data_7HWM
# 
_entry.id   7HWM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HWM         pdb_00007hwm 10.2210/pdb7hwm/pdb 
WWPDB D_1001408022 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HWM 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                  15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(2-aminopyridin-3-yl)acetyl]piperidine-3-carboxamide' 262.308   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                     65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                           78.133    2   ?         ? ? ? 
5 water       nat water                                                          18.015    290 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[(2-aminopyridin-3-yl)acetyl]piperidine-3-carboxamide' A1BQG 
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 
A1BQG non-polymer         . '(3S)-1-[(2-aminopyridin-3-yl)acetyl]piperidine-3-carboxamide' ? 'C13 H18 N4 O2'  262.308 
ALA   'L-peptide linking' y ALANINE                                                        ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                       ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                     ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                       ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                           ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                      ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                        ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                      ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                          ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                     ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                        ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                         ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                     ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                  ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                        ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                         ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                      ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                     ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                       ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                         ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                     ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 ?   ?   ?   C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BQG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BQG 
_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 A1BQG 1   201 201 A1BQG LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 6   DMS   DMS A . 
F 2 A1BQG 1   201 201 A1BQG LIG C . 
G 4 DMS   1   202 7   DMS   DMS C . 
H 3 ZN    1   203 1   ZN    ZN  C . 
I 5 HOH   1   301 512 HOH   HOH A . 
I 5 HOH   2   302 408 HOH   HOH A . 
I 5 HOH   3   303 502 HOH   HOH A . 
I 5 HOH   4   304 168 HOH   HOH A . 
I 5 HOH   5   305 456 HOH   HOH A . 
I 5 HOH   6   306 89  HOH   HOH A . 
I 5 HOH   7   307 87  HOH   HOH A . 
I 5 HOH   8   308 189 HOH   HOH A . 
I 5 HOH   9   309 55  HOH   HOH A . 
I 5 HOH   10  310 525 HOH   HOH A . 
I 5 HOH   11  311 229 HOH   HOH A . 
I 5 HOH   12  312 452 HOH   HOH A . 
I 5 HOH   13  313 57  HOH   HOH A . 
I 5 HOH   14  314 128 HOH   HOH A . 
I 5 HOH   15  315 10  HOH   HOH A . 
I 5 HOH   16  316 195 HOH   HOH A . 
I 5 HOH   17  317 12  HOH   HOH A . 
I 5 HOH   18  318 22  HOH   HOH A . 
I 5 HOH   19  319 262 HOH   HOH A . 
I 5 HOH   20  320 435 HOH   HOH A . 
I 5 HOH   21  321 212 HOH   HOH A . 
I 5 HOH   22  322 426 HOH   HOH A . 
I 5 HOH   23  323 234 HOH   HOH A . 
I 5 HOH   24  324 2   HOH   HOH A . 
I 5 HOH   25  325 139 HOH   HOH A . 
I 5 HOH   26  326 424 HOH   HOH A . 
I 5 HOH   27  327 76  HOH   HOH A . 
I 5 HOH   28  328 13  HOH   HOH A . 
I 5 HOH   29  329 52  HOH   HOH A . 
I 5 HOH   30  330 54  HOH   HOH A . 
I 5 HOH   31  331 63  HOH   HOH A . 
I 5 HOH   32  332 53  HOH   HOH A . 
I 5 HOH   33  333 108 HOH   HOH A . 
I 5 HOH   34  334 47  HOH   HOH A . 
I 5 HOH   35  335 462 HOH   HOH A . 
I 5 HOH   36  336 78  HOH   HOH A . 
I 5 HOH   37  337 122 HOH   HOH A . 
I 5 HOH   38  338 487 HOH   HOH A . 
I 5 HOH   39  339 96  HOH   HOH A . 
I 5 HOH   40  340 107 HOH   HOH A . 
I 5 HOH   41  341 29  HOH   HOH A . 
I 5 HOH   42  342 395 HOH   HOH A . 
I 5 HOH   43  343 458 HOH   HOH A . 
I 5 HOH   44  344 116 HOH   HOH A . 
I 5 HOH   45  345 27  HOH   HOH A . 
I 5 HOH   46  346 325 HOH   HOH A . 
I 5 HOH   47  347 184 HOH   HOH A . 
I 5 HOH   48  348 277 HOH   HOH A . 
I 5 HOH   49  349 336 HOH   HOH A . 
I 5 HOH   50  350 272 HOH   HOH A . 
I 5 HOH   51  351 459 HOH   HOH A . 
I 5 HOH   52  352 60  HOH   HOH A . 
I 5 HOH   53  353 40  HOH   HOH A . 
I 5 HOH   54  354 134 HOH   HOH A . 
I 5 HOH   55  355 120 HOH   HOH A . 
I 5 HOH   56  356 31  HOH   HOH A . 
I 5 HOH   57  357 423 HOH   HOH A . 
I 5 HOH   58  358 470 HOH   HOH A . 
I 5 HOH   59  359 460 HOH   HOH A . 
I 5 HOH   60  360 17  HOH   HOH A . 
I 5 HOH   61  361 9   HOH   HOH A . 
I 5 HOH   62  362 489 HOH   HOH A . 
I 5 HOH   63  363 170 HOH   HOH A . 
I 5 HOH   64  364 14  HOH   HOH A . 
I 5 HOH   65  365 445 HOH   HOH A . 
I 5 HOH   66  366 18  HOH   HOH A . 
I 5 HOH   67  367 84  HOH   HOH A . 
I 5 HOH   68  368 477 HOH   HOH A . 
I 5 HOH   69  369 466 HOH   HOH A . 
I 5 HOH   70  370 59  HOH   HOH A . 
I 5 HOH   71  371 517 HOH   HOH A . 
I 5 HOH   72  372 41  HOH   HOH A . 
I 5 HOH   73  373 188 HOH   HOH A . 
I 5 HOH   74  374 1   HOH   HOH A . 
I 5 HOH   75  375 494 HOH   HOH A . 
I 5 HOH   76  376 472 HOH   HOH A . 
I 5 HOH   77  377 162 HOH   HOH A . 
I 5 HOH   78  378 140 HOH   HOH A . 
I 5 HOH   79  379 476 HOH   HOH A . 
I 5 HOH   80  380 5   HOH   HOH A . 
I 5 HOH   81  381 443 HOH   HOH A . 
I 5 HOH   82  382 91  HOH   HOH A . 
I 5 HOH   83  383 62  HOH   HOH A . 
I 5 HOH   84  384 261 HOH   HOH A . 
I 5 HOH   85  385 24  HOH   HOH A . 
I 5 HOH   86  386 48  HOH   HOH A . 
I 5 HOH   87  387 44  HOH   HOH A . 
I 5 HOH   88  388 81  HOH   HOH A . 
I 5 HOH   89  389 65  HOH   HOH A . 
I 5 HOH   90  390 26  HOH   HOH A . 
I 5 HOH   91  391 177 HOH   HOH A . 
I 5 HOH   92  392 118 HOH   HOH A . 
I 5 HOH   93  393 524 HOH   HOH A . 
I 5 HOH   94  394 433 HOH   HOH A . 
I 5 HOH   95  395 461 HOH   HOH A . 
I 5 HOH   96  396 86  HOH   HOH A . 
I 5 HOH   97  397 136 HOH   HOH A . 
I 5 HOH   98  398 431 HOH   HOH A . 
I 5 HOH   99  399 109 HOH   HOH A . 
I 5 HOH   100 400 439 HOH   HOH A . 
I 5 HOH   101 401 148 HOH   HOH A . 
I 5 HOH   102 402 428 HOH   HOH A . 
I 5 HOH   103 403 171 HOH   HOH A . 
I 5 HOH   104 404 183 HOH   HOH A . 
I 5 HOH   105 405 493 HOH   HOH A . 
I 5 HOH   106 406 478 HOH   HOH A . 
I 5 HOH   107 407 491 HOH   HOH A . 
I 5 HOH   108 408 442 HOH   HOH A . 
I 5 HOH   109 409 471 HOH   HOH A . 
I 5 HOH   110 410 99  HOH   HOH A . 
I 5 HOH   111 411 448 HOH   HOH A . 
I 5 HOH   112 412 38  HOH   HOH A . 
I 5 HOH   113 413 51  HOH   HOH A . 
I 5 HOH   114 414 6   HOH   HOH A . 
I 5 HOH   115 415 125 HOH   HOH A . 
I 5 HOH   116 416 430 HOH   HOH A . 
I 5 HOH   117 417 166 HOH   HOH A . 
I 5 HOH   118 418 468 HOH   HOH A . 
I 5 HOH   119 419 449 HOH   HOH A . 
I 5 HOH   120 420 185 HOH   HOH A . 
I 5 HOH   121 421 152 HOH   HOH A . 
I 5 HOH   122 422 486 HOH   HOH A . 
I 5 HOH   123 423 506 HOH   HOH A . 
I 5 HOH   124 424 104 HOH   HOH A . 
I 5 HOH   125 425 377 HOH   HOH A . 
I 5 HOH   126 426 454 HOH   HOH A . 
I 5 HOH   127 427 238 HOH   HOH A . 
I 5 HOH   128 428 523 HOH   HOH A . 
I 5 HOH   129 429 501 HOH   HOH A . 
I 5 HOH   130 430 503 HOH   HOH A . 
I 5 HOH   131 431 515 HOH   HOH A . 
I 5 HOH   132 432 146 HOH   HOH A . 
I 5 HOH   133 433 218 HOH   HOH A . 
I 5 HOH   134 434 504 HOH   HOH A . 
I 5 HOH   135 435 202 HOH   HOH A . 
I 5 HOH   136 436 451 HOH   HOH A . 
I 5 HOH   137 437 369 HOH   HOH A . 
I 5 HOH   138 438 396 HOH   HOH A . 
I 5 HOH   139 439 520 HOH   HOH A . 
I 5 HOH   140 440 204 HOH   HOH A . 
I 5 HOH   141 441 496 HOH   HOH A . 
I 5 HOH   142 442 368 HOH   HOH A . 
J 5 HOH   1   301 505 HOH   HOH C . 
J 5 HOH   2   302 45  HOH   HOH C . 
J 5 HOH   3   303 150 HOH   HOH C . 
J 5 HOH   4   304 130 HOH   HOH C . 
J 5 HOH   5   305 174 HOH   HOH C . 
J 5 HOH   6   306 492 HOH   HOH C . 
J 5 HOH   7   307 73  HOH   HOH C . 
J 5 HOH   8   308 475 HOH   HOH C . 
J 5 HOH   9   309 117 HOH   HOH C . 
J 5 HOH   10  310 61  HOH   HOH C . 
J 5 HOH   11  311 111 HOH   HOH C . 
J 5 HOH   12  312 50  HOH   HOH C . 
J 5 HOH   13  313 16  HOH   HOH C . 
J 5 HOH   14  314 219 HOH   HOH C . 
J 5 HOH   15  315 280 HOH   HOH C . 
J 5 HOH   16  316 105 HOH   HOH C . 
J 5 HOH   17  317 144 HOH   HOH C . 
J 5 HOH   18  318 250 HOH   HOH C . 
J 5 HOH   19  319 522 HOH   HOH C . 
J 5 HOH   20  320 25  HOH   HOH C . 
J 5 HOH   21  321 457 HOH   HOH C . 
J 5 HOH   22  322 165 HOH   HOH C . 
J 5 HOH   23  323 39  HOH   HOH C . 
J 5 HOH   24  324 473 HOH   HOH C . 
J 5 HOH   25  325 432 HOH   HOH C . 
J 5 HOH   26  326 43  HOH   HOH C . 
J 5 HOH   27  327 482 HOH   HOH C . 
J 5 HOH   28  328 497 HOH   HOH C . 
J 5 HOH   29  329 465 HOH   HOH C . 
J 5 HOH   30  330 217 HOH   HOH C . 
J 5 HOH   31  331 163 HOH   HOH C . 
J 5 HOH   32  332 450 HOH   HOH C . 
J 5 HOH   33  333 425 HOH   HOH C . 
J 5 HOH   34  334 101 HOH   HOH C . 
J 5 HOH   35  335 266 HOH   HOH C . 
J 5 HOH   36  336 485 HOH   HOH C . 
J 5 HOH   37  337 436 HOH   HOH C . 
J 5 HOH   38  338 446 HOH   HOH C . 
J 5 HOH   39  339 74  HOH   HOH C . 
J 5 HOH   40  340 19  HOH   HOH C . 
J 5 HOH   41  341 209 HOH   HOH C . 
J 5 HOH   42  342 71  HOH   HOH C . 
J 5 HOH   43  343 126 HOH   HOH C . 
J 5 HOH   44  344 4   HOH   HOH C . 
J 5 HOH   45  345 233 HOH   HOH C . 
J 5 HOH   46  346 131 HOH   HOH C . 
J 5 HOH   47  347 37  HOH   HOH C . 
J 5 HOH   48  348 467 HOH   HOH C . 
J 5 HOH   49  349 20  HOH   HOH C . 
J 5 HOH   50  350 447 HOH   HOH C . 
J 5 HOH   51  351 115 HOH   HOH C . 
J 5 HOH   52  352 72  HOH   HOH C . 
J 5 HOH   53  353 32  HOH   HOH C . 
J 5 HOH   54  354 488 HOH   HOH C . 
J 5 HOH   55  355 455 HOH   HOH C . 
J 5 HOH   56  356 75  HOH   HOH C . 
J 5 HOH   57  357 422 HOH   HOH C . 
J 5 HOH   58  358 114 HOH   HOH C . 
J 5 HOH   59  359 95  HOH   HOH C . 
J 5 HOH   60  360 82  HOH   HOH C . 
J 5 HOH   61  361 98  HOH   HOH C . 
J 5 HOH   62  362 498 HOH   HOH C . 
J 5 HOH   63  363 178 HOH   HOH C . 
J 5 HOH   64  364 34  HOH   HOH C . 
J 5 HOH   65  365 80  HOH   HOH C . 
J 5 HOH   66  366 33  HOH   HOH C . 
J 5 HOH   67  367 381 HOH   HOH C . 
J 5 HOH   68  368 469 HOH   HOH C . 
J 5 HOH   69  369 88  HOH   HOH C . 
J 5 HOH   70  370 484 HOH   HOH C . 
J 5 HOH   71  371 440 HOH   HOH C . 
J 5 HOH   72  372 513 HOH   HOH C . 
J 5 HOH   73  373 453 HOH   HOH C . 
J 5 HOH   74  374 113 HOH   HOH C . 
J 5 HOH   75  375 8   HOH   HOH C . 
J 5 HOH   76  376 500 HOH   HOH C . 
J 5 HOH   77  377 437 HOH   HOH C . 
J 5 HOH   78  378 479 HOH   HOH C . 
J 5 HOH   79  379 153 HOH   HOH C . 
J 5 HOH   80  380 112 HOH   HOH C . 
J 5 HOH   81  381 68  HOH   HOH C . 
J 5 HOH   82  382 36  HOH   HOH C . 
J 5 HOH   83  383 23  HOH   HOH C . 
J 5 HOH   84  384 464 HOH   HOH C . 
J 5 HOH   85  385 69  HOH   HOH C . 
J 5 HOH   86  386 15  HOH   HOH C . 
J 5 HOH   87  387 42  HOH   HOH C . 
J 5 HOH   88  388 509 HOH   HOH C . 
J 5 HOH   89  389 137 HOH   HOH C . 
J 5 HOH   90  390 237 HOH   HOH C . 
J 5 HOH   91  391 35  HOH   HOH C . 
J 5 HOH   92  392 3   HOH   HOH C . 
J 5 HOH   93  393 7   HOH   HOH C . 
J 5 HOH   94  394 511 HOH   HOH C . 
J 5 HOH   95  395 438 HOH   HOH C . 
J 5 HOH   96  396 49  HOH   HOH C . 
J 5 HOH   97  397 480 HOH   HOH C . 
J 5 HOH   98  398 267 HOH   HOH C . 
J 5 HOH   99  399 495 HOH   HOH C . 
J 5 HOH   100 400 271 HOH   HOH C . 
J 5 HOH   101 401 46  HOH   HOH C . 
J 5 HOH   102 402 444 HOH   HOH C . 
J 5 HOH   103 403 28  HOH   HOH C . 
J 5 HOH   104 404 490 HOH   HOH C . 
J 5 HOH   105 405 481 HOH   HOH C . 
J 5 HOH   106 406 58  HOH   HOH C . 
J 5 HOH   107 407 441 HOH   HOH C . 
J 5 HOH   108 408 508 HOH   HOH C . 
J 5 HOH   109 409 434 HOH   HOH C . 
J 5 HOH   110 410 483 HOH   HOH C . 
J 5 HOH   111 411 106 HOH   HOH C . 
J 5 HOH   112 412 172 HOH   HOH C . 
J 5 HOH   113 413 526 HOH   HOH C . 
J 5 HOH   114 414 315 HOH   HOH C . 
J 5 HOH   115 415 374 HOH   HOH C . 
J 5 HOH   116 416 30  HOH   HOH C . 
J 5 HOH   117 417 499 HOH   HOH C . 
J 5 HOH   118 418 11  HOH   HOH C . 
J 5 HOH   119 419 463 HOH   HOH C . 
J 5 HOH   120 420 77  HOH   HOH C . 
J 5 HOH   121 421 519 HOH   HOH C . 
J 5 HOH   122 422 210 HOH   HOH C . 
J 5 HOH   123 423 66  HOH   HOH C . 
J 5 HOH   124 424 145 HOH   HOH C . 
J 5 HOH   125 425 119 HOH   HOH C . 
J 5 HOH   126 426 518 HOH   HOH C . 
J 5 HOH   127 427 224 HOH   HOH C . 
J 5 HOH   128 428 21  HOH   HOH C . 
J 5 HOH   129 429 474 HOH   HOH C . 
J 5 HOH   130 430 393 HOH   HOH C . 
J 5 HOH   131 431 127 HOH   HOH C . 
J 5 HOH   132 432 305 HOH   HOH C . 
J 5 HOH   133 433 192 HOH   HOH C . 
J 5 HOH   134 434 367 HOH   HOH C . 
J 5 HOH   135 435 181 HOH   HOH C . 
J 5 HOH   136 436 373 HOH   HOH C . 
J 5 HOH   137 437 398 HOH   HOH C . 
J 5 HOH   138 438 406 HOH   HOH C . 
J 5 HOH   139 439 521 HOH   HOH C . 
J 5 HOH   140 440 400 HOH   HOH C . 
J 5 HOH   141 441 102 HOH   HOH C . 
J 5 HOH   142 442 370 HOH   HOH C . 
J 5 HOH   143 443 516 HOH   HOH C . 
J 5 HOH   144 444 85  HOH   HOH C . 
J 5 HOH   145 445 507 HOH   HOH C . 
J 5 HOH   146 446 514 HOH   HOH C . 
J 5 HOH   147 447 376 HOH   HOH C . 
J 5 HOH   148 448 510 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           7HWM 
_cell.length_a           72.526 
_cell.length_b           61.554 
_cell.length_c           65.192 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.69 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HWM 
_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          7HWM 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.29 
_exptl_crystal.density_percent_sol   46.21 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-21 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92203 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HWM 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             65.08 
_reflns.d_resolution_high            1.41 
_reflns.number_obs                   55342 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.118 
_reflns.pdbx_netI_over_sigmaI        9.6 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.129 
_reflns.pdbx_Rpim_I_all              0.050 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     349809 
_reflns.pdbx_chi_squared             0.54 
_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                  1.41 
_reflns_shell.d_res_low                   1.43 
_reflns_shell.number_measured_all         11723 
_reflns_shell.number_unique_obs           2688 
_reflns_shell.Rmerge_I_obs                2.024 
_reflns_shell.pdbx_chi_squared            0.20 
_reflns_shell.pdbx_redundancy             4.4 
_reflns_shell.percent_possible_obs        97.4 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.6 
_reflns_shell.pdbx_Rrim_I_all             2.287 
_reflns_shell.pdbx_Rpim_I_all             1.044 
_reflns_shell.pdbx_CC_half                0.307 
_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                                 7HWM 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     54848 
_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                             19.93 
_refine.ls_d_res_high                            1.409 
_refine.ls_percent_reflns_obs                    99.0 
_refine.ls_R_factor_obs                          0.1943 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1935 
_refine.ls_R_factor_R_free                       0.2173 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 3.290 
_refine.ls_number_reflns_R_free                  1806 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.960 
_refine.B_iso_mean                               22.38 
_refine.aniso_B[1][1]                            -1.65320 
_refine.aniso_B[2][2]                            1.52040 
_refine.aniso_B[3][3]                            0.13280 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.21240 
_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             0.064 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.065 
_refine.pdbx_overall_SU_R_Blow_DPI               0.067 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.067 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HWM 
_refine_analyze.Luzzati_coordinate_error_obs    0.19 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.number_atoms_solvent             290 
_refine_hist.number_atoms_total               2486 
_refine_hist.d_res_high                       1.409 
_refine_hist.d_res_low                        19.93 
# 
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  2254 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.06  ? 2.00  3066 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  752  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  406  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2254 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.55  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.80 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  276  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  2010 '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                        1.42 
_refine_ls_shell.number_reflns_R_work             1050 
_refine_ls_shell.R_factor_R_work                  0.3189 
_refine_ls_shell.percent_reflns_obs               87.16 
_refine_ls_shell.R_factor_R_free                  0.2975 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.28 
_refine_ls_shell.number_reflns_R_free             47 
_refine_ls_shell.number_reflns_all                1097 
_refine_ls_shell.R_factor_all                     0.3179 
# 
_struct.entry_id                  7HWM 
_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-0034475-001 (A71EV2A-x3963)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HWM 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 4 ? 
H N N 3 ? 
I N N 5 ? 
J 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 7HWM A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HWM 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,I 
2 1 B,F,G,H,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P6  AA6 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P7  AA7 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P8  AA8 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P9  AA9 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P10 AB1 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P11 AB2 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.422 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.371 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 56  C ZN 203 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 58  C ZN 203 1_555 ? ? ? ? ? ? ? 2.369 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 116 C ZN 203 1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 H ZN . ZN ? ? C HIS 118 C ZN 203 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
# 
_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_555 109.1 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.1 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.0 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 107.4 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.7 ? 
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_555 115.1 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.9 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.3 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 116.6 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 107.7 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.0 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 116.1 ? 
# 
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 GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N GLY B 43  ? N GLY C 49  O GLY B 7   ? O GLY C 13  
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                   7HWM 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    330 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    343 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.10 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    C 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -130.71 
_pdbx_validate_torsion.psi             -30.24 
# 
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 15.0642 7.6449   14.2603 -0.0314 -0.0164 -0.0102 -0.0042 -0.0057 -0.0019 1.1643 1.8495 0.4874 
0.7834  -0.2879 -0.3463 -0.0360 0.0160  0.1231 -0.0092 0.0663 -0.0355 0.0310  -0.0515 -0.0302 
'X-RAY DIFFRACTION' 2 ? refined 19.4560 -23.0111 18.3983 -0.0235 -0.0096 -0.0143 0.0033  -0.0121 0.0071  0.9101 1.6559 0.4086 
-0.5391 0.0610  0.1568  -0.0351 -0.0277 0.0672 -0.0569 0.0578 0.0478  -0.0135 0.0334  -0.0227 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 146 ? A GLU 140 
2  1 Y 1 A ALA 147 ? A ALA 141 
3  1 Y 1 A MET 148 ? A MET 142 
4  1 Y 1 A GLU 149 ? A GLU 143 
5  1 Y 1 A GLN 150 ? A GLN 144 
6  1 Y 1 C GLU 146 ? B GLU 140 
7  1 Y 1 C ALA 147 ? B ALA 141 
8  1 Y 1 C MET 148 ? B MET 142 
9  1 Y 1 C GLU 149 ? B GLU 143 
10 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BQG N1   N  N N 1   
A1BQG N3   N  N N 2   
A1BQG C4   C  N N 3   
A1BQG C5   C  N N 4   
A1BQG C6   C  N N 5   
A1BQG C7   C  Y N 6   
A1BQG C8   C  Y N 7   
A1BQG C10  C  Y N 8   
A1BQG O1   O  N N 9   
A1BQG C3   C  N N 10  
A1BQG C2   C  N N 11  
A1BQG C12  C  N N 12  
A1BQG C1   C  N S 13  
A1BQG C    C  N N 14  
A1BQG O    O  N N 15  
A1BQG N    N  N N 16  
A1BQG C11  C  Y N 17  
A1BQG N2   N  Y N 18  
A1BQG C9   C  Y N 19  
A1BQG H14  H  N N 20  
A1BQG H15  H  N N 21  
A1BQG H8   H  N N 22  
A1BQG H7   H  N N 23  
A1BQG H10  H  N N 24  
A1BQG H9   H  N N 25  
A1BQG H11  H  N N 26  
A1BQG H13  H  N N 27  
A1BQG H6   H  N N 28  
A1BQG H5   H  N N 29  
A1BQG H4   H  N N 30  
A1BQG H3   H  N N 31  
A1BQG H17  H  N N 32  
A1BQG H16  H  N N 33  
A1BQG H    H  N N 34  
A1BQG H1   H  N N 35  
A1BQG H2   H  N N 36  
A1BQG H12  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BQG N   C    sing N N 1   
A1BQG O   C    doub N N 2   
A1BQG C   C1   sing N N 3   
A1BQG C1  C2   sing N N 4   
A1BQG C2  C3   sing N N 5   
A1BQG C3  C4   sing N N 6   
A1BQG C4  N1   sing N N 7   
A1BQG N1  C5   sing N N 8   
A1BQG C5  O1   doub N N 9   
A1BQG C6  C5   sing N N 10  
A1BQG C7  C6   sing N N 11  
A1BQG C7  C8   doub Y N 12  
A1BQG C8  C9   sing Y N 13  
A1BQG C9  C10  doub Y N 14  
A1BQG C10 N2   sing Y N 15  
A1BQG N2  C11  doub Y N 16  
A1BQG C11 C7   sing Y N 17  
A1BQG N3  C11  sing N N 18  
A1BQG C12 N1   sing N N 19  
A1BQG C1  C12  sing N N 20  
A1BQG N3  H14  sing N N 21  
A1BQG N3  H15  sing N N 22  
A1BQG C4  H8   sing N N 23  
A1BQG C4  H7   sing N N 24  
A1BQG C6  H10  sing N N 25  
A1BQG C6  H9   sing N N 26  
A1BQG C8  H11  sing N N 27  
A1BQG C10 H13  sing N N 28  
A1BQG C3  H6   sing N N 29  
A1BQG C3  H5   sing N N 30  
A1BQG C2  H4   sing N N 31  
A1BQG C2  H3   sing N N 32  
A1BQG C12 H17  sing N N 33  
A1BQG C12 H16  sing N N 34  
A1BQG C1  H    sing N N 35  
A1BQG N   H1   sing N N 36  
A1BQG N   H2   sing N N 37  
A1BQG C9  H12  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HWM 
_atom_sites.fract_transf_matrix[1][1]   0.013788 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000648 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016246 
_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]   0.015356 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.438 7.344   24.368 1.00 20.72  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.661 7.442   23.569 1.00 21.01  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.801 6.270   22.611 1.00 20.46  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.118 5.251   22.780 1.00 20.78  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.877 7.538   24.499 1.00 23.57  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.013 6.323   25.221 1.00 26.12  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.662 6.422   21.585 1.00 18.89  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.932 5.370   20.618 1.00 18.73  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.287 5.919   19.251 1.00 17.45  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.872 7.026   18.890 1.00 17.62  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.026 5.153   18.481 1.00 15.32  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.458 5.562   17.160 1.00 15.98  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.461 4.366   16.201 1.00 16.39  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.534 3.206   16.656 1.00 16.61  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.880 6.148   17.265 1.00 17.00  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.509 4.650   14.879 1.00 14.98  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.711 3.668   13.822 1.00 15.87  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.120 3.879   13.287 1.00 16.15  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.509 5.011   13.030 1.00 15.83  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.718 3.840   12.657 1.00 16.05  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.258 3.822   13.168 1.00 14.91  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.921 2.762   11.601 1.00 17.02  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.285 4.345   12.067 1.00 14.64  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.913 2.811   13.201 1.00 17.17  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.279 2.890   12.659 1.00 18.39  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.368 2.140   11.363 1.00 18.44  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.292 0.927   11.393 1.00 19.65  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.286 2.325   13.685 1.00 18.23  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.346 3.147   14.948 1.00 18.91  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 26.551 2.837   16.037 1.00 20.21  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 28.163 4.261   15.036 1.00 19.93  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 26.574 3.612   17.188 1.00 21.08  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 28.219 5.023   16.191 1.00 21.00  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.430 4.686   17.268 1.00 21.56  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.437 5.463   18.388 1.00 24.45  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.426 2.826   10.211 1.00 18.48  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.438 2.193   8.893  1.00 19.58  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.572 2.790   8.074  1.00 21.15  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.653 4.000   7.931  1.00 21.40  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.058 2.334   8.172  1.00 21.75  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.577 3.794   8.162  1.00 21.17  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.143 1.820   6.747  1.00 23.98  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.519 1.962   7.619  1.00 22.65  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.662 2.438   6.856  1.00 22.54  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.461 3.427   7.689  1.00 22.87  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.675 3.179   8.886  1.00 23.46  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.734 4.603   7.131  1.00 22.69  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.439 5.630   7.890  1.00 22.95  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.480 6.715   8.393  1.00 21.25  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.885 7.871   8.566  1.00 22.23  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.601 6.223   7.107  1.00 26.80  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.756 5.276   7.009  1.00 34.15  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.322 4.849   8.022  1.00 36.37  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.107 4.923   5.793  1.00 36.31  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.233 6.320   8.742  1.00 19.92  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.227 7.267   9.224  1.00 18.77  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.643 6.811   10.566 1.00 16.89  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.511 5.601   10.809 1.00 16.71  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.055 7.370   8.222  1.00 18.73  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.462 7.897   6.865  1.00 18.99  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.091 9.129   6.737  1.00 19.74  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.152 7.201   5.706  1.00 20.88  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.464 9.626   5.493  1.00 21.69  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.521 7.689   4.452  1.00 21.86  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.165 8.912   4.354  1.00 23.51  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.516 9.419   3.124  1.00 26.30  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.249 7.786   11.387 1.00 15.54  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.532 7.630   12.647 1.00 15.97  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.221 8.451   12.480 1.00 17.05  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.269 9.650   12.186 1.00 17.50  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.366 8.170   13.813 1.00 15.60  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.630 8.357   15.131 1.00 18.85  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.581 8.800   16.243 1.00 19.65  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.991 9.774   17.162 1.00 21.53  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.521 9.512   18.377 1.00 24.84  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.502 8.258   18.838 1.00 25.40  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.042 10.491  19.134 1.00 23.68  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.060 7.788   12.619 1.00 16.29  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.757 8.445   12.510 1.00 14.62  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.179 8.573   13.909 1.00 14.87  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.025 7.558   14.606 1.00 14.96  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.770 7.604   11.631 1.00 14.44  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.475 8.430   11.376 1.00 13.74  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.440 7.164   10.314 1.00 14.87  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.872 9.794   14.334 1.00 13.02  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.320 10.006  15.684 1.00 12.63  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.102 10.937  15.580 1.00 11.98  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.876 11.625  14.564 1.00 13.74  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.398 10.677  16.596 1.00 15.19  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.533 9.713   16.913 1.00 18.80  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.922 11.978  15.960 1.00 16.91  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.317 11.053  16.689 1.00 11.25  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.251 12.067  16.723 1.00 11.29  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 18.958 13.411  16.739 1.00 13.38  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 19.889 13.623  17.536 1.00 14.45  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.466 11.967  18.052 1.00 11.86  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.638 10.710  18.119 1.00 13.81  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.094 9.679   18.665 1.00 14.27  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.446 10.743  17.576 1.00 13.75  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.506 14.353  15.878 1.00 11.97  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.160 15.663  15.845 1.00 12.00  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.164 16.338  17.226 1.00 13.56  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.166 17.000  17.590 1.00 15.67  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.479 16.533  14.788 1.00 13.02  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.267 17.806  14.464 1.00 13.27  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.338 18.693  13.614 1.00 13.87  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 18.951 19.933  13.100 1.00 16.39  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 18.997 21.074  13.777 1.00 16.45  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.523 21.136  15.014 1.00 17.49  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.467 22.182  13.197 1.00 16.82  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.068 16.175  17.993 1.00 13.93  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 17.989 16.860  19.296 1.00 15.78  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 18.930 16.292  20.353 1.00 17.60  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.161 16.956  21.385 1.00 19.02  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.535 16.937  19.811 1.00 17.20  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 15.968 15.632  20.302 1.00 16.58  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.344 14.735  19.443 1.00 16.87  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 15.816 15.194  21.579 1.00 17.28  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 14.922 13.737  20.212 1.00 16.87  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.131 13.994  21.511 1.00 17.33  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.510 15.109  20.089 1.00 16.12  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.463 14.466  21.001 1.00 15.76  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 21.912 14.490  20.463 1.00 15.89  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 22.803 13.903  21.080 1.00 16.92  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.014 13.027  21.283 1.00 15.92  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.643 12.912  21.987 1.00 17.42  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.266 11.447  22.166 1.00 18.47  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.620 13.657  23.316 1.00 18.37  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.150 15.117  19.294 1.00 16.14  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.479 15.159  18.704 1.00 15.87  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.467 15.862  19.660 1.00 16.67  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.104 16.812  20.320 1.00 17.62  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.440 15.928  17.394 1.00 16.19  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.684 15.315  19.735 1.00 18.40  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 26.721 15.848  20.631 1.00 19.72  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.553 16.917  19.927 1.00 21.04  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.456 17.086  18.701 1.00 20.80  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.655 14.680  21.064 1.00 21.91  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.384 14.216  19.908 1.00 22.75  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 26.888 13.533  21.674 1.00 22.91  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.483 17.588  20.674 1.00 21.94  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.391 18.548  20.029 1.00 23.83  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.199 17.861  18.934 1.00 21.58  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.377 18.410  17.850 1.00 22.12  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.401 19.164  21.038 1.00 28.08  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 29.765 19.892  22.177 1.00 36.32  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 28.859 20.921  21.968 1.00 39.91  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 29.945 19.729  23.510 1.00 39.02  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 28.501 21.333  23.175 1.00 40.92  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.138 20.650  24.136 1.00 40.58  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.637 16.615  19.206 1.00 22.00  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.406 15.869  18.229 1.00 21.28  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.593 15.546  16.975 1.00 20.03  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.124 15.588  15.865 1.00 20.07  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 31.992 14.592  18.834 1.00 24.05  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.472 14.603  18.695 1.00 32.30  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.130 15.596  19.088 1.00 32.93  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.012 13.566  18.055 1.00 36.13  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.305 15.186  17.123 1.00 18.27  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.445 14.954  15.946 1.00 18.68  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.404 16.205  15.050 1.00 18.35  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.547 16.092  13.818 1.00 18.14  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.017 14.648  16.401 1.00 17.92  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 26.846 13.231  16.891 1.00 19.48  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.459 12.338  16.302 1.00 19.89  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.139 13.041  17.939 1.00 19.63  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.246 17.392  15.679 1.00 18.58  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.162 18.645  14.918 1.00 18.53  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.506 19.025  14.289 1.00 19.87  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.518 19.544  13.171 1.00 19.69  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.613 19.768  15.797 1.00 18.14  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.113 19.759  15.880 1.00 17.89  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.350 19.385  16.951 1.00 19.67  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.209 20.306  14.915 1.00 17.49  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.013 19.591  16.676 1.00 18.81  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 23.900 20.130  15.418 1.00 18.59  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.372 20.827  13.630 1.00 18.17  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 22.774 20.566  14.718 1.00 18.17  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.253 21.266  12.943 1.00 18.04  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 22.976 21.106  13.472 1.00 18.11  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.633 18.674  14.941 1.00 20.08  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 31.964 18.938  14.356 1.00 21.35  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.287 18.025  13.158 1.00 22.40  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.207 18.313  12.361 1.00 23.34  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.038 18.764  15.411 1.00 21.61  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.596 16.883  13.056 1.00 20.39  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.799 15.943  11.961 1.00 20.56  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.494 15.812  11.147 1.00 19.26  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.164 14.747  10.623 1.00 18.56  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.222 14.588  12.546 1.00 22.33  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.578 14.649  13.184 1.00 25.34  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.589 14.696  12.476 1.00 26.47  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.614 14.664  14.516 1.00 24.87  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.739 16.927  11.024 1.00 18.49  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.441 16.920  10.343 1.00 18.42  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.510 16.531  8.878  1.00 19.26  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.358 17.034  8.130  1.00 21.38  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.844 18.324  10.469 1.00 18.46  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.488 18.532  9.804  1.00 19.69  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.404 17.655  10.467 1.00 19.61  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.074 19.994  9.894  1.00 18.71  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.611 15.601  8.460  1.00 17.98  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.455 15.225  7.052  1.00 19.89  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.135 15.840  6.517  1.00 20.21  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.084 16.476  5.447  1.00 21.82  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.443 13.676  6.895  1.00 21.40  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.009 13.266  5.488  1.00 21.93  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.819 13.085  7.227  1.00 22.20  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.057 15.684  7.303  1.00 18.62  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.728 16.149  6.906  1.00 17.65  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.838 16.225  8.144  1.00 15.73  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.986 15.405  9.058  1.00 16.68  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.124 15.137  5.889  1.00 18.54  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.658 15.324  5.576  1.00 19.65  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.106 16.197  4.685  1.00 20.95  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.565 14.571  6.132  1.00 19.30  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.726 16.067  4.686  1.00 21.80  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.372 15.081  5.572  1.00 20.44  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.478 13.571  7.103  1.00 19.46  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.114 14.519  5.854  1.00 20.12  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.237 13.015  7.376  1.00 20.55  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.066 13.543  6.811  1.00 20.23  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.937 17.195  8.167  1.00 15.33  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.951 17.265  9.259  1.00 16.21  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.665 17.862  8.734  1.00 16.53  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.677 18.625  7.764  1.00 17.19  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.461 18.059  10.483 1.00 17.62  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.038 19.439  10.182 1.00 18.05  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.032 20.560  9.928  1.00 20.16  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.343 21.475  9.125  1.00 24.73  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 19.942 20.542  10.542 1.00 19.51  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.544 17.491  9.373  1.00 15.83  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.252 18.009  8.936  1.00 15.57  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.360 18.144  10.173 1.00 15.24  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.885 17.137  10.732 1.00 15.26  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.627 17.070  7.870  1.00 17.89  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.355 17.604  7.233  1.00 25.16  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.625 18.342  7.906  1.00 26.39  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.067 17.232  6.073  1.00 25.15  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.144 19.407  10.611 1.00 15.92  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.343 19.682  11.785 0.50 16.47  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.327 19.660  11.793 0.50 16.19  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 13.905 19.148  11.611 1.00 17.32  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.293 18.686  12.576 1.00 18.45  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.347 21.187  12.058 0.50 18.89  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.306 21.147  12.148 0.50 17.88  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.513 21.521  13.151 0.50 22.04  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.737 21.969  11.147 0.50 19.57  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.363 19.237  10.381 1.00 17.76  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 11.997 18.768  10.137 1.00 19.10  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.873 17.257  10.282 1.00 18.89  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.758 16.781  10.436 1.00 19.94  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.473 19.215  8.771  1.00 22.74  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.979 18.425  7.712  1.00 28.81  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.993 16.506  10.232 1.00 16.15  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.931 15.031  10.391 1.00 15.10  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.477 14.588  11.775 1.00 14.94  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.438 13.392  12.108 1.00 15.34  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.783 14.355  9.281  1.00 14.88  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.190 14.566  7.885  1.00 14.84  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.004 13.904  6.788  1.00 16.37  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.978 12.431  6.931  1.00 15.63  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.148 11.587  5.916  1.00 15.61  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.310 12.052  4.668  1.00 17.29  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.126 10.264  6.127  1.00 15.74  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.048 15.516  12.568 1.00 14.57  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.747 15.158  13.811 1.00 14.30  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 15.929 14.216  13.556 1.00 13.08  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.244 13.383  14.416 1.00 13.65  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.843 14.643  14.927 1.00 15.68  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.539 14.380  16.251 1.00 15.92  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.328 15.249  16.695 1.00 14.37  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.267 13.328  16.875 1.00 14.75  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.599 14.357  12.395 1.00 12.81  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.770 13.512  12.106 1.00 12.46  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.068 14.298  11.928 1.00 13.00  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.062 15.387  11.345 1.00 13.97  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.580 12.685  10.824 1.00 12.62  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.538 11.566  10.901 1.00 13.22  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.468 10.889  9.539  1.00 14.25  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.934 10.493  11.962 1.00 13.59  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.183 13.672  12.320 1.00 12.86  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.498 14.222  12.049 1.00 13.41  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.400 13.034  11.762 1.00 13.73  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.322 11.999  12.433 1.00 14.33  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.030 15.076  13.225 1.00 13.35  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.426 15.711  13.022 1.00 14.67  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.535 17.046  13.777 1.00 16.23  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.546 14.788  13.529 1.00 15.06  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.241 13.190  10.734 1.00 13.56  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.240 12.154  10.380 1.00 14.13  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.660 12.784  10.485 1.00 15.98  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.907 13.877  9.954  1.00 17.18  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.009 11.609  8.955  1.00 15.56  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.096 10.583  8.566  1.00 16.34  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.608 11.002  8.848  1.00 15.52  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.553 12.083  11.186 1.00 16.23  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.934 12.540  11.324 1.00 17.71  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.891 11.458  10.762 1.00 19.27  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.495 10.299  10.559 1.00 17.16  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.245 12.872  12.781 1.00 18.59  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.144 11.744  13.641 1.00 19.38  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.140 11.854  10.452 1.00 20.06  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.117 10.894  9.938  1.00 21.40  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.882 10.208  11.083 1.00 22.53  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.082 10.781  12.151 1.00 23.22  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.071 11.575  8.955  1.00 24.10  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.668 12.679  9.605  1.00 26.03  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.310 8.961   10.857 1.00 22.76  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.063 8.180   