   A O   1 
HETATM 2230 O  O   . HOH   H 5 .   ? 30.434 10.612  15.706 1.00 29.34 ? 311 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 5 .   ? 28.195 3.110   5.182  1.00 36.31 ? 312 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 5 .   ? 19.278 10.110  19.758 1.00 17.21 ? 313 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 5 .   ? 10.283 10.099  31.345 1.00 24.52 ? 314 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 5 .   ? 2.871  -3.655  20.954 1.00 31.62 ? 315 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 5 .   ? 11.374 12.698  10.786 1.00 18.77 ? 316 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 13.348 11.314  9.064  1.00 17.33 ? 317 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 25.006 5.380   21.623 1.00 39.04 ? 318 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 4.692  -3.802  28.914 1.00 28.06 ? 319 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? -2.192 -3.660  11.954 1.00 58.43 ? 320 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 31.514 20.333  11.881 1.00 25.73 ? 321 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 11.586 18.296  4.925  1.00 39.86 ? 322 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? 8.350  25.384  23.430 1.00 32.48 ? 323 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? 12.304 22.381  12.191 1.00 37.54 ? 324 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? 18.386 22.154  9.658  1.00 26.81 ? 325 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 22.778 0.827   17.473 1.00 22.41 ? 326 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? 27.931 8.326   1.696  1.00 40.22 ? 327 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 15.316 22.254  8.361  1.00 41.90 ? 328 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 14.480 14.939  26.485 1.00 41.95 ? 329 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 0.490  -1.140  19.467 1.00 39.43 ? 330 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 23.284 21.922  7.130  1.00 31.68 ? 331 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? -0.155 1.278   15.699 1.00 14.78 ? 332 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 31.385 -2.270  15.715 1.00 44.87 ? 333 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? 29.948 11.840  18.367 1.00 35.76 ? 334 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? 13.675 4.051   23.479 1.00 16.83 ? 335 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 16.516 4.011   23.733 1.00 20.80 ? 336 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? 4.004  9.607   27.939 1.00 29.62 ? 337 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 23.354 11.913  22.110 1.00 41.14 ? 338 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? 5.370  5.452   32.804 1.00 25.21 ? 339 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 14.912 11.549  0.085  1.00 36.27 ? 340 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 8.384  -2.848  31.769 1.00 28.21 ? 341 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? 37.746 15.078  14.226 1.00 61.03 ? 342 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 29.111 3.517   12.865 1.00 21.48 ? 343 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? 13.898 13.825  24.074 1.00 22.77 ? 344 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 8.579  19.468  19.339 1.00 25.31 ? 345 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 11.958 11.111  29.733 1.00 21.39 ? 346 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 9.510  22.295  9.760  1.00 42.38 ? 347 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? 3.196  0.013   29.215 1.00 48.74 ? 348 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 28.934 16.199  4.415  1.00 38.77 ? 349 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 1.209  5.205   27.215 1.00 29.71 ? 350 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 23.682 3.475   -2.341 1.00 46.69 ? 351 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? 20.916 -1.112  3.184  1.00 36.15 ? 352 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 0.717  -1.106  9.141  1.00 37.97 ? 353 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? 30.510 4.659   5.943  1.00 27.04 ? 354 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 4.978  14.631  20.254 1.00 28.87 ? 355 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 6.702  -6.949  23.893 1.00 33.28 ? 356 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 32.091 8.867   7.817  1.00 27.63 ? 357 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 9.515  4.113   33.530 1.00 17.78 ? 358 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 20.967 -2.535  16.968 1.00 20.42 ? 359 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 3.055  7.795   24.447 1.00 27.68 ? 360 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 20.969 -4.143  14.180 1.00 23.41 ? 361 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 10.612 5.146   3.266  1.00 29.06 ? 362 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 16.360 9.513   -1.613 1.00 23.61 ? 363 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? 17.539 10.959  26.011 1.00 30.03 ? 364 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 1.908  11.428  27.433 1.00 31.90 ? 365 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 16.006 24.252  14.621 1.00 62.55 ? 366 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 19.669 20.559  5.782  1.00 42.08 ? 367 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 16.897 6.315   27.117 1.00 27.42 ? 368 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 4.074  -4.211  6.044  1.00 30.28 ? 369 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 14.618 -2.375  18.025 1.00 22.56 ? 370 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 9.159  2.892   2.747  1.00 36.96 ? 371 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? 17.508 20.154  17.078 1.00 17.59 ? 372 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 34.051 18.753  10.939 1.00 28.46 ? 373 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 19.415 3.062   19.568 1.00 27.08 ? 374 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 32.397 2.117   6.177  1.00 33.75 ? 375 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 8.117  6.610   33.857 1.00 22.33 ? 376 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 29.946 -1.272  8.634  1.00 38.27 ? 377 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 27.139 -1.176  8.970  1.00 30.02 ? 378 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? 30.643 3.154   15.039 1.00 27.54 ? 379 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 23.040 -0.743  5.465  1.00 25.31 ? 380 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? 35.652 11.055  11.925 1.00 49.16 ? 381 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 0.144  5.511   5.835  1.00 31.05 ? 382 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 5.298  26.995  19.612 1.00 33.42 ? 383 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 14.441 24.537  17.759 1.00 38.78 ? 384 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? 20.097 13.554  2.450  1.00 54.41 ? 385 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 33.296 14.547  9.500  1.00 54.46 ? 386 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 30.722 15.854  22.971 1.00 36.11 ? 387 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? -1.431 13.044  22.039 1.00 51.20 ? 388 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 11.570 -7.054  24.941 1.00 32.71 ? 389 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 3.445  12.318  18.121 1.00 38.62 ? 390 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 27.744 17.829  24.301 1.00 28.50 ? 391 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 16.647 21.500  19.134 1.00 24.01 ? 392 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 34.006 5.129   16.756 1.00 35.48 ? 393 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 24.190 -3.620  16.266 1.00 43.84 ? 394 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 29.414 11.880  21.273 1.00 37.45 ? 395 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 17.516 1.005   20.389 1.00 23.13 ? 396 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 17.312 -5.557  12.304 1.00 46.79 ? 397 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 27.316 -1.186  16.097 1.00 39.31 ? 398 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 23.426 8.512   21.737 1.00 35.31 ? 399 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 33.978 11.092  15.843 1.00 49.75 ? 400 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 18.107 18.050  4.140  1.00 32.70 ? 401 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 15.042 15.210  3.151  1.00 34.02 ? 402 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 29.328 11.544  3.105  1.00 55.57 ? 403 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 7.287  13.658  4.559  1.00 23.51 ? 404 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 37.103 2.599   9.952  1.00 44.84 ? 405 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 3.953  -0.009  24.105 1.00 22.07 ? 406 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 2.770  16.399  19.141 1.00 29.56 ? 407 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 16.912 -4.030  2.785  1.00 29.69 ? 408 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 2.211  13.936  4.262  1.00 44.78 ? 409 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 25.392 19.917  21.839 1.00 41.85 ? 410 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 23.216 19.277  6.322  1.00 24.52 ? 411 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 36.367 -0.504  13.034 1.00 43.70 ? 412 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 3.188  15.152  23.782 1.00 45.71 ? 413 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 0.636  -1.165  16.784 1.00 22.87 ? 414 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 22.214 19.600  19.775 1.00 42.04 ? 415 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 34.124 7.688   16.816 1.00 43.16 ? 416 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 20.985 10.094  22.097 1.00 19.19 ? 417 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 6.279  24.294  10.285 1.00 45.27 ? 418 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 20.909 -4.739  11.526 1.00 32.26 ? 419 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 5.639  18.154  23.903 1.00 49.67 ? 420 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 22.665 3.397   20.950 1.00 26.79 ? 421 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 2.142  14.553  16.739 1.00 46.51 ? 422 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 30.919 19.830  8.770  1.00 41.60 ? 423 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 17.271 -2.308  19.797 1.00 25.06 ? 424 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 0.885  7.841   27.770 1.00 37.69 ? 425 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 19.875 9.541   -0.927 1.00 30.37 ? 426 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 0.930  -5.191  17.525 1.00 45.27 ? 427 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 8.615  21.194  7.242  1.00 43.39 ? 428 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 1.992  -5.504  14.523 1.00 55.01 ? 429 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 22.742 -7.034  11.807 1.00 49.41 ? 430 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 1.993  14.002  26.395 1.00 48.10 ? 431 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 18.483 2.210   22.940 1.00 39.15 ? 432 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 8.074  11.953  31.675 1.00 37.03 ? 433 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 2.505  -0.344  26.464 1.00 38.23 ? 434 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 16.006 13.179  26.290 1.00 36.13 ? 435 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? 2.406  -1.507  22.558 1.00 29.02 ? 436 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 12.200 -4.794  33.075 1.00 40.54 ? 437 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 30.507 7.158   18.129 1.00 44.98 ? 438 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 7.796  17.092  26.291 1.00 47.91 ? 439 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 31.318 4.773   17.058 1.00 33.72 ? 440 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 21.437 -1.023  19.039 1.00 34.27 ? 441 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 6.004  11.708  29.694 1.00 37.69 ? 442 HOH   A O   1 
HETATM 2362 O  O   . HOH   I 5 .   ? 29.311 -26.248 -1.078 1.00 31.49 ? 301 HOH   C O   1 
HETATM 2363 O  O   . HOH   I 5 .   ? 17.603 -33.500 24.080 1.00 39.84 ? 302 HOH   C O   1 
HETATM 2364 O  O   . HOH   I 5 .   ? 26.524 -5.574  10.072 1.00 37.38 ? 303 HOH   C O   1 
HETATM 2365 O  O   . HOH   I 5 .   ? 30.876 -33.368 0.856  1.00 36.39 ? 304 HOH   C O   1 
HETATM 2366 O  O   . HOH   I 5 .   ? 31.382 -18.103 -0.196 1.00 41.40 ? 305 HOH   C O   1 
HETATM 2367 O  O   . HOH   I 5 .   ? 19.723 -4.192  20.281 1.00 29.99 ? 306 HOH   C O   1 
HETATM 2368 O  O   . HOH   I 5 .   ? 30.840 -18.452 26.937 1.00 21.24 ? 307 HOH   C O   1 
HETATM 2369 O  O   . HOH   I 5 .   ? 7.248  -30.290 21.786 1.00 35.24 ? 308 HOH   C O   1 
HETATM 2370 O  O   . HOH   I 5 .   ? 20.798 -18.980 12.783 1.00 18.74 ? 309 HOH   C O   1 
HETATM 2371 O  O   . HOH   I 5 .   ? 14.801 -18.818 32.040 1.00 51.61 ? 310 HOH   C O   1 
HETATM 2372 O  O   . HOH   I 5 .   ? 26.546 -6.297  22.460 1.00 37.74 ? 311 HOH   C O   1 
HETATM 2373 O  O   . HOH   I 5 .   ? 10.062 -8.971  23.895 1.00 30.62 ? 312 HOH   C O   1 
HETATM 2374 O  O   . HOH   I 5 .   ? 24.011 -8.225  9.491  1.00 34.41 ? 313 HOH   C O   1 
HETATM 2375 O  O   . HOH   I 5 .   ? 38.972 -18.773 21.593 1.00 33.91 ? 314 HOH   C O   1 
HETATM 2376 O  O   . HOH   I 5 .   ? 21.731 -26.413 34.408 1.00 29.45 ? 315 HOH   C O   1 
HETATM 2377 O  O   . HOH   I 5 .   ? 23.705 -33.850 29.084 1.00 33.27 ? 316 HOH   C O   1 
HETATM 2378 O  O   . HOH   I 5 .   ? 22.998 -6.024  21.158 1.00 24.60 ? 317 HOH   C O   1 
HETATM 2379 O  O   . HOH   I 5 .   ? 25.552 -37.953 24.342 1.00 36.07 ? 318 HOH   C O   1 
HETATM 2380 O  O   . HOH   I 5 .   ? 37.177 -32.557 10.840 1.00 29.21 ? 319 HOH   C O   1 
HETATM 2381 O  O   . HOH   I 5 .   ? 17.585 -24.393 8.429  1.00 43.42 ? 320 HOH   C O   1 
HETATM 2382 O  O   . HOH   I 5 .   ? 9.224  -7.811  21.072 1.00 33.85 ? 321 HOH   C O   1 
HETATM 2383 O  O   . HOH   I 5 .   ? 31.051 -24.207 -1.161 1.00 32.21 ? 322 HOH   C O   1 
HETATM 2384 O  O   . HOH   I 5 .   ? 17.873 -27.837 16.560 1.00 21.37 ? 323 HOH   C O   1 
HETATM 2385 O  O   . HOH   I 5 .   ? 21.859 -28.825 4.808  1.00 26.96 ? 324 HOH   C O   1 
HETATM 2386 O  O   . HOH   I 5 .   ? 10.457 -16.936 12.487 1.00 43.01 ? 325 HOH   C O   1 
HETATM 2387 O  O   . HOH   I 5 .   ? 38.779 -14.609 13.412 1.00 53.09 ? 326 HOH   C O   1 
HETATM 2388 O  O   . HOH   I 5 .   ? 14.794 -24.038 12.367 1.00 36.48 ? 327 HOH   C O   1 
HETATM 2389 O  O   . HOH   I 5 .   ? 35.746 -28.843 2.988  1.00 46.06 ? 328 HOH   C O   1 
HETATM 2390 O  O   . HOH   I 5 .   ? 31.963 -10.399 13.717 1.00 24.41 ? 329 HOH   C O   1 
HETATM 2391 O  O   . HOH   I 5 .   ? 11.899 -24.438 21.847 1.00 19.86 ? 330 HOH   C O   1 
HETATM 2392 O  O   . HOH   I 5 .   ? 36.189 -26.551 34.417 1.00 36.89 ? 331 HOH   C O   1 
HETATM 2393 O  O   . HOH   I 5 .   ? 24.863 -15.977 7.248  1.00 24.37 ? 332 HOH   C O   1 
HETATM 2394 O  O   . HOH   I 5 .   ? 37.319 -18.991 28.206 1.00 25.22 ? 333 HOH   C O   1 
HETATM 2395 O  O   . HOH   I 5 .   ? 20.788 -25.910 13.822 1.00 29.03 ? 334 HOH   C O   1 
HETATM 2396 O  O   . HOH   I 5 .   ? 31.058 -21.714 28.517 1.00 19.39 ? 335 HOH   C O   1 
HETATM 2397 O  O   . HOH   I 5 .   ? 5.630  -16.164 23.067 1.00 56.25 ? 336 HOH   C O   1 
HETATM 2398 O  O   . HOH   I 5 .   ? 26.331 -31.515 14.957 1.00 23.77 ? 337 HOH   C O   1 
HETATM 2399 O  O   . HOH   I 5 .   ? 31.562 -35.946 31.504 1.00 48.95 ? 338 HOH   C O   1 
HETATM 2400 O  O   . HOH   I 5 .   ? 25.990 -25.498 8.846  1.00 17.65 ? 339 HOH   C O   1 
HETATM 2401 O  O   . HOH   I 5 .   ? 3.296  -13.106 20.307 1.00 50.14 ? 340 HOH   C O   1 
HETATM 2402 O  O   . HOH   I 5 .   ? 10.270 -17.759 18.269 1.00 29.59 ? 341 HOH   C O   1 
HETATM 2403 O  O   . HOH   I 5 .   ? 40.493 -27.595 15.121 1.00 15.24 ? 342 HOH   C O   1 
HETATM 2404 O  O   . HOH   I 5 .   ? 10.879 -6.491  13.401 1.00 32.16 ? 343 HOH   C O   1 
HETATM 2405 O  O   . HOH   I 5 .   ? 29.930 -15.398 19.508 1.00 21.58 ? 344 HOH   C O   1 
HETATM 2406 O  O   . HOH   I 5 .   ? 28.224 -4.960  18.333 1.00 46.23 ? 345 HOH   C O   1 
HETATM 2407 O  O   . HOH   I 5 .   ? 19.164 -28.015 28.375 1.00 22.00 ? 346 HOH   C O   1 
HETATM 2408 O  O   . HOH   I 5 .   ? 42.627 -11.913 11.013 1.00 28.38 ? 347 HOH   C O   1 
HETATM 2409 O  O   . HOH   I 5 .   ? 38.352 -26.576 28.456 1.00 39.37 ? 348 HOH   C O   1 
HETATM 2410 O  O   . HOH   I 5 .   ? 40.097 -30.012 11.860 1.00 30.08 ? 349 HOH   C O   1 
HETATM 2411 O  O   . HOH   I 5 .   ? 18.652 -8.845  13.477 1.00 33.25 ? 350 HOH   C O   1 
HETATM 2412 O  O   . HOH   I 5 .   ? 28.190 -16.640 22.177 1.00 18.96 ? 351 HOH   C O   1 
HETATM 2413 O  O   . HOH   I 5 .   ? 13.795 -24.076 29.442 1.00 39.28 ? 352 HOH   C O   1 
HETATM 2414 O  O   . HOH   I 5 .   ? 22.959 -8.606  14.068 1.00 20.47 ? 353 HOH   C O   1 
HETATM 2415 O  O   . HOH   I 5 .   ? 10.367 -17.053 15.354 1.00 37.64 ? 354 HOH   C O   1 
HETATM 2416 O  O   . HOH   I 5 .   ? 14.568 -29.000 25.637 1.00 44.37 ? 355 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 5 .   ? 40.249 -25.639 7.139  1.00 44.27 ? 356 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 5 .   ? 36.590 -16.838 12.034 1.00 39.33 ? 357 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 5 .   ? 33.156 -30.780 31.647 1.00 23.59 ? 358 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 5 .   ? 32.562 -23.916 29.243 1.00 19.93 ? 359 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 5 .   ? 26.450 -15.442 30.960 1.00 35.35 ? 360 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 5 .   ? 43.240 -26.060 23.568 1.00 24.28 ? 361 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 5 .   ? 37.785 -31.741 25.903 1.00 28.46 ? 362 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 5 .   ? 11.578 -22.794 28.760 1.00 27.74 ? 363 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 5 .   ? 35.191 -35.105 18.194 1.00 39.72 ? 364 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 5 .   ? 16.491 -17.537 11.055 1.00 43.65 ? 365 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 5 .   ? 35.642 -24.967 24.639 1.00 25.18 ? 366 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 5 .   ? 35.061 -13.320 8.548  1.00 22.81 ? 367 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 5 .   ? 41.801 -12.307 17.906 1.00 27.35 ? 368 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 5 .   ? 38.293 -7.368  7.026  1.00 25.86 ? 369 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 5 .   ? 27.048 -36.083 20.900 1.00 27.71 ? 370 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 5 .   ? 22.854 -28.382 12.688 1.00 25.25 ? 371 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 5 .   ? 22.720 -33.584 5.575  1.00 39.29 ? 372 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 5 .   ? 26.198 -31.280 30.872 1.00 21.91 ? 373 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 5 .   ? 32.886 -9.919  11.000 1.00 20.98 ? 374 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 5 .   ? 10.842 -12.004 9.016  1.00 38.67 ? 375 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 5 .   ? 12.901 -29.698 19.006 1.00 37.55 ? 376 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 5 .   ? 21.844 -18.872 6.099  1.00 38.44 ? 377 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 5 .   ? 35.473 -4.341  17.692 1.00 34.70 ? 378 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 5 .   ? 22.578 -13.869 29.786 1.00 38.48 ? 379 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 5 .   ? 34.335 -13.660 25.612 1.00 21.39 ? 380 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 5 .   ? 17.189 -25.446 12.897 1.00 27.04 ? 381 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 5 .   ? 29.631 -13.230 12.968 1.00 23.75 ? 382 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 5 .   ? 23.161 -25.672 8.942  1.00 21.43 ? 383 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 5 .   ? 37.779 -20.410 4.856  1.00 38.30 ? 384 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 5 .   ? 4.247  -10.633 19.717 1.00 33.05 ? 385 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 5 .   ? 3.863  -8.609  14.666 1.00 41.29 ? 386 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 5 .   ? 5.129  -28.830 23.143 1.00 37.15 ? 387 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 5 .   ? 10.238 -31.219 25.057 1.00 39.04 ? 388 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 26.685 -12.003 27.370 1.00 29.26 ? 389 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 9.796  -18.567 26.743 1.00 35.36 ? 390 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 10.042 -25.058 19.856 1.00 23.05 ? 391 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 36.258 -21.652 6.757  1.00 30.94 ? 392 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 30.171 -18.340 8.359  1.00 35.07 ? 393 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 30.867 -5.862  5.914  1.00 48.61 ? 394 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 6.508  -23.039 18.539 1.00 31.79 ? 395 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 33.147 -34.251 23.994 1.00 44.46 ? 396 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 38.960 -13.148 25.872 1.00 28.53 ? 397 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 8.748  -13.572 10.748 1.00 28.15 ? 398 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 31.271 -12.340 10.766 1.00 23.29 ? 399 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 20.426 -32.438 22.353 1.00 32.62 ? 400 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 15.250 -30.319 18.163 1.00 41.63 ? 401 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 28.720 -36.727 7.801  1.00 24.85 ? 402 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 35.734 -28.999 7.812  1.00 21.17 ? 403 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? 18.694 -8.258  25.523 1.00 23.42 ? 404 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 36.890 -29.675 10.005 1.00 27.96 ? 405 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 37.744 -14.086 10.371 1.00 36.70 ? 406 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 39.938 -30.263 14.494 1.00 22.16 ? 407 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 14.623 -19.100 10.346 1.00 57.88 ? 408 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 32.717 -14.536 9.244  1.00 22.05 ? 409 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 34.661 -23.502 -0.902 1.00 41.69 ? 410 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 18.646 -19.302 10.978 1.00 24.52 ? 411 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 34.292 -32.064 29.639 1.00 34.37 ? 412 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 16.451 -20.786 11.498 1.00 33.54 ? 413 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 20.108 -23.955 35.264 1.00 34.82 ? 414 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 6.552  -20.302 18.187 1.00 32.47 ? 415 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 31.465 -13.728 4.414  1.00 39.27 ? 416 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 23.568 -17.728 33.531 1.00 26.16 ? 417 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 37.309 -31.377 29.004 1.00 46.48 ? 418 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 43.595 -25.814 26.144 1.00 29.15 ? 419 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 36.518 -24.898 27.403 1.00 38.05 ? 420 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 34.056 -15.577 27.247 1.00 39.72 ? 421 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 31.518 -15.894 6.853  1.00 38.83 ? 422 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 18.600 -30.737 -1.552 1.00 54.26 ? 423 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 23.931 -15.838 31.623 1.00 37.09 ? 424 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 26.049 -36.017 7.414  1.00 33.99 ? 425 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 21.175 -17.668 34.827 1.00 32.45 ? 426 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 32.631 -19.550 29.188 1.00 28.92 ? 427 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 27.548 -3.994  8.133  1.00 50.52 ? 428 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 43.321 -28.922 23.177 1.00 29.35 ? 429 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 9.056  -23.471 17.791 1.00 33.19 ? 430 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 43.390 -21.280 3.521  1.00 41.63 ? 431 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 18.237 -26.620 10.140 1.00 45.82 ? 432 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 37.684 -4.768  6.659  1.00 31.87 ? 433 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 35.252 -23.318 29.039 1.00 31.79 ? 434 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   ? 0.2029 0.2418 0.2732 0.0068  -0.0260 -0.0120 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2118 0.2499 0.2868 0.0093  -0.0282 -0.0102 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2079 0.2429 0.2846 0.0124  -0.0297 -0.0057 7   SER   A C   