11.851 1.00 25.23  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.405 7.719   11.231 1.00 29.24  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.542 7.649   10.007 1.00 30.03  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.263 6.935   12.287 1.00 25.80  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.152 6.082   11.155 1.00 26.44  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.870 7.273   12.805 1.00 24.93  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.360 7.347   12.073 1.00 31.62  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.639 6.805   11.605 1.00 34.06  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.544 5.271   11.479 1.00 35.67  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.185 4.677   10.607 1.00 37.47  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.760 7.204   12.572 1.00 36.69  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.368 6.840   13.903 1.00 38.28  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.067 8.675   12.522 1.00 37.49  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.751 4.627   12.346 1.00 34.50  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.591 3.178   12.317 1.00 33.88  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.392 2.779   11.433 1.00 33.54  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.440 3.540   11.297 1.00 32.74  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.383 2.661   13.735 1.00 33.39  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.435 1.582   10.865 1.00 33.97  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.368 1.044   10.014 1.00 35.26  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.218 0.542   10.890 1.00 35.10  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.462 -0.195  11.845 1.00 35.77  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.936 -0.112  9.178  1.00 38.78  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.900 -0.811  8.302  1.00 44.73  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.612 -0.064  7.020  1.00 51.97  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.305 0.901   6.643  1.00 54.01  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.578 -0.514  6.307  1.00 52.49  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.988 0.938   10.594 1.00 34.29  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.836 0.579   11.426 1.00 34.25  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.250 -0.826  11.355 1.00 34.73  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.265 -1.462  10.304 1.00 35.82  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.559 -1.217  12.453 1.00 33.05  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.948 -2.510  12.697 1.00 32.26  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.586 -2.819  11.945 1.00 31.49  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 26.281 -3.998  11.771 1.00 31.42  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 27.797 -2.716  14.211 1.00 32.89  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 26.717 -1.506  15.063 1.00 32.92  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.816 -1.816  11.465 1.00 29.92  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.424 -1.959  10.952 1.00 27.69  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 24.174 -2.024  9.370  1.00 26.11  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 25.038 -1.564  8.600  1.00 27.77  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.579 -0.789  11.566 1.00 26.38  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.395 -0.860  13.093 1.00 29.67  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 22.892 -1.894  13.570 1.00 30.95  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.757 0.158   13.823 1.00 24.45  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.975 -2.605  8.921  1.00 23.45  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.408 -2.737  7.548  1.00 23.36  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 21.095 -1.905  7.508  1.00 21.28  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 20.292 -2.055  8.405  1.00 20.87  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 22.000 -4.237  7.230  1.00 27.34  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 23.192 -4.965  6.952  1.00 30.76  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 21.076 -4.371  5.967  1.00 28.31  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.872 -1.061  6.491  1.00 19.26  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.627 -0.304  6.374  1.00 17.32  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.631 -1.078  5.519  1.00 17.49  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.976 -1.545  4.404  1.00 18.92  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.873 1.083   5.747  1.00 16.18  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 21.012 1.840   6.455  1.00 16.79  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.566 1.915   5.709  1.00 17.25  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.707 2.104   7.971  1.00 17.56  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.391 -1.191  5.982  1.00 16.59  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.330 -1.845  5.205  1.00 16.13  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.986 -0.957  3.993  1.00 16.55  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.968 0.273   4.085  1.00 16.14  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 15.068 -1.987  6.082  1.00 15.88  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.715 -1.605  2.834  1.00 16.76  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 15.274 -0.864  1.635  1.00 17.67  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.997 -1.616  1.224  1.00 20.47  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 14.042 -2.616  0.479  1.00 21.62  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 16.340 -0.932  0.511  1.00 18.31  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.686 -0.338  0.917  1.00 19.22  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.657 1.141   1.334  1.00 21.00  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.996 1.585   1.702  1.00 19.66  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 19.263 2.749   2.289  1.00 21.96  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.279 3.590   2.599  1.00 19.52  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.513 3.082   2.571  1.00 21.39  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.853 -1.157  1.749  1.00 20.28  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.605 -1.920  1.659  1.00 21.22  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.398 -1.016  2.036  1.00 21.58  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.583 0.119   2.484  1.00 21.58  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.716 -3.077  2.655  1.00 19.66  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.689 -2.532  4.397  1.00 18.34  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 9.174  -1.604  1.997  1.00 22.74  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.974  -0.901  2.440  1.00 23.00  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 7.299  -1.625  3.596  1.00 23.59  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 6.088  -1.459  3.783  1.00 24.52  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.970  -0.694  1.291  1.00 27.41  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 6.484  -1.962  0.626  1.00 35.73  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.910  -3.069  1.049  1.00 35.47  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 5.674  -1.857  -0.319 1.00 42.66  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 8.073  -2.362  4.445  1.00 21.75  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.483  -3.003  5.622  1.00 20.79  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.724  -2.016  6.487  1.00 19.89  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 7.176  -0.861  6.669  1.00 18.76  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.561  -3.706  6.450  1.00 20.72  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 9.225  -5.250  5.734  1.00 19.86  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.608  -2.471  7.065  1.00 18.72  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.833  -1.729  8.053  1.00 17.35  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.705  -2.481  9.356  1.00 14.88  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.828  -2.185  10.174 1.00 15.23  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.455  -1.287  7.529  1.00 19.49  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.503  -0.138  6.571  1.00 24.90  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 2.081  0.262   6.196  1.00 29.34  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.630  0.046   5.065  1.00 30.59  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.332  0.851   7.139  1.00 25.06  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.573  -3.531  9.570  1.00 13.42  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.648  -4.244  10.846 1.00 14.74  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 7.148  -4.427  11.120 1.00 15.05  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.989  -4.509  10.204 1.00 15.87  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.918  -5.611  10.848 1.00 17.66  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.580  -6.501  9.954  1.00 19.47  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.462  -5.495  10.458 1.00 18.38  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.474  -4.470  12.389 1.00 14.67  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.849  -4.689  12.817 1.00 13.37  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.929  -4.742  14.328 1.00 12.64  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.911  -4.964  14.976 1.00 12.86  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.146 -4.600  14.855 1.00 11.69  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.367 -4.710  16.299 1.00 10.97  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.239 -3.518  16.684 1.00 10.93  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.250 -3.255  16.019 1.00 12.45  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.097 -6.049  16.611 1.00 12.96  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.480 -6.123  18.101 1.00 15.21  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.193 -7.239  16.266 1.00 14.37  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.917 -2.883  17.814 1.00 10.44  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.771 -1.773  18.291 1.00 10.84  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.299 -2.044  19.694 1.00 12.65  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.673 -2.750  20.489 1.00 12.74  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.052 -0.383  18.214 1.00 10.89  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.048 -0.116  19.339 1.00 10.73  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.771  -0.678  19.309 1.00 12.45  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.341 0.773   20.368 1.00 11.96  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.839  -0.423  20.319 1.00 12.22  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.404  1.049   21.376 1.00 12.93  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.152  0.465   21.334 1.00 12.76  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.224  0.692   22.344 1.00 15.02  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.430 -1.386  20.018 1.00 12.41  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 13.982 -1.492  21.361 1.00 13.33  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.496 -0.318  22.222 1.00 13.01  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.603 0.846   21.828 1.00 13.23  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.525 -1.554  21.321 1.00 13.26  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.073 -1.657  22.719 1.00 13.89  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.904 -2.810  23.462 1.00 15.52  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.733 -0.589  23.307 1.00 14.87  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.356 -2.893  24.769 1.00 16.28  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.166 -0.649  24.620 1.00 15.97  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.021 -1.819  25.329 1.00 17.59  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.449 -1.920  26.628 1.00 21.86  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 12.917 -0.650  23.402 1.00 13.03  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.390 0.342   24.331 1.00 13.95  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.257 0.355   25.591 1.00 14.41  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.134 -0.528  26.463 1.00 14.96  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 10.936 0.003   24.634 1.00 14.50  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.185 1.017   25.952 1.00 15.57  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.155 1.353   25.695 1.00 14.99  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.074 1.405   26.828 1.00 15.45  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.401 1.547   28.189 1.00 14.41  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 14.873 0.984   29.181 1.00 15.96  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.119 2.499   26.639 1.00 19.14  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.506 3.773   26.649 1.00 26.04  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.257 2.252   28.237 1.00 13.64  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.520 2.421   29.502 1.00 14.76  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 11.845 1.148   30.020 1.00 14.56  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.293 1.162   31.139 1.00 15.78  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.505 3.556   29.406 1.00 16.54  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.448 3.246   28.505 1.00 17.34  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 11.908 0.059   29.236 1.00 14.96  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.427 -1.245  29.660 1.00 14.85  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.518 -2.324  29.543 1.00 16.65  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.234 -3.507  29.793 1.00 17.96  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.182 -1.660  28.847 1.00 14.84  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 8.965  -0.753  29.080 1.00 14.53  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.328  -1.068  30.409 1.00 16.58  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.133  -0.239  30.664 1.00 19.88  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.151  0.942   31.266 1.00 20.97  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.297  1.462   31.688 1.00 18.66  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.020  1.618   31.456 1.00 20.21  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.718 -1.985  29.000 1.00 17.40  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.765 -2.974  28.693 1.00 18.96  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.185 -4.137  27.869 1.00 18.36  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.455 -5.317  28.151 1.00 20.10  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.427 -3.518  29.965 1.00 22.61  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.384 -2.526  30.539 1.00 27.95  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.304 -3.203  31.552 1.00 30.59  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 17.952 -2.202  32.380 1.00 32.73  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.726 -2.059  33.687 1.00 33.96  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 16.890 -2.886  34.323 1.00 34.99  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.315 -1.082  34.363 1.00 32.42  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.366 -3.804  26.869 1.00 16.61  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.666 -4.858  26.113 1.00 16.51  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.470 -4.464  24.687 1.00 15.72  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.323 -3.285  24.402 1.00 15.59  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.232 -5.036  26.700 1.00 19.29  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.080 -6.017  27.866 1.00 29.47  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.591  -6.117  28.217 1.00 36.93  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.245  -7.330  29.059 1.00 43.33  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.948  -7.322  30.371 1.00 47.53  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.292 -5.456  23.833 1.00 15.27  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 11.913 -5.205  22.447 1.00 14.40  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.428 -5.538  22.278 1.00 15.01  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 9.903  -6.477  22.903 1.00 16.20  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.688 -6.129  21.497 1.00 14.30  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.173 -5.924  21.517 1.00 15.45  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.833 -5.191  20.528 1.00 18.84  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.091 -6.455  22.342 1.00 16.11  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.122 -5.274  20.827 1.00 17.47  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.324 -6.011  21.902 1.00 19.65  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.721  -4.717  21.483 1.00 12.72  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.285  -4.932  21.260 1.00 12.93  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.993  -4.982  19.745 1.00 13.12  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.531  -4.199  18.955 1.00 12.85  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.459  -3.738  21.814 1.00 13.47  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.471  -3.638  23.314 1.00 14.87  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.707  -4.501  24.098 1.00 16.76  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.175  -2.631  23.956 1.00 15.24  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.703  -4.410  25.493 1.00 16.92  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.160  -2.514  25.346 1.00 15.71  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.428  -3.404  26.109 1.00 17.66  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.412  -3.275  27.486 1.00 20.21  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.091  -5.881  19.337 1.00 13.55  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.657  -5.880  17.928 1.00 12.97  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.620  -4.753  17.709 1.00 15.11  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.764  -4.522  18.594 1.00 18.02  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.988  -7.255  17.763 1.00 13.81  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.478  -7.578  19.190 1.00 15.65  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.385  -6.890  20.158 1.00 14.36  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.627  -4.144  16.535 1.00 13.90  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.702  -3.054  16.219 1.00 14.81  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.222  -3.105  14.804 1.00 13.92  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.930  -3.539  13.903 1.00 14.17  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.363  -1.661  16.444 1.00 17.18  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.419  -1.310  17.928 1.00 18.78  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.739  -1.581  15.798 1.00 16.76  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.001  -2.562  14.574 1.00 14.36  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.522  -2.237  13.227 1.00 15.69  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.665  -0.689  13.171 1.00 15.35  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.274  -0.027  14.124 1.00 16.38  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.045  -2.569  13.074 1.00 19.37  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.889  -3.977  13.120 1.00 26.41  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.239  -0.129  12.110 1.00 13.13  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.477  1.321   12.051 1.00 14.49  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.991  1.910   10.738 1.00 15.22  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.915  1.215   9.708  1.00 16.45  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.967  1.621   12.349 1.00 15.20  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 6.008  0.885   11.520 1.00 14.25  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.508  -0.347  11.932 1.00 13.81  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.480  1.417   10.322 1.00 13.79  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.471  -1.014  11.172 1.00 14.47  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.438  0.737   9.555  1.00 14.79  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.920  -0.482  9.989  1.00 14.54  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.554  3.210   10.780 1.00 15.05  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.071  3.895   9.588  1.00 16.33  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.210  4.224   8.625  1.00 16.71  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.377  4.244   9.024  1.00 16.81  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.325  5.170   9.974  1.00 16.86  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.178  6.048   10.703 1.00 18.32  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.872  4.502   7.346  1.00 16.98  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.875  4.890   6.346  1.00 17.81  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.474  6.246   6.747  1.00 19.11  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.791  7.054   7.373  1.00 18.96  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.232  4.964   4.939  1.00 21.37  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.893  3.564   4.448  1.00 24.69  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.486  3.615   2.985  1.00 29.47  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.354  2.186   2.536  1.00 35.48  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.642  2.088   1.260  1.00 39.78  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.723  6.543   6.336  1.00 17.72  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.320  7.842   6.711  1.00 18.08  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.453  9.007   6.213  1.00 18.59  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.071  9.047   5.044  1.00 19.54  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.687  7.842   6.009  1.00 19.92  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.946  6.418   5.583  1.00 21.76  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.638  5.689   5.548  1.00 19.02  ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.169  9.947   7.108  1.00 17.90  ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.271  11.045  6.735  1.00 19.33  ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.562  12.291  7.568  1.00 19.05  ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.429  12.284  8.436  1.00 19.11  ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.814  10.581  6.850  1.00 23.62  ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.455  10.471  8.209  1.00 29.85  ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.850  13.402  7.229  1.00 18.82  ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.021  14.671  7.931  1.00 19.77  ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.010  14.649  9.078  1.00 21.30  ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.800  14.573  8.822  1.00 22.46  ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.661  15.782  6.929  1.00 20.95  ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.090  17.157  7.302  1.00 25.81  ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 5.604  17.345  7.241  1.00 26.38  ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 3.428  18.159  6.394  1.00 28.63  ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.493  14.720  10.331 1.00 21.17  ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.670  14.577  11.533 1.00 22.10  ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 2.926  15.725  12.467 1.00 23.42  ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.078  16.103  12.675 1.00 23.16  ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.016  13.202  12.201 1.00 22.92  ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.517  12.072  11.301 1.00 24.53  ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.462  13.092  13.626 1.00 24.01  ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.763  10.709  11.772 1.00 26.11  ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 1.842  16.321  13.026 1.00 24.02  ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.008  17.431  13.947 1.00 26.02  ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.643  16.953  15.259 1.00 26.38  ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.222  15.945  15.816 1.00 27.82  ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 0.647  18.103  14.222 1.00 27.49  ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 0.745  19.224  15.224 1.00 30.66  ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.109  20.492  14.831 1.00 32.25  ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.539  18.990  16.570 1.00 32.39  ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.212  21.526  15.756 1.00 33.87  ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 0.663  20.011  17.486 1.00 34.00  ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 0.974  21.277  17.076 1.00 33.75  ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.686  17.686  15.739 1.00 24.72  ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.377  17.358  16.988 1.00 24.41  ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.338  18.603  17.863 1.00 25.63  ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 4.778  19.692  17.432 1.00 26.06  ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 5.855  16.936  16.705 1.00 24.35  ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 6.625  16.723  18.002 1.00 24.66  ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 5.899  15.671  15.872 1.00 24.20  ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 3.831  18.445  19.105 1.00 26.26  ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 3.708  19.536  20.066 1.00 27.57  ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.073  20.133  20.402 1.00 27.75  ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.104  19.449  20.276 1.00 27.79  ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.006  19.061  21.360 1.00 31.87  ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.115  20.137  21.966 1.00 43.56  ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.608  19.956  23.386 1.00 55.68  ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 2.170  19.129  24.141 1.00 59.04  ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.629  20.650  23.741 1.00 59.14  ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.077  21.415  20.856 1.00 28.24  ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 6.315  22.076  21.248 1.00 28.34  ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 6.995  21.312  22.393 1.00 27.68  ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 6.314  20.752  23.261 1.00 28.49  ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.035  23.507  21.685 1.00 28.94  ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 8.318  21.282  22.385 1.00 26.62  ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 9.108  20.639  23.438 1.00 25.62  ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 10.250 21.628  23.770 1.00 26.56  ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 10.281 22.749  23.232 1.00 27.05  ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 9.686  19.304  22.935 1.00 25.73  ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 10.728 19.512  21.992 1.00 25.46  ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 11.187 21.227  24.639 1.00 26.66  ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 12.346 22.094  24.918 1.00 27.67  ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 13.296 22.161  23.720 1.00 27.44  ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 14.164 23.026  23.669 1.00 28.15  ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 13.147 21.592  26.133 1.00 33.57  ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 12.327 20.892  27.200 1.00 43.21  ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 12.158 19.408  26.929 1.00 53.40  ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 13.100 18.640  27.231 1.00 57.49  ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 11.050 19.007  26.498 1.00 53.77  ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 13.163 21.215  22.758 1.00 26.72  ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 14.068 21.109  21.627 1.00 25.87  ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 13.555 21.750  20.360 1.00 24.38  ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.354 22.191  19.537 1.00 24.53  ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 14.359 19.629  21.365 1.00 25.53  ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 14.885 18.878  22.571 1.00 26.00  ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 14.043 18.110  23.360 1.00 26.93  ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 16.220 18.948  22.930 1.00 26.05  ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 14.534 17.379  24.442 1.00 27.85  ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 16.715 18.239  24.021 1.00 26.73  ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 15.868 17.470  24.784 1.00 28.52  ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.357 16.767  25.869 1.00 31.15  ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.222 21.854  20.209 1.00 23.56  ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 11.658 22.427  18.983 1.00 23.07  ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.363 23.139  19.266 1.00 25.06  ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 9.591  22.717  20.134 1.00 25.67  ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.277 21.307  17.962 1.00 21.70  ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.382 20.382  17.487 1.00 19.67  ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.280 20.779  16.504 1.00 20.08  ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 12.482 19.087  17.962 1.00 19.89  ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.273 19.924  16.041 1.00 19.63  ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 13.470 18.217  17.498 1.00 18.31  ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.321 18.619  16.493 1.00 18.31  ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.329 17.809  16.026 1.00 17.10  ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.051 24.189  18.486 1.00 26.48  ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 8.705  24.783  18.588 1.00 27.20  ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.676  23.791  18.014 1.00 27.26  ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.038  22.829  17.324 1.00 27.79  ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 8.807  26.015  17.678 1.00 27.51  ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 9.843  25.633  16.658 1.00 28.37  ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 10.842 24.784  17.389 1.00 26.74  ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.364  24.071  18.195 1.00 26.97  ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.317  23.225  17.614 1.00 27.59  ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.489  23.233  16.070 1.00 26.46  ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.722  24.295  15.497 1.00 26.70  ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 3.945  23.778  17.994 1.00 28.78  ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.556  22.045  15.438 1.00 24.48  ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.789  21.997  13.982 1.00 23.86  ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.277  20.681  13.369 1.00 24.21  ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 4.890  19.802  14.108 1.00 25.66  ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.308  22.156  13.709 1.00 22.69  ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.050  20.851  14.124 1.00 24.55  ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.459  21.039  14.626 1.00 24.34  ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.347 19.928  14.272 1.00 23.17  ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.359 18.739  14.883 1.00 21.03  ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.243 17.810  14.526 1.00 21.20  ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.483  18.472  15.845 1.00 20.76  ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.356  20.520  12.036 1.00 23.90  ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.065  19.232  11.417 1.00 24.06  ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.410  18.544  11.261 1.00 22.58  ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.350  19.153  10.753 1.00 23.44  ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.441  19.380  10.032 1.00 25.20  ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.006  19.819  10.130 1.00 26.55  ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.679  21.165  10.221 1.00 28.08  ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 1.976  18.892  10.191 1.00 27.54  ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 1.358  21.581  10.341 1.00 30.30  ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 0.646  19.296  10.317 1.00 29.85  ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.344  20.641  10.379 1.00 31.74  ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.966 21.063  10.482 1.00 35.73  ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.516  17.305  11.737 1.00 19.90  ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.742  16.532  11.555 1.00 17.91  ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.493  15.602  10.368 1.00 16.84  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.452  14.944  10.310 1.00 18.49  ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.109  15.751  12.804 1.00 16.49  ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.359  14.843  12.599 1.00 16.72  ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 9.969  14.374  13.902 1.00 16.48  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.075 15.107  14.900 1.00 17.47  ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.476 13.105  13.917 1.00 13.94  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.368  15.634  9.370  1.00 16.07  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.201  14.803  8.186  1.00 16.25  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.881  13.434  8.351  1.00 17.62  ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.705  13.252  9.276  1.00 18.18  ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.782  15.528  6.975  1.00 18.51  ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.146 15.845  7.202  1.00 20.18  ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.505  12.471  7.456  1.00 16.91  ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.095  11.129  7.418  1.00 16.41  ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.921  10.419  8.758  1.00 15.75  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.761  9.588   9.128  1.00 15.49  ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.583 11.231  7.017  1.00 17.11  ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.783 11.863  5.658  1.00 19.62  ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.874 11.083  4.513  1.00 22.96  ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.820 13.171  5.301  1.00 20.59  ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.994 11.946  3.497  1.00 23.08  ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.998 13.205  3.926  1.00 22.63  ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.800  10.692  9.449  1.00 14.79  ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.557  10.093  10.773 1.00 15.09  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.511  8.971   10.666 1.00 14.87  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.525  9.115   9.948  1.00 15.76  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.048  11.193  11.730 1.00 16.54  ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.839  10.806  13.218 1.00 17.60  ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.196  10.390  13.909 1.00 17.40  ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.204  12.007  14.011 1.00 20.14  ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.754  7.863   11.410 1.00 14.06  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.846  6.702   11.365 1.00 14.63  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.344  6.473   12.779 1.00 15.45  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.173  6.417   13.703 1.00 16.10  ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.672  5.491   10.935 1.00 14.82  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.158  5.633   9.505  1.00 16.03  ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.331  4.363   8.992  1.00 19.55  ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.688  4.666   10.170 1.00 22.93  ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.028  6.319   12.974 1.00 15.12  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.519  6.123   14.334 1.00 15.38  ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.093  4.676   14.552 1.00 14.71  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.579  4.011   13.625 1.00 15.38  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.282  7.015   14.629 1.00 17.48  ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.505  8.504   14.589 1.00 22.27  ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.226  9.269   15.056 1.00 23.37  ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.679  8.923   15.433 1.00 21.91  ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.182  4.249   15.812 1.00 14.40  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.703  2.928   16.197 1.00 14.74  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.158  2.987   17.618 1.00 14.88  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.491  3.918   18.369 1.00 15.74  ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 3.878  1.947   16.191 1.00 14.92  ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.342  2.000   17.988 1.00 13.74  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.888  1.890   19.373 1.00 13.40  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.988  1.120   20.139 1.00 15.85  ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.354  0.001   19.780 1.00 17.50  ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.479 1.159   19.448 1.00 14.91  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.879 0.968   20.911 1.00 15.19  ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.527 1.988   18.708 1.00 16.11  ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.507  1.768   21.176 1.00 15.45  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.559  1.162   21.986 1.00 16.69  ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.060  2.157   23.022 1.00 17.45  ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.715  3.346   23.001 1.00 18.10  ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.811  1.639   23.996 1.00 16.53  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.343  2.440   25.068 1.00 16.04  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.580  3.234   24.670 1.00 16.75  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.509  2.702   24.084 1.00 16.84  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.678  1.572   26.300 1.00 16.10  ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.155  2.407   27.457 1.00 17.18  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.297  3.291   28.093 1.00 18.65  ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.413  2.582   27.955 1.00 18.05  ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.041  3.943   28.989 1.00 18.59  ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.324  3.534   28.947 1.00 18.35  ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.617  4.516   25.045 1.00 16.11  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 7.793  5.337   24.855 1.00 16.85  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 7.734  6.473   25.868 1.00 19.99  ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 6.646  6.890   26.293 1.00 22.51  ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 7.903  5.854   23.427 1.00 19.44  ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 6.810  6.713   23.164 1.00 24.27  ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 8.891  6.819   26.353 1.00 18.35  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.170  7.911   27.246 1.00 19.51  ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.283 8.724   26.623 1.00 22.34  ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.059 8.247   25.774 1.00 22.31  ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 9.717  7.344   28.586 1.00 21.46  ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 8.613  6.720   29.370 1.00 20.88  ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.020  6.070   30.687 1.00 21.32  ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 9.778  6.696   31.469 1.00 23.96  ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.574  4.927   30.925 1.00 21.99  ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.422 10.006  27.069 1.00 25.54  ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 11.631 10.733  26.717 1.00 27.36  ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 12.730 9.973   27.530 1.00 27.01  ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 12.613 9.608   28.750 1.00 31.10  ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 11.399 12.168  27.231 1.00 27.87  ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.032 12.175  27.870 1.00 28.20  ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 9.588  10.733  28.043 1.00 25.70  ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 13.722 9.685   26.757 1.00 21.69  ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 14.883 8.864   27.043 1.00 19.62  ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 14.887 7.700   26.052 1.00 17.70  ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 15.937 7.109   25.780 1.00 17.09  ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 13.680 7.271   25.555 1.00 16.52  ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 13.634 6.178   24.587 1.00 14.38  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.093 6.563   23.178 1.00 14.85  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.313 5.696   22.354 1.00 14.32  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.243 5.515   24.505 1.00 14.47  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 11.965 4.707   25.747 1.00 15.12  ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 12.918 4.089   26.271 1.00 15.65  ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 10.784 4.705   26.211 1.00 15.95  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.242 7.866   22.907 1.00 14.50  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 14.672 8.315   21.558 1.00 13.72  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.015 7.705   21.215 1.00 14.58  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 16.890 7.596   22.078 1.00 16.03  ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 14.725 9.843   21.488 1.00 13.98  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.090 10.629  21.426 1.00 17.52  ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.131 7.232   19.985 1.00 13.41  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.366 6.583   19.560 1.00 13.91  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.247 5.064   19.476 1.00 14.58  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.064 4.431   18.822 1.00 15.20  ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.236 4.472   20.128 1.00 13.36  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.006 3.024   20.010 1.00 13.17  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.729 2.622   18.570 1.00 12.77  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 14.994 3.323   17.875 1.00 13.21  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.336 1.542   18.116 1.00 12.89  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.182 1.124   16.730 1.00 11.93  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.903 0.349   16.480 1.00 12.79  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.526 -0.516  17.289 1.00 12.90  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.459 0.305   16.305 1.00 14.28  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.633 1.282   16.096 1.00 16.28  ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.224 -0.583  15.075 1.00 16.01  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.984 0.567   15.750 1.00 17.65  ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.275 0.628   15.337 1.00 11.78  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.149 -0.161  14.796 1.00 11.12  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.740 -0.941  13.631 1.00 12.85  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.384 -0.343  12.750 1.00 13.36  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.081 0.805   14.226 1.00 10.75  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.899 0.125   13.449 1.00 12.37  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.090 -0.813  14.351 1.00 13.48  ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.958  1.236   12.835 1.00 13.83  ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.532 -2.297  13.620 1.00 12.10  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 14.064 -3.155  12.557 1.00 12.85  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.953 -4.035  12.034 1.00 13.86  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 12.079 -4.492  12.768 1.00 15.35  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 15.093 -4.150  13.182 1.00 15.36  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.308 -3.562  13.803 1.00 22.46  ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.181 -4.688  14.399 1.00 23.85  ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.867 -5.278  13.272 1.00 26.78  ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 19.036 -4.861  12.817 1.00 26.13  ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.738 -3.972  13.498 1.00 24.14  ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.518 -5.343  11.693 1.00 21.99  ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 13.078 -4.359  10.766 1.00 13.32  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 12.218 -5.395  10.148 1.00 14.22  ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 13.183 -6.523  9.689  1.00 15.83  ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.392 -6.466  9.954  1.00 16.90  ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.484 -4.781  8.971  1.00 13.31  ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.584 -4.306  7.605  1.00 15.77  ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.680 -7.573  8.980  1.00 16.89  ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.540 -8.661  8.505  1.00 18.52  ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.622 -8.210  7.501  1.00 19.48  ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.578 -8.977  7.239  1.00 21.50  ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.667 -9.766  7.845  1.00 20.28  ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.998 -9.270  6.562  1.00 25.26  ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.972 -10.243 6.026  1.00 35.78  ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.746  -10.102 6.233  1.00 39.31  ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 11.456 -11.237 5.320  1.00 34.48  ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 14.522 -6.975  6.950  1.00 18.34  ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 15.493 -6.462  5.951  1.00 17.74  ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.611 -5.610  6.543  1.00 17.48  ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.595 -5.331  5.838  1.00 18.40  ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.766 -5.661  4.842  1.00 17.89  ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.647 -6.454  4.213  1.00 20.03  ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 12.318 -6.113  4.389  1.00 21.91  ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.709 -7.511  3.351  1.00 23.41  ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.608 -7.023  3.725  1.00 23.91  ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 12.399 -7.890  3.095  1.00 24.40  ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.446 -5.189  7.794  1.00 15.12  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.438 -4.335  8.423  1.00 14.74  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.826 -3.198  9.213  1.00 13.75  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.660 -3.246  9.606  1.00 15.01  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.633 -2.173  9.441  1.00 14.25  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.191 -1.010  10.224 1.00 13.12  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.211 -0.161  9.447  1.00 12.48  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.498 0.224   8.301  1.00 14.05  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.414 -0.163  10.668 1.00 14.22  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.947 1.131   11.358 1.00 14.37  ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.317 -1.008  11.595 1.00 