4    O O   . SER   A 1   ? 0.2070 0.2404 0.2802 0.0120  -0.0300 -0.0033 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2428 0.2854 0.3156 0.0067  -0.0313 -0.0097 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2798 0.3241 0.3482 0.0055  -0.0346 -0.0050 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2064 0.2406 0.2886 0.0150  -0.0303 -0.0050 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2051 0.2363 0.2897 0.0176  -0.0308 -0.0022 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1972 0.2276 0.2871 0.0194  -0.0291 -0.0036 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1982 0.2291 0.2895 0.0187  -0.0275 -0.0058 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1832 0.2125 0.2766 0.0214  -0.0294 -0.0023 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1780 0.2076 0.2757 0.0221  -0.0275 -0.0038 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1772 0.2037 0.2764 0.0233  -0.0259 -0.0036 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1802 0.2040 0.2789 0.0243  -0.0268 -0.0018 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1741 0.2078 0.2765 0.0227  -0.0289 -0.0043 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1676 0.1945 0.2685 0.0226  -0.0234 -0.0054 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1676 0.1923 0.2702 0.0229  -0.0210 -0.0067 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1721 0.2002 0.2817 0.0244  -0.0203 -0.0082 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1761 0.2083 0.2870 0.0233  -0.0204 -0.0089 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1799 0.2043 0.2788 0.0197  -0.0184 -0.0080 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1947 0.2173 0.2881 0.0182  -0.0192 -0.0062 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1838 0.2061 0.2837 0.0190  -0.0152 -0.0106 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1987 0.2234 0.2895 0.0146  -0.0179 -0.0060 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1698 0.1962 0.2849 0.0269  -0.0193 -0.0088 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1750 0.2056 0.2984 0.0285  -0.0181 -0.0106 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1855 0.2142 0.3113 0.0278  -0.0130 -0.0149 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1912 0.2150 0.3203 0.0297  -0.0116 -0.0155 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1673 0.1992 0.2981 0.0323  -0.0213 -0.0076 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1663 0.2016 0.2939 0.0315  -0.0259 -0.0043 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1693 0.2108 0.2991 0.0306  -0.0270 -0.0050 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1765 0.2091 0.2984 0.0310  -0.0289 -0.0011 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1787 0.2232 0.3051 0.0290  -0.0306 -0.0030 11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1816 0.2177 0.2996 0.0293  -0.0323 0.0007  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1971 0.2389 0.3174 0.0283  -0.0331 -0.0005 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2279 0.2731 0.3441 0.0258  -0.0359 0.0002  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1812 0.2136 0.3052 0.0244  -0.0100 -0.0179 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1909 0.2227 0.3155 0.0221  -0.0046 -0.0228 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1975 0.2363 0.3276 0.0212  -0.0021 -0.0258 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1981 0.2417 0.3262 0.0193  -0.0041 -0.0240 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2021 0.2324 0.3164 0.0168  -0.0034 -0.0233 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2077 0.2422 0.3169 0.0140  -0.0062 -0.0201 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2060 0.2371 0.3196 0.0129  0.0025  -0.0291 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2012 0.2407 0.3400 0.0230  0.0022  -0.0302 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1965 0.2437 0.3419 0.0223  0.0051  -0.0335 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1856 0.2380 0.3357 0.0249  0.0003  -0.0292 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1845 0.2345 0.3382 0.0292  -0.0039 -0.0253 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1691 0.2282 0.3179 0.0215  0.0005  -0.0296 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1727 0.2363 0.3245 0.0227  -0.0040 -0.0260 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1812 0.2425 0.3227 0.0196  -0.0078 -0.0222 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1868 0.2522 0.3282 0.0176  -0.0097 -0.0208 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1873 0.2598 0.3464 0.0214  -0.0016 -0.0286 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2395 0.3151 0.4123 0.0261  0.0012  -0.0313 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2510 0.3299 0.4327 0.0301  -0.0023 -0.0284 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2381 0.3129 0.4135 0.0253  0.0074  -0.0369 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1730 0.2277 0.3074 0.0195  -0.0089 -0.0207 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1704 0.2228 0.2972 0.0173  -0.0121 -0.0173 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1703 0.2179 0.2953 0.0205  -0.0157 -0.0146 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1701 0.2140 0.2959 0.0230  -0.0153 -0.0147 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1791 0.2296 0.2985 0.0131  -0.0101 -0.0176 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1982 0.2541 0.3170 0.0082  -0.0069 -0.0195 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2171 0.2775 0.3372 0.0058  -0.0081 -0.0179 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2042 0.2608 0.3205 0.0050  -0.0026 -0.0229 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2225 0.2885 0.3415 0.0005  -0.0054 -0.0192 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2143 0.2770 0.3288 -0.0007 0.0004  -0.0248 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2283 0.2959 0.3440 -0.0030 -0.0012 -0.0225 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2655 0.3396 0.3789 -0.0095 0.0017  -0.0238 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1634 0.2107 0.2854 0.0197  -0.0187 -0.0124 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1618 0.2054 0.2804 0.0212  -0.0216 -0.0103 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1652 0.2061 0.2783 0.0187  -0.0215 -0.0094 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1630 0.2057 0.2769 0.0166  -0.0217 -0.0092 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1635 0.2103 0.2848 0.0220  -0.0247 -0.0094 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1860 0.2303 0.3023 0.0216  -0.0272 -0.0082 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2027 0.2513 0.3208 0.0213  -0.0304 -0.0076 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2168 0.2646 0.3305 0.0187  -0.0312 -0.0086 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2638 0.3106 0.3727 0.0180  -0.0326 -0.0082 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2550 0.3009 0.3624 0.0196  -0.0339 -0.0057 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2444 0.2906 0.3501 0.0152  -0.0323 -0.0105 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1595 0.1965 0.2683 0.0189  -0.0213 -0.0085 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1596 0.1949 0.2650 0.0170  -0.0213 -0.0071 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1696 0.2029 0.2733 0.0182  -0.0230 -0.0066 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1708 0.2023 0.2721 0.0195  -0.0235 -0.0064 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1597 0.1934 0.2615 0.0154  -0.0196 -0.0066 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1590 0.1929 0.2594 0.0133  -0.0202 -0.0041 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1695 0.2056 0.2721 0.0135  -0.0172 -0.0084 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1567 0.1902 0.2617 0.0174  -0.0234 -0.0067 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1562 0.1883 0.2596 0.0177  -0.0240 -0.0075 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1670 0.1992 0.2705 0.0178  -0.0241 -0.0075 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1610 0.1918 0.2664 0.0170  -0.0230 -0.0071 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1712 0.2023 0.2797 0.0160  -0.0227 -0.0053 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1506 0.1847 0.2553 0.0173  -0.0253 -0.0094 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.1834 0.2177 0.2884 0.0173  -0.0253 -0.0094 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1649 0.2011 0.2685 0.0183  -0.0271 -0.0089 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.1876 0.2215 0.2901 0.0165  -0.0255 -0.0113 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.1301 0.1654 0.2391 0.0160  -0.0250 -0.0100 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.1991 0.2361 0.3048 0.0184  -0.0267 -0.0088 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1519 0.1816 0.2562 0.0172  -0.0224 -0.0085 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1432 0.1717 0.2519 0.0172  -0.0210 -0.0086 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1435 0.1714 0.2572 0.0164  -0.0208 -0.0102 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1456 0.1741 0.2574 0.0156  -0.0212 -0.0131 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1456 0.1740 0.2525 0.0172  -0.0196 -0.0114 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1707 0.1997 0.2729 0.0174  -0.0197 -0.0097 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1748 0.2041 0.2712 0.0170  -0.0209 -0.0097 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1687 0.1980 0.2738 0.0177  -0.0189 -0.0077 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1439 0.1706 0.2640 0.0162  -0.0206 -0.0080 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1376 0.1626 0.2628 0.0151  -0.0204 -0.0091 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.1623 0.1852 0.2888 0.0148  -0.0184 -0.0145 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.1756 0.1983 0.3020 0.0131  -0.0185 -0.0173 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1544 0.1780 0.2872 0.0149  -0.0207 -0.0046 20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1708 0.1920 0.3093 0.0133  -0.0209 -0.0044 20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.1731 0.1925 0.3206 0.0133  -0.0215 0.0011  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.2129 0.2298 0.3661 0.0112  -0.0222 0.0029  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2429 0.2544 0.4037 0.0114  -0.0205 0.0001  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2153 0.2242 0.3778 0.0133  -0.0176 -0.0059 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2436 0.2523 0.4100 0.0092  -0.0214 0.0027  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1569 0.1792 0.2841 0.0159  -0.0164 -0.0164 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.1741 0.1949 0.3023 0.0147  -0.0136 -0.0227 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.1895 0.2133 0.3085 0.0123  -0.0144 -0.0263 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2157 0.2392 0.3340 0.0098  -0.0124 -0.0319 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.1784 0.1986 0.3111 0.0161  -0.0105 -0.0244 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.1911 0.2147 0.3162 0.0162  -0.0107 -0.0242 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2102 0.2354 0.3343 0.0178  -0.0124 -0.0189 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2014 0.2272 0.3198 0.0142  -0.0092 -0.0286 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2167 0.2443 0.3340 0.0170  -0.0119 -0.0201 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2115 0.2398 0.3251 0.0148  -0.0101 -0.0256 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.1780 0.2049 0.2907 0.0126  -0.0174 -0.0230 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.1753 0.2057 0.2807 0.0105  -0.0192 -0.0244 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.1850 0.2176 0.2907 0.0100  -0.0219 -0.0226 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.1892 0.2256 0.2906 0.0088  -0.0243 -0.0223 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.1780 0.2103 0.2772 0.0113  -0.0204 -0.0220 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2026 0.2344 0.3007 0.0109  -0.0176 -0.0241 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2121 0.2454 0.3040 0.0113  -0.0191 -0.0208 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2151 0.2482 0.3112 0.0073  -0.0152 -0.0303 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.1690 0.1999 0.2803 0.0108  -0.0219 -0.0209 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.1775 0.2111 0.2897 0.0102  -0.0239 -0.0194 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.1866 0.2228 0.2979 0.0069  -0.0246 -0.0230 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.1897 0.2232 0.3019 0.0047  -0.0226 -0.0271 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.1703 0.2019 0.2881 0.0104  -0.0234 -0.0171 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.1908 0.2322 0.3008 0.0064  -0.0274 -0.0215 24  THR   A N   
139  C CA  . THR   A 18  ? 0.1973 0.2429 0.3062 0.0026  -0.0288 -0.0241 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2041 0.2498 0.3183 0.0009  -0.0286 -0.0246 24  THR   A C   
141  O O   . THR   A 18  ? 0.2018 0.2453 0.3199 0.0027  -0.0277 -0.0222 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2141 0.2666 0.3207 0.0030  -0.0325 -0.0211 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2242 0.2788 0.3359 0.0059  -0.0334 -0.0177 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2132 0.2655 0.3147 0.0042  -0.0333 -0.0195 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2045 0.2537 0.3183 -0.0034 -0.0296 -0.0275 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2158 0.2658 0.3344 -0.0056 -0.0296 -0.0277 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2059 0.2614 0.3278 -0.0031 -0.0314 -0.0233 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2101 0.2643 0.3360 -0.0031 -0.0303 -0.0220 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2550 0.3088 0.3718 -0.0113 -0.0306 -0.0317 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3493 0.4066 0.4708 -0.0139 -0.0316 -0.0311 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.3941 0.4452 0.5197 -0.0156 -0.0292 -0.0324 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.3859 0.4524 0.5091 -0.0149 -0.0346 -0.0288 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.4062 0.4630 0.5348 -0.0183 -0.0308 -0.0313 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.4106 0.4771 0.5383 -0.0177 -0.0339 -0.0294 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.1885 0.2498 0.3092 -0.0010 -0.0339 -0.0210 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.1958 0.2621 0.3213 0.0018  -0.0347 -0.0177 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1923 0.2537 0.3188 0.0048  -0.0320 -0.0162 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.2008 0.2648 0.3314 0.0048  -0.0310 -0.0153 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2242 0.2967 0.3503 0.0040  -0.0378 -0.0150 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.3139 0.3921 0.4474 0.0067  -0.0379 -0.0128 26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3367 0.4213 0.4752 0.0046  -0.0387 -0.0131 26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3404 0.4163 0.4754 0.0109  -0.0367 -0.0111 26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1737 0.2289 0.2964 0.0065  -0.0308 -0.0162 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1678 0.2190 0.2908 0.0083  -0.0287 -0.0145 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1681 0.2173 0.2940 0.0056  -0.0273 -0.0143 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1760 0.2267 0.3035 0.0054  -0.0264 -0.0124 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1672 0.2129 0.2863 0.0099  -0.0278 -0.0143 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1854 0.2323 0.3014 0.0123  -0.0290 -0.0134 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1802 0.2302 0.2982 0.0142  -0.0295 -0.0119 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.2058 0.2503 0.3179 0.0123  -0.0291 -0.0142 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1641 0.2096 0.2906 0.0032  -0.0271 -0.0162 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1782 0.2209 0.3086 0.0005  -0.0261 -0.0153 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1798 0.2283 0.3129 -0.0022 -0.0268 -0.0148 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1841 0.2321 0.3196 -0.0044 -0.0261 -0.0124 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1844 0.2210 0.3162 -0.0013 -0.0252 -0.0183 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1940 0.2245 0.3262 0.0010  -0.0237 -0.0181 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2103 0.2396 0.3393 0.0026  -0.0230 -0.0209 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.1933 0.2196 0.3298 0.0019  -0.0231 -0.0141 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2047 0.2291 0.3367 0.0046  -0.0214 -0.0197 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.2047 0.2273 0.3415 0.0045  -0.0217 -0.0151 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2023 0.2284 0.3423 0.0003  -0.0237 -0.0094 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2132 0.2321 0.3551 0.0059  -0.0212 -0.0112 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2212 0.2435 0.3652 0.0013  -0.0236 -0.0051 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2216 0.2405 0.3672 0.0043  -0.0225 -0.0059 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1713 0.2259 0.3042 -0.0027 -0.0282 -0.0167 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1783 0.2399 0.3148 -0.0053 -0.0287 -0.0165 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1807 0.2477 0.3191 -0.0033 -0.0277 -0.0145 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.1771 0.2502 0.3191 -0.0055 -0.0273 -0.0144 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.1834 0.2511 0.3202 -0.0067 -0.0310 -0.0187 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1703 0.2354 0.3064 0.0005  -0.0270 -0.0136 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1716 0.2406 0.3091 0.0021  -0.0252 -0.0129 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1722 0.2358 0.3058 0.0025  -0.0236 -0.0113 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1783 0.2421 0.3107 0.0049  -0.0224 -0.0114 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1781 0.2509 0.3177 0.0063  -0.0261 -0.0136 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.2247 0.3051 0.3695 0.0055  -0.0281 -0.0141 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2330 0.3203 0.3834 0.0046  -0.0270 -0.0146 30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2231 0.3031 0.3659 0.0051  -0.0312 -0.0142 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1691 0.2279 0.3015 -0.0001 -0.0238 -0.0095 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1630 0.2172 0.2926 -0.0002 -0.0232 -0.0068 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1720 0.2301 0.3001 -0.0025 -0.0214 -0.0053 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1863 0.2489 0.3160 -0.0063 -0.0207 -0.0048 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1598 0.2084 0.2912 -0.0023 -0.0242 -0.0046 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1807 0.2252 0.3113 -0.0023 -0.0243 -0.0008 31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1764 0.2178 0.3044 0.0018  -0.0242 -0.0022 31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.1951 0.2343 0.3304 -0.0042 -0.0252 0.0020  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1608 0.2174 0.2853 -0.0011 -0.0206 -0.0047 32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1648 0.2251 0.2865 -0.0045 -0.0187 -0.0035 32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1733 0.2304 0.2929 -0.0072 -0.0202 0.0016  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1806 0.2407 0.2994 -0.0123 -0.0204 0.0050  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1744 0.2357 0.2939 -0.0021 -0.0164 -0.0068 32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1867 0.2509 0.3017 -0.0066 -0.0142 -0.0061 32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1700 0.2354 0.2941 0.0003  -0.0149 -0.0108 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1621 0.2138 0.2812 -0.0039 -0.0216 0.0027  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1714 0.2209 0.2905 -0.0056 -0.0232 0.0079  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1759 0.2196 0.2976 -0.0011 -0.0243 0.0077  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1692 0.2114 0.2892 0.0024  -0.0235 0.0037  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1790 0.2318 0.2925 -0.0080 -0.0222 0.0089  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1927 0.2447 0.3060 -0.0094 -0.0243 0.0145  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.2132 0.2676 0.3277 -0.0141 -0.0265 0.0212  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1916 0.2410 0.3037 -0.0065 -0.0247 0.0145  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2215 0.2755 0.3365 -0.0140 -0.0284 0.0256  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.2032 0.2541 0.3167 -0.0093 -0.0271 0.0212  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1923 0.2386 0.3026 -0.0020 -0.0234 0.0101  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2078 0.2581 0.3213 -0.0077 -0.0279 0.0230  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.1974 0.2425 0.3066 -0.0009 -0.0241 0.0117  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2003 0.2474 0.3114 -0.0035 -0.0262 0.0178  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1793 0.2198 0.3057 -0.0016 -0.0259 0.0120  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1781 0.2137 0.3080 0.0024  -0.0261 0.0112  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1941 0.2289 0.3289 0.0016  -0.0277 0.0175  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.2050 0.2409 0.3432 -0.0018 -0.0294 0.0229  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1855 0.2169 0.3197 0.0041  -0.0255 0.0074  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.1855 0.2152 0.3254 0.0012  -0.0263 0.0099  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2505 0.2755 0.3991 0.0014  -0.0272 0.0145  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2765 0.3006 0.4297 -0.0017 -0.0285 0.0190  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.2408 0.2634 0.3926 0.0046  -0.0266 0.0140  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1835 0.2169 0.3194 0.0045  -0.0275 0.0174  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1860 0.2195 0.3287 0.0044  -0.0292 0.0237  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1955 0.2251 0.3439 0.0089  -0.0277 0.0208  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1881 0.2188 0.3317 0.0107  -0.0266 0.0178  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.2244 0.2638 0.3614 0.0014  -0.0306 0.0279  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2807 0.3224 0.4249 0.0000  -0.0334 0.0362  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2814 0.3195 0.4360 0.0036  -0.0336 0.0375  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.3150 0.3626 0.4548 -0.0048 -0.0355 0.0414  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1984 0.2235 0.3574 0.0106  -0.0274 0.0214  36  SER   A N   
245  C CA  A SER   A 30  ? 0.2000 0.2216 0.3658 0.0145  -0.0250 0.0177  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.2070 0.2287 0.3724 0.0145  -0.0249 0.0176  36  SER   A CA  
247  C C   . SER   A 30  ? 0.1990 0.2242 0.3681 0.0159  -0.0257 0.0218  36  SER   A C   
248  O O   . SER   A 30  ? 0.1919 0.2171 0.3607 0.0185  -0.0234 0.0174  36  SER   A O   
249  C CB  A SER   A 30  ? 0.2067 0.2223 0.3849 0.0156  -0.0240 0.0176  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2340 0.2496 0.4115 0.0157  -0.0237 0.0169  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.2145 0.2272 0.4006 0.0192  -0.0208 0.0134  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.2760 0.2916 0.4624 0.0143  -0.0267 0.0257  36  SER   A OG  
253  N N   . SER   A 31  ? 0.1867 0.2159 0.3589 0.0136  -0.0292 0.0305  37  SER   A N   
254  C CA  . SER   A 31  ? 0.1896 0.2236 0.3654 0.0143  -0.0304 0.0352  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1869 0.2247 0.3503 0.0135  -0.0296 0.0317  37  SER   A C   
256  O O   . SER   A 31  ? 0.1950 0.2360 0.3607 0.0145  -0.0296 0.0331  37  SER   A O   
257  C CB  . SER   A 31  ? 0.2152 0.2540 0.3964 0.0109  -0.0350 0.0461  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2587 0.3023 0.4272 0.0056  -0.0368 0.0480  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1731 0.2105 0.3244 0.0116  -0.0288 0.0273  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1691 0.2085 0.3096 0.0110  -0.0278 0.0238  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1662 0.2016 0.3024 0.0139  -0.0249 0.0158  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1634 0.1995 0.2917 0.0138  -0.0241 0.0132  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1759 0.2182 0.3068 0.0066  -0.0288 0.0247  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1893 0.2373 0.3212 0.0019  -0.0318 0.0325  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1966 0.2475 0.3184 -0.0030 -0.0316 0.0317  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1910 0.2423 0.3038 -0.0036 -0.0296 0.0270  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.2231 0.2783 0.3278 -0.0088 -0.0292 0.0268  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.2271 0.2873 0.3304 -0.0145 -0.0307 0.0312  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1962 0.2503 0.2941 -0.0090 -0.0271 0.0222  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1423 0.1736 0.2831 0.0158  -0.0235 0.0122  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1434 0.1722 0.2794 0.0172  -0.0213 0.0053  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1369 0.1665 0.2634 0.0158  -0.0220 0.0037  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1464 0.1756 0.2669 0.0165  -0.0212 0.0000  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1648 0.1939 0.2999 0.0189  -0.0193 0.0022  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1779 0.2052 0.3079 0.0193  -0.0175 -0.0043 39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.1783 0.2032 0.3105 0.0190  -0.0168 -0.0073 39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.1812 0.2098 0.3049 0.0192  -0.0169 -0.0061 39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1155 0.1466 0.2411 0.0135  -0.0234 0.0065  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1174 0.1498 0.2360 0.0125  -0.0234 0.0043  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1371 0.1694 0.2574 0.0115  -0.0236 0.0032  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1483 0.1803 0.2737 0.0099  -0.0243 0.0060  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1291 0.1647 0.2432 0.0098  -0.0238 0.0071  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1588 0.1949 0.2688 0.0099  -0.0235 0.0075  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1754 0.2149 0.2807 0.0060  -0.0236 0.0095  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1533 0.1870 0.2592 0.0123  -0.0224 0.0033  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1330 0.1660 0.2495 0.0120  -0.0232 -0.0003 41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1388 0.1733 0.2568 0.0108  -0.0234 -0.0016 41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1450 0.1823 0.2592 0.0112  -0.0229 -0.0034 41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1542 0.1907 0.2656 0.0132  -0.0228 -0.0048 41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1309 0.1633 0.2512 0.0117  -0.0234 -0.0048 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1631 0.1975 0.2856 0.0098  -0.0239 -0.0060 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1670 0.1981 0.2937 0.0088  -0.0237 -0.0077 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1610 0.1990 0.2808 0.0107  -0.0243 -0.0086 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1308 0.1714 0.2458 0.0090  -0.0224 -0.0031 42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1368 0.1805 0.2508 0.0095  -0.0211 -0.0054 42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1424 0.1896 0.2602 0.0090  -0.0213 -0.0070 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1479 0.1966 0.2676 0.0060  -0.0214 -0.0056 42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1569 0.2030 0.2682 0.0066  -0.0193 -0.0047 42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1763 0.2254 0.2886 0.0073  -0.0170 -0.0082 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1640 0.2076 0.2714 0.0064  -0.0193 -0.0030 42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1293 0.1782 0.2488 0.0116  -0.0217 -0.0091 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1373 0.1910 0.2613 0.0110  -0.0221 -0.0104 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1535 0.2116 0.2809 0.0126  -0.0203 -0.0122 43  SER   A C   
304  O O   . SER   A 37  ? 0.1578 0.2137 0.2838 0.0145  -0.0190 -0.0127 43  SER   A O   
305  C CB  . SER   A 37  ? 0.1607 0.2142 0.2855 0.0121  -0.0246 -0.0110 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1776 0.2299 0.3009 0.0152  -0.0257 -0.0109 43  SER   A OG  
307  N N   . SER   A 38  ? 0.1555 0.2197 0.2882 0.0116  -0.0198 -0.0133 44  SER   A N   
308  C CA  . SER   A 38  ? 0.1708 0.2397 0.3092 0.0135  -0.0175 -0.0155 44  SER   A CA  
309  C C   . SER   A 38  ? 0.1892 0.2598 0.3331 0.0178  -0.0200 -0.0149 44  SER   A C   
310  O O   . SER   A 38  ? 0.1936 0.2650 0.3371 0.0176  -0.0235 -0.0134 44  SER   A O   
311  C CB  . SER   A 38  ? 0.1925 0.2684 0.3349 0.0102  -0.0153 -0.0170 44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2303 0.3091 0.3751 0.0091  -0.0182 -0.0159 44  SER   A OG  
313  N N   . THR   A 39  ? 0.1878 0.2596 0.3375 0.0211  -0.0181 -0.0161 45  THR   A N   
314  C CA  . THR   A 39  ? 0.2071 0.2808 0.3635 0.0253  -0.0209 -0.0142 45  THR   A CA  
315  C C   . THR   A 39  ? 0.2356 0.3164 0.4043 0.0276  -0.0186 -0.0160 45  THR   A C   
316  O O   . THR   A 39  ? 0.2387 0.3211 0.4095 0.0263  -0.0136 -0.0198 45  THR   A O   
317  C CB  . THR   A 39  ? 0.2264 0.2929 0.3800 0.0282  -0.0215 -0.0128 45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.2419 0.3056 0.3975 0.0291  -0.0167 -0.0159 45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.2133 0.2737 0.3560 0.0262  -0.0234 -0.0113 45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2454 0.3310 0.4226 0.0306  -0.0222 -0.0132 46  THR   A N   
321  C CA  . THR   A 40  ? 0.2593 0.3524 0.4508 0.0336  -0.0202 -0.0143 46  THR   A CA  
322  C C   . THR   A 40  ? 0.2593 0.3474 0.4574 0.0384  -0.0177 -0.0150 46  THR   A C   
323  O O   . THR   A 40  ? 0.2655 0.3558 0.4720 0.0397  -0.0122 -0.0194 46  THR   A O   