15.53  ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 15.087 0.131   10.055 1.00 12.65  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 14.039 0.970   9.453  1.00 12.79  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.149 2.452   9.905  1.00 13.31  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.888 3.390   9.123  1.00 13.16  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.647 0.404   9.816  1.00 14.32  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.520 1.350   9.370  1.00 15.27  ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.426 -1.005  9.259  1.00 14.25  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.370 2.641   11.209 1.00 12.18  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.478 4.001   11.733 1.00 12.43  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.709 4.009   13.223 1.00 12.07  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.100 2.975   13.803 1.00 11.78  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.616 5.210   13.830 1.00 12.19  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.864 5.330   15.281 1.00 12.14  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.707 6.016   15.981 1.00 11.56  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.053 6.896   15.394 1.00 11.23  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.182 6.108   15.557 1.00 13.83  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.226 7.437   14.770 1.00 14.90  ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.415 5.233   15.301 1.00 15.90  ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.478 8.305   15.311 1.00 16.30  ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.492 5.689   17.272 1.00 11.09  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.433 6.368   18.055 1.00 11.55  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.726 7.871   18.093 1.00 11.40  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 13.868 8.254   18.310 1.00 11.94  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.413 5.823   19.500 1.00 11.82  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.399 6.624   20.362 1.00 12.47  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.041 4.323   19.513 1.00 12.16  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.705 8.701   17.809 1.00 11.76  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 11.855 10.153  17.787 1.00 12.57  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 10.749 10.869  18.576 1.00 14.45  ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 10.989 11.964  19.073 1.00 16.16  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 11.874 10.616  16.335 1.00 12.89  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 11.939 12.036  16.229 1.00 14.80  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.543  10.265  18.666 1.00 14.95  ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.448  10.913  19.434 1.00 16.10  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.700  9.847   20.282 1.00 17.47  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 7.939  8.643   20.142 1.00 15.65  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.427  11.659  18.492 1.00 18.08  ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.588  10.676  17.831 1.00 19.65  ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.090  12.605  17.478 1.00 18.91  ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 6.792  10.293  21.154 1.00 19.56  ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 5.980  9.371   21.909 1.00 21.24  ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 4.967  10.065  22.780 1.00 22.84  ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 4.730  11.257  22.636 1.00 22.69  ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.434  9.300   23.705 1.00 25.92  ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.470  9.743   24.700 1.00 26.98  ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.123  9.118   24.439 1.00 27.17  ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.833  8.726   23.316 1.00 28.02  ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.267  9.071   25.455 1.00 27.27  ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? -0.107 8.586   25.332 1.00 27.61  ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.273 7.163   24.780 1.00 24.13  ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.328 6.877   24.203 1.00 24.35  ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.885 9.575   24.427 1.00 31.90  ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.910 11.009  24.922 1.00 39.38  ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.065 11.261  26.124 1.00 41.29  ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.814 11.977  23.991 1.00 40.75  ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.701  6.262   24.962 1.00 20.87  ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.594  4.913   24.415 1.00 19.36  ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 0.965  4.843   22.936 1.00 18.45  ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.701  3.832   22.278 1.00 19.26  ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.594  5.892   22.426 1.00 16.88  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.075  5.939   21.048 1.00 15.59  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.601  6.004   21.030 1.00 16.42  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.219  6.557   21.954 1.00 18.00  ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.499  7.178   20.327 1.00 16.04  ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? -0.023 7.093   20.077 1.00 19.31  ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.627 8.474   19.785 1.00 21.53  ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.349 6.071   18.915 1.00 19.52  ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.190  5.586   19.902 1.00 13.95  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.618  5.752   19.709 1.00 13.06  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.827  6.157   18.229 1.00 13.10  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.183  5.597   17.342 1.00 14.73  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.418  4.497   20.113 1.00 14.03  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 5.882  3.251   19.412 1.00 15.99  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 7.895  4.715   19.843 1.00 14.93  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.671  7.156   18.021 1.00 13.45  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 6.948  7.613   16.664 1.00 13.41  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.386  7.358   16.281 1.00 13.63  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.284  7.631   17.071 1.00 13.47  ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.614  6.943   15.028 1.00 12.82  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.942  6.597   14.521 1.00 13.12  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.272 7.467   13.311 1.00 13.14  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.476  7.585   12.385 1.00 13.42  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.958  5.128   14.046 1.00 12.05  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.464  4.140   15.076 1.00 12.64  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.310 3.651   16.044 1.00 12.67  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.142  3.680   15.044 1.00 14.94  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.855  2.741   16.990 1.00 12.94  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.688  2.738   15.963 1.00 15.03  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.548  2.272   16.947 1.00 13.57  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.486 8.046   13.340 1.00 12.43  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.020 8.761   12.199 1.00 12.31  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.516 7.722   11.188 1.00 12.87  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.444 6.928   11.490 1.00 13.12  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.181 9.639   12.645 1.00 12.32  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.958 7.732   9.985  1.00 13.69  ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.341 6.770   8.948  1.00 14.55  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.711 7.118   8.375  1.00 14.28  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.046 8.307   8.244  1.00 14.30  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.327 6.792   7.794  1.00 18.03  ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.568 5.764   6.702  1.00 20.92  ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.763 4.593   7.030  1.00 19.01  ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.653 6.162   5.513  1.00 24.05  ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.527 6.071   8.062  1.00 13.03  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.799 6.305   7.380  1.00 13.61  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.895 5.543   6.056  1.00 13.85  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.932 5.630   5.387  1.00 15.58  ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.045 5.989   8.235  1.00 14.84  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.082 6.858   9.519  1.00 15.12  ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.113 4.501   8.581  1.00 15.12  ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.855 4.762   5.667  1.00 14.28  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.948 3.903   4.481  1.00 14.21  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 15.105 4.620   3.173  1.00 17.29  ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.606 4.029   2.205  1.00 19.06  ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.732 2.940   4.413  1.00 13.49  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.670 1.956   5.593  1.00 15.66  ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.372 1.156   5.493  1.00 16.14  ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.243 2.011   5.821  1.00 16.79  ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.991  1.595   5.938  1.00 18.72  ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.673  0.321   5.657  1.00 17.22  ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 9.044  2.436   6.340  1.00 17.67  ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.705 5.912   3.138  1.00 16.49  ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.835 6.668   1.897  1.00 17.59  ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 16.236 7.270   1.714  1.00 17.96  ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.506 7.808   0.638  1.00 19.09  ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.790 7.801   1.861  1.00 18.36  ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.984 8.836   2.959  1.00 21.47  ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.201 8.432   4.132  1.00 20.03  ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.892 10.057  2.655  1.00 24.17  ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.105 7.218   2.725  1.00 16.55  ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.453 7.832   2.661  1.00 16.48  ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.408 6.873   1.991  1.00 17.07  ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 20.197 6.157   2.644  1.00 16.71  ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.904 8.213   4.080  1.00 15.52  ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.926 9.158   4.813  1.00 17.28  ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.366 9.379   6.254  1.00 17.77  ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.738 10.494  4.073  1.00 18.89  ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 19.298 6.785   0.652  1.00 18.01  ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 20.066 5.771   -0.081 1.00 20.18  ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.578 5.926   0.001  1.00 20.94  ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 22.319 4.917   -0.046 1.00 21.00  ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.619 5.684   -1.552 1.00 20.78  ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 18.100 5.603   -1.787 1.00 21.96  ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.822 5.341   -3.275 1.00 23.53  ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.439 4.462   -0.951 1.00 22.35  ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 22.030 7.186   0.191  1.00 20.54  ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.449 7.513   0.289  1.00 21.29  ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 24.119 6.925   1.531  1.00 22.14  ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.354 6.863   1.570  1.00 23.32  ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.688 9.036   0.186  1.00 21.28  ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.858 9.845   1.157  1.00 21.55  ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.611 10.378  0.951  1.00 21.59  ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 23.217 10.173  2.503  1.00 21.45  ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 21.192 11.043  2.082  1.00 22.06  ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 22.164 10.942  3.045  1.00 22.12  ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.353 9.931   3.284  1.00 21.96  ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.218 11.477  4.342  1.00 22.66  ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.416 10.482  4.557  1.00 22.47  ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.352 11.239  5.069  1.00 22.54  ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.341 6.469   2.544  1.00 20.92  ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.948 5.899   3.750  1.00 22.40  ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.809 4.668   3.440  1.00 26.42  ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.701 4.344   4.225  1.00 26.13  ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.888 5.515   4.795  1.00 21.10  ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.222 6.651   5.528  1.00 19.63  ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.109 6.125   6.423  1.00 19.86  ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.256 7.464   6.397  1.00 19.27  ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.501 3.936   2.340  1.00 30.83  ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 25.308 2.764   1.987  1.00 36.28  ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.747 2.743   0.536  1.00 41.36  ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.050 1.664   0.025  1.00 42.96  ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 24.625 1.442   2.362  1.00 39.52  ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 23.141 1.403   2.096  1.00 44.94  ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 22.379 1.186   3.054  1.00 46.89  ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 22.739 1.647   0.948  1.00 46.63  ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.749 3.911   -0.144 1.00 43.71  ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.130 4.015   -1.551 1.00 46.44  ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.634 4.168   -1.628 1.00 48.27  ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.130 5.254   -1.340 1.00 49.61  ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 25.473 5.245   -2.210 1.00 49.93  ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 24.166 4.945   -2.926 1.00 56.62  ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 23.651 6.089   -3.780 1.00 66.11  ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 23.982 6.124   -4.988 1.00 69.13  ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 22.918 6.951   -3.242 1.00 68.59  ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 15.205 -23.735 8.571  1.00 24.57  ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 14.074 -23.605 9.503  1.00 24.80  ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 14.058 -24.762 10.511 1.00 23.30  ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 14.734 -25.777 10.305 1.00 24.17  ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 12.752 -23.568 8.732  1.00 27.76  ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 12.560 -24.811 8.068  1.00 31.95  ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 13.306 -24.600 11.598 1.00 20.62  ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 13.171 -25.635 12.617 1.00 20.03  ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 12.914 -25.058 13.991 1.00 18.77  ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 13.348 -23.940 14.288 1.00 19.06  ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 12.248 -25.804 14.849 1.00 18.09  ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 11.907 -25.375 16.203 1.00 18.84  ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 12.006 -26.535 17.199 1.00 16.88  ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 11.926 -27.696 16.812 1.00 18.18  ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 10.470 -24.824 16.208 1.00 20.01  ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 12.065 -26.214 18.505 1.00 15.39  ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 11.971 -27.164 19.601 1.00 15.56  ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 10.613 -26.939 20.287 1.00 16.72  ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 10.216 -25.810 20.539 1.00 17.15  ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 13.086 -26.920 20.637 1.00 15.77  ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 14.468 -26.976 19.977 1.00 15.98  ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 12.987 -27.912 21.784 1.00 17.44  ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 15.535 -26.377 20.927 1.00 16.04  ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 9.858  -28.017 20.517 1.00 18.21  ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 8.553  -27.961 21.153 1.00 18.41  ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 8.608  -28.676 22.486 1.00 19.75  ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 8.759  -29.900 22.511 1.00 20.42  ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 7.497  -28.613 20.237 1.00 18.81  ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 7.297  -27.836 18.947 1.00 18.53  ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 6.433  -26.750 18.890 1.00 19.64  ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 8.040  -28.132 17.812 1.00 18.82  ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 6.282  -26.011 17.724 1.00 21.62  ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 7.903  -27.392 16.641 1.00 20.33  ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 7.005  -26.349 16.593 1.00 21.77  ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 6.888  -25.611 15.436 1.00 24.68  ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 8.548  -27.939 23.594 1.00 20.33  ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 8.655  -28.544 24.917 1.00 21.25  ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 7.574  -27.934 25.805 1.00 21.77  ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 7.464  -26.710 25.927 1.00 21.14  ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 10.095 -28.361 25.513 1.00 22.64  ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 10.543 -26.904 25.420 1.00 23.75  ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 10.165 -28.863 26.955 1.00 23.22  ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 6.685  -28.770 26.349 1.00 23.48  ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 5.598  -28.282 27.197 1.00 24.02  ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 4.714  -27.330 26.415 1.00 24.73  ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 4.418  -27.611 25.256 1.00 25.46  ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 4.454  -26.136 26.938 1.00 24.24  ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 3.666  -25.150 26.185 1.00 24.46  ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 4.552  -24.057 25.571 1.00 22.03  ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 4.102  -22.919 25.388 1.00 22.06  ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 2.554  -24.559 27.034 1.00 27.99  ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 1.424  -25.533 27.241 1.00 36.23  ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 0.816  -26.035 26.279 1.00 39.07  ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 1.123  -25.822 28.496 1.00 37.22  ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 5.776  -24.436 25.152 1.00 20.22  ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 6.723  -23.506 24.545 1.00 19.69  ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 7.228  -23.994 23.187 1.00 18.39  ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 7.366  -25.209 22.957 1.00 18.22  ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 7.967  -23.359 25.442 1.00 19.68  ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 7.674  -22.796 26.815 1.00 20.43  ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 7.013  -21.581 26.963 1.00 21.71  ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 8.094  -23.453 27.962 1.00 21.52  ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 6.734  -21.063 28.222 1.00 23.78  ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 7.840  -22.930 29.229 1.00 23.29  ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 7.164  -21.729 29.353 1.00 24.83  ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 6.910  -21.178 30.599 1.00 27.28  ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 7.517  -23.029 22.307 1.00 16.53  ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 8.136  -23.231 20.989 1.00 16.04  ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 9.421  -22.379 20.999 1.00 16.23  ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 9.365  -21.170 21.257 1.00 17.37  ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 7.198  -22.758 19.872 1.00 17.63  ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 7.825  -22.579 18.487 1.00 18.62  ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 6.780  -22.199 17.442 1.00 20.28  ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 7.237  -21.227 16.438 1.00 21.02  ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 7.642  -21.518 15.199 1.00 24.54  ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 7.721  -22.784 14.794 1.00 23.58  ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 8.021  -20.546 14.370 1.00 23.95  ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 10.582 -23.023 20.785 1.00 15.78  ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 11.877 -22.336 20.768 1.00 14.72  ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 12.350 -22.241 19.305 1.00 15.05  ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 12.470 -23.279 18.626 1.00 16.08  ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 12.956 -23.132 21.559 1.00 15.78  ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 14.244 -22.267 21.678 1.00 15.80  ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 12.427 -23.546 22.940 1.00 16.39  ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 12.574 -21.016 18.813 1.00 13.79  ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 13.013 -20.841 17.417 1.00 13.20  ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 14.223 -19.887 17.374 1.00 12.59  ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 14.498 -19.162 18.344 1.00 13.41  ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 11.854 -20.216 16.591 1.00 16.73  ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 10.726 -21.222 16.403 1.00 19.75  ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 11.348 -18.909 17.217 1.00 17.15  ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 14.915 -19.799 16.203 1.00 12.21  ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 15.965 -18.771 16.041 1.00 12.41  ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 15.207 -17.422 16.070 1.00 13.41  ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 14.214 -17.244 15.341 1.00 15.00  ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 16.602 -18.861 14.655 1.00 12.35  ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.459 -20.118 14.531 1.00 15.37  ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 16.983 -21.181 14.061 1.00 14.39  ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 18.697 -20.044 14.965 1.00 14.02  ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 15.707 -16.450 16.879 1.00 12.45  ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 15.028 -15.155 16.941 1.00 13.05  ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 14.885 -14.515 15.561 1.00 14.09  ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 13.851 -13.889 15.269 1.00 15.05  ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 15.770 -14.246 17.918 1.00 13.61  ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 14.997 -12.957 18.293 1.00 14.98  ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 15.958 -12.049 19.046 1.00 15.54  ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 15.379 -10.799 19.570 1.00 16.38  ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 15.260 -9.682  18.877 1.00 18.71  ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 15.630 -9.638  17.601 1.00 18.22  ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 14.826 -8.571  19.467 1.00 18.72  ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 15.916 -14.657 14.704 1.00 14.01  ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 15.841 -14.006 13.387 1.00 14.73  ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 14.803 -14.625 12.432 1.00 16.24  ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 14.427 -13.979 11.429 1.00 18.16  ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.223 -13.910 12.726 1.00 15.03  ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 17.786 -15.205 12.211 1.00 15.53  ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 18.503 -16.078 13.034 1.00 16.17  ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 17.825 -15.672 10.942 1.00 16.42  ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 18.894 -17.079 12.250 1.00 17.19  ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 18.553 -16.855 10.974 1.00 18.10  ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 14.300 -15.811 12.761 1.00 16.11  ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 13.281 -16.484 11.939 1.00 15.98  ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 11.890 -16.473 12.591 1.00 17.40  ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 10.962 -17.122 12.096 1.00 18.22  ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 13.736 -17.956 11.678 1.00 16.36  ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 15.043 -18.056 10.848 1.00 17.67  ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 15.441 -19.534 10.655 1.00 18.67  ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 14.928 -17.310 9.477  1.00 18.50  ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 11.748 -15.815 13.761 1.00 16.47  ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 10.467 -15.782 14.479 1.00 17.47  ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 9.394  -15.139 13.608 1.00 17.69  ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 9.680  -14.195 12.887 1.00 19.06  ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 10.611 -14.970 15.757 1.00 17.15  ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 8.169  -15.711 13.647 1.00 18.11  ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 7.047  -15.210 12.840 1.00 18.56  ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 6.247  -14.118 13.579 1.00 19.42  ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 6.447  -13.909 14.781 1.00 19.40  ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 6.110  -16.403 12.527 1.00 19.89  ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 5.511  -16.846 13.760 1.00 22.15  ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 6.825  -17.521 11.852 1.00 20.01  ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 5.233  -13.486 12.910 1.00 20.24  ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 4.350  -12.547 13.607 1.00 20.85  ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 3.669  -13.228 14.786 1.00 20.58  ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 3.567  -12.653 15.868 1.00 20.96  ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 3.250  -12.025 12.641 1.00 24.03  ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 3.799  -11.184 11.534 1.00 31.81  ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 4.533  -10.036 11.796 1.00 35.27  ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 3.688  -11.332 10.191 1.00 35.23  ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 4.835  -9.519  10.613 1.00 36.48  ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 4.353  -10.264 9.617  1.00 36.33  ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 3.253  -14.505 14.580 1.00 19.52  ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 2.570  -15.228 15.653 1.00 20.11  ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 3.509  -15.464 16.820 1.00 19.30  ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 3.078  -15.364 17.977 1.00 19.44  ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 2.025  -16.547 15.139 1.00 23.09  ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 1.175  -17.241 16.171 1.00 29.38  ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? 0.115  -16.739 16.546 1.00 31.03  ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 1.647  -18.389 16.682 1.00 30.99  ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 4.796  -15.785 16.535 1.00 18.82  ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 5.755  -15.964 17.650 1.00 19.04  ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 5.884  -14.672 18.483 1.00 18.37  ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 5.866  -14.718 19.712 1.00 19.03  ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 7.146  -16.315 17.126 1.00 18.67  ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 7.244  -17.736 16.611 1.00 19.60  ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 6.613  -18.628 17.221 1.00 19.69  ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 7.913  -17.938 15.560 1.00 18.77  ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 5.945  -13.509 17.822 1.00 18.46  ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 6.071  -12.246 18.545 1.00 19.18  ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 4.769  -11.853 19.285 1.00 19.93  ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 4.844  -11.246 20.358 1.00 20.48  ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 6.517  -11.139 17.581 1.00 19.57  ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 8.005  -11.126 17.391 1.00 17.44  ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 8.695  -11.544 16.293 1.00 18.40  ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 8.970  -10.535 18.281 1.00 16.28  ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 10.043 -11.292 16.458 1.00 18.77  ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 10.239 -10.678 17.675 1.00 17.84  ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 8.886  -9.934  19.538 1.00 17.19  ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 11.411 -10.215 18.277 1.00 17.62  ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 10.056 -9.488  20.141 1.00 17.08  ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 11.299 -9.660  19.516 1.00 17.05  ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 3.606  -12.260 18.754 1.00 19.46  ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 2.325  -11.956 19.421 1.00 21.01  ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 2.114  -12.830 20.665 1.00 21.88  ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 1.247  -12.522 21.487 1.00 22.97  ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 1.159  -12.169 18.452 1.00 21.31  ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 2.817  -13.974 20.748 1.00 20.56  ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 2.734  -14.917 21.872 1.00 19.86  ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 4.106  -15.035 22.554 1.00 19.75  ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 4.491  -16.098 23.014 1.00 19.39  ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 2.233  -16.279 21.380 1.00 19.86  ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 0.803  -16.160 20.889 1.00 24.76  ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? -0.142 -16.087 21.689 1.00 24.05  ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 0.626  -16.116 19.563 1.00 25.16  ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 4.830  -13.911 22.638 1.00 20.01  ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 6.174  -13.887 23.189 1.00 19.35  ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 6.250  -14.256 24.663 1.00 19.57  ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 5.479  -13.735 25.477 1.00 21.12  ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 6.754  -12.486 22.965 1.00 19.82  ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 8.157  -12.254 23.497 1.00 20.58  ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 9.181  -13.148 22.750 1.00 20.34  ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 8.538  -10.787 23.332 1.00 20.32  ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 7.200  -15.156 25.019 1.00 17.65  ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 7.484  -15.529 26.405 1.00 18.42  ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 8.824  -14.870 26.815 1.00 18.95  ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 8.938  -14.216 27.866 1.00 20.58  ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 7.546  -17.071 26.586 1.00 20.23  ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 8.098  -17.437 27.973 1.00 21.03  ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 6.159  -17.692 26.361 1.00 21.22  ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 9.836  -15.025 25.954 1.00 17.66  ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 11.180 -14.540 26.217 1.00 16.66  ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 11.955 -14.466 24.912 1.00 16.36  ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 11.748 -15.304 24.026 1.00 17.31  ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 11.882 -15.531 27.201 1.00 17.14  ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 13.360 -15.315 27.401 1.00 18.26  ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 13.966 -14.424 28.240 1.00 20.28  ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 14.419 -16.048 26.758 1.00 17.98  ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 15.345 -14.534 28.130 1.00 21.17  ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 15.643 -15.525 27.225 1.00 19.59  ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 14.448 -17.071 25.788 1.00 18.08  ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 16.889 -16.077 26.836 1.00 18.84  ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 15.674 -17.619 25.425 1.00 18.30  ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 16.875 -17.067 25.882 1.00 17.95  ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 12.843 -13.476 24.792 1.00 15.25  ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 13.726 -13.433 23.620 1.00 16.05  ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 15.044 -12.806 24.042 1.00 15.98  ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 15.098 -12.025 24.997 1.00 16.46  ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 13.114 -12.662 22.430 1.00 17.14  ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 12.555 -11.274 22.765 1.00 17.78  ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 13.569 -10.144 22.893 1.00 20.02  ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 13.331 -9.183  23.666 1.00 23.17  ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 14.596 -10.187 22.180 1.00 18.18  ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 16.114 -13.176 23.337 1.00 14.97  ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.434 -12.630 23.656 1.00 14.60  ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 18.221 -12.498 22.348 1.00 15.06  ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 18.663 -13.501 21.763 1.00 15.62  ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 18.159 -13.547 24.674 1.00 15.67  ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 19.474 -13.000 25.186 1.00 21.26  ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 20.136 -12.278 24.444 1.00 23.59  ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 19.863 -13.360 26.322 1.00 21.58  ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 18.373 -11.236 21.880 1.00 14.65  ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 19.068 -10.965 20.642 0.50 15.27  ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 19.084 -10.982 20.629 0.50 15.39  ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 20.522 -11.465 20.696 1.00 16.45  ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 21.026 -11.954 19.692 1.00 16.47  ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 19.018 -9.466  20.353 0.50 17.58  ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 19.101 -9.492  20.291 0.50 18.08  ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 19.735 -9.142  19.177 0.50 19.77  ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 17.831 -8.929  20.060 0.50 20.71  ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 21.172 -11.339 21.868 1.00 15.75  ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 22.555 -11.777 21.990 1.00 16.80  ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 22.703 -13.280 21.829 1.00 16.73  ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 23.815 -13.712 21.535 1.00 18.62  ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 23.184 -11.307 23.301 1.00 21.39  ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 22.789 -12.110 24.402 1.00 25.15  ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 21.617 -14.067 21.997 1.00 13.83  ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 21.688 -15.540 21.846 1.00 13.46  ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 21.049 -16.018 20.522 1.00 13.16  ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 21.065 -17.214 20.218 1.00 14.02  ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 20.939 -16.224 23.034 1.00 14.33  ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 21.654 -15.971 24.353 1.00 14.66  ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 20.926 -16.627 25.542 1.00 14.99  ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 20.955 -18.096 25.438 1.00 13.84  ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 20.910 -18.911 26.490 1.00 14.72  ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 20.837 -18.414 27.732 1.00 17.01  ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 20.972 -20.235 26.316 1.00 15.52  ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 20.379 -15.110 19.787 1.00 13.99  ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 19.582 -15.510 18.611 1.00 13.18  ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 18.472 -16.471 18.976 1.00 11.86  ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 18.084 -17.325 18.162 1.00 13.62  ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 20.411 -16.039 17.422 1.00 13.52  ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 19.622 -16.328 16.154 1.00 14.57  ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 18.744 -15.481 15.775 1.00 15.54  ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 19.870 -17.395 15.507 1.00 14.61  ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 17.889 -16.312 20.188 1.00 12.57  ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 16.755 -17.180 20.579 1.00 12.32  ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 15.462 -16.416 20.856 1.00 13.86  ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 15.492 -15.338 21.435 1.00 14.68  ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 17.064 -18.004 21.850 1.00 12.35  ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 18.130 -19.080 21.707 1.00 13.33  ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 18.318 -19.752 23.077 1.00 13.66  ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 17.675 -20.178 20.709 1.00 13.93  ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 14.330 -17.060 20.550 1.00 12.90  ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 13.032 -16.524 20.923 1.00 13.53  ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 12.145 -17.708 21.310 1.00 13.27  ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 12.214 -18.771 20.688 1.00 14.98  ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 12.396 -15.702 19.785 1.00 13.90  ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 11.005 -15.081 20.097 1.00 14.26  ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 10.810 -13.746 19.331 1.00 15.19  ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 9.838  -16.046 19.713 1.00 16.06  ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 11.393 -17.559 22.420 1.00 13.16  ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 10.466 -18.588 22.878 1.00 14.94  ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 9.040  -17.987 22.870 1.00 15.91  ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 8.817  -16.903 23.439 1.00 15.43  ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 10.839 -19.099 24.301 1.00 16.10  ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 9.810  -20.121 24.825 1.00 17.92  ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 12.252 -19.691 24.301 1.00 15.72  ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 8.106  -18.720 22.257 1.00 15.88  ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 6.705  -18.296 22.239 1.00 17.33  ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 5.813  -19.379 22.904 1.00 18.74  ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 6.248  -20.521 23.105 1.00 18.21  ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 6.272  -17.998 20.806 1.00 18.62  ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 6.354  -19.142 19.968 1.00 20.56  ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 4.586  -18.992 23.290 1.00 19.60  ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 3.677  -19.947 23.920 1.00 21.93  ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 2.829  -20.679 22.853 1.00 24.08  ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 2.539  -20.134 21.778 1.00 23.89  ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 2.784  -19.250 24.938 1.00 24.06  ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 2.090  -18.197 24.295 1.00 27.17  ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 2.483  -21.942 23.143 1.00 25.39  ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 1.678  -22.779 22.243 1.00 28.17  ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 0.423  -23.282 22.991 1.00 31.81  ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 0.393  -23.307 24.226 1.00 32.20  ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 2.493  -24.026 21.805 1.00 29.66  ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 2.715  -24.835 22.964 1.00 31.56  ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 3.829  -23.668 21.157 1.00 29.85  ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? -0.580 -23.734 22.243 1.00 34.32  ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? -1.784 -24.332 22.824 1.00 37.01  ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? -1.612 -25.846 22.984 1.00 38.28  ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? -2.170 -26.433 23.918 1.00 39.85  ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? -2.996 -23.997 21.960 1.00 39.84  ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? -2.697 -24.324 20.596 1.00 42.50  ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? -3.388 -22.527 22.070 1.00 40.61  ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? -0.848 -26.484 22.079 1.00 37.40  ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? -0.597 -27.924 22.119 1.00 37.35  ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 0.648  -28.252 22.944 1.00 37.02  ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 1.576  -27.448 23.015 1.00 36.89  ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? -0.432 -28.466 20.705 1.00 37.47  ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 0.677  -29.441 23.533 1.00 36.35  ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 1.779  -29.909 24.363 1.00 36.18  ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 2.935  -30.419 23.494 1.00 34.75  ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 2.742  -31.263 22.624 1.00 35.65  ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 1.280  -31.033 25.286 1.00 38.78  ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 2.357  -31.658 26.172 1.00 44.38  ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 2.689  -30.825 27.394 1.00 51.79  ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 1.995  -29.862 27.746 1.00 53.60  ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 3.759  -31.192 28.083 1.00 53.92  ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 4.134  -29.913 23.768 1.00 31.97  ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 5.345  -30.315 23.062 1.00 30.16  ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 5.972  -31.494 23.770 1.00 28.33  ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 5.904  -31.586 25.005 1.00 28.94  ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 6.584  -32.387 23.011 1.00 26.43  ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 7.134  -33.590 23.589 1.00 25.80  ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 8.637  -33.729 23.454 1.00 24.57  ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 9.142  -34.833 23.712 1.00 25.17  ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 6.412  -34.815 23.040 1.00 28.16  ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 4.676  -34.904 23.526 1.00 33.67  ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 9.365  -32.657 23.088 1.00 21.75  ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 10.831 -32.781 23.021 1.00 21.12  ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 11.392 -32.785 24.441 1.00 21.86  ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 10.857 -32.123 25.344 1.00 22.96  ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 11.477 -31.629 22.220 1.00 21.95  ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 11.132 -31.634 20.740 1.00 26.18  ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 10.755 -32.690 20.228 1.00 26.90  ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 11.186 -30.558 20.108 1.00 25.22  ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 12.422 -33.564 24.648 1.00 20.64  ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 13.100 -33.600 25.938 1.00 21.83  ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 14.347 -32.702 25.802 1.00 18.93  ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 15.080 -32.877 24.847 1.00 19.39  ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 13.568 -35.046 26.252 1.00 25.70  ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 12.416 -35.857 26.565 1.00 28.92  ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 14.551 -35.091 27.421 1.00 26.32  ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 14.599 -31.787 26.738 1.00 18.02  ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 15.785 -30.953 26.718 1.00 16.94  ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 16.904 -31.646 27.498 1.00 16.54  ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 16.687 -32.091 28.650 1.00 16.84  ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 15.523 -29.552 27.309 1.00 18.31  ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 14.294 -28.884 26.682 1.00 20.13  ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 16.781 -28.652 27.228 1.00 18.33  ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 14.435 -28.650 25.188 1.00 21.10  ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 18.089 -31.698 26.925 1.00 14.90  ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 19.241 -32.273 27.627 1.00 13.78  ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 19.652 -31.354 28.781 1.00 13.59  ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 19.614 -30.135 28.633 1.00 12.82  ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 20.414 -32.388 26.652 1.00 13.36  ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 20.075 -31.946 29.932 1.00 13.30  ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 20.561 -31.165 31.093 1.00 14.05  ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 21.911 -31.830 31.399 1.00 15.48  ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 21.991 -32.801 32.164 1.00 16.99  ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 19.580 -31.292 32.274 1.00 15.29  ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 18.183 -30.746 31.969 1.00 16.27  ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 18.123 -29.278 31.536 1.00 18.60  ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 16.738 -28.881 31.247 1.00 18.80  ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 16.388 -27.740 30.653 1.00 20.98  ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.315 -26.889 30.242 1.00 18.25  ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 15.106 -27.451 30.455 1.00 22.28  ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 23.000 -31.278 30.807 1.00 14.82  ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 24.290 -31.947 30.805 1.00 16.12  ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 25.422 -31.005 30.287 1.00 16.62  ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 25.125 -29.906 29.824 1.00 15.67  ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 24.147 -33.138 29.860 1.00 15.70  ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 24.005 -32.662 28.096 1.00 14.58  ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 26.668 -31.514 30.260 1.00 16.03  ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 27.800 -30.823 29.659 1.00 17.06  ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 28.406 -31.627 28.503 1.00 16.96  ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 29.599 -31.466 28.206 1.00 17.52  ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 28.881 -30.457 30.695 1.00 19.81  ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 29.500 -31.637 31.377 1.00 23.49  ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 29.125 -32.798 31.049 1.00 24.48  ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 30.398 -31.422 32.221 1.00 29.78  ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 27.595 -32.439 27.781 1.00 14.84  ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 28.074 -33.161 26.602 1.00 14.27  ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 28.737 -32.246 25.627 1.00 13.99  ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 28.279 -31.087 25.431 1.00 13.53  ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 26.913 -33.880 25.903 1.00 15.21  ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 26.384 -35.397 26.736 1.00 16.67  ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 29.757 -32.779 24.975 1.00 13.85  ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 30.446 -32.151 23.861 1.00 14.06  ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 30.439 -33.007 22.639 1.00 12.93  ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 31.236 -32.770 21.706 1.00 13.73  ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 31.864 -31.682 24.222 1.00 14.84  ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 31.869 -30.380 25.099 1.00 16.70  ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 33.281 -29.955 25.394 1.00 19.49  ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 33.778 -30.157 26.519 1.00 20.97  ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 33.985 -29.484 24.363 1.00 17.05  ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 29.563 -34.032 22.563 1.00 13.32  ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 29.398 -34.829 21.347 1.00 14.82  ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 27.909 -35.046 21.149 1.00 14.58  ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 27.131 -35.115 22.118 1.00 15.53  ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 30.120 -36.182 21.399 1.00 19.90  ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 29.525 -37.004 22.416 1.00 23.25  ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 31.619 -36.044 21.659 1.00 20.53  ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 27.504 -35.061 19.883 1.00 13.92  ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 26.091 -35.279 19.568 1.00 13.82  ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 25.879 -35.383 18.075 1.00 12.30  ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 26.843 -35.600 17.339 1.00 13.33  ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 24.620 -35.229 17.640 1.00 11.42  ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 24.300 -35.373 16.212 1.00 10.81  ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 23.400 -34.179 15.845 1.00 11.09  ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 22.426 -33.935 16.557 1.00 11.77  ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 23.535 -36.712 15.980 1.00 12.36  ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 23.044 -36.829 14.516 1.00 14.34  ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 24.432 -37.894 16.324 1.00 12.64  ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 23.633 -33.566 14.682 1.00 11.29  ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 22.731 -32.482 14.231 1.00 11.22  ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 22.114 -32.769 12.869 1.00 11.93  ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 22.696 -33.493 12.050 1.00 12.37  ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 23.423 -31.071 14.243 1.00 11.43  ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 24.352 -30.795 13.065 1.00 11.15  ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 25.638 -31.335 13.022 1.00 14.19  ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 23.973 -29.927 12.039 1.00 11.91  ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 26.511 -31.063 11.956 1.00 15.00  ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 24.826 -29.662 10.963 1.00 13.40  ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 26.105 -30.213 10.937 1.00 14.93  ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 26.957 -29.927 9.887  1.00 17.26  ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 20.959 -32.153 12.606 1.00 12.76  ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 20.308 -32.284 11.321 1.00 13.32  ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 20.716 -31.137 10.417 1.00 13.42  ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 20.586 -29.961 10.777 1.00 13.16  ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 18.769 -32.384 11.464 1.00 13.82  ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 18.127 -32.531 10.108 1.00 15.49  ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 18.278 -33.700 9.375  1.00 17.13  ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.415 -31.488 9.540  1.00 17.87  ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 17.739 -33.834 8.091  1.00 18.88  ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 16.863 -31.612 8.263  1.00 19.04  ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 17.010 -32.796 7.556  1.00 19.83  ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 16.481 -32.960 6.279  1.00 22.91  ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 21.220 -31.495 9.217  1.00 13.96  ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 21.639 -30.515 8.212  1.00 15.15  ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 20.684 -30.570 7.001  1.00 16.59  ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 20.784 -31.476 6.153  1.00 17.44  ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 23.078 -30.806 7.830  1.00 15.62  ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 23.706 -29.788 6.462  1.00 17.67  ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 19.730 -29.584 6.923  1.00 15.90  ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 18.757 -29.630 5.846  1.00 18.45  ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 19.353 -29.513 4.459  1.00 18.29  ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 18.838 -30.144 3.522  1.00 19.58  ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 17.664 -28.580 6.030  1.00 22.77  ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 18.203 -27.280 6.025  1.00 30.44  ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 20.446 -28.764 4.324  1.00 17.34  ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 21.079 -28.611 2.992  1.00 18.28  ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 21.783 -29.867 2.474  1.00 19.25  ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 22.236 -29.891 1.313  1.00 19.78  ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 22.024 -27.417 2.995  1.00 19.01  ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 23.146 -27.638 3.818  1.00 18.42  ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 21.854 -30.918 3.287  1.00 18.08  ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 22.358 -32.209 2.877  1.00 17.90  ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 21.309 -33.330 3.086  1.00 19.03  ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 21.614 -34.495 2.818  1.00 20.00  ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 23.659 -32.557 3.632  1.00 19.19  ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 24.806 -31.601 3.347  1.00 19.61  ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 25.396 -31.867 1.960  1.00 20.43  ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 26.544 -30.995 1.692  1.00 24.92  ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 26.465 -29.805 1.113  1.00 29.46  ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 25.290 -29.338 0.689  1.00 30.40  ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 27.563 -29.084 0.916  1.00 29.02  ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 20.107 -33.013 3.665  1.00 19.81  ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 19.084 -34.011 4.047  1.00 20.47  ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 19.748 -35.130 4.855  1.00 20.63  ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 19.522 -36.310 4.603  1.00 21.54  ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 18.368 -34.591 2.802  1.00 23.28  ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 17.393 -33.591 2.196  1.00 28.15  ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 16.590 -34.266 1.099  1.00 35.43  ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 15.974 -33.293 0.196  1.00 42.07  ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 16.125 -33.298 -1.125 1.00 47.67  ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 16.887 -34.216 -1.712 1.00 48.38  ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 15.541 -32.362 -1.872 1.00 48.66  ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 20.634 -34.736 5.821  1.00 18.82  ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 21.396 -35.754 6.537  1.00 18.98  ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 21.653 -35.313 7.949  1.00 16.73  ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 21.804 -34.115 8.189  1.00 16.04  ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 22.818 -35.901 5.887  1.00 23.28  ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 22.965 -36.902 4.759  1.00 33.32  ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 24.443 -36.952 4.350  1.00 40.70  ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 24.823 -38.147 3.495  1.00 47.88  ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 24.073 -38.189 2.211  1.00 50.94  ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 21.901 -36.283 8.811  1.00 15.36  ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 22.357 -35.985 10.168 1.00 14.12  ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 23.848 -36.284 10.243 1.00 15.96  ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 24.341 -37.241 9.610  1.00 18.38  ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 21.662 -36.912 11.173 1.00 14.52  ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 20.180 -36.707 11.254 1.00 16.03  ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 19.580 -35.970 12.282 1.00 18.19  ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 19.203 -37.256 10.497 1.00 17.12  ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 18.268 -36.077 12.069 1.00 16.67  ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 18.003 -36.820 11.023 1.00 19.16  ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 24.597 -35.443 10.988 1.00 13.58  ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 26.036 -35.646 11.136 1.00 13.61  ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 26.415 -35.702 12.629 1.00 13.67  ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 25.987 -34.875 13.443 1.00 14.03  ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 26.814 -34.451 10.543 1.00 14.76  ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 26.728 -34.345 9.042  1.00 16.35  ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 27.469 -35.185 8.225  1.00 17.44  ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 25.964 -33.349 8.435  1.00 17.72  ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 27.416 -35.072 6.835  1.00 18.46  ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 25.896 -33.241 7.047  1.00 18.80  ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 26.623 -34.106 6.257  1.00 20.14  ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 26.597 -33.976 4.876  1.00 22.66  ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 27.294 -36.667 12.975 1.00 13.09  ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 27.807 -36.715 14.343 1.00 12.86  ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 28.947 -35.691 14.454 1.00 14.25  ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 29.778 -35.604 13.517 1.00 16.14  ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 28.335 -38.153 14.474 1.00 13.64  ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 28.668 -38.571 13.068 1.00 14.72  ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 27.839 -37.752 12.116 1.00 13.87  ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 29.002 -34.955 15.554 1.00 13.71  ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 30.069 -33.953 15.714 1.00 14.51  ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 30.477 -33.828 17.160 1.00 13.41  ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 29.691 -34.074 18.091 1.00 14.06  ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 29.582 -32.550 15.250 1.00 16.10  ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 29.445 -32.458 13.714 1.00 18.34  ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 28.310 -32.119 15.978 1.00 16.06  ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 31.711 -33.338 17.361 1.00 12.98  ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 32.212 -32.838 18.626 1.00 13.97  ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 31.935 -31.295 18.578 1.00 13.71  ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 32.011 -30.663 17.502 1.00 15.63  ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 33.740 -33.043 18.724 1.00 16.96  ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 34.037 -34.426 18.800 1.00 21.48  ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 31.522 -30.710 19.719 1.00 12.78  ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 31.219 -29.262 19.726 1.00 13.98  ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 31.782 -28.585 20.973 1.00 14.11  ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 32.022 -29.254 21.991 1.00 15.22  ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 29.708 -28.980 19.536 1.00 13.61  ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 28.793 -29.707 20.502 1.00 12.88  ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 28.290 -30.962 20.199 1.00 13.10  ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 28.402 -29.115 21.682 1.00 13.46  ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 27.435 -31.624 21.084 1.00 13.45  ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 27.550 -29.760 22.557 1.00 14.05  ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 27.061 -31.018 22.260 1.00 13.06  ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 31.992 -27.268 20.904 1.00 13.72  ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 32.638 -26.577 22.012 1.00 14.76  ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 31.703 -26.296 23.202 1.00 15.31  ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 30.520 -26.630 23.168 1.00 15.68  ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 33.308 -25.302 21.506 1.00 15.30  ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 32.359 -24.353 21.052 1.00 15.53  ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 32.250 -25.698 24.254 1.00 15.42  ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 31.417 -25.286 25.382 1.00 16.52  ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 30.722 -23.948 25.028 1.00 15.65  ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 31.295 -23.128 24.318 1.00 19.02  ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 32.294 -25.101 26.611 1.00 20.24  ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 32.966 -26.427 26.997 1.00 24.92  ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 33.343 -26.444 28.479 1.00 35.09  ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 33.545 -27.866 28.975 1.00 43.14  ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? 32.719 -28.200 30.196 1.00 48.42  ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 29.508 -23.678 25.541 1.00 14.97  ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 28.818 -22.414 25.193 1.00 14.65  ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 29.653 -21.195 25.562 1.00 16.31  ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 30.171 -21.101 26.687 1.00 17.54  ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 27.517 -22.445 26.012 1.00 17.14  ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 27.345 -23.865 26.449 1.00 18.27  ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 28.698 -24.528 26.436 1.00 14.59  ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 29.803 -20.274 24.598 1.00 16.50  ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 30.682 -19.131 24.852 1.00 18.57  ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 30.314 -17.945 23.966 1.00 18.32  ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 29.390 -18.027 23.149 1.00 16.97  ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 32.133 -19.565 24.628 1.00 23.38  ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 32.410 -19.744 23.245 1.00 28.72  ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 31.019 -16.814 24.163 1.00 18.07  ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 30.794 -15.597 23.390 1.00 18.94  ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 31.696 -15.699 22.162 1.00 20.81  ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 32.931 -15.741 22.319 1.00 22.85  ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 31.281 -14.416 24.245 1.00 20.32  ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 30.258 -13.777 25.081 1.00 23.54  ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 30.944 -12.996 26.230 1.00 26.18  ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 29.332 -12.908 24.251 1.00 24.32  ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 31.114 -15.670 20.954 1.00 19.54  ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 31.819 -15.858 19.687 1.00 20.28  ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 31.437 -14.777 18.703 1.00 21.51  ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 30.270 -14.414 18.612 1.00 20.09  ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 31.450 -17.262 19.132 1.00 21.12  ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 32.037 -18.335 20.076 1.00 23.64  ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 31.875 -17.446 17.666 1.00 22.78  ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 31.830 -19.713 19.708 1.00 27.33  ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 32.432 -14.205 17.993 1.00 22.53  ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 32.158 -13.135 17.043 1.00 24.76  ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 31.385 -13.656 15.838 1.00 25.05  ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 31.758 -14.680 15.267 1.00 26.29  ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 33.486 -12.484 16.579 1.00 26.92  ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 33.285 -11.379 15.575 1.00 29.05  ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 32.961 -10.105 15.989 1.00 31.06  ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 33.328 -11.643 14.210 1.00 31.57  ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 32.745 -9.085  15.054 1.00 32.96  ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 33.090 -10.630 13.278 1.00 32.95  ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 32.811 -9.361  13.706 1.00 32.95  ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 30.329 -12.941 15.445 1.00 24.40  ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 29.482 -13.279 14.294 1.00 24.32  ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 29.407 -12.041 13.391 1.00 24.91  ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 29.035 -10.953 13.843 1.00 24.29  ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 28.056 -13.697 14.754 1.00 22.43  ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 27.144 -13.976 13.553 1.00 21.92  ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 28.125 -14.925 15.655 1.00 21.18  ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 29.717 -12.218 12.102 1.00 26.25  ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 29.675 -11.130 11.126 1.00 27.51  ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 28.271 -10.543 10.977 1.00 26.84  ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 27.275 -11.236 11.242 1.00 25.79  ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 30.168 -11.642 9.760  1.00 32.34  ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 30.948 -10.617 8.960  1.00 43.28  ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 32.389 -10.503 9.401  1.00 50.61  ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 33.129 -11.507 9.279  1.00 51.58  ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 32.763 -9.424  9.913  1.00 54.17  ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 28.182 -9.279  10.531 1.00 26.45  ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 26.897 -8.609  10.327 1.00 26.35  ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 26.066 -9.352  9.288  1.00 25.19  ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 26.602 -9.902  8.330  1.00 25.78  ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 27.109 -7.166  9.847  1.00 27.67  ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 24.750 -9.296  9.447  1.00 23.63  ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 23.809 -9.834  8.485  1.00 22.30  ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 22.658 -8.789  8.376  1.00 23.61  ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 22.713 -7.708  9.003  1.00 24.84  ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 23.269 -11.187 8.962  1.00 21.12  ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 22.553 -11.014 10.177 1.00 20.59  ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 21.638 -9.100  7.583  1.00 23.95  ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 20.456 -8.226  7.498  1.00 25.33  ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 19.645 -8.292  8.824  1.00 25.10  ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 18.796 -7.434  9.062  1.00 25.48  ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 19.537 -8.656  6.349  1.00 30.72  ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 20.227 -9.362  5.186  1.00 40.44  ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 20.359 -10.860 5.419  1.00 47.67  ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 21.466 -11.309 5.792  1.00 45.20  ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 19.328 -11.569 5.321  1.00 52.14  ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 19.938 -9.284  9.693  1.00 24.21  ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 19.223 -9.511  10.930 1.00 24.76  ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 19.914 -8.874  12.141 1.00 24.77  ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 19.243 -8.475  13.100 1.00 26.72  ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 19.091 -11.032 11.135 1.00 24.54  ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 18.463 -11.763 9.974  1.00 25.62  ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 17.090 -11.725 9.761  1.00 27.83  ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 19.225 -12.560 9.137  1.00 26.35  ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 16.506 -12.398 8.695  1.00 29.29  ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 18.646 -13.280 8.103  1.00 27.94  ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 17.286 -13.179 7.869  1.00 30.40  ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 16.695 -13.929 6.868  1.00 34.81  ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 21.245 -8.776  12.120 1.00 23.14  ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 21.993 -8.248  13.260 1.00 22.77  ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 23.200 -7.488  12.838 1.00 24.99  ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 23.865 -7.854  11.863 1.00 24.32  ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 22.551 -9.422  14.134 1.00 20.56  ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 21.530 -10.346 14.734 1.00 19.14  ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 21.365 -11.635 14.248 1.00 19.22  ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 20.753 -9.949  15.816 1.00 18.61  ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 20.435 -12.497 14.791 1.00 18.65  ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 19.830 -10.812 16.381 1.00 17.62  ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 19.707 -12.108 15.895 1.00 17.98  ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 18.754 -12.932 16.417 1.00 17.00  ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 23.610 -6.474  13.632 1.00 26.30  ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 24.907 -5.886  13.396 1.00 26.88  ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 26.020 -6.889  13.736 1.00 27.36  ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 25.769 -7.878  14.453 1.00 26.34  ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 24.929 -4.713  14.401 1.00 27.16  ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 24.066 -5.162  15.506 1.00 27.90  ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 22.978 -5.971  14.876 1.00 26.65  ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 27.275 -6.615  13.344 1.00 27.41  ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 28.428 -7.435  13.741 1.00 28.51  ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 28.500 -7.407  15.281 1.00 27.70  ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 28.327 -6.328  15.866 1.00 28.51  ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 29.716 -6.867  13.151 1.00 29.85  ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 28.648 -8.572  15.920 1.00 25.76  ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 28.564 -8.617  17.371 1.00 24.24  ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 29.083 -9.918  17.930 1.00 24.70  ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 29.371 -10.857 17.186 1.00 24.91  ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 27.074 -8.466  17.766 1.00 23.79  ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 26.252 -9.754  17.404 1.00 20.79  ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 24.762 -9.548  17.271 1.00 21.24  ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 23.917 -10.653 17.744 1.00 21.51  ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 23.815 -11.854 17.169 1.00 21.24  ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 22.979 -12.758 17.657 1.00 17.48  ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 24.544 -12.152 16.090 1.00 21.01  ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 29.102 -10.006 19.271 1.00 24.55  ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 29.428 -11.259 19.898 1.00 25.61  ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 28.101 -11.918 20.235 1.00 22.00  ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 27.234 -11.300 20.880 1.00 21.93  ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 30.184 -11.011 21.184 1.00 27.99  ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 31.624 -10.667 20.919 1.00 32.15  ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 32.572 -11.662 20.752 1.00 34.44  ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 32.029 -9.349  20.789 1.00 35.27  ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 33.899 -11.355 20.479 1.00 37.17  ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 33.353 -9.027  20.523 1.00 37.08  ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 34.283 -10.033 20.367 1.00 38.84  ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? 35.594 -9.717  20.117 1.00 42.68  ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 27.925 -13.165 19.782 1.00 18.44  ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 26.735 -13.928 20.148 1.00 16.90  ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 27.112 -14.803 21.348 1.00 15.98  ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 28.161 -15.455 21.339 1.00 17.19  ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 26.250 -14.759 18.953 1.00 16.25  ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 25.058 -15.678 19.321 1.00 17.14  ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 24.337 -16.200 18.103 1.00 16.83  ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 24.127 -15.473 17.113 1.00 16.01  ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 23.866 -17.475 18.184 1.00 15.48  ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 26.300 -14.783 22.404 1.00 15.12  ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 26.594 -15.573 23.596 1.00 15.00  ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 25.925 -16.967 23.542 1.00 14.87  ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 25.039 -17.215 22.701 1.00 15.02  ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 26.109 -14.845 24.851 1.00 17.89  ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 24.710 -14.599 24.735 1.00 19.27  ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 26.397 -17.885 24.457 1.00 14.09  ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 25.857 -19.242 24.605 1.00 14.29  ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 25.942 -20.006 23.276 1.00 14.79  ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 25.086 -20.880 23.000 1.00 15.11  ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 24.402 -19.163 25.121 1.00 13.83  ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 24.282 -18.494 26.461 1.00 16.25  ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 24.306 -19.237 27.632 1.00 18.70  ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 24.237 -17.174 26.776 1.00 17.00  ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 24.229 -18.359 28.630 1.00 19.30  ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 24.157 -17.101 28.166 1.00 19.35  ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 26.984 -19.729 22.478 1.00 14.54  ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 27.135 -20.352 21.161 1.00 14.46  ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 28.222 -21.461 21.221 1.00 14.81  ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 29.258 -21.276 21.848 1.00 15.37  ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 27.527 -19.278 20.116 1.00 14.98  ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 27.631 -19.717 18.650 1.00 17.83  ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 26.215 -20.119 18.110 1.00 17.33  ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 28.120 -18.547 17.752 1.00 20.20  ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 27.979 -22.596 20.522 1.00 13.67  ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 28.933 -23.728 20.508 1.00 14.19  ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 29.320 -23.990 19.070 1.00 15.59  ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 28.422 -24.027 18.213 1.00 16.41  ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 28.203 -24.964 21.050 1.00 13.10  ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 27.845 -24.754 22.509 1.00 17.33  ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 26.782 -26.021 23.144 1.00 17.78  ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 25.247 -25.808 22.035 1.00 17.94  ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 30.621 -24.224 18.779 1.00 13.54  ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 31.022 -24.453 17.393 1.00 14.00  ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 31.395 -25.904 17.180 1.00 13.72  ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 31.911 -26.575 18.073 1.00 13.68  ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 32.259 -23.582 16.984 1.00 15.74  ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 32.046 -22.091 17.063 1.00 17.50  ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 33.292 -21.332 16.518 1.00 19.31  ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 30.792 -21.640 16.279 1.00 17.98  ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 31.236 -26.355 15.933 1.00 14.08  ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 31.688 -27.688 15.528 1.00 14.06  ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 32.219 -27.574 14.084 1.00 13.73  ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 31.841 -26.641 13.368 1.00 15.34  ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 30.520 -28.683 15.546 1.00 14.39  ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 33.052 -28.532 13.661 1.00 13.43  ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 33.486 -28.615 12.282 1.00 13.98  ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 32.363 -29.336 11.514 1.00 16.66  ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 32.105 -30.498 11.770 1.00 18.31  ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? 34.851 -29.366 12.191 1.00 15.14  ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? 35.268 -29.495 10.722 1.00 16.09  ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? 35.923 -28.568 12.971 1.00 16.72  ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 31.751 -28.645 10.562 1.00 18.13  ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 30.663 -29.261 9.804  1.00 20.21  ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 30.025 -28.284 8.859  1.00 21.27  ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 30.324 -27.081 8.894  1.00 21.35  ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 29.253 -28.812 7.922  1.00 20.34  ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 28.610 -27.990 6.919  1.00 21.08  ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 27.368 -27.328 7.467  1.00 21.86  ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 26.584 -27.954 8.182  1.00 20.59  ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 28.269 -28.878 5.693  1.00 21.36  ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 27.586 -28.111 4.614  1.00 22.66  ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 28.254 -27.123 3.879  1.00 23.92  ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 26.280 -28.119 4.246  1.00 24.11  ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 27.338 -26.592 3.082  1.00 24.62  ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 26.146 -27.184 3.242  1.00 25.61  ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 27.145 -26.067 7.081  1.00 22.41  ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 25.994 -25.246 7.421  1.00 24.48  ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 25.799 -24.271 6.231  1.00 24.99  ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 26.765 -23.827 5.609  1.00 25.77  ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 26.295 -24.426 8.685  1.00 27.83  ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 25.177 -23.761 9.259  1.00 36.49  ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 24.548 -23.939 5.938  1.00 23.74  ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 24.120 -22.897 4.986  1.00 24.05  ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 23.013 -22.101 5.667  1.00 23.92  ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 22.473 -22.607 6.650  1.00 23.88  ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 23.643 -23.510 3.694  1.00 25.53  ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 24.831 -23.899 2.863  1.00 32.13  ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 24.408 -24.635 1.616  1.00 36.57  ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 23.371 -24.261 1.026  1.00 39.73  ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 25.083 -25.622 1.262  1.00 37.28  ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 22.649 -20.841 5.267  1.00 23.85  ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 21.672 -20.087 6.104  1.00 23.75  ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 20.349 -20.805 6.382  1.00 21.97  ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 19.836 -20.738 7.533  1.00 22.44  ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 21.472 -18.775 5.346  1.00 25.46  ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 22.780 -18.577 4.567  1.00 26.27  ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 23.219 -20.000 4.196  1.00 24.68  ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 19.816 -21.490 5.354  1.00 20.77  ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 18.580 -22.261 5.480  1.00 20.20  ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 18.670 -23.426 6.463  1.00 19.70  ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 17.656 -24.061 6.789  1.00 20.19  ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 19.881 -23.723 6.938  1.00 17.53  ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 20.068 -24.786 7.931  1.00 16.60  ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 19.705 -24.348 9.353  1.00 15.47  ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 19.614 -25.189 10.225 1.00 15.30  ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 21.508 -25.350 7.908  1.00 17.23  ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 21.754 -26.189 6.670  1.00 18.34  ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 20.807 -26.849 6.208  1.00 17.45  ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 22.885 -26.176 6.164  1.00 19.38  ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 19.564 -23.029 9.609  1.00 14.89  ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 19.212 -22.550 10.966 1.00 15.06  ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 17.940 -23.192 11.439 1.00 15.89  ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 17.006 -23.359 10.651 1.00 16.70  ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 19.110 -21.019 11.002 1.00 16.65  ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 20.720 -20.182 10.917 1.00 20.60  ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 17.949 -23.629 12.691 1.00 13.89  ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 16.783 -24.305 13.237 1.00 14.96  ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 16.957 -25.816 13.347 1.00 15.61  ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 16.205 -26.464 14.074 1.00 15.80  ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 17.933 -26.388 12.619 1.00 13.76  ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 18.217 -27.827 12.728 1.00 12.91  ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 18.610 -28.187 14.165 1.00 12.97  ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 19.384 -27.449 14.777 1.00 14.01  ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 18.101 -29.300 14.678 1.00 12.93  ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 18.360 -29.658 16.065 1.00 13.14  ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 19.680 -30.395 16.236 1.00 13.09  ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 20.039 -31.246 15.405 1.00 13.53  ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.144 -30.486 16.617 1.00 16.87  ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 15.939 -29.540 16.894 1.00 19.01  ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.488 -31.321 17.867 1.00 18.91  ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 14.663 -30.259 17.380 1.00 21.50  ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 20.380 -30.068 17.329 1.00 12.02  ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 21.572 -30.825 17.778 1.00 11.32  ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 21.083 -31.581 19.008 1.00 12.28  ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 20.489 -30.987 19.924 1.00 12.88  ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 22.659 -29.822 18.242 1.00 10.89  ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 23.885 -30.457 18.939 1.00 12.77  ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 24.656 -31.409 18.008 1.00 14.10  ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 24.841 -29.303 19.454 1.00 12.93  ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 21.324 -32.935 19.026 1.00 11.94  ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 20.894 -33.781 20.150 1.00 12.00  ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 22.076 -34.594 20.636 1.00 12.77  ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 22.910 -35.061 19.861 1.00 14.96  ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 19.864 -34.832 19.622 1.00 14.42  ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 18.585 -34.287 19.091 1.00 20.11  ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 17.669 -35.421 18.572 1.00 25.28  ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 17.135 -36.057 19.766 1.00 32.08  ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 16.001 -35.694 20.356 1.00 34.36  ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 15.171 -34.847 19.752 1.00 36.45  ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 15.670 -36.202 21.524 1.00 34.75  ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 22.069 -34.848 21.904 1.00 11.89  ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 23.047 -35.769 22.532 1.00 12.62  ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 22.250 -36.941 23.111 1.00 15.80  ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 21.030 -37.029 22.946 1.00 14.95  ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 23.848 -35.040 23.615 1.00 12.01  ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 22.854 -34.539 25.044 1.00 13.68  ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 22.948 -37.867 23.835 1.00 17.45  ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 22.269 -38.992 24.425 1.00 19.22  ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 21.202 -38.581 25.482 1.00 20.62  ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 20.346 -39.390 25.829 1.00 22.90  ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 23.321 -39.936 25.046 1.00 20.80  ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 23.988 -39.336 26.284 1.00 23.36  ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 25.013 -40.287 26.874 1.00 33.80  ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 26.216 -40.119 26.657 1.00 38.09  ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 24.551 -41.280 27.639 1.00 34.20  ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 21.211 -37.300 25.952 1.00 18.51  ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 20.267 -36.840 26.981 1.00 17.62  ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 19.047 -36.088 26.423 1.00 18.51  ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 18.128 -35.809 27.177 1.00 20.84  ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 20.989 -35.946 28.006 1.00 17.39  ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 22.178 -36.639 28.617 1.00 17.46  ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 23.477 -36.226 28.371 1.00 18.42  ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 22.215 -37.630 29.547 1.00 19.71  ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 24.273 -37.042 29.045 1.00 20.83  ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 23.570 -37.889 29.801 1.00 21.24  ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 19.079 -35.739 25.134 1.00 16.35  ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 17.979 -34.976 24.554 1.00 15.58  ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 18.443 -33.826 23.693 1.00 14.52  ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 19.569 -33.827 23.195 1.00 14.43  ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 17.576 -32.827 23.519 1.00 13.90  ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 17.897 -31.662 22.683 1.00 13.25  ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 18.897 -30.743 23.346 1.00 12.64  ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 18.679 -30.324 24.498 1.00 14.17  ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 16.611 -30.881 22.336 1.00 15.34  ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 16.946 -29.584 21.588 1.00 16.31  ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 15.666 -31.773 21.511 1.00 16.06  ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 19.970 -30.434 22.645 1.00 11.84  ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 21.023 -29.543 23.148 1.00 11.24  ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 20.825 -28.091 22.692 1.00 12.18  ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 21.118 -27.140 23.444 1.00 12.42  ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 22.407 -30.061 22.677 1.00 12.58  ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 23.524 -29.067 23.019 1.00 13.34  ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 22.710 -31.418 23.270 1.00 12.97  ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 20.501 -27.940 21.405 1.00 11.43  ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 20.312 -26.603 20.862 1.00 12.21  ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 19.990 -26.652 19.386 1.00 11.56  ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 19.558 -27.704 18.876 1.00 11.83  ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 20.018 -25.462 18.738 1.00 12.47  ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 19.655 -25.387 17.322 1.00 12.80  ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 20.720 -24.670 16.523 1.00 11.89  ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 21.405 -23.748 17.039 1.00 11.83  ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 18.306 -24.651 17.144 1.00 14.67  ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 18.300 -23.291 17.890 1.00 14.63  ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.100 -25.545 17.508 1.00 16.79  ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 16.954 -22.454 17.471 1.00 15.79  ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 20.860 -25.029 15.220 1.00 11.28  ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 21.828 -24.338 14.353 1.00 11.66  ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 21.478 -22.839 14.297 1.00 11.66  ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 20.302 -22.485 14.141 1.00 13.02  ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 21.761 -24.905 12.916 1.00 11.94  ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 22.649 -24.102 11.954 1.00 14.12  ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 22.174 -26.389 12.912 1.00 12.63  ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 22.481 -21.971 14.490 1.00 12.27  ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 22.287 -20.533 14.491 1.00 12.91  ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 23.291 -19.799 13.592 1.00 14.28  ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 22.946 -18.739 13.034 1.00 14.69  ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 22.367 -20.038 15.938 1.00 12.55  ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 22.253 -18.609 15.989 1.00 13.71  ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 24.499 -20.318 13.420 1.00 14.80  ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 25.526 -19.658 12.571 1.00 16.33  ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 26.264 -20.658 11.697 1.00 17.06  ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 26.236 -21.861 11.957 1.00 15.68  ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 26.569 -18.877 13.440 1.00 17.28  ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 27.425 -19.792 14.127 1.00 18.29  ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 25.950 -17.984 14.459 1.00 18.43  ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 26.963 -20.166 10.677 1.00 18.52  ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 27.794 -21.021 9.839  1.00 21.56  ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 28.786 -20.234 9.020  1.00 23.48  ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 28.629 -19.031 8.853  1.00 23.25  ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 29.747 -20.929 8.432  1.00 25.69  ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 30.749 -20.306 7.564  1.00 26.39  ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 32.112 -20.933 7.770  1.00 26.69  ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 32.403 -21.406 8.868  1.00 26.71  ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 32.934 -20.985 6.701  1.00 27.25  ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 34.292 -21.533 6.809  1.00 27.96  ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 34.372 -22.970 7.310  1.00 26.58  ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? 35.378 -23.367 7.928  1.00 27.30  ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? 35.132 -20.641 7.715  1.00 30.30  ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? 35.333 -19.257 7.191  1.00 35.54  ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? 35.420 -19.027 5.977  1.00 36.28  ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? 35.448 -18.308 8.108  1.00 37.82  ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 33.327 -23.746 7.034  1.00 23.61  ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 33.304 -25.125 7.476  1.00 21.70  ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 33.070 -25.306 8.965  1.00 19.70  ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 33.375 -26.362 9.492  1.00 20.13  ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 32.547 -24.295 9.633  1.00 18.40  ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 32.205 -24.360 11.037 1.00 18.31  ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 30.694 -24.147 11.139 1.00 20.56  ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 30.126 -23.297 10.419 1.00 24.08  ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 32.970 -23.285 11.821 1.00 19.10  ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 34.508 -23.465 11.798 1.00 21.27  ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? 35.200 -22.156 12.157 1.00 23.29  ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? 