324  C CB  . THR   A 40  ? 0.2972 0.3992 0.4961 0.0342  -0.0254 -0.0104 46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3282 0.4272 0.5249 0.0360  -0.0309 -0.0053 46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.3072 0.4135 0.4998 0.0287  -0.0269 -0.0111 46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2597 0.3411 0.4540 0.0405  -0.0211 -0.0111 47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2714 0.3464 0.4716 0.0447  -0.0190 -0.0112 47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2775 0.3438 0.4674 0.0423  -0.0143 -0.0155 47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2780 0.3415 0.4546 0.0382  -0.0152 -0.0156 47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2840 0.3562 0.4848 0.0472  -0.0253 -0.0043 47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.2634 0.3250 0.4600 0.0449  -0.0096 -0.0188 48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2646 0.3183 0.4519 0.0422  -0.0050 -0.0230 48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2496 0.2945 0.4297 0.0430  -0.0087 -0.0187 48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2407 0.2836 0.4281 0.0471  -0.0123 -0.0139 48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.3039 0.3562 0.5013 0.0438  0.0023  -0.0296 48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3756 0.4357 0.5742 0.0402  0.0080  -0.0359 48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.4679 0.5261 0.6744 0.0405  0.0164  -0.0438 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.4622 0.5209 0.6852 0.0460  0.0185  -0.0451 48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.5116 0.5681 0.7070 0.0343  0.0214  -0.0494 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.2260 0.2664 0.3923 0.0387  -0.0080 -0.0198 49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.2217 0.2546 0.3802 0.0386  -0.0109 -0.0163 49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.2157 0.2406 0.3753 0.0390  -0.0068 -0.0192 49  GLY   A C   
344  O O   . GLY   A 43  ? 0.2138 0.2385 0.3777 0.0383  -0.0009 -0.0252 49  GLY   A O   
345  N N   . CYS   A 44  ? 0.2154 0.2335 0.3705 0.0396  -0.0097 -0.0152 50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.2329 0.2421 0.3892 0.0398  -0.0063 -0.0174 50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.2266 0.2313 0.3694 0.0349  -0.0051 -0.0188 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.2381 0.2353 0.3807 0.0341  -0.0019 -0.0213 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.2599 0.2643 0.4243 0.0443  -0.0101 -0.0116 50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.3147 0.3244 0.4991 0.0505  -0.0109 -0.0098 50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1985 0.2073 0.3309 0.0316  -0.0075 -0.0172 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.2018 0.2078 0.3228 0.0270  -0.0067 -0.0179 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.2133 0.2207 0.3315 0.0225  -0.0011 -0.0242 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.2098 0.2229 0.3314 0.0220  0.0011  -0.0271 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.2053 0.2156 0.3187 0.0254  -0.0108 -0.0142 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.2305 0.2398 0.3440 0.0279  -0.0158 -0.0088 51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.2123 0.2158 0.3267 0.0290  -0.0165 -0.0067 51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.2429 0.2571 0.3548 0.0280  -0.0189 -0.0066 51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.2192 0.2223 0.3303 0.0186  0.0010  -0.0260 52  THR   A N   
360  C CA  . THR   A 46  ? 0.2324 0.2377 0.3382 0.0126  0.0057  -0.0313 52  THR   A CA  
361  C C   . THR   A 46  ? 0.2265 0.2349 0.3216 0.0080  0.0029  -0.0279 52  THR   A C   
362  O O   . THR   A 46  ? 0.2339 0.2387 0.3256 0.0086  0.0000  -0.0243 52  THR   A O   
363  C CB  . THR   A 46  ? 0.2817 0.2798 0.3887 0.0109  0.0107  -0.0366 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.3117 0.3080 0.4311 0.0153  0.0141  -0.0403 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.3094 0.3100 0.4078 0.0029  0.0151  -0.0418 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.2122 0.2275 0.3026 0.0031  0.0038  -0.0288 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.1995 0.2183 0.2820 -0.0010 0.0008  -0.0248 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.2111 0.2286 0.2864 -0.0074 0.0034  -0.0273 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.2089 0.2269 0.2830 -0.0117 0.0083  -0.0332 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.2016 0.2285 0.2830 -0.0036 -0.0005 -0.0228 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.2066 0.2351 0.2952 0.0018  -0.0025 -0.0213 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.2166 0.2470 0.2926 -0.0068 -0.0042 -0.0173 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.2134 0.2386 0.3040 0.0070  -0.0067 -0.0171 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.2059 0.2228 0.2763 -0.0089 0.0005  -0.0234 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.2198 0.2366 0.2828 -0.0157 0.0022  -0.0249 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.2374 0.2635 0.2953 -0.0228 0.0022  -0.0243 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.2397 0.2715 0.2989 -0.0220 -0.0012 -0.0194 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.2163 0.2319 0.2766 -0.0153 -0.0015 -0.0200 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.2456 0.2729 0.2974 -0.0304 0.0060  -0.0290 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.2556 0.2925 0.3009 -0.0389 0.0057  -0.0277 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2762 0.3134 0.3135 -0.0461 0.0060  -0.0282 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.2856 0.3198 0.3187 -0.0513 0.0112  -0.0354 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.2637 0.3033 0.3086 -0.0425 0.0111  -0.0345 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.2645 0.3035 0.3183 -0.0352 0.0112  -0.0346 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.2423 0.2875 0.2978 -0.0335 0.0057  -0.0268 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.2302 0.2747 0.2937 -0.0273 0.0063  -0.0279 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.2651 0.3114 0.3328 -0.0231 0.0019  -0.0222 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.2181 0.2669 0.2841 -0.0240 -0.0030 -0.0151 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2433 0.2892 0.3179 -0.0182 0.0025  -0.0237 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.2662 0.3066 0.3027 -0.0459 0.0008  -0.0209 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.2781 0.3188 0.3088 -0.0513 0.0002  -0.0202 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.2893 0.3376 0.3210 -0.0515 -0.0060 -0.0109 56  CYS   A C   
393  O O   . CYS   A 50  ? 0.2886 0.3405 0.3261 -0.0469 -0.0095 -0.0054 56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.2901 0.3195 0.3236 -0.0459 0.0022  -0.0235 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.2836 0.3097 0.3252 -0.0350 -0.0025 -0.0171 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.2999 0.3498 0.3272 -0.0563 -0.0072 -0.0094 57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.3116 0.3689 0.3417 -0.0561 -0.0126 -0.0009 57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.3019 0.3534 0.3340 -0.0519 -0.0129 -0.0006 57  ASP   A C   
399  O O   . ASP   A 51  ? 0.3107 0.3682 0.3426 -0.0548 -0.0158 0.0041  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.3849 0.4534 0.4083 -0.0671 -0.0146 0.0025  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.5070 0.5733 0.5210 -0.0756 -0.0110 -0.0038 57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.5246 0.5799 0.5383 -0.0724 -0.0070 -0.0102 57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.5722 0.6480 0.5792 -0.0861 -0.0122 -0.0022 57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.2853 0.3260 0.3197 -0.0454 -0.0103 -0.0050 58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.2618 0.2972 0.2975 -0.0421 -0.0108 -0.0041 58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.2408 0.2821 0.2825 -0.0378 -0.0149 0.0026  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.2521 0.2964 0.2995 -0.0333 -0.0166 0.0053  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2455 0.2693 0.2836 -0.0359 -0.0081 -0.0085 58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2753 0.2894 0.3086 -0.0404 -0.0023 -0.0171 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.2138 0.2564 0.2549 -0.0392 -0.0159 0.0047  59  GLN   A N   
411  C CA  A GLN   A 53  ? 0.2062 0.2544 0.2538 -0.0352 -0.0188 0.0100  59  GLN   A CA  
412  C CA  B GLN   A 53  ? 0.2031 0.2508 0.2511 -0.0346 -0.0187 0.0098  59  GLN   A CA  
413  C C   . GLN   A 53  ? 0.2023 0.2438 0.2499 -0.0316 -0.0176 0.0086  59  GLN   A C   
414  O O   . GLN   A 53  ? 0.2034 0.2493 0.2552 -0.0296 -0.0190 0.0117  59  GLN   A O   
415  C CB  A GLN   A 53  ? 0.2149 0.2747 0.2636 -0.0409 -0.0216 0.0152  59  GLN   A CB  
416  C CB  B GLN   A 53  ? 0.2057 0.2658 0.2566 -0.0388 -0.0219 0.0158  59  GLN   A CB  
417  C CG  A GLN   A 53  ? 0.2252 0.2946 0.2792 -0.0416 -0.0247 0.0206  59  GLN   A CG  
418  C CG  B GLN   A 53  ? 0.2045 0.2706 0.2562 -0.0414 -0.0236 0.0181  59  GLN   A CG  
419  C CD  A GLN   A 53  ? 0.2467 0.3282 0.3064 -0.0444 -0.0284 0.0276  59  GLN   A CD  
420  C CD  B GLN   A 53  ? 0.2315 0.2956 0.2900 -0.0344 -0.0241 0.0189  59  GLN   A CD  
421  O OE1 A GLN   A 53  ? 0.2503 0.3397 0.3062 -0.0523 -0.0303 0.0305  59  GLN   A OE1 
422  O OE1 B GLN   A 53  ? 0.2161 0.2799 0.2732 -0.0354 -0.0237 0.0178  59  GLN   A OE1 
423  N NE2 A GLN   A 53  ? 0.2270 0.3110 0.2965 -0.0383 -0.0293 0.0306  59  GLN   A NE2 
424  N NE2 B GLN   A 53  ? 0.2393 0.3023 0.3052 -0.0277 -0.0246 0.0203  59  GLN   A NE2 
425  N N   . THR   A 54  ? 0.1980 0.2289 0.2414 -0.0311 -0.0151 0.0041  60  THR   A N   
426  C CA  . THR   A 54  ? 0.2077 0.2313 0.2505 -0.0282 -0.0144 0.0035  60  THR   A CA  
427  C C   . THR   A 54  ? 0.2066 0.2212 0.2508 -0.0231 -0.0131 0.0005  60  THR   A C   
428  O O   . THR   A 54  ? 0.2189 0.2304 0.2624 -0.0240 -0.0113 -0.0029 60  THR   A O   
429  C CB  . THR   A 54  ? 0.2567 0.2768 0.2937 -0.0339 -0.0132 0.0026  60  THR   A CB  
430  O OG1 . THR   A 54  ? 0.3055 0.3179 0.3383 -0.0374 -0.0105 -0.0021 60  THR   A OG1 
431  C CG2 . THR   A 54  ? 0.2542 0.2844 0.2904 -0.0393 -0.0147 0.0057  60  THR   A CG2 
432  N N   . GLY   A 55  ? 0.1953 0.2071 0.2419 -0.0182 -0.0140 0.0019  61  GLY   A N   
433  C CA  . GLY   A 55  ? 0.1893 0.1941 0.2383 -0.0134 -0.0136 0.0004  61  GLY   A CA  
434  C C   . GLY   A 55  ? 0.1926 0.1953 0.2423 -0.0102 -0.0152 0.0028  61  GLY   A C   
435  O O   . GLY   A 55  ? 0.1979 0.2023 0.2450 -0.0125 -0.0157 0.0048  61  GLY   A O   
436  N N   . VAL   A 56  ? 0.1711 0.1709 0.2241 -0.0054 -0.0160 0.0028  62  VAL   A N   
437  C CA  . VAL   A 56  ? 0.1800 0.1786 0.2330 -0.0032 -0.0178 0.0054  62  VAL   A CA  
438  C C   . VAL   A 56  ? 0.1746 0.1774 0.2315 0.0010  -0.0190 0.0052  62  VAL   A C   
439  O O   . VAL   A 56  ? 0.1690 0.1711 0.2293 0.0032  -0.0186 0.0034  62  VAL   A O   
440  C CB  . VAL   A 56  ? 0.2063 0.1953 0.2595 -0.0025 -0.0180 0.0062  62  VAL   A CB  
441  C CG1 . VAL   A 56  ? 0.2220 0.2106 0.2754 -0.0004 -0.0208 0.0099  62  VAL   A CG1 
442  C CG2 . VAL   A 56  ? 0.2183 0.2020 0.2676 -0.0073 -0.0166 0.0061  62  VAL   A CG2 
443  N N   . TYR   A 57  ? 0.1594 0.1668 0.2156 0.0016  -0.0202 0.0066  63  TYR   A N   
444  C CA  . TYR   A 57  ? 0.1643 0.1751 0.2240 0.0049  -0.0210 0.0058  63  TYR   A CA  
445  C C   . TYR   A 57  ? 0.1708 0.1811 0.2284 0.0053  -0.0230 0.0077  63  TYR   A C   
446  O O   . TYR   A 57  ? 0.1756 0.1854 0.2288 0.0026  -0.0234 0.0097  63  TYR   A O   
447  C CB  . TYR   A 57  ? 0.1638 0.1817 0.2261 0.0050  -0.0201 0.0045  63  TYR   A CB  
448  C CG  . TYR   A 57  ? 0.1788 0.2012 0.2396 0.0035  -0.0195 0.0047  63  TYR   A CG  
449  C CD1 . TYR   A 57  ? 0.1976 0.2216 0.2557 0.0003  -0.0186 0.0058  63  TYR   A CD1 
450  C CD2 . TYR   A 57  ? 0.1817 0.2073 0.2437 0.0047  -0.0194 0.0032  63  TYR   A CD2 
451  C CE1 . TYR   A 57  ? 0.1945 0.2237 0.2519 -0.0014 -0.0174 0.0054  63  TYR   A CE1 
452  C CE2 . TYR   A 57  ? 0.1736 0.2040 0.2344 0.0027  -0.0178 0.0022  63  TYR   A CE2 
453  C CZ  . TYR   A 57  ? 0.1832 0.2156 0.2419 -0.0001 -0.0168 0.0033  63  TYR   A CZ  
454  O OH  . TYR   A 57  ? 0.2007 0.2386 0.2586 -0.0023 -0.0147 0.0018  63  TYR   A OH  
455  N N   . TYR   A 58  ? 0.1691 0.1806 0.2295 0.0079  -0.0243 0.0072  64  TYR   A N   
456  C CA  . TYR   A 58  ? 0.1754 0.1882 0.2335 0.0075  -0.0266 0.0093  64  TYR   A CA  
457  C C   . TYR   A 58  ? 0.1721 0.1915 0.2285 0.0061  -0.0256 0.0070  64  TYR   A C   
458  O O   . TYR   A 58  ? 0.1716 0.1937 0.2320 0.0078  -0.0244 0.0040  64  TYR   A O   
459  C CB  . TYR   A 58  ? 0.1715 0.1829 0.2337 0.0104  -0.0289 0.0104  64  TYR   A CB  
460  C CG  . TYR   A 58  ? 0.1836 0.1975 0.2429 0.0089  -0.0321 0.0135  64  TYR   A CG  
461  C CD1 . TYR   A 58  ? 0.1979 0.2093 0.2532 0.0064  -0.0341 0.0181  64  TYR   A CD1 
462  C CD2 . TYR   A 58  ? 0.1892 0.2083 0.2493 0.0091  -0.0332 0.0123  64  TYR   A CD2 
463  C CE1 . TYR   A 58  ? 0.2055 0.2204 0.2573 0.0039  -0.0375 0.0220  64  TYR   A CE1 
464  C CE2 . TYR   A 58  ? 0.1938 0.2166 0.2500 0.0064  -0.0363 0.0152  64  TYR   A CE2 
465  C CZ  . TYR   A 58  ? 0.2106 0.2316 0.2626 0.0037  -0.0387 0.0204  64  TYR   A CZ  
466  O OH  . TYR   A 58  ? 0.2192 0.2449 0.2667 0.0001  -0.0423 0.0243  64  TYR   A OH  
467  N N   . CYS   A 59  ? 0.1605 0.1824 0.2114 0.0026  -0.0260 0.0083  65  CYS   A N   
468  C CA  . CYS   A 59  ? 0.1622 0.1905 0.2110 0.0003  -0.0242 0.0052  65  CYS   A CA  
469  C C   . CYS   A 59  ? 0.1756 0.2064 0.2200 -0.0020 -0.0268 0.0066  65  CYS   A C   
470  O O   . CYS   A 59  ? 0.1828 0.2141 0.2211 -0.0057 -0.0286 0.0103  65  CYS   A O   
471  C CB  . CYS   A 59  ? 0.1683 0.1991 0.2138 -0.0031 -0.0219 0.0050  65  CYS   A CB  
472  S SG  . CYS   A 59  ? 0.2091 0.2484 0.2529 -0.0063 -0.0183 0.0000  65  CYS   A SG  
473  N N   . SER   A 60  ? 0.1807 0.2138 0.2278 -0.0006 -0.0272 0.0041  66  SER   A N   
474  C CA  . SER   A 60  ? 0.1910 0.2278 0.2336 -0.0037 -0.0302 0.0057  66  SER   A CA  
475  C C   . SER   A 60  ? 0.1983 0.2411 0.2330 -0.0098 -0.0288 0.0042  66  SER   A C   
476  O O   . SER   A 60  ? 0.2074 0.2528 0.2356 -0.0141 -0.0322 0.0084  66  SER   A O   
477  C CB  . SER   A 60  ? 0.2187 0.2573 0.2655 -0.0018 -0.0307 0.0028  66  SER   A CB  
478  O OG  . SER   A 60  ? 0.2485 0.2902 0.2966 -0.0026 -0.0266 -0.0037 66  SER   A OG  
479  N N   . SER   A 61  ? 0.1788 0.2243 0.2143 -0.0107 -0.0237 -0.0015 67  SER   A N   
480  C CA  . SER   A 61  ? 0.1743 0.2262 0.2032 -0.0167 -0.0209 -0.0047 67  SER   A CA  
481  C C   . SER   A 61  ? 0.1804 0.2326 0.2024 -0.0207 -0.0222 0.0004  67  SER   A C   
482  O O   . SER   A 61  ? 0.1841 0.2424 0.1993 -0.0267 -0.0201 -0.0015 67  SER   A O   
483  C CB  . SER   A 61  ? 0.1870 0.2415 0.2214 -0.0157 -0.0147 -0.0122 67  SER   A CB  
484  O OG  . SER   A 61  ? 0.2084 0.2605 0.2480 -0.0126 -0.0130 -0.0111 67  SER   A OG  
485  N N   . ARG   A 62  ? 0.1752 0.2209 0.1989 -0.0179 -0.0252 0.0064  68  ARG   A N   
486  C CA  . ARG   A 62  ? 0.1840 0.2284 0.2015 -0.0218 -0.0270 0.0121  68  ARG   A CA  
487  C C   . ARG   A 62  ? 0.2133 0.2515 0.2310 -0.0205 -0.0330 0.0202  68  ARG   A C   
488  O O   . ARG   A 62  ? 0.2271 0.2624 0.2410 -0.0233 -0.0352 0.0259  68  ARG   A O   
489  C CB  . ARG   A 62  ? 0.1973 0.2390 0.2177 -0.0205 -0.0241 0.0114  68  ARG   A CB  
490  C CG  . ARG   A 62  ? 0.2105 0.2590 0.2324 -0.0219 -0.0184 0.0048  68  ARG   A CG  
491  C CD  . ARG   A 62  ? 0.2228 0.2778 0.2363 -0.0292 -0.0168 0.0047  68  ARG   A CD  
492  N NE  . ARG   A 62  ? 0.2082 0.2702 0.2251 -0.0301 -0.0107 -0.0023 68  ARG   A NE  
493  C CZ  . ARG   A 62  ? 0.2028 0.2705 0.2212 -0.0311 -0.0068 -0.0092 68  ARG   A CZ  
494  N NH1 . ARG   A 62  ? 0.1923 0.2600 0.2078 -0.0318 -0.0088 -0.0102 68  ARG   A NH1 
495  N NH2 . ARG   A 62  ? 0.1946 0.2683 0.2185 -0.0313 -0.0008 -0.0155 68  ARG   A NH2 
496  N N   . ARG   A 63  ? 0.2087 0.2444 0.2324 -0.0158 -0.0354 0.0205  69  ARG   A N   
497  C CA  . ARG   A 63  ? 0.2288 0.2586 0.2562 -0.0131 -0.0403 0.0274  69  ARG   A CA  
498  C C   . ARG   A 63  ? 0.2456 0.2671 0.2755 -0.0113 -0.0398 0.0302  69  ARG   A C   
499  O O   . ARG   A 63  ? 0.2628 0.2798 0.2920 -0.0126 -0.0432 0.0370  69  ARG   A O   
500  C CB  . ARG   A 63  ? 0.2599 0.2935 0.2815 -0.0182 -0.0454 0.0344  69  ARG   A CB  
501  C CG  . ARG   A 63  ? 0.2907 0.3313 0.3115 -0.0194 -0.0473 0.0331  69  ARG   A CG  
502  C CD  . ARG   A 63  ? 0.3142 0.3565 0.3338 -0.0221 -0.0544 0.0427  69  ARG   A CD  
503  N NE  . ARG   A 63  ? 0.3274 0.3787 0.3438 -0.0255 -0.0561 0.0410  69  ARG   A NE  
504  C CZ  . ARG   A 63  ? 0.3112 0.3712 0.3169 -0.0338 -0.0562 0.0402  69  ARG   A CZ  
505  N NH1 . ARG   A 63  ? 0.3152 0.3764 0.3126 -0.0395 -0.0551 0.0419  69  ARG   A NH1 
506  N NH2 . ARG   A 63  ? 0.2910 0.3589 0.2937 -0.0372 -0.0572 0.0375  69  ARG   A NH2 
507  N N   . LYS   A 64  ? 0.2224 0.2420 0.2550 -0.0091 -0.0355 0.0250  70  LYS   A N   
508  C CA  . LYS   A 64  ? 0.2288 0.2414 0.2624 -0.0087 -0.0344 0.0265  70  LYS   A CA  
509  C C   . LYS   A 64  ? 0.2260 0.2359 0.2656 -0.0045 -0.0314 0.0218  70  LYS   A C   
510  O O   . LYS   A 64  ? 0.2260 0.2407 0.2677 -0.0030 -0.0291 0.0171  70  LYS   A O   
511  C CB  . LYS   A 64  ? 0.2756 0.2916 0.3025 -0.0140 -0.0322 0.0262  70  LYS   A CB  
512  C CG  . LYS   A 64  ? 0.3826 0.3981 0.4028 -0.0193 -0.0354 0.0327  70  LYS   A CG  
513  C CD  . LYS   A 64  ? 0.4886 0.5075 0.5028 -0.0248 -0.0327 0.0321  70  LYS   A CD  
514  C CE  . LYS   A 64  ? 0.5644 0.5831 0.5711 -0.0310 -0.0360 0.0393  70  LYS   A CE  
515  N NZ  . LYS   A 64  ? 0.6072 0.6327 0.6093 -0.0339 -0.0389 0.0415  70  LYS   A NZ  
516  N N   . HIS   A 65  ? 0.2225 0.2246 0.2648 -0.0034 -0.0311 0.0231  71  HIS   A N   
517  C CA  . HIS   A 65  ? 0.2155 0.2153 0.2618 -0.0012 -0.0282 0.0190  71  HIS   A CA  
518  C C   . HIS   A 65  ? 0.2168 0.2171 0.2588 -0.0052 -0.0260 0.0183  71  HIS   A C   
519  O O   . HIS   A 65  ? 0.2361 0.2328 0.2743 -0.0085 -0.0268 0.0217  71  HIS   A O   
520  C CB  . HIS   A 65  ? 0.2158 0.2068 0.2673 0.0015  -0.0286 0.0199  71  HIS   A CB  
521  C CG  . HIS   A 65  ? 0.2365 0.2274 0.2938 0.0057  -0.0307 0.0208  71  HIS   A CG  
522  N ND1 . HIS   A 65  ? 0.2696 0.2621 0.3320 0.0090  -0.0291 0.0167  71  HIS   A ND1 
523  C CD2 . HIS   A 65  ? 0.2314 0.2219 0.2903 0.0064  -0.0345 0.0257  71  HIS   A CD2 
524  C CE1 . HIS   A 65  ? 0.2547 0.2477 0.3220 0.0119  -0.0317 0.0188  71  HIS   A CE1 
525  N NE2 . HIS   A 65  ? 0.2603 0.2525 0.3259 0.0105  -0.0352 0.0244  71  HIS   A NE2 
526  N N   . TYR   A 66  ? 0.1875 0.1931 0.2309 -0.0052 -0.0234 0.0146  72  TYR   A N   
527  C CA  . TYR   A 66  ? 0.1938 0.2019 0.2344 -0.0091 -0.0216 0.0143  72  TYR   A CA  
528  C C   . TYR   A 66  ? 0.1771 0.1836 0.2201 -0.0092 -0.0200 0.0122  72  TYR   A C   
529  O O   . TYR   A 66  ? 0.1625 0.1711 0.2097 -0.0063 -0.0195 0.0100  72  TYR   A O   
530  C CB  . TYR   A 66  ? 0.1844 0.2023 0.2255 -0.0098 -0.0199 0.0123  72  TYR   A CB  
531  C CG  . TYR   A 66  ? 0.1943 0.2160 0.2314 -0.0117 -0.0204 0.0132  72  TYR   A CG  
532  C CD1 . TYR   A 66  ? 0.2138 0.2363 0.2450 -0.0167 -0.0204 0.0157  72  TYR   A CD1 
533  C CD2 . TYR   A 66  ? 0.2069 0.2321 0.2456 -0.0096 -0.0206 0.0113  72  TYR   A CD2 
534  C CE1 . TYR   A 66  ? 0.2289 0.2563 0.2554 -0.0197 -0.0205 0.0162  72  TYR   A CE1 
535  C CE2 . TYR   A 66  ? 0.2269 0.2569 0.2609 -0.0127 -0.0205 0.0112  72  TYR   A CE2 
536  C CZ  . TYR   A 66  ? 0.2459 0.2772 0.2735 -0.0179 -0.0205 0.0138  72  TYR   A CZ  
537  O OH  . TYR   A 66  ? 0.2610 0.2978 0.2829 -0.0220 -0.0204 0.0139  72  TYR   A OH  
538  N N   . PRO   A 67  ? 0.1792 0.1829 0.2191 -0.0132 -0.0192 0.0129  73  PRO   A N   
539  C CA  . PRO   A 67  ? 0.1821 0.1861 0.2231 -0.0147 -0.0177 0.0107  73  PRO   A CA  
540  C C   . PRO   A 67  ? 0.2037 0.2184 0.2470 -0.0155 -0.0170 0.0103  73  PRO   A C   
541  O O   . PRO   A 67  ? 0.2208 0.2412 0.2635 -0.0169 -0.0167 0.0114  73  PRO   A O   
542  C CB  . PRO   A 67  ? 0.2104 0.2087 0.2469 -0.0198 -0.0170 0.0116  73  PRO   A CB  
543  C CG  . PRO   A 67  ? 0.2202 0.2181 0.2532 -0.0215 -0.0181 0.0149  73  PRO   A CG  
544  C CD  . PRO   A 67  ? 0.1911 0.1918 0.2258 -0.0174 -0.0197 0.0159  73  PRO   A CD  
545  N N   . VAL   A 68  ? 0.1892 0.2074 0.2360 -0.0148 -0.0167 0.0089  74  VAL   A N   
546  C CA  . VAL   A 68  ? 0.2009 0.2291 0.2521 -0.0150 -0.0166 0.0097  74  VAL   A CA  
547  C C   . VAL   A 68  ? 0.2014 0.2326 0.2533 -0.0180 -0.0168 0.0098  74  VAL   A C   
548  O O   . VAL   A 68  ? 0.1897 0.2156 0.2392 -0.0188 -0.0164 0.0081  74  VAL   A O   
549  C CB  . VAL   A 68  ? 0.2262 0.2581 0.2835 -0.0100 -0.0169 0.0090  74  VAL   A CB  
550  C CG1 . VAL   A 68  ? 0.2436 0.2767 0.3006 -0.0085 -0.0163 0.0086  74  VAL   A CG1 
551  C CG2 . VAL   A 68  ? 0.2418 0.2686 0.2999 -0.0070 -0.0174 0.0076  74  VAL   A CG2 
552  N N   . SER   A 69  ? 0.2020 0.2426 0.2575 -0.0201 -0.0173 0.0119  75  SER   A N   
553  C CA  . SER   A 69  ? 0.2016 0.2484 0.2590 -0.0231 -0.0183 0.0136  75  SER   A CA  
554  C C   . SER   A 69  ? 0.1792 0.2314 0.2453 -0.0184 -0.0193 0.0151  75  SER   A C   
555  O O   . SER   A 69  ? 0.1740 0.2299 0.2460 -0.0150 -0.0188 0.0155  75  SER   A O   
556  C CB  . SER   A 69  ? 0.2401 0.2953 0.2982 -0.0280 -0.0189 0.0163  75  SER   A CB  
557  O OG  . SER   A 69  ? 0.3094 0.3593 0.3593 -0.0332 -0.0179 0.0149  75  SER   A OG  
558  N N   . PHE   A 70  ? 0.1741 0.2272 0.2414 -0.0187 -0.0204 0.0158  76  PHE   A N   
559  C CA  . PHE   A 70  ? 0.1648 0.2219 0.2406 -0.0145 -0.0215 0.0176  76  PHE   A CA  
560  C C   . PHE   A 70  ? 0.1769 0.2418 0.2561 -0.0179 -0.0239 0.0220  76  PHE   A C   
561  O O   . PHE   A 70  ? 0.1913 0.2569 0.2637 -0.0237 -0.0244 0.0221  76  PHE   A O   
562  C CB  . PHE   A 70  ? 0.1604 0.2102 0.2356 -0.0100 -0.0207 0.0145  76  PHE   A CB  
563  C CG  . PHE   A 70  ? 0.1579 0.2017 0.2261 -0.0123 -0.0201 0.0120  76  PHE   A CG  
564  C CD1 . PHE   A 70  ? 0.1632 0.1992 0.2250 -0.0130 -0.0185 0.0088  76  PHE   A CD1 
565  C CD2 . PHE   A 70  ? 0.1601 0.2061 0.2289 -0.0139 -0.0209 0.0127  76  PHE   A CD2 
566  C CE1 . PHE   A 70  ? 0.1817 0.2121 0.2392 -0.0147 -0.0171 0.0057  76  PHE   A CE1 
567  C CE2 . PHE   A 70  ? 0.1747 0.2159 0.2376 -0.0164 -0.0193 0.0093  76  PHE   A CE2 
568  C CZ  . PHE   A 70  ? 0.1737 0.2069 0.2318 -0.0163 -0.0172 0.0055  76  PHE   A CZ  
569  N N   . SER   A 71  ? 0.1714 0.2425 0.2613 -0.0148 -0.0255 0.0258  77  SER   A N   
570  C CA  . SER   A 71  ? 0.1789 0.2586 0.2739 -0.0179 -0.0287 0.0318  77  SER   A CA  
571  C C   . SER   A 71  ? 0.1821 0.2593 0.2730 -0.0196 -0.0296 0.0318  77  SER   A C   
572  O O   . SER   A 71  ? 0.1899 0.2591 0.2770 -0.0168 -0.0276 0.0271  77  SER   A O   
573  C CB  . SER   A 71  ? 0.1887 0.2747 0.2987 -0.0133 -0.0299 0.0362  77  SER   A CB  
574  O OG  . SER   A 71  ? 0.2060 0.2866 0.3211 -0.0076 -0.0288 0.0342  77  SER   A OG  
575  N N   . LYS   A 72  ? 0.1816 0.2666 0.2737 -0.0246 -0.0327 0.0374  78  LYS   A N   
576  C CA  . LYS   A 72  ? 0.1926 0.2769 0.2807 -0.0273 -0.0335 0.0379  78  LYS   A CA  
577  C C   . LYS   A 72  ? 0.1916 0.2740 0.2894 -0.0212 -0.0343 0.0398  78  LYS   A C   
578  O O   . LYS   A 72  ? 0.1858 0.2710 0.2953 -0.0168 -0.0354 0.0434  78  LYS   A O   
579  C CB  . LYS   A 72  ? 0.2196 0.3143 0.3052 -0.0358 -0.0370 0.0440  78  LYS   A CB  
580  C CG  . LYS   A 72  ? 0.2931 0.3880 0.3664 -0.0434 -0.0354 0.0401  78  LYS   A CG  
581  C CD  . LYS   A 72  ? 0.3754 0.4809 0.4438 -0.0535 -0.0387 0.0453  78  LYS   A CD  
582  C CE  . LYS   A 72  ? 0.4525 0.5577 0.5083 -0.0617 -0.0364 0.0403  78  LYS   A CE  
583  N NZ  . LYS   A 72  ? 0.4907 0.6042 0.5381 -0.0726 -0.0381 0.0423  78  LYS   A NZ  
584  N N   . PRO   A 73  ? 0.2049 0.2828 0.2988 -0.0211 -0.0334 0.0372  79  PRO   A N   
585  C CA  . PRO   A 73  ? 0.2053 0.2809 0.3081 -0.0160 -0.0340 0.0389  79  PRO   A CA  
586  C C   . PRO   A 73  ? 0.2072 0.2906 0.3216 -0.0164 -0.0381 0.0480  79  PRO   A C   
587  O O   . PRO   A 73  ? 0.2033 0.2944 0.3157 -0.0228 -0.0413 0.0539  79  PRO   A O   
588  C CB  . PRO   A 73  ? 0.2288 0.3012 0.3243 -0.0184 -0.0329 0.0358  79  PRO   A CB  
589  C CG  . PRO   A 73  ? 0.2435 0.3160 0.3271 -0.0244 -0.0311 0.0319  79  PRO   A CG  
590  C CD  . PRO   A 73  ? 0.2183 0.2928 0.3002 -0.0258 -0.0312 0.0321  79  PRO   A CD  
591  N N   . SER   A 74  ? 0.2085 0.2904 0.3355 -0.0099 -0.0380 0.0492  80  SER   A N   
592  C CA  . SER   A 74  ? 0.2191 0.3076 0.3604 -0.0091 -0.0416 0.0580  80  SER   A CA  
593  C C   . SER   A 74  ? 0.2087 0.2918 0.3630 -0.0023 -0.0406 0.0577  80  SER   A C   
594  O O   . SER   A 74  ? 0.1928 0.2678 0.3440 0.0016  -0.0371 0.0502  80  SER   A O   
595  C CB  . SER   A 74  ? 0.2600 0.3552 0.4076 -0.0087 -0.0422 0.0605  80  SER   A CB  
596  O OG  . SER   A 74  ? 0.3231 0.4200 0.4584 -0.0134 -0.0412 0.0573  80  SER   A OG  
597  N N   . LEU   A 75  ? 0.2112 0.2990 0.3807 -0.0010 -0.0439 0.0661  81  LEU   A N   
598  C CA  . LEU   A 75  ? 0.2195 0.3022 0.4038 0.0053  -0.0428 0.0663  81  LEU   A CA  
599  C C   . LEU   A 75  ? 0.2263 0.3098 0.4217 0.0108  -0.0397 0.0631  81  LEU   A C   
600  O O   . LEU   A 75  ? 0.2312 0.3232 0.4360 0.0103  -0.0420 0.0693  81  LEU   A O   
601  C CB  . LEU   A 75  ? 0.2219 0.3094 0.4181 0.0035  -0.0481 0.0778  81  LEU   A CB  
602  C CG  . LEU   A 75  ? 0.2503 0.3312 0.4617 0.0088  -0.0474 0.0790  81  LEU   A CG  
603  C CD1 . LEU   A 75  ? 0.2518 0.3239 0.4536 0.0086  -0.0450 0.0725  81  LEU   A CD1 
604  C CD2 . LEU   A 75  ? 0.2584 0.3453 0.4838 0.0069  -0.0535 0.0926  81  LEU   A CD2 
605  N N   . ILE   A 76  ? 0.2233 0.2994 0.4169 0.0151  -0.0345 0.0534  82  ILE   A N   
606  C CA  . ILE   A 76  ? 0.2330 0.3100 0.4342 0.0192  -0.0305 0.0485  82  ILE   A CA  
607  C C   . ILE   A 76  ? 0.2291 0.2997 0.4435 0.0250  -0.0267 0.0440  82  ILE   A C   
608  O O   . ILE   A 76  ? 0.2170 0.2799 0.4262 0.0254  -0.0253 0.0395  82  ILE   A O   
609  C CB  . ILE   A 76  ? 0.2615 0.3358 0.4462 0.0178  -0.0272 0.0401  82  ILE   A CB  
610  C CG1 . ILE   A 76  ? 0.2957 0.3748 0.4668 0.0117  -0.0301 0.0431  82  ILE   A CG1 
611  C CG2 . ILE   A 76  ? 0.2685 0.3434 0.4589 0.0212  -0.0223 0.0339  82  ILE   A CG2 
612  C CD1 . ILE   A 76  ? 0.3310 0.4194 0.5075 0.0100  -0.0316 0.0479  82  ILE   A CD1 
613  N N   . PHE   A 77  ? 0.2218 0.2956 0.4534 0.0290  -0.0244 0.0443  83  PHE   A N   
614  C CA  . PHE   A 77  ? 0.2274 0.2949 0.4720 0.0341  -0.0197 0.0385  83  PHE   A CA  
615  C C   . PHE   A 77  ? 0.2363 0.2992 0.4693 0.0343  -0.0138 0.0263  83  PHE   A C   
616  O O   . PHE   A 77  ? 0.2404 0.3078 0.4665 0.0331  -0.0120 0.0232  83  PHE   A O   
617  C CB  . PHE   A 77  ? 0.2261 0.2991 0.4943 0.0385  -0.0184 0.0421  83  PHE   A CB  
618  C CG  . PHE   A 77  ? 0.2403 0.3058 0.5242 0.0435  -0.0134 0.0365  83  PHE   A CG  
619  C CD1 . PHE   A 77  ? 0.2581 0.3175 0.5512 0.0447  -0.0158 0.0412  83  PHE   A CD1 
620  C CD2 . PHE   A 77  ? 0.2504 0.3150 0.5396 0.0463  -0.0060 0.0261  83  PHE   A CD2 
621  C CE1 . PHE   A 77  ? 0.2694 0.3209 0.5772 0.0489  -0.0108 0.0354  83  PHE   A CE1 
622  C CE2 . PHE   A 77  ? 0.2514 0.3088 0.5548 0.0502  -0.0007 0.0196  83  PHE   A CE2 
623  C CZ  . PHE   A 77  ? 0.2593 0.3099 0.5726 0.0517  -0.0030 0.0243  83  PHE   A CZ  
624  N N   . VAL   A 78  ? 0.2298 0.2842 0.4595 0.0351  -0.0113 0.0200  84  VAL   A N   
625  C CA  . VAL   A 78  ? 0.2340 0.2845 0.4528 0.0345  -0.0064 0.0092  84  VAL   A CA  
626  C C   . VAL   A 78  ? 0.2332 0.2791 0.4655 0.0378  -0.0006 0.0019  84  VAL   A C   
627  O O   . VAL   A 78  ? 0.2276 0.2681 0.4698 0.0395  -0.0011 0.0036  84  VAL   A O   
628  C CB  . VAL   A 78  ? 0.2410 0.2863 0.4422 0.0314  -0.0086 0.0075  84  VAL   A CB  
629  C CG1 . VAL   A 78  ? 0.2526 0.2949 0.4429 0.0303  -0.0044 -0.0025 84  VAL   A CG1 
630  C CG2 . VAL   A 78  ? 0.2393 0.2885 0.4283 0.0280  -0.0135 0.0137  84  VAL   A CG2 
631  N N   . GLU   A 79  ? 0.2413 0.2890 0.4730 0.0380  0.0051  -0.0066 85  GLU   A N   
632  C CA  . GLU   A 79  ? 0.2548 0.2990 0.4983 0.0402  0.0121  -0.0156 85  GLU   A CA  
633  C C   . GLU   A 79  ? 0.2581 0.2938 0.4946 0.0385  0.0134  -0.0217 85  GLU   A C   
634  O O   . GLU   A 79  ? 0.2664 0.3004 0.4857 0.0353  0.0100  -0.0210 85  GLU   A O   
635  C CB  . GLU   A 79  ? 0.3024 0.3519 0.5418 0.0388  0.0180  -0.0239 85  GLU   A CB  
636  C CG  . GLU   A 79  ? 0.4195 0.4781 0.6682 0.0404  0.0179  -0.0193 85  GLU   A CG  
637  C CD  . GLU   A 79  ? 0.5464 0.6063 0.8213 0.0457  0.0191  -0.0154 85  GLU   A CD  
638  O OE1 . GLU   A 79  ? 0.5744 0.6301 0.8628 0.0482  0.0253  -0.0229 85  GLU   A OE1 
639  O OE2 . GLU   A 79  ? 0.5856 0.6506 0.8680 0.0470  0.0136  -0.0047 85  GLU   A OE2 
640  N N   . ALA   A 80  ? 0.2577 0.2884 0.5080 0.0405  0.0190  -0.0285 86  ALA   A N   
641  C CA  . ALA   A 80  ? 0.2672 0.2901 0.5119 0.0383  0.0211  -0.0355 86  ALA   A CA  
642  C C   . ALA   A 80  ? 0.2716 0.2965 0.4961 0.0334  0.0231  -0.0435 86  ALA   A C   
643  O O   . ALA   A 80  ? 0.2761 0.3069 0.4967 0.0322  0.0265  -0.0478 86  ALA   A O   
644  C CB  . ALA   A 80  ? 0.2729 0.2904 0.5367 0.0409  0.0280  -0.0428 86  ALA   A CB  
645  N N   . SER   A 81  ? 0.2610 0.2818 0.4726 0.0302  0.0206  -0.0447 87  SER   A N   
646  C CA  . SER   A 81  ? 0.2635 0.2861 0.4565 0.0252  0.0214  -0.0509 87  SER   A CA  
647  C C   . SER   A 81  ? 0.2726 0.2889 0.4640 0.0226  0.0229  -0.0571 87  SER   A C   
648  O O   . SER   A 81  ? 0.2635 0.2736 0.4682 0.0249  0.0236  -0.0563 87  SER   A O   
649  C CB  . SER   A 81  ? 0.2700 0.2957 0.4478 0.0239  0.0146  -0.0434 87  SER   A CB  
650  O OG  . SER   A 81  ? 0.2724 0.2939 0.4509 0.0247  0.0098  -0.0374 87  SER   A OG  
651  N N   . GLU   A 82  ? 0.2862 0.3043 0.4615 0.0174  0.0230  -0.0624 88  GLU   A N   
652  C CA  . GLU   A 82  ? 0.2982 0.3114 0.4710 0.0141  0.0239  -0.0678 88  GLU   A CA  
653  C C   . GLU   A 82  ? 0.2784 0.2879 0.4504 0.0154  0.0175  -0.0597 88  GLU   A C   
654  O O   . GLU   A 82  ? 0.2670 0.2717 0.4405 0.0134  0.0179  -0.0627 88  GLU   A O   
655  C CB  . GLU   A 82  ? 0.3492 0.3665 0.5056 0.0075  0.0253  -0.0750 88  GLU   A CB  
656  C CG  . GLU   A 82  ? 0.4482 0.4706 0.5888 0.0058  0.0189  -0.0685 88  GLU   A CG  
657  C CD  . GLU   A 82  ? 0.5898 0.6164 0.7153 -0.0012 0.0189  -0.0739 88  GLU   A CD  
658  O OE1 . GLU   A 82  ? 0.6069 0.6393 0.7238 -0.0041 0.0200  -0.0755 88  GLU   A OE1 
659  O OE2 . GLU   A 82  ? 0.6446 0.6693 0.7670 -0.0042 0.0177  -0.0761 88  GLU   A OE2 
660  N N   . TYR   A 83  ? 0.2696 0.2816 0.4397 0.0181  0.0120  -0.0498 89  TYR   A N   
661  C CA  . TYR   A 83  ? 0.2585 0.2687 0.4266 0.0186  0.0063  -0.0424 89  TYR   A CA  
662  C C   . TYR   A 83  ? 0.2439 0.2509 0.4256 0.0222  0.0044  -0.0349 89  TYR   A C   
663  O O   . TYR   A 83  ? 0.2302 0.2345 0.4124 0.0216  0.0012  -0.0309 89  TYR   A O   
664  C CB  . TYR   A 83  ? 0.2584 0.2736 0.4131 0.0179  0.0015  -0.0371 89  TYR   A CB  
665  C CG  . TYR   A 83  ? 0.2808 0.2994 0.4220 0.0140  0.0019  -0.0422 89  TYR   A CG  
666  C CD1 . TYR   A 83  ? 0.3010 0.3191 0.4358 0.0107  0.0007  -0.0451 89  TYR   A CD1 
667  C CD2 . TYR   A 83  ? 0.3051 0.3282 0.4399 0.0133  0.0030  -0.0434 89  TYR   A CD2 
668  C CE1 . TYR   A 83  ? 0.3224 0.3448 0.4452 0.0066  0.0002  -0.0485 89  TYR   A CE1 
669  C CE2 . TYR   A 83  ? 0.3243 0.3510 0.4466 0.0091  0.0028  -0.0468 89  TYR   A CE2 
670  C CZ  . TYR   A 83  ? 0.3441 0.3706 0.4606 0.0058  0.0012  -0.0492 89  TYR   A CZ  
671  O OH  . TYR   A 83  ? 0.3816 0.4129 0.4861 0.0012  0.0000  -0.0512 89  TYR   A OH  
672  N N   . TYR   A 84  ? 0.2327 0.2411 0.4255 0.0256  0.0059  -0.0323 90  TYR   A N   
673  C CA  . TYR   A 84  ? 0.2260 0.2326 0.4328 0.0287  0.0033  -0.0238 90  TYR   A CA  
674  C C   . TYR   A 84  ? 0.2392 0.2451 0.4637 0.0324  0.0079  -0.0257 90  TYR   A C   
675  O O   . TYR   A 84  ? 0.2398 0.2501 0.4628 0.0328  0.0113  -0.0303 90  TYR   A O   
676  C CB  . TYR   A 84  ? 0.2141 0.2265 0.4152 0.0291  -0.0021 -0.0143 90  TYR   A CB  
677  C CG  . TYR   A 84  ? 0.1912 0.2052 0.3771 0.0262  -0.0064 -0.0114 90  TYR   A CG  
678  C CD1 . TYR   A 84  ? 0.1921 0.2038 0.3790 0.0250  -0.0098 -0.0064 90  TYR   A CD1 
679  C CD2 . TYR   A 84  ? 0.1915 0.2093 0.3631 0.0246  -0.0070 -0.0136 90  TYR   A CD2 
680  C CE1 . TYR   A 84  ? 0.1848 0.1986 0.3591 0.0224  -0.0130 -0.0044 90  TYR   A CE1 
681  C CE2 . TYR   A 84  ? 0.1870 0.2061 0.3470 0.0226  -0.0105 -0.0112 90  TYR   A CE2 
682  C CZ  . TYR   A 84  ? 0.1874 0.2048 0.3490 0.0215  -0.0132 -0.0071 90  TYR   A CZ  
683  O OH  . TYR   A 84  ? 0.1754 0.1948 0.3266 0.0196  -0.0159 -0.0056 90  TYR   A OH  
684  N N   . PRO   A 85  ? 0.2478 0.2495 0.4897 0.0351  0.0074  -0.0207 91  PRO   A N   
685  C CA  . PRO   A 85  ? 0.2624 0.2648 0.5238 0.0395  0.0109  -0.0205 91  PRO   A CA  
686  C C   . PRO   A 85  ? 0.2740 0.2853 0.5353 0.0410  0.0070  -0.0118 91  PRO   A C   
687  O O   . PRO   A 85  ? 0.2802 0.2957 0.5266 0.0385  0.0018  -0.0063 91  PRO   A O   
688  C CB  . PRO   A 85  ? 0.2650 0.2602 0.5444 0.0416  0.0096  -0.0149 91  PRO   A CB  
689  C CG  . PRO   A 85  ? 0.2659 0.2608 0.5341 0.0385  0.0028  -0.0069 91  PRO   A CG  
690  C CD  . PRO   A 85  ? 0.2431 0.2401 0.4887 0.0344  0.0029  -0.0135 91  PRO   A CD  
691  N N   . ALA   A 86  ? 0.2702 0.2847 0.5486 0.0449  0.0096  -0.0106 92  ALA   A N   
692  C CA  . ALA   A 86  ? 0.2699 0.2937 0.5494 0.0459  0.0057  -0.0021 92  ALA   A CA  
693  C C   . ALA   A 86  ? 0.2641 0.2886 0.5464 0.0454  -0.0021 0.0113  92  ALA   A C   
694  O O   . ALA   A 86  ? 0.2734 0.2923 0.5696 0.0470  -0.0031 0.0153  92  ALA   A O   
695  C CB  . ALA   A 86  ? 0.2681 0.2955 0.5687 0.0504  0.0102  -0.0033 92  ALA   A CB  
696  N N   . ARG   A 87  ? 0.2522 0.2828 0.5195 0.0421  -0.0074 0.0173  93  ARG   A N   
697  C CA  . ARG   A 87  ? 0.2333 0.2655 0.4996 0.0399  -0.0145 0.0290  93  ARG   A CA  
698  C C   . ARG   A 87  ? 0.2275 0.2687 0.4808 0.0366  -0.0187 0.0344  93  ARG   A C   
699  O O   . ARG   A 87  ? 0.2330 0.2778 0.4779 0.0363  -0.0162 0.0290  93  ARG   A O   
700  C CB  . ARG   A 87  ? 0.2410 0.2663 0.4960 0.0369  -0.0156 0.0269  93  ARG   A CB  
701  C CG  . ARG   A 87  ? 0.2402 0.2675 0.4715 0.0328  -0.0168 0.0233  93  ARG   A CG  
702  C CD  . ARG   A 87  ? 0.2315 0.2524 0.4526 0.0312  -0.0144 0.0151  93  ARG   A CD  
703  N NE  . ARG   A 87  ? 0.2224 0.2456 0.4249 0.0276  -0.0169 0.0150  93  ARG   A NE  
704  C CZ  . ARG   A 87  ? 0.2250 0.2515 0.4150 0.0267  -0.0160 0.0111  93  ARG   A CZ  
705  N NH1 . ARG   A 87  ? 0.2028 0.2312 0.3951 0.0286  -0.0127 0.0068  93  ARG   A NH1 
706  N NH2 . ARG   A 87  ? 0.2073 0.2349 0.3829 0.0239  -0.0181 0.0111  93  ARG   A NH2 
707  N N   . TYR   A 88  ? 0.2176 0.2623 0.4684 0.0334  -0.0249 0.0446  94  TYR   A N   
708  C CA  . TYR   A 88  ? 0.2185 0.2707 0.4552 0.0291  -0.0286 0.0488  94  TYR   A CA  
709  C C   . TYR   A 88  ? 0.2052 0.2538 0.4220 0.0253  -0.0288 0.0443  94  TYR   A C   
710  O O   . TYR   A 88  ? 0.2142 0.2582 0.4304 0.0241  -0.0300 0.0455  94  TYR   A O   
711  C CB  . TYR   A 88  ? 0.2275 0.2864 0.4716 0.0265  -0.0350 0.0621  94  TYR   A CB  
712  C CG  . TYR   A 88  ? 0.2397 0.3054 0.5022 0.0297  -0.0358 0.0678  94  TYR   A CG  
713  C CD1 . TYR   A 88  ? 0.2550 0.3294 0.5133 0.0282  -0.0364 0.0688  94  TYR   A CD1 
714  C CD2 . TYR   A 88  ? 0.2529 0.3160 0.5382 0.0344  -0.0354 0.0717  94  TYR   A CD2 
715  C CE1 . TYR   A 88  ? 0.2659 0.3476 0.5421 0.0312  -0.0369 0.0738  94  TYR   A CE1 
716  C CE2 . TYR   A 88  ? 0.2627 0.3324 0.5673 0.0381  -0.0356 0.0765  94  TYR   A CE2 
717  C CZ  . TYR   A 88  ? 0.2731 0.3528 0.5730 0.0364  -0.0365 0.0777  94  TYR   A CZ  
718  O OH  . TYR   A 88  ? 0.3015 0.3891 0.6213 0.0399  -0.0367 0.0827  94  TYR   A OH  
719  N N   . GLN   A 89  ? 0.1807 0.2315 0.3827 0.0234  -0.0276 0.0395  95  GLN   A N   
720  C CA  . GLN   A 89  ? 0.1625 0.2108 0.3471 0.0201  -0.0278 0.0357  95  GLN   A CA  
721  C C   . GLN   A 89  ? 0.1660 0.2210 0.3416 0.0151  -0.0316 0.0418  95  GLN   A C   
722  O O   . GLN   A 89  ? 0.1668 0.2275 0.3426 0.0143  -0.0323 0.0440  95  GLN   A O   
723  C CB  . GLN   A 89  ? 0.1557 0.2008 0.3305 0.0214  -0.0236 0.0260  95  GLN   A CB  
724  C CG  . GLN   A 89  ? 0.1492 0.1923 0.3083 0.0187  -0.0240 0.0227  95  GLN   A CG  
725  C CD  . GLN   A 89  ? 0.1656 0.2047 0.3176 0.0201  -0.0206 0.0141  95  GLN   A CD  
726  O OE1 . GLN   A 89  ? 0.1887 0.2247 0.3466 0.0225  -0.0178 0.0095  95  GLN   A OE1 
727  N NE2 . GLN   A 89  ? 0.1443 0.1834 0.2838 0.0183  -0.0209 0.0120  95  GLN   A NE2 
728  N N   . SER   A 90  ? 0.1609 0.2156 0.3285 0.0112  -0.0338 0.0440  96  SER   A N   
729  C CA  . SER   A 90  ? 0.1671 0.2282 0.3255 0.0053  -0.0367 0.0487  96  SER   A CA  
730  C C   . SER   A 90  ? 0.1688 0.2282 0.3113 0.0034  -0.0344 0.0416  96  SER   A C   
731  O O   . SER   A 90  ? 0.1624 0.2159 0.3012 0.0063  -0.0314 0.0344  96  SER   A O   
732  C CB  . SER   A 90  ? 0.2006 0.2637 0.3597 0.0011  -0.0402 0.0554  96  SER   A CB  
733  O OG  . SER   A 90  ? 0.2362 0.2935 0.3901 0.0014  -0.0382 0.0503  96  SER   A OG  
734  N N   . HIS   A 91  ? 0.1618 0.2267 0.2960 -0.0019 -0.0358 0.0439  97  HIS   A N   
735  C CA  . HIS   A 91  ? 0.1716 0.2348 0.2922 -0.0043 -0.0335 0.0378  97  HIS   A CA  
736  C C   . HIS   A 91  ? 0.1697 0.2283 0.2886 0.0001  -0.0305 0.0315  97  HIS   A C   
737  O O   . HIS   A 91  ? 0.1656 0.2195 0.2764 0.0006  -0.0282 0.0256  97  HIS   A O   
738  C CB  . HIS   A 91  ? 0.1873 0.2472 0.3013 -0.0059 -0.0324 0.0345  97  HIS   A CB  
739  C CG  . HIS   A 91  ? 0.2270 0.2923 0.3407 -0.0116 -0.0351 0.0405  97  HIS   A CG  
740  N ND1 . HIS   A 91  ? 0.2526 0.3228 0.3565 -0.0186 -0.0353 0.0409  97  HIS   A ND1 
741  C CD2 . HIS   A 91  ? 0.2422 0.3086 0.3640 -0.0117 -0.0376 0.0463  97  HIS   A CD2 
742  C CE1 . HIS   A 91  ? 0.2488 0.3238 0.3542 -0.0232 -0.0380 0.0471  97  HIS   A CE1 
743  N NE2 . HIS   A 91  ? 0.2501 0.3227 0.3664 -0.0191 -0.0397 0.0510  97  HIS   A NE2 
744  N N   . LEU   A 92  ? 0.1560 0.2165 0.2832 0.0029  -0.0305 0.0331  98  LEU   A N   
745  C CA  . LEU   A 92  ? 0.1607 0.2183 0.2866 0.0061  -0.0276 0.0276  98  LEU   A CA  
746  C C   . LEU   A 92  ? 0.1550 0.2168 0.2759 0.0030  -0.0278 0.0286  98  LEU   A C   
747  O O   . LEU   A 92  ? 0.1603 0.2291 0.2852 0.0002  -0.0303 0.0345  98  LEU   A O   
748  C CB  . LEU   A 92  ? 0.1607 0.2180 0.2996 0.0109  -0.0264 0.0275  98  LEU   A CB  
749  C CG  . LEU   A 92  ? 0.1818 0.2366 0.3196 0.0138  -0.0228 0.0211  98  LEU   A CG  
750  C CD1 . LEU   A 92  ? 0.1707 0.2192 0.2988 0.0143  -0.0212 0.0151  98  LEU   A CD1 
751  C CD2 . LEU   A 92  ? 0.1867 0.2419 0.3386 0.0179  -0.0207 0.0202  98  LEU   A CD2 
752  N N   . MET   A 93  ? 0.1508 0.2087 0.2634 0.0032  -0.0255 0.0233  99  MET   A N   
753  C CA  . MET   A 93  ? 0.1575 0.2184 0.2649 -0.0001 -0.0254 0.0237  99  MET   A CA  
754  C C   . MET   A 93  ? 0.1634 0.2230 0.2724 0.0029  -0.0229 0.0203  99  MET   A C   
755  O O   . MET   A 93  ? 0.1642 0.2182 0.2709 0.0058  -0.0212 0.0158  99  MET   A O   
756  C CB  . MET   A 93  ? 0.1793 0.2358 0.2745 -0.0036 -0.0247 0.0207  99  MET   A CB  
757  C CG  . MET   A 93  ? 0.2054 0.2634 0.2976 -0.0073 -0.0261 0.0225  99  MET   A CG  
758  S SD  . MET   A 93  ? 0.2286 0.2803 0.3089 -0.0104 -0.0237 0.0168  99  MET   A SD  
759  C CE  . MET   A 93  ? 0.2308 0.2745 0.3125 -0.0037 -0.0220 0.0121  99  MET   A CE  
760  N N   . LEU   A 94  ? 0.1445 0.2099 0.2575 0.0019  -0.0229 0.0224  100 LEU   A N   
761  C CA  . LEU   A 94  ? 0.1590 0.2245 0.2735 0.0039  -0.0201 0.0190  100 LEU   A CA  
762  C C   . LEU   A 94  ? 0.1681 0.2332 0.2728 0.0001  -0.0195 0.0179  100 LEU   A C   
763  O O   . LEU   A 94  ? 0.1696 0.2375 0.2704 -0.0043 -0.0212 0.0207  100 LEU   A O   
764  C CB  . LEU   A 94  ? 0.1677 0.2410 0.2964 0.0060  -0.0196 0.0215  100 LEU   A CB  
765  C CG  . LEU   A 94  ? 0.2104 0.2840 0.3521 0.0102  -0.0196 0.0228  100 LEU   A CG  
766  C CD1 . LEU   A 94  ? 0.2241 0.3051 0.3816 0.0128  -0.0181 0.0245  100 LEU   A CD1 
767  C CD2 . LEU   A 94  ? 0.2269 0.2929 0.3664 0.0133  -0.0171 0.0168  100 LEU   A CD2 
768  N N   . ALA   A 95  ? 0.1576 0.2202 0.2591 0.0011  -0.0171 0.0139  101 ALA   A N   
769  C CA  . ALA   A 95  ? 0.1750 0.2366 0.2679 -0.0024 -0.0163 0.0131  101 ALA   A CA  
770  C C   . ALA   A 95  ? 0.1726 0.2368 0.2676 -0.0014 -0.0135 0.0103  101 ALA   A C   
771  O O   . ALA   A 95  ? 0.1667 0.2310 0.2672 0.0020  -0.0117 0.0075  101 ALA   A O   
772  C CB  . ALA   A 95  ? 0.1835 0.2359 0.2657 -0.0033 -0.0168 0.0111  101 ALA   A CB  
773  N N   . VAL   A 96  ? 0.1605 0.2263 0.2501 -0.0051 -0.0127 0.0105  102 VAL   A N   
774  C CA  . VAL   A 96  ? 0.1560 0.2244 0.2450 -0.0055 -0.0098 0.0075  102 VAL   A CA  
775  C C   . VAL   A 96  ? 0.1802 0.2403 0.2580 -0.0064 -0.0101 0.0057  102 VAL   A C   
776  O O   . VAL   A 96  ? 0.1879 0.2423 0.2577 -0.0089 -0.0119 0.0074  102 VAL   A O   
777  C CB  . VAL   A 96  ? 0.1567 0.2316 0.2453 -0.0098 -0.0090 0.0093  102 VAL   A CB  
778  C CG1 . VAL   A 96  ? 0.1646 0.2418 0.2498 -0.0116 -0.0059 0.0063  102 VAL   A CG1 
779  C CG2 . VAL   A 96  ? 0.1614 0.2460 0.2631 -0.0086 -0.0092 0.0120  102 VAL   A CG2 
780  N N   . GLY   A 97  ? 0.1844 0.2440 0.2625 -0.0046 -0.0084 0.0023  103 GLY   A N   
781  C CA  . GLY   A 97  ? 0.1898 0.2432 0.2585 -0.0056 -0.0093 0.0014  103 GLY   A CA  
782  C C   . GLY   A 97  ? 0.1913 0.2465 0.2620 -0.0040 -0.0072 -0.0028 103 GLY   A C   
783  O O   . GLY   A 97  ? 0.1945 0.2532 0.2746 -0.0011 -0.0051 -0.0053 103 GLY   A O   
784  N N   . HIS   A 98  ? 0.1863 0.2397 0.2485 -0.0066 -0.0075 -0.0035 104 HIS   A N   
785  C CA  . HIS   A 98  ? 0.1830 0.2387 0.2450 -0.0067 -0.0055 -0.0079 104 HIS   A CA  
786  C C   . HIS   A 98  ? 0.1870 0.2385 0.2523 -0.0029 -0.0071 -0.0088 104 HIS   A C   
787  O O   . HIS   A 98  ? 0.1960 0.2417 0.2581 -0.0017 -0.0107 -0.0056 104 HIS   A O   
788  C CB  . HIS   A 98  ? 0.1860 0.2419 0.2367 -0.0117 -0.0063 -0.0072 104 HIS   A CB  
789  C CG  . HIS   A 98  ? 0.2071 0.2670 0.2563 -0.0134 -0.0039 -0.0123 104 HIS   A CG  
790  N ND1 . HIS   A 98  ? 0.2181 0.2850 0.2720 -0.0147 0.0016  -0.0182 104 HIS   A ND1 
791  C CD2 . HIS   A 98  ? 0.2096 0.2675 0.2542 -0.0141 -0.0060 -0.0128 104 HIS   A CD2 
792  C CE1 . HIS   A 98  ? 0.2215 0.2900 0.2726 -0.0166 0.0030  -0.0228 104 HIS   A CE1 
793  N NE2 . HIS   A 98  ? 0.2166 0.2802 0.2614 -0.0166 -0.0017 -0.0194 104 HIS   A NE2 
794  N N   . SER   A 99  ? 0.1809 0.2352 0.2522 -0.0014 -0.0042 -0.0137 105 SER   A N   
795  C CA  . SER   A 99  ? 0.1763 0.2270 0.2498 0.0012  -0.0054 -0.0152 105 SER   A CA  
796  C C   . SER   A 99  ? 0.1933 0.2474 0.2699 0.0003  -0.0014 -0.0219 105 SER   A C   
797  O O   . SER   A 99  ? 0.2049 0.2637 0.2874 -0.0001 0.0031  -0.0256 105 SER   A O   
798  C CB  . SER   A 99  ? 0.1924 0.2401 0.2740 0.0055  -0.0071 -0.0127 105 SER   A CB  
799  O OG  . SER   A 99  ? 0.2046 0.2559 0.2972 0.0075  -0.0042 -0.0142 105 SER   A OG  
800  N N   . GLU   A 100 ? 0.1904 0.2424 0.2632 -0.0004 -0.0027 -0.0237 106 GLU   A N   
801  C CA  . GLU   A 100 ? 0.2070 0.2609 0.2814 -0.0020 0.0007  -0.0306 106 GLU   A CA  
802  C C   . GLU   A 100 ? 0.2125 0.2617 0.2917 0.0013  -0.0013 -0.0305 106 GLU   A C   
803  O O   . GLU   A 100 ? 0.2060 0.2516 0.2842 0.0036  -0.0056 -0.0252 106 GLU   A O   
804  C CB  . GLU   A 100 ? 0.2389 0.2963 0.3011 -0.0082 0.0004  -0.0323 106 GLU   A CB  
805  C CG  . GLU   A 100 ? 0.2428 0.3054 0.2998 -0.0124 0.0028  -0.0326 106 GLU   A CG  
806  C CD  . GLU   A 100 ? 0.2648 0.3316 0.3085 -0.0196 0.0016  -0.0323 106 GLU   A CD  
807  O OE1 . GLU   A 100 ? 0.2911 0.3595 0.3303 -0.0229 0.0015  -0.0357 106 GLU   A OE1 
808  O OE2 . GLU   A 100 ? 0.2508 0.3199 0.2884 -0.0227 0.0008  -0.0287 106 GLU   A OE2 
809  N N   . PRO   A 101 ? 0.2227 0.2718 0.3073 0.0012  0.0020  -0.0367 107 PRO   A N   
810  C CA  . PRO   A 101 ? 0.2326 0.2772 0.3225 0.0042  0.0000  -0.0361 107 PRO   A CA  
811  C C   . PRO   A 101 ? 0.2204 0.2632 0.3029 0.0037  -0.0055 -0.0315 107 PRO   A C   
812  O O   . PRO   A 101 ? 0.2269 0.2663 0.3133 0.0071  -0.0083 -0.0275 107 PRO   A O   
813  C CB  . PRO   A 101 ? 0.2492 0.2943 0.3428 0.0021  0.0047  -0.0445 107 PRO   A CB  
814  C CG  . PRO   A 101 ? 0.2525 0.3015 0.3495 0.0008  0.0105  -0.0494 107 PRO   A CG  
815  C CD  . PRO   A 101 ? 0.2270 0.2797 0.3150 -0.0013 0.0084  -0.0449 107 PRO   A CD  
816  N N   . GLY   A 102 ? 0.1980 0.2436 0.2703 -0.0006 -0.0072 -0.0316 108 GLY   A N   
817  C CA  . GLY   A 102 ? 0.1909 0.2360 0.2573 -0.0012 -0.0125 -0.0270 108 GLY   A CA  
818  C C   . GLY   A 102 ? 0.1670 0.2094 0.2326 0.0017  -0.0162 -0.0200 108 GLY   A C   
819  O O   . GLY   A 102 ? 0.1844 0.2258 0.2480 0.0023  -0.0202 -0.0160 108 GLY   A O   
820  N N   . ASP   A 103 ? 0.1498 0.1914 0.2171 0.0030  -0.0146 -0.0185 109 ASP   A N   
821  C CA  . ASP   A 103 ? 0.1626 0.2010 0.2294 0.0052  -0.0173 -0.0128 109 ASP   A CA  
822  C C   . ASP   A 103 ? 0.1758 0.2108 0.2493 0.0092  -0.0183 -0.0114 109 ASP   A C   
823  O O   . ASP   A 103 ? 0.1728 0.2050 0.2458 0.0106  -0.0204 -0.0076 109 ASP   A O   
824  C CB  . ASP   A 103 ? 0.1670 0.2063 0.2330 0.0044  -0.0153 -0.0118 109 ASP   A CB  
825  C CG  . ASP   A 103 ? 0.1809 0.2232 0.2385 -0.0002 -0.0155 -0.0114 109 ASP   A CG  
826  O OD1 . ASP   A 103 ? 0.1883 0.2301 0.2401 -0.0020 -0.0189 -0.0084 109 ASP   A OD1 
827  O OD2 . ASP   A 103 ? 0.2103 0.2561 0.2675 -0.0023 -0.0122 -0.0135 109 ASP   A OD2 
828  N N   . CYS   A 104 ? 0.1748 0.2099 0.2548 0.0105  -0.0165 -0.0145 110 CYS   A N   
829  C CA  . CYS   A 104 ? 0.1781 0.2107 0.2639 0.0133  -0.0175 -0.0128 110 CYS   A CA  
830  C C   . CYS   A 104 ? 0.1688 0.2001 0.2520 0.0139  -0.0207 -0.0104 110 CYS   A C   
831  O O   . CYS   A 104 ? 0.1567 0.1894 0.2363 0.0124  -0.0223 -0.0109 110 CYS   A O   
832  C CB  . CYS   A 104 ? 0.1969 0.2295 0.2898 0.0140  -0.0156 -0.0161 110 CYS   A CB  
833  S SG  . CYS   A 104 ? 0.1976 0.2313 0.2990 0.0151  -0.0118 -0.0176 110 CYS   A SG  
834  N N   . GLY   A 105 ? 0.1727 0.2020 0.2577 0.0155  -0.0216 -0.0077 111 GLY   A N   
835  C CA  . GLY   A 105 ? 0.1728 0.2010 0.2571 0.0165  -0.0237 -0.0059 111 GLY   A CA  
836  C C   . GLY   A 105 ? 0.1768 0.2026 0.2576 0.0165  -0.0247 -0.0032 111 GLY   A C   
837  O O   . GLY   A 105 ? 0.1808 0.2049 0.2631 0.0178  -0.0256 -0.0020 111 GLY   A O   
838  N N   . GLY   A 106 ? 0.1796 0.2052 0.2563 0.0149  -0.0242 -0.0025 112 GLY   A N   
839  C CA  . GLY   A 106 ? 0.1785 0.2010 0.2519 0.0145  -0.0250 0.0002  112 GLY   A CA  
840  C C   . GLY   A 106 ? 0.1589 0.1788 0.2342 0.0151  -0.0237 0.0004  112 GLY   A C   
841  O O   . GLY   A 106 ? 0.1571 0.1788 0.2343 0.0147  -0.0223 -0.0005 112 GLY   A O   
842  N N   . ILE   A 107 ? 0.1498 0.1658 0.2254 0.0158  -0.0242 0.0015  113 ILE   A N   
843  C CA  . ILE   A 107 ? 0.1489 0.1627 0.2254 0.0153  -0.0224 0.0006  113 ILE   A CA  
844  C C   . ILE   A 107 ? 0.1595 0.1719 0.2320 0.0126  -0.0212 0.0013  113 ILE   A C   
845  O O   . ILE   A 107 ? 0.1590 0.1688 0.2283 0.0116  -0.0220 0.0029  113 ILE   A O   
846  C CB  . ILE   A 107 ? 0.1585 0.1684 0.2382 0.0171  -0.0224 0.0004  113 ILE   A CB  
847  C CG1 . ILE   A 107 ? 0.1581 0.1711 0.2430 0.0193  -0.0227 -0.0009 113 ILE   A CG1 
848  C CG2 . ILE   A 107 ? 0.1727 0.1787 0.2519 0.0156  -0.0197 -0.0013 113 ILE   A CG2 
849  C CD1 . ILE   A 107 ? 0.1796 0.1902 0.2699 0.0218  -0.0227 -0.0011 113 ILE   A CD1 
850  N N   . LEU   A 108 ? 0.1481 0.1622 0.2206 0.0107  -0.0197 0.0004  114 LEU   A N   
851  C CA  . LEU   A 108 ? 0.1489 0.1622 0.2179 0.0073  -0.0187 0.0008  114 LEU   A CA  
852  C C   . LEU   A 108 ? 0.1589 0.1682 0.2276 0.0061  -0.0169 -0.0014 114 LEU   A C   
853  O O   . LEU   A 108 ? 0.1672 0.1785 0.2385 0.0065  -0.0161 -0.0030 114 LEU   A O   
854  C CB  . LEU   A 108 ? 0.1603 0.1797 0.2303 0.0054  -0.0185 0.0018  114 LEU   A CB  
855  C CG  . LEU   A 108 ? 0.1932 0.2138 0.2599 0.0009  -0.0177 0.0024  114 LEU   A CG  
856  C CD1 . LEU   A 108 ? 0.1907 0.2100 0.2540 -0.0006 -0.0178 0.0035  114 LEU   A CD1 
857  C CD2 . LEU   A 108 ? 0.2056 0.2334 0.2753 -0.0007 -0.0184 0.0045  114 LEU   A CD2 
858  N N   . ARG   A 109 ? 0.1554 0.1596 0.2212 0.0040  -0.0157 -0.0019 115 ARG   A N   
859  C CA  . ARG   A 109 ? 0.1527 0.1525 0.2189 0.0026  -0.0130 -0.0052 115 ARG   A CA  
860  C C   . ARG   A 109 ? 0.1834 0.1806 0.2446 -0.0025 -0.0114 -0.0062 115 ARG   A C   
861  O O   . ARG   A 109 ? 0.1926 0.1896 0.2506 -0.0040 -0.0126 -0.0037 115 ARG   A O   
862  C CB  . ARG   A 109 ? 0.1609 0.1544 0.2318 0.0065  -0.0130 -0.0057 115 ARG   A CB  
863  C CG  . ARG   A 109 ? 0.1862 0.1742 0.2558 0.0070  -0.0146 -0.0025 115 ARG   A CG  
864  C CD  . ARG   A 109 ? 0.2165 0.1989 0.2927 0.0112  -0.0153 -0.0016 115 ARG   A CD  
865  N NE  . ARG   A 109 ? 0.2522 0.2394 0.3317 0.0148  -0.0183 0.0008  115 ARG   A NE  
866  C CZ  . ARG   A 109 ? 0.2563 0.2446 0.3428 0.0183  -0.0183 -0.0002 115 ARG   A CZ  
867  N NH1 . ARG   A 109 ? 0.2358 0.2208 0.3273 0.0190  -0.0149 -0.0041 115 ARG   A NH1 
868  N NH2 . ARG   A 109 ? 0.2364 0.2297 0.3248 0.0206  -0.0213 0.0021  115 ARG   A NH2 
869  N N   . CYS   A 110 ? 0.1952 0.1903 0.2554 -0.0057 -0.0082 -0.0103 116 CYS   A N   
870  C CA  . CYS   A 110 ? 0.2192 0.2113 0.2743 -0.0115 -0.0060 -0.0123 116 CYS   A CA  
871  C C   . CYS   A 110 ? 0.2642 0.2471 0.3223 -0.0111 -0.0020 -0.0175 116 CYS   A C   
872  O O   . CYS   A 110 ? 0.2663 0.2463 0.3311 -0.0058 -0.0017 -0.0182 116 CYS   A O   
873  C CB  . CYS   A 110 ? 0.2426 0.2427 0.2933 -0.0172 -0.0055 -0.0130 116 CYS   A CB  
874  S SG  . CYS   A 110 ? 0.2595 0.2629 0.3120 -0.0182 -0.0028 -0.0174 116 CYS   A SG  
875  N N   . GLN   A 111 ? 0.2939 0.2729 0.3478 -0.0170 0.0014  -0.0216 117 GLN   A N   
876  C CA  . GLN   A 111 ? 0.3275 0.2973 0.3855 -0.0169 0.0062  -0.0276 117 GLN   A CA  
877  C C   . GLN   A 111 ? 0.3354 0.3084 0.3979 -0.0156 0.0094  -0.0325 117 GLN   A C   
878  O O   . GLN   A 111 ? 0.3602 0.3264 0.4299 -0.0127 0.0130  -0.0368 117 GLN   A O   
879  C CB  . GLN   A 111 ? 0.3736 0.3391 0.4252 -0.0249 0.0098  -0.0321 117 GLN   A CB  
880  C CG  . GLN   A 111 ? 0.4428 0.4178 0.4867 -0.0327 0.0112  -0.0348 117 GLN   A CG  
881  C CD  . GLN   A 111 ? 0.5459 0.5183 0.5824 -0.0418 0.0142  -0.0390 117 GLN   A CD  
882  O OE1 . GLN   A 111 ? 0.5538 0.5313 0.5839 -0.0465 0.0114  -0.0352 117 GLN   A OE1 
883  N NE2 . GLN   A 111 ? 0.5696 0.5344 0.6072 -0.0447 0.0204  -0.0473 117 GLN   A NE2 
884  N N   . HIS   A 112 ? 0.3065 0.2898 0.3654 -0.0178 0.0081  -0.0315 118 HIS   A N   
885  C CA  . HIS   A 112 ? 0.2892 0.2769 0.3509 -0.0179 0.0110  -0.0358 118 HIS   A CA  
886  C C   . HIS   A 112 ? 0.2822 0.2722 0.3519 -0.0103 0.0086  -0.0330 118 HIS   A C   
887  O O   . HIS   A 112 ? 0.2996 0.2922 0.3734 -0.0096 0.0115  -0.0368 118 HIS   A O   
888  C CB  . HIS   A 112 ? 0.2914 0.2894 0.3450 -0.0255 0.0108  -0.0358 118 HIS   A CB  
889  C CG  . HIS   A 112 ? 0.3216 0.3195 0.3667 -0.0341 0.0126  -0.0381 118 HIS   A CG  
890  N ND1 . HIS   A 112 ? 0.3454 0.3477 0.3851 -0.0370 0.0083  -0.0324 118 HIS   A ND1 
891  C CD2 . HIS   A 112 ? 0.3407 0.3349 0.3824 -0.0404 0.0184  -0.0459 118 HIS   A CD2 
892  C CE1 . HIS   A 112 ? 0.3589 0.3608 0.3915 -0.0454 0.0110  -0.0361 118 HIS   A CE1 
893  N NE2 . HIS   A 112 ? 0.3572 0.3538 0.3903 -0.0480 0.0172  -0.0447 118 HIS   A NE2 
894  N N   . GLY   A 113 ? 0.2530 0.2430 0.3242 -0.0055 0.0036  -0.0266 119 GLY   A N   
895  C CA  . GLY   A 113 ? 0.2299 0.2227 0.3077 0.0006  0.0011  -0.0239 119 GLY   A CA  
896  C C   . GLY   A 113 ? 0.2120 0.2105 0.2871 0.0019  -0.0039 -0.0180 119 GLY   A C   
897  O O   . GLY   A 113 ? 0.2085 0.2070 0.2788 -0.0001 -0.0058 -0.0151 119 GLY   A O   
898  N N   . VAL   A 114 ? 0.1832 0.1864 0.2624 0.0051  -0.0057 -0.0166 120 VAL   A N   
899  C CA  . VAL   A 114 ? 0.1747 0.1826 0.2529 0.0066  -0.0096 -0.0121 120 VAL   A CA  
900  C C   . VAL   A 114 ? 0.1645 0.1786 0.2383 0.0020  -0.0100 -0.0109 120 VAL   A C   
901  O O   . VAL   A 114 ? 0.1669 0.1849 0.2405 -0.0008 -0.0084 -0.0126 120 VAL   A O   
902  C CB  . VAL   A 114 ? 0.1745 0.1850 0.2586 0.0109  -0.0111 -0.0114 120 VAL   A CB  
903  C CG1 . VAL   A 114 ? 0.1767 0.1913 0.2599 0.0117  -0.0144 -0.0079 120 VAL   A CG1 
904  C CG2 . VAL   A 114 ? 0.1777 0.1834 0.2669 0.0153  -0.0119 -0.0110 120 VAL   A CG2 
905  N N   . VAL   A 115 ? 0.1544 0.1704 0.2259 0.0013  -0.0123 -0.0074 121 VAL   A N   
906  C CA  . VAL   A 115 ? 0.1665 0.1888 0.2359 -0.0025 -0.0135 -0.0047 121 VAL   A CA  
907  C C   . VAL   A 115 ? 0.1742 0.2006 0.2481 0.0003  -0.0159 -0.0018 121 VAL   A C   
908  O O   . VAL   A 115 ? 0.1918 0.2233 0.2667 -0.0021 -0.0167 0.0002  121 VAL   A O   
909  C CB  . VAL   A 115 ? 0.1823 0.2046 0.2480 -0.0050 -0.0143 -0.0027 121 VAL   A CB  
910  C CG1 . VAL   A 115 ? 0.1777 0.2077 0.2437 -0.0081 -0.0162 0.0013  121 VAL   A CG1 
911  C CG2 . VAL   A 115 ? 0.1902 0.2081 0.2511 -0.0088 -0.0117 -0.0059 121 VAL   A CG2 
912  N N   . GLY   A 116 ? 0.1712 0.1954 0.2478 0.0047  -0.0171 -0.0013 122 GLY   A N   
913  C CA  . GLY   A 116 ? 0.1657 0.1929 0.2467 0.0071  -0.0187 0.0004  122 GLY   A CA  
914  C C   . GLY   A 116 ? 0.1669 0.1917 0.2491 0.0107  -0.0195 -0.0002 122 GLY   A C   
915  O O   . GLY   A 116 ? 0.1751 0.1961 0.2551 0.0117  -0.0193 -0.0012 122 GLY   A O   
916  N N   . ILE   A 117 ? 0.1499 0.1770 0.2357 0.0122  -0.0203 0.0005  123 ILE   A N   
917  C CA  . ILE   A 117 ? 0.1389 0.1648 0.2247 0.0143  -0.0208 -0.0007 123 ILE   A CA  
918  C C   . ILE   A 117 ? 0.1332 0.1616 0.2212 0.0143  -0.0203 -0.0004 123 ILE   A C   
919  O O   . ILE   A 117 ? 0.1331 0.1640 0.2258 0.0141  -0.0201 0.0009  123 ILE   A O   
920  C CB  . ILE   A 117 ? 0.1480 0.1741 0.2367 0.0161  -0.0215 -0.0022 123 ILE   A CB  
921  C CG1 . ILE   A 117 ? 0.1445 0.1728 0.2381 0.0159  -0.0213 -0.0018 123 ILE   A CG1 
922  C CG2 . ILE   A 117 ? 0.1610 0.1852 0.2490 0.0169  -0.0218 -0.0028 123 ILE   A CG2 
923  C CD1 . ILE   A 117 ? 0.1643 0.1928 0.2607 0.0171  -0.0220 -0.0037 123 ILE   A CD1 
924  N N   . VAL   A 118 ? 0.1269 0.1549 0.2122 0.0145  -0.0201 -0.0016 124 VAL   A N   
925  C CA  . VAL   A 118 ? 0.1294 0.1602 0.2174 0.0143  -0.0186 -0.0026 124 VAL   A CA  
926  C C   . VAL   A 118 ? 0.1301 0.1619 0.2252 0.0158  -0.0179 -0.0042 124 VAL   A C   
927  O O   . VAL   A 118 ? 0.1278 0.1583 0.2227 0.0164  -0.0186 -0.0057 124 VAL   A O   
928  C CB  . VAL   A 118 ? 0.1504 0.1814 0.2333 0.0133  -0.0182 -0.0043 124 VAL   A CB  
929  C CG1 . VAL   A 118 ? 0.1594 0.1939 0.2456 0.0128  -0.0156 -0.0069 124 VAL   A CG1 
930  C CG2 . VAL   A 118 ? 0.1528 0.1821 0.2296 0.0116  -0.0190 -0.0020 124 VAL   A CG2 
931  N N   . SER   A 119 ? 0.1372 0.1714 0.2394 0.0163  -0.0167 -0.0035 125 SER   A N   
932  C CA  . SER   A 119 ? 0.1439 0.1779 0.2544 0.0178  -0.0159 -0.0046 125 SER   A CA  
933  C C   . SER   A 119 ? 0.1503 0.1864 0.2681 0.0187  -0.0130 -0.0068 125 SER   A C   
934  O O   . SER   A 119 ? 0.1512 0.1860 0.2750 0.0197  -0.0113 -0.0098 125 SER   A O   
935  C CB  . SER   A 119 ? 0.1679 0.2024 0.2831 0.0178  -0.0177 -0.0002 125 SER   A CB  
936  O OG  . SER   A 119 ? 0.1723 0.2061 0.2967 0.0190  -0.0174 0.0001  125 SER   A OG  
937  N N   . THR   A 120 ? 0.1285 0.1680 0.2469 0.0182  -0.0122 -0.0054 126 THR   A N   
938  C CA  . THR   A 120 ? 0.1395 0.1819 0.2667 0.0193  -0.0089 -0.0078 126 THR   A CA  
939  C C   . THR   A 120 ? 0.1705 0.2164 0.2917 0.0173  -0.0072 -0.0094 126 THR   A C   
940  O O   . THR   A 120 ? 0.1705 0.2157 0.2818 0.0152  -0.0092 -0.0074 126 THR   A O   
941  C CB  . THR   A 120 ? 0.1537 0.1990 0.2933 0.0210  -0.0097 -0.0028 126 THR   A CB  
942  O OG1 . THR   A 120 ? 0.1521 0.2015 0.2889 0.0194  -0.0114 0.0016  126 THR   A OG1 
943  C CG2 . THR   A 120 ? 0.1405 0.1831 0.2849 0.0219  -0.0122 0.0007  126 THR   A CG2 
944  N N   . GLY   A 121 ? 0.1836 0.2333 0.3121 0.0178  -0.0034 -0.0124 127 GLY   A N   
945  C CA  . GLY   A 121 ? 0.1965 0.2504 0.3199 0.0153  -0.0017 -0.0134 127 GLY   A CA  
946  C C   . GLY   A 121 ? 0.2089 0.2671 0.3405 0.0157  0.0037  -0.0189 127 GLY   A C   
947  O O   . GLY   A 121 ? 0.2079 0.2651 0.3506 0.0182  0.0063  -0.0220 127 GLY   A O   
948  N N   . GLY   A 122 ? 0.2148 0.2772 0.3405 0.0126  0.0057  -0.0207 128 GLY   A N   