34.955 -24.574 12.764 1.00 21.23  ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 30.040 -24.893 12.009 1.00 16.53  ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 28.619 -24.706 12.268 1.00 15.21  ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 28.482 -24.300 13.735 1.00 14.72  ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 29.159 -24.868 14.615 1.00 14.37  ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 27.804 -25.998 11.937 1.00 16.39  ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 28.409 -27.247 12.579 1.00 18.23  ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 26.306 -25.845 12.275 1.00 16.83  ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 27.605 -23.321 13.984 1.00 13.68  ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 27.377 -22.872 15.351 1.00 14.17  ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 25.971 -23.182 15.816 1.00 13.32  ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 25.013 -22.953 15.079 1.00 13.97  ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 25.858 -23.583 17.087 1.00 12.05  ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 24.581 -23.960 17.701 1.00 12.93  ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 24.320 -23.094 18.913 1.00 13.44  ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 25.190 -22.934 19.775 1.00 13.54  ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 24.643 -25.426 18.214 1.00 13.06  ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 25.089 -26.408 17.153 1.00 13.79  ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 24.181 -26.958 16.268 1.00 13.98  ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 26.410 -26.844 17.096 1.00 14.69  ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 24.602 -27.857 15.287 1.00 14.53  ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 26.816 -27.773 16.148 1.00 15.50  ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 25.911 -28.271 15.239 1.00 14.84  ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 23.072 -22.554 18.965 1.00 12.31  ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 22.613 -21.821 20.134 1.00 11.66  ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 22.217 -22.837 21.197 1.00 12.04  ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 21.287 -23.645 20.985 1.00 11.91  ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 21.403 -20.974 19.744 1.00 11.42  ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 22.901 -22.812 22.347 1.00 12.19  ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 22.598 -23.733 23.434 1.00 13.08  ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 21.276 -23.415 24.106 1.00 13.49  ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 20.920 -22.235 24.254 1.00 12.94  ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 23.715 -23.601 24.496 1.00 14.30  ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 23.614 -24.612 25.619 1.00 17.45  ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 23.465 -25.805 25.331 1.00 17.53  ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 23.621 -24.192 26.792 1.00 20.35  ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 20.514 -24.470 24.499 1.00 12.57  ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 19.287 -24.239 25.292 1.00 12.65  ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 19.341 -24.984 26.624 1.00 13.59  ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 18.370 -24.915 27.388 1.00 15.16  ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 17.971 -24.615 24.540 1.00 13.74  ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 17.810 -23.798 23.246 1.00 13.97  ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 17.926 -26.120 24.231 1.00 14.50  ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 20.434 -25.727 26.933 1.00 13.20  ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 20.492 -26.558 28.118 1.00 12.26  ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 20.415 -25.803 29.420 1.00 14.65  ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 20.041 -26.399 30.433 1.00 16.10  ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 21.749 -27.445 28.096 1.00 11.71  ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 21.749 -28.457 26.939 1.00 12.33  ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 23.083 -29.186 26.923 1.00 12.67  ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 24.162 -28.292 26.499 1.00 13.53  ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 25.416 -28.672 26.271 1.00 14.08  ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 25.816 -29.904 26.578 1.00 13.51  ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 26.305 -27.804 25.799 1.00 15.71  ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 20.791 -24.515 29.416 1.00 14.32  ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 20.743 -23.740 30.638 1.00 15.00  ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 19.354 -23.157 30.915 1.00 16.03  ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 19.167 -22.612 32.015 1.00 17.00  ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 21.765 -22.591 30.588 1.00 16.41  ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 21.439 -21.568 29.484 1.00 19.25  ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 21.140 -22.004 28.341 1.00 18.49  ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 21.517 -20.314 29.772 1.00 19.56  ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 18.393 -23.264 29.990 1.00 15.92  ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.050 -22.683 30.160 1.00 17.26  ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 16.178 -23.653 30.929 1.00 17.51  ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 15.316 -24.353 30.373 1.00 16.99  ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 16.449 -22.335 28.774 1.00 17.23  ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.330 -21.414 27.924 1.00 18.61  ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 16.733 -21.226 26.530 1.00 19.01  ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.545 -20.062 28.597 1.00 18.91  ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 16.404 -23.704 32.253 1.00 17.87  ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 15.735 -24.723 33.071 1.00 18.98  ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 14.231 -24.564 33.137 1.00 20.36  ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 13.515 -25.573 33.287 1.00 21.25  ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 16.331 -24.804 34.479 1.00 17.66  ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 17.850 -24.848 34.593 1.00 18.17  ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 18.261 -25.057 36.045 1.00 20.17  ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 18.463 -25.952 33.717 1.00 18.40  ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 13.742 -23.297 32.970 1.00 19.48  ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 12.315 -22.994 33.041 1.00 20.75  ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 11.524 -23.607 31.862 1.00 20.96  ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 10.296 -23.642 31.932 1.00 21.85  ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 12.087 -21.463 33.111 1.00 20.27  ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 12.789 -20.678 32.029 1.00 20.15  ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 14.040 -20.134 32.081 1.00 20.64  ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 12.277 -20.391 30.709 1.00 19.98  ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 14.332 -19.509 30.880 1.00 20.45  ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 13.253 -19.633 30.036 1.00 20.34  ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 11.061 -20.662 30.056 1.00 21.21  ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 13.058 -19.157 28.735 1.00 21.85  ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 10.845 -20.131 28.789 1.00 22.58  ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 11.838 -19.401 28.140 1.00 22.40  ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 12.195 -24.085 30.795 1.00 20.81  ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 11.471 -24.690 29.666 1.00 21.31  ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 10.654 -25.908 30.108 1.00 25.47  ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 9.647  -26.202 29.454 1.00 26.18  ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 12.449 -25.111 28.538 1.00 19.80  ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 13.033 -23.984 27.689 1.00 19.39  ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 14.068 -24.547 26.724 1.00 18.41  ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 11.920 -23.211 26.891 1.00 18.87  ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 11.136 -26.627 31.154 1.00 28.01  ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 10.607 -27.855 31.777 1.00 32.64  ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 9.493  -27.636 32.779 1.00 36.52  ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 9.015  -28.624 33.335 1.00 37.95  ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 11.717 -28.520 32.605 1.00 35.86  ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 12.831 -29.184 31.851 1.00 40.97  ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 12.619 -29.538 30.684 1.00 41.52  ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 13.921 -29.377 32.452 1.00 45.51  ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 9.180  -26.394 33.128 1.00 37.83  ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 8.140  -26.113 34.109 1.00 40.89  ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 7.121  -25.111 33.544 1.00 43.07  ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 6.074  -24.856 34.158 1.00 44.59  ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 8.775  -25.594 35.407 1.00 44.29  ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 9.679  -24.397 35.207 1.00 51.08  ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 10.590 -24.104 36.386 1.00 60.69  ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 10.718 -22.913 36.758 1.00 61.87  ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 11.171 -25.065 36.940 1.00 63.44  ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1BQG C 2 .   ? 9.474  14.763  22.011 1.00 23.11  ? 201 A1BQG A N1  1 
HETATM 2156 N  N3  . A1BQG C 2 .   ? 9.568  10.035  23.369 1.00 36.29  ? 201 A1BQG A N3  1 
HETATM 2157 C  C4  . A1BQG C 2 .   ? 10.502 15.438  22.819 1.00 22.27  ? 201 A1BQG A C4  1 
HETATM 2158 C  C5  . A1BQG C 2 .   ? 8.777  13.677  22.392 1.00 25.93  ? 201 A1BQG A C5  1 
HETATM 2159 C  C6  . A1BQG C 2 .   ? 9.321  12.963  23.615 1.00 30.14  ? 201 A1BQG A C6  1 
HETATM 2160 C  C7  . A1BQG C 2 .   ? 8.351  11.962  24.193 1.00 33.84  ? 201 A1BQG A C7  1 
HETATM 2161 C  C8  . A1BQG C 2 .   ? 7.316  12.399  25.015 1.00 35.26  ? 201 A1BQG A C8  1 
HETATM 2162 C  C10 . A1BQG C 2 .   ? 6.839  10.158  25.589 1.00 36.32  ? 201 A1BQG A C10 1 
HETATM 2163 O  O1  . A1BQG C 2 .   ? 7.833  13.250  21.748 1.00 24.69  ? 201 A1BQG A O1  1 
HETATM 2164 C  C3  . A1BQG C 2 .   ? 11.865 15.399  22.133 1.00 22.04  ? 201 A1BQG A C3  1 
HETATM 2165 C  C2  . A1BQG C 2 .   ? 11.756 15.858  20.677 1.00 21.53  ? 201 A1BQG A C2  1 
HETATM 2166 C  C12 . A1BQG C 2 .   ? 9.341  15.266  20.642 1.00 21.65  ? 201 A1BQG A C12 1 
HETATM 2167 C  C1  . A1BQG C 2 .   ? 10.675 15.070  19.922 1.00 20.90  ? 201 A1BQG A C1  1 
HETATM 2168 C  C   . A1BQG C 2 .   ? 10.630 15.437  18.450 1.00 20.68  ? 201 A1BQG A C   1 
HETATM 2169 O  O   . A1BQG C 2 .   ? 10.953 14.619  17.581 1.00 22.08  ? 201 A1BQG A O   1 
HETATM 2170 N  N   . A1BQG C 2 .   ? 10.201 16.659  18.166 1.00 18.90  ? 201 A1BQG A N   1 
HETATM 2171 C  C11 . A1BQG C 2 .   ? 8.556  10.549  24.089 1.00 35.79  ? 201 A1BQG A C11 1 
HETATM 2172 N  N2  . A1BQG C 2 .   ? 7.786  9.677   24.771 1.00 36.57  ? 201 A1BQG A N2  1 
HETATM 2173 C  C9  . A1BQG C 2 .   ? 6.564  11.492  25.734 1.00 36.03  ? 201 A1BQG A C9  1 
HETATM 2174 ZN ZN  . ZN    D 3 .   ? 11.508 -4.626  5.600  1.00 18.61  2 202 ZN    A ZN  1 
HETATM 2175 S  S   . DMS   E 4 .   ? 19.580 0.558   20.237 1.00 40.08  ? 203 DMS   A S   1 
HETATM 2176 O  O   . DMS   E 4 .   ? 18.262 0.146   19.672 1.00 36.57  ? 203 DMS   A O   1 
HETATM 2177 C  C1  . DMS   E 4 .   ? 19.535 1.332   21.869 1.00 40.13  ? 203 DMS   A C1  1 
HETATM 2178 C  C2  . DMS   E 4 .   ? 20.318 1.979   19.330 1.00 39.47  ? 203 DMS   A C2  1 
HETATM 2179 N  N1  . A1BQG F 2 .   ? 23.969 -15.886 9.938  1.00 19.93  ? 201 A1BQG C N1  1 
HETATM 2180 N  N3  . A1BQG F 2 .   ? 24.126 -20.401 8.982  1.00 35.56  ? 201 A1BQG C N3  1 
HETATM 2181 C  C4  . A1BQG F 2 .   ? 22.896 -15.171 9.226  1.00 20.04  ? 201 A1BQG C C4  1 
HETATM 2182 C  C5  . A1BQG F 2 .   ? 24.689 -16.934 9.477  1.00 23.42  ? 201 A1BQG C C5  1 
HETATM 2183 C  C6  . A1BQG F 2 .   ? 24.157 -17.551 8.194  1.00 27.56  ? 201 A1BQG C C6  1 
HETATM 2184 C  C7  . A1BQG F 2 .   ? 25.066 -18.621 7.637  1.00 31.92  ? 201 A1BQG C C7  1 
HETATM 2185 C  C8  . A1BQG F 2 .   ? 25.979 -18.302 6.636  1.00 32.90  ? 201 A1BQG C C8  1 
HETATM 2186 C  C10 . A1BQG F 2 .   ? 26.547 -20.586 6.431  1.00 34.36  ? 201 A1BQG C C10 1 
HETATM 2187 O  O1  . A1BQG F 2 .   ? 25.675 -17.375 10.073 1.00 21.50  ? 201 A1BQG C O1  1 
HETATM 2188 C  C3  . A1BQG F 2 .   ? 21.594 -15.233 10.016 1.00 18.92  ? 201 A1BQG C C3  1 
HETATM 2189 C  C2  . A1BQG F 2 .   ? 21.812 -14.760 11.450 1.00 18.04  ? 201 A1BQG C C2  1 
HETATM 2190 C  C12 . A1BQG F 2 .   ? 24.212 -15.397 11.298 1.00 18.17  ? 201 A1BQG C C12 1 
HETATM 2191 C  C1  . A1BQG F 2 .   ? 22.938 -15.555 12.129 1.00 17.98  ? 201 A1BQG C C1  1 
HETATM 2192 C  C   . A1BQG F 2 .   ? 23.196 -15.058 13.538 1.00 17.63  ? 201 A1BQG C C   1 
HETATM 2193 O  O   . A1BQG F 2 .   ? 23.620 -13.908 13.742 1.00 16.13  ? 201 A1BQG C O   1 
HETATM 2194 N  N   . A1BQG F 2 .   ? 23.004 -15.953 14.504 1.00 17.11  ? 201 A1BQG C N   1 
HETATM 2195 C  C11 . A1BQG F 2 .   ? 24.961 -19.998 8.013  1.00 34.30  ? 201 A1BQG C C11 1 
HETATM 2196 N  N2  . A1BQG F 2 .   ? 25.705 -20.950 7.410  1.00 34.89  ? 201 A1BQG C N2  1 
HETATM 2197 C  C9  . A1BQG F 2 .   ? 26.717 -19.292 6.019  1.00 33.91  ? 201 A1BQG C C9  1 
HETATM 2198 S  S   . DMS   G 4 .   ? 30.798 -18.716 13.794 1.00 62.87  ? 202 DMS   C S   1 
HETATM 2199 O  O   . DMS   G 4 .   ? 30.478 -17.260 13.557 1.00 62.81  ? 202 DMS   C O   1 
HETATM 2200 C  C1  . DMS   G 4 .   ? 32.581 -18.910 13.474 1.00 62.77  ? 202 DMS   C C1  1 
HETATM 2201 C  C2  . DMS   G 4 .   ? 30.292 -19.689 12.356 1.00 62.54  ? 202 DMS   C C2  1 
HETATM 2202 ZN ZN  . ZN    H 3 .   ? 24.121 -34.750 27.003 1.00 15.14  2 203 ZN    C ZN  1 
HETATM 2203 O  O   . HOH   I 5 .   ? 19.810 22.999  8.083  1.00 26.14  ? 301 HOH   A O   1 
HETATM 2204 O  O   . HOH   I 5 .   ? 33.971 18.051  19.007 1.00 44.89  ? 302 HOH   A O   1 
HETATM 2205 O  O   . HOH   I 5 .   ? 10.892 8.305   4.379  1.00 24.27  ? 303 HOH   A O   1 
HETATM 2206 O  O   . HOH   I 5 .   ? 2.794  8.206   9.429  1.00 35.24  ? 304 HOH   A O   1 
HETATM 2207 O  O   . HOH   I 5 .   ? 3.614  -4.406  20.878 1.00 34.54  ? 305 HOH   A O   1 
HETATM 2208 O  O   . HOH   I 5 .   ? 23.022 -0.839  4.530  1.00 27.77  ? 306 HOH   A O   1 
HETATM 2209 O  O   . HOH   I 5 .   ? 23.558 22.239  8.024  1.00 29.15  ? 307 HOH   A O   1 
HETATM 2210 O  O   . HOH   I 5 .   ? 0.944  -2.201  19.685 1.00 36.76  ? 308 HOH   A O   1 
HETATM 2211 O  O   . HOH   I 5 .   ? 5.030  8.101   27.962 1.00 39.04  ? 309 HOH   A O   1 
HETATM 2212 O  O   . HOH   I 5 .   ? -0.063 14.712  16.191 1.00 33.91  ? 310 HOH   A O   1 
HETATM 2213 O  O   . HOH   I 5 .   ? -0.143 15.879  7.618  1.00 40.52  ? 311 HOH   A O   1 
HETATM 2214 O  O   . HOH   I 5 .   ? 21.958 -3.730  11.895 1.00 37.35  ? 312 HOH   A O   1 
HETATM 2215 O  O   . HOH   I 5 .   ? 36.493 16.532  12.224 1.00 28.87  ? 313 HOH   A O   1 
HETATM 2216 O  O   . HOH   I 5 .   ? 12.291 7.418   30.979 1.00 26.17  ? 314 HOH   A O   1 
HETATM 2217 O  O   . HOH   I 5 .   ? 10.647 4.922   3.363  1.00 22.86  ? 315 HOH   A O   1 
HETATM 2218 O  O   . HOH   I 5 .   ? 18.701 0.186   27.721 1.00 29.37  ? 316 HOH   A O   1 
HETATM 2219 O  O   . HOH   I 5 .   ? 2.729  3.818   27.508 1.00 30.44  ? 317 HOH   A O   1 
HETATM 2220 O  O   . HOH   I 5 .   ? 19.776 9.464   19.162 1.00 15.12  ? 318 HOH   A O   1 
HETATM 2221 O  O   . HOH   I 5 .   ? 5.693  -6.772  7.262  1.00 55.42  ? 319 HOH   A O   1 
HETATM 2222 O  O   . HOH   I 5 .   ? 16.035 -10.679 5.177  1.00 31.91  ? 320 HOH   A O   1 
HETATM 2223 O  O   . HOH   I 5 .   ? 5.397  14.233  21.039 1.00 36.87  ? 321 HOH   A O   1 
HETATM 2224 O  O   . HOH   I 5 .   ? 17.642 21.588  9.531  1.00 21.74  ? 322 HOH   A O   1 
HETATM 2225 O  O   . HOH   I 5 .   ? 24.567 17.798  3.603  1.00 44.77  ? 323 HOH   A O   1 
HETATM 2226 O  O   . HOH   I 5 .   ? 0.327  0.106   16.039 1.00 16.39  ? 324 HOH   A O   1 
HETATM 2227 O  O   . HOH   I 5 .   ? 17.492 1.142   29.963 1.00 36.73  ? 325 HOH   A O   1 
HETATM 2228 O  O   . HOH   I 5 .   ? 11.200 11.904  11.145 1.00 14.57  ? 326 HOH   A O   1 
HETATM 2229 O  O   . HOH   I 5 .   ? 16.895 -6.828  11.029 1.00 24.66  ? 327 HOH   A O   1 
HETATM 2230 O  O   . HOH   I 5 .   ? 14.579 3.022   23.200 1.00 14.83  ? 328 HOH   A O   1 
HETATM 2231 O  O   . HOH   I 5 .   ? 28.317 3.788   3.578  1.00 40.57  ? 329 HOH   A O   1 
HETATM 2232 O  O   . HOH   I 5 .   ? 22.289 18.632  19.336 1.00 32.67  ? 330 HOH   A O   1 
HETATM 2233 O  O   . HOH   I 5 .   ? 11.151 2.691   33.429 1.00 17.40  ? 331 HOH   A O   1 
HETATM 2234 O  O   . HOH   I 5 .   ? 9.300  18.782  19.747 1.00 20.61  ? 332 HOH   A O   1 
HETATM 2235 O  O   . HOH   I 5 .   ? 30.560 10.732  14.517 1.00 35.26  ? 333 HOH   A O   1 
HETATM 2236 O  O   . HOH   I 5 .   ? 6.288  -5.261  29.054 1.00 27.94  ? 334 HOH   A O   1 
HETATM 2237 O  O   . HOH   I 5 .   ? 29.680 11.781  20.148 1.00 35.63  ? 335 HOH   A O   1 
HETATM 2238 O  O   . HOH   I 5 .   ? 6.771  4.078   32.861 1.00 23.05  ? 336 HOH   A O   1 
HETATM 2239 O  O   . HOH   I 5 .   ? 19.104 16.463  26.175 1.00 49.19  ? 337 HOH   A O   1 
HETATM 2240 O  O   . HOH   I 5 .   ? 10.840 15.489  2.347  1.00 55.94  ? 338 HOH   A O   1 
HETATM 2241 O  O   . HOH   I 5 .   ? 29.660 3.955   11.449 1.00 23.16  ? 339 HOH   A O   1 
HETATM 2242 O  O   . HOH   I 5 .   ? 6.298  18.142  24.226 1.00 41.46  ? 340 HOH   A O   1 
HETATM 2243 O  O   . HOH   I 5 .   ? 23.525 0.600   16.629 1.00 25.71  ? 341 HOH   A O   1 
HETATM 2244 O  O   . HOH   I 5 .   ? 10.178 9.448   31.240 1.00 40.70  ? 342 HOH   A O   1 
HETATM 2245 O  O   . HOH   I 5 .   ? 21.138 19.603  17.876 1.00 26.82  ? 343 HOH   A O   1 
HETATM 2246 O  O   . HOH   I 5 .   ? 13.894 -11.327 3.945  1.00 59.27  ? 344 HOH   A O   1 
HETATM 2247 O  O   . HOH   I 5 .   ? -0.075 -5.441  10.935 1.00 41.22  ? 345 HOH   A O   1 
HETATM 2248 O  O   . HOH   I 5 .   ? 18.048 -6.475  3.318  1.00 30.85  ? 346 HOH   A O   1 
HETATM 2249 O  O   . HOH   I 5 .   ? 34.614 20.716  12.016 1.00 47.64  ? 347 HOH   A O   1 
HETATM 2250 O  O   . HOH   I 5 .   ? 10.884 17.685  5.215  1.00 39.16  ? 348 HOH   A O   1 
HETATM 2251 O  O   . HOH   I 5 .   ? 6.700  17.195  21.847 1.00 29.03  ? 349 HOH   A O   1 
HETATM 2252 O  O   . HOH   I 5 .   ? 17.965 5.392   26.712 1.00 27.58  ? 350 HOH   A O   1 
HETATM 2253 O  O   . HOH   I 5 .   ? 12.276 -5.187  32.053 1.00 52.35  ? 351 HOH   A O   1 
HETATM 2254 O  O   . HOH   I 5 .   ? 17.464 3.010   23.242 1.00 20.40  ? 352 HOH   A O   1 
HETATM 2255 O  O   . HOH   I 5 .   ? 7.727  20.028  17.549 1.00 21.37  ? 353 HOH   A O   1 
HETATM 2256 O  O   . HOH   I 5 .   ? 3.412  -1.155  2.916  1.00 45.97  ? 354 HOH   A O   1 
HETATM 2257 O  O   . HOH   I 5 .   ? 31.301 18.916  8.978  1.00 33.01  ? 355 HOH   A O   1 
HETATM 2258 O  O   . HOH   I 5 .   ? 17.550 19.341  16.982 1.00 16.55  ? 356 HOH   A O   1 
HETATM 2259 O  O   . HOH   I 5 .   ? 13.110 10.802  9.231  1.00 13.93  ? 357 HOH   A O   1 
HETATM 2260 O  O   . HOH   I 5 .   ? 32.101 2.193   4.414  1.00 43.11  ? 358 HOH   A O   1 
HETATM 2261 O  O   . HOH   I 5 .   ? 18.237 9.834   25.770 1.00 24.02  ? 359 HOH   A O   1 
HETATM 2262 O  O   . HOH   I 5 .   ? 14.696 12.751  24.056 1.00 20.56  ? 360 HOH   A O   1 
HETATM 2263 O  O   . HOH   I 5 .   ? 3.959  6.087   24.769 1.00 27.57  ? 361 HOH   A O   1 
HETATM 2264 O  O   . HOH   I 5 .   ? 9.996  -8.324  9.648  1.00 41.43  ? 362 HOH   A O   1 
HETATM 2265 O  O   . HOH   I 5 .   ? 30.373 5.161   4.343  1.00 40.31  ? 363 HOH   A O   1 
HETATM 2266 O  O   . HOH   I 5 .   ? 5.107  -1.209  24.170 1.00 22.52  ? 364 HOH   A O   1 
HETATM 2267 O  O   . HOH   I 5 .   ? 9.127  2.583   2.690  1.00 25.70  ? 365 HOH   A O   1 
HETATM 2268 O  O   . HOH   I 5 .   ? -0.794 15.465  12.261 1.00 30.69  ? 366 HOH   A O   1 
HETATM 2269 O  O   . HOH   I 5 .   ? 0.153  4.662   6.425  1.00 31.40  ? 367 HOH   A O   1 
HETATM 2270 O  O   . HOH   I 5 .   ? 5.070  26.882  16.573 1.00 39.10  ? 368 HOH   A O   1 
HETATM 2271 O  O   . HOH   I 5 .   ? 5.589  26.645  19.257 1.00 31.17  ? 369 HOH   A O   1 
HETATM 2272 O  O   . HOH   I 5 .   ? 32.092 9.466   6.477  1.00 34.44  ? 370 HOH   A O   1 
HETATM 2273 O  O   . HOH   I 5 .   ? 29.500 -4.346  10.341 1.00 50.81  ? 371 HOH   A O   1 
HETATM 2274 O  O   . HOH   I 5 .   ? 9.783  5.067   33.866 1.00 21.84  ? 372 HOH   A O   1 
HETATM 2275 O  O   . HOH   I 5 .   ? 3.411  13.822  22.938 1.00 43.10  ? 373 HOH   A O   1 
HETATM 2276 O  O   . HOH   I 5 .   ? 6.283  1.753   5.773  1.00 22.59  ? 374 HOH   A O   1 
HETATM 2277 O  O   . HOH   I 5 .   ? 18.230 19.574  5.436  1.00 42.53  ? 375 HOH   A O   1 
HETATM 2278 O  O   . HOH   I 5 .   ? 18.284 -2.544  18.581 1.00 30.91  ? 376 HOH   A O   1 
HETATM 2279 O  O   . HOH   I 5 .   ? 30.594 21.212  17.119 1.00 37.21  ? 377 HOH   A O   1 
HETATM 2280 O  O   . HOH   I 5 .   ? 16.927 20.938  19.044 1.00 29.21  ? 378 HOH   A O   1 
HETATM 2281 O  O   . HOH   I 5 .   ? 22.168 3.947   23.979 1.00 41.97  ? 379 HOH   A O   1 
HETATM 2282 O  O   . HOH   I 5 .   ? 4.318  -4.944  6.199  1.00 27.93  ? 380 HOH   A O   1 
HETATM 2283 O  O   . HOH   I 5 .   ? 11.796 21.766  12.101 1.00 25.85  ? 381 HOH   A O   1 
HETATM 2284 O  O   . HOH   I 5 .   ? 2.303  9.910   28.060 1.00 46.39  ? 382 HOH   A O   1 
HETATM 2285 O  O   . HOH   I 5 .   ? 23.313 11.586  22.807 1.00 45.06  ? 383 HOH   A O   1 
HETATM 2286 O  O   . HOH   I 5 .   ? 7.546  -7.757  24.109 1.00 32.98  ? 384 HOH   A O   1 
HETATM 2287 O  O   . HOH   I 5 .   ? 16.623 -6.409  26.486 1.00 50.60  ? 385 HOH   A O   1 
HETATM 2288 O  O   . HOH   I 5 .   ? 15.195 -5.262  -0.121 1.00 41.93  ? 386 HOH   A O   1 
HETATM 2289 O  O   . HOH   I 5 .   ? 8.272  -6.923  8.534  1.00 34.26  ? 387 HOH   A O   1 
HETATM 2290 O  O   . HOH   I 5 .   ? 30.712 20.903  10.842 1.00 29.52  ? 388 HOH   A O   1 
HETATM 2291 O  O   . HOH   I 5 .   ? 16.556 -4.310  2.007  1.00 28.77  ? 389 HOH   A O   1 
HETATM 2292 O  O   . HOH   I 5 .   ? 14.833 -3.842  17.329 1.00 28.05  ? 390 HOH   A O   1 
HETATM 2293 O  O   . HOH   I 5 .   ? 14.358 21.323  8.267  1.00 35.76  ? 391 HOH   A O   1 
HETATM 2294 O  O   . HOH   I 5 .   ? 4.176  -2.078  20.893 1.00 32.13  ? 392 HOH   A O   1 
HETATM 2295 O  O   . HOH   I 5 .   ? 2.964  15.660  19.756 1.00 33.15  ? 393 HOH   A O   1 
HETATM 2296 O  O   . HOH   I 5 .   ? 6.787  12.859  5.040  1.00 24.98  ? 394 HOH   A O   1 
HETATM 2297 O  O   . HOH   I 5 .   ? 18.872 12.890  1.690  1.00 37.37  ? 395 HOH   A O   1 
HETATM 2298 O  O   . HOH   I 5 .   ? 14.509 14.798  3.489  1.00 31.01  ? 396 HOH   A O   1 
HETATM 2299 O  O   . HOH   I 5 .   ? 7.697  8.274   32.954 1.00 50.82  ? 397 HOH   A O   1 
HETATM 2300 O  O   . HOH   I 5 .   ? 1.743  -1.701  17.374 1.00 28.21  ? 398 HOH   A O   1 
HETATM 2301 O  O   . HOH   I 5 .   ? 1.945  13.212  4.897  1.00 40.37  ? 399 HOH   A O   1 
HETATM 2302 O  O   . HOH   I 5 .   ? 2.467  -6.033  14.685 1.00 42.00  ? 400 HOH   A O   1 
HETATM 2303 O  O   . HOH   I 5 .   ? 31.327 3.222   13.456 1.00 31.87  ? 401 HOH   A O   1 
HETATM 2304 O  O   . HOH   I 5 .   ? 19.576 24.070  15.583 1.00 23.61  ? 402 HOH   A O   1 
HETATM 2305 O  O   . HOH   I 5 .   ? 4.794  7.202   2.638  1.00 33.93  ? 403 HOH   A O   1 
HETATM 2306 O  O   . HOH   I 5 .   ? 30.876 15.716  22.106 1.00 29.17  ? 404 HOH   A O   1 
HETATM 2307 O  O   . HOH   I 5 .   ? 0.870  -1.922  9.470  1.00 42.09  ? 405 HOH   A O   1 
HETATM 2308 O  O   . HOH   I 5 .   ? 34.643 15.588  9.554  1.00 51.38  ? 406 HOH   A O   1 
HETATM 2309 O  O   . HOH   I 5 .   ? 2.643  23.248  21.213 1.00 31.89  ? 407 HOH   A O   1 
HETATM 2310 O  O   . HOH   I 5 .   ? 5.998  23.023  10.364 1.00 33.93  ? 408 HOH   A O   1 
HETATM 2311 O  O   . HOH   I 5 .   ? 20.008 -3.144  16.481 1.00 31.60  ? 409 HOH   A O   1 
HETATM 2312 O  O   . HOH   I 5 .   ? 23.622 3.051   20.148 1.00 27.84  ? 410 HOH   A O   1 
HETATM 2313 O  O   . HOH   I 5 .   ? 12.488 -7.567  13.182 1.00 30.46  ? 411 HOH   A O   1 
HETATM 2314 O  O   . HOH   I 5 .   ? 21.533 9.424   21.417 1.00 21.33  ? 412 HOH   A O   1 
HETATM 2315 O  O   . HOH   I 5 .   ? 27.976 17.161  23.738 1.00 34.25  ? 413 HOH   A O   1 
HETATM 2316 O  O   . HOH   I 5 .   ? 22.528 19.388  6.004  1.00 25.34  ? 414 HOH   A O   1 
HETATM 2317 O  O   . HOH   I 5 .   ? 22.627 -1.844  16.712 1.00 38.99  ? 415 HOH   A O   1 
HETATM 2318 O  O   . HOH   I 5 .   ? 3.514  11.096  18.496 1.00 40.21  ? 416 HOH   A O   1 
HETATM 2319 O  O   . HOH   I 5 .   ? 30.005 11.428  17.968 1.00 42.87  ? 417 HOH   A O   1 
HETATM 2320 O  O   . HOH   I 5 .   ? 32.426 15.170  7.638  1.00 54.53  ? 418 HOH   A O   1 
HETATM 2321 O  O   . HOH   I 5 .   ? 4.564  -0.950  28.827 1.00 44.95  ? 419 HOH   A O   1 
HETATM 2322 O  O   . HOH   I 5 .   ? 29.584 12.457  2.632  1.00 51.81  ? 420 HOH   A O   1 
HETATM 2323 O  O   . HOH   I 5 .   ? 9.780  19.903  29.416 1.00 51.40  ? 421 HOH   A O   1 
HETATM 2324 O  O   . HOH   I 5 .   ? 18.536 -4.362  20.072 1.00 34.86  ? 422 HOH   A O   1 
HETATM 2325 O  O   . HOH   I 5 .   ? 15.071 -8.903  12.113 1.00 38.05  ? 423 HOH   A O   1 
HETATM 2326 O  O   . HOH   I 5 .   ? 16.618 11.794  25.932 1.00 37.95  ? 424 HOH   A O   1 
HETATM 2327 O  O   . HOH   I 5 .   ? 32.529 22.150  24.168 1.00 47.14  ? 425 HOH   A O   1 
HETATM 2328 O  O   . HOH   I 5 .   ? 11.575 23.779  13.826 1.00 39.21  ? 426 HOH   A O   1 
HETATM 2329 O  O   . HOH   I 5 .   ? 3.943  -2.068  26.637 1.00 38.74  ? 427 HOH   A O   1 
HETATM 2330 O  O   . HOH   I 5 .   ? 9.536  15.527  26.411 1.00 48.63  ? 428 HOH   A O   1 
HETATM 2331 O  O   . HOH   I 5 .   ? 20.844 22.441  17.751 1.00 28.15  ? 429 HOH   A O   1 
HETATM 2332 O  O   . HOH   I 5 .   ? 1.802  1.688   26.435 1.00 32.13  ? 430 HOH   A O   1 
HETATM 2333 O  O   . HOH   I 5 .   ? 13.557 24.775  15.133 1.00 38.15  ? 431 HOH   A O   1 
HETATM 2334 O  O   . HOH   I 5 .   ? 6.478  2.747   3.201  1.00 30.73  ? 432 HOH   A O   1 
HETATM 2335 O  O   . HOH   I 5 .   ? 30.308 17.154  25.908 1.00 110.26 ? 433 HOH   A O   1 
HETATM 2336 O  O   . HOH   I 5 .   ? 0.965  -1.299  23.418 1.00 28.29  ? 434 HOH   A O   1 
HETATM 2337 O  O   . HOH   I 5 .   ? 32.416 22.135  20.155 1.00 43.49  ? 435 HOH   A O   1 
HETATM 2338 O  O   . HOH   I 5 .   ? 7.245  15.073  3.347  1.00 44.80  ? 436 HOH   A O   1 
HETATM 2339 O  O   . HOH   I 5 .   ? 9.285  7.501   2.191  1.00 58.50  ? 437 HOH   A O   1 
HETATM 2340 O  O   . HOH   I 5 .   ? 25.490 -2.591  0.561  1.00 69.04  ? 438 HOH   A O   1 
HETATM 2341 O  O   . HOH   I 5 .   ? 3.408  -3.000  22.917 1.00 32.54  ? 439 HOH   A O   1 
HETATM 2342 O  O   . HOH   I 5 .   ? 1.704  -4.632  6.798  1.00 51.43  ? 440 HOH   A O   1 
HETATM 2343 O  O   . HOH   I 5 .   ? 9.822  25.439  12.978 1.00 41.00  ? 441 HOH   A O   1 
HETATM 2344 O  O   . HOH   I 5 .   ? 5.685  -7.960  25.762 1.00 51.73  ? 442 HOH   A O   1 
HETATM 2345 O  O   . HOH   J 5 .   ? 32.111 -22.102 22.198 1.00 30.71  ? 301 HOH   C O   1 
HETATM 2346 O  O   . HOH   J 5 .   ? 24.476 -21.966 27.751 1.00 20.40  ? 302 HOH   C O   1 
HETATM 2347 O  O   . HOH   J 5 .   ? 30.505 -35.126 11.082 1.00 29.90  ? 303 HOH   C O   1 
HETATM 2348 O  O   . HOH   J 5 .   ? 22.806 -19.422 31.850 1.00 34.87  ? 304 HOH   C O   1 
HETATM 2349 O  O   . HOH   J 5 .   ? 17.497 -36.849 29.485 1.00 41.54  ? 305 HOH   C O   1 
HETATM 2350 O  O   . HOH   J 5 .   ? 7.287  -14.279 29.917 1.00 44.84  ? 306 HOH   C O   1 
HETATM 2351 O  O   . HOH   J 5 .   ? 22.383 -28.501 -0.923 1.00 24.42  ? 307 HOH   C O   1 
HETATM 2352 O  O   . HOH   J 5 .   ? 31.988 -30.509 28.781 1.00 35.36  ? 308 HOH   C O   1 
HETATM 2353 O  O   . HOH   J 5 .   ? 24.171 -26.375 -1.109 1.00 31.64  ? 309 HOH   C O   1 
HETATM 2354 O  O   . HOH   J 5 .   ? 24.234 -11.825 12.066 1.00 20.44  ? 310 HOH   C O   1 
HETATM 2355 O  O   . HOH   J 5 .   ? 24.746 -25.246 28.957 1.00 16.52  ? 311 HOH   C O   1 
HETATM 2356 O  O   . HOH   J 5 .   ? 11.029 -8.350  24.707 1.00 22.78  ? 312 HOH   C O   1 
HETATM 2357 O  O   . HOH   J 5 .   ? 14.252 -21.467 13.866 1.00 15.23  ? 313 HOH   C O   1 
HETATM 2358 O  O   . HOH   J 5 .   ? 37.475 -23.465 6.270  1.00 41.81  ? 314 HOH   C O   1 
HETATM 2359 O  O   . HOH   J 5 .   ? 34.032 -15.946 14.632 1.00 35.16  ? 315 HOH   C O   1 
HETATM 2360 O  O   . HOH   J 5 .   ? 3.907  -20.286 19.479 1.00 32.51  ? 316 HOH   C O   1 
HETATM 2361 O  O   . HOH   J 5 .   ? 11.864 -35.126 20.362 1.00 40.55  ? 317 HOH   C O   1 
HETATM 2362 O  O   . HOH   J 5 .   ? 13.463 -26.450 37.110 1.00 48.69  ? 318 HOH   C O   1 
HETATM 2363 O  O   . HOH   J 5 .   ? 8.233  -21.987 32.789 1.00 44.76  ? 319 HOH   C O   1 
HETATM 2364 O  O   . HOH   J 5 .   ? 33.826 -30.647 15.523 1.00 16.57  ? 320 HOH   C O   1 
HETATM 2365 O  O   . HOH   J 5 .   ? 13.287 -35.656 22.636 1.00 28.37  ? 321 HOH   C O   1 
HETATM 2366 O  O   . HOH   J 5 .   ? 36.146 -30.528 27.759 1.00 36.14  ? 322 HOH   C O   1 
HETATM 2367 O  O   . HOH   J 5 .   ? 5.323  -26.948 22.654 1.00 26.04  ? 323 HOH   C O   1 
HETATM 2368 O  O   . HOH   J 5 .   ? 30.870 -22.559 28.857 1.00 31.87  ? 324 HOH   C O   1 
HETATM 2369 O  O   . HOH   J 5 .   ? 23.345 -34.895 33.223 1.00 29.98  ? 325 HOH   C O   1 
HETATM 2370 O  O   . HOH   J 5 .   ? 11.203 -30.349 17.405 1.00 27.01  ? 326 HOH   C O   1 
HETATM 2371 O  O   . HOH   J 5 .   ? 15.127 -35.075 5.257  1.00 48.38  ? 327 HOH   C O   1 
HETATM 2372 O  O   . HOH   J 5 .   ? 4.515  -24.476 14.776 1.00 42.59  ? 328 HOH   C O   1 
HETATM 2373 O  O   . HOH   J 5 .   ? 23.681 -13.000 26.809 1.00 58.14  ? 329 HOH   C O   1 
HETATM 2374 O  O   . HOH   J 5 .   ? 29.170 -16.811 7.382  1.00 45.79  ? 330 HOH   C O   1 
HETATM 2375 O  O   . HOH   J 5 .   ? 20.417 -18.748 31.711 1.00 35.76  ? 331 HOH   C O   1 
HETATM 2376 O  O   . HOH   J 5 .   ? 7.138  -26.746 30.382 1.00 37.27  ? 332 HOH   C O   1 
HETATM 2377 O  O   . HOH   J 5 .   ? 23.406 -18.648 21.042 1.00 15.14  ? 333 HOH   C O   1 
HETATM 2378 O  O   . HOH   J 5 .   ? 8.224  -26.344 13.165 1.00 37.62  ? 334 HOH   C O   1 
HETATM 2379 O  O   . HOH   J 5 .   ? 10.054 -19.703 12.093 1.00 40.86  ? 335 HOH   C O   1 
HETATM 2380 O  O   . HOH   J 5 .   ? 29.765 -29.936 34.433 1.00 40.17  ? 336 HOH   C O   1 
HETATM 2381 O  O   . HOH   J 5 .   ? 26.071 -10.584 14.077 1.00 19.55  ? 337 HOH   C O   1 
HETATM 2382 O  O   . HOH   J 5 .   ? 12.725 -11.381 15.361 1.00 28.06  ? 338 HOH   C O   1 
HETATM 2383 O  O   . HOH   J 5 .   ? 4.273  -19.294 13.466 1.00 32.17  ? 339 HOH   C O   1 
HETATM 2384 O  O   . HOH   J 5 .   ? 19.320 -27.918 9.420  1.00 15.89  ? 340 HOH   C O   1 
HETATM 2385 O  O   . HOH   J 5 .   ? 28.788 -31.909 3.018  1.00 51.44  ? 341 HOH   C O   1 
HETATM 2386 O  O   . HOH   J 5 .   ? 26.286 -27.410 29.595 1.00 20.33  ? 342 HOH   C O   1 
HETATM 2387 O  O   . HOH   J 5 .   ? 8.480  -32.027 26.750 1.00 46.01  ? 343 HOH   C O   1 
HETATM 2388 O  O   . HOH   J 5 .   ? 16.946 -9.118  23.168 1.00 19.96  ? 344 HOH   C O   1 
HETATM 2389 O  O   . HOH   J 5 .   ? 18.172 -12.852 28.452 1.00 46.35  ? 345 HOH   C O   1 
HETATM 2390 O  O   . HOH   J 5 .   ? 15.003 -30.737 5.519  1.00 36.80  ? 346 HOH   C O   1 
HETATM 2391 O  O   . HOH   J 5 .   ? 29.471 -24.415 7.962  1.00 38.63  ? 347 HOH   C O   1 
HETATM 2392 O  O   . HOH   J 5 .   ? 27.853 -35.976 3.403  1.00 35.71  ? 348 HOH   C O   1 
HETATM 2393 O  O   . HOH   J 5 .   ? 22.105 -5.366  10.383 1.00 27.57  ? 349 HOH   C O   1 
HETATM 2394 O  O   . HOH   J 5 .   ? 12.561 -31.569 28.777 1.00 29.37  ? 350 HOH   C O   1 
HETATM 2395 O  O   . HOH   J 5 .   ? 3.602  -25.488 35.310 1.00 53.93  ? 351 HOH   C O   1 
HETATM 2396 O  O   . HOH   J 5 .   ? 18.744 -17.992 8.422  1.00 22.36  ? 352 HOH   C O   1 
HETATM 2397 O  O   . HOH   J 5 .   ? 11.362 -11.997 13.323 1.00 38.46  ? 353 HOH   C O   1 
HETATM 2398 O  O   . HOH   J 5 .   ? 4.215  -19.557 16.084 1.00 33.78  ? 354 HOH   C O   1 
HETATM 2399 O  O   . HOH   J 5 .   ? 27.994 -15.801 9.834  1.00 32.93  ? 355 HOH   C O   1 
HETATM 2400 O  O   . HOH   J 5 .   ? 16.400 -11.478 15.610 1.00 17.24  ? 356 HOH   C O   1 
HETATM 2401 O  O   . HOH   J 5 .   ? 21.724 -19.746 23.132 1.00 13.31  ? 357 HOH   C O   1 
HETATM 2402 O  O   . HOH   J 5 .   ? 20.327 -21.530 2.552  1.00 31.35  ? 358 HOH   C O   1 
HETATM 2403 O  O   . HOH   J 5 .   ? 33.751 -28.547 7.702  1.00 35.38  ? 359 HOH   C O   1 
HETATM 2404 O  O   . HOH   J 5 .   ? 16.643 -10.921 27.122 1.00 38.26  ? 360 HOH   C O   1 
HETATM 2405 O  O   . HOH   J 5 .   ? 3.468  -9.812  16.114 1.00 24.76  ? 361 HOH   C O   1 
HETATM 2406 O  O   . HOH   J 5 .   ? 30.520 -7.660  9.821  1.00 35.47  ? 362 HOH   C O   1 
HETATM 2407 O  O   . HOH   J 5 .   ? 15.110 -21.314 7.060  1.00 32.36  ? 363 HOH   C O   1 
HETATM 2408 O  O   . HOH   J 5 .   ? 26.773 -34.084 32.046 1.00 21.55  ? 364 HOH   C O   1 
HETATM 2409 O  O   . HOH   J 5 .   ? 19.887 -34.838 15.555 1.00 22.80  ? 365 HOH   C O   1 
HETATM 2410 O  O   . HOH   J 5 .   ? 16.505 -27.914 9.547  1.00 24.31  ? 366 HOH   C O   1 
HETATM 2411 O  O   . HOH   J 5 .   ? 12.870 -13.866 9.012  1.00 36.27  ? 367 HOH   C O   1 
HETATM 2412 O  O   . HOH   J 5 .   ? 13.689 -11.199 11.300 1.00 36.08  ? 368 HOH   C O   1 
HETATM 2413 O  O   . HOH   J 5 .   ? 5.017  -25.546 29.704 1.00 40.50  ? 369 HOH   C O   1 
HETATM 2414 O  O   . HOH   J 5 .   ? 35.217 -14.882 18.331 1.00 33.91  ? 370 HOH   C O   1 
HETATM 2415 O  O   . HOH   J 5 .   ? 6.052  -32.386 20.167 1.00 32.05  ? 371 HOH   C O   1 
HETATM 2416 O  O   . HOH   J 5 .   ? 33.677 -32.903 12.203 1.00 30.79  ? 372 HOH   C O   1 
HETATM 2417 O  O   . HOH   J 5 .   ? 32.962 -16.709 26.324 1.00 31.18  ? 373 HOH   C O   1 
HETATM 2418 O  O   . HOH   J 5 .   ? 19.429 -34.646 30.820 1.00 20.35  ? 374 HOH   C O   1 
HETATM 2419 O  O   . HOH   J 5 .   ? 30.970 -35.303 25.790 1.00 26.17  ? 375 HOH   C O   1 
HETATM 2420 O  O   . HOH   J 5 .   ? -1.652 -31.183 23.228 1.00 45.61  ? 376 HOH   C O   1 
HETATM 2421 O  O   . HOH   J 5 .   ? 23.659 -35.552 1.013  1.00 33.82  ? 377 HOH   C O   1 
HETATM 2422 O  O   . HOH   J 5 .   ? 16.711 -9.882  13.520 1.00 43.14  ? 378 HOH   C O   1 
HETATM 2423 O  O   . HOH   J 5 .   ? 25.306 -9.174  21.456 1.00 45.16  ? 379 HOH   C O   1 
HETATM 2424 O  O   . HOH   J 5 .   ? 15.374 -26.090 6.835  1.00 41.32  ? 380 HOH   C O   1 
HETATM 2425 O  O   . HOH   J 5 .   ? 26.083 -37.695 23.052 1.00 25.77  ? 381 HOH   C O   1 
HETATM 2426 O  O   . HOH   J 5 .   ? 16.489 -17.512 31.019 1.00 42.13  ? 382 HOH   C O   1 
HETATM 2427 O  O   . HOH   J 5 .   ? 29.165 -28.240 25.230 1.00 16.97  ? 383 HOH   C O   1 
HETATM 2428 O  O   . HOH   J 5 .   ? 18.057 -6.924  17.913 1.00 40.49  ? 384 HOH   C O   1 
HETATM 2429 O  O   . HOH   J 5 .   ? 36.914 -29.295 24.103 1.00 22.46  ? 385 HOH   C O   1 
HETATM 2430 O  O   . HOH   J 5 .   ? 12.413 -11.351 26.794 1.00 24.73  ? 386 HOH   C O   1 
HETATM 2431 O  O   . HOH   J 5 .   ? 28.206 -17.437 26.749 1.00 24.71  ? 387 HOH   C O   1 
HETATM 2432 O  O   . HOH   J 5 .   ? 15.891 -30.660 13.223 1.00 22.17  ? 388 HOH   C O   1 
HETATM 2433 O  O   . HOH   J 5 .   ? 2.570  -15.740 11.954 1.00 24.54  ? 389 HOH   C O   1 
HETATM 2434 O  O   . HOH   J 5 .   ? 18.213 -37.690 22.227 1.00 45.08  ? 390 HOH   C O   1 
HETATM 2435 O  O   . HOH   J 5 .   ? 15.265 -6.465  17.400 1.00 22.03  ? 391 HOH   C O   1 
HETATM 2436 O  O   . HOH   J 5 .   ? 28.985 -31.780 8.100  1.00 22.34  ? 392 HOH   C O   1 
HETATM 2437 O  O   . HOH   J 5 .   ? 20.561 -15.674 28.888 1.00 25.24  ? 393 HOH   C O   1 
HETATM 2438 O  O   . HOH   J 5 .   ? 35.089 -34.922 16.048 1.00 35.33  ? 394 HOH   C O   1 
HETATM 2439 O  O   . HOH   J 5 .   ? 16.118 -30.193 2.279  1.00 44.93  ? 395 HOH   C O   1 
HETATM 2440 O  O   . HOH   J 5 .   ? 5.523  -13.924 9.961  1.00 37.78  ? 396 HOH   C O   1 
HETATM 2441 O  O   . HOH   J 5 .   ? 3.388  -21.107 27.665 1.00 37.95  ? 397 HOH   C O   1 
HETATM 2442 O  O   . HOH   J 5 .   ? -0.055 -23.985 19.213 1.00 65.74  ? 398 HOH   C O   1 
HETATM 2443 O  O   . HOH   J 5 .   ? 30.540 -23.385 5.963  1.00 36.13  ? 399 HOH   C O   1 
HETATM 2444 O  O   . HOH   J 5 .   ? 35.604 -15.725 20.911 1.00 46.00  ? 400 HOH   C O   1 
HETATM 2445 O  O   . HOH   J 5 .   ? 8.219  -32.139 18.667 1.00 30.56  ? 401 HOH   C O   1 
HETATM 2446 O  O   . HOH   J 5 .   ? 2.197  -15.689 25.992 1.00 43.99  ? 402 HOH   C O   1 
HETATM 2447 O  O   . HOH   J 5 .   ? 24.943 -40.229 31.184 1.00 54.16  ? 403 HOH   C O   1 
HETATM 2448 O  O   . HOH   J 5 .   ? 26.518 -13.578 9.445  1.00 31.58  ? 404 HOH   C O   1 
HETATM 2449 O  O   . HOH   J 5 .   ? 23.958 -14.221 29.160 1.00 46.58  ? 405 HOH   C O   1 
HETATM 2450 O  O   . HOH   J 5 .   ? 28.668 -7.433  20.873 1.00 38.82  ? 406 HOH   C O   1 
HETATM 2451 O  O   . HOH   J 5 .   ? 22.734 -8.862  19.961 1.00 28.34  ? 407 HOH   C O   1 
HETATM 2452 O  O   . HOH   J 5 .   ? 20.276 -9.209  24.108 1.00 35.74  ? 408 HOH   C O   1 
HETATM 2453 O  O   . HOH   J 5 .   ? 33.379 -33.260 14.741 1.00 22.67  ? 409 HOH   C O   1 
HETATM 2454 O  O   . HOH   J 5 .   ? 30.194 -15.123 11.089 1.00 31.55  ? 410 HOH   C O   1 
HETATM 2455 O  O   . HOH   J 5 .   ? 10.574 -28.135 13.596 1.00 28.22  ? 411 HOH   C O   1 
HETATM 2456 O  O   . HOH   J 5 .   ? 30.379 -32.634 10.244 1.00 37.45  ? 412 HOH   C O   1 
HETATM 2457 O  O   . HOH   J 5 .   ? 18.733 -16.285 6.455  1.00 49.64  ? 413 HOH   C O   1 
HETATM 2458 O  O   . HOH   J 5 .   ? 3.580  -27.837 20.611 1.00 35.04  ? 414 HOH   C O   1 
HETATM 2459 O  O   . HOH   J 5 .   ? 5.306  -27.642 35.474 1.00 62.74  ? 415 HOH   C O   1 
HETATM 2460 O  O   . HOH   J 5 .   ? 12.335 -21.539 11.762 1.00 23.79  ? 416 HOH   C O   1 
HETATM 2461 O  O   . HOH   J 5 .   ? 26.063 -12.800 7.019  1.00 47.99  ? 417 HOH   C O   1 
HETATM 2462 O  O   . HOH   J 5 .   ? 22.592 -38.275 19.597 1.00 36.35  ? 418 HOH   C O   1 
HETATM 2463 O  O   . HOH   J 5 .   ? 21.364 -41.488 28.253 1.00 48.73  ? 419 HOH   C O   1 
HETATM 2464 O  O   . HOH   J 5 .   ? 9.978  -23.081 12.450 1.00 36.78  ? 420 HOH   C O   1 
HETATM 2465 O  O   . HOH   J 5 .   ? 15.592 -21.316 34.882 1.00 37.61  ? 421 HOH   C O   1 
HETATM 2466 O  O   . HOH   J 5 .   ? 4.116  -23.011 30.441 1.00 44.60  ? 422 HOH   C O   1 
HETATM 2467 O  O   . HOH   J 5 .   ? 27.773 -35.517 29.624 1.00 26.33  ? 423 HOH   C O   1 
HETATM 2468 O  O   . HOH   J 5 .   ? 27.766 -19.353 28.252 1.00 43.63  ? 424 HOH   C O   1 
HETATM 2469 O  O   . HOH   J 5 .   ? 14.122 -8.161  14.963 1.00 33.74  ? 425 HOH   C O   1 
HETATM 2470 O  O   . HOH   J 5 .   ? 18.151 -19.411 32.424 1.00 41.69  ? 426 HOH   C O   1 
HETATM 2471 O  O   . HOH   J 5 .   ? 16.749 -19.330 6.900  1.00 36.90  ? 427 HOH   C O   1 
HETATM 2472 O  O   . HOH   J 5 .   ? 29.664 -28.051 27.690 1.00 50.56  ? 428 HOH   C O   1 
HETATM 2473 O  O   . HOH   J 5 .   ? 17.458 -9.163  3.487  1.00 42.31  ? 429 HOH   C O   1 
HETATM 2474 O  O   . HOH   J 5 .   ? 4.033  -30.329 19.411 1.00 41.81  ? 430 HOH   C O   1 
HETATM 2475 O  O   . HOH   J 5 .   ? 17.536 -33.743 14.567 1.00 35.61  ? 431 HOH   C O   1 
HETATM 2476 O  O   . HOH   J 5 .   ? 36.894 -21.929 4.236  1.00 53.59  ? 432 HOH   C O   1 
HETATM 2477 O  O   . HOH   J 5 .   ? 6.871  -29.462 30.448 1.00 55.28  ? 433 HOH   C O   1 
HETATM 2478 O  O   . HOH   J 5 .   ? 10.321 -15.264 8.917  1.00 56.05  ? 434 HOH   C O   1 
HETATM 2479 O  O   . HOH   J 5 .   ? 2.946  -21.883 17.232 1.00 45.43  ? 435 HOH   C O   1 
HETATM 2480 O  O   . HOH   J 5 .   ? 5.950  -28.340 12.910 1.00 63.85  ? 436 HOH   C O   1 
HETATM 2481 O  O   . HOH   J 5 .   ? -1.310 -10.699 23.714 1.00 73.67  ? 437 HOH   C O   1 
HETATM 2482 O  O   . HOH   J 5 .   ? 35.389 -6.460  17.959 1.00 48.65  ? 438 HOH   C O   1 
HETATM 2483 O  O   . HOH   J 5 .   ? 2.399  -18.412 11.784 1.00 37.12  ? 439 HOH   C O   1 
HETATM 2484 O  O   . HOH   J 5 .   ? 18.862 -39.925 21.071 1.00 40.31  ? 440 HOH   C O   1 
HETATM 2485 O  O   . HOH   J 5 .   ? 26.212 -23.012 29.737 1.00 29.00  ? 441 HOH   C O   1 
HETATM 2486 O  O   . HOH   J 5 .   ? 1.872  -8.560  17.935 1.00 32.60  ? 442 HOH   C O   1 
HETATM 2487 O  O   . HOH   J 5 .   ? 0.150  -10.370 14.961 1.00 36.98  ? 443 HOH   C O   1 
HETATM 2488 O  O   . HOH   J 5 .   ? 5.059  -7.658  23.353 1.00 31.77  ? 444 HOH   C O   1 
HETATM 2489 O  O   . HOH   J 5 .   ? 29.483 -38.643 9.327  1.00 30.96  ? 445 HOH   C O   1 
HETATM 2490 O  O   . HOH   J 5 .   ? 15.311 -32.959 13.711 1.00 41.33  ? 446 HOH   C O   1 
HETATM 2491 O  O   . HOH   J 5 .   ? 6.690  -30.449 14.744 1.00 54.45  ? 447 HOH   C O   1 
HETATM 2492 O  O   . HOH   J 5 .   ? -0.781 -9.301  17.045 1.00 32.87  ? 448 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   ? 0.2724 0.2655 0.2494 -0.0121 -0.0312 -0.0189 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2695 0.2667 0.2622 -0.0101 -0.0352 -0.0165 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2584 0.2592 0.2600 -0.0068 -0.0341 -0.0117 7   SER   A C   
4    O O   . SER   A 1   ? 0.2650 0.2649 0.2596 -0.0067 -0.0329 -0.0096 7   SER   A O   
5    C CB  . SER   A 1   ? 0.3027 0.2985 0.2943 -0.0140 -0.0448 -0.0155 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3378 0.3325 0.3222 -0.0157 -0.0506 -0.0107 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2322 0.2364 0.2490 -0.0045 -0.0336 -0.0105 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2267 0.2327 0.2521 -0.0020 -0.0310 -0.0072 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2061 0.2142 0.2427 -0.0003 -0.0257 -0.0081 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2083 0.2169 0.2442 -0.0005 -0.0230 -0.0105 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1755 0.1842 0.2224 0.0010  -0.0236 -0.0060 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1806 0.1901 0.2363 0.0017  -0.0176 -0.0068 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1861 0.1934 0.2433 0.0021  -0.0115 -0.0059 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1892 0.1949 0.2469 0.0027  -0.0129 -0.0040 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1876 0.1993 0.2590 0.0020  -0.0204 -0.0063 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1682 0.1744 0.2266 0.0012  -0.0045 -0.0070 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1805 0.1828 0.2398 0.0003  0.0031  -0.0075 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1785 0.1809 0.2544 0.0010  0.0075  -0.0079 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1721 0.1768 0.2525 0.0006  0.0074  -0.0082 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1880 0.1880 0.2337 -0.0031 0.0082  -0.0085 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1773 0.1788 0.2102 -0.0039 0.0038  -0.0076 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2031 0.1972 0.2463 -0.0055 0.0166  -0.0102 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1775 0.1787 0.2002 -0.0075 0.0061  -0.0069 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1882 0.1883 0.2757 0.0024  0.0112  -0.0075 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1972 0.1973 0.3042 0.0033  0.0172  -0.0077 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2010 0.1941 0.3056 0.0011  0.0300  -0.0108 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2173 0.2062 0.3230 0.0017  0.0332  -0.0111 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1871 0.1905 0.3149 0.0067  0.0112  -0.0040 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1936 0.2029 0.3220 0.0071  -0.0015 -0.0014 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2143 0.2239 0.3299 0.0069  -0.0101 0.0003  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2013 0.2149 0.3412 0.0068  -0.0044 -0.0012 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2251 0.2382 0.3376 0.0060  -0.0207 0.0016  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2140 0.2314 0.3524 0.0060  -0.0157 0.0002  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2262 0.2430 0.3500 0.0054  -0.0237 0.0014  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2639 0.2826 0.3824 0.0033  -0.0337 0.0017  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2045 0.1949 0.3029 -0.0022 0.0375  -0.0132 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2239 0.2057 0.3143 -0.0063 0.0506  -0.0169 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2401 0.2207 0.3428 -0.0074 0.0599  -0.0183 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2423 0.2266 0.3440 -0.0083 0.0571  -0.0170 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2618 0.2399 0.3246 -0.0118 0.0503  -0.0179 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2549 0.2384 0.3109 -0.0128 0.0435  -0.0153 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2972 0.2653 0.3484 -0.0180 0.0635  -0.0221 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2558 0.2313 0.3734 -0.0069 0.0714  -0.0208 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2502 0.2242 0.3821 -0.0079 0.0823  -0.0223 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2436 0.2279 0.3972 -0.0038 0.0733  -0.0182 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2441 0.2349 0.4123 0.0009  0.0627  -0.0146 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2416 0.2272 0.3934 -0.0063 0.0755  -0.0181 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2355 0.2302 0.4063 -0.0034 0.0668  -0.0146 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2184 0.2170 0.3722 -0.0042 0.0544  -0.0127 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2267 0.2297 0.3882 -0.0042 0.0504  -0.0112 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2788 0.2730 0.4665 -0.0049 0.0776  -0.0154 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3631 0.3563 0.5783 -0.0023 0.0877  -0.0161 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3811 0.3810 0.6199 0.0025  0.0798  -0.0127 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3942 0.3786 0.6070 -0.0058 0.1053  -0.0204 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2087 0.2060 0.3423 -0.0044 0.0481  -0.0127 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1979 0.1984 0.3171 -0.0049 0.0379  -0.0111 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1735 0.1776 0.2906 -0.0018 0.0268  -0.0099 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1720 0.1741 0.2887 -0.0006 0.0276  -0.0102 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2073 0.2026 0.3017 -0.0094 0.0416  -0.0116 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2136 0.2040 0.3039 -0.0141 0.0518  -0.0121 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2189 0.2120 0.3191 -0.0143 0.0516  -0.0105 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2457 0.2280 0.3197 -0.0194 0.0614  -0.0141 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2469 0.2351 0.3422 -0.0192 0.0613  -0.0103 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2624 0.2390 0.3292 -0.0250 0.0711  -0.0145 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2786 0.2584 0.3562 -0.0247 0.0710  -0.0122 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3186 0.2924 0.3880 -0.0308 0.0807  -0.0119 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1560 0.1642 0.2704 -0.0011 0.0175  -0.0089 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1629 0.1734 0.2704 0.0005  0.0076  -0.0083 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1825 0.1922 0.2729 -0.0011 0.0060  -0.0086 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1875 0.1979 0.2796 -0.0020 0.0062  -0.0084 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1521 0.1671 0.2734 0.0017  -0.0011 -0.0073 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1966 0.2126 0.3072 0.0018  -0.0108 -0.0075 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2015 0.2209 0.3240 0.0013  -0.0198 -0.0065 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2294 0.2481 0.3407 -0.0006 -0.0261 -0.0088 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2755 0.2930 0.3755 -0.0018 -0.0332 -0.0090 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2832 0.3007 0.3813 -0.0011 -0.0363 -0.0061 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2648 0.2801 0.3548 -0.0041 -0.0366 -0.0122 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1781 0.1864 0.2542 -0.0014 0.0049  -0.0085 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1612 0.1696 0.2247 -0.0025 0.0032  -0.0079 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1647 0.1750 0.2251 -0.0008 -0.0037 -0.0086 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1672 0.1771 0.2242 -0.0001 -0.0061 -0.0086 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1644 0.1700 0.2144 -0.0050 0.0070  -0.0070 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1578 0.1649 0.1994 -0.0065 0.0048  -0.0048 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1713 0.1728 0.2210 -0.0079 0.0153  -0.0075 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1407 0.1520 0.2019 -0.0007 -0.0062 -0.0092 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1374 0.1488 0.1938 0.0000  -0.0111 -0.0111 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1306 0.1418 0.1829 -0.0001 -0.0095 -0.0110 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1517 0.1633 0.2072 -0.0006 -0.0066 -0.0089 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1672 0.1787 0.2315 -0.0003 -0.0157 -0.0131 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2100 0.2227 0.2815 -0.0001 -0.0190 -0.0118 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1856 0.1973 0.2596 -0.0008 -0.0136 -0.0135 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1237 0.1340 0.1699 0.0002  -0.0112 -0.0132 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1240 0.1339 0.1711 0.0006  -0.0087 -0.0135 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1481 0.1564 0.2041 0.0005  -0.0086 -0.0153 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1619 0.1685 0.2188 -0.0006 -0.0117 -0.0186 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1346 0.1422 0.1738 0.0004  -0.0087 -0.0168 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1616 0.1706 0.1926 0.0004  -0.0084 -0.0149 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1699 0.1780 0.1943 -0.0004 -0.0112 -0.0152 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1596 0.1708 0.1921 0.0009  -0.0055 -0.0122 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1276 0.1365 0.1908 0.0010  -0.0058 -0.0126 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1254 0.1322 0.1983 0.0008  -0.0052 -0.0140 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1470 0.1494 0.2186 0.0002  -0.0055 -0.0203 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1730 0.1731 0.2490 -0.0013 -0.0073 -0.0235 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1354 0.1431 0.2161 0.0014  -0.0025 -0.0090 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1358 0.1412 0.2273 0.0010  -0.0016 -0.0090 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1405 0.1463 0.2402 0.0018  0.0005  -0.0029 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1696 0.1729 0.2804 0.0012  0.0018  -0.0011 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1686 0.1677 0.2886 0.0020  0.0037  -0.0049 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1835 0.1797 0.3013 0.0029  0.0051  -0.0114 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1704 0.1672 0.3015 0.0015  0.0050  -0.0022 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1544 0.1552 0.2197 0.0007  -0.0034 -0.0225 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1812 0.1758 0.2425 -0.0010 -0.0019 -0.0295 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2087 0.2010 0.2590 -0.0044 -0.0074 -0.0335 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2305 0.2166 0.2756 -0.0075 -0.0074 -0.0396 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2007 0.1933 0.2597 0.0001  0.0040  -0.0310 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1963 0.1906 0.2429 -0.0003 0.0032  -0.0305 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.1975 0.1979 0.2454 0.0015  0.0026  -0.0244 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2114 0.2012 0.2440 -0.0030 0.0036  -0.0355 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2018 0.2015 0.2379 0.0004  0.0025  -0.0257 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2129 0.2063 0.2394 -0.0022 0.0034  -0.0321 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1895 0.1862 0.2367 -0.0042 -0.0121 -0.0299 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1878 0.1834 0.2276 -0.0073 -0.0190 -0.0313 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1843 0.1834 0.2359 -0.0076 -0.0237 -0.0289 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.1977 0.1975 0.2478 -0.0098 -0.0305 -0.0283 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1925 0.1899 0.2224 -0.0068 -0.0206 -0.0287 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2166 0.2106 0.2347 -0.0072 -0.0158 -0.0312 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2321 0.2280 0.2417 -0.0069 -0.0175 -0.0278 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2347 0.2212 0.2422 -0.0116 -0.0155 -0.0378 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1826 0.1839 0.2466 -0.0056 -0.0202 -0.0267 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1739 0.1784 0.2506 -0.0059 -0.0226 -0.0245 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1837 0.1860 0.2636 -0.0097 -0.0286 -0.0281 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.1991 0.1962 0.2741 -0.0119 -0.0279 -0.0328 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1743 0.1797 0.2610 -0.0043 -0.0170 -0.0220 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2015 0.2075 0.2899 -0.0108 -0.0343 -0.0257 24  THR   A N   
135  C CA  . THR   A 18  ? 0.2171 0.2222 0.3098 -0.0154 -0.0421 -0.0278 24  THR   A CA  
136  C C   . THR   A 18  ? 0.2278 0.2341 0.3373 -0.0159 -0.0401 -0.0280 24  THR   A C   
137  O O   . THR   A 18  ? 0.2215 0.2296 0.3393 -0.0126 -0.0329 -0.0255 24  THR   A O   
138  C CB  . THR   A 18  ? 0.2416 0.2514 0.3395 -0.0163 -0.0504 -0.0233 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2442 0.2596 0.3604 -0.0128 -0.0467 -0.0188 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2599 0.2685 0.3423 -0.0158 -0.0522 -0.0220 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2378 0.2430 0.3527 -0.0208 -0.0472 -0.0303 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2552 0.2620 0.3882 -0.0217 -0.0457 -0.0300 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2184 0.2324 0.3691 -0.0183 -0.0428 -0.0240 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2216 0.2362 0.3827 -0.0165 -0.0355 -0.0227 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3080 0.3136 0.4454 -0.0284 -0.0555 -0.0326 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4216 0.4182 0.5403 -0.0336 -0.0577 -0.0398 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4713 0.4607 0.5844 -0.0326 -0.0489 -0.0449 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4617 0.4547 0.5664 -0.0402 -0.0673 -0.0426 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4925 0.4737 0.5887 -0.0383 -0.0518 -0.0516 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4902 0.4728 0.5789 -0.0436 -0.0630 -0.0507 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2212 0.2398 0.3749 -0.0175 -0.0476 -0.0203 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2042 0.2286 0.3757 -0.0143 -0.0433 -0.0154 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1910 0.2138 0.3562 -0.0101 -0.0318 -0.0145 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1868 0.2113 0.3644 -0.0089 -0.0243 -0.0125 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2357 0.2645 0.4134 -0.0140 -0.0507 -0.0112 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3291 0.3642 0.5340 -0.0151 -0.0541 -0.0074 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3340 0.3698 0.5472 -0.0193 -0.0596 -0.0088 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3709 0.4103 0.5917 -0.0115 -0.0495 -0.0031 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1763 0.1957 0.3222 -0.0087 -0.0301 -0.0159 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1845 0.2023 0.3231 -0.0060 -0.0207 -0.0147 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1794 0.1953 0.3224 -0.0067 -0.0148 -0.0148 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1755 0.1916 0.3222 -0.0061 -0.0074 -0.0122 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1823 0.1972 0.3016 -0.0051 -0.0211 -0.0161 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2038 0.2198 0.3167 -0.0041 -0.0241 -0.0148 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2053 0.2236 0.3267 -0.0027 -0.0216 -0.0121 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2107 0.2247 0.3106 -0.0049 -0.0287 -0.0166 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1834 0.1966 0.3260 -0.0085 -0.0179 -0.0178 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1819 0.1925 0.3298 -0.0091 -0.0128 -0.0173 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1920 0.2050 0.3579 -0.0106 -0.0107 -0.0155 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1889 0.2008 0.3585 -0.0106 -0.0038 -0.0128 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1800 0.1857 0.3236 -0.0106 -0.0154 -0.0217 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1823 0.1849 0.3124 -0.0085 -0.0128 -0.0221 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2097 0.2102 0.3273 -0.0086 -0.0156 -0.0257 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1779 0.1790 0.3077 -0.0067 -0.0070 -0.0186 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2016 0.2000 0.3130 -0.0063 -0.0110 -0.0248 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1959 0.1951 0.3152 -0.0051 -0.0065 -0.0199 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1840 0.1854 0.3211 -0.0067 -0.0024 -0.0135 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1908 0.1892 0.3102 -0.0033 -0.0025 -0.0160 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.1837 0.1835 0.3181 -0.0055 0.0009  -0.0093 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1874 0.1864 0.3143 -0.0036 0.0004  -0.0102 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1894 0.2062 0.3672 -0.0120 -0.0163 -0.0161 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1973 0.2176 0.3961 -0.0133 -0.0137 -0.0140 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2084 0.2308 0.4121 -0.0113 -0.0047 -0.0105 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2145 0.2383 0.4338 -0.0123 0.0015  -0.0087 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1947 0.2193 0.4070 -0.0157 -0.0235 -0.0146 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1871 0.2091 0.3783 -0.0090 -0.0033 -0.0099 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1889 0.2108 0.3815 -0.0079 0.0061  -0.0079 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1813 0.1985 0.3522 -0.0078 0.0115  -0.0073 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1757 0.1915 0.3383 -0.0071 0.0162  -0.0068 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2081 0.2334 0.4071 -0.0060 0.0028  -0.0074 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2360 0.2670 0.4597 -0.0065 -0.0027 -0.0061 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2433 0.2763 0.4862 -0.0069 0.0043  -0.0047 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2293 0.2627 0.4528 -0.0074 -0.0152 -0.0063 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1751 0.1895 0.3378 -0.0087 0.0105  -0.0070 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1814 0.1924 0.3261 -0.0090 0.0133  -0.0050 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1950 0.2031 0.3337 -0.0113 0.0226  -0.0022 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2192 0.2263 0.3668 -0.0135 0.0287  -0.0009 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1828 0.1916 0.3269 -0.0095 0.0109  -0.0042 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2039 0.2102 0.3341 -0.0097 0.0122  -0.0006 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2066 0.2138 0.3246 -0.0077 0.0082  -0.0020 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1906 0.1945 0.3259 -0.0098 0.0108  0.0009  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1848 0.1912 0.3074 -0.0117 0.0242  -0.0015 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2143 0.2162 0.3251 -0.0157 0.0324  0.0009  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2242 0.2240 0.3199 -0.0178 0.0296  0.0054  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2475 0.2440 0.3378 -0.0219 0.0334  0.0097  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2363 0.2367 0.3399 -0.0157 0.0364  -0.0016 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2513 0.2454 0.3366 -0.0213 0.0441  0.0000  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2396 0.2419 0.3620 -0.0137 0.0404  -0.0045 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2051 0.2072 0.2954 -0.0152 0.0225  0.0052  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1963 0.1978 0.2764 -0.0166 0.0190  0.0101  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1702 0.1750 0.2526 -0.0124 0.0122  0.0083  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1815 0.1879 0.2643 -0.0099 0.0104  0.0038  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2146 0.2132 0.2764 -0.0211 0.0217  0.0123  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2317 0.2312 0.2837 -0.0228 0.0162  0.0179  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2499 0.2481 0.2981 -0.0266 0.0144  0.0254  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2284 0.2305 0.2745 -0.0212 0.0115  0.0174  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2616 0.2624 0.3043 -0.0271 0.0082  0.0300  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2441 0.2473 0.2855 -0.0238 0.0068  0.0247  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2298 0.2338 0.2758 -0.0179 0.0104  0.0121  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2405 0.2467 0.2771 -0.0236 0.0019  0.0265  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2452 0.2513 0.2844 -0.0177 0.0063  0.0135  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2416 0.2493 0.2776 -0.0202 0.0021  0.0204  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1643 0.1694 0.2489 -0.0118 0.0090  0.0122  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1741 0.1813 0.2604 -0.0083 0.0047  0.0104  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1782 0.1860 0.2640 -0.0090 0.0025  0.0172  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1863 0.1927 0.2741 -0.0116 0.0031  0.0233  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1883 0.1950 0.2861 -0.0054 0.0034  0.0050  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1905 0.1950 0.3001 -0.0060 0.0049  0.0066  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2158 0.2189 0.3314 -0.0053 0.0044  0.0116  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2721 0.2733 0.3942 -0.0071 0.0060  0.0165  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2073 0.2113 0.3227 -0.0031 0.0028  0.0112  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1691 0.1793 0.2532 -0.0069 -0.0001 0.0168  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1640 0.1760 0.2516 -0.0072 -0.0026 0.0241  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1570 0.1705 0.2517 -0.0030 -0.0030 0.0206  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1590 0.1743 0.2464 -0.0024 -0.0036 0.0175  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1974 0.2109 0.2715 -0.0119 -0.0049 0.0298  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2869 0.3032 0.3658 -0.0135 -0.0094 0.0396  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2968 0.3152 0.3905 -0.0094 -0.0101 0.0407  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2905 0.3068 0.3584 -0.0193 -0.0122 0.0462  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1612 0.1731 0.2705 -0.0004 -0.0016 0.0207  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1659 0.1774 0.2825 0.0031  0.0003  0.0164  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1623 0.1739 0.2788 0.0031  0.0003  0.0164  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1748 0.1910 0.2924 0.0035  -0.0014 0.0218  36  SER   A C   
244  O O   . SER   A 30  ? 0.1893 0.2061 0.3057 0.0053  0.0006  0.0171  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1923 0.1999 0.3256 0.0052  0.0033  0.0162  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.1796 0.1872 0.3126 0.0053  0.0034  0.0157  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2302 0.2360 0.3711 0.0082  0.0072  0.0116  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.1964 0.2053 0.3418 0.0052  0.0020  0.0258  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1785 0.1980 0.2984 0.0010  -0.0053 0.0321  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1925 0.2174 0.3156 0.0005  -0.0083 0.0385  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1948 0.2217 0.3011 -0.0016 -0.0096 0.0351  37  SER   A C   
252  O O   . SER   A 31  ? 0.2057 0.2368 0.3150 -0.0014 -0.0111 0.0379  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2359 0.2638 0.3643 -0.0030 -0.0141 0.0514  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3193 0.3467 0.4285 -0.0091 -0.0177 0.0542  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1663 0.1902 0.2571 -0.0034 -0.0088 0.0295  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1577 0.1824 0.2336 -0.0052 -0.0094 0.0260  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1577 0.1799 0.2302 -0.0020 -0.0060 0.0164  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1661 0.1885 0.2283 -0.0027 -0.0062 0.0134  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1606 0.1829 0.2221 -0.0101 -0.0102 0.0271  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1606 0.1843 0.2191 -0.0155 -0.0144 0.0369  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1871 0.2065 0.2285 -0.0215 -0.0133 0.0369  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1825 0.2007 0.2108 -0.0233 -0.0121 0.0319  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1890 0.2034 0.2007 -0.0300 -0.0114 0.0326  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2138 0.2254 0.2177 -0.0363 -0.0124 0.0383  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1946 0.2072 0.1964 -0.0312 -0.0096 0.0276  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1514 0.1706 0.2315 0.0008  -0.0034 0.0116  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1509 0.1670 0.2254 0.0022  -0.0019 0.0032  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1391 0.1543 0.2038 0.0005  -0.0033 0.0011  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1489 0.1631 0.2066 0.0008  -0.0039 -0.0033 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1694 0.1857 0.2407 0.0035  -0.0002 -0.0002 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1764 0.1886 0.2400 0.0037  0.0005  -0.0081 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1568 0.1653 0.2237 0.0038  0.0010  -0.0120 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1647 0.1770 0.2185 0.0031  0.0000  -0.0099 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1356 0.1506 0.2006 -0.0016 -0.0034 0.0045  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1336 0.1472 0.1927 -0.0030 -0.0029 0.0023  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1384 0.1503 0.2053 -0.0031 -0.0016 0.0009  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1487 0.1600 0.2222 -0.0037 -0.0008 0.0040  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1386 0.1522 0.1887 -0.0067 -0.0020 0.0063  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1488 0.1638 0.1899 -0.0077 -0.0034 0.0071  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1659 0.1791 0.1965 -0.0129 -0.0023 0.0105  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1549 0.1690 0.1925 -0.0057 -0.0032 0.0019  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1368 0.1480 0.2040 -0.0029 -0.0015 -0.0028 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1410 0.1513 0.2172 -0.0034 -0.0001 -0.0037 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1455 0.1557 0.2207 -0.0041 0.0020  -0.0048 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1541 0.1649 0.2254 -0.0030 0.0001  -0.0065 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1376 0.1475 0.2221 -0.0021 -0.0030 -0.0077 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1505 0.1601 0.2469 -0.0030 -0.0023 -0.0085 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1684 0.1762 0.2720 -0.0030 -0.0044 -0.0113 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1534 0.1648 0.2541 -0.0029 -0.0044 -0.0105 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1422 0.1512 0.2218 -0.0060 0.0068  -0.0034 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1487 0.1568 0.2314 -0.0065 0.0111  -0.0048 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1662 0.1754 0.2657 -0.0061 0.0123  -0.0058 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1800 0.1886 0.2840 -0.0076 0.0143  -0.0043 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1716 0.1759 0.2435 -0.0104 0.0180  -0.0030 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1805 0.1824 0.2578 -0.0109 0.0250  -0.0054 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1765 0.1801 0.2330 -0.0116 0.0155  -0.0016 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1651 0.1764 0.2751 -0.0044 0.0106  -0.0075 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1769 0.1904 0.3058 -0.0042 0.0110  -0.0079 43  SER   A CA  
299  C C   . SER   A 37  ? 0.1933 0.2064 0.3325 -0.0040 0.0181  -0.0079 43  SER   A C   
300  O O   . SER   A 37  ? 0.1699 0.1807 0.3012 -0.0036 0.0210  -0.0083 43  SER   A O   
301  C CB  . SER   A 37  ? 0.1845 0.2013 0.3207 -0.0030 0.0011  -0.0091 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1948 0.2128 0.3286 -0.0015 -0.0038 -0.0091 43  SER   A OG  
303  N N   . SER   A 38  ? 0.1966 0.2113 0.3545 -0.0045 0.0221  -0.0075 44  SER   A N   
304  C CA  . SER   A 38  ? 0.2089 0.2232 0.3810 -0.0039 0.0304  -0.0077 44  SER   A CA  
305  C C   . SER   A 38  ? 0.2152 0.2347 0.4062 -0.0009 0.0229  -0.0065 44  SER   A C   
306  O O   . SER   A 38  ? 0.2204 0.2444 0.4175 -0.0005 0.0119  -0.0055 44  SER   A O   
307  C CB  . SER   A 38  ? 0.2392 0.2525 0.4237 -0.0062 0.0401  -0.0075 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2573 0.2755 0.4562 -0.0061 0.0330  -0.0065 44  SER   A OG  
309  N N   . THR   A 39  ? 0.2154 0.2338 0.4155 0.0007  0.0288  -0.0063 45  THR   A N   
310  C CA  . THR   A 39  ? 0.2382 0.2615 0.4588 0.0036  0.0218  -0.0034 45  THR   A CA  
311  C C   . THR   A 39  ? 0.2790 0.3034 0.5285 0.0047  0.0321  -0.0025 45  THR   A C   
312  O O   . THR   A 39  ? 0.2915 0.3105 0.5389 0.0032  0.0468  -0.0053 45  THR   A O   
313  C CB  . THR   A 39  ? 0.2505 0.2711 0.4587 0.0053  0.0192  -0.0031 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2621 0.2760 0.4664 0.0050  0.0332  -0.0057 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2492 0.2682 0.4298 0.0042  0.0115  -0.0043 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2981 0.3290 0.5743 0.0070  0.0248  0.0017  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3173 0.3502 0.6265 0.0088  0.0343  0.0035  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3376 0.3662 0.6514 0.0118  0.0409  0.0038  46  THR   A C   
319  O O   . THR   A 40  ? 0.3561 0.3810 0.6865 0.0127  0.0563  0.0021  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3371 0.3802 0.6768 0.0095  0.0219  0.0092  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3583 0.4047 0.6917 0.0100  0.0048  0.0131  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3460 0.3923 0.6862 0.0062  0.0186  0.0082  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3277 0.3560 0.6273 0.0129  0.0302  0.0057  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3200 0.3437 0.6234 0.0156  0.0353  0.0064  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3299 0.3434 0.6009 0.0135  0.0458  0.0000  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3297 0.3416 0.5729 0.0106  0.0425  -0.0027 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3119 0.3402 0.6166 0.0173  0.0179  0.0126  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3362 0.3426 0.6120 0.0146  0.0577  -0.0020 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3659 0.3618 0.6122 0.0116  0.0676  -0.0080 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3705 0.3665 0.5967 0.0121  0.0554  -0.0061 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3730 0.3721 0.6140 0.0155  0.0474  -0.0010 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4084 0.3957 0.6695 0.0122  0.0855  -0.0114 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4978 0.4729 0.7288 0.0079  0.0958  -0.0180 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.5994 0.5680 0.8074 0.0015  0.1070  -0.0239 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6211 0.5931 0.8379 0.0005  0.1101  -0.0237 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6193 0.5781 0.7971 -0.0038 0.1128  -0.0288 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3720 0.3647 0.5661 0.0085  0.0538  -0.0092 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3777 0.3709 0.5526 0.0086  0.0429  -0.0076 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3886 0.3747 0.5565 0.0087  0.0473  -0.0087 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4063 0.3838 0.5709 0.0065  0.0612  -0.0134 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3689 0.3575 0.5292 0.0101  0.0356  -0.0050 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3627 0.3459 0.5172 0.0104  0.0363  -0.0045 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3650 0.3411 0.4902 0.0058  0.0418  -0.0096 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3672 0.3362 0.4904 0.0053  0.0471  -0.0109 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3677 0.3566 0.5253 0.0129  0.0212  0.0022  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3745 0.3692 0.5070 0.0107  0.0082  0.0027  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3514 0.3289 0.4563 0.0022  0.0406  -0.0121 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3333 0.3068 0.4118 -0.0024 0.0414  -0.0148 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3211 0.2861 0.3847 -0.0087 0.0537  -0.0204 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3405 0.3035 0.4110 -0.0098 0.0617  -0.0225 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3183 0.2994 0.3847 -0.0026 0.0304  -0.0124 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3567 0.3433 0.4271 0.0010  0.0189  -0.0081 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3752 0.3591 0.4418 0.0012  0.0174  -0.0069 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.2867 0.2796 0.3627 0.0027  0.0115  -0.0061 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2964 0.2561 0.3386 -0.0137 0.0546  -0.0224 52  THR   A N   
356  C CA  . THR   A 46  ? 0.3050 0.2564 0.3263 -0.0219 0.0626  -0.0269 52  THR   A CA  
357  C C   . THR   A 46  ? 0.2830 0.2400 0.2856 -0.0252 0.0529  -0.0239 52  THR   A C   
358  O O   . THR   A 46  ? 0.2765 0.2386 0.2778 -0.0229 0.0442  -0.0210 52  THR   A O   
359  C CB  . THR   A 46  ? 0.3614 0.3024 0.3751 -0.0254 0.0695  -0.0308 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4014 0.3351 0.4320 -0.0235 0.0816  -0.0343 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3855 0.3185 0.3718 -0.0357 0.0738  -0.0347 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2621 0.2180 0.2517 -0.0308 0.0545  -0.0242 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2405 0.2017 0.2158 -0.0341 0.0454  -0.0203 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2519 0.2062 0.2064 -0.0427 0.0469  -0.0220 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2773 0.2213 0.2201 -0.0496 0.0565  -0.0264 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2256 0.1899 0.1991 -0.0359 0.0445  -0.0179 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2246 0.1943 0.2189 -0.0286 0.0443  -0.0172 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2404 0.2110 0.2041 -0.0383 0.0343  -0.0125 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2275 0.2062 0.2335 -0.0214 0.0340  -0.0142 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2407 0.2000 0.1896 -0.0433 0.0381  -0.0187 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2430 0.1973 0.1728 -0.0523 0.0372  -0.0192 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2537 0.2070 0.1680 -0.0605 0.0354  -0.0166 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2441 0.2050 0.1642 -0.0578 0.0301  -0.0118 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2365 0.1987 0.1681 -0.0503 0.0273  -0.0150 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2668 0.2098 0.1603 -0.0713 0.0400  -0.0197 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.2850 0.2263 0.1600 -0.0812 0.0367  -0.0161 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3268 0.2658 0.1851 -0.0904 0.0306  -0.0149 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3514 0.2780 0.1921 -0.0994 0.0376  -0.0210 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3016 0.2302 0.1638 -0.0877 0.0496  -0.0218 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.3060 0.2367 0.1875 -0.0788 0.0567  -0.0234 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3205 0.2631 0.2144 -0.0729 0.0479  -0.0159 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.2971 0.2406 0.2093 -0.0655 0.0551  -0.0183 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3179 0.2708 0.2457 -0.0587 0.0495  -0.0137 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2838 0.2456 0.2123 -0.0576 0.0377  -0.0069 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.3049 0.2584 0.2493 -0.0531 0.0560  -0.0160 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3183 0.2689 0.1835 -0.0884 0.0181  -0.0074 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3330 0.2841 0.1893 -0.0951 0.0113  -0.0057 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3292 0.2947 0.1960 -0.0933 -0.0025 0.0046  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3215 0.2955 0.2030 -0.0858 -0.0055 0.0092  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3105 0.2597 0.1769 -0.0888 0.0162  -0.0111 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2798 0.2429 0.1743 -0.0734 0.0116  -0.0073 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3443 0.3126 0.2071 -0.0991 -0.0100 0.0077  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3382 0.3204 0.2153 -0.0968 -0.0217 0.0172  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.3393 0.3270 0.2301 -0.0910 -0.0225 0.0163  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3451 0.3420 0.2444 -0.0925 -0.0313 0.0231  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3982 0.3817 0.2618 -0.1099 -0.0325 0.0250  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.5133 0.4879 0.3566 -0.1222 -0.0329 0.0212  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5136 0.4802 0.3540 -0.1202 -0.0237 0.0121  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.6050 0.5802 0.4356 -0.1344 -0.0428 0.0276  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3161 0.2988 0.2114 -0.0837 -0.0135 0.0087  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2983 0.2857 0.2059 -0.0780 -0.0140 0.0084  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2761 0.2769 0.2026 -0.0711 -0.0201 0.0153  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2575 0.2626 0.1926 -0.0653 -0.0204 0.0174  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2982 0.2791 0.2099 -0.0705 -0.0047 0.0013  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2984 0.2627 0.1937 -0.0776 0.0048  -0.0075 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2569 0.2635 0.1909 -0.0713 -0.0238 0.0181  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2292 0.2472 0.1826 -0.0645 -0.0268 0.0232  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.1958 0.2138 0.1556 -0.0587 -0.0221 0.0199  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.1930 0.2191 0.1666 -0.0551 -0.0234 0.0234  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2505 0.2781 0.2118 -0.0702 -0.0361 0.0321  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3180 0.3487 0.2794 -0.0733 -0.0420 0.0381  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3664 0.4078 0.3404 -0.0782 -0.0521 0.0485  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.3862 0.4268 0.3494 -0.0892 -0.0600 0.0532  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3010 0.3525 0.2988 -0.0709 -0.0521 0.0525  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1838 0.1919 0.1341 -0.0580 -0.0160 0.0133  60  THR   A N   
416  C CA  . THR   A 54  ? 0.1995 0.2062 0.1545 -0.0524 -0.0117 0.0108  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2071 0.2060 0.1588 -0.0474 -0.0060 0.0055  60  THR   A C   
418  O O   . THR   A 54  ? 0.2223 0.2146 0.1661 -0.0502 -0.0036 0.0024  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2393 0.2423 0.1895 -0.0580 -0.0113 0.0101  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2705 0.2623 0.2071 -0.0637 -0.0082 0.0052  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2441 0.2552 0.1990 -0.0642 -0.0177 0.0158  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1998 0.1996 0.1580 -0.0405 -0.0039 0.0049  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1854 0.1791 0.1437 -0.0356 -0.0001 0.0014  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1737 0.1692 0.1374 -0.0297 0.0000  0.0023  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1749 0.1739 0.1398 -0.0303 -0.0008 0.0046  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1616 0.1543 0.1282 -0.0249 0.0011  0.0008  62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1517 0.1447 0.1205 -0.0206 0.0002  0.0021  62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1488 0.1446 0.1220 -0.0163 -0.0015 0.0014  62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1676 0.1615 0.1439 -0.0154 -0.0007 -0.0002 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1796 0.1648 0.1482 -0.0200 0.0019  0.0020  62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2077 0.1928 0.1773 -0.0164 -0.0007 0.0045  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2001 0.1816 0.1643 -0.0247 0.0040  0.0022  62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1415 0.1405 0.1146 -0.0142 -0.0030 0.0023  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1450 0.1455 0.1213 -0.0110 -0.0048 0.0011  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1700 0.1677 0.1428 -0.0095 -0.0072 0.0019  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1738 0.1697 0.1406 -0.0108 -0.0068 0.0036  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1429 0.1489 0.1221 -0.0106 -0.0043 0.0005  63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1411 0.1488 0.1178 -0.0106 -0.0027 0.0006  63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1623 0.1719 0.1386 -0.0129 -0.0005 0.0024  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1575 0.1644 0.1325 -0.0090 -0.0026 -0.0015 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1593 0.1702 0.1347 -0.0130 0.0028  0.0023  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1709 0.1778 0.1425 -0.0097 0.0011  -0.0024 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1677 0.1768 0.1404 -0.0114 0.0043  -0.0004 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.1973 0.2059 0.1676 -0.0123 0.0096  -0.0015 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1661 0.1635 0.1421 -0.0075 -0.0101 0.0011  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1801 0.1750 0.1515 -0.0073 -0.0142 0.0026  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1776 0.1738 0.1428 -0.0081 -0.0139 0.0001  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1779 0.1768 0.1478 -0.0070 -0.0129 -0.0026 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1767 0.1706 0.1565 -0.0055 -0.0185 0.0038  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.1873 0.1789 0.1616 -0.0066 -0.0248 0.0065  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2111 0.1989 0.1797 -0.0080 -0.0270 0.0108  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.1996 0.1922 0.1732 -0.0071 -0.0291 0.0051  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2241 0.2093 0.1851 -0.0102 -0.0338 0.0143  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2173 0.2070 0.1825 -0.0098 -0.0358 0.0077  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2412 0.2274 0.2000 -0.0115 -0.0386 0.0127  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.2998 0.2826 0.2482 -0.0153 -0.0464 0.0164  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1826 0.1759 0.1367 -0.0103 -0.0137 0.0009  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1973 0.1896 0.1432 -0.0120 -0.0114 -0.0024 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.2085 0.1958 0.1435 -0.0147 -0.0171 -0.0016 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2203 0.2035 0.1446 -0.0174 -0.0190 0.0016  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.2058 0.1981 0.1468 -0.0137 -0.0050 -0.0024 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2244 0.2130 0.1540 -0.0165 0.0011  -0.0071 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.2149 0.2023 0.1522 -0.0146 -0.0207 -0.0041 66  SER   A N   
464  C CA  . SER   A 60  ? 0.2255 0.2085 0.1528 -0.0182 -0.0282 -0.0028 66  SER   A CA  
465  C C   . SER   A 60  ? 0.2214 0.1980 0.1280 -0.0236 -0.0260 -0.0048 66  SER   A C   
466  O O   . SER   A 60  ? 0.2467 0.2187 0.1408 -0.0279 -0.0326 -0.0010 66  SER   A O   
467  C CB  . SER   A 60  ? 0.2694 0.2539 0.2040 -0.0177 -0.0323 -0.0054 66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3576 0.3415 0.2902 -0.0180 -0.0259 -0.0118 66  SER   A OG  
469  N N   . SER   A 61  ? 0.2130 0.1889 0.1164 -0.0238 -0.0163 -0.0102 67  SER   A N   
470  C CA  . SER   A 61  ? 0.2362 0.2048 0.1198 -0.0294 -0.0112 -0.0133 67  SER   A CA  
471  C C   . SER   A 61  ? 0.2379 0.2040 0.1114 -0.0317 -0.0096 -0.0087 67  SER   A C   
472  O O   . SER   A 61  ? 0.2619 0.2210 0.1166 -0.0372 -0.0052 -0.0106 67  SER   A O   
473  C CB  . SER   A 61  ? 0.2577 0.2262 0.1448 -0.0285 0.0003  -0.0204 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2609 0.2356 0.1625 -0.0242 0.0069  -0.0189 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.2376 0.2083 0.1226 -0.0281 -0.0126 -0.0029 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.2396 0.2077 0.1171 -0.0301 -0.0125 0.0024  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2609 0.2288 0.1428 -0.0293 -0.0229 0.0100  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2795 0.2450 0.1579 -0.0304 -0.0236 0.0154  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2344 0.2070 0.1225 -0.0273 -0.0040 0.0021  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.2308 0.2038 0.1176 -0.0281 0.0070  -0.0038 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.2658 0.2313 0.1329 -0.0340 0.0123  -0.0041 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.3073 0.2725 0.1756 -0.0347 0.0250  -0.0100 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.3250 0.2856 0.1862 -0.0368 0.0302  -0.0167 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.3008 0.2569 0.1513 -0.0391 0.0227  -0.0184 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.3139 0.2742 0.1798 -0.0370 0.0432  -0.0218 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2654 0.2365 0.1593 -0.0265 -0.0300 0.0107  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2811 0.2530 0.1861 -0.0244 -0.0382 0.0177  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2699 0.2431 0.1846 -0.0214 -0.0335 0.0202  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.2927 0.2627 0.2082 -0.0219 -0.0374 0.0269  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3334 0.3000 0.2258 -0.0295 -0.0479 0.0245  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.4028 0.3688 0.2905 -0.0326 -0.0556 0.0233  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4397 0.4020 0.3207 -0.0372 -0.0686 0.0326  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.4717 0.4317 0.3403 -0.0431 -0.0760 0.0307  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.4989 0.4511 0.3403 -0.0519 -0.0794 0.0314  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.5193 0.4658 0.3443 -0.0554 -0.0761 0.0347  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.4844 0.4337 0.3137 -0.0581 -0.0858 0.0285  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2440 0.2211 0.1658 -0.0188 -0.0255 0.0154  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2406 0.2181 0.1686 -0.0175 -0.0209 0.0169  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2247 0.2072 0.1653 -0.0145 -0.0167 0.0130  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2214 0.2075 0.1636 -0.0137 -0.0148 0.0087  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.2800 0.2562 0.1966 -0.0207 -0.0145 0.0161  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.4154 0.3853 0.3190 -0.0246 -0.0165 0.0217  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.5126 0.4821 0.4084 -0.0274 -0.0079 0.0199  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5992 0.5627 0.4846 -0.0310 -0.0081 0.0259  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6602 0.6173 0.5286 -0.0352 -0.0142 0.0297  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2169 0.1988 0.1645 -0.0138 -0.0145 0.0143  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2020 0.1875 0.1576 -0.0129 -0.0103 0.0109  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2105 0.1974 0.1625 -0.0155 -0.0055 0.0105  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2284 0.2120 0.1750 -0.0175 -0.0046 0.0133  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.1987 0.1811 0.1634 -0.0117 -0.0101 0.0117  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2108 0.1924 0.1840 -0.0090 -0.0139 0.0126  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2501 0.2342 0.2315 -0.0073 -0.0125 0.0094  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2190 0.1977 0.1954 -0.0080 -0.0191 0.0173  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2302 0.2132 0.2205 -0.0051 -0.0164 0.0117  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2593 0.2395 0.2477 -0.0054 -0.0210 0.0167  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1783 0.1706 0.1343 -0.0156 -0.0029 0.0078  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1799 0.1752 0.1361 -0.0183 0.0008  0.0082  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.1793 0.1774 0.1417 -0.0198 0.0010  0.0075  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1740 0.1741 0.1403 -0.0186 -0.0003 0.0058  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.1849 0.1850 0.1419 -0.0179 0.0037  0.0068  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2072 0.2035 0.1544 -0.0183 0.0051  0.0067  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2342 0.2278 0.1749 -0.0211 0.0082  0.0089  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2136 0.2087 0.1569 -0.0170 0.0039  0.0042  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2418 0.2307 0.1702 -0.0228 0.0100  0.0088  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2253 0.2155 0.1561 -0.0191 0.0053  0.0036  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2538 0.2408 0.1762 -0.0221 0.0084  0.0060  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.2933 0.2743 0.2001 -0.0253 0.0102  0.0055  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.1849 0.1827 0.1471 -0.0235 0.0024  0.0088  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.1757 0.1759 0.1411 -0.0268 0.0017  0.0083  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.1976 0.2066 0.1700 -0.0273 0.0012  0.0097  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2322 0.2447 0.2076 -0.0267 0.0035  0.0110  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.1885 0.1850 0.1512 -0.0313 0.0029  0.0095  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2124 0.2087 0.1734 -0.0301 0.0049  0.0116  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.1973 0.1924 0.1558 -0.0255 0.0044  0.0111  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1803 0.1924 0.1556 -0.0290 -0.0013 0.0098  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1857 0.2063 0.1706 -0.0293 -0.0027 0.0125  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1733 0.1965 0.1590 -0.0350 -0.0069 0.0150  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1812 0.1989 0.1582 -0.0379 -0.0080 0.0132  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2137 0.2362 0.2029 -0.0244 -0.0025 0.0113  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2342 0.2558 0.2236 -0.0203 0.0014  0.0094  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2120 0.2295 0.1953 -0.0236 -0.0038 0.0088  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1723 0.2040 0.1691 -0.0369 -0.0093 0.0197  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1870 0.2229 0.1861 -0.0426 -0.0154 0.0239  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1774 0.2187 0.1871 -0.0382 -0.0164 0.0262  75  SER   A C   
545  O O   . SER   A 69  ? 0.1852 0.2306 0.2065 -0.0331 -0.0128 0.0265  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2279 0.2711 0.2370 -0.0475 -0.0186 0.0293  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3221 0.3598 0.3217 -0.0520 -0.0176 0.0271  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1511 0.1913 0.1564 -0.0403 -0.0202 0.0273  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1638 0.2078 0.1791 -0.0360 -0.0208 0.0295  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1702 0.2189 0.1891 -0.0416 -0.0284 0.0367  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1909 0.2368 0.1975 -0.0496 -0.0329 0.0381  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1778 0.2148 0.1849 -0.0314 -0.0169 0.0235  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1739 0.2028 0.1649 -0.0352 -0.0168 0.0200  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1737 0.1958 0.1553 -0.0353 -0.0132 0.0152  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1702 0.1975 0.1561 -0.0388 -0.0194 0.0217  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1886 0.2026 0.1584 -0.0384 -0.0113 0.0115  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1907 0.2094 0.1619 -0.0426 -0.0171 0.0177  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1920 0.2041 0.1563 -0.0422 -0.0126 0.0123  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1600 0.2157 0.1963 -0.0382 -0.0301 0.0420  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1725 0.2333 0.2147 -0.0433 -0.0384 0.0508  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1847 0.2388 0.2113 -0.0461 -0.0400 0.0496  77  SER   A C   
562  O O   . SER   A 71  ? 0.1910 0.2384 0.2092 -0.0418 -0.0339 0.0423  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1677 0.2371 0.2359 -0.0381 -0.0387 0.0570  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1863 0.2521 0.2577 -0.0303 -0.0318 0.0516  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1888 0.2448 0.2117 -0.0538 -0.0485 0.0573  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2066 0.2559 0.2140 -0.0576 -0.0496 0.0571  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2183 0.2689 0.2389 -0.0496 -0.0463 0.0575  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2066 0.2645 0.2493 -0.0440 -0.0466 0.0616  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2535 0.3048 0.2536 -0.0689 -0.0604 0.0667  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.3033 0.3500 0.2847 -0.0784 -0.0627 0.0641  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3689 0.4146 0.3362 -0.0916 -0.0733 0.0724  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4551 0.4931 0.4000 -0.1014 -0.0732 0.0669  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.5132 0.5520 0.4461 -0.1157 -0.0856 0.0757  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2072 0.2505 0.2156 -0.0495 -0.0427 0.0534  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2072 0.2513 0.2283 -0.0424 -0.0398 0.0536  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2055 0.2569 0.2440 -0.0432 -0.0470 0.0652  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2195 0.2718 0.2511 -0.0515 -0.0550 0.0735  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2393 0.2746 0.2431 -0.0450 -0.0363 0.0493  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2717 0.3004 0.2547 -0.0514 -0.0344 0.0440  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2351 0.2686 0.2191 -0.0559 -0.0401 0.0480  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.1879 0.2438 0.2486 -0.0351 -0.0440 0.0658  80  SER   A N   
582  C CA  . SER   A 74  ? 0.1962 0.2595 0.2789 -0.0348 -0.0501 0.0774  80  SER   A CA  
583  C C   . SER   A 74  ? 0.1861 0.2493 0.2883 -0.0258 -0.0437 0.0752  80  SER   A C   
584  O O   . SER   A 74  ? 0.1904 0.2482 0.2874 -0.0206 -0.0355 0.0648  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2430 0.3150 0.3395 -0.0368 -0.0551 0.0839  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3168 0.3907 0.4268 -0.0293 -0.0469 0.0773  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1737 0.2426 0.2988 -0.0246 -0.0481 0.0858  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.1791 0.2471 0.3250 -0.0166 -0.0417 0.0844  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.1898 0.2626 0.3569 -0.0109 -0.0358 0.0820  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.1960 0.2771 0.3804 -0.0126 -0.0409 0.0913  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.1875 0.2590 0.3494 -0.0188 -0.0495 0.0983  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2443 0.3127 0.4238 -0.0123 -0.0440 0.0977  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2612 0.3204 0.4208 -0.0123 -0.0396 0.0894  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2711 0.3446 0.4720 -0.0140 -0.0524 0.1137  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.1904 0.2579 0.3561 -0.0050 -0.0250 0.0700  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.1969 0.2664 0.3764 -0.0004 -0.0170 0.0653  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2107 0.2751 0.4042 0.0061  -0.0070 0.0591  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2140 0.2709 0.3950 0.0072  -0.0042 0.0522  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2163 0.2824 0.3720 -0.0021 -0.0138 0.0556  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2384 0.3094 0.3841 -0.0089 -0.0228 0.0619  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2279 0.2928 0.3914 0.0023  -0.0034 0.0481  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2664 0.3342 0.3914 -0.0110 -0.0207 0.0544  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2078 0.2759 0.4290 0.0102  -0.0010 0.0616  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2308 0.2923 0.4656 0.0158  0.0103  0.0548  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2453 0.2981 0.4589 0.0167  0.0198  0.0397  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.2662 0.3205 0.4705 0.0153  0.0221  0.0361  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2354 0.3025 0.5066 0.0197  0.0161  0.0608  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2736 0.3322 0.5590 0.0251  0.0299  0.0523  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.2898 0.3451 0.5904 0.0276  0.0300  0.0558  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.2992 0.3518 0.5797 0.0267  0.0432  0.0402  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.3092 0.3553 0.6223 0.0318  0.0435  0.0470  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.3196 0.3625 0.6096 0.0303  0.0566  0.0312  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3118 0.3514 0.6190 0.0329  0.0569  0.0344  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.2300 0.2737 0.4355 0.0183  0.0245  0.0313  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.2360 0.2708 0.4206 0.0180  0.0319  0.0178  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.2496 0.2764 0.4477 0.0213  0.0434  0.0107  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.2524 0.2764 0.4616 0.0228  0.0428  0.0127  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.2453 0.2761 0.4040 0.0152  0.0251  0.0140  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.2586 0.2804 0.3980 0.0145  0.0310  0.0015  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.2458 0.2827 0.3909 0.0117  0.0159  0.0195  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.2601 0.2818 0.4559 0.0217  0.0546  0.0021  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.2767 0.2886 0.4824 0.0237  0.0680  -0.0066 85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.2880 0.2899 0.4765 0.0219  0.0674  -0.0151 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.2965 0.2982 0.4611 0.0189  0.0587  -0.0167 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.3349 0.3420 0.5341 0.0226  0.0804  -0.0153 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.4761 0.4778 0.7014 0.0258  0.0961  -0.0190 85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.6359 0.6281 0.8517 0.0238  0.1121  -0.0308 85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.6914 0.6777 0.8743 0.0190  0.1112  -0.0385 85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.6715 0.6617 0.9137 0.0268  0.1259  -0.0320 85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.2925 0.2856 0.4948 0.0236  0.0772  -0.0207 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.3021 0.2850 0.4899 0.0213  0.0773  -0.0293 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.3073 0.2828 0.4617 0.0160  0.0782  -0.0405 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.3210 0.2940 0.4675 0.0146  0.0857  -0.0453 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.3061 0.2793 0.5140 0.0233  0.0898  -0.0348 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.3011 0.2734 0.4372 0.0129  0.0702  -0.0437 87  SER   A N   