949  C CA  . GLY   A 122 ? 0.2204 0.2881 0.3524 0.0120  0.0117  -0.0270 128 GLY   A CA  
950  C C   . GLY   A 122 ? 0.2294 0.3041 0.3632 0.0105  0.0129  -0.0249 128 GLY   A C   
951  O O   . GLY   A 122 ? 0.2354 0.3114 0.3720 0.0115  0.0094  -0.0184 128 GLY   A O   
952  N N   . ASN   A 123 ? 0.2231 0.3031 0.3546 0.0072  0.0179  -0.0306 129 ASN   A N   
953  C CA  . ASN   A 123 ? 0.2167 0.3047 0.3506 0.0053  0.0199  -0.0297 129 ASN   A CA  
954  C C   . ASN   A 123 ? 0.1989 0.2867 0.3238 0.0030  0.0147  -0.0220 129 ASN   A C   
955  O O   . ASN   A 123 ? 0.1997 0.2934 0.3322 0.0034  0.0144  -0.0184 129 ASN   A O   
956  C CB  . ASN   A 123 ? 0.2466 0.3401 0.4014 0.0098  0.0233  -0.0303 129 ASN   A CB  
957  C CG  . ASN   A 123 ? 0.3085 0.4024 0.4735 0.0115  0.0300  -0.0393 129 ASN   A CG  
958  O OD1 . ASN   A 123 ? 0.3280 0.4257 0.4877 0.0075  0.0354  -0.0466 129 ASN   A OD1 
959  N ND2 . ASN   A 123 ? 0.3116 0.4014 0.4906 0.0168  0.0299  -0.0389 129 ASN   A ND2 
960  N N   . GLY   A 124 ? 0.1811 0.2627 0.2910 0.0004  0.0107  -0.0197 130 GLY   A N   
961  C CA  . GLY   A 124 ? 0.1853 0.2652 0.2867 -0.0020 0.0064  -0.0134 130 GLY   A CA  
962  C C   . GLY   A 124 ? 0.1803 0.2563 0.2849 0.0008  0.0019  -0.0079 130 GLY   A C   
963  O O   . GLY   A 124 ? 0.1920 0.2671 0.2911 -0.0015 -0.0010 -0.0035 130 GLY   A O   
964  N N   . LEU   A 125 ? 0.1630 0.2362 0.2755 0.0050  0.0014  -0.0084 131 LEU   A N   
965  C CA  . LEU   A 125 ? 0.1744 0.2442 0.2888 0.0069  -0.0029 -0.0034 131 LEU   A CA  
966  C C   . LEU   A 125 ? 0.1707 0.2325 0.2782 0.0079  -0.0048 -0.0045 131 LEU   A C   
967  O O   . LEU   A 125 ? 0.1702 0.2302 0.2760 0.0083  -0.0028 -0.0092 131 LEU   A O   
968  C CB  . LEU   A 125 ? 0.1799 0.2536 0.3105 0.0107  -0.0025 -0.0017 131 LEU   A CB  
969  C CG  . LEU   A 125 ? 0.1999 0.2827 0.3405 0.0103  -0.0018 0.0013  131 LEU   A CG  
970  C CD1 . LEU   A 125 ? 0.2131 0.2994 0.3719 0.0147  -0.0011 0.0029  131 LEU   A CD1 
971  C CD2 . LEU   A 125 ? 0.2000 0.2842 0.3342 0.0069  -0.0061 0.0075  131 LEU   A CD2 
972  N N   . VAL   A 126 ? 0.1451 0.2030 0.2487 0.0078  -0.0085 -0.0006 132 VAL   A N   
973  C CA  . VAL   A 126 ? 0.1524 0.2038 0.2516 0.0090  -0.0104 -0.0013 132 VAL   A CA  
974  C C   . VAL   A 126 ? 0.1383 0.1891 0.2416 0.0100  -0.0130 0.0028  132 VAL   A C   
975  O O   . VAL   A 126 ? 0.1482 0.2016 0.2507 0.0079  -0.0144 0.0063  132 VAL   A O   
976  C CB  . VAL   A 126 ? 0.1724 0.2189 0.2593 0.0067  -0.0118 -0.0013 132 VAL   A CB  
977  C CG1 . VAL   A 126 ? 0.1798 0.2254 0.2617 0.0041  -0.0134 0.0022  132 VAL   A CG1 
978  C CG2 . VAL   A 126 ? 0.1760 0.2172 0.2604 0.0085  -0.0135 -0.0021 132 VAL   A CG2 
979  N N   . GLY   A 127 ? 0.1362 0.1848 0.2443 0.0125  -0.0135 0.0023  133 GLY   A N   
980  C CA  . GLY   A 127 ? 0.1367 0.1853 0.2485 0.0127  -0.0160 0.0062  133 GLY   A CA  
981  C C   . GLY   A 127 ? 0.1488 0.1920 0.2539 0.0126  -0.0174 0.0053  133 GLY   A C   
982  O O   . GLY   A 127 ? 0.1458 0.1857 0.2486 0.0139  -0.0166 0.0018  133 GLY   A O   
983  N N   . PHE   A 128 ? 0.1425 0.1856 0.2445 0.0105  -0.0193 0.0082  134 PHE   A N   
984  C CA  . PHE   A 128 ? 0.1483 0.1871 0.2448 0.0103  -0.0200 0.0070  134 PHE   A CA  
985  C C   . PHE   A 128 ? 0.1503 0.1908 0.2510 0.0097  -0.0214 0.0096  134 PHE   A C   
986  O O   . PHE   A 128 ? 0.1480 0.1928 0.2512 0.0074  -0.0227 0.0136  134 PHE   A O   
987  C CB  . PHE   A 128 ? 0.1551 0.1920 0.2434 0.0075  -0.0201 0.0069  134 PHE   A CB  
988  C CG  . PHE   A 128 ? 0.1580 0.1934 0.2418 0.0070  -0.0192 0.0057  134 PHE   A CG  
989  C CD1 . PHE   A 128 ? 0.1649 0.1961 0.2449 0.0084  -0.0190 0.0034  134 PHE   A CD1 
990  C CD2 . PHE   A 128 ? 0.1598 0.1987 0.2433 0.0046  -0.0190 0.0075  134 PHE   A CD2 
991  C CE1 . PHE   A 128 ? 0.1751 0.2054 0.2506 0.0072  -0.0185 0.0032  134 PHE   A CE1 
992  C CE2 . PHE   A 128 ? 0.1723 0.2101 0.2512 0.0035  -0.0182 0.0066  134 PHE   A CE2 
993  C CZ  . PHE   A 128 ? 0.1713 0.2045 0.2460 0.0047  -0.0179 0.0046  134 PHE   A CZ  
994  N N   . ALA   A 129 ? 0.1381 0.1758 0.2392 0.0111  -0.0214 0.0078  135 ALA   A N   
995  C CA  . ALA   A 129 ? 0.1463 0.1855 0.2501 0.0098  -0.0227 0.0103  135 ALA   A CA  
996  C C   . ALA   A 129 ? 0.1533 0.1924 0.2497 0.0065  -0.0226 0.0098  135 ALA   A C   
997  O O   . ALA   A 129 ? 0.1480 0.1836 0.2402 0.0074  -0.0215 0.0063  135 ALA   A O   
998  C CB  . ALA   A 129 ? 0.1438 0.1804 0.2507 0.0120  -0.0224 0.0081  135 ALA   A CB  
999  N N   . ASP   A 130 ? 0.1558 0.1993 0.2512 0.0024  -0.0236 0.0134  136 ASP   A N   
1000 C CA  . ASP   A 130 ? 0.1648 0.2085 0.2528 -0.0018 -0.0227 0.0118  136 ASP   A CA  
1001 C C   . ASP   A 130 ? 0.1617 0.2047 0.2494 -0.0022 -0.0219 0.0099  136 ASP   A C   
1002 O O   . ASP   A 130 ? 0.1696 0.2142 0.2623 -0.0015 -0.0232 0.0123  136 ASP   A O   
1003 C CB  . ASP   A 130 ? 0.1835 0.2336 0.2703 -0.0074 -0.0243 0.0165  136 ASP   A CB  
1004 C CG  . ASP   A 130 ? 0.2713 0.3227 0.3497 -0.0133 -0.0228 0.0144  136 ASP   A CG  
1005 O OD1 . ASP   A 130 ? 0.2484 0.2950 0.3219 -0.0130 -0.0203 0.0095  136 ASP   A OD1 
1006 O OD2 . ASP   A 130 ? 0.3418 0.3991 0.4187 -0.0187 -0.0241 0.0176  136 ASP   A OD2 
1007 N N   . VAL   A 131 ? 0.1467 0.1873 0.2293 -0.0033 -0.0195 0.0056  137 VAL   A N   
1008 C CA  . VAL   A 131 ? 0.1531 0.1945 0.2359 -0.0043 -0.0182 0.0033  137 VAL   A CA  
1009 C C   . VAL   A 131 ? 0.1644 0.2083 0.2412 -0.0103 -0.0158 0.0010  137 VAL   A C   
1010 O O   . VAL   A 131 ? 0.1693 0.2148 0.2460 -0.0119 -0.0139 -0.0015 137 VAL   A O   
1011 C CB  . VAL   A 131 ? 0.1565 0.1934 0.2416 0.0007  -0.0169 -0.0008 137 VAL   A CB  
1012 C CG1 . VAL   A 131 ? 0.1638 0.1992 0.2538 0.0051  -0.0189 0.0007  137 VAL   A CG1 
1013 C CG2 . VAL   A 131 ? 0.1615 0.1938 0.2438 0.0018  -0.0149 -0.0043 137 VAL   A CG2 
1014 N N   . ARG   A 132 ? 0.1658 0.2105 0.2376 -0.0142 -0.0155 0.0013  138 ARG   A N   
1015 C CA  . ARG   A 132 ? 0.1651 0.2118 0.2303 -0.0207 -0.0125 -0.0021 138 ARG   A CA  
1016 C C   . ARG   A 132 ? 0.1734 0.2279 0.2361 -0.0274 -0.0129 0.0000  138 ARG   A C   
1017 O O   . ARG   A 132 ? 0.1788 0.2352 0.2362 -0.0330 -0.0094 -0.0045 138 ARG   A O   
1018 C CB  . ARG   A 132 ? 0.1682 0.2145 0.2284 -0.0242 -0.0125 -0.0019 138 ARG   A CB  
1019 C CG  . ARG   A 132 ? 0.1639 0.2023 0.2254 -0.0189 -0.0116 -0.0044 138 ARG   A CG  
1020 C CD  . ARG   A 132 ? 0.1856 0.2242 0.2422 -0.0230 -0.0119 -0.0035 138 ARG   A CD  
1021 N NE  . ARG   A 132 ? 0.1994 0.2436 0.2584 -0.0230 -0.0159 0.0031  138 ARG   A NE  
1022 C CZ  . ARG   A 132 ? 0.2314 0.2776 0.2881 -0.0259 -0.0170 0.0052  138 ARG   A CZ  
1023 N NH1 . ARG   A 132 ? 0.2088 0.2517 0.2591 -0.0302 -0.0145 0.0012  138 ARG   A NH1 
1024 N NH2 . ARG   A 132 ? 0.2100 0.2616 0.2714 -0.0248 -0.0203 0.0110  138 ARG   A NH2 
1025 N N   . ASP   A 133 ? 0.1638 0.2227 0.2302 -0.0275 -0.0169 0.0069  139 ASP   A N   
1026 C CA  . ASP   A 133 ? 0.1686 0.2353 0.2329 -0.0344 -0.0180 0.0105  139 ASP   A CA  
1027 C C   . ASP   A 133 ? 0.1753 0.2418 0.2424 -0.0329 -0.0163 0.0081  139 ASP   A C   
1028 O O   . ASP   A 133 ? 0.1909 0.2638 0.2554 -0.0392 -0.0167 0.0105  139 ASP   A O   
1029 C CB  . ASP   A 133 ? 0.1954 0.2669 0.2642 -0.0352 -0.0235 0.0202  139 ASP   A CB  
1030 C CG  . ASP   A 133 ? 0.2625 0.3295 0.3412 -0.0271 -0.0254 0.0225  139 ASP   A CG  
1031 O OD1 . ASP   A 133 ? 0.2748 0.3352 0.3558 -0.0206 -0.0239 0.0183  139 ASP   A OD1 
1032 O OD2 . ASP   A 133 ? 0.2779 0.3477 0.3617 -0.0279 -0.0282 0.0283  139 ASP   A OD2 
1033 N N   . LEU   A 134 ? 0.1691 0.2291 0.2412 -0.0253 -0.0148 0.0041  140 LEU   A N   
1034 C CA  . LEU   A 134 ? 0.1609 0.2211 0.2367 -0.0235 -0.0136 0.0021  140 LEU   A CA  
1035 C C   . LEU   A 134 ? 0.1729 0.2337 0.2457 -0.0258 -0.0082 -0.0057 140 LEU   A C   
1036 O O   . LEU   A 134 ? 0.1674 0.2232 0.2439 -0.0203 -0.0059 -0.0107 140 LEU   A O   
1037 C CB  . LEU   A 134 ? 0.1682 0.2226 0.2511 -0.0152 -0.0150 0.0018  140 LEU   A CB  
1038 C CG  . LEU   A 134 ? 0.1804 0.2338 0.2678 -0.0126 -0.0192 0.0080  140 LEU   A CG  
1039 C CD1 . LEU   A 134 ? 0.1839 0.2321 0.2768 -0.0056 -0.0196 0.0061  140 LEU   A CD1 
1040 C CD2 . LEU   A 134 ? 0.1947 0.2529 0.2844 -0.0166 -0.0218 0.0141  140 LEU   A CD2 
1041 N N   . LEU   A 135 ? 0.1774 0.2444 0.2437 -0.0342 -0.0062 -0.0066 141 LEU   A N   
1042 C CA  . LEU   A 135 ? 0.2025 0.2704 0.2658 -0.0375 0.0000  -0.0152 141 LEU   A CA  
1043 C C   . LEU   A 135 ? 0.2049 0.2730 0.2744 -0.0340 0.0030  -0.0196 141 LEU   A C   
1044 O O   . LEU   A 135 ? 0.2151 0.2809 0.2868 -0.0324 0.0082  -0.0273 141 LEU   A O   
1045 C CB  . LEU   A 135 ? 0.2113 0.2872 0.2652 -0.0489 0.0017  -0.0155 141 LEU   A CB  
1046 C CG  . LEU   A 135 ? 0.2367 0.3147 0.2845 -0.0537 -0.0019 -0.0101 141 LEU   A CG  
1047 C CD1 . LEU   A 135 ? 0.2519 0.3392 0.2897 -0.0661 -0.0002 -0.0106 141 LEU   A CD1 
1048 C CD2 . LEU   A 135 ? 0.2449 0.3150 0.2929 -0.0491 -0.0010 -0.0133 141 LEU   A CD2 
1049 N N   . TRP   A 136 ? 0.1998 0.2706 0.2731 -0.0329 -0.0002 -0.0148 142 TRP   A N   
1050 C CA  . TRP   A 136 ? 0.1951 0.2675 0.2745 -0.0302 0.0021  -0.0182 142 TRP   A CA  
1051 C C   . TRP   A 136 ? 0.1982 0.2641 0.2856 -0.0209 0.0027  -0.0216 142 TRP   A C   
1052 O O   . TRP   A 136 ? 0.1896 0.2573 0.2830 -0.0186 0.0055  -0.0258 142 TRP   A O   
1053 C CB  . TRP   A 136 ? 0.1903 0.2666 0.2717 -0.0318 -0.0018 -0.0117 142 TRP   A CB  
1054 C CG  . TRP   A 136 ? 0.1886 0.2601 0.2729 -0.0274 -0.0075 -0.0048 142 TRP   A CG  
1055 C CD1 . TRP   A 136 ? 0.1977 0.2701 0.2794 -0.0305 -0.0116 0.0023  142 TRP   A CD1 
1056 C CD2 . TRP   A 136 ? 0.1885 0.2545 0.2796 -0.0195 -0.0096 -0.0046 142 TRP   A CD2 
1057 N NE1 . TRP   A 136 ? 0.2019 0.2691 0.2893 -0.0245 -0.0154 0.0063  142 TRP   A NE1 
1058 C CE2 . TRP   A 136 ? 0.1999 0.2631 0.2922 -0.0182 -0.0141 0.0018  142 TRP   A CE2 
1059 C CE3 . TRP   A 136 ? 0.1986 0.2625 0.2954 -0.0139 -0.0081 -0.0090 142 TRP   A CE3 
1060 C CZ2 . TRP   A 136 ? 0.2020 0.2600 0.2999 -0.0119 -0.0163 0.0026  142 TRP   A CZ2 
1061 C CZ3 . TRP   A 136 ? 0.2034 0.2630 0.3050 -0.0082 -0.0112 -0.0072 142 TRP   A CZ3 
1062 C CH2 . TRP   A 136 ? 0.2001 0.2565 0.3016 -0.0075 -0.0149 -0.0020 142 TRP   A CH2 
1063 N N   . LEU   A 137 ? 0.1887 0.2478 0.2764 -0.0159 0.0001  -0.0197 143 LEU   A N   
1064 C CA  . LEU   A 137 ? 0.2079 0.2615 0.3024 -0.0081 0.0001  -0.0220 143 LEU   A CA  
1065 C C   . LEU   A 137 ? 0.2357 0.2881 0.3332 -0.0073 0.0058  -0.0294 143 LEU   A C   
1066 O O   . LEU   A 137 ? 0.2260 0.2760 0.3314 -0.0013 0.0062  -0.0311 143 LEU   A O   
1067 C CB  . LEU   A 137 ? 0.1977 0.2450 0.2906 -0.0044 -0.0032 -0.0188 143 LEU   A CB  
1068 C CG  . LEU   A 137 ? 0.2033 0.2503 0.2964 -0.0029 -0.0082 -0.0127 143 LEU   A CG  
1069 C CD1 . LEU   A 137 ? 0.2106 0.2526 0.3016 -0.0004 -0.0104 -0.0105 143 LEU   A CD1 
1070 C CD2 . LEU   A 137 ? 0.1963 0.2435 0.2959 0.0015  -0.0099 -0.0124 143 LEU   A CD2 
1071 N N   . ASP   A 138 ? 0.2726 0.3267 0.3645 -0.0136 0.0100  -0.0335 144 ASP   A N   
1072 C CA  . ASP   A 138 ? 0.3230 0.3750 0.4183 -0.0134 0.0164  -0.0415 144 ASP   A CA  
1073 C C   . ASP   A 138 ? 0.3738 0.4324 0.4744 -0.0151 0.0215  -0.0470 144 ASP   A C   
1074 O O   . ASP   A 138 ? 0.3741 0.4315 0.4791 -0.0150 0.0277  -0.0546 144 ASP   A O   
1075 C CB  . ASP   A 138 ? 0.3506 0.4019 0.4368 -0.0206 0.0196  -0.0448 144 ASP   A CB  
1076 C CG  . ASP   A 138 ? 0.4399 0.4850 0.5212 -0.0196 0.0159  -0.0408 144 ASP   A CG  
1077 O OD1 . ASP   A 138 ? 0.4490 0.4889 0.5349 -0.0125 0.0120  -0.0369 144 ASP   A OD1 
1078 O OD2 . ASP   A 138 ? 0.4987 0.5449 0.5714 -0.0266 0.0171  -0.0417 144 ASP   A OD2 
1079 N N   . GLU   A 139 ? 0.4080 0.4734 0.5087 -0.0170 0.0193  -0.0437 145 GLU   A N   
1080 C CA  . GLU   A 139 ? 0.4464 0.5194 0.5517 -0.0196 0.0244  -0.0489 145 GLU   A CA  
1081 C C   . GLU   A 139 ? 0.4790 0.5564 0.5904 -0.0166 0.0208  -0.0447 145 GLU   A C   
1082 O O   . GLU   A 139 ? 0.4797 0.5539 0.5908 -0.0131 0.0145  -0.0380 145 GLU   A O   
1083 C CB  . GLU   A 139 ? 0.4845 0.5647 0.5792 -0.0308 0.0275  -0.0508 145 GLU   A CB  
1084 C CG  . GLU   A 139 ? 0.5606 0.6444 0.6480 -0.0352 0.0212  -0.0417 145 GLU   A CG  
1085 C CD  . GLU   A 139 ? 0.6654 0.7542 0.7407 -0.0459 0.0214  -0.0399 145 GLU   A CD  
1086 O OE1 . GLU   A 139 ? 0.6672 0.7603 0.7383 -0.0502 0.0165  -0.0322 145 GLU   A OE1 
1087 O OE2 . GLU   A 139 ? 0.7080 0.7965 0.7782 -0.0503 0.0261  -0.0459 145 GLU   A OE2 
1088 N N   . GLU   A 140 ? 0.5044 0.5896 0.6209 -0.0189 0.0251  -0.0490 146 GLU   A N   
1089 C CA  . GLU   A 140 ? 0.5324 0.6234 0.6539 -0.0181 0.0226  -0.0459 146 GLU   A CA  
1090 C C   . GLU   A 140 ? 0.5547 0.6409 0.6820 -0.0102 0.0163  -0.0404 146 GLU   A C   
1091 O O   . GLU   A 140 ? 0.5646 0.6549 0.6992 -0.0079 0.0150  -0.0396 146 GLU   A O   
1092 C CB  . GLU   A 140 ? 0.5783 0.6753 0.6902 -0.0272 0.0209  -0.0416 146 GLU   A CB  
1093 C CG  . GLU   A 140 ? 0.6673 0.7650 0.7800 -0.0267 0.0148  -0.0341 146 GLU   A CG  
1094 C CD  . GLU   A 140 ? 0.7679 0.8732 0.8876 -0.0273 0.0163  -0.0355 146 GLU   A CD  
1095 O OE1 . GLU   A 140 ? 0.7970 0.9044 0.9145 -0.0308 0.0126  -0.0300 146 GLU   A OE1 
1096 O OE2 . GLU   A 140 ? 0.7879 0.8969 0.9162 -0.0244 0.0211  -0.0419 146 GLU   A OE2 
1097 N N   . SER   B 1   ? 0.2592 0.2882 0.3369 -0.0034 -0.0376 0.0354  7   SER   C N   
1098 C CA  . SER   B 1   ? 0.2622 0.2915 0.3495 -0.0045 -0.0384 0.0361  7   SER   C CA  
1099 C C   . SER   B 1   ? 0.2527 0.2803 0.3392 -0.0042 -0.0376 0.0326  7   SER   C C   
1100 O O   . SER   B 1   ? 0.2539 0.2792 0.3319 -0.0032 -0.0381 0.0298  7   SER   C O   
1101 C CB  . SER   B 1   ? 0.2980 0.3263 0.3873 -0.0060 -0.0435 0.0392  7   SER   C CB  
1102 O OG  . SER   B 1   ? 0.3467 0.3716 0.4278 -0.0062 -0.0474 0.0373  7   SER   C OG  
1103 N N   . GLY   B 2   ? 0.2400 0.2687 0.3352 -0.0047 -0.0363 0.0328  8   GLY   C N   
1104 C CA  . GLY   B 2   ? 0.2351 0.2623 0.3301 -0.0044 -0.0352 0.0305  8   GLY   C CA  
1105 C C   . GLY   B 2   ? 0.2189 0.2483 0.3218 -0.0041 -0.0313 0.0304  8   GLY   C C   
1106 O O   . GLY   B 2   ? 0.2196 0.2513 0.3263 -0.0035 -0.0288 0.0305  8   GLY   C O   
1107 N N   . ALA   B 3   ? 0.1990 0.2275 0.3042 -0.0044 -0.0306 0.0301  9   ALA   C N   
1108 C CA  . ALA   B 3   ? 0.1935 0.2237 0.3045 -0.0037 -0.0265 0.0297  9   ALA   C CA  
1109 C C   . ALA   B 3   ? 0.1847 0.2129 0.2918 -0.0031 -0.0249 0.0283  9   ALA   C C   
1110 O O   . ALA   B 3   ? 0.1999 0.2252 0.3022 -0.0036 -0.0274 0.0282  9   ALA   C O   
1111 C CB  . ALA   B 3   ? 0.1899 0.2222 0.3118 -0.0050 -0.0266 0.0329  9   ALA   C CB  
1112 N N   . ILE   B 4   ? 0.1729 0.2023 0.2815 -0.0019 -0.0207 0.0271  10  ILE   C N   
1113 C CA  . ILE   B 4   ? 0.1749 0.2026 0.2800 -0.0012 -0.0188 0.0267  10  ILE   C CA  
1114 C C   . ILE   B 4   ? 0.1822 0.2115 0.2959 -0.0021 -0.0163 0.0294  10  ILE   C C   
1115 O O   . ILE   B 4   ? 0.1903 0.2225 0.3107 -0.0017 -0.0140 0.0295  10  ILE   C O   
1116 C CB  . ILE   B 4   ? 0.1796 0.2076 0.2792 0.0011  -0.0159 0.0235  10  ILE   C CB  
1117 C CG1 . ILE   B 4   ? 0.1850 0.2125 0.2783 0.0020  -0.0180 0.0209  10  ILE   C CG1 
1118 C CG2 . ILE   B 4   ? 0.1893 0.2153 0.2845 0.0019  -0.0140 0.0238  10  ILE   C CG2 
1119 C CD1 . ILE   B 4   ? 0.1932 0.2220 0.2837 0.0041  -0.0158 0.0175  10  ILE   C CD1 
1120 N N   . TYR   B 5   ? 0.1811 0.2087 0.2957 -0.0032 -0.0164 0.0315  11  TYR   C N   
1121 C CA  . TYR   B 5   ? 0.1901 0.2199 0.3138 -0.0040 -0.0133 0.0344  11  TYR   C CA  
1122 C C   . TYR   B 5   ? 0.2039 0.2324 0.3230 -0.0028 -0.0090 0.0346  11  TYR   C C   
1123 O O   . TYR   B 5   ? 0.2124 0.2377 0.3277 -0.0036 -0.0103 0.0359  11  TYR   C O   
1124 C CB  . TYR   B 5   ? 0.1801 0.2097 0.3114 -0.0068 -0.0172 0.0377  11  TYR   C CB  
1125 C CG  . TYR   B 5   ? 0.1788 0.2098 0.3143 -0.0078 -0.0214 0.0380  11  TYR   C CG  
1126 C CD1 . TYR   B 5   ? 0.1822 0.2172 0.3283 -0.0079 -0.0201 0.0397  11  TYR   C CD1 
1127 C CD2 . TYR   B 5   ? 0.1844 0.2127 0.3132 -0.0083 -0.0265 0.0368  11  TYR   C CD2 
1128 C CE1 . TYR   B 5   ? 0.1890 0.2251 0.3386 -0.0086 -0.0242 0.0406  11  TYR   C CE1 
1129 C CE2 . TYR   B 5   ? 0.2024 0.2320 0.3337 -0.0090 -0.0303 0.0375  11  TYR   C CE2 
1130 C CZ  . TYR   B 5   ? 0.2125 0.2459 0.3542 -0.0092 -0.0293 0.0397  11  TYR   C CZ  
1131 O OH  . TYR   B 5   ? 0.2434 0.2777 0.3869 -0.0097 -0.0332 0.0409  11  TYR   C OH  
1132 N N   . VAL   B 6   ? 0.1867 0.2173 0.3053 -0.0008 -0.0039 0.0333  12  VAL   C N   
1133 C CA  . VAL   B 6   ? 0.1860 0.2154 0.2986 0.0007  0.0004  0.0337  12  VAL   C CA  
1134 C C   . VAL   B 6   ? 0.1865 0.2192 0.3064 0.0013  0.0063  0.0352  12  VAL   C C   
1135 O O   . VAL   B 6   ? 0.1806 0.2160 0.3055 0.0022  0.0077  0.0334  12  VAL   C O   
1136 C CB  . VAL   B 6   ? 0.2077 0.2355 0.3087 0.0033  0.0004  0.0296  12  VAL   C CB  
1137 C CG1 . VAL   B 6   ? 0.2045 0.2346 0.3072 0.0046  0.0008  0.0259  12  VAL   C CG1 
1138 C CG2 . VAL   B 6   ? 0.2208 0.2473 0.3144 0.0052  0.0047  0.0302  12  VAL   C CG2 
1139 N N   . GLY   B 7   ? 0.1920 0.2248 0.3142 0.0007  0.0099  0.0390  13  GLY   C N   
1140 C CA  . GLY   B 7   ? 0.1922 0.2288 0.3224 0.0014  0.0163  0.0408  13  GLY   C CA  
1141 C C   . GLY   B 7   ? 0.1936 0.2340 0.3380 0.0001  0.0151  0.0417  13  GLY   C C   
1142 O O   . GLY   B 7   ? 0.1994 0.2395 0.3496 -0.0026 0.0095  0.0435  13  GLY   C O   
1143 N N   . ASN   B 8   ? 0.1853 0.2290 0.3349 0.0020  0.0195  0.0402  14  ASN   C N   
1144 C CA  . ASN   B 8   ? 0.1846 0.2317 0.3479 0.0012  0.0179  0.0410  14  ASN   C CA  
1145 C C   . ASN   B 8   ? 0.1694 0.2155 0.3294 0.0023  0.0145  0.0368  14  ASN   C C   
1146 O O   . ASN   B 8   ? 0.1681 0.2166 0.3367 0.0033  0.0157  0.0360  14  ASN   C O   
1147 C CB  . ASN   B 8   ? 0.2180 0.2696 0.3927 0.0025  0.0247  0.0427  14  ASN   C CB  
1148 C CG  . ASN   B 8   ? 0.2846 0.3383 0.4673 0.0004  0.0269  0.0481  14  ASN   C CG  
1149 O OD1 . ASN   B 8   ? 0.3106 0.3671 0.5068 -0.0021 0.0239  0.0516  14  ASN   C OD1 
1150 N ND2 . ASN   B 8   ? 0.2991 0.3514 0.4736 0.0012  0.0318  0.0491  14  ASN   C ND2 
1151 N N   . TYR   B 9   ? 0.1581 0.2007 0.3070 0.0021  0.0103  0.0346  15  TYR   C N   
1152 C CA  . TYR   B 9   ? 0.1669 0.2086 0.3132 0.0028  0.0072  0.0311  15  TYR   C CA  
1153 C C   . TYR   B 9   ? 0.1713 0.2114 0.3159 0.0006  0.0003  0.0322  15  TYR   C C   
1154 O O   . TYR   B 9   ? 0.1778 0.2157 0.3171 -0.0007 -0.0020 0.0335  15  TYR   C O   
1155 C CB  . TYR   B 9   ? 0.1785 0.2179 0.3123 0.0051  0.0087  0.0265  15  TYR   C CB  
1156 C CG  . TYR   B 9   ? 0.1948 0.2350 0.3272 0.0078  0.0150  0.0243  15  TYR   C CG  
1157 C CD1 . TYR   B 9   ? 0.2138 0.2560 0.3547 0.0091  0.0179  0.0228  15  TYR   C CD1 
1158 C CD2 . TYR   B 9   ? 0.2131 0.2516 0.3348 0.0093  0.0180  0.0234  15  TYR   C CD2 
1159 C CE1 . TYR   B 9   ? 0.2332 0.2758 0.3721 0.0120  0.0240  0.0201  15  TYR   C CE1 
1160 C CE2 . TYR   B 9   ? 0.2347 0.2737 0.3533 0.0121  0.0239  0.0210  15  TYR   C CE2 
1161 C CZ  . TYR   B 9   ? 0.2648 0.3058 0.3917 0.0135  0.0270  0.0190  15  TYR   C CZ  
1162 O OH  . TYR   B 9   ? 0.3093 0.3504 0.4323 0.0166  0.0330  0.0160  15  TYR   C OH  
1163 N N   . ARG   B 10  ? 0.1520 0.1928 0.3002 0.0004  -0.0025 0.0316  16  ARG   C N   
1164 C CA  . ARG   B 10  ? 0.1478 0.1871 0.2928 -0.0012 -0.0083 0.0322  16  ARG   C CA  
1165 C C   . ARG   B 10  ? 0.1484 0.1869 0.2881 0.0001  -0.0085 0.0287  16  ARG   C C   
1166 O O   . ARG   B 10  ? 0.1368 0.1766 0.2822 0.0012  -0.0065 0.0276  16  ARG   C O   
1167 C CB  . ARG   B 10  ? 0.1671 0.2083 0.3225 -0.0029 -0.0118 0.0358  16  ARG   C CB  
1168 C CG  . ARG   B 10  ? 0.1750 0.2151 0.3270 -0.0039 -0.0171 0.0363  16  ARG   C CG  
1169 C CD  . ARG   B 10  ? 0.1825 0.2242 0.3437 -0.0055 -0.0213 0.0403  16  ARG   C CD  
1170 N NE  . ARG   B 10  ? 0.2149 0.2567 0.3765 -0.0054 -0.0240 0.0412  16  ARG   C NE  
1171 C CZ  . ARG   B 10  ? 0.2426 0.2827 0.3976 -0.0065 -0.0288 0.0421  16  ARG   C CZ  
1172 N NH1 . ARG   B 10  ? 0.2196 0.2575 0.3665 -0.0074 -0.0315 0.0414  16  ARG   C NH1 
1173 N NH2 . ARG   B 10  ? 0.2395 0.2798 0.3949 -0.0063 -0.0305 0.0436  16  ARG   C NH2 
1174 N N   . VAL   B 11  ? 0.1506 0.1870 0.2802 0.0002  -0.0105 0.0268  17  VAL   C N   
1175 C CA  . VAL   B 11  ? 0.1538 0.1899 0.2791 0.0013  -0.0108 0.0237  17  VAL   C CA  
1176 C C   . VAL   B 11  ? 0.1674 0.2033 0.2918 0.0000  -0.0148 0.0252  17  VAL   C C   
1177 O O   . VAL   B 11  ? 0.1676 0.2019 0.2865 -0.0009 -0.0176 0.0262  17  VAL   C O   
1178 C CB  . VAL   B 11  ? 0.1665 0.2010 0.2817 0.0027  -0.0100 0.0204  17  VAL   C CB  
1179 C CG1 . VAL   B 11  ? 0.1780 0.2129 0.2912 0.0036  -0.0101 0.0170  17  VAL   C CG1 
1180 C CG2 . VAL   B 11  ? 0.1668 0.2010 0.2804 0.0039  -0.0062 0.0198  17  VAL   C CG2 
1181 N N   . VAL   B 12  ? 0.1582 0.1951 0.2874 -0.0001 -0.0150 0.0255  18  VAL   C N   
1182 C CA  A VAL   B 12  ? 0.1467 0.1836 0.2747 -0.0012 -0.0182 0.0276  18  VAL   C CA  
1183 C CA  B VAL   B 12  ? 0.1571 0.1941 0.2853 -0.0012 -0.0182 0.0276  18  VAL   C CA  
1184 C C   . VAL   B 12  ? 0.1543 0.1918 0.2826 -0.0007 -0.0172 0.0259  18  VAL   C C   
1185 O O   . VAL   B 12  ? 0.1550 0.1929 0.2869 0.0003  -0.0146 0.0232  18  VAL   C O   
1186 C CB  A VAL   B 12  ? 0.1420 0.1798 0.2780 -0.0024 -0.0203 0.0318  18  VAL   C CB  
1187 C CB  B VAL   B 12  ? 0.1733 0.2113 0.3102 -0.0024 -0.0200 0.0318  18  VAL   C CB  
1188 C CG1 A VAL   B 12  ? 0.1501 0.1874 0.2858 -0.0035 -0.0229 0.0340  18  VAL   C CG1 
1189 C CG1 B VAL   B 12  ? 0.1726 0.2104 0.3075 -0.0034 -0.0235 0.0346  18  VAL   C CG1 
1190 C CG2 A VAL   B 12  ? 0.1203 0.1595 0.2669 -0.0017 -0.0176 0.0320  18  VAL   C CG2 
1191 C CG2 B VAL   B 12  ? 0.1886 0.2265 0.3276 -0.0031 -0.0210 0.0335  18  VAL   C CG2 
1192 N N   . ASN   B 13  ? 0.1473 0.1849 0.2722 -0.0014 -0.0192 0.0274  19  ASN   C N   
1193 C CA  . ASN   B 13  ? 0.1447 0.1833 0.2719 -0.0014 -0.0181 0.0269  19  ASN   C CA  
1194 C C   . ASN   B 13  ? 0.1482 0.1871 0.2861 -0.0018 -0.0174 0.0291  19  ASN   C C   
1195 O O   . ASN   B 13  ? 0.1533 0.1922 0.2945 -0.0025 -0.0193 0.0329  19  ASN   C O   
1196 C CB  . ASN   B 13  ? 0.1587 0.1975 0.2809 -0.0021 -0.0198 0.0294  19  ASN   C CB  
1197 C CG  . ASN   B 13  ? 0.1871 0.2255 0.2996 -0.0013 -0.0203 0.0271  19  ASN   C CG  
1198 O OD1 . ASN   B 13  ? 0.1966 0.2334 0.3033 -0.0014 -0.0224 0.0277  19  ASN   C OD1 
1199 N ND2 . ASN   B 13  ? 0.1726 0.2122 0.2838 -0.0006 -0.0186 0.0242  19  ASN   C ND2 
1200 N N   . ARG   B 14  ? 0.1541 0.1931 0.2979 -0.0013 -0.0153 0.0267  20  ARG   C N   
1201 C CA  . ARG   B 14  ? 0.1411 0.1797 0.2956 -0.0013 -0.0145 0.0284  20  ARG   C CA  
1202 C C   . ARG   B 14  ? 0.1448 0.1836 0.3023 -0.0026 -0.0166 0.0340  20  ARG   C C   
1203 O O   . ARG   B 14  ? 0.1467 0.1852 0.3113 -0.0027 -0.0175 0.0373  20  ARG   C O   
1204 C CB  . ARG   B 14  ? 0.1519 0.1899 0.3113 -0.0007 -0.0124 0.0243  20  ARG   C CB  
1205 C CG  . ARG   B 14  ? 0.1669 0.2038 0.3379 -0.0002 -0.0112 0.0248  20  ARG   C CG  
1206 C CD  . ARG   B 14  ? 0.1787 0.2143 0.3540 0.0001  -0.0098 0.0204  20  ARG   C CD  
1207 N NE  . ARG   B 14  ? 0.1792 0.2128 0.3652 0.0010  -0.0084 0.0192  20  ARG   C NE  
1208 C CZ  . ARG   B 14  ? 0.1876 0.2199 0.3831 0.0002  -0.0090 0.0228  20  ARG   C CZ  
1209 N NH1 . ARG   B 14  ? 0.1703 0.2035 0.3653 -0.0016 -0.0108 0.0283  20  ARG   C NH1 
1210 N NH2 . ARG   B 14  ? 0.1748 0.2048 0.3803 0.0013  -0.0076 0.0208  20  ARG   C NH2 
1211 N N   . HIS   B 15  ? 0.1482 0.1875 0.2997 -0.0034 -0.0173 0.0353  21  HIS   C N   
1212 C CA  . HIS   B 15  ? 0.1494 0.1887 0.3021 -0.0044 -0.0189 0.0410  21  HIS   C CA  
1213 C C   . HIS   B 15  ? 0.1637 0.2028 0.3121 -0.0047 -0.0223 0.0448  21  HIS   C C   
1214 O O   . HIS   B 15  ? 0.1807 0.2196 0.3302 -0.0053 -0.0243 0.0498  21  HIS   C O   
1215 C CB  . HIS   B 15  ? 0.1563 0.1965 0.3045 -0.0051 -0.0179 0.0418  21  HIS   C CB  
1216 C CG  . HIS   B 15  ? 0.1760 0.2169 0.3123 -0.0047 -0.0186 0.0408  21  HIS   C CG  
1217 N ND1 . HIS   B 15  ? 0.1980 0.2396 0.3299 -0.0039 -0.0174 0.0357  21  HIS   C ND1 
1218 C CD2 . HIS   B 15  ? 0.1992 0.2400 0.3273 -0.0050 -0.0204 0.0440  21  HIS   C CD2 
1219 C CE1 . HIS   B 15  ? 0.2151 0.2568 0.3372 -0.0036 -0.0183 0.0360  21  HIS   C CE1 
1220 N NE2 . HIS   B 15  ? 0.2201 0.2613 0.3392 -0.0042 -0.0200 0.0406  21  HIS   C NE2 
1221 N N   . LEU   B 16  ? 0.1560 0.1950 0.2996 -0.0043 -0.0233 0.0424  22  LEU   C N   
1222 C CA  . LEU   B 16  ? 0.1676 0.2062 0.3084 -0.0049 -0.0271 0.0453  22  LEU   C CA  
1223 C C   . LEU   B 16  ? 0.1735 0.2127 0.3232 -0.0047 -0.0275 0.0456  22  LEU   C C   
1224 O O   . LEU   B 16  ? 0.1819 0.2211 0.3308 -0.0053 -0.0308 0.0474  22  LEU   C O   
1225 C CB  . LEU   B 16  ? 0.1830 0.2209 0.3121 -0.0049 -0.0284 0.0431  22  LEU   C CB  
1226 C CG  . LEU   B 16  ? 0.2052 0.2430 0.3254 -0.0047 -0.0278 0.0432  22  LEU   C CG  
1227 C CD1 . LEU   B 16  ? 0.2203 0.2569 0.3298 -0.0043 -0.0288 0.0402  22  LEU   C CD1 
1228 C CD2 . LEU   B 16  ? 0.2145 0.2522 0.3333 -0.0054 -0.0300 0.0485  22  LEU   C CD2 
1229 N N   . ALA   B 17  ? 0.1704 0.2100 0.3285 -0.0038 -0.0242 0.0434  23  ALA   C N   
1230 C CA  . ALA   B 17  ? 0.1784 0.2189 0.3452 -0.0032 -0.0234 0.0434  23  ALA   C CA  
1231 C C   . ALA   B 17  ? 0.1873 0.2286 0.3626 -0.0037 -0.0267 0.0487  23  ALA   C C   
1232 O O   . ALA   B 17  ? 0.1899 0.2307 0.3676 -0.0039 -0.0281 0.0519  23  ALA   C O   
1233 C CB  . ALA   B 17  ? 0.1832 0.2236 0.3563 -0.0018 -0.0190 0.0397  23  ALA   C CB  
1234 N N   . THR   B 18  ? 0.1813 0.2240 0.3612 -0.0039 -0.0283 0.0499  24  THR   C N   
1235 C CA  . THR   B 18  ? 0.1856 0.2297 0.3748 -0.0043 -0.0321 0.0549  24  THR   C CA  
1236 C C   . THR   B 18  ? 0.2017 0.2472 0.4057 -0.0027 -0.0290 0.0552  24  THR   C C   
1237 O O   . THR   B 18  ? 0.2082 0.2535 0.4140 -0.0014 -0.0239 0.0510  24  THR   C O   
1238 C CB  . THR   B 18  ? 0.1967 0.2419 0.3852 -0.0056 -0.0358 0.0561  24  THR   C CB  
1239 O OG1 . THR   B 18  ? 0.2071 0.2538 0.4006 -0.0050 -0.0318 0.0534  24  THR   C OG1 
1240 C CG2 . THR   B 18  ? 0.2067 0.2499 0.3807 -0.0068 -0.0390 0.0551  24  THR   C CG2 
1241 N N   . HIS   B 19  ? 0.2049 0.2519 0.4198 -0.0026 -0.0322 0.0599  25  HIS   C N   
1242 C CA  . HIS   B 19  ? 0.2156 0.2642 0.4457 -0.0007 -0.0292 0.0601  25  HIS   C CA  
1243 C C   . HIS   B 19  ? 0.1996 0.2505 0.4335 -0.0001 -0.0254 0.0570  25  HIS   C C   
1244 O O   . HIS   B 19  ? 0.2125 0.2636 0.4521 0.0018  -0.0199 0.0538  25  HIS   C O   
1245 C CB  . HIS   B 19  ? 0.2479 0.2980 0.4893 -0.0006 -0.0342 0.0662  25  HIS   C CB  
1246 C CG  . HIS   B 19  ? 0.3084 0.3611 0.5669 0.0014  -0.0315 0.0666  25  HIS   C CG  
1247 N ND1 . HIS   B 19  ? 0.3435 0.3947 0.6103 0.0036  -0.0274 0.0652  25  HIS   C ND1 
1248 C CD2 . HIS   B 19  ? 0.3330 0.3896 0.6019 0.0016  -0.0320 0.0680  25  HIS   C CD2 
1249 C CE1 . HIS   B 19  ? 0.3526 0.4068 0.6340 0.0053  -0.0255 0.0658  25  HIS   C CE1 
1250 N NE2 . HIS   B 19  ? 0.3463 0.4043 0.6301 0.0042  -0.0280 0.0676  25  HIS   C NE2 
1251 N N   . ASN   B 20  ? 0.1876 0.2399 0.4177 -0.0018 -0.0279 0.0578  26  ASN   C N   
1252 C CA  . ASN   B 20  ? 0.1945 0.2491 0.4283 -0.0015 -0.0239 0.0557  26  ASN   C CA  
1253 C C   . ASN   B 20  ? 0.1864 0.2391 0.4110 -0.0003 -0.0178 0.0501  26  ASN   C C   
1254 O O   . ASN   B 20  ? 0.1868 0.2410 0.4165 0.0013  -0.0122 0.0479  26  ASN   C O   
1255 C CB  . ASN   B 20  ? 0.2308 0.2867 0.4624 -0.0038 -0.0281 0.0577  26  ASN   C CB  
1256 C CG  . ASN   B 20  ? 0.3104 0.3692 0.5491 -0.0036 -0.0236 0.0568  26  ASN   C CG  
1257 O OD1 . ASN   B 20  ? 0.3282 0.3906 0.5817 -0.0027 -0.0219 0.0589  26  ASN   C OD1 
1258 N ND2 . ASN   B 20  ? 0.3325 0.3897 0.5610 -0.0042 -0.0212 0.0540  26  ASN   C ND2 
1259 N N   . ASP   B 21  ? 0.1781 0.2276 0.3892 -0.0010 -0.0188 0.0479  27  ASP   C N   
1260 C CA  . ASP   B 21  ? 0.1748 0.2226 0.3775 0.0002  -0.0140 0.0427  27  ASP   C CA  
1261 C C   . ASP   B 21  ? 0.1777 0.2251 0.3875 0.0025  -0.0096 0.0401  27  ASP   C C   
1262 O O   . ASP   B 21  ? 0.1804 0.2279 0.3895 0.0042  -0.0046 0.0363  27  ASP   C O   
1263 C CB  . ASP   B 21  ? 0.1784 0.2235 0.3679 -0.0008 -0.0163 0.0412  27  ASP   C CB  