636  C CA  . SER   A 81  ? 0.3007 0.2662 0.4065 0.0074  0.0686  -0.0527 87  SER   A CA  
637  C C   . SER   A 81  ? 0.3178 0.2738 0.4177 0.0043  0.0680  -0.0600 87  SER   A C   
638  O O   . SER   A 81  ? 0.3179 0.2723 0.4377 0.0070  0.0706  -0.0585 87  SER   A O   
639  C CB  . SER   A 81  ? 0.3044 0.2785 0.3949 0.0063  0.0559  -0.0466 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.2987 0.2767 0.3920 0.0068  0.0462  -0.0419 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.3297 0.2795 0.4036 -0.0015 0.0640  -0.0673 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.3471 0.2888 0.4154 -0.0054 0.0614  -0.0735 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.3381 0.2883 0.4162 -0.0030 0.0501  -0.0653 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.3477 0.2932 0.4286 -0.0050 0.0482  -0.0684 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.4345 0.3686 0.4726 -0.0133 0.0574  -0.0817 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.5641 0.4930 0.5844 -0.0165 0.0646  -0.0866 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.6924 0.6316 0.7049 -0.0150 0.0569  -0.0787 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.7499 0.6901 0.7442 -0.0190 0.0461  -0.0778 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.6909 0.6364 0.7156 -0.0103 0.0620  -0.0736 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.3237 0.2858 0.4056 0.0004  0.0429  -0.0552 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.3087 0.2780 0.3963 0.0017  0.0334  -0.0479 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.2804 0.2551 0.3909 0.0063  0.0343  -0.0391 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.2794 0.2561 0.3966 0.0065  0.0296  -0.0351 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.3062 0.2831 0.3808 0.0012  0.0252  -0.0432 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.3210 0.2933 0.3735 -0.0035 0.0224  -0.0496 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.3373 0.3081 0.3780 -0.0046 0.0262  -0.0518 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.3254 0.2951 0.3695 -0.0074 0.0156  -0.0527 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.3576 0.3240 0.3766 -0.0096 0.0226  -0.0562 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.3418 0.3078 0.3660 -0.0124 0.0111  -0.0567 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.3697 0.3337 0.3804 -0.0137 0.0145  -0.0584 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.4113 0.3711 0.4011 -0.0193 0.0093  -0.0613 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.2649 0.2419 0.3886 0.0096  0.0404  -0.0355 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.2491 0.2322 0.3955 0.0134  0.0396  -0.0251 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.2683 0.2492 0.4348 0.0167  0.0495  -0.0248 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.2781 0.2570 0.4404 0.0165  0.0562  -0.0298 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.2288 0.2229 0.3728 0.0141  0.0319  -0.0149 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.2078 0.2052 0.3344 0.0115  0.0232  -0.0136 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.2115 0.2103 0.3413 0.0108  0.0182  -0.0091 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.2159 0.2151 0.3248 0.0097  0.0206  -0.0164 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.2093 0.2107 0.3258 0.0085  0.0121  -0.0081 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.1991 0.2010 0.2956 0.0078  0.0137  -0.0149 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.1971 0.2005 0.2982 0.0073  0.0099  -0.0107 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.1843 0.1897 0.2756 0.0055  0.0051  -0.0098 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.2779 0.2597 0.4686 0.0197  0.0506  -0.0178 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.2784 0.2604 0.4945 0.0236  0.0594  -0.0147 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.2737 0.2674 0.4945 0.0250  0.0547  -0.0049 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.2830 0.2838 0.4893 0.0229  0.0445  0.0005  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.2746 0.2562 0.5147 0.0261  0.0581  -0.0067 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.2881 0.2749 0.5150 0.0236  0.0459  -0.0004 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.2783 0.2620 0.4758 0.0196  0.0436  -0.0106 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.2616 0.2574 0.5058 0.0284  0.0623  -0.0017 92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.2627 0.2702 0.5153 0.0293  0.0573  0.0087  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2433 0.2598 0.5022 0.0286  0.0436  0.0233  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.2417 0.2563 0.5166 0.0301  0.0426  0.0286  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.2671 0.2755 0.5508 0.0334  0.0681  0.0108  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2213 0.2455 0.4632 0.0254  0.0336  0.0285  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2112 0.2420 0.4533 0.0230  0.0213  0.0412  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2165 0.2562 0.4473 0.0195  0.0127  0.0477  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2374 0.2780 0.4595 0.0193  0.0162  0.0418  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.2051 0.2300 0.4271 0.0206  0.0180  0.0365  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.2390 0.2629 0.4308 0.0175  0.0160  0.0281  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.2443 0.2604 0.4201 0.0164  0.0178  0.0182  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.2367 0.2543 0.3894 0.0129  0.0117  0.0168  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.2148 0.2331 0.3512 0.0117  0.0117  0.0116  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2227 0.2415 0.3414 0.0090  0.0069  0.0106  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.2108 0.2287 0.3493 0.0132  0.0171  0.0075  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2117 0.2568 0.4395 0.0158  0.0016  0.0591  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2170 0.2683 0.4289 0.0109  -0.0066 0.0635  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2101 0.2562 0.3917 0.0076  -0.0084 0.0562  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2239 0.2659 0.4010 0.0067  -0.0098 0.0567  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2256 0.2844 0.4473 0.0069  -0.0179 0.0796  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2295 0.2957 0.4835 0.0098  -0.0179 0.0887  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2393 0.3047 0.5229 0.0145  -0.0141 0.0937  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2384 0.3122 0.4958 0.0079  -0.0206 0.0919  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2537 0.3262 0.5716 0.0177  -0.0130 0.1024  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2539 0.3354 0.5450 0.0108  -0.0199 0.1005  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2676 0.3486 0.5897 0.0159  -0.0161 0.1060  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3030 0.3920 0.6627 0.0191  -0.0149 0.1153  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1824 0.2284 0.3455 0.0060  -0.0075 0.0494  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1671 0.2087 0.3046 0.0030  -0.0092 0.0434  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1562 0.2020 0.2817 -0.0031 -0.0174 0.0508  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1743 0.2255 0.3029 -0.0048 -0.0201 0.0548  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1546 0.1925 0.2794 0.0046  -0.0035 0.0319  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1664 0.2006 0.2683 0.0017  -0.0056 0.0268  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.1684 0.1978 0.2601 0.0036  -0.0010 0.0164  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.1803 0.2060 0.2777 0.0063  0.0041  0.0107  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1420 0.1706 0.2171 0.0013  -0.0028 0.0136  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1515 0.1945 0.2645 -0.0071 -0.0211 0.0532  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1582 0.2029 0.2564 -0.0144 -0.0279 0.0594  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1842 0.2250 0.2601 -0.0167 -0.0256 0.0509  96  SER   A C   
721  O O   . SER   A 90  ? 0.1939 0.2308 0.2659 -0.0128 -0.0198 0.0414  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1889 0.2312 0.2833 -0.0186 -0.0318 0.0663  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2143 0.2502 0.3021 -0.0166 -0.0261 0.0588  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1796 0.2213 0.2415 -0.0237 -0.0306 0.0547  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1817 0.2187 0.2232 -0.0268 -0.0282 0.0476  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1723 0.2099 0.2162 -0.0217 -0.0237 0.0400  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1745 0.2074 0.2067 -0.0212 -0.0198 0.0325  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1967 0.2267 0.2268 -0.0276 -0.0239 0.0427  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2311 0.2591 0.2554 -0.0337 -0.0274 0.0502  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2815 0.3054 0.2856 -0.0427 -0.0291 0.0518  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2392 0.2684 0.2748 -0.0328 -0.0294 0.0566  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2843 0.3068 0.2861 -0.0473 -0.0323 0.0594  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2710 0.2968 0.2921 -0.0414 -0.0328 0.0628  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1531 0.1964 0.2124 -0.0186 -0.0242 0.0426  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1565 0.1998 0.2171 -0.0144 -0.0193 0.0358  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1535 0.2005 0.2108 -0.0183 -0.0221 0.0383  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1604 0.2130 0.2256 -0.0219 -0.0277 0.0467  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1675 0.2132 0.2478 -0.0085 -0.0152 0.0353  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1815 0.2255 0.2618 -0.0047 -0.0087 0.0277  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1866 0.2235 0.2512 -0.0034 -0.0058 0.0187  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2066 0.2517 0.3070 0.0001  -0.0031 0.0274  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1480 0.1917 0.1945 -0.0177 -0.0186 0.0316  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1558 0.2018 0.1982 -0.0215 -0.0205 0.0332  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1637 0.2108 0.2126 -0.0170 -0.0150 0.0291  99  MET   A C   
745  O O   . MET   A 93  ? 0.1757 0.2176 0.2184 -0.0134 -0.0103 0.0223  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1671 0.2065 0.1895 -0.0255 -0.0202 0.0287  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1865 0.2232 0.1992 -0.0313 -0.0240 0.0319  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2415 0.2682 0.2330 -0.0353 -0.0204 0.0250  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2841 0.3073 0.2798 -0.0268 -0.0141 0.0177  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1535 0.2068 0.2142 -0.0178 -0.0155 0.0334  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1550 0.2084 0.2209 -0.0142 -0.0086 0.0293  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1499 0.2027 0.2061 -0.0177 -0.0087 0.0283  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1582 0.2138 0.2123 -0.0232 -0.0145 0.0330  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1710 0.2317 0.2614 -0.0117 -0.0061 0.0342  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2269 0.2879 0.3313 -0.0076 -0.0044 0.0353  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2298 0.2970 0.3614 -0.0045 0.0006  0.0393  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2287 0.2813 0.3222 -0.0040 0.0013  0.0263  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1490 0.1979 0.2001 -0.0150 -0.0023 0.0227  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1560 0.2040 0.1998 -0.0179 -0.0013 0.0220  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1568 0.2040 0.2046 -0.0150 0.0069  0.0188  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1678 0.2124 0.2179 -0.0112 0.0119  0.0151  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1675 0.2075 0.1918 -0.0190 -0.0024 0.0176  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1420 0.1905 0.1894 -0.0176 0.0088  0.0200  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1387 0.1847 0.1857 -0.0160 0.0176  0.0166  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1803 0.2168 0.2051 -0.0161 0.0181  0.0115  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.2055 0.2393 0.2201 -0.0187 0.0140  0.0123  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1525 0.2042 0.2099 -0.0191 0.0197  0.0207  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1587 0.2062 0.2124 -0.0182 0.0302  0.0167  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1558 0.2178 0.2385 -0.0190 0.0180  0.0270  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1790 0.2103 0.1977 -0.0135 0.0231  0.0066  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.2041 0.2268 0.2032 -0.0140 0.0223  0.0030  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.2174 0.2349 0.2108 -0.0123 0.0268  -0.0022 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2211 0.2407 0.2259 -0.0103 0.0309  -0.0038 103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2142 0.2241 0.1897 -0.0138 0.0262  -0.0046 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.2136 0.2170 0.1790 -0.0142 0.0294  -0.0098 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.2228 0.2252 0.1885 -0.0122 0.0235  -0.0117 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2245 0.2273 0.1881 -0.0117 0.0160  -0.0094 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2239 0.2193 0.1685 -0.0179 0.0294  -0.0104 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2448 0.2324 0.1757 -0.0202 0.0325  -0.0160 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2637 0.2487 0.1961 -0.0211 0.0436  -0.0209 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2621 0.2441 0.1797 -0.0218 0.0258  -0.0175 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.2709 0.2476 0.1878 -0.0240 0.0437  -0.0261 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2716 0.2467 0.1791 -0.0247 0.0322  -0.0237 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.2145 0.2147 0.1830 -0.0114 0.0280  -0.0163 105 SER   A N   
785  C CA  . SER   A 99  ? 0.2246 0.2229 0.1926 -0.0103 0.0231  -0.0187 105 SER   A CA  
786  C C   . SER   A 99  ? 0.2683 0.2601 0.2313 -0.0117 0.0300  -0.0254 105 SER   A C   
787  O O   . SER   A 99  ? 0.2988 0.2896 0.2667 -0.0119 0.0399  -0.0278 105 SER   A O   
788  C CB  . SER   A 99  ? 0.2494 0.2547 0.2346 -0.0069 0.0197  -0.0156 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.3041 0.3131 0.3049 -0.0052 0.0263  -0.0155 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.2529 0.2393 0.2049 -0.0136 0.0251  -0.0284 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.2729 0.2515 0.2170 -0.0162 0.0294  -0.0355 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.3057 0.2857 0.2574 -0.0144 0.0229  -0.0361 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.3017 0.2869 0.2590 -0.0123 0.0144  -0.0313 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.3091 0.2788 0.2273 -0.0225 0.0266  -0.0376 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.3063 0.2726 0.2145 -0.0254 0.0351  -0.0382 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.3241 0.2811 0.2047 -0.0326 0.0323  -0.0389 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.3654 0.3144 0.2306 -0.0376 0.0298  -0.0436 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.3347 0.2922 0.2086 -0.0339 0.0322  -0.0344 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.3481 0.3223 0.3001 -0.0156 0.0278  -0.0426 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.3701 0.3439 0.3257 -0.0153 0.0210  -0.0437 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.3734 0.3432 0.3095 -0.0203 0.0114  -0.0431 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.4346 0.3969 0.3502 -0.0260 0.0124  -0.0459 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.3784 0.3448 0.3360 -0.0168 0.0297  -0.0516 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.3842 0.3470 0.3401 -0.0175 0.0422  -0.0549 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.3547 0.3208 0.3011 -0.0183 0.0399  -0.0499 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.3014 0.2768 0.2458 -0.0181 0.0024  -0.0385 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2778 0.2533 0.2145 -0.0204 -0.0085 -0.0348 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.2476 0.2306 0.1942 -0.0162 -0.0116 -0.0276 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.2379 0.2234 0.1882 -0.0157 -0.0197 -0.0236 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.2302 0.2163 0.1811 -0.0136 -0.0051 -0.0260 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.1986 0.1904 0.1572 -0.0107 -0.0075 -0.0202 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1975 0.1948 0.1720 -0.0071 -0.0087 -0.0184 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1881 0.1885 0.1673 -0.0057 -0.0108 -0.0145 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.1996 0.1931 0.1572 -0.0103 -0.0014 -0.0186 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.2152 0.2033 0.1560 -0.0141 -0.0012 -0.0185 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.2256 0.2109 0.1582 -0.0162 -0.0084 -0.0163 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.2275 0.2142 0.1645 -0.0153 0.0064  -0.0201 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1905 0.1880 0.1726 -0.0062 -0.0067 -0.0213 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1745 0.1765 0.1704 -0.0036 -0.0075 -0.0191 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1844 0.1872 0.1825 -0.0035 -0.0135 -0.0169 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.2052 0.2053 0.1985 -0.0053 -0.0183 -0.0179 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1756 0.1765 0.1791 -0.0030 -0.0047 -0.0224 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.2178 0.2194 0.2283 -0.0015 0.0038  -0.0232 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1661 0.1723 0.1712 -0.0019 -0.0129 -0.0136 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1707 0.1772 0.1805 -0.0016 -0.0163 -0.0118 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.1807 0.1866 0.1866 -0.0017 -0.0167 -0.0090 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1865 0.1925 0.1987 -0.0010 -0.0170 -0.0074 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1688 0.1735 0.1654 -0.0027 -0.0158 -0.0086 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1678 0.1713 0.1611 -0.0030 -0.0157 -0.0059 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1610 0.1658 0.1585 -0.0030 -0.0119 -0.0050 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1653 0.1727 0.1640 -0.0034 -0.0095 -0.0053 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1623 0.1650 0.1624 -0.0029 -0.0115 -0.0037 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1500 0.1518 0.1512 -0.0043 -0.0073 -0.0038 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1638 0.1650 0.1573 -0.0068 -0.0055 -0.0029 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1671 0.1667 0.1565 -0.0069 -0.0064 -0.0018 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1785 0.1768 0.1874 -0.0034 -0.0056 -0.0037 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.1998 0.1999 0.2187 -0.0018 -0.0061 -0.0046 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2027 0.1970 0.2087 -0.0061 0.0002  -0.0047 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2140 0.2113 0.2453 -0.0004 -0.0037 -0.0043 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1511 0.1537 0.1427 -0.0093 -0.0033 -0.0028 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1451 0.1472 0.1304 -0.0131 -0.0022 -0.0017 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1697 0.1662 0.1523 -0.0161 0.0015  -0.0032 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1760 0.1717 0.1600 -0.0169 0.0033  -0.0042 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1386 0.1459 0.1242 -0.0151 -0.0035 0.0004  114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1607 0.1686 0.1408 -0.0203 -0.0039 0.0025  114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1753 0.1832 0.1536 -0.0204 -0.0038 0.0030  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1756 0.1899 0.1600 -0.0222 -0.0067 0.0063  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1632 0.1548 0.1417 -0.0181 0.0035  -0.0038 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1763 0.1604 0.1516 -0.0215 0.0088  -0.0065 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.1932 0.1746 0.1589 -0.0274 0.0095  -0.0066 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2116 0.1952 0.1764 -0.0273 0.0069  -0.0047 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2072 0.1861 0.1902 -0.0180 0.0115  -0.0074 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.2926 0.2737 0.2871 -0.0128 0.0100  -0.0067 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3085 0.2848 0.3128 -0.0099 0.0113  -0.0058 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.3468 0.3160 0.3546 -0.0117 0.0198  -0.0093 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.3353 0.3039 0.3536 -0.0100 0.0236  -0.0107 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.3048 0.2796 0.3329 -0.0059 0.0184  -0.0083 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.2852 0.2463 0.3041 -0.0127 0.0332  -0.0149 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.1909 0.1664 0.1488 -0.0331 0.0136  -0.0093 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2076 0.1778 0.1550 -0.0403 0.0149  -0.0105 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2322 0.1905 0.1786 -0.0416 0.0237  -0.0158 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2431 0.1994 0.1997 -0.0364 0.0276  -0.0171 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.1991 0.1710 0.1356 -0.0478 0.0121  -0.0093 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2352 0.1999 0.1639 -0.0518 0.0183  -0.0130 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.2520 0.2020 0.1877 -0.0490 0.0273  -0.0189 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.2769 0.2141 0.2125 -0.0507 0.0374  -0.0246 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.2918 0.2231 0.2253 -0.0524 0.0452  -0.0290 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.3189 0.2401 0.2579 -0.0517 0.0555  -0.0338 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.3069 0.2353 0.2285 -0.0600 0.0398  -0.0279 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.3766 0.3038 0.2792 -0.0705 0.0377  -0.0290 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.5168 0.4374 0.4052 -0.0807 0.0371  -0.0312 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.5597 0.4884 0.4454 -0.0839 0.0278  -0.0263 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.5081 0.4137 0.3883 -0.0864 0.0474  -0.0387 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.2774 0.2146 0.2047 -0.0544 0.0414  -0.0270 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.2729 0.2046 0.1965 -0.0569 0.0490  -0.0306 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.2616 0.1994 0.2032 -0.0479 0.0494  -0.0287 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.2745 0.2073 0.2174 -0.0489 0.0576  -0.0320 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.2808 0.2135 0.1853 -0.0662 0.0449  -0.0290 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.3159 0.2429 0.2021 -0.0765 0.0429  -0.0303 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.3380 0.2742 0.2203 -0.0793 0.0311  -0.0241 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.3685 0.2811 0.2397 -0.0855 0.0515  -0.0371 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.3712 0.2996 0.2377 -0.0894 0.0317  -0.0268 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.3852 0.2987 0.2432 -0.0938 0.0438  -0.0351 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2240 0.1722 0.1782 -0.0402 0.0410  -0.0237 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2118 0.1662 0.1820 -0.0327 0.0396  -0.0217 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.1946 0.1605 0.1673 -0.0291 0.0292  -0.0166 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2112 0.1812 0.1780 -0.0303 0.0232  -0.0140 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.1960 0.1666 0.1787 -0.0249 0.0281  -0.0154 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1774 0.1575 0.1636 -0.0213 0.0197  -0.0116 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1718 0.1548 0.1475 -0.0261 0.0166  -0.0094 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.1949 0.1746 0.1643 -0.0306 0.0203  -0.0102 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.1856 0.1688 0.1860 -0.0162 0.0195  -0.0113 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.1841 0.1753 0.1866 -0.0137 0.0122  -0.0085 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.1982 0.1801 0.2116 -0.0115 0.0199  -0.0115 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1723 0.1614 0.1469 -0.0254 0.0103  -0.0062 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1744 0.1680 0.1436 -0.0292 0.0059  -0.0024 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1755 0.1757 0.1546 -0.0247 0.0024  0.0001  121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1733 0.1755 0.1511 -0.0274 0.0006  0.0033  121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1940 0.1906 0.1596 -0.0312 0.0018  -0.0001 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2037 0.2069 0.1697 -0.0340 -0.0039 0.0054  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.1990 0.1884 0.1540 -0.0368 0.0049  -0.0026 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1573 0.1604 0.1451 -0.0188 0.0009  -0.0007 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1560 0.1638 0.1524 -0.0151 -0.0015 0.0004  122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1494 0.1584 0.1510 -0.0103 -0.0030 -0.0014 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1471 0.1533 0.1470 -0.0094 -0.0025 -0.0030 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1477 0.1599 0.1556 -0.0077 -0.0047 -0.0013 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1465 0.1586 0.1562 -0.0046 -0.0061 -0.0036 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1379 0.1526 0.1487 -0.0038 -0.0061 -0.0033 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1310 0.1486 0.1472 -0.0041 -0.0056 -0.0011 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1660 0.1772 0.1823 -0.0028 -0.0070 -0.0057 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1770 0.1898 0.1994 -0.0029 -0.0061 -0.0047 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1924 0.2010 0.2108 -0.0027 -0.0066 -0.0062 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.1925 0.2045 0.2224 -0.0012 -0.0074 -0.0072 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1339 0.1472 0.1404 -0.0030 -0.0063 -0.0053 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1388 0.1533 0.1466 -0.0024 -0.0040 -0.0062 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1343 0.1488 0.1499 -0.0010 -0.0031 -0.0079 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1420 0.1542 0.1577 -0.0006 -0.0050 -0.0102 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1465 0.1574 0.1452 -0.0029 -0.0038 -0.0088 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1546 0.1651 0.1540 -0.0027 0.0009  -0.0111 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1531 0.1636 0.1452 -0.0043 -0.0044 -0.0065 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1351 0.1524 0.1593 -0.0003 -0.0004 -0.0062 125 SER   A N   
922  C CA  . SER   A 119 ? 0.1424 0.1591 0.1763 0.0013  0.0013  -0.0074 125 SER   A CA  
923  C C   . SER   A 119 ? 0.1640 0.1804 0.2045 0.0025  0.0068  -0.0092 125 SER   A C   
924  O O   . SER   A 119 ? 0.1853 0.1982 0.2304 0.0034  0.0098  -0.0129 125 SER   A O   
925  C CB  . SER   A 119 ? 0.1424 0.1627 0.1846 0.0010  -0.0008 -0.0020 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1630 0.1828 0.2166 0.0026  0.0008  -0.0019 125 SER   A OG  
927  N N   . THR   A 120 ? 0.1689 0.1883 0.2108 0.0021  0.0090  -0.0067 126 THR   A N   
928  C CA  . THR   A 120 ? 0.1806 0.1996 0.2314 0.0034  0.0163  -0.0086 126 THR   A CA  
929  C C   . THR   A 120 ? 0.2012 0.2195 0.2431 0.0018  0.0195  -0.0100 126 THR   A C   
930  O O   . THR   A 120 ? 0.1815 0.2006 0.2126 0.0001  0.0153  -0.0083 126 THR   A O   
931  C CB  . THR   A 120 ? 0.1966 0.2219 0.2684 0.0051  0.0170  -0.0019 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.2138 0.2455 0.2871 0.0034  0.0136  0.0043  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.2041 0.2304 0.2842 0.0059  0.0130  0.0015  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.2265 0.2429 0.2737 0.0024  0.0279  -0.0130 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.2501 0.2662 0.2907 0.0007  0.0322  -0.0137 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.2683 0.2818 0.3179 0.0013  0.0437  -0.0174 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.2612 0.2744 0.3265 0.0037  0.0482  -0.0183 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.3117 0.3222 0.3508 -0.0010 0.0490  -0.0198 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.3250 0.3314 0.3688 -0.0015 0.0622  -0.0245 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.3198 0.3339 0.3786 -0.0010 0.0658  -0.0189 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.3235 0.3469 0.3944 0.0001  0.0579  -0.0111 128 GLY   A O   
942  N N   . ASN   A 123 ? 0.3225 0.3326 0.3811 -0.0024 0.0781  -0.0230 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.3183 0.3358 0.3949 -0.0021 0.0836  -0.0181 129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.2740 0.2981 0.3448 -0.0042 0.0743  -0.0113 129 ASN   A C   
945  O O   . ASN   A 123 ? 0.2668 0.3003 0.3582 -0.0036 0.0744  -0.0048 129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.3579 0.3844 0.4696 0.0024  0.0848  -0.0123 129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.4510 0.4710 0.5743 0.0050  0.0958  -0.0185 129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.4817 0.4917 0.5955 0.0031  0.1092  -0.0273 129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.4595 0.4845 0.6041 0.0088  0.0910  -0.0138 129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.2427 0.2622 0.2880 -0.0068 0.0667  -0.0125 130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.2237 0.2479 0.2639 -0.0089 0.0587  -0.0067 130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.2068 0.2384 0.2558 -0.0076 0.0466  -0.0006 130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2157 0.2518 0.2645 -0.0097 0.0405  0.0043  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1850 0.2167 0.2398 -0.0050 0.0436  -0.0013 131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1652 0.2021 0.2249 -0.0046 0.0330  0.0039  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1837 0.2142 0.2262 -0.0043 0.0278  0.0001  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.2090 0.2325 0.2426 -0.0036 0.0318  -0.0060 131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1606 0.2038 0.2450 -0.0019 0.0335  0.0080  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.1915 0.2436 0.2988 -0.0022 0.0362  0.0143  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2088 0.2655 0.3437 0.0013  0.0397  0.0177  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.1917 0.2509 0.2989 -0.0062 0.0255  0.0220  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1524 0.1854 0.1923 -0.0053 0.0191  0.0037  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1463 0.1746 0.1753 -0.0047 0.0146  0.0010  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1425 0.1754 0.1799 -0.0048 0.0085  0.0059  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1603 0.1980 0.2014 -0.0074 0.0049  0.0111  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1662 0.1895 0.1774 -0.0065 0.0118  -0.0008 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1905 0.2166 0.2003 -0.0092 0.0088  0.0034  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1809 0.2006 0.1858 -0.0056 0.0072  -0.0028 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1469 0.1778 0.1864 -0.0029 0.0076  0.0042  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1433 0.1774 0.1888 -0.0037 0.0025  0.0089  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1513 0.1810 0.1854 -0.0042 -0.0007 0.0065  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1525 0.1777 0.1817 -0.0025 0.0008  0.0015  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1418 0.1726 0.1726 -0.0072 -0.0049 0.0101  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1501 0.1767 0.1719 -0.0081 -0.0063 0.0080  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1486 0.1762 0.1746 -0.0095 -0.0084 0.0115  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1499 0.1811 0.1787 -0.0126 -0.0113 0.0173  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1408 0.1653 0.1518 -0.0117 -0.0074 0.0082  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1499 0.1735 0.1567 -0.0112 -0.0058 0.0063  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1537 0.1729 0.1548 -0.0092 -0.0047 0.0024  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1771 0.2044 0.1860 -0.0135 -0.0061 0.0094  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1594 0.1770 0.1553 -0.0094 -0.0035 0.0016  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1801 0.2061 0.1848 -0.0135 -0.0040 0.0080  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1658 0.1866 0.1631 -0.0115 -0.0026 0.0042  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1406 0.1650 0.1667 -0.0077 -0.0075 0.0086  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1386 0.1627 0.1666 -0.0095 -0.0086 0.0116  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1507 0.1715 0.1667 -0.0140 -0.0086 0.0117  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1570 0.1738 0.1677 -0.0133 -0.0063 0.0071  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1379 0.1594 0.1708 -0.0064 -0.0069 0.0079  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1622 0.1839 0.1740 -0.0191 -0.0111 0.0169  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1794 0.1963 0.1772 -0.0249 -0.0099 0.0162  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1784 0.1904 0.1737 -0.0254 -0.0060 0.0138  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1757 0.1891 0.1787 -0.0237 -0.0065 0.0160  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2249 0.2435 0.2166 -0.0320 -0.0147 0.0231  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2697 0.2817 0.2433 -0.0399 -0.0132 0.0217  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2488 0.2570 0.2164 -0.0400 -0.0098 0.0165  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3131 0.3226 0.2780 -0.0462 -0.0147 0.0255  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1675 0.1734 0.1541 -0.0274 -0.0012 0.0092  137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1770 0.1779 0.1622 -0.0287 0.0042  0.0069  137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.1878 0.1816 0.1567 -0.0369 0.0083  0.0062  137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2124 0.2008 0.1787 -0.0389 0.0147  0.0039  137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1900 0.1894 0.1845 -0.0231 0.0082  0.0016  137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1872 0.1922 0.1949 -0.0167 0.0042  0.0016  137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1960 0.1919 0.1866 -0.0231 0.0109  -0.0021 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.1976 0.1903 0.1549 -0.0423 0.0055  0.0077  138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.2057 0.1896 0.1445 -0.0513 0.0100  0.0055  138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.2500 0.2301 0.1770 -0.0589 0.0106  0.0090  138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2808 0.2512 0.1921 -0.0662 0.0177  0.0053  138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.1998 0.1837 0.1290 -0.0562 0.0056  0.0065  138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2243 0.2092 0.1616 -0.0502 0.0070  0.0024  138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2327 0.2186 0.1620 -0.0555 0.0021  0.0043  138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2347 0.2308 0.1725 -0.0541 -0.0068 0.0116  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2579 0.2582 0.1954 -0.0572 -0.0125 0.0151  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2446 0.2392 0.1706 -0.0630 -0.0110 0.0119  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2371 0.2471 0.1873 -0.0545 -0.0192 0.0216  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2351 0.2219 0.1696 -0.0575 0.0039  0.0162  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2540 0.2372 0.1772 -0.0651 0.0034  0.0211  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2584 0.2377 0.1864 -0.0626 0.0118  0.0180  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2781 0.2525 0.1946 -0.0696 0.0135  0.0213  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2582 0.2499 0.1895 -0.0650 -0.0075 0.0316  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.2872 0.2864 0.2423 -0.0543 -0.0088 0.0325  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2646 0.2662 0.2304 -0.0466 -0.0063 0.0266  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3180 0.3200 0.2803 -0.0540 -0.0124 0.0392  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2343 0.2156 0.1789 -0.0536 0.0164  0.0125  140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.2312 0.2102 0.1847 -0.0507 0.0236  0.0099  140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.2451 0.2143 0.1892 -0.0550 0.0354  0.0031  140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.2372 0.2055 0.1924 -0.0498 0.0412  -0.0029 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.2093 0.1953 0.1852 -0.0402 0.0216  0.0078  140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2256 0.2199 0.2112 -0.0360 0.0121  0.0131  140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2245 0.2234 0.2274 -0.0273 0.0109  0.0095  140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2454 0.2406 0.2317 -0.0388 0.0091  0.0202  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2668 0.2279 0.1895 -0.0655 0.0392  0.0043  141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.3023 0.2517 0.2128 -0.0712 0.0523  -0.0032 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.3077 0.2545 0.2333 -0.0668 0.0640  -0.0081 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.3099 0.2499 0.2380 -0.0666 0.0752  -0.0155 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.3231 0.2627 0.2037 -0.0852 0.0543  -0.0014 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.3419 0.2846 0.2078 -0.0913 0.0413  0.0051  141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.3767 0.3076 0.2099 -0.1069 0.0439  0.0060  141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.3445 0.2899 0.2149 -0.0874 0.0381  0.0013  141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.2963 0.2490 0.2353 -0.0629 0.0613  -0.0038 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.3002 0.2521 0.2564 -0.0589 0.0709  -0.0071 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.3011 0.2583 0.2818 -0.0490 0.0716  -0.0115 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.3113 0.2670 0.3078 -0.0463 0.0808  -0.0150 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.2960 0.2526 0.2600 -0.0579 0.0669  -0.0010 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2923 0.2594 0.2672 -0.0516 0.0527  0.0045  142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2951 0.2652 0.2600 -0.0545 0.0425  0.0115  142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2804 0.2558 0.2789 -0.0418 0.0480  0.0032  142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2923 0.2714 0.2743 -0.0465 0.0335  0.0139  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2860 0.2679 0.2865 -0.0392 0.0366  0.0085  142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2794 0.2571 0.2978 -0.0356 0.0520  -0.0015 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2843 0.2734 0.3032 -0.0313 0.0305  0.0080  142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2774 0.2630 0.3134 -0.0283 0.0440  -0.0010 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2772 0.2677 0.3116 -0.0265 0.0340  0.0031  142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.2824 0.2454 0.2671 -0.0439 0.0621  -0.0109 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.2926 0.2602 0.2984 -0.0355 0.0613  -0.0139 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.3446 0.3045 0.3548 -0.0362 0.0738  -0.0199 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.3324 0.2956 0.3649 -0.0298 0.0753  -0.0214 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2745 0.2478 0.2796 -0.0316 0.0504  -0.0122 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2514 0.2333 0.2610 -0.0281 0.0391  -0.0074 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2542 0.2400 0.2605 -0.0256 0.0310  -0.0065 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2378 0.2252 0.2691 -0.0218 0.0373  -0.0075 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.4109 0.3603 0.4004 -0.0444 0.0824  -0.0233 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.4815 0.4216 0.4756 -0.0454 0.0966  -0.0299 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.5553 0.4833 0.5329 -0.0549 0.1113  -0.0340 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.5807 0.4978 0.5537 -0.0585 0.1241  -0.0405 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.5256 0.4623 0.5138 -0.0453 0.0953  -0.0327 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.6027 0.5390 0.5659 -0.0513 0.0861  -0.0302 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.6236 0.5670 0.5909 -0.0467 0.0753  -0.0274 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.6340 0.5635 0.5741 -0.0609 0.0891  -0.0304 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.5884 0.5168 0.5557 -0.0596 0.1102  -0.0302 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.6335 0.5497 0.5813 -0.0701 0.1237  -0.0332 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.6495 0.5643 0.6205 -0.0665 0.1377  -0.0365 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.6582 0.5813 0.6454 -0.0620 0.1332  -0.0320 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.6836 0.6015 0.6121 -0.0766 0.1153  -0.0259 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.7813 0.6934 0.6769 -0.0869 0.1090  -0.0239 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.9078 0.8197 0.7845 -0.0950 0.1023  -0.0159 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.9573 0.8573 0.8121 -0.1059 0.1128  -0.0175 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.9332 0.8561 0.8169 -0.0907 0.0871  -0.0077 145 GLU   A OE2 
1078 N N   . SER   B 1   ? 0.3388 0.2984 0.2965 0.0064  -0.0465 0.0153  7   SER   C N   
1079 C CA  . SER   B 1   ? 0.3335 0.2994 0.3093 0.0055  -0.0496 0.0147  7   SER   C CA  
1080 C C   . SER   B 1   ? 0.3079 0.2818 0.2954 0.0041  -0.0470 0.0127  7   SER   C C   
1081 O O   . SER   B 1   ? 0.3211 0.2945 0.3027 0.0043  -0.0454 0.0113  7   SER   C O   
1082 C CB  . SER   B 1   ? 0.3724 0.3326 0.3499 0.0076  -0.0601 0.0139  7   SER   C CB  
1083 O OG  . SER   B 1   ? 0.4279 0.3845 0.4014 0.0090  -0.0657 0.0109  7   SER   C OG  
1084 N N   . GLY   B 2   ? 0.2665 0.2472 0.2699 0.0032  -0.0460 0.0130  8   GLY   C N   
1085 C CA  . GLY   B 2   ? 0.2532 0.2405 0.2675 0.0024  -0.0427 0.0122  8   GLY   C CA  
1086 C C   . GLY   B 2   ? 0.2312 0.2256 0.2564 0.0020  -0.0373 0.0134  8   GLY   C C   
1087 O O   . GLY   B 2   ? 0.2357 0.2308 0.2578 0.0020  -0.0344 0.0141  8   GLY   C O   
1088 N N   . ALA   B 3   ? 0.2169 0.2159 0.2545 0.0019  -0.0353 0.0137  9   ALA   C N   
1089 C CA  . ALA   B 3   ? 0.2215 0.2264 0.2681 0.0024  -0.0294 0.0149  9   ALA   C CA  
1090 C C   . ALA   B 3   ? 0.1941 0.2024 0.2449 0.0027  -0.0239 0.0159  9   ALA   C C   
1091 O O   . ALA   B 3   ? 0.2104 0.2171 0.2633 0.0020  -0.0258 0.0157  9   ALA   C O   
1092 C CB  . ALA   B 3   ? 0.2311 0.2370 0.2920 0.0027  -0.0323 0.0153  9   ALA   C CB  
1093 N N   . ILE   B 4   ? 0.1732 0.1858 0.2258 0.0041  -0.0173 0.0170  10  ILE   C N   
1094 C CA  . ILE   B 4   ? 0.1733 0.1883 0.2295 0.0053  -0.0111 0.0190  10  ILE   C CA  
1095 C C   . ILE   B 4   ? 0.1821 0.2000 0.2531 0.0061  -0.0074 0.0209  10  ILE   C C   
1096 O O   . ILE   B 4   ? 0.1862 0.2057 0.2597 0.0071  -0.0068 0.0202  10  ILE   C O   
1097 C CB  . ILE   B 4   ? 0.1794 0.1960 0.2239 0.0076  -0.0062 0.0186  10  ILE   C CB  
1098 C CG1 . ILE   B 4   ? 0.1865 0.2013 0.2193 0.0068  -0.0092 0.0164  10  ILE   C CG1 
1099 C CG2 . ILE   B 4   ? 0.1999 0.2173 0.2452 0.0098  0.0002  0.0214  10  ILE   C CG2 
1100 C CD1 . ILE   B 4   ? 0.1895 0.2064 0.2137 0.0091  -0.0063 0.0148  10  ILE   C CD1 
1101 N N   . TYR   B 5   ? 0.1969 0.2152 0.2797 0.0055  -0.0049 0.0233  11  TYR   C N   
1102 C CA  . TYR   B 5   ? 0.1927 0.2142 0.2926 0.0061  0.0000  0.0256  11  TYR   C CA  
1103 C C   . TYR   B 5   ? 0.2098 0.2321 0.3084 0.0083  0.0103  0.0295  11  TYR   C C   
1104 O O   . TYR   B 5   ? 0.2185 0.2387 0.3187 0.0075  0.0117  0.0316  11  TYR   C O   
1105 C CB  . TYR   B 5   ? 0.1918 0.2127 0.3103 0.0033  -0.0058 0.0253  11  TYR   C CB  
1106 C CG  . TYR   B 5   ? 0.1889 0.2079 0.3074 0.0023  -0.0165 0.0217  11  TYR   C CG  
1107 C CD1 . TYR   B 5   ? 0.1989 0.2201 0.3271 0.0030  -0.0182 0.0210  11  TYR   C CD1 
1108 C CD2 . TYR   B 5   ? 0.1981 0.2123 0.3046 0.0012  -0.0244 0.0192  11  TYR   C CD2 
1109 C CE1 . TYR   B 5   ? 0.2258 0.2439 0.3518 0.0027  -0.0282 0.0183  11  TYR   C CE1 
1110 C CE2 . TYR   B 5   ? 0.2196 0.2304 0.3224 0.0011  -0.0335 0.0166  11  TYR   C CE2 
1111 C CZ  . TYR   B 5   ? 0.2340 0.2465 0.3466 0.0018  -0.0358 0.0163  11  TYR   C CZ  
1112 O OH  . TYR   B 5   ? 0.2743 0.2821 0.3814 0.0023  -0.0451 0.0143  11  TYR   C OH  
1113 N N   . VAL   B 6   ? 0.2181 0.2423 0.3119 0.0117  0.0174  0.0304  12  VAL   C N   
1114 C CA  . VAL   B 6   ? 0.2319 0.2553 0.3200 0.0152  0.0276  0.0344  12  VAL   C CA  
1115 C C   . VAL   B 6   ? 0.2345 0.2606 0.3320 0.0178  0.0361  0.0364  12  VAL   C C   
1116 O O   . VAL   B 6   ? 0.2267 0.2546 0.3219 0.0195  0.0351  0.0334  12  VAL   C O   
1117 C CB  . VAL   B 6   ? 0.2581 0.2793 0.3229 0.0184  0.0274  0.0327  12  VAL   C CB  
1118 C CG1 . VAL   B 6   ? 0.2742 0.2968 0.3312 0.0193  0.0232  0.0280  12  VAL   C CG1 
1119 C CG2 . VAL   B 6   ? 0.2691 0.2882 0.3248 0.0233  0.0374  0.0368  12  VAL   C CG2 
1120 N N   . GLY   B 7   ? 0.2516 0.2780 0.3624 0.0181  0.0448  0.0415  13  GLY   C N   
1121 C CA  . GLY   B 7   ? 0.2540 0.2831 0.3756 0.0208  0.0547  0.0439  13  GLY   C CA  
1122 C C   . GLY   B 7   ? 0.2555 0.2891 0.3948 0.0186  0.0489  0.0403  13  GLY   C C   
1123 O O   . GLY   B 7   ? 0.2601 0.2945 0.4127 0.0143  0.0398  0.0386  13  GLY   C O   
1124 N N   . ASN   B 8   ? 0.2496 0.2851 0.3861 0.0220  0.0519  0.0382  14  ASN   C N   
1125 C CA  . ASN   B 8   ? 0.2460 0.2851 0.3984 0.0205  0.0455  0.0347  14  ASN   C CA  
1126 C C   . ASN   B 8   ? 0.2209 0.2582 0.3579 0.0203  0.0352  0.0295  14  ASN   C C   
1127 O O   . ASN   B 8   ? 0.2189 0.2578 0.3616 0.0213  0.0324  0.0266  14  ASN   C O   
1128 C CB  . ASN   B 8   ? 0.2849 0.3278 0.4508 0.0240  0.0557  0.0360  14  ASN   C CB  
1129 C CG  . ASN   B 8   ? 0.3801 0.4260 0.5706 0.0225  0.0641  0.0410  14  ASN   C CG  
1130 O OD1 . ASN   B 8   ? 0.4082 0.4562 0.6201 0.0180  0.0572  0.0407  14  ASN   C OD1 
1131 N ND2 . ASN   B 8   ? 0.3936 0.4391 0.5816 0.0266  0.0791  0.0456  14  ASN   C ND2 
1132 N N   . TYR   B 9   ? 0.2049 0.2386 0.3248 0.0188  0.0294  0.0284  15  TYR   C N   
1133 C CA  . TYR   B 9   ? 0.2034 0.2350 0.3097 0.0182  0.0208  0.0241  15  TYR   C CA  
1134 C C   . TYR   B 9   ? 0.1883 0.2175 0.2931 0.0139  0.0109  0.0232  15  TYR   C C   
1135 O O   . TYR   B 9   ? 0.1860 0.2142 0.2921 0.0121  0.0108  0.0252  15  TYR   C O   
1136 C CB  . TYR   B 9   ? 0.2113 0.2406 0.2957 0.0214  0.0239  0.0229  15  TYR   C CB  
1137 C CG  . TYR   B 9   ? 0.2223 0.2522 0.3019 0.0269  0.0328  0.0228  15  TYR   C CG  
1138 C CD1 . TYR   B 9   ? 0.2357 0.2672 0.3221 0.0287  0.0333  0.0202  15  TYR   C CD1 
1139 C CD2 . TYR   B 9   ? 0.2410 0.2690 0.3076 0.0309  0.0405  0.0250  15  TYR   C CD2 
1140 C CE1 . TYR   B 9   ? 0.2638 0.2952 0.3447 0.0344  0.0417  0.0195  15  TYR   C CE1 
1141 C CE2 . TYR   B 9   ? 0.2662 0.2934 0.3251 0.0370  0.0487  0.0247  15  TYR   C CE2 
1142 C CZ  . TYR   B 9   ? 0.2828 0.3118 0.3488 0.0387  0.0494  0.0216  15  TYR   C CZ  
1143 O OH  . TYR   B 9   ? 0.3172 0.3448 0.3744 0.0454  0.0577  0.0205  15  TYR   C OH  
1144 N N   . ARG   B 10  ? 0.1666 0.1940 0.2677 0.0127  0.0029  0.0202  16  ARG   C N   
1145 C CA  . ARG   B 10  ? 0.1636 0.1875 0.2584 0.0097  -0.0061 0.0190  16  ARG   C CA  
1146 C C   . ARG   B 10  ? 0.1724 0.1940 0.2502 0.0102  -0.0074 0.0167  16  ARG   C C   
1147 O O   . ARG   B 10  ? 0.1870 0.2087 0.2643 0.0116  -0.0074 0.0151  16  ARG   C O   
1148 C CB  . ARG   B 10  ? 0.1802 0.2029 0.2869 0.0083  -0.0142 0.0181  16  ARG   C CB  
1149 C CG  . ARG   B 10  ? 0.1980 0.2152 0.2942 0.0065  -0.0234 0.0167  16  ARG   C CG  