1264 C CG  . ASP   B 21  ? 0.1820 0.2265 0.3621 -0.0025 -0.0195 0.0420  27  ASP   C CG  
1265 O OD1 . ASP   B 21  ? 0.1757 0.2209 0.3558 -0.0027 -0.0182 0.0415  27  ASP   C OD1 
1266 O OD2 . ASP   B 21  ? 0.1941 0.2372 0.3670 -0.0035 -0.0232 0.0430  27  ASP   C OD2 
1267 N N   . TRP   B 22  ? 0.1752 0.2218 0.3912 0.0027  -0.0115 0.0420  28  TRP   C N   
1268 C CA  . TRP   B 22  ? 0.1754 0.2208 0.3992 0.0049  -0.0078 0.0393  28  TRP   C CA  
1269 C C   . TRP   B 22  ? 0.1660 0.2138 0.4023 0.0070  -0.0041 0.0393  28  TRP   C C   
1270 O O   . TRP   B 22  ? 0.1600 0.2069 0.3991 0.0093  0.0008  0.0350  28  TRP   C O   
1271 C CB  . TRP   B 22  ? 0.1754 0.2189 0.4040 0.0045  -0.0109 0.0424  28  TRP   C CB  
1272 C CG  . TRP   B 22  ? 0.1830 0.2240 0.4013 0.0032  -0.0120 0.0407  28  TRP   C CG  
1273 C CD1 . TRP   B 22  ? 0.1976 0.2384 0.4074 0.0012  -0.0159 0.0438  28  TRP   C CD1 
1274 C CD2 . TRP   B 22  ? 0.1803 0.2189 0.3956 0.0040  -0.0090 0.0354  28  TRP   C CD2 
1275 N NE1 . TRP   B 22  ? 0.2045 0.2434 0.4076 0.0008  -0.0151 0.0411  28  TRP   C NE1 
1276 C CE2 . TRP   B 22  ? 0.2008 0.2384 0.4074 0.0023  -0.0112 0.0360  28  TRP   C CE2 
1277 C CE3 . TRP   B 22  ? 0.1877 0.2249 0.4070 0.0061  -0.0048 0.0300  28  TRP   C CE3 
1278 C CZ2 . TRP   B 22  ? 0.2099 0.2456 0.4135 0.0023  -0.0097 0.0317  28  TRP   C CZ2 
1279 C CZ3 . TRP   B 22  ? 0.2112 0.2458 0.4261 0.0062  -0.0038 0.0253  28  TRP   C CZ3 
1280 C CH2 . TRP   B 22  ? 0.2126 0.2468 0.4206 0.0041  -0.0064 0.0264  28  TRP   C CH2 
1281 N N   . ALA   B 23  ? 0.1604 0.2116 0.4046 0.0062  -0.0065 0.0441  29  ALA   C N   
1282 C CA  . ALA   B 23  ? 0.1684 0.2229 0.4262 0.0081  -0.0028 0.0447  29  ALA   C CA  
1283 C C   . ALA   B 23  ? 0.1834 0.2395 0.4365 0.0089  0.0029  0.0414  29  ALA   C C   
1284 O O   . ALA   B 23  ? 0.1853 0.2441 0.4482 0.0110  0.0078  0.0409  29  ALA   C O   
1285 C CB  . ALA   B 23  ? 0.1672 0.2252 0.4357 0.0068  -0.0078 0.0510  29  ALA   C CB  
1286 N N   . ASN   B 24  ? 0.1840 0.2385 0.4226 0.0073  0.0023  0.0396  30  ASN   C N   
1287 C CA  . ASN   B 24  ? 0.1857 0.2409 0.4180 0.0080  0.0074  0.0371  30  ASN   C CA  
1288 C C   . ASN   B 24  ? 0.1868 0.2383 0.4040 0.0086  0.0089  0.0318  30  ASN   C C   
1289 O O   . ASN   B 24  ? 0.1871 0.2379 0.3936 0.0078  0.0095  0.0308  30  ASN   C O   
1290 C CB  . ASN   B 24  ? 0.1987 0.2560 0.4297 0.0053  0.0043  0.0410  30  ASN   C CB  
1291 C CG  . ASN   B 24  ? 0.2252 0.2868 0.4721 0.0047  0.0028  0.0459  30  ASN   C CG  
1292 O OD1 . ASN   B 24  ? 0.2297 0.2948 0.4860 0.0060  0.0080  0.0464  30  ASN   C OD1 
1293 N ND2 . ASN   B 24  ? 0.2305 0.2922 0.4811 0.0028  -0.0043 0.0497  30  ASN   C ND2 
1294 N N   . LEU   B 25  ? 0.1901 0.2388 0.4070 0.0099  0.0091  0.0285  31  LEU   C N   
1295 C CA  . LEU   B 25  ? 0.1871 0.2325 0.3916 0.0102  0.0094  0.0235  31  LEU   C CA  
1296 C C   . LEU   B 25  ? 0.1926 0.2374 0.3895 0.0124  0.0149  0.0187  31  LEU   C C   
1297 O O   . LEU   B 25  ? 0.2015 0.2471 0.4045 0.0149  0.0199  0.0169  31  LEU   C O   
1298 C CB  . LEU   B 25  ? 0.1754 0.2182 0.3845 0.0109  0.0083  0.0215  31  LEU   C CB  
1299 C CG  . LEU   B 25  ? 0.1857 0.2253 0.3845 0.0109  0.0077  0.0166  31  LEU   C CG  
1300 C CD1 . LEU   B 25  ? 0.1889 0.2285 0.3783 0.0083  0.0033  0.0188  31  LEU   C CD1 
1301 C CD2 . LEU   B 25  ? 0.1919 0.2289 0.3980 0.0116  0.0072  0.0145  31  LEU   C CD2 
1302 N N   . VAL   B 26  ? 0.1797 0.2229 0.3629 0.0117  0.0140  0.0167  32  VAL   C N   
1303 C CA  . VAL   B 26  ? 0.1889 0.2310 0.3623 0.0138  0.0182  0.0121  32  VAL   C CA  
1304 C C   . VAL   B 26  ? 0.2038 0.2425 0.3703 0.0146  0.0167  0.0064  32  VAL   C C   
1305 O O   . VAL   B 26  ? 0.2117 0.2488 0.3770 0.0171  0.0200  0.0013  32  VAL   C O   
1306 C CB  . VAL   B 26  ? 0.2057 0.2482 0.3690 0.0127  0.0180  0.0141  32  VAL   C CB  
1307 C CG1 . VAL   B 26  ? 0.2224 0.2630 0.3729 0.0148  0.0212  0.0096  32  VAL   C CG1 
1308 C CG2 . VAL   B 26  ? 0.2011 0.2468 0.3721 0.0119  0.0201  0.0192  32  VAL   C CG2 
1309 N N   . TRP   B 27  ? 0.1974 0.2352 0.3601 0.0124  0.0116  0.0072  33  TRP   C N   
1310 C CA  . TRP   B 27  ? 0.2017 0.2371 0.3594 0.0127  0.0098  0.0024  33  TRP   C CA  
1311 C C   . TRP   B 27  ? 0.1970 0.2324 0.3563 0.0101  0.0048  0.0053  33  TRP   C C   
1312 O O   . TRP   B 27  ? 0.1977 0.2345 0.3554 0.0084  0.0026  0.0098  33  TRP   C O   
1313 C CB  . TRP   B 27  ? 0.2116 0.2460 0.3554 0.0137  0.0103  -0.0010 33  TRP   C CB  
1314 C CG  . TRP   B 27  ? 0.2209 0.2536 0.3588 0.0135  0.0072  -0.0054 33  TRP   C CG  
1315 C CD1 . TRP   B 27  ? 0.2352 0.2657 0.3723 0.0151  0.0076  -0.0114 33  TRP   C CD1 
1316 C CD2 . TRP   B 27  ? 0.2144 0.2476 0.3467 0.0118  0.0031  -0.0042 33  TRP   C CD2 
1317 N NE1 . TRP   B 27  ? 0.2408 0.2708 0.3731 0.0142  0.0037  -0.0139 33  TRP   C NE1 
1318 C CE2 . TRP   B 27  ? 0.2291 0.2608 0.3586 0.0123  0.0012  -0.0094 33  TRP   C CE2 
1319 C CE3 . TRP   B 27  ? 0.2183 0.2527 0.3481 0.0100  0.0008  0.0004  33  TRP   C CE3 
1320 C CZ2 . TRP   B 27  ? 0.2308 0.2632 0.3559 0.0111  -0.0024 -0.0096 33  TRP   C CZ2 
1321 C CZ3 . TRP   B 27  ? 0.2341 0.2687 0.3583 0.0092  -0.0025 -0.0002 33  TRP   C CZ3 
1322 C CH2 . TRP   B 27  ? 0.2363 0.2702 0.3590 0.0097  -0.0039 -0.0049 33  TRP   C CH2 
1323 N N   . GLU   B 28  ? 0.1752 0.2090 0.3379 0.0098  0.0032  0.0027  34  GLU   C N   
1324 C CA  . GLU   B 28  ? 0.1778 0.2119 0.3417 0.0075  -0.0006 0.0056  34  GLU   C CA  
1325 C C   . GLU   B 28  ? 0.1899 0.2225 0.3527 0.0074  -0.0018 0.0010  34  GLU   C C   
1326 O O   . GLU   B 28  ? 0.1855 0.2160 0.3516 0.0088  -0.0004 -0.0037 34  GLU   C O   
1327 C CB  . GLU   B 28  ? 0.1881 0.2226 0.3632 0.0064  -0.0017 0.0107  34  GLU   C CB  
1328 C CG  . GLU   B 28  ? 0.2058 0.2385 0.3918 0.0078  0.0003  0.0088  34  GLU   C CG  
1329 C CD  . GLU   B 28  ? 0.2257 0.2560 0.4161 0.0072  -0.0009 0.0063  34  GLU   C CD  
1330 O OE1 . GLU   B 28  ? 0.2386 0.2664 0.4357 0.0087  0.0008  0.0025  34  GLU   C OE1 
1331 O OE2 . GLU   B 28  ? 0.2100 0.2408 0.3976 0.0052  -0.0035 0.0081  34  GLU   C OE2 
1332 N N   . ASP   B 29  ? 0.1856 0.2191 0.3443 0.0057  -0.0046 0.0022  35  ASP   C N   
1333 C CA  . ASP   B 29  ? 0.1888 0.2216 0.3484 0.0052  -0.0061 -0.0016 35  ASP   C CA  
1334 C C   . ASP   B 29  ? 0.1842 0.2185 0.3466 0.0029  -0.0082 0.0027  35  ASP   C C   
1335 O O   . ASP   B 29  ? 0.1932 0.2293 0.3486 0.0023  -0.0094 0.0048  35  ASP   C O   
1336 C CB  . ASP   B 29  ? 0.2130 0.2459 0.3621 0.0064  -0.0067 -0.0064 35  ASP   C CB  
1337 C CG  . ASP   B 29  ? 0.2827 0.3151 0.4336 0.0061  -0.0086 -0.0113 35  ASP   C CG  
1338 O OD1 . ASP   B 29  ? 0.2881 0.3209 0.4469 0.0042  -0.0099 -0.0096 35  ASP   C OD1 
1339 O OD2 . ASP   B 29  ? 0.3012 0.3327 0.4455 0.0077  -0.0091 -0.0166 35  ASP   C OD2 
1340 N N   . SER   B 30  ? 0.1783 0.2116 0.3508 0.0017  -0.0085 0.0042  36  SER   C N   
1341 C CA  A SER   B 30  ? 0.1821 0.2168 0.3576 -0.0005 -0.0098 0.0089  36  SER   C CA  
1342 C CA  B SER   B 30  ? 0.1827 0.2175 0.3579 -0.0005 -0.0098 0.0090  36  SER   C CA  
1343 C C   . SER   B 30  ? 0.1804 0.2171 0.3514 -0.0012 -0.0109 0.0066  36  SER   C C   
1344 O O   . SER   B 30  ? 0.1811 0.2201 0.3488 -0.0022 -0.0114 0.0104  36  SER   C O   
1345 C CB  A SER   B 30  ? 0.1948 0.2276 0.3826 -0.0015 -0.0096 0.0107  36  SER   C CB  
1346 C CB  B SER   B 30  ? 0.1970 0.2299 0.3845 -0.0016 -0.0096 0.0112  36  SER   C CB  
1347 O OG  A SER   B 30  ? 0.1990 0.2332 0.3896 -0.0037 -0.0103 0.0154  36  SER   C OG  
1348 O OG  B SER   B 30  ? 0.2018 0.2323 0.3950 -0.0011 -0.0094 0.0054  36  SER   C OG  
1349 N N   . SER   B 31  ? 0.1784 0.2144 0.3495 -0.0004 -0.0115 0.0003  37  SER   C N   
1350 C CA  . SER   B 31  ? 0.1866 0.2249 0.3551 -0.0010 -0.0130 -0.0020 37  SER   C CA  
1351 C C   . SER   B 31  ? 0.1700 0.2105 0.3270 0.0000  -0.0135 -0.0012 37  SER   C C   
1352 O O   . SER   B 31  ? 0.1866 0.2298 0.3422 -0.0006 -0.0145 -0.0012 37  SER   C O   
1353 C CB  . SER   B 31  ? 0.2385 0.2755 0.4092 -0.0004 -0.0145 -0.0091 37  SER   C CB  
1354 O OG  . SER   B 31  ? 0.3124 0.3482 0.4738 0.0020  -0.0144 -0.0133 37  SER   C OG  
1355 N N   . ARG   B 32  ? 0.1497 0.1892 0.2996 0.0014  -0.0127 -0.0005 38  ARG   C N   
1356 C CA  . ARG   B 32  ? 0.1670 0.2078 0.3067 0.0023  -0.0132 0.0003  38  ARG   C CA  
1357 C C   . ARG   B 32  ? 0.1669 0.2081 0.3044 0.0015  -0.0129 0.0062  38  ARG   C C   
1358 O O   . ARG   B 32  ? 0.1602 0.2018 0.2899 0.0021  -0.0135 0.0070  38  ARG   C O   
1359 C CB  . ARG   B 32  ? 0.1996 0.2386 0.3320 0.0043  -0.0126 -0.0027 38  ARG   C CB  
1360 C CG  . ARG   B 32  ? 0.2353 0.2735 0.3664 0.0056  -0.0134 -0.0089 38  ARG   C CG  
1361 C CD  . ARG   B 32  ? 0.2435 0.2798 0.3664 0.0078  -0.0121 -0.0111 38  ARG   C CD  
1362 N NE  . ARG   B 32  ? 0.2276 0.2646 0.3411 0.0086  -0.0126 -0.0093 38  ARG   C NE  
1363 C CZ  . ARG   B 32  ? 0.2253 0.2611 0.3297 0.0106  -0.0125 -0.0116 38  ARG   C CZ  
1364 N NH1 . ARG   B 32  ? 0.2088 0.2430 0.3113 0.0121  -0.0118 -0.0161 38  ARG   C NH1 
1365 N NH2 . ARG   B 32  ? 0.1956 0.2315 0.2926 0.0112  -0.0133 -0.0096 38  ARG   C NH2 
1366 N N   . ASP   B 33  ? 0.1532 0.1938 0.2977 0.0003  -0.0123 0.0100  39  ASP   C N   
1367 C CA  . ASP   B 33  ? 0.1487 0.1894 0.2913 -0.0004 -0.0127 0.0153  39  ASP   C CA  
1368 C C   . ASP   B 33  ? 0.1455 0.1851 0.2829 0.0006  -0.0127 0.0152  39  ASP   C C   
1369 O O   . ASP   B 33  ? 0.1422 0.1820 0.2743 0.0003  -0.0139 0.0180  39  ASP   C O   
1370 C CB  . ASP   B 33  ? 0.1552 0.1977 0.2929 -0.0011 -0.0134 0.0179  39  ASP   C CB  
1371 C CG  . ASP   B 33  ? 0.1833 0.2253 0.3185 -0.0018 -0.0144 0.0231  39  ASP   C CG  
1372 O OD1 . ASP   B 33  ? 0.1995 0.2407 0.3407 -0.0025 -0.0146 0.0262  39  ASP   C OD1 
1373 O OD2 . ASP   B 33  ? 0.1574 0.1999 0.2845 -0.0016 -0.0153 0.0240  39  ASP   C OD2 
1374 N N   . LEU   B 34  ? 0.1368 0.1753 0.2758 0.0018  -0.0112 0.0121  40  LEU   C N   
1375 C CA  . LEU   B 34  ? 0.1223 0.1601 0.2576 0.0026  -0.0105 0.0127  40  LEU   C CA  
1376 C C   . LEU   B 34  ? 0.1327 0.1701 0.2761 0.0029  -0.0088 0.0139  40  LEU   C C   
1377 O O   . LEU   B 34  ? 0.1451 0.1818 0.2949 0.0035  -0.0074 0.0117  40  LEU   C O   
1378 C CB  . LEU   B 34  ? 0.1230 0.1603 0.2509 0.0042  -0.0096 0.0086  40  LEU   C CB  
1379 C CG  . LEU   B 34  ? 0.1501 0.1878 0.2693 0.0045  -0.0114 0.0077  40  LEU   C CG  
1380 C CD1 . LEU   B 34  ? 0.1504 0.1872 0.2626 0.0063  -0.0107 0.0040  40  LEU   C CD1 
1381 C CD2 . LEU   B 34  ? 0.1567 0.1942 0.2720 0.0036  -0.0128 0.0115  40  LEU   C CD2 
1382 N N   . LEU   B 35  ? 0.1282 0.1659 0.2715 0.0027  -0.0088 0.0170  41  LEU   C N   
1383 C CA  . LEU   B 35  ? 0.1402 0.1782 0.2916 0.0033  -0.0069 0.0184  41  LEU   C CA  
1384 C C   . LEU   B 35  ? 0.1472 0.1857 0.2948 0.0035  -0.0059 0.0194  41  LEU   C C   
1385 O O   . LEU   B 35  ? 0.1700 0.2084 0.3121 0.0024  -0.0083 0.0215  41  LEU   C O   
1386 C CB  . LEU   B 35  ? 0.1392 0.1779 0.2992 0.0020  -0.0090 0.0232  41  LEU   C CB  
1387 C CG  . LEU   B 35  ? 0.1570 0.1964 0.3278 0.0029  -0.0071 0.0248  41  LEU   C CG  
1388 C CD1 . LEU   B 35  ? 0.1804 0.2194 0.3610 0.0025  -0.0083 0.0273  41  LEU   C CD1 
1389 C CD2 . LEU   B 35  ? 0.1584 0.1994 0.3302 0.0021  -0.0082 0.0284  41  LEU   C CD2 
1390 N N   . VAL   B 36  ? 0.1408 0.1795 0.2913 0.0050  -0.0023 0.0179  42  VAL   C N   
1391 C CA  . VAL   B 36  ? 0.1439 0.1834 0.2927 0.0052  -0.0005 0.0195  42  VAL   C CA  
1392 C C   . VAL   B 36  ? 0.1529 0.1943 0.3135 0.0055  0.0017  0.0220  42  VAL   C C   
1393 O O   . VAL   B 36  ? 0.1581 0.1996 0.3246 0.0072  0.0046  0.0198  42  VAL   C O   
1394 C CB  . VAL   B 36  ? 0.1618 0.2003 0.3020 0.0071  0.0029  0.0155  42  VAL   C CB  
1395 C CG1 . VAL   B 36  ? 0.1611 0.2003 0.3005 0.0072  0.0055  0.0180  42  VAL   C CG1 
1396 C CG2 . VAL   B 36  ? 0.1667 0.2036 0.2961 0.0070  0.0002  0.0131  42  VAL   C CG2 
1397 N N   . SER   B 37  ? 0.1503 0.1933 0.3149 0.0040  0.0002  0.0264  43  SER   C N   
1398 C CA  . SER   B 37  ? 0.1529 0.1986 0.3302 0.0042  0.0021  0.0293  43  SER   C CA  
1399 C C   . SER   B 37  ? 0.1680 0.2151 0.3452 0.0040  0.0049  0.0310  43  SER   C C   
1400 O O   . SER   B 37  ? 0.1658 0.2113 0.3332 0.0032  0.0042  0.0307  43  SER   C O   
1401 C CB  . SER   B 37  ? 0.1573 0.2041 0.3423 0.0023  -0.0030 0.0337  43  SER   C CB  
1402 O OG  . SER   B 37  ? 0.1784 0.2245 0.3574 0.0001  -0.0075 0.0360  43  SER   C OG  
1403 N N   . SER   B 38  ? 0.1711 0.2213 0.3597 0.0048  0.0085  0.0328  44  SER   C N   
1404 C CA  . SER   B 38  ? 0.1868 0.2388 0.3771 0.0044  0.0119  0.0351  44  SER   C CA  
1405 C C   . SER   B 38  ? 0.2051 0.2589 0.4030 0.0014  0.0072  0.0402  44  SER   C C   
1406 O O   . SER   B 38  ? 0.2048 0.2596 0.4102 0.0003  0.0024  0.0423  44  SER   C O   
1407 C CB  . SER   B 38  ? 0.2174 0.2723 0.4165 0.0070  0.0190  0.0344  44  SER   C CB  
1408 O OG  . SER   B 38  ? 0.2446 0.3021 0.4584 0.0071  0.0176  0.0365  44  SER   C OG  
1409 N N   . THR   B 39  ? 0.2051 0.2591 0.4014 0.0000  0.0083  0.0423  45  THR   C N   
1410 C CA  . THR   B 39  ? 0.2104 0.2656 0.4136 -0.0031 0.0034  0.0467  45  THR   C CA  
1411 C C   . THR   B 39  ? 0.2407 0.2996 0.4549 -0.0036 0.0080  0.0501  45  THR   C C   
1412 O O   . THR   B 39  ? 0.2394 0.2990 0.4510 -0.0017 0.0152  0.0491  45  THR   C O   
1413 C CB  . THR   B 39  ? 0.2236 0.2744 0.4143 -0.0050 -0.0013 0.0462  45  THR   C CB  
1414 O OG1 . THR   B 39  ? 0.2312 0.2803 0.4138 -0.0043 0.0033  0.0454  45  THR   C OG1 
1415 C CG2 . THR   B 39  ? 0.2313 0.2789 0.4117 -0.0045 -0.0055 0.0431  45  THR   C CG2 
1416 N N   . THR   B 40  ? 0.2602 0.3216 0.4864 -0.0063 0.0038  0.0542  46  THR   C N   
1417 C CA  . THR   B 40  ? 0.2825 0.3480 0.5212 -0.0073 0.0080  0.0580  46  THR   C CA  
1418 C C   . THR   B 40  ? 0.2848 0.3473 0.5161 -0.0094 0.0079  0.0593  46  THR   C C   
1419 O O   . THR   B 40  ? 0.3010 0.3650 0.5336 -0.0089 0.0147  0.0609  46  THR   C O   
1420 C CB  . THR   B 40  ? 0.3234 0.3936 0.5804 -0.0091 0.0035  0.0618  46  THR   C CB  
1421 O OG1 . THR   B 40  ? 0.3626 0.4298 0.6163 -0.0121 -0.0060 0.0626  46  THR   C OG1 
1422 C CG2 . THR   B 40  ? 0.3279 0.4006 0.5923 -0.0065 0.0039  0.0608  46  THR   C CG2 
1423 N N   . ALA   B 41  ? 0.2685 0.3266 0.4918 -0.0117 0.0004  0.0588  47  ALA   C N   
1424 C CA  . ALA   B 41  ? 0.2652 0.3194 0.4813 -0.0136 -0.0003 0.0597  47  ALA   C CA  
1425 C C   . ALA   B 41  ? 0.2593 0.3089 0.4572 -0.0113 0.0025  0.0561  47  ALA   C C   
1426 O O   . ALA   B 41  ? 0.2511 0.2995 0.4407 -0.0091 0.0019  0.0523  47  ALA   C O   
1427 C CB  . ALA   B 41  ? 0.2704 0.3216 0.4866 -0.0168 -0.0098 0.0603  47  ALA   C CB  
1428 N N   . GLN   B 42  ? 0.2563 0.3031 0.4486 -0.0119 0.0049  0.0575  48  GLN   C N   
1429 C CA  . GLN   B 42  ? 0.2717 0.3141 0.4472 -0.0098 0.0069  0.0547  48  GLN   C CA  
1430 C C   . GLN   B 42  ? 0.2700 0.3072 0.4356 -0.0108 -0.0006 0.0523  48  GLN   C C   
1431 O O   . GLN   B 42  ? 0.2757 0.3111 0.4459 -0.0136 -0.0061 0.0540  48  GLN   C O   
1432 C CB  . GLN   B 42  ? 0.3163 0.3578 0.4898 -0.0098 0.0126  0.0579  48  GLN   C CB  
1433 C CG  . GLN   B 42  ? 0.4090 0.4546 0.5846 -0.0072 0.0218  0.0585  48  GLN   C CG  
1434 C CD  . GLN   B 42  ? 0.5355 0.5792 0.7047 -0.0068 0.0274  0.0616  48  GLN   C CD  
1435 O OE1 . GLN   B 42  ? 0.5715 0.6152 0.7486 -0.0096 0.0279  0.0665  48  GLN   C OE1 
1436 N NE2 . GLN   B 42  ? 0.5591 0.6007 0.7138 -0.0035 0.0312  0.0589  48  GLN   C NE2 
1437 N N   . GLY   B 43  ? 0.2491 0.2839 0.4019 -0.0083 -0.0009 0.0482  49  GLY   C N   
1438 C CA  . GLY   B 43  ? 0.2418 0.2720 0.3846 -0.0086 -0.0068 0.0457  49  GLY   C CA  
1439 C C   . GLY   B 43  ? 0.2405 0.2660 0.3737 -0.0082 -0.0062 0.0459  49  GLY   C C   
1440 O O   . GLY   B 43  ? 0.2501 0.2758 0.3819 -0.0073 -0.0008 0.0479  49  GLY   C O   
1441 N N   . CYS   B 44  ? 0.2274 0.2485 0.3538 -0.0087 -0.0117 0.0442  50  CYS   C N   
1442 C CA  . CYS   B 44  ? 0.2456 0.2617 0.3642 -0.0083 -0.0118 0.0448  50  CYS   C CA  
1443 C C   . CYS   B 44  ? 0.2469 0.2604 0.3526 -0.0056 -0.0130 0.0408  50  CYS   C C   
1444 O O   . CYS   B 44  ? 0.2601 0.2692 0.3592 -0.0049 -0.0136 0.0412  50  CYS   C O   
1445 C CB  . CYS   B 44  ? 0.2662 0.2785 0.3894 -0.0114 -0.0169 0.0466  50  CYS   C CB  
1446 S SG  . CYS   B 44  ? 0.3377 0.3534 0.4781 -0.0150 -0.0158 0.0517  50  CYS   C SG  
1447 N N   . ASP   B 45  ? 0.2223 0.2384 0.3253 -0.0040 -0.0134 0.0374  51  ASP   C N   
1448 C CA  . ASP   B 45  ? 0.2167 0.2312 0.3092 -0.0014 -0.0144 0.0337  51  ASP   C CA  
1449 C C   . ASP   B 45  ? 0.2197 0.2348 0.3064 0.0010  -0.0097 0.0334  51  ASP   C C   
1450 O O   . ASP   B 45  ? 0.2204 0.2385 0.3108 0.0013  -0.0052 0.0347  51  ASP   C O   
1451 C CB  . ASP   B 45  ? 0.2282 0.2456 0.3210 -0.0009 -0.0160 0.0306  51  ASP   C CB  
1452 C CG  . ASP   B 45  ? 0.2881 0.3045 0.3833 -0.0027 -0.0210 0.0305  51  ASP   C CG  
1453 O OD1 . ASP   B 45  ? 0.2928 0.3051 0.3852 -0.0035 -0.0242 0.0307  51  ASP   C OD1 
1454 O OD2 . ASP   B 45  ? 0.2867 0.3061 0.3861 -0.0032 -0.0218 0.0301  51  ASP   C OD2 
1455 N N   . THR   B 46  ? 0.2120 0.2243 0.2893 0.0031  -0.0110 0.0317  52  THR   C N   
1456 C CA  . THR   B 46  ? 0.2176 0.2301 0.2875 0.0057  -0.0078 0.0309  52  THR   C CA  
1457 C C   . THR   B 46  ? 0.2085 0.2228 0.2738 0.0077  -0.0097 0.0261  52  THR   C C   
1458 O O   . THR   B 46  ? 0.1974 0.2104 0.2611 0.0079  -0.0135 0.0244  52  THR   C O   
1459 C CB  . THR   B 46  ? 0.2542 0.2619 0.3175 0.0066  -0.0086 0.0331  52  THR   C CB  
1460 O OG1 . THR   B 46  ? 0.2759 0.2820 0.3444 0.0044  -0.0065 0.0380  52  THR   C OG1 
1461 C CG2 . THR   B 46  ? 0.2762 0.2839 0.3299 0.0097  -0.0066 0.0320  52  THR   C CG2 
1462 N N   . ILE   B 47  ? 0.1943 0.2112 0.2575 0.0094  -0.0070 0.0239  53  ILE   C N   
1463 C CA  . ILE   B 47  ? 0.1911 0.2098 0.2512 0.0111  -0.0088 0.0194  53  ILE   C CA  
1464 C C   . ILE   B 47  ? 0.1931 0.2096 0.2437 0.0136  -0.0104 0.0183  53  ILE   C C   
1465 O O   . ILE   B 47  ? 0.2022 0.2171 0.2471 0.0148  -0.0082 0.0200  53  ILE   C O   
1466 C CB  . ILE   B 47  ? 0.1887 0.2106 0.2512 0.0118  -0.0059 0.0169  53  ILE   C CB  
1467 C CG1 . ILE   B 47  ? 0.1960 0.2201 0.2687 0.0097  -0.0039 0.0186  53  ILE   C CG1 
1468 C CG2 . ILE   B 47  ? 0.1986 0.2222 0.2598 0.0129  -0.0083 0.0123  53  ILE   C CG2 
1469 C CD1 . ILE   B 47  ? 0.2104 0.2350 0.2889 0.0076  -0.0076 0.0190  53  ILE   C CD1 
1470 N N   . ALA   B 48  ? 0.1948 0.2117 0.2438 0.0145  -0.0140 0.0155  54  ALA   C N   
1471 C CA  . ALA   B 48  ? 0.1908 0.2062 0.2321 0.0171  -0.0161 0.0142  54  ALA   C CA  
1472 C C   . ALA   B 48  ? 0.1933 0.2108 0.2304 0.0190  -0.0149 0.0113  54  ALA   C C   
1473 O O   . ALA   B 48  ? 0.2083 0.2288 0.2499 0.0184  -0.0141 0.0086  54  ALA   C O   
1474 C CB  . ALA   B 48  ? 0.1839 0.2003 0.2266 0.0177  -0.0198 0.0117  54  ALA   C CB  
1475 N N   . ARG   B 49  ? 0.1839 0.1994 0.2122 0.0213  -0.0153 0.0118  55  ARG   C N   
1476 C CA  . ARG   B 49  ? 0.1925 0.2094 0.2151 0.0234  -0.0152 0.0085  55  ARG   C CA  
1477 C C   . ARG   B 49  ? 0.1983 0.2143 0.2148 0.0259  -0.0198 0.0074  55  ARG   C C   
1478 O O   . ARG   B 49  ? 0.2082 0.2210 0.2173 0.0275  -0.0202 0.0104  55  ARG   C O   
1479 C CB  . ARG   B 49  ? 0.1960 0.2114 0.2127 0.0241  -0.0107 0.0108  55  ARG   C CB  
1480 C CG  . ARG   B 49  ? 0.2039 0.2205 0.2283 0.0218  -0.0060 0.0125  55  ARG   C CG  
1481 C CD  . ARG   B 49  ? 0.2153 0.2352 0.2461 0.0211  -0.0053 0.0081  55  ARG   C CD  
1482 N NE  . ARG   B 49  ? 0.2117 0.2327 0.2504 0.0192  -0.0010 0.0103  55  ARG   C NE  
1483 C CZ  . ARG   B 49  ? 0.2497 0.2732 0.2974 0.0179  -0.0006 0.0083  55  ARG   C CZ  
1484 N NH1 . ARG   B 49  ? 0.2137 0.2386 0.2635 0.0180  -0.0038 0.0041  55  ARG   C NH1 
1485 N NH2 . ARG   B 49  ? 0.2412 0.2658 0.2965 0.0164  0.0029  0.0107  55  ARG   C NH2 
1486 N N   . CYS   B 50  ? 0.1958 0.2147 0.2167 0.0261  -0.0233 0.0036  56  CYS   C N   
1487 C CA  . CYS   B 50  ? 0.1931 0.2120 0.2116 0.0282  -0.0279 0.0026  56  CYS   C CA  
1488 C C   . CYS   B 50  ? 0.2076 0.2312 0.2330 0.0281  -0.0306 -0.0021 56  CYS   C C   
1489 O O   . CYS   B 50  ? 0.1936 0.2197 0.2255 0.0261  -0.0288 -0.0040 56  CYS   C O   
1490 C CB  . CYS   B 50  ? 0.2077 0.2242 0.2287 0.0277  -0.0284 0.0059  56  CYS   C CB  
1491 S SG  . CYS   B 50  ? 0.2223 0.2412 0.2540 0.0248  -0.0274 0.0050  56  CYS   C SG  
1492 N N   . ASP   B 51  ? 0.2026 0.2275 0.2281 0.0300  -0.0348 -0.0033 57  ASP   C N   
1493 C CA  . ASP   B 51  ? 0.2083 0.2379 0.2418 0.0298  -0.0372 -0.0071 57  ASP   C CA  
1494 C C   . ASP   B 51  ? 0.2097 0.2401 0.2483 0.0302  -0.0382 -0.0058 57  ASP   C C   
1495 O O   . ASP   B 51  ? 0.2264 0.2604 0.2697 0.0314  -0.0410 -0.0080 57  ASP   C O   
1496 C CB  . ASP   B 51  ? 0.2442 0.2759 0.2748 0.0320  -0.0416 -0.0106 57  ASP   C CB  
1497 C CG  . ASP   B 51  ? 0.2925 0.3220 0.3159 0.0352  -0.0452 -0.0088 57  ASP   C CG  
1498 O OD1 . ASP   B 51  ? 0.2883 0.3144 0.3095 0.0357  -0.0441 -0.0049 57  ASP   C OD1 
1499 O OD2 . ASP   B 51  ? 0.3605 0.3916 0.3809 0.0372  -0.0495 -0.0115 57  ASP   C OD2 
1500 N N   . CYS   B 52  ? 0.1990 0.2260 0.2370 0.0292  -0.0359 -0.0025 58  CYS   C N   
1501 C CA  . CYS   B 52  ? 0.1784 0.2053 0.2199 0.0298  -0.0365 -0.0018 58  CYS   C CA  
1502 C C   . CYS   B 52  ? 0.1760 0.2081 0.2262 0.0287  -0.0360 -0.0042 58  CYS   C C   
1503 O O   . CYS   B 52  ? 0.1809 0.2151 0.2349 0.0263  -0.0340 -0.0050 58  CYS   C O   
1504 C CB  . CYS   B 52  ? 0.1836 0.2058 0.2234 0.0284  -0.0343 0.0015  58  CYS   C CB  
1505 S SG  . CYS   B 52  ? 0.2140 0.2294 0.2454 0.0301  -0.0352 0.0053  58  CYS   C SG  
1506 N N   . GLN   B 53  ? 0.1597 0.1936 0.2132 0.0305  -0.0374 -0.0050 59  GLN   C N   
1507 C CA  . GLN   B 53  ? 0.1698 0.2086 0.2314 0.0296  -0.0361 -0.0066 59  GLN   C CA  
1508 C C   . GLN   B 53  ? 0.1739 0.2109 0.2355 0.0302  -0.0347 -0.0055 59  GLN   C C   
1509 O O   . GLN   B 53  ? 0.1661 0.2071 0.2333 0.0303  -0.0334 -0.0065 59  GLN   C O   
1510 C CB  . GLN   B 53  ? 0.1883 0.2330 0.2564 0.0310  -0.0385 -0.0093 59  GLN   C CB  
1511 C CG  . GLN   B 53  ? 0.2135 0.2606 0.2835 0.0296  -0.0396 -0.0114 59  GLN   C CG  
1512 C CD  . GLN   B 53  ? 0.2622 0.3155 0.3405 0.0305  -0.0423 -0.0142 59  GLN   C CD  
1513 O OE1 . GLN   B 53  ? 0.2842 0.3382 0.3608 0.0323  -0.0465 -0.0160 59  GLN   C OE1 
1514 N NE2 . GLN   B 53  ? 0.2164 0.2744 0.3039 0.0293  -0.0402 -0.0145 59  GLN   C NE2 
1515 N N   . THR   B 54  ? 0.1764 0.2073 0.2318 0.0306  -0.0347 -0.0034 60  THR   C N   
1516 C CA  . THR   B 54  ? 0.1940 0.2219 0.2483 0.0310  -0.0337 -0.0029 60  THR   C CA  
1517 C C   . THR   B 54  ? 0.1956 0.2181 0.2457 0.0285  -0.0327 -0.0005 60  THR   C C   
1518 O O   . THR   B 54  ? 0.1993 0.2192 0.2462 0.0278  -0.0332 0.0013  60  THR   C O   
1519 C CB  . THR   B 54  ? 0.2352 0.2605 0.2879 0.0347  -0.0358 -0.0034 60  THR   C CB  
1520 O OG1 . THR   B 54  ? 0.2477 0.2674 0.2948 0.0354  -0.0377 -0.0013 60  THR   C OG1 
1521 C CG2 . THR   B 54  ? 0.2455 0.2769 0.3039 0.0373  -0.0371 -0.0056 60  THR   C CG2 
1522 N N   . GLY   B 55  ? 0.1880 0.2094 0.2383 0.0272  -0.0314 -0.0004 61  GLY   C N   
1523 C CA  . GLY   B 55  ? 0.1937 0.2106 0.2415 0.0247  -0.0310 0.0017  61  GLY   C CA  
1524 C C   . GLY   B 55  ? 0.1923 0.2078 0.2393 0.0241  -0.0305 0.0011  61  GLY   C C   
1525 O O   . GLY   B 55  ? 0.1856 0.2024 0.2326 0.0263  -0.0302 -0.0010 61  GLY   C O   
1526 N N   . VAL   B 56  ? 0.1734 0.1865 0.2197 0.0213  -0.0304 0.0028  62  VAL   C N   
1527 C CA  . VAL   B 56  ? 0.1668 0.1781 0.2110 0.0205  -0.0306 0.0023  62  VAL   C CA  
1528 C C   . VAL   B 56  ? 0.1675 0.1814 0.2144 0.0173  -0.0297 0.0041  62  VAL   C C   
1529 O O   . VAL   B 56  ? 0.1829 0.1966 0.2323 0.0153  -0.0296 0.0062  62  VAL   C O   
1530 C CB  . VAL   B 56  ? 0.1857 0.1895 0.2263 0.0204  -0.0331 0.0026  62  VAL   C CB  
1531 C CG1 . VAL   B 56  ? 0.1948 0.1959 0.2325 0.0191  -0.0342 0.0018  62  VAL   C CG1 
1532 C CG2 . VAL   B 56  ? 0.1979 0.1984 0.2363 0.0238  -0.0342 0.0009  62  VAL   C CG2 
1533 N N   . TYR   B 57  ? 0.1634 0.1798 0.2099 0.0169  -0.0287 0.0037  63  TYR   C N   
1534 C CA  . TYR   B 57  ? 0.1717 0.1901 0.2209 0.0140  -0.0282 0.0060  63  TYR   C CA  
1535 C C   . TYR   B 57  ? 0.1761 0.1916 0.2209 0.0131  -0.0298 0.0063  63  TYR   C C   
1536 O O   . TYR   B 57  ? 0.1854 0.1990 0.2250 0.0151  -0.0301 0.0041  63  TYR   C O   
1537 C CB  . TYR   B 57  ? 0.1852 0.2099 0.2392 0.0137  -0.0256 0.0063  63  TYR   C CB  
1538 C CG  . TYR   B 57  ? 0.1901 0.2174 0.2423 0.0147  -0.0239 0.0057  63  TYR   C CG  
1539 C CD1 . TYR   B 57  ? 0.1942 0.2230 0.2452 0.0176  -0.0227 0.0033  63  TYR   C CD1 
1540 C CD2 . TYR   B 57  ? 0.1895 0.2182 0.2418 0.0130  -0.0232 0.0079  63  TYR   C CD2 
1541 C CE1 . TYR   B 57  ? 0.2019 0.2338 0.2518 0.0186  -0.0202 0.0030  63  TYR   C CE1 
1542 C CE2 . TYR   B 57  ? 0.1930 0.2245 0.2433 0.0139  -0.0210 0.0080  63  TYR   C CE2 
1543 C CZ  . TYR   B 57  ? 0.2101 0.2432 0.2590 0.0168  -0.0192 0.0054  63  TYR   C CZ  
1544 O OH  . TYR   B 57  ? 0.2274 0.2638 0.2747 0.0178  -0.0161 0.0058  63  TYR   C OH  
1545 N N   . TYR   B 58  ? 0.1726 0.1879 0.2196 0.0103  -0.0310 0.0088  64  TYR   C N   
1546 C CA  . TYR   B 58  ? 0.1905 0.2032 0.2332 0.0093  -0.0333 0.0092  64  TYR   C CA  
1547 C C   . TYR   B 58  ? 0.1865 0.2034 0.2287 0.0091  -0.0315 0.0105  64  TYR   C C   
1548 O O   . TYR   B 58  ? 0.1753 0.1961 0.2237 0.0077  -0.0300 0.0128  64  TYR   C O   
1549 C CB  . TYR   B 58  ? 0.1980 0.2082 0.2438 0.0065  -0.0364 0.0115  64  TYR   C CB  
1550 C CG  . TYR   B 58  ? 0.2149 0.2221 0.2556 0.0055  -0.0398 0.0115  64  TYR   C CG  
1551 C CD1 . TYR   B 58  ? 0.2220 0.2243 0.2548 0.0070  -0.0420 0.0084  64  TYR   C CD1 
1552 C CD2 . TYR   B 58  ? 0.2196 0.2288 0.2630 0.0034  -0.0412 0.0145  64  TYR   C CD2 
1553 C CE1 . TYR   B 58  ? 0.2265 0.2257 0.2533 0.0063  -0.0456 0.0079  64  TYR   C CE1 
1554 C CE2 . TYR   B 58  ? 0.2284 0.2348 0.2663 0.0026  -0.0451 0.0145  64  TYR   C CE2 
1555 C CZ  . TYR   B 58  ? 0.2388 0.2402 0.2678 0.0041  -0.0474 0.0110  64  TYR   C CZ  
1556 O OH  . TYR   B 58  ? 0.2670 0.2653 0.2892 0.0035  -0.0516 0.0105  64  TYR   C OH  
1557 N N   . CYS   B 59  ? 0.1825 0.1981 0.2172 0.0105  -0.0317 0.0091  65  CYS   C N   
1558 C CA  . CYS   B 59  ? 0.1915 0.2107 0.2240 0.0105  -0.0296 0.0107  65  CYS   C CA  
1559 C C   . CYS   B 59  ? 0.2034 0.2190 0.2294 0.0093  -0.0333 0.0118  65  CYS   C C   
1560 O O   . CYS   B 59  ? 0.2051 0.2168 0.2221 0.0109  -0.0348 0.0091  65  CYS   C O   
1561 C CB  . CYS   B 59  ? 0.1993 0.2204 0.2278 0.0136  -0.0261 0.0083  65  CYS   C CB  
1562 S SG  . CYS   B 59  ? 0.2337 0.2591 0.2588 0.0138  -0.0226 0.0109  65  CYS   C SG  
1563 N N   . SER   B 60  ? 0.2036 0.2204 0.2340 0.0067  -0.0351 0.0155  66  SER   C N   
1564 C CA  A SER   B 60  ? 0.2177 0.2313 0.2424 0.0055  -0.0396 0.0166  66  SER   C CA  
1565 C CA  B SER   B 60  ? 0.2124 0.2260 0.2372 0.0055  -0.0395 0.0166  66  SER   C CA  
1566 C C   . SER   B 60  ? 0.2207 0.2342 0.2347 0.0071  -0.0387 0.0164  66  SER   C C   
1567 O O   . SER   B 60  ? 0.2318 0.2410 0.2368 0.0074  -0.0426 0.0149  66  SER   C O   
1568 C CB  A SER   B 60  ? 0.2396 0.2551 0.2722 0.0028  -0.0416 0.0209  66  SER   C CB  
1569 C CB  B SER   B 60  ? 0.2188 0.2345 0.2514 0.0028  -0.0414 0.0210  66  SER   C CB  
1570 O OG  A SER   B 60  ? 0.2671 0.2874 0.3036 0.0026  -0.0380 0.0240  66  SER   C OG  
1571 O OG  B SER   B 60  ? 0.2250 0.2377 0.2526 0.0017  -0.0466 0.0220  66  SER   C OG  
1572 N N   . SER   B 61  ? 0.2259 0.2441 0.2405 0.0082  -0.0336 0.0179  67  SER   C N   
1573 C CA  . SER   B 61  ? 0.2361 0.2550 0.2406 0.0099  -0.0316 0.0185  67  SER   C CA  
1574 C C   . SER   B 61  ? 0.2536 0.2693 0.2479 0.0131  -0.0307 0.0133  67  SER   C C   
1575 O O   . SER   B 61  ? 0.2748 0.2902 0.2588 0.0150  -0.0289 0.0130  67  SER   C O   
1576 C CB  . SER   B 61  ? 0.2409 0.2659 0.2506 0.0100  -0.0259 0.0220  67  SER   C CB  
1577 O OG  . SER   B 61  ? 0.2753 0.3034 0.2910 0.0114  -0.0218 0.0196  67  SER   C OG  
1578 N N   . ARG   B 62  ? 0.2428 0.2559 0.2399 0.0140  -0.0315 0.0094  68  ARG   C N   
1579 C CA  . ARG   B 62  ? 0.2527 0.2617 0.2412 0.0171  -0.0314 0.0042  68  ARG   C CA  
1580 C C   . ARG   B 62  ? 0.2612 0.2628 0.2480 0.0163  -0.0375 0.0011  68  ARG   C C   
1581 O O   . ARG   B 62  ? 0.2636 0.2607 0.2443 0.0189  -0.0380 -0.0036 68  ARG   C O   
1582 C CB  . ARG   B 62  ? 0.2687 0.2810 0.2625 0.0196  -0.0265 0.0021  68  ARG   C CB  
1583 C CG  . ARG   B 62  ? 0.3144 0.3339 0.3107 0.0206  -0.0203 0.0046  68  ARG   C CG  
1584 C CD  . ARG   B 62  ? 0.3438 0.3632 0.3289 0.0235  -0.0171 0.0031  68  ARG   C CD  
1585 N NE  . ARG   B 62  ? 0.3696 0.3964 0.3587 0.0241  -0.0107 0.0062  68  ARG   C NE  
1586 C CZ  . ARG   B 62  ? 0.4187 0.4485 0.4069 0.0223  -0.0091 0.0112  68  ARG   C CZ  
1587 N NH1 . ARG   B 62  ? 0.4524 0.4787 0.4356 0.0201  -0.0137 0.0136  68  ARG   C NH1 
1588 N NH2 . ARG   B 62  ? 0.3938 0.4301 0.3867 0.0228  -0.0030 0.0141  68  ARG   C NH2 
1589 N N   . ARG   B 63  ? 0.2462 0.2470 0.2402 0.0130  -0.0415 0.0037  69  ARG   C N   
1590 C CA  . ARG   B 63  ? 0.2566 0.2514 0.2522 0.0115  -0.0469 0.0018  69  ARG   C CA  
1591 C C   . ARG   B 63  ? 0.2595 0.2519 0.2573 0.0136  -0.0453 -0.0016 69  ARG   C C   
1592 O O   . ARG   B 63  ? 0.2746 0.2604 0.2679 0.0144  -0.0486 -0.0052 69  ARG   C O   
1593 C CB  . ARG   B 63  ? 0.2819 0.2706 0.2670 0.0115  -0.0523 -0.0007 69  ARG   C CB  
1594 C CG  . ARG   B 63  ? 0.3282 0.3182 0.3114 0.0092  -0.0557 0.0028  69  ARG   C CG  
1595 C CD  . ARG   B 63  ? 0.3949 0.3858 0.3895 0.0055  -0.0593 0.0063  69  ARG   C CD  
1596 N NE  . ARG   B 63  ? 0.4402 0.4303 0.4315 0.0036  -0.0647 0.0085  69  ARG   C NE  
1597 C CZ  . ARG   B 63  ? 0.4331 0.4279 0.4257 0.0028  -0.0637 0.0132  69  ARG   C CZ  
1598 N NH1 . ARG   B 63  ? 0.4028 0.4033 0.4003 0.0036  -0.0573 0.0159  69  ARG   C NH1 
1599 N NH2 . ARG   B 63  ? 0.4093 0.4030 0.3988 0.0013  -0.0694 0.0152  69  ARG   C NH2 
1600 N N   . LYS   B 64  ? 0.2366 0.2340 0.2408 0.0146  -0.0406 -0.0005 70  LYS   C N   
1601 C CA  . LYS   B 64  ? 0.2491 0.2448 0.2550 0.0170  -0.0392 -0.0034 70  LYS   C CA  
1602 C C   . LYS   B 64  ? 0.2322 0.2321 0.2479 0.0163  -0.0369 -0.0010 70  LYS   C C   
1603 O O   . LYS   B 64  ? 0.2246 0.2303 0.2451 0.0150  -0.0345 0.0018  70  LYS   C O   
1604 C CB  . LYS   B 64  ? 0.3098 0.3075 0.3102 0.0209  -0.0350 -0.0062 70  LYS   C CB  
1605 C CG  . LYS   B 64  ? 0.4332 0.4245 0.4229 0.0233  -0.0368 -0.0107 70  LYS   C CG  
1606 C CD  . LYS   B 64  ? 0.5440 0.5379 0.5298 0.0277  -0.0318 -0.0136 70  LYS   C CD  
1607 C CE  . LYS   B 64  ? 0.6288 0.6159 0.6033 0.0305  -0.0333 -0.0187 70  LYS   C CE  
1608 N NZ  . LYS   B 64  ? 0.6830 0.6675 0.6481 0.0288  -0.0364 -0.0184 70  LYS   C NZ  
1609 N N   . HIS   B 65  ? 0.2238 0.2204 0.2419 0.0172  -0.0378 -0.0024 71  HIS   C N   
1610 C CA  . HIS   B 65  ? 0.2177 0.2175 0.2431 0.0173  -0.0359 -0.0009 71  HIS   C CA  
1611 C C   . HIS   B 65  ? 0.2351 0.2371 0.2596 0.0211  -0.0330 -0.0034 71  HIS   C C   
1612 O O   . HIS   B 65  ? 0.2565 0.2541 0.2762 0.0237  -0.0338 -0.0066 71  HIS   C O   
1613 C CB  . HIS   B 65  ? 0.2160 0.2104 0.2439 0.0162  -0.0387 -0.0002 71  HIS   C CB  
1614 C CG  . HIS   B 65  ? 0.2202 0.2129 0.2508 0.0124  -0.0414 0.0025  71  HIS   C CG  
1615 N ND1 . HIS   B 65  ? 0.2472 0.2436 0.2848 0.0102  -0.0402 0.0059  71  HIS   C ND1 
1616 C CD2 . HIS   B 65  ? 0.2371 0.2253 0.2651 0.0107  -0.0452 0.0020  71  HIS   C CD2 
1617 C CE1 . HIS   B 65  ? 0.2375 0.2318 0.2772 0.0073  -0.0430 0.0077  71  HIS   C CE1 
1618 N NE2 . HIS   B 65  ? 0.2532 0.2426 0.2875 0.0073  -0.0465 0.0055  71  HIS   C NE2 
1619 N N   . TYR   B 66  ? 0.2152 0.2239 0.2449 0.0215  -0.0299 -0.0023 72  TYR   C N   
1620 C CA  . TYR   B 66  ? 0.2176 0.2293 0.2483 0.0250  -0.0274 -0.0046 72  TYR   C CA  
1621 C C   . TYR   B 66  ? 0.1982 0.2116 0.2345 0.0257  -0.0276 -0.0041 72  TYR   C C   
1622 O O   . TYR   B 66  ? 0.1879 0.2043 0.2287 0.0234  -0.0274 -0.0018 72  TYR   C O   
1623 C CB  . TYR   B 66  ? 0.2246 0.2435 0.2574 0.0251  -0.0235 -0.0038 72  TYR   C CB  
1624 C CG  . TYR   B 66  ? 0.2399 0.2582 0.2659 0.0253  -0.0223 -0.0042 72  TYR   C CG  
1625 C CD1 . TYR   B 66  ? 0.2512 0.2682 0.2717 0.0288  -0.0207 -0.0074 72  TYR   C CD1 
1626 C CD2 . TYR   B 66  ? 0.2586 0.2781 0.2837 0.0224  -0.0225 -0.0013 72  TYR   C CD2 
1627 C CE1 . TYR   B 66  ? 0.2617 0.2783 0.2746 0.0293  -0.0192 -0.0078 72  TYR   C CE1 
1628 C CE2 . TYR   B 66  ? 0.2690 0.2881 0.2867 0.0228  -0.0215 -0.0013 72  TYR   C CE2 
1629 C CZ  . TYR   B 66  ? 0.2793 0.2969 0.2902 0.0262  -0.0197 -0.0046 72  TYR   C CZ  
1630 O OH  . TYR   B 66  ? 0.3020 0.3189 0.3040 0.0268  -0.0185 -0.0046 72  TYR   C OH  
1631 N N   . PRO   B 67  ? 0.1966 0.2082 0.2326 0.0290  -0.0281 -0.0062 73  PRO   C N   
1632 C CA  . PRO   B 67  ? 0.1969 0.2109 0.2378 0.0299  -0.0286 -0.0055 73  PRO   C CA  
1633 C C   . PRO   B 67  ? 0.2000 0.2224 0.2467 0.0306  -0.0259 -0.0058 73  PRO   C C   
1634 O O   . PRO   B 67  ? 0.2074 0.2330 0.2544 0.0322  -0.0234 -0.0072 73  PRO   C O   
1635 C CB  . PRO   B 67  ? 0.2270 0.2365 0.2660 0.0336  -0.0301 -0.0075 73  PRO   C CB  
1636 C CG  . PRO   B 67  ? 0.2379 0.2449 0.2724 0.0354  -0.0291 -0.0102 73  PRO   C CG  
1637 C CD  . PRO   B 67  ? 0.2096 0.2174 0.2411 0.0323  -0.0282 -0.0094 73  PRO   C CD  
1638 N N   . VAL   B 68  ? 0.1868 0.2128 0.2382 0.0292  -0.0262 -0.0045 74  VAL   C N   
1639 C CA  . VAL   B 68  ? 0.1881 0.2216 0.2461 0.0293  -0.0242 -0.0049 74  VAL   C CA  
1640 C C   . VAL   B 68  ? 0.1680 0.2036 0.2298 0.0299  -0.0263 -0.0052 74  VAL   C C   
1641 O O   . VAL   B 68  ? 0.1721 0.2036 0.2307 0.0294  -0.0284 -0.0042 74  VAL   C O   
1642 C CB  . VAL   B 68  ? 0.2113 0.2479 0.2717 0.0257  -0.0224 -0.0030 74  VAL   C CB  
1643 C CG1 . VAL   B 68  ? 0.2322 0.2690 0.2897 0.0254  -0.0200 -0.0025 74  VAL   C CG1 
1644 C CG2 . VAL   B 68  ? 0.2127 0.2457 0.2715 0.0230  -0.0240 -0.0011 74  VAL   C CG2 
1645 N N   . SER   B 69  ? 0.1591 0.2013 0.2278 0.0311  -0.0255 -0.0064 75  SER   C N   
1646 C CA  . SER   B 69  ? 0.1640 0.2096 0.2373 0.0312  -0.0276 -0.0071 75  SER   C CA  
1647 C C   . SER   B 69  ? 0.1552 0.2045 0.2332 0.0278  -0.0260 -0.0064 75  SER   C C   
1648 O O   . SER   B 69  ? 0.1583 0.2107 0.2396 0.0266  -0.0230 -0.0057 75  SER   C O   
1649 C CB  . SER   B 69  ? 0.1935 0.2446 0.2735 0.0342  -0.0281 -0.0090 75  SER   C CB  
1650 O OG  . SER   B 69  ? 0.2593 0.3067 0.3357 0.0377  -0.0299 -0.0096 75  SER   C OG  
1651 N N   . PHE   B 70  ? 0.1558 0.2046 0.2340 0.0263  -0.0277 -0.0064 76  PHE   C N   
1652 C CA  . PHE   B 70  ? 0.1613 0.2129 0.2445 0.0233  -0.0263 -0.0061 76  PHE   C CA  
1653 C C   . PHE   B 70  ? 0.1705 0.2249 0.2580 0.0232  -0.0287 -0.0082 76  PHE   C C   
1654 O O   . PHE   B 70  ? 0.1910 0.2437 0.2747 0.0252  -0.0316 -0.0094 76  PHE   C O   
1655 C CB  . PHE   B 70  ? 0.1600 0.2074 0.2390 0.0208  -0.0251 -0.0039 76  PHE   C CB  
1656 C CG  . PHE   B 70  ? 0.1586 0.2008 0.2308 0.0213  -0.0269 -0.0035 76  PHE   C CG  
1657 C CD1 . PHE   B 70  ? 0.1647 0.2021 0.2307 0.0225  -0.0274 -0.0024 76  PHE   C CD1 
1658 C CD2 . PHE   B 70  ? 0.1564 0.1982 0.2285 0.0205  -0.0276 -0.0041 76  PHE   C CD2 
1659 C CE1 . PHE   B 70  ? 0.1732 0.2059 0.2337 0.0227  -0.0287 -0.0013 76  PHE   C CE1 
1660 C CE2 . PHE   B 70  ? 0.1616 0.1989 0.2271 0.0210  -0.0284 -0.0032 76  PHE   C CE2 
1661 C CZ  . PHE   B 70  ? 0.1661 0.1991 0.2263 0.0220  -0.0288 -0.0014 76  PHE   C CZ  
1662 N N   . SER   B 71  ? 0.1527 0.2113 0.2483 0.0211  -0.0277 -0.0088 77  SER   C N   
1663 C CA  . SER   B 71  ? 0.1569 0.2184 0.2578 0.0209  -0.0304 -0.0115 77  SER   C CA  
1664 C C   . SER   B 71  ? 0.1757 0.2331 0.2713 0.0201  -0.0318 -0.0125 77  SER   C C   
1665 O O   . SER   B 71  ? 0.1916 0.2447 0.2810 0.0194  -0.0301 -0.0105 77  SER   C O   
1666 C CB  . SER   B 71  ? 0.1603 0.2270 0.2726 0.0186  -0.0288 -0.0117 77  SER   C CB  
1667 O OG  . SER   B 71  ? 0.1853 0.2502 0.2986 0.0158  -0.0263 -0.0099 77  SER   C OG  
1668 N N   . LYS   B 72  ? 0.1685 0.2275 0.2667 0.0203  -0.0348 -0.0157 78  LYS   C N   
1669 C CA  . LYS   B 72  ? 0.1842 0.2394 0.2765 0.0200  -0.0357 -0.0172 78  LYS   C CA  
1670 C C   . LYS   B 72  ? 0.1871 0.2420 0.2848 0.0170  -0.0331 -0.0170 78  LYS   C C   
1671 O O   . LYS   B 72  ? 0.1940 0.2525 0.3015 0.0152  -0.0322 -0.0170 78  LYS   C O   
1672 C CB  . LYS   B 72  ? 0.2349 0.2916 0.3272 0.0214  -0.0404 -0.0212 78  LYS   C CB  
1673 C CG  . LYS   B 72  ? 0.3015 0.3581 0.3881 0.0247  -0.0438 -0.0212 78  LYS   C CG  
1674 C CD  . LYS   B 72  ? 0.4229 0.4795 0.5060 0.0262  -0.0488 -0.0249 78  LYS   C CD  
1675 C CE  . LYS   B 72  ? 0.5164 0.5730 0.5943 0.0296  -0.0527 -0.0245 78  LYS   C CE  
1676 N NZ  . LYS   B 72  ? 0.5693 0.6243 0.6397 0.0314  -0.0575 -0.0274 78  LYS   C NZ  
1677 N N   . PRO   B 73  ? 0.1851 0.2359 0.2774 0.0165  -0.0316 -0.0167 79  PRO   C N   
1678 C CA  . PRO   B 73  ? 0.1838 0.2341 0.2821 0.0140  -0.0291 -0.0163 79  PRO   C CA  
1679 C C   . PRO   B 73  ? 0.1910 0.2439 0.2982 0.0129  -0.0310 -0.0200 79  PRO   C C   
1680 O O   . PRO   B 73  ? 0.2011 0.2538 0.3062 0.0141  -0.0342 -0.0241 79  PRO   C O   
1681 C CB  . PRO   B 73  ? 0.2052 0.2512 0.2962 0.0145  -0.0277 -0.0163 79  PRO   C CB  
1682 C CG  . PRO   B 73  ? 0.2170 0.2611 0.2978 0.0170  -0.0292 -0.0161 79  PRO   C CG  
1683 C CD  . PRO   B 73  ? 0.1878 0.2345 0.2692 0.0183  -0.0318 -0.0161 79  PRO   C CD  
1684 N N   . SER   B 74  ? 0.1851 0.2403 0.3024 0.0105  -0.0293 -0.0185 80  SER   C N   
1685 C CA  . SER   B 74  ? 0.1988 0.2565 0.3268 0.0090  -0.0311 -0.0216 80  SER   C CA  
1686 C C   . SER   B 74  ? 0.1919 0.2494 0.3293 0.0061  -0.0282 -0.0193 80  SER   C C   
1687 O O   . SER   B 74  ? 0.1792 0.2352 0.3145 0.0055  -0.0251 -0.0151 80  SER   C O   
1688 C CB  . SER   B 74  ? 0.2492 0.3122 0.3832 0.0092  -0.0330 -0.0219 80  SER   C CB  
1689 O OG  . SER   B 74  ? 0.3412 0.4049 0.4677 0.0119  -0.0343 -0.0214 80  SER   C OG  
1690 N N   . LEU   B 75  ? 0.1929 0.2520 0.3413 0.0043  -0.0297 -0.0218 81  LEU   C N   
1691 C CA  . LEU   B 75  ? 0.2125 0.2716 0.3715 0.0015  -0.0273 -0.0194 81  LEU   C CA  
1692 C C   . LEU   B 75  ? 0.2096 0.2738 0.3760 0.0002  -0.0257 -0.0154 81  LEU   C C   
1693 O O   . LEU   B 75  ? 0.2083 0.2767 0.3815 0.0000  -0.0278 -0.0175 81  LEU   C O   
1694 C CB  . LEU   B 75  ? 0.2307 0.2884 0.3984 0.0002  -0.0300 -0.0243 81  LEU   C CB  
1695 C CG  . LEU   B 75  ? 0.2620 0.3178 0.4407 -0.0025 -0.0279 -0.0224 81  LEU   C CG  
1696 C CD1 . LEU   B 75  ? 0.2659 0.3171 0.4391 -0.0019 -0.0251 -0.0202 81  LEU   C CD1 
1697 C CD2 . LEU   B 75  ? 0.2820 0.3366 0.4704 -0.0038 -0.0313 -0.0281 81  LEU   C CD2 
1698 N N   . ILE   B 76  ? 0.2014 0.2657 0.3659 -0.0003 -0.0219 -0.0098 82  ILE   C N   
1699 C CA  . ILE   B 76  ? 0.2021 0.2710 0.3707 -0.0010 -0.0194 -0.0058 82  ILE   C CA  
1700 C C   . ILE   B 76  ? 0.2002 0.2690 0.3767 -0.0036 -0.0162 -0.0009 82  ILE   C C   
1701 O O   . ILE   B 76  ? 0.1920 0.2568 0.3652 -0.0041 -0.0150 0.0014  82  ILE   C O   
1702 C CB  . ILE   B 76  ? 0.2221 0.2907 0.3787 0.0013  -0.0179 -0.0034 82  ILE   C CB  
1703 C CG1 . ILE   B 76  ? 0.2491 0.3174 0.3976 0.0041  -0.0210 -0.0072 82  ILE   C CG1 
1704 C CG2 . ILE   B 76  ? 0.2352 0.3079 0.3941 0.0010  -0.0145 0.0009  82  ILE   C CG2 
1705 C CD1 . ILE   B 76  ? 0.2788 0.3520 0.4322 0.0051  -0.0226 -0.0093 82  ILE   C CD1 
1706 N N   . PHE   B 77  ? 0.1942 0.2677 0.3814 -0.0053 -0.0145 0.0013  83  PHE   C N   
1707 C CA  . PHE   B 77  ? 0.2105 0.2841 0.4046 -0.0078 -0.0110 0.0069  83  PHE   C CA  
1708 C C   . PHE   B 77  ? 0.2224 0.2963 0.4063 -0.0066 -0.0076 0.0122  83  PHE   C C   
1709 O O   . PHE   B 77  ? 0.2370 0.3143 0.4161 -0.0049 -0.0065 0.0123  83  PHE   C O   
1710 C CB  . PHE   B 77  ? 0.2078 0.2867 0.4169 -0.0101 -0.0099 0.0081  83  PHE   C CB  
1711 C CG  . PHE   B 77  ? 0.2180 0.2961 0.4350 -0.0129 -0.0064 0.0143  83  PHE   C CG  
1712 C CD1 . PHE   B 77  ? 0.2365 0.3099 0.4603 -0.0148 -0.0078 0.0139  83  PHE   C CD1 
1713 C CD2 . PHE   B 77  ? 0.2249 0.3065 0.4416 -0.0133 -0.0017 0.0207  83  PHE   C CD2 
1714 C CE1 . PHE   B 77  ? 0.2476 0.3198 0.4786 -0.0172 -0.0048 0.0202  83  PHE   C CE1 
1715 C CE2 . PHE   B 77  ? 0.2341 0.3148 0.4570 -0.0157 0.0015  0.0270  83  PHE   C CE2 
1716 C CZ  . PHE   B 77  ? 0.2418 0.3178 0.4723 -0.0177 -0.0002 0.0270  83  PHE   C CZ  
1717 N N   . VAL   B 78  ? 0.2002 0.2703 0.3810 -0.0074 -0.0063 0.0162  84  VAL   C N   
1718 C CA  . VAL   B 78  ? 0.1987 0.2681 0.3692 -0.0065 -0.0040 0.0209  84  VAL   C CA  
1719 C C   . VAL   B 78  ? 0.1914 0.2618 0.3676 -0.0086 -0.0006 0.0275  84  VAL   C C   
1720 O O   . VAL   B 78  ? 0.1897 0.2576 0.3737 -0.0105 -0.0010 0.0291  84  VAL   C O   
1721 C CB  . VAL   B 78  ? 0.2104 0.2745 0.3723 -0.0056 -0.0060 0.0204  84  VAL   C CB  
1722 C CG1 . VAL   B 78  ? 0.2255 0.2885 0.3770 -0.0048 -0.0046 0.0249  84  VAL   C CG1 
1723 C CG2 . VAL   B 78  ? 0.2142 0.2767 0.3702 -0.0036 -0.0090 0.0145  84  VAL   C CG2 
1724 N N   . GLU   B 79  ? 0.1847 0.2583 0.3562 -0.0080 0.0029  0.0316  85  GLU   C N   
1725 C CA  . GLU   B 79  ? 0.1873 0.2617 0.3619 -0.0097 0.0066  0.0388  85  GLU   C CA  
1726 C C   . GLU   B 79  ? 0.1867 0.2558 0.3552 -0.0101 0.0054  0.0426  85  GLU   C C   
1727 O O   . GLU   B 79  ? 0.1786 0.2442 0.3383 -0.0086 0.0025  0.0401  85  GLU   C O   
1728 C CB  . GLU   B 79  ? 0.2314 0.3099 0.3991 -0.0083 0.0108  0.0417  85  GLU   C CB  
1729 C CG  . GLU   B 79  ? 0.2917 0.3764 0.4676 -0.0080 0.0127  0.0391  85  GLU   C CG  
1730 C CD  . GLU   B 79  ? 0.4096 0.4973 0.6030 -0.0111 0.0141  0.0409  85  GLU   C CD  
1731 O OE1 . GLU   B 79  ? 0.4387 0.5263 0.6361 -0.0131 0.0173  0.0475  85  GLU   C OE1 
1732 O OE2 . GLU   B 79  ? 0.4429 0.5326 0.6460 -0.0116 0.0115  0.0359  85  GLU   C OE2 
1733 N N   . ALA   B 80  ? 0.1955 0.2641 0.3688 -0.0119 0.0077  0.0492  86  ALA   C N   
1734 C CA  . ALA   B 80  ? 0.2135 0.2775 0.3822 -0.0122 0.0062  0.0536  86  ALA   C CA  
1735 C C   . ALA   B 80  ? 0.2391 0.3019 0.3912 -0.0099 0.0053  0.0543  86  ALA   C C   
1736 O O   . ALA   B 80  ? 0.2383 0.3039 0.3824 -0.0085 0.0077  0.0542  86  ALA   C O   
1737 C CB  . ALA   B 80  ? 0.2153 0.2796 0.3910 -0.0143 0.0092  0.0615  86  ALA   C CB  
1738 N N   . SER   B 81  ? 0.2525 0.3111 0.4004 -0.0095 0.0018  0.0539  87  SER   C N   
1739 C CA  . SER   B 81  ? 0.2752 0.3319 0.4088 -0.0078 -0.0001 0.0545  87  SER   C CA  
1740 C C   . SER   B 81  ? 0.2904 0.3439 0.4234 -0.0086 -0.0019 0.0606  87  SER   C C   
1741 O O   . SER   B 81  ? 0.2949 0.3476 0.4386 -0.0102 -0.0014 0.0639  87  SER   C O   
1742 C CB  . SER   B 81  ? 0.2933 0.3481 0.4232 -0.0064 -0.0035 0.0480  87  SER   C CB  
1743 O OG  . SER   B 81  ? 0.3168 0.3687 0.4535 -0.0072 -0.0060 0.0474  87  SER   C OG  
1744 N N   . GLU   B 82  ? 0.3023 0.3537 0.4234 -0.0074 -0.0045 0.0619  88  GLU   C N   
1745 C CA  . GLU   B 82  ? 0.3105 0.3591 0.4314 -0.0081 -0.0071 0.0677  88  GLU   C CA  
1746 C C   . GLU   B 82  ? 0.3060 0.3522 0.4375 -0.0087 -0.0100 0.0662  88  GLU   C C   
1747 O O   . GLU   B 82  ? 0.3093 0.3535 0.4454 -0.0093 -0.0116 0.0712  88  GLU   C O   
1748 C CB  . GLU   B 82  ? 0.3602 0.4071 0.4661 -0.0068 -0.0099 0.0693  88  GLU   C CB  
1749 C CG  . GLU   B 82  ? 0.4400 0.4855 0.5398 -0.0056 -0.0133 0.0634  88  GLU   C CG  
1750 C CD  . GLU   B 82  ? 0.5311 0.5746 0.6170 -0.0046 -0.0167 0.0646  88  GLU   C CD  
1751 O OE1 . GLU   B 82  ? 0.5372 0.5813 0.6130 -0.0039 -0.0148 0.0670  88  GLU   C OE1 
1752 O OE2 . GLU   B 82  ? 0.5742 0.6154 0.6592 -0.0046 -0.0212 0.0629  88  GLU   C OE2 
1753 N N   . TYR   B 83  ? 0.2864 0.3328 0.4221 -0.0083 -0.0104 0.0595  89  TYR   C N   
1754 C CA  . TYR   B 83  ? 0.2742 0.3183 0.4184 -0.0083 -0.0125 0.0573  89  TYR   C CA  
1755 C C   . TYR   B 83  ? 0.2579 0.3022 0.4147 -0.0091 -0.0107 0.0538  89  TYR   C C   
1756 O O   . TYR   B 83  ? 0.2649 0.3071 0.4300 -0.0091 -0.0118 0.0530  89  TYR   C O   
1757 C CB  . TYR   B 83  ? 0.2712 0.3145 0.4088 -0.0071 -0.0152 0.0529  89  TYR   C CB  
1758 C CG  . TYR   B 83  ? 0.2799 0.3247 0.4092 -0.0061 -0.0142 0.0480  89  TYR   C CG  
1759 C CD1 . TYR   B 83  ? 0.2900 0.3353 0.4076 -0.0054 -0.0144 0.0490  89  TYR   C CD1 
1760 C CD2 . TYR   B 83  ? 0.2876 0.3331 0.4205 -0.0056 -0.0132 0.0422  89  TYR   C CD2 
1761 C CE1 . TYR   B 83  ? 0.2937 0.3401 0.4047 -0.0042 -0.0135 0.0445  89  TYR   C CE1 
1762 C CE2 . TYR   B 83  ? 0.2988 0.3456 0.4247 -0.0045 -0.0127 0.0381  89  TYR   C CE2 
1763 C CZ  . TYR   B 83  ? 0.3111 0.3583 0.4266 -0.0037 -0.0127 0.0393  89  TYR   C CZ  
1764 O OH  . TYR   B 83  ? 0.3169 0.3651 0.4263 -0.0023 -0.0122 0.0351  89  TYR   C OH  
1765 N N   . TYR   B 84  ? 0.2237 0.2705 0.3824 -0.0096 -0.0080 0.0516  90  TYR   C N   
1766 C CA  . TYR   B 84  ? 0.1962 0.2430 0.3671 -0.0105 -0.0070 0.0481  90  TYR   C CA  
1767 C C   . TYR   B 84  ? 0.1945 0.2440 0.3710 -0.0121 -0.0040 0.0508  90  TYR   C C   
1768 O O   . TYR   B 84  ? 0.1924 0.2448 0.3615 -0.0118 -0.0022 0.0526  90  TYR   C O   
1769 C CB  . TYR   B 84  ? 0.1821 0.2297 0.3508 -0.0093 -0.0077 0.0401  90  TYR   C CB  
1770 C CG  . TYR   B 84  ? 0.1752 0.2204 0.3410 -0.0079 -0.0098 0.0366  90  TYR   C CG  
1771 C CD1 . TYR   B 84  ? 0.1811 0.2235 0.3553 -0.0079 -0.0105 0.0363  90  TYR   C CD1 
1772 C CD2 . TYR   B 84  ? 0.1799 0.2256 0.3357 -0.0064 -0.0108 0.0335  90  TYR   C CD2 
1773 C CE1 . TYR   B 84  ? 0.1851 0.2259 0.3574 -0.0065 -0.0116 0.0332  90  TYR   C CE1 
1774 C CE2 . TYR   B 84  ? 0.1795 0.2233 0.3332 -0.0053 -0.0122 0.0311  90  TYR   C CE2 
1775 C CZ  . TYR   B 84  ? 0.1925 0.2341 0.3546 -0.0053 -0.0123 0.0307  90  TYR   C CZ  
1776 O OH  . TYR   B 84  ? 0.1797 0.2199 0.3402 -0.0040 -0.0129 0.0284  90  TYR   C OH  
1777 N N   . PRO   B 85  ? 0.1941 0.2428 0.3839 -0.0137 -0.0034 0.0504  91  PRO   C N   
1778 C CA  . PRO   B 85  ? 0.1974 0.2492 0.3943 -0.0155 -0.0005 0.0524  91  PRO   C CA  
1779 C C   . PRO   B 85  ? 0.1950 0.2504 0.3910 -0.0149 -0.0004 0.0457  91  PRO   C C   
1780 O O   . PRO   B 85  ? 0.1875 0.2424 0.3769 -0.0131 -0.0026 0.0399  91  PRO   C O   
1781 C CB  . PRO   B 85  ? 0.2090 0.2578 0.4213 -0.0174 -0.0008 0.0531  91  PRO   C CB  
1782 C CG  . PRO   B 85  ? 0.2148 0.2600 0.4277 -0.0159 -0.0039 0.0468  91  PRO   C CG  
1783 C CD  . PRO   B 85  ? 0.1949 0.2397 0.3945 -0.0138 -0.0051 0.0475  91  PRO   C CD  
1784 N N   . ALA   B 86  ? 0.1893 0.2487 0.3927 -0.0164 0.0021  0.0467  92  ALA   C N   
1785 C CA  . ALA   B 86  ? 0.1965 0.2597 0.4016 -0.0159 0.0018  0.0406  92  ALA   C CA  
1786 C C   . ALA   B 86  ? 0.2040 0.2644 0.4165 -0.0162 -0.0018 0.0336  92  ALA   C C   
1787 O O   . ALA   B 86  ? 0.2076 0.2650 0.4309 -0.0180 -0.0023 0.0345  92  ALA   C O   
1788 C CB  . ALA   B 86  ? 0.1882 0.2564 0.4030 -0.0179 0.0052  0.0437  92  ALA   C CB  
1789 N N   . ARG   B 87  ? 0.2005 0.2610 0.4061 -0.0141 -0.0043 0.0269  93  ARG   C N   
1790 C CA  . ARG   B 87  ? 0.2051 0.2626 0.4150 -0.0138 -0.0075 0.0201  93  ARG   C CA  
1791 C C   . ARG   B 87  ? 0.2109 0.2700 0.4125 -0.0116 -0.0098 0.0137  93  ARG   C C   
1792 O O   . ARG   B 87  ? 0.2132 0.2751 0.4059 -0.0101 -0.0089 0.0147  93  ARG   C O   
1793 C CB  . ARG   B 87  ? 0.2158 0.2678 0.4230 -0.0131 -0.0083 0.0208  93  ARG   C CB  
1794 C CG  . ARG   B 87  ? 0.2375 0.2891 0.4304 -0.0108 -0.0084 0.0217  93  ARG   C CG  
1795 C CD  . ARG   B 87  ? 0.2503 0.2975 0.4410 -0.0097 -0.0094 0.0212  93  ARG   C CD  
1796 N NE  . ARG   B 87  ? 0.2623 0.3095 0.4405 -0.0077 -0.0100 0.0205  93  ARG   C NE  
1797 C CZ  . ARG   B 87  ? 0.2802 0.3247 0.4550 -0.0063 -0.0109 0.0183  93  ARG   C CZ  
1798 N NH1 . ARG   B 87  ? 0.2590 0.3005 0.4413 -0.0063 -0.0111 0.0162  93  ARG   C NH1 
1799 N NH2 . ARG   B 87  ? 0.2640 0.3087 0.4284 -0.0048 -0.0114 0.0179  93  ARG   C NH2 
1800 N N   . TYR   B 88  ? 0.2082 0.2649 0.4117 -0.0110 -0.0128 0.0071  94  TYR   C N   
1801 C CA  . TYR   B 88  ? 0.2242 0.2816 0.4187 -0.0086 -0.0152 0.0015  94  TYR   C CA  
1802 C C   . TYR   B 88  ? 0.2079 0.2616 0.3910 -0.0065 -0.0152 0.0011  94  TYR   C C   
1803 O O   . TYR   B 88  ? 0.2137 0.2634 0.3990 -0.0067 -0.0150 0.0009  94  TYR   C O   
1804 C CB  . TYR   B 88  ? 0.2476 0.3042 0.4479 -0.0088 -0.0187 -0.0057 94  TYR   C CB  
1805 C CG  . TYR   B 88  ? 0.2809 0.3423 0.4921 -0.0106 -0.0196 -0.0063 94  TYR   C CG  
1806 C CD1 . TYR   B 88  ? 0.3045 0.3706 0.5124 -0.0093 -0.0208 -0.0079 94  TYR   C CD1 
1807 C CD2 . TYR   B 88  ? 0.3019 0.3631 0.5276 -0.0136 -0.0190 -0.0045 94  TYR   C CD2 
1808 C CE1 . TYR   B 88  ? 0.3179 0.3892 0.5374 -0.0110 -0.0214 -0.0081 94  TYR   C CE1 
1809 C CE2 . TYR   B 88  ? 0.3152 0.3813 0.5525 -0.0156 -0.0195 -0.0045 94  TYR   C CE2 
1810 C CZ  . TYR   B 88  ? 0.3325 0.4040 0.5670 -0.0143 -0.0207 -0.0064 94  TYR   C CZ  
1811 O OH  . TYR   B 88  ? 0.3610 0.4378 0.6091 -0.0164 -0.0211 -0.0061 94  TYR   C OH  
1812 N N   . GLN   B 89  ? 0.1849 0.2398 0.3569 -0.0046 -0.0153 0.0010  95  GLN   C N   
1813 C CA  . GLN   B 89  ? 0.1729 0.2246 0.3349 -0.0028 -0.0155 0.0005  95  GLN   C CA  
1814 C C   . GLN   B 89  ? 0.1725 0.2242 0.3277 -0.0007 -0.0178 -0.0052 95  GLN   C C   
1815 O O   . GLN   B 89  ? 0.1696 0.2245 0.3236 -0.0001 -0.0191 -0.0067 95  GLN   C O   
1816 C CB  . GLN   B 89  ? 0.1804 0.2328 0.3347 -0.0023 -0.0139 0.0055  95  GLN   C CB  
1817 C CG  . GLN   B 89  ? 0.1952 0.2446 0.3402 -0.0008 -0.0142 0.0054  95  GLN   C CG  
1818 C CD  . GLN   B 89  ? 0.2026 0.2517 0.3427 -0.0010 -0.0133 0.0106  95  GLN   C CD  
1819 O OE1 . GLN   B 89  ? 0.2181 0.2676 0.3623 -0.0024 -0.0122 0.0150  95  GLN   C OE1 
1820 N NE2 . GLN   B 89  ? 0.1988 0.2466 0.3297 0.0004  -0.0140 0.0103  95  GLN   C NE2 
1821 N N   . SER   B 90  ? 0.1593 0.2075 0.3105 0.0006  -0.0183 -0.0083 96  SER   C N   
1822 C CA  . SER   B 90  ? 0.1683 0.2159 0.3118 0.0027  -0.0205 -0.0134 96  SER   C CA  
1823 C C   . SER   B 90  ? 0.1630 0.2096 0.2946 0.0046  -0.0199 -0.0117 96  SER   C C   
1824 O O   . SER   B 90  ? 0.1539 0.1998 0.2839 0.0041  -0.0179 -0.0074 96  SER   C O   
1825 C CB  . SER   B 90  ? 0.1933 0.2375 0.3381 0.0033  -0.0212 -0.0184 96  SER   C CB  
1826 O OG  . SER   B 90  ? 0.2262 0.2675 0.3693 0.0038  -0.0186 -0.0164 96  SER   C OG  
1827 N N   . HIS   B 91  ? 0.1576 0.2043 0.2816 0.0066  -0.0219 -0.0149 97  HIS   C N   
1828 C CA  . HIS   B 91  ? 0.1670 0.2125 0.2803 0.0084  -0.0216 -0.0135 97  HIS   C CA  
1829 C C   . HIS   B 91  ? 0.1533 0.2003 0.2653 0.0079  -0.0207 -0.0088 97  HIS   C C   
1830 O O   . HIS   B 91  ? 0.1644 0.2094 0.2704 0.0083  -0.0197 -0.0062 97  HIS   C O   
1831 C CB  . HIS   B 91  ? 0.1877 0.2296 0.2965 0.0091  -0.0195 -0.0132 97  HIS   C CB  
1832 C CG  . HIS   B 91  ? 0.2339 0.2740 0.3419 0.0102  -0.0200 -0.0183 97  HIS   C CG  
1833 N ND1 . HIS   B 91  ? 0.2606 0.2993 0.3586 0.0125  -0.0210 -0.0211 97  HIS   C ND1 
1834 C CD2 . HIS   B 91  ? 0.2435 0.2826 0.3587 0.0094  -0.0196 -0.0211 97  HIS   C CD2 
1835 C CE1 . HIS   B 91  ? 0.2582 0.2952 0.3568 0.0132  -0.0211 -0.0257 97  HIS   C CE1 
1836 N NE2 . HIS   B 91  ? 0.2610 0.2979 0.3701 0.0114  -0.0203 -0.0261 97  HIS   C NE2 
1837 N N   . LEU   B 92  ? 0.1370 0.1874 0.2551 0.0069  -0.0210 -0.0081 98  LEU   C N   
1838 C CA  . LEU   B 92  ? 0.1484 0.2003 0.2650 0.0068  -0.0199 -0.0044 98  LEU   C CA  
1839 C C   . LEU   B 92  ? 0.1507 0.2046 0.2633 0.0088  -0.0215 -0.0059 98  LEU   C C   
1840 O O   . LEU   B 92  ? 0.1563 0.2125 0.2722 0.0094  -0.0236 -0.0092 98  LEU   C O   
1841 C CB  . LEU   B 92  ? 0.1467 0.2013 0.2727 0.0046  -0.0182 -0.0018 98  LEU   C CB  
1842 C CG  . LEU   B 92  ? 0.1706 0.2266 0.2944 0.0044  -0.0163 0.0024  98  LEU   C CG  
1843 C CD1 . LEU   B 92  ? 0.1907 0.2430 0.3077 0.0043  -0.0158 0.0053  98  LEU   C CD1 
1844 C CD2 . LEU   B 92  ? 0.1531 0.2121 0.2861 0.0023  -0.0143 0.0052  98  LEU   C CD2 
1845 N N   . MET   B 93  ? 0.1359 0.1889 0.2420 0.0098  -0.0209 -0.0036 99  MET   C N   
1846 C CA  . MET   B 93  ? 0.1411 0.1955 0.2438 0.0121  -0.0223 -0.0047 99  MET   C CA  
1847 C C   . MET   B 93  ? 0.1477 0.2039 0.2510 0.0120  -0.0201 -0.0020 99  MET   C C   
1848 O O   . MET   B 93  ? 0.1558 0.2098 0.2560 0.0109  -0.0186 0.0008  99  MET   C O   
1849 C CB  . MET   B 93  ? 0.1599 0.2100 0.2528 0.0139  -0.0236 -0.0048 99  MET   C CB  
1850 C CG  . MET   B 93  ? 0.1819 0.2299 0.2722 0.0142  -0.0249 -0.0069 99  MET   C CG  
1851 S SD  . MET   B 93  ? 0.2094 0.2522 0.2889 0.0157  -0.0251 -0.0055 99  MET   C SD  
1852 C CE  . MET   B 93  ? 0.2087 0.2492 0.2885 0.0135  -0.0226 -0.0015 99  MET   C CE  
1853 N N   . LEU   B 94  ? 0.1303 0.1907 0.2374 0.0131  -0.0200 -0.0029 100 LEU   C N   
1854 C CA  . LEU   B 94  ? 0.1467 0.2091 0.2537 0.0135  -0.0172 -0.0007 100 LEU   C CA  
1855 C C   . LEU   B 94  ? 0.1507 0.2121 0.2513 0.0165  -0.0178 -0.0017 100 LEU   C C   
1856 O O   . LEU   B 94  ? 0.1589 0.2205 0.2591 0.0185  -0.0203 -0.0041 100 LEU   C O   
1857 C CB  . LEU   B 94  ? 0.1499 0.2186 0.2676 0.0126  -0.0153 -0.0004 100 LEU   C CB  
1858 C CG  . LEU   B 94  ? 0.1719 0.2420 0.2982 0.0096  -0.0144 0.0008  100 LEU   C CG  
1859 C CD1 . LEU   B 94  ? 0.1845 0.2611 0.3222 0.0088  -0.0123 0.0015  100 LEU   C CD1 
1860 C CD2 . LEU   B 94  ? 0.1898 0.2566 0.3124 0.0078  -0.0125 0.0046  100 LEU   C CD2 
1861 N N   . ALA   B 95  ? 0.1424 0.2026 0.2381 0.0170  -0.0156 0.0002  101 ALA   C N   
1862 C CA  . ALA   B 95  ? 0.1582 0.2174 0.2486 0.0200  -0.0156 -0.0009 101 ALA   C CA  
1863 C C   . ALA   B 95  ? 0.1559 0.2183 0.2471 0.0205  -0.0116 0.0005  101 ALA   C C   
1864 O O   . ALA   B 95  ? 0.1629 0.2266 0.2560 0.0182  -0.0094 0.0031  101 ALA   C O   
1865 C CB  . ALA   B 95  ? 0.1616 0.2138 0.2422 0.0205  -0.0174 -0.0007 101 ALA   C CB  
1866 N N   . VAL   B 96  ? 0.1481 0.2116 0.2376 0.0236  -0.0106 -0.0010 102 VAL   C N   
1867 C CA  . VAL   B 96  ? 0.1625 0.2285 0.2507 0.0246  -0.0063 0.0001  102 VAL   C CA  
1868 C C   . VAL   B 96  ? 0.1775 0.2365 0.2534 0.0248  -0.0068 0.0005  102 VAL   C C   
1869 O O   . VAL   B 96  ? 0.1800 0.2340 0.2498 0.0267  -0.0094 -0.0015 102 VAL   C O   
1870 C CB  . VAL   B 96  ? 0.1752 0.2453 0.2671 0.0283  -0.0047 -0.0022 102 VAL   C CB  
1871 C CG1 . VAL   B 96  ? 0.1901 0.2620 0.2785 0.0299  0.0004  -0.0013 102 VAL   C CG1 
1872 C CG2 . VAL   B 96  ? 0.1745 0.2517 0.2797 0.0277  -0.0049 -0.0026 102 VAL   C CG2 
1873 N N   . GLY   B 97  ? 0.1910 0.2497 0.2640 0.0226  -0.0050 0.0034  103 GLY   C N   
1874 C CA  . GLY   B 97  ? 0.2053 0.2577 0.2673 0.0224  -0.0064 0.0039  103 GLY   C CA  
1875 C C   . GLY   B 97  ? 0.2136 0.2662 0.2733 0.0199  -0.0050 0.0077  103 GLY   C C   
1876 O O   . GLY   B 97  ? 0.2196 0.2766 0.2869 0.0179  -0.0028 0.0104  103 GLY   C O   
1877 N N   . HIS   B 98  ? 0.2035 0.2508 0.2530 0.0199  -0.0065 0.0080  104 HIS   C N   
1878 C CA  . HIS   B 98  ? 0.2140 0.2608 0.2595 0.0179  -0.0059 0.0118  104 HIS   C CA  
1879 C C   . HIS   B 98  ? 0.2116 0.2562 0.2605 0.0146  -0.0094 0.0142  104 HIS   C C   
1880 O O   . HIS   B 98  ? 0.2112 0.2517 0.2591 0.0142  -0.0131 0.0125  104 HIS   C O   
1881 C CB  . HIS   B 98  ? 0.2432 0.2852 0.2755 0.0195  -0.0067 0.0106  104 HIS   C CB  
1882 C CG  . HIS   B 98  ? 0.3058 0.3476 0.3327 0.0179  -0.0062 0.0147  104 HIS   C CG  
1883 N ND1 . HIS   B 98  ? 0.3368 0.3839 0.3657 0.0178  -0.0012 0.0181  104 HIS   C ND1 
1884 C CD2 . HIS   B 98  ? 0.3364 0.3736 0.3571 0.0162  -0.0103 0.0162  104 HIS   C CD2 
1885 C CE1 . HIS   B 98  ? 0.3571 0.4022 0.3798 0.0162  -0.0024 0.0218  104 HIS   C CE1 
1886 N NE2 . HIS   B 98  ? 0.3576 0.3969 0.3751 0.0153  -0.0082 0.0206  104 HIS   C NE2 
1887 N N   . SER   B 99  ? 0.2139 0.2610 0.2668 0.0124  -0.0079 0.0183  105 SER   C N   
1888 C CA  . SER   B 99  ? 0.2193 0.2649 0.2766 0.0095  -0.0107 0.0209  105 SER   C CA  
1889 C C   . SER   B 99  ? 0.2359 0.2828 0.2935 0.0078  -0.0092 0.0261  105 SER   C C   
1890 O O   . SER   B 99  ? 0.2476 0.2990 0.3118 0.0073  -0.0056 0.0282  105 SER   C O   
1891 C CB  . SER   B 99  ? 0.2221 0.2699 0.2903 0.0086  -0.0106 0.0198  105 SER   C CB  
1892 O OG  . SER   B 99  ? 0.2675 0.3143 0.3411 0.0062  -0.0124 0.0219  105 SER   C OG  
1893 N N   . GLU   B 100 ? 0.2282 0.2714 0.2792 0.0070  -0.0124 0.0282  106 GLU   C N   
1894 C CA  . GLU   B 100 ? 0.2321 0.2756 0.2823 0.0054  -0.0123 0.0336  106 GLU   C CA  
1895 C C   . GLU   B 100 ? 0.2216 0.2643 0.2812 0.0030  -0.0150 0.0356  106 GLU   C C   
1896 O O   . GLU   B 100 ? 0.2127 0.2535 0.2753 0.0028  -0.0176 0.0327  106 GLU   C O   
1897 C CB  . GLU   B 100 ? 0.2715 0.3109 0.3086 0.0061  -0.0155 0.0342  106 GLU   C CB  
1898 C CG  . GLU   B 100 ? 0.3777 0.4162 0.4030 0.0088  -0.0138 0.0313  106 GLU   C CG  
1899 C CD  . GLU   B 100 ? 0.4498 0.4914 0.4701 0.0099  -0.0088 0.0345  106 GLU   C CD  
1900 O OE1 . GLU   B 100 ? 0.4622 0.5031 0.4721 0.0125  -0.0069 0.0320  106 GLU   C OE1 
1901 O OE2 . GLU   B 100 ? 0.4664 0.5111 0.4933 0.0082  -0.0066 0.0396  106 GLU   C OE2 
1902 N N   . PRO   B 101 ? 0.2196 0.2632 0.2833 0.0014  -0.0147 0.0408  107 PRO   C N   
1903 C CA  . PRO   B 101 ? 0.2138 0.2564 0.2866 -0.0004 -0.0174 0.0424  107 PRO   C CA  
1904 C C   . PRO   B 101 ? 0.2150 0.2541 0.2851 -0.0006 -0.0222 0.0406  107 PRO   C C   
1905 O O   . PRO   B 101 ? 0.2249 0.2636 0.3026 -0.0012 -0.0231 0.0390  107 PRO   C O   
1906 C CB  . PRO   B 101 ? 0.2337 0.2767 0.3078 -0.0015 -0.0171 0.0488  107 PRO   C CB  
1907 C CG  . PRO   B 101 ? 0.2435 0.2895 0.3147 -0.0008 -0.0122 0.0504  107 PRO   C CG  
1908 C CD  . PRO   B 101 ? 0.2266 0.2723 0.2877 0.0013  -0.0115 0.0456  107 PRO   C CD  
1909 N N   . GLY   B 102 ? 0.1979 0.2343 0.2572 0.0000  -0.0252 0.0407  108 GLY   C N   
1910 C CA  . GLY   B 102 ? 0.1952 0.2282 0.2529 -0.0005 -0.0302 0.0393  108 GLY   C CA  
1911 C C   . GLY   B 102 ? 0.2017 0.2332 0.2596 0.0002  -0.0304 0.0342  108 GLY   C C   
1912 O O   . GLY   B 102 ? 0.2107 0.2397 0.2698 -0.0006 -0.0339 0.0333  108 GLY   C O   
1913 N N   . ASP   B 103 ? 0.1866 0.2197 0.2434 0.0017  -0.0267 0.0312  109 ASP   C N   
1914 C CA  . ASP   B 103 ? 0.1813 0.2130 0.2382 0.0027  -0.0269 0.0268  109 ASP   C CA  
1915 C C   . ASP   B 103 ? 0.1826 0.2155 0.2498 0.0017  -0.0262 0.0264  109 ASP   C C   
1916 O O   . ASP   B 103 ? 0.1732 0.2044 0.2405 0.0022  -0.0269 0.0237  109 ASP   C O   
1917 C CB  . ASP   B 103 ? 0.1798 0.2132 0.2330 0.0049  -0.0235 0.0238  109 ASP   C CB  
1918 C CG  . ASP   B 103 ? 0.2129 0.2440 0.2546 0.0065  -0.0241 0.0227  109 ASP   C CG  
1919 O OD1 . ASP   B 103 ? 0.2225 0.2493 0.2583 0.0062  -0.0281 0.0220  109 ASP   C OD1 
1920 O OD2 . ASP   B 103 ? 0.2316 0.2652 0.2703 0.0080  -0.0205 0.0226  109 ASP   C OD2 
1921 N N   . CYS   B 104 ? 0.1708 0.2063 0.2463 0.0005  -0.0247 0.0291  110 CYS   C N   
1922 C CA  . CYS   B 104 ? 0.1764 0.2128 0.2611 0.0000  -0.0238 0.0282  110 CYS   C CA  
1923 C C   . CYS   B 104 ? 0.1716 0.2055 0.2571 -0.0006 -0.0264 0.0279  110 CYS   C C   
1924 O O   . CYS   B 104 ? 0.1854 0.2176 0.2689 -0.0015 -0.0295 0.0301  110 CYS   C O   
1925 C CB  . CYS   B 104 ? 0.1904 0.2288 0.2836 -0.0012 -0.0225 0.0313  110 CYS   C CB  
1926 S SG  . CYS   B 104 ? 0.2146 0.2564 0.3112 -0.0009 -0.0187 0.0313  110 CYS   C SG  
1927 N N   . GLY   B 105 ? 0.1572 0.1908 0.2448 -0.0001 -0.0254 0.0253  111 GLY   C N   
1928 C CA  . GLY   B 105 ? 0.1666 0.1981 0.2555 -0.0007 -0.0270 0.0253  111 GLY   C CA  
1929 C C   . GLY   B 105 ? 0.1680 0.1965 0.2499 0.0002  -0.0283 0.0231  111 GLY   C C   
1930 O O   . GLY   B 105 ? 0.1720 0.1988 0.2554 -0.0002 -0.0288 0.0230  111 GLY   C O   
1931 N N   . GLY   B 106 ? 0.1644 0.1922 0.2391 0.0014  -0.0286 0.0214  112 GLY   C N   
1932 C CA  . GLY   B 106 ? 0.1681 0.1926 0.2362 0.0026  -0.0298 0.0190  112 GLY   C CA  
1933 C C   . GLY   B 106 ? 0.1590 0.1836 0.2286 0.0037  -0.0279 0.0170  112 GLY   C C   
1934 O O   . GLY   B 106 ? 0.1673 0.1951 0.2401 0.0044  -0.0255 0.0162  112 GLY   C O   
1935 N N   . ILE   B 107 ? 0.1475 0.1687 0.2154 0.0038  -0.0292 0.0166  113 ILE   C N   
1936 C CA  . ILE   B 107 ? 0.1488 0.1699 0.2172 0.0049  -0.0275 0.0154  113 ILE   C CA  
1937 C C   . ILE   B 107 ? 0.1575 0.1781 0.2207 0.0074  -0.0273 0.0127  113 ILE   C C   
1938 O O   . ILE   B 107 ? 0.1481 0.1661 0.2065 0.0083  -0.0289 0.0116  113 ILE   C O   
1939 C CB  . ILE   B 107 ? 0.1822 0.1999 0.2516 0.0038  -0.0285 0.0171  113 ILE   C CB  
1940 C CG1 . ILE   B 107 ? 0.2019 0.2218 0.2790 0.0019  -0.0272 0.0197  113 ILE   C CG1 
1941 C CG2 . ILE   B 107 ? 0.1899 0.2055 0.2561 0.0055  -0.0276 0.0161  113 ILE   C CG2 
1942 C CD1 . ILE   B 107 ? 0.2375 0.2549 0.3177 0.0003  -0.0280 0.0220  113 ILE   C CD1 
1943 N N   . LEU   B 108 ? 0.1454 0.1683 0.2099 0.0088  -0.0255 0.0113  114 LEU   C N   
1944 C CA  . LEU   B 108 ? 0.1456 0.1684 0.2065 0.0113  -0.0257 0.0090  114 LEU   C CA  
1945 C C   . LEU   B 108 ? 0.1534 0.1731 0.2124 0.0118  -0.0260 0.0097  114 LEU   C C   
1946 O O   . LEU   B 108 ? 0.1491 0.1698 0.2106 0.0110  -0.0245 0.0106  114 LEU   C O   
1947 C CB  . LEU   B 108 ? 0.1595 0.1871 0.2237 0.0122  -0.0242 0.0072  114 LEU   C CB  
1948 C CG  . LEU   B 108 ? 0.1787 0.2069 0.2409 0.0149  -0.0248 0.0049  114 LEU   C CG  
1949 C CD1 . LEU   B 108 ? 0.1952 0.2228 0.2545 0.0168  -0.0256 0.0037  114 LEU   C CD1 
1950 C CD2 . LEU   B 108 ? 0.1831 0.2161 0.2500 0.0151  -0.0240 0.0032  114 LEU   C CD2 
1951 N N   . ARG   B 109 ? 0.1557 0.1714 0.2102 0.0133  -0.0275 0.0093  115 ARG   C N   
1952 C CA  . ARG   B 109 ? 0.1622 0.1746 0.2145 0.0138  -0.0277 0.0108  115 ARG   C CA  
1953 C C   . ARG   B 109 ? 0.1746 0.1853 0.2227 0.0169  -0.0289 0.0094  115 ARG   C C   
1954 O O   . ARG   B 109 ? 0.1864 0.1968 0.2333 0.0185  -0.0301 0.0074  115 ARG   C O   
1955 C CB  . ARG   B 109 ? 0.1870 0.1945 0.2394 0.0119  -0.0289 0.0131  115 ARG   C CB  
1956 C CG  . ARG   B 109 ? 0.2799 0.2836 0.3294 0.0126  -0.0315 0.0117  115 ARG   C CG  
1957 C CD  . ARG   B 109 ? 0.3829 0.3812 0.4330 0.0105  -0.0335 0.0136  115 ARG   C CD  
1958 N NE  . ARG   B 109 ? 0.4669 0.4668 0.5222 0.0074  -0.0329 0.0161  115 ARG   C NE  
1959 C CZ  . ARG   B 109 ? 0.5348 0.5348 0.5921 0.0054  -0.0348 0.0162  115 ARG   C CZ  
1960 N NH1 . ARG   B 109 ? 0.5396 0.5374 0.5928 0.0061  -0.0372 0.0138  115 ARG   C NH1 
1961 N NH2 . ARG   B 109 ? 0.5530 0.5551 0.6164 0.0029  -0.0343 0.0187  115 ARG   C NH2 
1962 N N   . CYS   B 110 ? 0.1797 0.1894 0.2255 0.0179  -0.0285 0.0105  116 CYS   C N   
1963 C CA  . CYS   B 110 ? 0.1857 0.1934 0.2274 0.0209  -0.0302 0.0099  116 CYS   C CA  
1964 C C   . CYS   B 110 ? 0.2063 0.2082 0.2449 0.0207  -0.0304 0.0134  116 CYS   C C   
1965 O O   . CYS   B 110 ? 0.2272 0.2272 0.2680 0.0180  -0.0293 0.0158  116 CYS   C O   
1966 C CB  . CYS   B 110 ? 0.1971 0.2090 0.2380 0.0226  -0.0300 0.0083  116 CYS   C CB  
1967 S SG  . CYS   B 110 ? 0.2038 0.2160 0.2429 0.0213  -0.0275 0.0102  116 CYS   C SG  
1968 N N   . GLN   B 111 ? 0.2110 0.2101 0.2453 0.0233  -0.0318 0.0142  117 GLN   C N   
1969 C CA  . GLN   B 111 ? 0.2324 0.2258 0.2640 0.0230  -0.0316 0.0183  117 GLN   C CA  
1970 C C   . GLN   B 111 ? 0.2459 0.2403 0.2770 0.0211  -0.0284 0.0213  117 GLN   C C   
1971 O O   . GLN   B 111 ? 0.2633 0.2537 0.2945 0.0196  -0.0272 0.0252  117 GLN   C O   
1972 C CB  . GLN   B 111 ? 0.2752 0.2657 0.3021 0.0265  -0.0339 0.0190  117 GLN   C CB  
1973 C CG  . GLN   B 111 ? 0.3426 0.3372 0.3656 0.0286  -0.0339 0.0181  117 GLN   C CG  
1974 C CD  . GLN   B 111 ? 0.4363 0.4285 0.4548 0.0323  -0.0369 0.0189  117 GLN   C CD  
1975 O OE1 . GLN   B 111 ? 0.4549 0.4501 0.4747 0.0348  -0.0393 0.0157  117 GLN   C OE1 
1976 N NE2 . GLN   B 111 ? 0.4387 0.4258 0.4523 0.0328  -0.0366 0.0234  117 GLN   C NE2 
1977 N N   . HIS   B 112 ? 0.2280 0.2276 0.2591 0.0211  -0.0267 0.0194  118 HIS   C N   
1978 C CA  . HIS   B 112 ? 0.2215 0.2224 0.2517 0.0200  -0.0232 0.0214  118 HIS   C CA  
1979 C C   . HIS   B 112 ? 0.2317 0.2347 0.2688 0.0168  -0.0208 0.0220  118 HIS   C C   
1980 O O   . HIS   B 112 ? 0.2486 0.2522 0.2864 0.0158  -0.0174 0.0244  118 HIS   C O   
1981 C CB  . HIS   B 112 ? 0.2382 0.2430 0.2644 0.0221  -0.0229 0.0186  118 HIS   C CB  
1982 C CG  . HIS   B 112 ? 0.2541 0.2577 0.2740 0.0254  -0.0260 0.0179  118 HIS   C CG  
1983 N ND1 . HIS   B 112 ? 0.2616 0.2681 0.2832 0.0271  -0.0292 0.0140  118 HIS   C ND1 
1984 C CD2 . HIS   B 112 ? 0.2578 0.2579 0.2704 0.0274  -0.0264 0.0209  118 HIS   C CD2 
1985 C CE1 . HIS   B 112 ? 0.2719 0.2768 0.2878 0.0300  -0.0318 0.0145  118 HIS   C CE1 
1986 N NE2 . HIS   B 112 ? 0.2652 0.2658 0.2749 0.0304  -0.0304 0.0188  118 HIS   C NE2 
1987 N N   . GLY   B 113 ? 0.2111 0.2155 0.2534 0.0154  -0.0224 0.0200  119 GLY   C N   
1988 C CA  . GLY   B 113 ? 0.1929 0.1992 0.2417 0.0125  -0.0208 0.0208  119 GLY   C CA  
1989 C C   . GLY   B 113 ? 0.1743 0.1847 0.2267 0.0121  -0.0216 0.0177  119 GLY   C C   
1990 O O   . GLY   B 113 ? 0.1716 0.1824 0.2222 0.0135  -0.0238 0.0151  119 GLY   C O   
1991 N N   . VAL   B 114 ? 0.1476 0.1609 0.2057 0.0102  -0.0198 0.0182  120 VAL   C N   
1992 C CA  . VAL   B 114 ? 0.1551 0.1719 0.2172 0.0095  -0.0203 0.0161  120 VAL   C CA  
1993 C C   . VAL   B 114 ? 0.1558 0.1759 0.2167 0.0113  -0.0194 0.0130  120 VAL   C C   
1994 O O   . VAL   B 114 ? 0.1703 0.1915 0.2309 0.0118  -0.0172 0.0127  120 VAL   C O   
1995 C CB  . VAL   B 114 ? 0.1625 0.1811 0.2319 0.0071  -0.0189 0.0180  120 VAL   C CB  
1996 C CG1 . VAL   B 114 ? 0.1694 0.1913 0.2427 0.0066  -0.0194 0.0164  120 VAL   C CG1 
1997 C CG2 . VAL   B 114 ? 0.1727 0.1882 0.2443 0.0050  -0.0206 0.0209  120 VAL   C CG2 
1998 N N   . VAL   B 115 ? 0.1541 0.1761 0.2152 0.0120  -0.0211 0.0106  121 VAL   C N   
1999 C CA  . VAL   B 115 ? 0.1683 0.1937 0.2299 0.0133  -0.0210 0.0074  121 VAL   C CA  
2000 C C   . VAL   B 115 ? 0.1779 0.2064 0.2462 0.0118  -0.0198 0.0068  121 VAL   C C   
2001 O O   . VAL   B 115 ? 0.1902 0.2207 0.2605 0.0121  -0.0188 0.0047  121 VAL   C O   
2002 C CB  . VAL   B 115 ? 0.1751 0.2011 0.2346 0.0151  -0.0233 0.0055  121 VAL   C CB  
2003 C CG1 . VAL   B 115 ? 0.1666 0.1967 0.2289 0.0160  -0.0237 0.0024  121 VAL   C CG1 
2004 C CG2 . VAL   B 115 ? 0.1920 0.2144 0.2452 0.0171  -0.0247 0.0062  121 VAL   C CG2 
2005 N N   . GLY   B 116 ? 0.1658 0.1946 0.2373 0.0102  -0.0202 0.0084  122 GLY   C N   
2006 C CA  . GLY   B 116 ? 0.1747 0.2061 0.2527 0.0086  -0.0192 0.0087  122 GLY   C CA  
2007 C C   . GLY   B 116 ? 0.1683 0.1993 0.2476 0.0071  -0.0202 0.0111  122 GLY   C C   
2008 O O   . GLY   B 116 ? 0.1698 0.1981 0.2454 0.0070  -0.0216 0.0123  122 GLY   C O   
2009 N N   . ILE   B 117 ? 0.1462 0.1796 0.2307 0.0060  -0.0197 0.0118  123 ILE   C N   
2010 C CA  . ILE   B 117 ? 0.1380 0.1711 0.2228 0.0047  -0.0208 0.0143  123 ILE   C CA  
2011 C C   . ILE   B 117 ? 0.1373 0.1732 0.2237 0.0047  -0.0202 0.0142  123 ILE   C C   
2012 O O   . ILE   B 117 ? 0.1412 0.1796 0.2323 0.0047  -0.0189 0.0129  123 ILE   C O   
2013 C CB  . ILE   B 117 ? 0.1571 0.1901 0.2476 0.0029  -0.0207 0.0172  123 ILE   C CB  
2014 C CG1 . ILE   B 117 ? 0.1688 0.2041 0.2666 0.0027  -0.0187 0.0167  123 ILE   C CG1 
2015 C CG2 . ILE   B 117 ? 0.1615 0.1921 0.2513 0.0024  -0.0214 0.0184  123 ILE   C CG2 
2016 C CD1 . ILE   B 117 ? 0.1809 0.2163 0.2860 0.0011  -0.0187 0.0200  123 ILE   C CD1 
2017 N N   . VAL   B 118 ? 0.1364 0.1718 0.2189 0.0045  -0.0212 0.0155  124 VAL   C N   
2018 C CA  . VAL   B 118 ? 0.1383 0.1765 0.2219 0.0045  -0.0199 0.0163  124 VAL   C CA  
2019 C C   . VAL   B 118 ? 0.1456 0.1858 0.2373 0.0028  -0.0188 0.0185  124 VAL   C C   
2020 O O   . VAL   B 118 ? 0.1433 0.1821 0.2375 0.0016  -0.0197 0.0207  124 VAL   C O   
2021 C CB  . VAL   B 118 ? 0.1529 0.1897 0.2297 0.0046  -0.0210 0.0177  124 VAL   C CB  
2022 C CG1 . VAL   B 118 ? 0.1726 0.2125 0.2503 0.0045  -0.0189 0.0194  124 VAL   C CG1 
2023 C CG2 . VAL   B 118 ? 0.1580 0.1925 0.2278 0.0065  -0.0219 0.0150  124 VAL   C CG2 
2024 N N   . SER   B 119 ? 0.1455 0.1888 0.2422 0.0028  -0.0169 0.0179  125 SER   C N   
2025 C CA  . SER   B 119 ? 0.1493 0.1939 0.2543 0.0013  -0.0159 0.0199  125 SER   C CA  
2026 C C   . SER   B 119 ? 0.1462 0.1936 0.2540 0.0007  -0.0140 0.0219  125 SER   C C   
2027 O O   . SER   B 119 ? 0.1496 0.1973 0.2625 -0.0007 -0.0134 0.0253  125 SER   C O   
2028 C CB  . SER   B 119 ? 0.1716 0.2164 0.2825 0.0014  -0.0154 0.0167  125 SER   C CB  
2029 O OG  . SER   B 119 ? 0.1925 0.2379 0.3123 0.0001  -0.0145 0.0179  125 SER   C OG  
2030 N N   . THR   B 120 ? 0.1293 0.1789 0.2343 0.0019  -0.0129 0.0201  126 THR   C N   
2031 C CA  . THR   B 120 ? 0.1462 0.1993 0.2548 0.0014  -0.0104 0.0223  126 THR   C CA  
2032 C C   . THR   B 120 ? 0.1682 0.2224 0.2687 0.0031  -0.0092 0.0222  126 THR   C C   
2033 O O   . THR   B 120 ? 0.1752 0.2276 0.2689 0.0048  -0.0107 0.0195  126 THR   C O   
2034 C CB  . THR   B 120 ? 0.1584 0.2147 0.2769 0.0009  -0.0094 0.0198  126 THR   C CB  
2035 O OG1 . THR   B 120 ? 0.1586 0.2167 0.2749 0.0028  -0.0098 0.0159  126 THR   C OG1 
2036 C CG2 . THR   B 120 ? 0.1649 0.2196 0.2904 -0.0002 -0.0106 0.0184  126 THR   C CG2 
2037 N N   . GLY   B 121 ? 0.1903 0.2473 0.2919 0.0027  -0.0063 0.0254  127 GLY   C N   
2038 C CA  . GLY   B 121 ? 0.2180 0.2766 0.3125 0.0045  -0.0041 0.0254  127 GLY   C CA  
2039 C C   . GLY   B 121 ? 0.2545 0.3178 0.3546 0.0039  0.0002  0.0286  127 GLY   C C   
2040 O O   . GLY   B 121 ? 0.2483 0.3123 0.3549 0.0017  0.0012  0.0324  127 GLY   C O   
2041 N N   . GLY   B 122 ? 0.2881 0.3548 0.3863 0.0058  0.0031  0.0274  128 GLY   C N   
2042 C CA  . GLY   B 122 ? 0.3046 0.3766 0.4086 0.0053  0.0080  0.0306  128 GLY   C CA  
2043 C C   . GLY   B 122 ? 0.3052 0.3821 0.4140 0.0073  0.0103  0.0274  128 GLY   C C   
2044 O O   . GLY   B 122 ? 0.3088 0.3855 0.4204 0.0082  0.0073  0.0228  128 GLY   C O   
2045 N N   . ASN   B 123 ? 0.3008 0.3825 0.4108 0.0081  0.0156  0.0299  129 ASN   C N   
2046 C CA  . ASN   B 123 ? 0.2955 0.3830 0.4116 0.0101  0.0183  0.0273  129 ASN   C CA  
2047 C C   . ASN   B 123 ? 0.2799 0.3651 0.3883 0.0136  0.0158  0.0218  129 ASN   C C   
2048 O O   . ASN   B 123 ? 0.2820 0.3707 0.3978 0.0150  0.0153  0.0185  129 ASN   C O   
2049 C CB  . ASN   B 123 ? 0.3300 0.4222 0.4631 0.0080  0.0177  0.0266  129 ASN   C CB  
2050 C CG  . ASN   B 123 ? 0.4126 0.5096 0.5563 0.0054  0.0225  0.0319  129 ASN   C CG  
2051 O OD1 . ASN   B 123 ? 0.4277 0.5267 0.5673 0.0059  0.0278  0.0363  129 ASN   C OD1 
2052 N ND2 . ASN   B 123 ? 0.4362 0.5351 0.5942 0.0026  0.0207  0.0317  129 ASN   C ND2 
2053 N N   . GLY   B 124 ? 0.2606 0.3398 0.3550 0.0149  0.0139  0.0211  130 GLY   C N   
2054 C CA  . GLY   B 124 ? 0.2526 0.3286 0.3398 0.0181  0.0114  0.0162  130 GLY   C CA  
2055 C C   . GLY   B 124 ? 0.2326 0.3062 0.3238 0.0176  0.0061  0.0129  130 GLY   C C   
2056 O O   . GLY   B 124 ? 0.2330 0.3055 0.3223 0.0202  0.0043  0.0091  130 GLY   C O   
2057 N N   . LEU   B 125 ? 0.2069 0.2795 0.3035 0.0145  0.0037  0.0143  131 LEU   C N   
2058 C CA  . LEU   B 125 ? 0.2001 0.2702 0.2993 0.0141  -0.0009 0.0114  131 LEU   C CA  
2059 C C   . LEU   B 125 ? 0.1971 0.2614 0.2906 0.0122  -0.0038 0.0126  131 LEU   C C   
2060 O O   . LEU   B 125 ? 0.2085 0.2720 0.3007 0.0104  -0.0026 0.0163  131 LEU   C O   
2061 C CB  . LEU   B 125 ? 0.2043 0.2789 0.3168 0.0123  -0.0012 0.0110  131 LEU   C CB  
2062 C CG  . LEU   B 125 ? 0.2340 0.3155 0.3556 0.0136  0.0011  0.0099  131 LEU   C CG  
2063 C CD1 . LEU   B 125 ? 0.2503 0.3361 0.3858 0.0107  0.0013  0.0108  131 LEU   C CD1 
2064 C CD2 . LEU   B 125 ? 0.2345 0.3159 0.3547 0.0166  -0.0017 0.0056  131 LEU   C CD2 
2065 N N   . VAL   B 126 ? 0.1662 0.2265 0.2559 0.0130  -0.0074 0.0100  132 VAL   C N   
2066 C CA  . VAL   B 126 ? 0.1635 0.2189 0.2497 0.0113  -0.0100 0.0111  132 VAL   C CA  
2067 C C   . VAL   B 126 ? 0.1496 0.2051 0.2421 0.0104  -0.0120 0.0092  132 VAL   C C   
2068 O O   . VAL   B 126 ? 0.1561 0.2128 0.2501 0.0120  -0.0132 0.0062  132 VAL   C O   
2069 C CB  . VAL   B 126 ? 0.1825 0.2324 0.2584 0.0126  -0.0123 0.0100  132 VAL   C CB  
2070 C CG1 . VAL   B 126 ? 0.1963 0.2454 0.2702 0.0153  -0.0135 0.0065  132 VAL   C CG1 
2071 C CG2 . VAL   B 126 ? 0.1812 0.2270 0.2560 0.0106  -0.0149 0.0112  132 VAL   C CG2 
2072 N N   . GLY   B 127 ? 0.1271 0.1813 0.2229 0.0081  -0.0125 0.0110  133 GLY   C N   
2073 C CA  . GLY   B 127 ? 0.1280 0.1819 0.2288 0.0075  -0.0141 0.0089  133 GLY   C CA  
2074 C C   . GLY   B 127 ? 0.1461 0.1954 0.2426 0.0071  -0.0158 0.0092  133 GLY   C C   
2075 O O   . GLY   B 127 ? 0.1538 0.2011 0.2481 0.0059  -0.0158 0.0121  133 GLY   C O   
2076 N N   . PHE   B 128 ? 0.1314 0.1793 0.2267 0.0080  -0.0173 0.0064  134 PHE   C N   
2077 C CA  . PHE   B 128 ? 0.1374 0.1815 0.2292 0.0078  -0.0183 0.0069  134 PHE   C CA  
2078 C C   . PHE   B 128 ? 0.1430 0.1872 0.2394 0.0073  -0.0182 0.0052  134 PHE   C C   
2079 O O   . PHE   B 128 ? 0.1446 0.1905 0.2430 0.0081  -0.0188 0.0021  134 PHE   C O   
2080 C CB  . PHE   B 128 ? 0.1373 0.1788 0.2217 0.0097  -0.0198 0.0054  134 PHE   C CB  
2081 C CG  . PHE   B 128 ? 0.1365 0.1776 0.2161 0.0109  -0.0201 0.0058  134 PHE   C CG  
2082 C CD1 . PHE   B 128 ? 0.1434 0.1813 0.2185 0.0103  -0.0206 0.0078  134 PHE   C CD1 
2083 C CD2 . PHE   B 128 ? 0.1453 0.1888 0.2251 0.0129  -0.0200 0.0038  134 PHE   C CD2 
2084 C CE1 . PHE   B 128 ? 0.1621 0.1988 0.2319 0.0117  -0.0209 0.0074  134 PHE   C CE1 
2085 C CE2 . PHE   B 128 ? 0.1639 0.2067 0.2391 0.0145  -0.0199 0.0037  134 PHE   C CE2 
2086 C CZ  . PHE   B 128 ? 0.1645 0.2036 0.2343 0.0139  -0.0203 0.0053  134 PHE   C CZ  
2087 N N   . ALA   B 129 ? 0.1287 0.1710 0.2269 0.0060  -0.0176 0.0069  135 ALA   C N   
2088 C CA  . ALA   B 129 ? 0.1392 0.1811 0.2411 0.0060  -0.0170 0.0050  135 ALA   C CA  
2089 C C   . ALA   B 129 ? 0.1528 0.1924 0.2479 0.0076  -0.0174 0.0035  135 ALA   C C   
2090 O O   . ALA   B 129 ? 0.1504 0.1878 0.2419 0.0074  -0.0173 0.0057  135 ALA   C O   
2091 C CB  . ALA   B 129 ? 0.1333 0.1743 0.2405 0.0045  -0.0159 0.0077  135 ALA   C CB  
2092 N N   . ASP   B 130 ? 0.1529 0.1930 0.2464 0.0090  -0.0180 -0.0001 136 ASP   C N   
2093 C CA  . ASP   B 130 ? 0.1625 0.2003 0.2484 0.0107  -0.0183 -0.0011 136 ASP   C CA  
2094 C C   . ASP   B 130 ? 0.1689 0.2048 0.2550 0.0105  -0.0161 -0.0004 136 ASP   C C   
2095 O O   . ASP   B 130 ? 0.1684 0.2050 0.2606 0.0097  -0.0148 -0.0014 136 ASP   C O   
2096 C CB  . ASP   B 130 ? 0.1857 0.2247 0.2698 0.0123  -0.0201 -0.0052 136 ASP   C CB  
2097 C CG  . ASP   B 130 ? 0.2326 0.2693 0.3078 0.0145  -0.0208 -0.0062 136 ASP   C CG  
2098 O OD1 . ASP   B 130 ? 0.2233 0.2582 0.2935 0.0151  -0.0210 -0.0037 136 ASP   C OD1 
2099 O OD2 . ASP   B 130 ? 0.2633 0.2999 0.3364 0.0156  -0.0213 -0.0094 136 ASP   C OD2 
2100 N N   . VAL   B 131 ? 0.1680 0.2016 0.2482 0.0112  -0.0153 0.0012  137 VAL   C N   
2101 C CA  . VAL   B 131 ? 0.1612 0.1937 0.2416 0.0113  -0.0125 0.0019  137 VAL   C CA  
2102 C C   . VAL   B 131 ? 0.1673 0.1980 0.2389 0.0135  -0.0118 0.0006  137 VAL   C C   
2103 O O   . VAL   B 131 ? 0.1819 0.2117 0.2523 0.0140  -0.0088 0.0012  137 VAL   C O   
2104 C CB  . VAL   B 131 ? 0.1730 0.2047 0.2568 0.0097  -0.0113 0.0063  137 VAL   C CB  
2105 C CG1 . VAL   B 131 ? 0.1711 0.2044 0.2627 0.0078  -0.0120 0.0077  137 VAL   C CG1 
2106 C CG2 . VAL   B 131 ? 0.1912 0.2208 0.2694 0.0097  -0.0127 0.0087  137 VAL   C CG2 
2107 N N   . ARG   B 132 ? 0.1657 0.1959 0.2310 0.0149  -0.0145 -0.0006 138 ARG   C N   
2108 C CA  . ARG   B 132 ? 0.1565 0.1847 0.2124 0.0171  -0.0144 -0.0010 138 ARG   C CA  
2109 C C   . ARG   B 132 ? 0.1741 0.2023 0.2265 0.0187  -0.0130 -0.0046 138 ARG   C C   
2110 O O   . ARG   B 132 ? 0.1944 0.2206 0.2382 0.0205  -0.0118 -0.0041 138 ARG   C O   
2111 C CB  . ARG   B 132 ? 0.1514 0.1793 0.2025 0.0185  -0.0181 -0.0016 138 ARG   C CB  
2112 C CG  . ARG   B 132 ? 0.1607 0.1878 0.2136 0.0175  -0.0192 0.0015  138 ARG   C CG  
2113 C CD  . ARG   B 132 ? 0.1803 0.2075 0.2298 0.0194  -0.0227 0.0004  138 ARG   C CD  
2114 N NE  . ARG   B 132 ? 0.1678 0.1988 0.2229 0.0193  -0.0245 -0.0028 138 ARG   C NE  
2115 C CZ  . ARG   B 132 ? 0.1992 0.2318 0.2543 0.0208  -0.0273 -0.0043 138 ARG   C CZ  
2116 N NH1 . ARG   B 132 ? 0.1893 0.2196 0.2385 0.0228  -0.0291 -0.0032 138 ARG   C NH1 
2117 N NH2 . ARG   B 132 ? 0.1903 0.2269 0.2521 0.0203  -0.0284 -0.0067 138 ARG   C NH2 
2118 N N   . ASP   B 133 ? 0.1633 0.1933 0.2214 0.0182  -0.0134 -0.0083 139 ASP   C N   
2119 C CA  . ASP   B 133 ? 0.1774 0.2067 0.2323 0.0198  -0.0124 -0.0127 139 ASP   C CA  
2120 C C   . ASP   B 133 ? 0.1938 0.2224 0.2514 0.0197  -0.0074 -0.0118 139 ASP   C C   
2121 O O   . ASP   B 133 ? 0.2020 0.2296 0.2556 0.0214  -0.0055 -0.0154 139 ASP   C O   
2122 C CB  . ASP   B 133 ? 0.1955 0.2266 0.2566 0.0193  -0.0154 -0.0175 139 ASP   C CB  
2123 C CG  . ASP   B 133 ? 0.2520 0.2844 0.3252 0.0168  -0.0141 -0.0162 139 ASP   C CG  
2124 O OD1 . ASP   B 133 ? 0.2388 0.2720 0.3155 0.0153  -0.0137 -0.0119 139 ASP   C OD1 
2125 O OD2 . ASP   B 133 ? 0.2872 0.3195 0.3658 0.0166  -0.0135 -0.0196 139 ASP   C OD2 
2126 N N   . LEU   B 134 ? 0.1877 0.2169 0.2520 0.0178  -0.0052 -0.0073 140 LEU   C N   
2127 C CA  . LEU   B 134 ? 0.1846 0.2139 0.2540 0.0176  -0.0006 -0.0060 140 LEU   C CA  
2128 C C   . LEU   B 134 ? 0.1892 0.2173 0.2518 0.0186  0.0030  -0.0028 140 LEU   C C   
2129 O O   . LEU   B 134 ? 0.1803 0.2086 0.2466 0.0171  0.0044  0.0021  140 LEU   C O   
2130 C CB  . LEU   B 134 ? 0.1837 0.2145 0.2643 0.0150  -0.0008 -0.0025 140 LEU   C CB  
2131 C CG  . LEU   B 134 ? 0.2056 0.2376 0.2934 0.0137  -0.0038 -0.0046 140 LEU   C CG  
2132 C CD1 . LEU   B 134 ? 0.2095 0.2426 0.3065 0.0113  -0.0041 -0.0003 140 LEU   C CD1 
2133 C CD2 . LEU   B 134 ? 0.2068 0.2384 0.2977 0.0147  -0.0028 -0.0096 140 LEU   C CD2 
2134 N N   . LEU   B 135 ? 0.1956 0.2222 0.2478 0.0212  0.0043  -0.0055 141 LEU   C N   
2135 C CA  . LEU   B 135 ? 0.2159 0.2412 0.2600 0.0225  0.0078  -0.0021 141 LEU   C CA  
2136 C C   . LEU   B 135 ? 0.2120 0.2384 0.2622 0.0220  0.0138  0.0012  141 LEU   C C   
2137 O O   . LEU   B 135 ? 0.2203 0.2462 0.2682 0.0217  0.0166  0.0061  141 LEU   C O   
2138 C CB  . LEU   B 135 ? 0.2298 0.2533 0.2601 0.0256  0.0078  -0.0056 141 LEU   C CB  
2139 C CG  . LEU   B 135 ? 0.2473 0.2702 0.2723 0.0264  0.0013  -0.0093 141 LEU   C CG  
2140 C CD1 . LEU   B 135 ? 0.2641 0.2850 0.2748 0.0297  0.0009  -0.0127 141 LEU   C CD1 
2141 C CD2 . LEU   B 135 ? 0.2433 0.2661 0.2692 0.0250  -0.0025 -0.0054 141 LEU   C CD2 
2142 N N   . TRP   B 136 ? 0.2097 0.2375 0.2685 0.0219  0.0159  -0.0014 142 TRP   C N   
2143 C CA  . TRP   B 136 ? 0.2184 0.2479 0.2853 0.0218  0.0216  0.0013  142 TRP   C CA  
2144 C C   . TRP   B 136 ? 0.2098 0.2408 0.2866 0.0187  0.0211  0.0075  142 TRP   C C   
2145 O O   . TRP   B 136 ? 0.2170 0.2498 0.3001 0.0184  0.0256  0.0111  142 TRP   C O   
2146 C CB  . TRP   B 136 ? 0.2206 0.2509 0.2951 0.0227  0.0232  -0.0032 142 TRP   C CB  
2147 C CG  . TRP   B 136 ? 0.2181 0.2487 0.3007 0.0208  0.0181  -0.0050 142 TRP   C CG  
2148 C CD1 . TRP   B 136 ? 0.2254 0.2547 0.3052 0.0213  0.0142  -0.0101 142 TRP   C CD1 
2149 C CD2 . TRP   B 136 ? 0.2166 0.2491 0.3121 0.0182  0.0166  -0.0013 142 TRP   C CD2 
2150 N NE1 . TRP   B 136 ? 0.2243 0.2546 0.3147 0.0190  0.0109  -0.0096 142 TRP   C NE1 
2151 C CE2 . TRP   B 136 ? 0.2269 0.2590 0.3261 0.0173  0.0123  -0.0042 142 TRP   C CE2 
2152 C CE3 . TRP   B 136 ? 0.2196 0.2541 0.3240 0.0166  0.0183  0.0041  142 TRP   C CE3 
2153 C CZ2 . TRP   B 136 ? 0.2307 0.2640 0.3406 0.0149  0.0099  -0.0014 142 TRP   C CZ2 
2154 C CZ3 . TRP   B 136 ? 0.2289 0.2646 0.3440 0.0144  0.0154  0.0063  142 TRP   C CZ3 
2155 C CH2 . TRP   B 136 ? 0.2303 0.2653 0.3474 0.0137  0.0114  0.0037  142 TRP   C CH2 
2156 N N   . LEU   B 137 ? 0.1923 0.2229 0.2703 0.0166  0.0154  0.0088  143 LEU   C N   
2157 C CA  . LEU   B 137 ? 0.1993 0.2307 0.2851 0.0138  0.0141  0.0141  143 LEU   C CA  
2158 C C   . LEU   B 137 ? 0.2249 0.2553 0.3068 0.0136  0.0167  0.0187  143 LEU   C C   
2159 O O   . LEU   B 137 ? 0.2358 0.2671 0.3258 0.0114  0.0170  0.0231  143 LEU   C O   
2160 C CB  . LEU   B 137 ? 0.1977 0.2282 0.2834 0.0121  0.0079  0.0140  143 LEU   C CB  
2161 C CG  . LEU   B 137 ? 0.2012 0.2330 0.2932 0.0115  0.0052  0.0113  143 LEU   C CG  
2162 C CD1 . LEU   B 137 ? 0.1930 0.2240 0.2826 0.0103  0.0000  0.0113  143 LEU   C CD1 
2163 C CD2 . LEU   B 137 ? 0.2111 0.2450 0.3155 0.0099  0.0062  0.0140  143 LEU   C CD2 
2164 N N   . ASP   B 138 ? 0.2317 0.2601 0.3015 0.0157  0.0181  0.0179  144 ASP   C N   
2165 C CA  . ASP   B 138 ? 0.2556 0.2824 0.3207 0.0156  0.0207  0.0228  144 ASP   C CA  
2166 C C   . ASP   B 138 ? 0.2985 0.3271 0.3659 0.0165  0.0282  0.0252  144 ASP   C C   
2167 O O   . ASP   B 138 ? 0.2927 0.3202 0.3566 0.0164  0.0312  0.0298  144 ASP   C O   
2168 C CB  . ASP   B 138 ? 0.2638 0.2875 0.3143 0.0177  0.0189  0.0216  144 ASP   C CB  
2169 C CG  . ASP   B 138 ? 0.2944 0.3163 0.3424 0.0171  0.0119  0.0200  144 ASP   C CG  
2170 O OD1 . ASP   B 138 ? 0.2706 0.2932 0.3271 0.0147  0.0088  0.0208  144 ASP   C OD1 
2171 O OD2 . ASP   B 138 ? 0.3297 0.3497 0.3672 0.0192  0.0097  0.0180  144 ASP   C OD2 
2172 N N   . GLU   B 139 ? 0.3373 0.3686 0.4106 0.0176  0.0317  0.0223  145 GLU   C N   
2173 C CA  . GLU   B 139 ? 0.3937 0.4271 0.4692 0.0191  0.0397  0.0242  145 GLU   C CA  
2174 C C   . GLU   B 139 ? 0.4415 0.4787 0.5322 0.0186  0.0422  0.0236  145 GLU   C C   
2175 O O   . GLU   B 139 ? 0.4489 0.4866 0.5469 0.0173  0.0375  0.0215  145 GLU   C O   
2176 C CB  . GLU   B 139 ? 0.4376 0.4693 0.4984 0.0230  0.0429  0.0199  145 GLU   C CB  
2177 C CG  . GLU   B 139 ? 0.5188 0.5504 0.5795 0.0247  0.0408  0.0125  145 GLU   C CG  
2178 C CD  . GLU   B 139 ? 0.6431 0.6718 0.6880 0.0278  0.0397  0.0069  145 GLU   C CD  
2179 O OE1 . GLU   B 139 ? 0.6542 0.6826 0.6995 0.0293  0.0389  0.0006  145 GLU   C OE1 
2180 O OE2 . GLU   B 139 ? 0.6945 0.7210 0.7270 0.0287  0.0392  0.0089  145 GLU   C OE2 
2181 N N   . GLU   B 140 ? 0.4731 0.5130 0.5680 0.0201  0.0500  0.0252  146 GLU   C N   
2182 C CA  . GLU   B 140 ? 0.4971 0.5407 0.6060 0.0207  0.0537  0.0243  146 GLU   C CA  
2183 C C   . GLU   B 140 ? 0.5153 0.5607 0.6392 0.0176  0.0481  0.0259  146 GLU   C C   
2184 O O   . GLU   B 140 ? 0.5242 0.5733 0.6625 0.0172  0.0507  0.0278  146 GLU   C O   
2185 C CB  . GLU   B 140 ? 0.5387 0.5811 0.6412 0.0245  0.0561  0.0170  146 GLU   C CB  
2186 C CG  . GLU   B 140 ? 0.6196 0.6635 0.7345 0.0250  0.0552  0.0135  146 GLU   C CG  
2187 C CD  . GLU   B 140 ? 0.7082 0.7562 0.8365 0.0264  0.0622  0.0148  146 GLU   C CD  
2188 O OE1 . GLU   B 140 ? 0.7297 0.7777 0.8643 0.0282  0.0630  0.0104  146 GLU   C OE1 
2189 O OE2 . GLU   B 140 ? 0.7344 0.7855 0.8679 0.0256  0.0670  0.0204  146 GLU   C OE2 
2190 N N1  . A1B40 C .   ? 0.2266 0.2580 0.3727 0.0228  -0.0118 -0.0057 201 A1B40 A N1  
2191 C C4  . A1B40 C .   ? 0.2556 0.3109 0.3770 0.0098  0.0134  -0.0398 201 A1B40 A C4  
2192 C C5  . A1B40 C .   ? 0.2610 0.3110 0.3887 0.0125  0.0124  -0.0402 201 A1B40 A C5  
2193 C C6  . A1B40 C .   ? 0.2650 0.3108 0.3883 0.0137  0.0068  -0.0343 201 A1B40 A C6  
2194 C C7  . A1B40 C .   ? 0.2774 0.3181 0.4059 0.0154  0.0060  -0.0353 201 A1B40 A C7  
2195 C C8  . A1B40 C .   ? 0.2853 0.3243 0.4271 0.0196  0.0047  -0.0303 201 A1B40 A C8  
2196 C C10 . A1B40 C .   ? 0.2656 0.2953 0.4021 0.0204  -0.0051 -0.0214 201 A1B40 A C10 
2197 C C13 . A1B40 C .   ? 0.2407 0.2711 0.3961 0.0243  -0.0082 -0.0097 201 A1B40 A C13 
2198 O O1  . A1B40 C .   ? 0.2386 0.2687 0.4071 0.0263  -0.0078 -0.0070 201 A1B40 A O1  
2199 C C12 . A1B40 C .   ? 0.2583 0.2886 0.4083 0.0231  -0.0045 -0.0177 201 A1B40 A C12 
2200 C C11 . A1B40 C .   ? 0.2658 0.2924 0.4150 0.0219  -0.0025 -0.0239 201 A1B40 A C11 
2201 C C9  . A1B40 C .   ? 0.2719 0.3050 0.4023 0.0187  -0.0025 -0.0256 201 A1B40 A C9  
2202 C C14 . A1B40 C .   ? 0.2586 0.2929 0.4120 0.0236  -0.0010 -0.0203 201 A1B40 A C14 
2203 N N   . A1B40 C .   ? 0.2736 0.3089 0.4150 0.0206  0.0007  -0.0259 201 A1B40 A N   
2204 O O   . A1B40 C .   ? 0.2932 0.3349 0.4457 0.0216  0.0071  -0.0297 201 A1B40 A O   
2205 C C1  . A1B40 C .   ? 0.2587 0.3051 0.3724 0.0127  0.0025  -0.0284 201 A1B40 A C1  
2206 S S   . A1B40 C .   ? 0.2610 0.3026 0.3718 0.0145  -0.0034 -0.0221 201 A1B40 A S   
2207 C C   . A1B40 C .   ? 0.2694 0.3114 0.3672 0.0121  -0.0068 -0.0178 201 A1B40 A C   
2208 C C3  . A1B40 C .   ? 0.2564 0.3117 0.3675 0.0086  0.0086  -0.0335 201 A1B40 A C3  
2209 C C2  . A1B40 C .   ? 0.2575 0.3080 0.3652 0.0102  0.0033  -0.0280 201 A1B40 A C2  
# 