1150 C CD  . ARG   B 10  ? 0.2161 0.2312 0.3233 0.0063  -0.0321 0.0160  16  ARG   C CD  
1151 N NE  . ARG   B 10  ? 0.2314 0.2405 0.3268 0.0064  -0.0389 0.0152  16  ARG   C NE  
1152 C CZ  . ARG   B 10  ? 0.2816 0.2845 0.3663 0.0056  -0.0460 0.0148  16  ARG   C CZ  
1153 N NH1 . ARG   B 10  ? 0.2700 0.2720 0.3540 0.0046  -0.0481 0.0144  16  ARG   C NH1 
1154 N NH2 . ARG   B 10  ? 0.2800 0.2766 0.3534 0.0062  -0.0504 0.0151  16  ARG   C NH2 
1155 N N   . VAL   B 11  ? 0.1714 0.1913 0.2370 0.0092  -0.0082 0.0165  17  VAL   C N   
1156 C CA  . VAL   B 11  ? 0.1628 0.1812 0.2153 0.0093  -0.0092 0.0143  17  VAL   C CA  
1157 C C   . VAL   B 11  ? 0.1699 0.1842 0.2176 0.0065  -0.0157 0.0140  17  VAL   C C   
1158 O O   . VAL   B 11  ? 0.1841 0.1967 0.2301 0.0052  -0.0179 0.0148  17  VAL   C O   
1159 C CB  . VAL   B 11  ? 0.1792 0.1986 0.2218 0.0106  -0.0054 0.0141  17  VAL   C CB  
1160 C CG1 . VAL   B 11  ? 0.1828 0.2016 0.2159 0.0109  -0.0067 0.0110  17  VAL   C CG1 
1161 C CG2 . VAL   B 11  ? 0.1855 0.2072 0.2300 0.0140  0.0015  0.0155  17  VAL   C CG2 
1162 N N   . VAL   B 12  ? 0.1557 0.1674 0.2009 0.0061  -0.0184 0.0130  18  VAL   C N   
1163 C CA  . VAL   B 12  ? 0.1522 0.1586 0.1907 0.0041  -0.0234 0.0136  18  VAL   C CA  
1164 C C   . VAL   B 12  ? 0.1476 0.1523 0.1784 0.0035  -0.0220 0.0125  18  VAL   C C   
1165 O O   . VAL   B 12  ? 0.1565 0.1637 0.1894 0.0045  -0.0192 0.0108  18  VAL   C O   
1166 C CB  . VAL   B 12  ? 0.1960 0.1988 0.2408 0.0043  -0.0290 0.0145  18  VAL   C CB  
1167 C CG1 . VAL   B 12  ? 0.2306 0.2347 0.2852 0.0045  -0.0318 0.0150  18  VAL   C CG1 
1168 C CG2 . VAL   B 12  ? 0.1986 0.2026 0.2503 0.0057  -0.0279 0.0139  18  VAL   C CG2 
1169 N N   . ASN   B 13  ? 0.1472 0.1469 0.1697 0.0019  -0.0239 0.0136  19  ASN   C N   
1170 C CA  . ASN   B 13  ? 0.1518 0.1494 0.1703 0.0008  -0.0220 0.0133  19  ASN   C CA  
1171 C C   . ASN   B 13  ? 0.1635 0.1584 0.1877 0.0014  -0.0240 0.0138  19  ASN   C C   
1172 O O   . ASN   B 13  ? 0.1846 0.1754 0.2098 0.0020  -0.0283 0.0156  19  ASN   C O   
1173 C CB  . ASN   B 13  ? 0.1564 0.1477 0.1650 -0.0005 -0.0227 0.0154  19  ASN   C CB  
1174 C CG  . ASN   B 13  ? 0.1959 0.1893 0.1989 -0.0008 -0.0204 0.0146  19  ASN   C CG  
1175 O OD1 . ASN   B 13  ? 0.1848 0.1770 0.1848 -0.0002 -0.0229 0.0148  19  ASN   C OD1 
1176 N ND2 . ASN   B 13  ? 0.1776 0.1743 0.1808 -0.0016 -0.0163 0.0131  19  ASN   C ND2 
1177 N N   . ARG   B 14  ? 0.1494 0.1460 0.1776 0.0014  -0.0217 0.0117  20  ARG   C N   
1178 C CA  . ARG   B 14  ? 0.1560 0.1497 0.1902 0.0022  -0.0236 0.0118  20  ARG   C CA  
1179 C C   . ARG   B 14  ? 0.1736 0.1588 0.2032 0.0012  -0.0266 0.0156  20  ARG   C C   
1180 O O   . ARG   B 14  ? 0.1856 0.1673 0.2191 0.0025  -0.0304 0.0168  20  ARG   C O   
1181 C CB  . ARG   B 14  ? 0.1611 0.1567 0.1994 0.0024  -0.0212 0.0082  20  ARG   C CB  
1182 C CG  . ARG   B 14  ? 0.1766 0.1700 0.2225 0.0039  -0.0229 0.0071  20  ARG   C CG  
1183 C CD  . ARG   B 14  ? 0.1825 0.1763 0.2318 0.0037  -0.0215 0.0031  20  ARG   C CD  
1184 N NE  . ARG   B 14  ? 0.1914 0.1829 0.2480 0.0055  -0.0229 0.0006  20  ARG   C NE  
1185 C CZ  . ARG   B 14  ? 0.2219 0.2067 0.2821 0.0043  -0.0247 0.0027  20  ARG   C CZ  
1186 N NH1 . ARG   B 14  ? 0.2193 0.1983 0.2749 0.0016  -0.0250 0.0077  20  ARG   C NH1 
1187 N NH2 . ARG   B 14  ? 0.2203 0.2032 0.2879 0.0063  -0.0260 -0.0004 20  ARG   C NH2 
1188 N N   . HIS   B 15  ? 0.1768 0.1580 0.1976 -0.0007 -0.0247 0.0176  21  HIS   C N   
1189 C CA  . HIS   B 15  ? 0.1917 0.1631 0.2051 -0.0010 -0.0266 0.0220  21  HIS   C CA  
1190 C C   . HIS   B 15  ? 0.2144 0.1813 0.2213 0.0010  -0.0325 0.0241  21  HIS   C C   
1191 O O   . HIS   B 15  ? 0.2440 0.2018 0.2444 0.0021  -0.0359 0.0276  21  HIS   C O   
1192 C CB  . HIS   B 15  ? 0.1991 0.1669 0.2051 -0.0032 -0.0214 0.0241  21  HIS   C CB  
1193 C CG  . HIS   B 15  ? 0.2080 0.1771 0.2049 -0.0034 -0.0196 0.0242  21  HIS   C CG  
1194 N ND1 . HIS   B 15  ? 0.2121 0.1896 0.2128 -0.0041 -0.0167 0.0207  21  HIS   C ND1 
1195 C CD2 . HIS   B 15  ? 0.2263 0.1881 0.2095 -0.0025 -0.0202 0.0274  21  HIS   C CD2 
1196 C CE1 . HIS   B 15  ? 0.2288 0.2045 0.2197 -0.0039 -0.0156 0.0217  21  HIS   C CE1 
1197 N NE2 . HIS   B 15  ? 0.2473 0.2135 0.2270 -0.0029 -0.0174 0.0255  21  HIS   C NE2 
1198 N N   . LEU   B 16  ? 0.2101 0.1826 0.2195 0.0017  -0.0342 0.0220  22  LEU   C N   
1199 C CA  . LEU   B 16  ? 0.2106 0.1796 0.2169 0.0035  -0.0409 0.0228  22  LEU   C CA  
1200 C C   . LEU   B 16  ? 0.2221 0.1958 0.2432 0.0050  -0.0449 0.0210  22  LEU   C C   
1201 O O   . LEU   B 16  ? 0.2321 0.2047 0.2556 0.0063  -0.0510 0.0207  22  LEU   C O   
1202 C CB  . LEU   B 16  ? 0.2170 0.1879 0.2167 0.0030  -0.0401 0.0216  22  LEU   C CB  
1203 C CG  . LEU   B 16  ? 0.2402 0.2059 0.2251 0.0022  -0.0360 0.0233  22  LEU   C CG  
1204 C CD1 . LEU   B 16  ? 0.2540 0.2218 0.2336 0.0022  -0.0354 0.0215  22  LEU   C CD1 
1205 C CD2 . LEU   B 16  ? 0.2593 0.2129 0.2308 0.0039  -0.0391 0.0272  22  LEU   C CD2 
1206 N N   . ALA   B 17  ? 0.2048 0.1841 0.2368 0.0049  -0.0413 0.0194  23  ALA   C N   
1207 C CA  . ALA   B 17  ? 0.2108 0.1952 0.2577 0.0066  -0.0430 0.0178  23  ALA   C CA  
1208 C C   . ALA   B 17  ? 0.2143 0.1928 0.2649 0.0086  -0.0508 0.0193  23  ALA   C C   
1209 O O   . ALA   B 17  ? 0.2369 0.2076 0.2798 0.0089  -0.0531 0.0215  23  ALA   C O   
1210 C CB  . ALA   B 17  ? 0.2028 0.1919 0.2570 0.0071  -0.0377 0.0157  23  ALA   C CB  
1211 N N   . THR   B 18  ? 0.2143 0.1964 0.2772 0.0099  -0.0551 0.0182  24  THR   C N   
1212 C CA  . THR   B 18  ? 0.2197 0.1969 0.2886 0.0123  -0.0642 0.0188  24  THR   C CA  
1213 C C   . THR   B 18  ? 0.2245 0.2047 0.3086 0.0141  -0.0633 0.0179  24  THR   C C   
1214 O O   . THR   B 18  ? 0.2201 0.2067 0.3102 0.0137  -0.0555 0.0163  24  THR   C O   
1215 C CB  . THR   B 18  ? 0.2324 0.2125 0.3110 0.0127  -0.0699 0.0173  24  THR   C CB  
1216 O OG1 . THR   B 18  ? 0.2514 0.2419 0.3483 0.0123  -0.0639 0.0156  24  THR   C OG1 
1217 C CG2 . THR   B 18  ? 0.2395 0.2165 0.3043 0.0114  -0.0710 0.0173  24  THR   C CG2 
1218 N N   . HIS   B 19  ? 0.2341 0.2098 0.3252 0.0168  -0.0718 0.0184  25  HIS   C N   
1219 C CA  . HIS   B 19  ? 0.2349 0.2142 0.3429 0.0190  -0.0712 0.0171  25  HIS   C CA  
1220 C C   . HIS   B 19  ? 0.2216 0.2124 0.3479 0.0189  -0.0650 0.0144  25  HIS   C C   
1221 O O   . HIS   B 19  ? 0.2222 0.2178 0.3563 0.0199  -0.0581 0.0129  25  HIS   C O   
1222 C CB  . HIS   B 19  ? 0.2749 0.2483 0.3899 0.0223  -0.0828 0.0177  25  HIS   C CB  
1223 C CG  . HIS   B 19  ? 0.3839 0.3443 0.4804 0.0234  -0.0882 0.0211  25  HIS   C CG  
1224 N ND1 . HIS   B 19  ? 0.4315 0.3874 0.5211 0.0229  -0.0832 0.0229  25  HIS   C ND1 
1225 C CD2 . HIS   B 19  ? 0.4348 0.3852 0.5185 0.0253  -0.0980 0.0233  25  HIS   C CD2 
1226 C CE1 . HIS   B 19  ? 0.4564 0.3998 0.5301 0.0243  -0.0890 0.0268  25  HIS   C CE1 
1227 N NE2 . HIS   B 19  ? 0.4577 0.3970 0.5256 0.0261  -0.0979 0.0272  25  HIS   C NE2 
1228 N N   . ASN   B 20  ? 0.2049 0.1996 0.3373 0.0179  -0.0670 0.0140  26  ASN   C N   
1229 C CA  . ASN   B 20  ? 0.2029 0.2077 0.3534 0.0177  -0.0601 0.0125  26  ASN   C CA  
1230 C C   . ASN   B 20  ? 0.1942 0.2032 0.3361 0.0165  -0.0484 0.0125  26  ASN   C C   
1231 O O   . ASN   B 20  ? 0.1902 0.2056 0.3429 0.0179  -0.0404 0.0115  26  ASN   C O   
1232 C CB  . ASN   B 20  ? 0.2370 0.2440 0.3962 0.0165  -0.0649 0.0122  26  ASN   C CB  
1233 C CG  . ASN   B 20  ? 0.3061 0.3229 0.4874 0.0163  -0.0575 0.0116  26  ASN   C CG  
1234 O OD1 . ASN   B 20  ? 0.3187 0.3400 0.5202 0.0184  -0.0570 0.0106  26  ASN   C OD1 
1235 N ND2 . ASN   B 20  ? 0.3264 0.3465 0.5045 0.0141  -0.0507 0.0124  26  ASN   C ND2 
1236 N N   . ASP   B 21  ? 0.1960 0.2010 0.3180 0.0143  -0.0474 0.0134  27  ASP   C N   
1237 C CA  . ASP   B 21  ? 0.2005 0.2090 0.3140 0.0137  -0.0377 0.0128  27  ASP   C CA  
1238 C C   . ASP   B 21  ? 0.1918 0.2005 0.3058 0.0158  -0.0335 0.0111  27  ASP   C C   
1239 O O   . ASP   B 21  ? 0.1975 0.2112 0.3144 0.0175  -0.0257 0.0096  27  ASP   C O   
1240 C CB  . ASP   B 21  ? 0.2036 0.2077 0.2979 0.0114  -0.0381 0.0137  27  ASP   C CB  
1241 C CG  . ASP   B 21  ? 0.2162 0.2207 0.3079 0.0096  -0.0399 0.0145  27  ASP   C CG  
1242 O OD1 . ASP   B 21  ? 0.2117 0.2218 0.3147 0.0097  -0.0366 0.0144  27  ASP   C OD1 
1243 O OD2 . ASP   B 21  ? 0.2120 0.2106 0.2908 0.0084  -0.0445 0.0153  27  ASP   C OD2 
1244 N N   . TRP   B 22  ? 0.1958 0.1983 0.3072 0.0163  -0.0389 0.0113  28  TRP   C N   
1245 C CA  . TRP   B 22  ? 0.2047 0.2064 0.3176 0.0183  -0.0359 0.0092  28  TRP   C CA  
1246 C C   . TRP   B 22  ? 0.2065 0.2132 0.3374 0.0218  -0.0336 0.0073  28  TRP   C C   
1247 O O   . TRP   B 22  ? 0.2124 0.2212 0.3446 0.0242  -0.0276 0.0046  28  TRP   C O   
1248 C CB  . TRP   B 22  ? 0.2151 0.2077 0.3208 0.0177  -0.0419 0.0106  28  TRP   C CB  
1249 C CG  . TRP   B 22  ? 0.1946 0.1835 0.2845 0.0149  -0.0398 0.0112  28  TRP   C CG  
1250 C CD1 . TRP   B 22  ? 0.2125 0.1961 0.2904 0.0125  -0.0428 0.0143  28  TRP   C CD1 
1251 C CD2 . TRP   B 22  ? 0.1811 0.1706 0.2670 0.0146  -0.0348 0.0085  28  TRP   C CD2 
1252 N NE1 . TRP   B 22  ? 0.2210 0.2029 0.2894 0.0104  -0.0389 0.0139  28  TRP   C NE1 
1253 C CE2 . TRP   B 22  ? 0.2062 0.1917 0.2800 0.0115  -0.0347 0.0101  28  TRP   C CE2 
1254 C CE3 . TRP   B 22  ? 0.1896 0.1825 0.2810 0.0171  -0.0306 0.0042  28  TRP   C CE3 
1255 C CZ2 . TRP   B 22  ? 0.2047 0.1902 0.2747 0.0104  -0.0311 0.0076  28  TRP   C CZ2 
1256 C CZ3 . TRP   B 22  ? 0.1906 0.1827 0.2757 0.0165  -0.0280 0.0013  28  TRP   C CZ3 
1257 C CH2 . TRP   B 22  ? 0.1943 0.1832 0.2701 0.0129  -0.0285 0.0029  28  TRP   C CH2 
1258 N N   . ALA   B 23  ? 0.1951 0.2039 0.3403 0.0224  -0.0379 0.0084  29  ALA   C N   
1259 C CA  . ALA   B 23  ? 0.2060 0.2205 0.3716 0.0257  -0.0350 0.0068  29  ALA   C CA  
1260 C C   . ALA   B 23  ? 0.2126 0.2352 0.3835 0.0265  -0.0240 0.0063  29  ALA   C C   
1261 O O   . ALA   B 23  ? 0.2201 0.2476 0.4052 0.0297  -0.0180 0.0049  29  ALA   C O   
1262 C CB  . ALA   B 23  ? 0.2044 0.2191 0.3862 0.0260  -0.0438 0.0078  29  ALA   C CB  
1263 N N   . ASN   B 24  ? 0.1990 0.2226 0.3595 0.0239  -0.0211 0.0079  30  ASN   C N   
1264 C CA  . ASN   B 24  ? 0.1876 0.2171 0.3499 0.0247  -0.0105 0.0085  30  ASN   C CA  
1265 C C   . ASN   B 24  ? 0.1940 0.2216 0.3349 0.0247  -0.0059 0.0077  30  ASN   C C   
1266 O O   . ASN   B 24  ? 0.1908 0.2203 0.3257 0.0240  -0.0008 0.0093  30  ASN   C O   
1267 C CB  . ASN   B 24  ? 0.1833 0.2158 0.3557 0.0221  -0.0119 0.0111  30  ASN   C CB  
1268 C CG  . ASN   B 24  ? 0.2359 0.2716 0.4333 0.0228  -0.0164 0.0110  30  ASN   C CG  
1269 O OD1 . ASN   B 24  ? 0.2193 0.2607 0.4340 0.0252  -0.0089 0.0108  30  ASN   C OD1 
1270 N ND2 . ASN   B 24  ? 0.2417 0.2733 0.4411 0.0211  -0.0287 0.0109  30  ASN   C ND2 
1271 N N   . LEU   B 25  ? 0.2022 0.2254 0.3327 0.0256  -0.0080 0.0051  31  LEU   C N   
1272 C CA  . LEU   B 25  ? 0.2005 0.2217 0.3130 0.0255  -0.0057 0.0034  31  LEU   C CA  
1273 C C   . LEU   B 25  ? 0.2039 0.2283 0.3112 0.0294  0.0039  0.0020  31  LEU   C C   
1274 O O   . LEU   B 25  ? 0.2207 0.2470 0.3348 0.0335  0.0093  0.0002  31  LEU   C O   
1275 C CB  . LEU   B 25  ? 0.2099 0.2258 0.3175 0.0258  -0.0102 0.0005  31  LEU   C CB  
1276 C CG  . LEU   B 25  ? 0.2252 0.2388 0.3178 0.0256  -0.0093 -0.0023 31  LEU   C CG  
1277 C CD1 . LEU   B 25  ? 0.2258 0.2384 0.3086 0.0214  -0.0119 0.0002  31  LEU   C CD1 
1278 C CD2 . LEU   B 25  ? 0.2237 0.2321 0.3164 0.0259  -0.0133 -0.0053 31  LEU   C CD2 
1279 N N   . VAL   B 26  ? 0.1841 0.2085 0.2780 0.0286  0.0062  0.0027  32  VAL   C N   
1280 C CA  . VAL   B 26  ? 0.1968 0.2224 0.2807 0.0330  0.0143  0.0015  32  VAL   C CA  
1281 C C   . VAL   B 26  ? 0.2099 0.2320 0.2783 0.0341  0.0111  -0.0031 32  VAL   C C   
1282 O O   . VAL   B 26  ? 0.2330 0.2538 0.2950 0.0390  0.0142  -0.0072 32  VAL   C O   
1283 C CB  . VAL   B 26  ? 0.2200 0.2476 0.3010 0.0320  0.0188  0.0058  32  VAL   C CB  
1284 C CG1 . VAL   B 26  ? 0.2355 0.2623 0.3010 0.0370  0.0259  0.0049  32  VAL   C CG1 
1285 C CG2 . VAL   B 26  ? 0.2251 0.2566 0.3246 0.0312  0.0228  0.0098  32  VAL   C CG2 
1286 N N   . TRP   B 27  ? 0.1958 0.2161 0.2592 0.0298  0.0048  -0.0027 33  TRP   C N   
1287 C CA  . TRP   B 27  ? 0.1876 0.2054 0.2400 0.0299  0.0015  -0.0068 33  TRP   C CA  
1288 C C   . TRP   B 27  ? 0.1842 0.2000 0.2373 0.0243  -0.0049 -0.0054 33  TRP   C C   
1289 O O   . TRP   B 27  ? 0.1953 0.2117 0.2507 0.0211  -0.0059 -0.0012 33  TRP   C O   
1290 C CB  . TRP   B 27  ? 0.1977 0.2166 0.2371 0.0328  0.0052  -0.0073 33  TRP   C CB  
1291 C CG  . TRP   B 27  ? 0.2155 0.2328 0.2453 0.0327  0.0007  -0.0115 33  TRP   C CG  
1292 C CD1 . TRP   B 27  ? 0.2438 0.2589 0.2680 0.0363  -0.0014 -0.0177 33  TRP   C CD1 
1293 C CD2 . TRP   B 27  ? 0.2131 0.2308 0.2393 0.0289  -0.0025 -0.0101 33  TRP   C CD2 
1294 N NE1 . TRP   B 27  ? 0.2566 0.2715 0.2761 0.0346  -0.0062 -0.0204 33  TRP   C NE1 
1295 C CE2 . TRP   B 27  ? 0.2357 0.2524 0.2563 0.0301  -0.0064 -0.0155 33  TRP   C CE2 
1296 C CE3 . TRP   B 27  ? 0.2133 0.2322 0.2416 0.0247  -0.0028 -0.0052 33  TRP   C CE3 
1297 C CZ2 . TRP   B 27  ? 0.2269 0.2444 0.2446 0.0275  -0.0095 -0.0158 33  TRP   C CZ2 
1298 C CZ3 . TRP   B 27  ? 0.2177 0.2369 0.2409 0.0225  -0.0055 -0.0056 33  TRP   C CZ3 
1299 C CH2 . TRP   B 27  ? 0.2146 0.2334 0.2338 0.0236  -0.0086 -0.0107 33  TRP   C CH2 
1300 N N   . GLU   B 28  ? 0.1718 0.1846 0.2230 0.0234  -0.0088 -0.0089 34  GLU   C N   
1301 C CA  . GLU   B 28  ? 0.1829 0.1933 0.2335 0.0184  -0.0129 -0.0071 34  GLU   C CA  
1302 C C   . GLU   B 28  ? 0.1835 0.1928 0.2308 0.0183  -0.0149 -0.0119 34  GLU   C C   
1303 O O   . GLU   B 28  ? 0.1899 0.1984 0.2373 0.0217  -0.0152 -0.0170 34  GLU   C O   
1304 C CB  . GLU   B 28  ? 0.1956 0.2020 0.2537 0.0157  -0.0163 -0.0042 34  GLU   C CB  
1305 C CG  . GLU   B 28  ? 0.2023 0.2059 0.2674 0.0179  -0.0175 -0.0071 34  GLU   C CG  
1306 C CD  . GLU   B 28  ? 0.2318 0.2316 0.2971 0.0170  -0.0198 -0.0109 34  GLU   C CD  
1307 O OE1 . GLU   B 28  ? 0.2709 0.2694 0.3400 0.0201  -0.0201 -0.0154 34  GLU   C OE1 
1308 O OE2 . GLU   B 28  ? 0.2101 0.2079 0.2729 0.0132  -0.0213 -0.0094 34  GLU   C OE2 
1309 N N   . ASP   B 29  ? 0.1716 0.1806 0.2166 0.0146  -0.0164 -0.0107 35  ASP   C N   
1310 C CA  . ASP   B 29  ? 0.1670 0.1755 0.2123 0.0139  -0.0186 -0.0152 35  ASP   C CA  
1311 C C   . ASP   B 29  ? 0.1726 0.1788 0.2209 0.0086  -0.0193 -0.0119 35  ASP   C C   
1312 O O   . ASP   B 29  ? 0.1806 0.1884 0.2246 0.0067  -0.0181 -0.0089 35  ASP   C O   
1313 C CB  . ASP   B 29  ? 0.1816 0.1941 0.2195 0.0170  -0.0181 -0.0185 35  ASP   C CB  
1314 C CG  . ASP   B 29  ? 0.2517 0.2644 0.2917 0.0173  -0.0216 -0.0246 35  ASP   C CG  
1315 O OD1 . ASP   B 29  ? 0.2791 0.2900 0.3273 0.0132  -0.0232 -0.0247 35  ASP   C OD1 
1316 O OD2 . ASP   B 29  ? 0.2573 0.2718 0.2909 0.0218  -0.0229 -0.0291 35  ASP   C OD2 
1317 N N   . SER   B 30  ? 0.1665 0.1680 0.2219 0.0065  -0.0208 -0.0122 36  SER   C N   
1318 C CA  A SER   B 30  ? 0.1750 0.1728 0.2326 0.0019  -0.0201 -0.0083 36  SER   C CA  
1319 C CA  B SER   B 30  ? 0.1765 0.1743 0.2340 0.0018  -0.0201 -0.0082 36  SER   C CA  
1320 C C   . SER   B 30  ? 0.1884 0.1897 0.2469 0.0000  -0.0191 -0.0103 36  SER   C C   
1321 O O   . SER   B 30  ? 0.1898 0.1901 0.2458 -0.0029 -0.0167 -0.0061 36  SER   C O   
1322 C CB  A SER   B 30  ? 0.2034 0.1950 0.2694 0.0005  -0.0214 -0.0085 36  SER   C CB  
1323 C CB  B SER   B 30  ? 0.2098 0.2014 0.2757 0.0002  -0.0213 -0.0082 36  SER   C CB  
1324 O OG  A SER   B 30  ? 0.2323 0.2192 0.2999 -0.0037 -0.0194 -0.0039 36  SER   C OG  
1325 O OG  B SER   B 30  ? 0.2443 0.2319 0.3108 0.0018  -0.0226 -0.0060 36  SER   C OG  
1326 N N   . SER   B 31  ? 0.1773 0.1822 0.2390 0.0023  -0.0212 -0.0170 37  SER   C N   
1327 C CA  . SER   B 31  ? 0.1882 0.1970 0.2533 0.0009  -0.0214 -0.0197 37  SER   C CA  
1328 C C   . SER   B 31  ? 0.1888 0.2017 0.2451 0.0016  -0.0195 -0.0172 37  SER   C C   
1329 O O   . SER   B 31  ? 0.2109 0.2263 0.2703 -0.0003 -0.0185 -0.0177 37  SER   C O   
1330 C CB  . SER   B 31  ? 0.2438 0.2549 0.3140 0.0040  -0.0259 -0.0283 37  SER   C CB  
1331 O OG  . SER   B 31  ? 0.2938 0.3081 0.3536 0.0095  -0.0274 -0.0312 37  SER   C OG  
1332 N N   . ARG   B 32  ? 0.1551 0.1683 0.2020 0.0041  -0.0186 -0.0146 38  ARG   C N   
1333 C CA  . ARG   B 32  ? 0.1520 0.1683 0.1913 0.0048  -0.0170 -0.0120 38  ARG   C CA  
1334 C C   . ARG   B 32  ? 0.1505 0.1636 0.1859 0.0021  -0.0148 -0.0056 38  ARG   C C   
1335 O O   . ARG   B 32  ? 0.1627 0.1773 0.1925 0.0022  -0.0136 -0.0035 38  ARG   C O   
1336 C CB  . ARG   B 32  ? 0.1646 0.1831 0.1968 0.0097  -0.0172 -0.0135 38  ARG   C CB  
1337 C CG  . ARG   B 32  ? 0.1683 0.1888 0.2000 0.0137  -0.0201 -0.0201 38  ARG   C CG  
1338 C CD  . ARG   B 32  ? 0.1755 0.1968 0.1974 0.0194  -0.0191 -0.0207 38  ARG   C CD  
1339 N NE  . ARG   B 32  ? 0.1624 0.1854 0.1779 0.0199  -0.0169 -0.0169 38  ARG   C NE  
1340 C CZ  . ARG   B 32  ? 0.1765 0.2000 0.1827 0.0249  -0.0162 -0.0175 38  ARG   C CZ  
1341 N NH1 . ARG   B 32  ? 0.2079 0.2302 0.2083 0.0304  -0.0175 -0.0220 38  ARG   C NH1 
1342 N NH2 . ARG   B 32  ? 0.1879 0.2123 0.1896 0.0249  -0.0142 -0.0137 38  ARG   C NH2 
1343 N N   . ASP   B 33  ? 0.1619 0.1701 0.1995 0.0004  -0.0150 -0.0028 39  ASP   C N   
1344 C CA  . ASP   B 33  ? 0.1547 0.1589 0.1872 -0.0008 -0.0147 0.0026  39  ASP   C CA  
1345 C C   . ASP   B 33  ? 0.1383 0.1447 0.1676 0.0016  -0.0154 0.0035  39  ASP   C C   
1346 O O   . ASP   B 33  ? 0.1626 0.1676 0.1875 0.0009  -0.0158 0.0066  39  ASP   C O   
1347 C CB  . ASP   B 33  ? 0.1614 0.1634 0.1890 -0.0034 -0.0125 0.0056  39  ASP   C CB  
1348 C CG  . ASP   B 33  ? 0.1790 0.1752 0.1992 -0.0039 -0.0134 0.0105  39  ASP   C CG  
1349 O OD1 . ASP   B 33  ? 0.1927 0.1840 0.2138 -0.0036 -0.0156 0.0126  39  ASP   C OD1 
1350 O OD2 . ASP   B 33  ? 0.1820 0.1778 0.1951 -0.0040 -0.0125 0.0119  39  ASP   C OD2 
1351 N N   . LEU   B 34  ? 0.1454 0.1548 0.1775 0.0046  -0.0155 0.0008  40  LEU   C N   
1352 C CA  . LEU   B 34  ? 0.1417 0.1531 0.1731 0.0068  -0.0147 0.0023  40  LEU   C CA  
1353 C C   . LEU   B 34  ? 0.1596 0.1700 0.1972 0.0085  -0.0152 0.0025  40  LEU   C C   
1354 O O   . LEU   B 34  ? 0.1691 0.1789 0.2098 0.0099  -0.0154 -0.0004 40  LEU   C O   
1355 C CB  . LEU   B 34  ? 0.1419 0.1576 0.1697 0.0099  -0.0124 0.0001  40  LEU   C CB  
1356 C CG  . LEU   B 34  ? 0.1554 0.1729 0.1780 0.0092  -0.0120 0.0001  40  LEU   C CG  
1357 C CD1 . LEU   B 34  ? 0.1602 0.1805 0.1782 0.0134  -0.0102 -0.0018 40  LEU   C CD1 
1358 C CD2 . LEU   B 34  ? 0.1640 0.1802 0.1852 0.0073  -0.0119 0.0041  40  LEU   C CD2 
1359 N N   . LEU   B 35  ? 0.1462 0.1570 0.1869 0.0088  -0.0153 0.0053  41  LEU   C N   
1360 C CA  . LEU   B 35  ? 0.1512 0.1626 0.2002 0.0109  -0.0150 0.0054  41  LEU   C CA  
1361 C C   . LEU   B 35  ? 0.1455 0.1605 0.1984 0.0122  -0.0122 0.0073  41  LEU   C C   
1362 O O   . LEU   B 35  ? 0.1677 0.1825 0.2189 0.0103  -0.0133 0.0095  41  LEU   C O   
1363 C CB  . LEU   B 35  ? 0.1558 0.1626 0.2096 0.0094  -0.0197 0.0073  41  LEU   C CB  
1364 C CG  . LEU   B 35  ? 0.1564 0.1639 0.2214 0.0118  -0.0201 0.0071  41  LEU   C CG  
1365 C CD1 . LEU   B 35  ? 0.1692 0.1709 0.2369 0.0114  -0.0247 0.0075  41  LEU   C CD1 
1366 C CD2 . LEU   B 35  ? 0.1759 0.1856 0.2489 0.0118  -0.0213 0.0096  41  LEU   C CD2 
1367 N N   . VAL   B 36  ? 0.1416 0.1594 0.1993 0.0155  -0.0078 0.0064  42  VAL   C N   
1368 C CA  . VAL   B 36  ? 0.1609 0.1819 0.2248 0.0168  -0.0034 0.0089  42  VAL   C CA  
1369 C C   . VAL   B 36  ? 0.1680 0.1903 0.2463 0.0181  -0.0029 0.0093  42  VAL   C C   
1370 O O   . VAL   B 36  ? 0.1614 0.1835 0.2414 0.0207  -0.0016 0.0068  42  VAL   C O   
1371 C CB  . VAL   B 36  ? 0.1776 0.2005 0.2336 0.0206  0.0034  0.0082  42  VAL   C CB  
1372 C CG1 . VAL   B 36  ? 0.1973 0.2228 0.2607 0.0220  0.0098  0.0118  42  VAL   C CG1 
1373 C CG2 . VAL   B 36  ? 0.1774 0.1993 0.2208 0.0197  0.0019  0.0073  42  VAL   C CG2 
1374 N N   . SER   B 37  ? 0.1634 0.1869 0.2531 0.0165  -0.0044 0.0120  43  SER   C N   
1375 C CA  . SER   B 37  ? 0.1752 0.2010 0.2821 0.0177  -0.0041 0.0124  43  SER   C CA  
1376 C C   . SER   B 37  ? 0.1876 0.2179 0.3063 0.0186  0.0031  0.0150  43  SER   C C   
1377 O O   . SER   B 37  ? 0.1827 0.2133 0.2961 0.0176  0.0059  0.0170  43  SER   C O   
1378 C CB  . SER   B 37  ? 0.1904 0.2132 0.3038 0.0153  -0.0139 0.0127  43  SER   C CB  
1379 O OG  . SER   B 37  ? 0.2155 0.2372 0.3285 0.0125  -0.0180 0.0143  43  SER   C OG  
1380 N N   . SER   B 38  ? 0.1918 0.2256 0.3273 0.0207  0.0067  0.0151  44  SER   C N   
1381 C CA  . SER   B 38  ? 0.2152 0.2533 0.3649 0.0214  0.0149  0.0181  44  SER   C CA  
1382 C C   . SER   B 38  ? 0.2356 0.2751 0.4043 0.0178  0.0083  0.0195  44  SER   C C   
1383 O O   . SER   B 38  ? 0.2319 0.2697 0.4062 0.0165  -0.0019 0.0176  44  SER   C O   
1384 C CB  . SER   B 38  ? 0.2377 0.2792 0.3973 0.0257  0.0237  0.0177  44  SER   C CB  
1385 O OG  . SER   B 38  ? 0.2726 0.3147 0.4449 0.0259  0.0171  0.0152  44  SER   C OG  
1386 N N   . THR   B 39  ? 0.2485 0.2902 0.4261 0.0166  0.0137  0.0226  45  THR   C N   
1387 C CA  . THR   B 39  ? 0.2766 0.3196 0.4743 0.0133  0.0076  0.0233  45  THR   C CA  
1388 C C   . THR   B 39  ? 0.3122 0.3610 0.5354 0.0140  0.0175  0.0261  45  THR   C C   
1389 O O   . THR   B 39  ? 0.3178 0.3682 0.5376 0.0170  0.0305  0.0287  45  THR   C O   
1390 C CB  . THR   B 39  ? 0.3001 0.3396 0.4873 0.0104  0.0047  0.0245  45  THR   C CB  
1391 O OG1 . THR   B 39  ? 0.3251 0.3656 0.5085 0.0115  0.0168  0.0282  45  THR   C OG1 
1392 C CG2 . THR   B 39  ? 0.3126 0.3468 0.4748 0.0097  -0.0026 0.0223  45  THR   C CG2 
1393 N N   . THR   B 40  ? 0.3346 0.3860 0.5832 0.0116  0.0114  0.0256  46  THR   C N   
1394 C CA  . THR   B 40  ? 0.3572 0.4144 0.6348 0.0114  0.0206  0.0284  46  THR   C CA  
1395 C C   . THR   B 40  ? 0.3724 0.4284 0.6535 0.0086  0.0251  0.0321  46  THR   C C   
1396 O O   . THR   B 40  ? 0.3868 0.4458 0.6813 0.0091  0.0386  0.0366  46  THR   C O   
1397 C CB  . THR   B 40  ? 0.3819 0.4430 0.6888 0.0104  0.0109  0.0254  46  THR   C CB  
1398 O OG1 . THR   B 40  ? 0.4185 0.4750 0.7214 0.0077  -0.0054 0.0222  46  THR   C OG1 
1399 C CG2 . THR   B 40  ? 0.3906 0.4535 0.6989 0.0140  0.0096  0.0228  46  THR   C CG2 
1400 N N   . ALA   B 41  ? 0.3670 0.4181 0.6359 0.0057  0.0146  0.0305  47  ALA   C N   
1401 C CA  . ALA   B 41  ? 0.3664 0.4152 0.6375 0.0030  0.0172  0.0333  47  ALA   C CA  
1402 C C   . ALA   B 41  ? 0.3733 0.4180 0.6155 0.0048  0.0255  0.0363  47  ALA   C C   
1403 O O   . ALA   B 41  ? 0.3805 0.4229 0.5982 0.0069  0.0234  0.0344  47  ALA   C O   
1404 C CB  . ALA   B 41  ? 0.3688 0.4137 0.6414 -0.0001 0.0012  0.0291  47  ALA   C CB  
1405 N N   . GLN   B 42  ? 0.3639 0.4073 0.6101 0.0039  0.0341  0.0410  48  GLN   C N   
1406 C CA  . GLN   B 42  ? 0.3716 0.4106 0.5923 0.0060  0.0418  0.0444  48  GLN   C CA  
1407 C C   . GLN   B 42  ? 0.3613 0.3952 0.5639 0.0041  0.0309  0.0415  48  GLN   C C   
1408 O O   . GLN   B 42  ? 0.3692 0.4015 0.5837 0.0006  0.0234  0.0401  48  GLN   C O   
1409 C CB  . GLN   B 42  ? 0.4005 0.4390 0.6337 0.0061  0.0555  0.0513  48  GLN   C CB  
1410 C CG  . GLN   B 42  ? 0.4820 0.5149 0.6894 0.0090  0.0631  0.0555  48  GLN   C CG  
1411 C CD  . GLN   B 42  ? 0.5828 0.6153 0.7698 0.0149  0.0734  0.0572  48  GLN   C CD  
1412 O OE1 . GLN   B 42  ? 0.6022 0.6387 0.7959 0.0171  0.0776  0.0562  48  GLN   C OE1 
1413 N NE2 . GLN   B 42  ? 0.6201 0.6472 0.7814 0.0183  0.0773  0.0595  48  GLN   C NE2 
1414 N N   . GLY   B 43  ? 0.3361 0.3674 0.5110 0.0066  0.0304  0.0402  49  GLY   C N   
1415 C CA  . GLY   B 43  ? 0.3208 0.3478 0.4774 0.0054  0.0221  0.0377  49  GLY   C CA  
1416 C C   . GLY   B 43  ? 0.3017 0.3252 0.4496 0.0063  0.0290  0.0418  49  GLY   C C   
1417 O O   . GLY   B 43  ? 0.3109 0.3342 0.4544 0.0096  0.0405  0.0463  49  GLY   C O   
1418 N N   . CYS   B 44  ? 0.2801 0.2999 0.4242 0.0041  0.0222  0.0404  50  CYS   C N   
1419 C CA  . CYS   B 44  ? 0.2755 0.2913 0.4134 0.0049  0.0277  0.0444  50  CYS   C CA  
1420 C C   . CYS   B 44  ? 0.2690 0.2816 0.3829 0.0064  0.0236  0.0421  50  CYS   C C   
1421 O O   . CYS   B 44  ? 0.2794 0.2880 0.3891 0.0069  0.0259  0.0447  50  CYS   C O   
1422 C CB  . CYS   B 44  ? 0.2988 0.3127 0.4585 0.0012  0.0257  0.0456  50  CYS   C CB  
1423 S SG  . CYS   B 44  ? 0.3564 0.3743 0.5486 -0.0003 0.0341  0.0498  50  CYS   C SG  
1424 N N   . ASP   B 45  ? 0.2377 0.2517 0.3371 0.0073  0.0181  0.0377  51  ASP   C N   
1425 C CA  . ASP   B 45  ? 0.2372 0.2489 0.3163 0.0088  0.0151  0.0356  51  ASP   C CA  
1426 C C   . ASP   B 45  ? 0.2513 0.2623 0.3169 0.0135  0.0233  0.0388  51  ASP   C C   
1427 O O   . ASP   B 45  ? 0.2647 0.2774 0.3303 0.0160  0.0299  0.0407  51  ASP   C O   
1428 C CB  . ASP   B 45  ? 0.2505 0.2637 0.3200 0.0082  0.0077  0.0304  51  ASP   C CB  
1429 C CG  . ASP   B 45  ? 0.3020 0.3141 0.3788 0.0048  -0.0013 0.0270  51  ASP   C CG  
1430 O OD1 . ASP   B 45  ? 0.3089 0.3184 0.3948 0.0029  -0.0039 0.0273  51  ASP   C OD1 
1431 O OD2 . ASP   B 45  ? 0.2907 0.3035 0.3639 0.0042  -0.0061 0.0242  51  ASP   C OD2 
1432 N N   . THR   B 46  ? 0.2408 0.2486 0.2947 0.0151  0.0229  0.0393  52  THR   C N   
1433 C CA  . THR   B 46  ? 0.2617 0.2677 0.3000 0.0204  0.0286  0.0416  52  THR   C CA  
1434 C C   . THR   B 46  ? 0.2292 0.2372 0.2527 0.0219  0.0226  0.0361  52  THR   C C   
1435 O O   . THR   B 46  ? 0.2353 0.2435 0.2578 0.0195  0.0160  0.0326  52  THR   C O   
1436 C CB  . THR   B 46  ? 0.3136 0.3144 0.3484 0.0218  0.0308  0.0455  52  THR   C CB  
1437 O OG1 . THR   B 46  ? 0.3504 0.3488 0.3997 0.0207  0.0380  0.0515  52  THR   C OG1 
1438 C CG2 . THR   B 46  ? 0.3290 0.3270 0.3441 0.0280  0.0336  0.0467  52  THR   C CG2 
1439 N N   . ILE   B 47  ? 0.2209 0.2299 0.2338 0.0259  0.0250  0.0350  53  ILE   C N   
1440 C CA  . ILE   B 47  ? 0.2104 0.2212 0.2121 0.0274  0.0194  0.0296  53  ILE   C CA  
1441 C C   . ILE   B 47  ? 0.2109 0.2188 0.1989 0.0320  0.0191  0.0299  53  ILE   C C   
1442 O O   . ILE   B 47  ? 0.2186 0.2228 0.1986 0.0369  0.0250  0.0339  53  ILE   C O   
1443 C CB  . ILE   B 47  ? 0.2281 0.2411 0.2265 0.0296  0.0206  0.0270  53  ILE   C CB  
1444 C CG1 . ILE   B 47  ? 0.2456 0.2611 0.2583 0.0259  0.0214  0.0273  53  ILE   C CG1 
1445 C CG2 . ILE   B 47  ? 0.2305 0.2453 0.2205 0.0304  0.0141  0.0209  53  ILE   C CG2 
1446 C CD1 . ILE   B 47  ? 0.2547 0.2717 0.2751 0.0205  0.0141  0.0245  53  ILE   C CD1 
1447 N N   . ALA   B 48  ? 0.1908 0.2000 0.1755 0.0311  0.0128  0.0258  54  ALA   C N   
1448 C CA  . ALA   B 48  ? 0.1812 0.1883 0.1543 0.0358  0.0110  0.0251  54  ALA   C CA  
1449 C C   . ALA   B 48  ? 0.1827 0.1898 0.1440 0.0414  0.0104  0.0223  54  ALA   C C   
1450 O O   . ALA   B 48  ? 0.1711 0.1816 0.1346 0.0401  0.0083  0.0183  54  ALA   C O   
1451 C CB  . ALA   B 48  ? 0.1741 0.1838 0.1496 0.0332  0.0044  0.0206  54  ALA   C CB  
1452 N N   . ARG   B 49  ? 0.1849 0.1875 0.1328 0.0480  0.0117  0.0243  55  ARG   C N   
1453 C CA  . ARG   B 49  ? 0.1995 0.2008 0.1334 0.0547  0.0096  0.0208  55  ARG   C CA  
1454 C C   . ARG   B 49  ? 0.2208 0.2206 0.1468 0.0588  0.0034  0.0185  55  ARG   C C   
1455 O O   . ARG   B 49  ? 0.2455 0.2392 0.1607 0.0641  0.0056  0.0230  55  ARG   C O   
1456 C CB  . ARG   B 49  ? 0.2208 0.2163 0.1438 0.0603  0.0181  0.0262  55  ARG   C CB  
1457 C CG  . ARG   B 49  ? 0.2289 0.2265 0.1629 0.0564  0.0250  0.0288  55  ARG   C CG  
1458 C CD  . ARG   B 49  ? 0.2545 0.2574 0.1949 0.0535  0.0209  0.0224  55  ARG   C CD  
1459 N NE  . ARG   B 49  ? 0.2526 0.2572 0.2046 0.0503  0.0273  0.0253  55  ARG   C NE  
1460 C CZ  . ARG   B 49  ? 0.2757 0.2845 0.2371 0.0467  0.0249  0.0214  55  ARG   C CZ  
1461 N NH1 . ARG   B 49  ? 0.2402 0.2517 0.2014 0.0452  0.0170  0.0149  55  ARG   C NH1 
1462 N NH2 . ARG   B 49  ? 0.2879 0.2981 0.2604 0.0444  0.0304  0.0241  55  ARG   C NH2 
1463 N N   . CYS   B 50  ? 0.2086 0.2138 0.1407 0.0566  -0.0044 0.0117  56  CYS   C N   
1464 C CA  . CYS   B 50  ? 0.2255 0.2310 0.1561 0.0590  -0.0106 0.0091  56  CYS   C CA  
1465 C C   . CYS   B 50  ? 0.2265 0.2388 0.1660 0.0566  -0.0181 0.0008  56  CYS   C C   
1466 O O   . CYS   B 50  ? 0.2109 0.2268 0.1576 0.0525  -0.0179 -0.0020 56  CYS   C O   
1467 C CB  . CYS   B 50  ? 0.2175 0.2225 0.1565 0.0546  -0.0079 0.0134  56  CYS   C CB  
1468 S SG  . CYS   B 50  ? 0.1953 0.2067 0.1519 0.0449  -0.0081 0.0109  56  CYS   C SG  
1469 N N   . ASP   B 51  ? 0.2179 0.2319 0.1592 0.0588  -0.0240 -0.0025 57  ASP   C N   
1470 C CA  . ASP   B 51  ? 0.2245 0.2454 0.1781 0.0560  -0.0299 -0.0096 57  ASP   C CA  
1471 C C   . ASP   B 51  ? 0.2185 0.2425 0.1833 0.0517  -0.0293 -0.0091 57  ASP   C C   
1472 O O   . ASP   B 51  ? 0.2209 0.2500 0.1950 0.0514  -0.0340 -0.0144 57  ASP   C O   
1473 C CB  . ASP   B 51  ? 0.2608 0.2822 0.2098 0.0628  -0.0387 -0.0162 57  ASP   C CB  
1474 C CG  . ASP   B 51  ? 0.3116 0.3291 0.2518 0.0696  -0.0423 -0.0149 57  ASP   C CG  
1475 O OD1 . ASP   B 51  ? 0.3261 0.3401 0.2640 0.0689  -0.0375 -0.0086 57  ASP   C OD1 
1476 O OD2 . ASP   B 51  ? 0.3927 0.4100 0.3287 0.0760  -0.0508 -0.0205 57  ASP   C OD2 
1477 N N   . CYS   B 52  ? 0.1924 0.2138 0.1579 0.0481  -0.0234 -0.0034 58  CYS   C N   
1478 C CA  . CYS   B 52  ? 0.1814 0.2048 0.1560 0.0443  -0.0226 -0.0034 58  CYS   C CA  
1479 C C   . CYS   B 52  ? 0.1718 0.2015 0.1581 0.0395  -0.0234 -0.0082 58  CYS   C C   
1480 O O   . CYS   B 52  ? 0.1647 0.1960 0.1534 0.0363  -0.0223 -0.0091 58  CYS   C O   
1481 C CB  . CYS   B 52  ? 0.1946 0.2140 0.1691 0.0406  -0.0170 0.0023  58  CYS   C CB  
1482 S SG  . CYS   B 52  ? 0.2188 0.2302 0.1842 0.0454  -0.0147 0.0089  58  CYS   C SG  
1483 N N   . GLN   B 53  ? 0.1666 0.1993 0.1604 0.0389  -0.0245 -0.0106 59  GLN   C N   
1484 C CA  . GLN   B 53  ? 0.1636 0.2016 0.1690 0.0343  -0.0231 -0.0140 59  GLN   C CA  
1485 C C   . GLN   B 53  ? 0.1490 0.1856 0.1565 0.0315  -0.0191 -0.0122 59  GLN   C C   
1486 O O   . GLN   B 53  ? 0.1552 0.1955 0.1711 0.0290  -0.0171 -0.0148 59  GLN   C O   
1487 C CB  . GLN   B 53  ? 0.1680 0.2122 0.1836 0.0364  -0.0277 -0.0202 59  GLN   C CB  
1488 C CG  . GLN   B 53  ? 0.1906 0.2366 0.2072 0.0374  -0.0318 -0.0237 59  GLN   C CG  
1489 C CD  . GLN   B 53  ? 0.2194 0.2718 0.2493 0.0392  -0.0373 -0.0305 59  GLN   C CD  
1490 O OE1 . GLN   B 53  ? 0.2392 0.2914 0.2661 0.0453  -0.0445 -0.0338 59  GLN   C OE1 
1491 N NE2 . GLN   B 53  ? 0.1818 0.2393 0.2268 0.0343  -0.0339 -0.0325 59  GLN   C NE2 
1492 N N   . THR   B 54  ? 0.1584 0.1892 0.1586 0.0320  -0.0175 -0.0078 60  THR   C N   
1493 C CA  . THR   B 54  ? 0.1779 0.2062 0.1791 0.0295  -0.0145 -0.0067 60  THR   C CA  
1494 C C   . THR   B 54  ? 0.1785 0.2011 0.1743 0.0272  -0.0126 -0.0021 60  THR   C C   
1495 O O   . THR   B 54  ? 0.1929 0.2129 0.1842 0.0290  -0.0129 0.0011  60  THR   C O   
1496 C CB  . THR   B 54  ? 0.2423 0.2692 0.2444 0.0331  -0.0157 -0.0074 60  THR   C CB  
1497 O OG1 . THR   B 54  ? 0.2887 0.3104 0.2841 0.0367  -0.0173 -0.0035 60  THR   C OG1 
1498 C CG2 . THR   B 54  ? 0.2456 0.2787 0.2556 0.0359  -0.0182 -0.0123 60  THR   C CG2 
1499 N N   . GLY   B 55  ? 0.1707 0.1913 0.1670 0.0235  -0.0107 -0.0020 61  GLY   C N   
1500 C CA  . GLY   B 55  ? 0.1719 0.1875 0.1657 0.0213  -0.0101 0.0014  61  GLY   C CA  
1501 C C   . GLY   B 55  ? 0.1538 0.1665 0.1469 0.0184  -0.0096 0.0002  61  GLY   C C   
1502 O O   . GLY   B 55  ? 0.1666 0.1802 0.1596 0.0188  -0.0086 -0.0027 61  GLY   C O   
1503 N N   . VAL   B 56  ? 0.1442 0.1532 0.1364 0.0159  -0.0103 0.0023  62  VAL   C N   
1504 C CA  . VAL   B 56  ? 0.1390 0.1436 0.1282 0.0141  -0.0112 0.0009  62  VAL   C CA  
1505 C C   . VAL   B 56  ? 0.1429 0.1471 0.1314 0.0114  -0.0119 0.0021  62  VAL   C C   
1506 O O   . VAL   B 56  ? 0.1501 0.1547 0.1424 0.0107  -0.0126 0.0047  62  VAL   C O   
1507 C CB  . VAL   B 56  ? 0.1600 0.1588 0.1508 0.0145  -0.0137 0.0014  62  VAL   C CB  
1508 C CG1 . VAL   B 56  ? 0.1885 0.1816 0.1749 0.0132  -0.0165 -0.0008 62  VAL   C CG1 
1509 C CG2 . VAL   B 56  ? 0.1635 0.1618 0.1551 0.0175  -0.0132 0.0003  62  VAL   C CG2 
1510 N N   . TYR   B 57  ? 0.1479 0.1501 0.1310 0.0102  -0.0116 0.0007  63  TYR   C N   
1511 C CA  . TYR   B 57  ? 0.1481 0.1484 0.1297 0.0081  -0.0130 0.0022  63  TYR   C CA  
1512 C C   . TYR   B 57  ? 0.1619 0.1548 0.1367 0.0080  -0.0164 0.0012  63  TYR   C C   
1513 O O   . TYR   B 57  ? 0.1707 0.1601 0.1391 0.0095  -0.0161 -0.0011 63  TYR   C O   
1514 C CB  . TYR   B 57  ? 0.1499 0.1536 0.1309 0.0070  -0.0098 0.0024  63  TYR   C CB  
1515 C CG  . TYR   B 57  ? 0.1493 0.1507 0.1236 0.0070  -0.0066 0.0012  63  TYR   C CG  
1516 C CD1 . TYR   B 57  ? 0.1865 0.1907 0.1618 0.0084  -0.0030 -0.0010 63  TYR   C CD1 
1517 C CD2 . TYR   B 57  ? 0.1630 0.1593 0.1302 0.0059  -0.0065 0.0025  63  TYR   C CD2 
1518 C CE1 . TYR   B 57  ? 0.1994 0.2015 0.1692 0.0086  0.0018  -0.0017 63  TYR   C CE1 
1519 C CE2 . TYR   B 57  ? 0.1856 0.1786 0.1450 0.0064  -0.0020 0.0023  63  TYR   C CE2 
1520 C CZ  . TYR   B 57  ? 0.2032 0.1995 0.1645 0.0076  0.0028  0.0002  63  TYR   C CZ  
1521 O OH  . TYR   B 57  ? 0.2360 0.2293 0.1906 0.0082  0.0089  0.0004  63  TYR   C OH  
1522 N N   . TYR   B 58  ? 0.1730 0.1634 0.1486 0.0067  -0.0200 0.0026  64  TYR   C N   
1523 C CA  . TYR   B 58  ? 0.1851 0.1679 0.1533 0.0072  -0.0249 0.0013  64  TYR   C CA  
1524 C C   . TYR   B 58  ? 0.1909 0.1706 0.1485 0.0073  -0.0230 0.0020  64  TYR   C C   
1525 O O   . TYR   B 58  ? 0.1858 0.1681 0.1462 0.0058  -0.0215 0.0043  64  TYR   C O   
1526 C CB  . TYR   B 58  ? 0.1890 0.1702 0.1657 0.0062  -0.0309 0.0020  64  TYR   C CB  
1527 C CG  . TYR   B 58  ? 0.2157 0.1884 0.1846 0.0074  -0.0379 -0.0002 64  TYR   C CG  
1528 C CD1 . TYR   B 58  ? 0.2400 0.2072 0.2037 0.0093  -0.0412 -0.0038 64  TYR   C CD1 
1529 C CD2 . TYR   B 58  ? 0.2480 0.2175 0.2135 0.0074  -0.0416 0.0008  64  TYR   C CD2 
1530 C CE1 . TYR   B 58  ? 0.2684 0.2266 0.2223 0.0114  -0.0486 -0.0068 64  TYR   C CE1 
1531 C CE2 . TYR   B 58  ? 0.2690 0.2296 0.2249 0.0095  -0.0492 -0.0016 64  TYR   C CE2 
1532 C CZ  . TYR   B 58  ? 0.2830 0.2378 0.2327 0.0116  -0.0529 -0.0056 64  TYR   C CZ  
1533 O OH  . TYR   B 58  ? 0.3292 0.2740 0.2673 0.0146  -0.0614 -0.0089 64  TYR   C OH  
1534 N N   . CYS   B 59  ? 0.2042 0.1773 0.1489 0.0093  -0.0228 0.0001  65  CYS   C N   
1535 C CA  . CYS   B 59  ? 0.2253 0.1933 0.1572 0.0101  -0.0200 0.0015  65  CYS   C CA  
1536 C C   . CYS   B 59  ? 0.2511 0.2086 0.1706 0.0124  -0.0273 0.0006  65  CYS   C C   
1537 O O   . CYS   B 59  ? 0.2675 0.2185 0.1767 0.0153  -0.0299 -0.0027 65  CYS   C O   
1538 C CB  . CYS   B 59  ? 0.2331 0.2016 0.1588 0.0114  -0.0123 0.0005  65  CYS   C CB  
1539 S SG  . CYS   B 59  ? 0.2676 0.2281 0.1758 0.0130  -0.0063 0.0029  65  CYS   C SG  
1540 N N   . SER   B 60  ? 0.2427 0.1981 0.1632 0.0116  -0.0317 0.0029  66  SER   C N   
1541 C CA  . SER   B 60  ? 0.2819 0.2274 0.1919 0.0142  -0.0405 0.0016  66  SER   C CA  
1542 C C   . SER   B 60  ? 0.2911 0.2259 0.1779 0.0181  -0.0388 0.0014  66  SER   C C   
1543 O O   . SER   B 60  ? 0.3143 0.2400 0.1895 0.0217  -0.0464 -0.0020 66  SER   C O   
1544 C CB  . SER   B 60  ? 0.3344 0.2798 0.2507 0.0131  -0.0456 0.0041  66  SER   C CB  
1545 O OG  . SER   B 60  ? 0.4331 0.3785 0.3450 0.0122  -0.0393 0.0083  66  SER   C OG  
1546 N N   . SER   B 61  ? 0.2810 0.2164 0.1613 0.0177  -0.0288 0.0047  67  SER   C N   
1547 C CA  . SER   B 61  ? 0.3043 0.2289 0.1614 0.0217  -0.0247 0.0055  67  SER   C CA  
1548 C C   . SER   B 61  ? 0.3205 0.2423 0.1685 0.0248  -0.0225 0.0011  67  SER   C C   
1549 O O   . SER   B 61  ? 0.3378 0.2494 0.1644 0.0292  -0.0193 0.0010  67  SER   C O   
1550 C CB  . SER   B 61  ? 0.3136 0.2395 0.1690 0.0200  -0.0136 0.0108  67  SER   C CB  
1551 O OG  . SER   B 61  ? 0.2980 0.2345 0.1672 0.0172  -0.0048 0.0104  67  SER   C OG  
1552 N N   . ARG   B 62  ? 0.2982 0.2277 0.1610 0.0232  -0.0240 -0.0025 68  ARG   C N   
1553 C CA  . ARG   B 62  ? 0.2988 0.2256 0.1556 0.0262  -0.0238 -0.0074 68  ARG   C CA  
1554 C C   . ARG   B 62  ? 0.3109 0.2366 0.1757 0.0265  -0.0353 -0.0122 68  ARG   C C   
1555 O O   . ARG   B 62  ? 0.3248 0.2479 0.1870 0.0289  -0.0365 -0.0169 68  ARG   C O   
1556 C CB  . ARG   B 62  ? 0.3081 0.2448 0.1762 0.0244  -0.0136 -0.0074 68  ARG   C CB  
1557 C CG  . ARG   B 62  ? 0.3148 0.2527 0.1777 0.0241  -0.0017 -0.0035 68  ARG   C CG  
1558 C CD  . ARG   B 62  ? 0.3364 0.2635 0.1765 0.0294  0.0034  -0.0047 68  ARG   C CD  
1559 N NE  . ARG   B 62  ? 0.3935 0.3221 0.2312 0.0289  0.0167  -0.0004 68  ARG   C NE  
1560 C CZ  . ARG   B 62  ? 0.4566 0.3790 0.2837 0.0290  0.0206  0.0049  68  ARG   C CZ  
1561 N NH1 . ARG   B 62  ? 0.4750 0.3889 0.2911 0.0302  0.0115  0.0063  68  ARG   C NH1 
1562 N NH2 . ARG   B 62  ? 0.4502 0.3743 0.2783 0.0281  0.0337  0.0089  68  ARG   C NH2 
1563 N N   . ARG   B 63  ? 0.3154 0.2439 0.1934 0.0238  -0.0431 -0.0111 69  ARG   C N   
1564 C CA  . ARG   B 63  ? 0.3189 0.2482 0.2107 0.0230  -0.0527 -0.0148 69  ARG   C CA  
1565 C C   . ARG   B 63  ? 0.3148 0.2506 0.2183 0.0218  -0.0483 -0.0165 69  ARG   C C   
1566 O O   . ARG   B 63  ? 0.3272 0.2589 0.2322 0.0234  -0.0537 -0.0211 69  ARG   C O   
1567 C CB  . ARG   B 63  ? 0.3633 0.2800 0.2414 0.0276  -0.0638 -0.0202 69  ARG   C CB  
1568 C CG  . ARG   B 63  ? 0.4293 0.3399 0.3002 0.0289  -0.0714 -0.0187 69  ARG   C CG  
1569 C CD  . ARG   B 63  ? 0.5291 0.4278 0.3894 0.0336  -0.0848 -0.0251 69  ARG   C CD  
1570 N NE  . ARG   B 63  ? 0.6215 0.5110 0.4659 0.0371  -0.0915 -0.0239 69  ARG   C NE  
1571 C CZ  . ARG   B 63  ? 0.7064 0.5819 0.5230 0.0436  -0.0956 -0.0266 69  ARG   C CZ  
1572 N NH1 . ARG   B 63  ? 0.7222 0.5919 0.5243 0.0473  -0.0930 -0.0310 69  ARG   C NH1 
1573 N NH2 . ARG   B 63  ? 0.7267 0.5934 0.5287 0.0471  -0.1019 -0.0247 69  ARG   C NH2 
1574 N N   . LYS   B 64  ? 0.2861 0.2314 0.1978 0.0192  -0.0388 -0.0129 70  LYS   C N   
1575 C CA  . LYS   B 64  ? 0.2833 0.2340 0.2039 0.0189  -0.0347 -0.0143 70  LYS   C CA  
1576 C C   . LYS   B 64  ? 0.2462 0.2076 0.1818 0.0156  -0.0296 -0.0104 70  LYS   C C   
1577 O O   . LYS   B 64  ? 0.2363 0.2013 0.1717 0.0140  -0.0259 -0.0071 70  LYS   C O   
1578 C CB  . LYS   B 64  ? 0.3426 0.2916 0.2505 0.0218  -0.0268 -0.0159 70  LYS   C CB  
1579 C CG  . LYS   B 64  ? 0.4775 0.4169 0.3717 0.0263  -0.0299 -0.0213 70  LYS   C CG  
1580 C CD  . LYS   B 64  ? 0.5736 0.5138 0.4591 0.0288  -0.0196 -0.0220 70  LYS   C CD  
1581 C CE  . LYS   B 64  ? 0.6706 0.6031 0.5455 0.0336  -0.0207 -0.0279 70  LYS   C CE  
1582 N NZ  . LYS   B 64  ? 0.7204 0.6398 0.5753 0.0376  -0.0277 -0.0312 70  LYS   C NZ  
1583 N N   . HIS   B 65  ? 0.2240 0.1896 0.1702 0.0153  -0.0287 -0.0110 71  HIS   C N   
1584 C CA  . HIS   B 65  ? 0.2014 0.1762 0.1587 0.0135  -0.0237 -0.0078 71  HIS   C CA  
1585 C C   . HIS   B 65  ? 0.2243 0.2025 0.1794 0.0153  -0.0174 -0.0092 71  HIS   C C   
1586 O O   . HIS   B 65  ? 0.2581 0.2322 0.2082 0.0178  -0.0175 -0.0126 71  HIS   C O   
1587 C CB  . HIS   B 65  ? 0.2016 0.1781 0.1718 0.0127  -0.0264 -0.0068 71  HIS   C CB  
1588 C CG  . HIS   B 65  ? 0.2190 0.1937 0.1964 0.0107  -0.0318 -0.0054 71  HIS   C CG  
1589 N ND1 . HIS   B 65  ? 0.2415 0.2217 0.2279 0.0087  -0.0301 -0.0015 71  HIS   C ND1 
1590 C CD2 . HIS   B 65  ? 0.2345 0.2027 0.2132 0.0109  -0.0390 -0.0079 71  HIS   C CD2 
1591 C CE1 . HIS   B 65  ? 0.2208 0.1982 0.2145 0.0075  -0.0355 -0.0014 71  HIS   C CE1 
1592 N NE2 . HIS   B 65  ? 0.2558 0.2261 0.2459 0.0086  -0.0414 -0.0053 71  HIS   C NE2 
1593 N N   . TYR   B 66  ? 0.1902 0.1758 0.1498 0.0142  -0.0123 -0.0072 72  TYR   C N   
1594 C CA  . TYR   B 66  ? 0.1886 0.1786 0.1497 0.0158  -0.0068 -0.0087 72  TYR   C CA  
1595 C C   . TYR   B 66  ? 0.1830 0.1808 0.1555 0.0156  -0.0062 -0.0074 72  TYR   C C   
1596 O O   . TYR   B 66  ? 0.1849 0.1863 0.1619 0.0139  -0.0068 -0.0050 72  TYR   C O   
1597 C CB  . TYR   B 66  ? 0.2040 0.1958 0.1610 0.0150  -0.0009 -0.0081 72  TYR   C CB  
1598 C CG  . TYR   B 66  ? 0.2318 0.2152 0.1743 0.0164  0.0003  -0.0090 72  TYR   C CG  
1599 C CD1 . TYR   B 66  ? 0.2492 0.2289 0.1846 0.0196  0.0034  -0.0122 72  TYR   C CD1 
1600 C CD2 . TYR   B 66  ? 0.2534 0.2319 0.1879 0.0152  -0.0011 -0.0065 72  TYR   C CD2 
1601 C CE1 . TYR   B 66  ? 0.2706 0.2414 0.1895 0.0218  0.0050  -0.0131 72  TYR   C CE1 
1602 C CE2 . TYR   B 66  ? 0.2756 0.2449 0.1937 0.0174  -0.0002 -0.0071 72  TYR   C CE2 
1603 C CZ  . TYR   B 66  ? 0.2969 0.2622 0.2063 0.0209  0.0030  -0.0104 72  TYR   C CZ  
1604 O OH  . TYR   B 66  ? 0.3387 0.2937 0.2288 0.0240  0.0045  -0.0109 72  TYR   C OH  
1605 N N   . PRO   B 67  ? 0.1738 0.1736 0.1501 0.0181  -0.0052 -0.0094 73  PRO   C N   
1606 C CA  . PRO   B 67  ? 0.1658 0.1720 0.1506 0.0191  -0.0052 -0.0086 73  PRO   C CA  
1607 C C   . PRO   B 67  ? 0.1797 0.1928 0.1689 0.0188  -0.0013 -0.0097 73  PRO   C C   
1608 O O   . PRO   B 67  ? 0.2040 0.2173 0.1918 0.0191  0.0030  -0.0119 73  PRO   C O   
1609 C CB  . PRO   B 67  ? 0.1757 0.1802 0.1624 0.0224  -0.0061 -0.0105 73  PRO   C CB  
1610 C CG  . PRO   B 67  ? 0.1931 0.1929 0.1734 0.0233  -0.0042 -0.0137 73  PRO   C CG  
1611 C CD  . PRO   B 67  ? 0.1864 0.1820 0.1585 0.0208  -0.0044 -0.0129 73  PRO   C CD  
1612 N N   . VAL   B 68  ? 0.1693 0.1875 0.1640 0.0183  -0.0024 -0.0086 74  VAL   C N   
1613 C CA  . VAL   B 68  ? 0.1749 0.1997 0.1767 0.0177  0.0003  -0.0104 74  VAL   C CA  
1614 C C   . VAL   B 68  ? 0.1569 0.1870 0.1654 0.0197  -0.0030 -0.0112 74  VAL   C C   
1615 O O   . VAL   B 68  ? 0.1668 0.1951 0.1722 0.0209  -0.0065 -0.0091 74  VAL   C O   
1616 C CB  . VAL   B 68  ? 0.1959 0.2199 0.1958 0.0141  0.0022  -0.0086 74  VAL   C CB  
1617 C CG1 . VAL   B 68  ? 0.2289 0.2473 0.2205 0.0128  0.0061  -0.0080 74  VAL   C CG1 
1618 C CG2 . VAL   B 68  ? 0.1969 0.2192 0.1943 0.0130  -0.0016 -0.0059 74  VAL   C CG2 
1619 N N   . SER   B 69  ? 0.1461 0.1827 0.1643 0.0203  -0.0019 -0.0143 75  SER   C N   
1620 C CA  . SER   B 69  ? 0.1545 0.1964 0.1798 0.0221  -0.0060 -0.0163 75  SER   C CA  
1621 C C   . SER   B 69  ? 0.1498 0.1932 0.1779 0.0185  -0.0049 -0.0160 75  SER   C C   
1622 O O   . SER   B 69  ? 0.1740 0.2166 0.2032 0.0151  0.0001  -0.0152 75  SER   C O   
1623 C CB  . SER   B 69  ? 0.1860 0.2345 0.2240 0.0243  -0.0060 -0.0208 75  SER   C CB  
1624 O OG  . SER   B 69  ? 0.2443 0.2912 0.2805 0.0281  -0.0074 -0.0213 75  SER   C OG  
1625 N N   . PHE   B 70  ? 0.1380 0.1822 0.1654 0.0195  -0.0093 -0.0162 76  PHE   C N   
1626 C CA  . PHE   B 70  ? 0.1520 0.1970 0.1824 0.0164  -0.0087 -0.0162 76  PHE   C CA  
1627 C C   . PHE   B 70  ? 0.1498 0.1992 0.1871 0.0187  -0.0140 -0.0203 76  PHE   C C   
1628 O O   . PHE   B 70  ? 0.1645 0.2146 0.1993 0.0235  -0.0188 -0.0219 76  PHE   C O   
1629 C CB  . PHE   B 70  ? 0.1526 0.1918 0.1728 0.0145  -0.0080 -0.0119 76  PHE   C CB  
1630 C CG  . PHE   B 70  ? 0.1471 0.1833 0.1590 0.0176  -0.0110 -0.0099 76  PHE   C CG  
1631 C CD1 . PHE   B 70  ? 0.1531 0.1855 0.1592 0.0186  -0.0103 -0.0073 76  PHE   C CD1 
1632 C CD2 . PHE   B 70  ? 0.1548 0.1915 0.1649 0.0197  -0.0140 -0.0105 76  PHE   C CD2 
1633 C CE1 . PHE   B 70  ? 0.1606 0.1898 0.1607 0.0212  -0.0117 -0.0045 76  PHE   C CE1 
1634 C CE2 . PHE   B 70  ? 0.1661 0.1995 0.1680 0.0228  -0.0149 -0.0078 76  PHE   C CE2 
1635 C CZ  . PHE   B 70  ? 0.1563 0.1859 0.1539 0.0233  -0.0134 -0.0044 76  PHE   C CZ  
1636 N N   . SER   B 71  ? 0.1414 0.1930 0.1870 0.0159  -0.0136 -0.0221 77  SER   C N   
1637 C CA  . SER   B 71  ? 0.1504 0.2061 0.2044 0.0182  -0.0196 -0.0274 77  SER   C CA  
1638 C C   . SER   B 71  ? 0.1622 0.2144 0.2052 0.0215  -0.0244 -0.0274 77  SER   C C   
1639 O O   . SER   B 71  ? 0.1725 0.2199 0.2034 0.0215  -0.0223 -0.0228 77  SER   C O   
1640 C CB  . SER   B 71  ? 0.1510 0.2100 0.2205 0.0139  -0.0174 -0.0298 77  SER   C CB  
1641 O OG  . SER   B 71  ? 0.1567 0.2114 0.2218 0.0103  -0.0143 -0.0264 77  SER   C OG  
1642 N N   . LYS   B 72  ? 0.1611 0.2158 0.2090 0.0246  -0.0309 -0.0328 78  LYS   C N   
1643 C CA  . LYS   B 72  ? 0.1800 0.2309 0.2167 0.0282  -0.0348 -0.0335 78  LYS   C CA  
1644 C C   . LYS   B 72  ? 0.1685 0.2178 0.2082 0.0240  -0.0323 -0.0329 78  LYS   C C   
1645 O O   . LYS   B 72  ? 0.2057 0.2577 0.2592 0.0195  -0.0307 -0.0345 78  LYS   C O   
1646 C CB  . LYS   B 72  ? 0.2254 0.2786 0.2649 0.0340  -0.0438 -0.0405 78  LYS   C CB  
1647 C CG  . LYS   B 72  ? 0.2857 0.3396 0.3215 0.0390  -0.0469 -0.0408 78  LYS   C CG  
1648 C CD  . LYS   B 72  ? 0.4175 0.4698 0.4459 0.0471  -0.0566 -0.0461 78  LYS   C CD  
1649 C CE  . LYS   B 72  ? 0.5242 0.5737 0.5411 0.0531  -0.0586 -0.0436 78  LYS   C CE  
1650 N NZ  . LYS   B 72  ? 0.6014 0.6429 0.5955 0.0597  -0.0598 -0.0406 78  LYS   C NZ  
1651 N N   . PRO   B 73  ? 0.1654 0.2101 0.1933 0.0255  -0.0318 -0.0305 79  PRO   C N   
1652 C CA  . PRO   B 73  ? 0.1608 0.2038 0.1922 0.0218  -0.0297 -0.0300 79  PRO   C CA  
1653 C C   . PRO   B 73  ? 0.1768 0.2222 0.2209 0.0213  -0.0345 -0.0367 79  PRO   C C   
1654 O O   . PRO   B 73  ? 0.1923 0.2386 0.2356 0.0264  -0.0414 -0.0427 79  PRO   C O   
1655 C CB  . PRO   B 73  ? 0.1985 0.2369 0.2158 0.0254  -0.0293 -0.0277 79  PRO   C CB  
1656 C CG  . PRO   B 73  ? 0.2170 0.2541 0.2233 0.0294  -0.0286 -0.0246 79  PRO   C CG  
1657 C CD  . PRO   B 73  ? 0.1672 0.2080 0.1791 0.0307  -0.0320 -0.0277 79  PRO   C CD  
1658 N N   . SER   B 74  ? 0.1750 0.2208 0.2310 0.0155  -0.0312 -0.0359 80  SER   C N   
1659 C CA  . SER   B 74  ? 0.1951 0.2433 0.2671 0.0142  -0.0352 -0.0422 80  SER   C CA  
1660 C C   . SER   B 74  ? 0.1901 0.2356 0.2702 0.0085  -0.0307 -0.0395 80  SER   C C   
1661 O O   . SER   B 74  ? 0.1771 0.2187 0.2491 0.0060  -0.0251 -0.0330 80  SER   C O   
1662 C CB  . SER   B 74  ? 0.2492 0.3035 0.3357 0.0135  -0.0365 -0.0455 80  SER   C CB  
1663 O OG  . SER   B 74  ? 0.3143 0.3694 0.4074 0.0081  -0.0283 -0.0403 80  SER   C OG  
1664 N N   . LEU   B 75  ? 0.1812 0.2279 0.2776 0.0067  -0.0339 -0.0448 81  LEU   C N   
1665 C CA  . LEU   B 75  ? 0.1902 0.2334 0.2960 0.0015  -0.0299 -0.0424 81  LEU   C CA  
1666 C C   . LEU   B 75  ? 0.2089 0.2544 0.3274 -0.0038 -0.0228 -0.0387 81  LEU   C C   
1667 O O   . LEU   B 75  ? 0.2274 0.2784 0.3623 -0.0043 -0.0246 -0.0434 81  LEU   C O   
1668 C CB  . LEU   B 75  ? 0.2029 0.2464 0.3228 0.0022  -0.0370 -0.0506 81  LEU   C CB  
1669 C CG  . LEU   B 75  ? 0.2487 0.2875 0.3582 0.0058  -0.0411 -0.0531 81  LEU   C CG  
1670 C CD1 . LEU   B 75  ? 0.2784 0.3182 0.3982 0.0092  -0.0510 -0.0638 81  LEU   C CD1 
1671 C CD2 . LEU   B 75  ? 0.2606 0.2936 0.3697 0.0017  -0.0356 -0.0473 81  LEU   C CD2 
1672 N N   . ILE   B 76  ? 0.1965 0.2374 0.3084 -0.0074 -0.0150 -0.0308 82  ILE   C N   
1673 C CA  . ILE   B 76  ? 0.2036 0.2449 0.3221 -0.0115 -0.0066 -0.0261 82  ILE   C CA  
1674 C C   . ILE   B 76  ? 0.2208 0.2551 0.3413 -0.0158 -0.0005 -0.0204 82  ILE   C C   
1675 O O   . ILE   B 76  ? 0.2088 0.2373 0.3174 -0.0153 -0.0014 -0.0173 82  ILE   C O   
1676 C CB  . ILE   B 76  ? 0.2199 0.2610 0.3217 -0.0096 -0.0033 -0.0216 82  ILE   C CB  
1677 C CG1 . ILE   B 76  ? 0.2494 0.2970 0.3516 -0.0053 -0.0088 -0.0270 82  ILE   C CG1 
1678 C CG2 . ILE   B 76  ? 0.2416 0.2803 0.3436 -0.0130 0.0064  -0.0157 82  ILE   C CG2 
1679 C CD1 . ILE   B 76  ? 0.3005 0.3482 0.3897 -0.0033 -0.0066 -0.0239 82  ILE   C CD1 
1680 N N   . PHE   B 77  ? 0.2281 0.2629 0.3652 -0.0200 0.0058  -0.0190 83  PHE   C N   
1681 C CA  . PHE   B 77  ? 0.2582 0.2851 0.3973 -0.0240 0.0123  -0.0128 83  PHE   C CA  
1682 C C   . PHE   B 77  ? 0.2712 0.2912 0.3892 -0.0238 0.0186  -0.0043 83  PHE   C C   
1683 O O   . PHE   B 77  ? 0.2886 0.3105 0.3998 -0.0230 0.0230  -0.0023 83  PHE   C O   
1684 C CB  . PHE   B 77  ? 0.2769 0.3059 0.4400 -0.0285 0.0190  -0.0128 83  PHE   C CB  
1685 C CG  . PHE   B 77  ? 0.3064 0.3260 0.4715 -0.0325 0.0270  -0.0053 83  PHE   C CG  
1686 C CD1 . PHE   B 77  ? 0.3300 0.3453 0.5048 -0.0342 0.0233  -0.0068 83  PHE   C CD1 
1687 C CD2 . PHE   B 77  ? 0.3438 0.3576 0.4980 -0.0338 0.0380  0.0035  83  PHE   C CD2 
1688 C CE1 . PHE   B 77  ? 0.3571 0.3625 0.5329 -0.0375 0.0307  0.0009  83  PHE   C CE1 
1689 C CE2 . PHE   B 77  ? 0.3652 0.3687 0.5179 -0.0366 0.0454  0.0112  83  PHE   C CE2 
1690 C CZ  . PHE   B 77  ? 0.3628 0.3622 0.5270 -0.0386 0.0417  0.0102  83  PHE   C CZ  
1691 N N   . VAL   B 78  ? 0.2692 0.2807 0.3771 -0.0242 0.0185  0.0003  84  VAL   C N   
1692 C CA  . VAL   B 78  ? 0.2777 0.2811 0.3651 -0.0234 0.0225  0.0079  84  VAL   C CA  
1693 C C   . VAL   B 78  ? 0.2878 0.2815 0.3772 -0.0264 0.0283  0.0144  84  VAL   C C   
1694 O O   . VAL   B 78  ? 0.2781 0.2690 0.3756 -0.0274 0.0248  0.0133  84  VAL   C O   
1695 C CB  . VAL   B 78  ? 0.2594 0.2615 0.3314 -0.0199 0.0150  0.0073  84  VAL   C CB  
1696 C CG1 . VAL   B 78  ? 0.2623 0.2556 0.3150 -0.0190 0.0173  0.0143  84  VAL   C CG1 
1697 C CG2 . VAL   B 78  ? 0.2417 0.2520 0.3111 -0.0169 0.0103  0.0020  84  VAL   C CG2 
1698 N N   . GLU   B 79  ? 0.3098 0.2974 0.3903 -0.0272 0.0374  0.0213  85  GLU   C N   
1699 C CA  . GLU   B 79  ? 0.3299 0.3065 0.4090 -0.0294 0.0442  0.0289  85  GLU   C CA  
1700 C C   . GLU   B 79  ? 0.3289 0.2966 0.3944 -0.0275 0.0383  0.0321  85  GLU   C C   
1701 O O   . GLU   B 79  ? 0.3195 0.2885 0.3718 -0.0243 0.0310  0.0301  85  GLU   C O   
1702 C CB  . GLU   B 79  ? 0.3973 0.3681 0.4634 -0.0290 0.0551  0.0358  85  GLU   C CB  
1703 C CG  . GLU   B 79  ? 0.5351 0.4987 0.6105 -0.0324 0.0666  0.0425  85  GLU   C CG  
1704 C CD  . GLU   B 79  ? 0.6154 0.5886 0.7188 -0.0361 0.0724  0.0386  85  GLU   C CD  
1705 O OE1 . GLU   B 79  ? 0.6250 0.6051 0.7297 -0.0353 0.0766  0.0365  85  GLU   C OE1 
1706 O OE2 . GLU   B 79  ? 0.6529 0.6270 0.7783 -0.0397 0.0718  0.0369  85  GLU   C OE2 
1707 N N   . ALA   B 80  ? 0.3255 0.2840 0.3953 -0.0295 0.0416  0.0372  86  ALA   C N   
1708 C CA  . ALA   B 80  ? 0.3311 0.2804 0.3897 -0.0276 0.0361  0.0406  86  ALA   C CA  
1709 C C   . ALA   B 80  ? 0.3277 0.2696 0.3598 -0.0238 0.0356  0.0458  86  ALA   C C   
1710 O O   . ALA   B 80  ? 0.3401 0.2784 0.3609 -0.0232 0.0430  0.0502  86  ALA   C O   
1711 C CB  . ALA   B 80  ? 0.3484 0.2874 0.4154 -0.0303 0.0413  0.0465  86  ALA   C CB  
1712 N N   . SER   B 81  ? 0.3120 0.2510 0.3348 -0.0209 0.0268  0.0453  87  SER   C N   
1713 C CA  . SER   B 81  ? 0.3055 0.2365 0.3053 -0.0169 0.0238  0.0497  87  SER   C CA  
1714 C C   . SER   B 81  ? 0.3258 0.2480 0.3232 -0.0153 0.0177  0.0526  87  SER   C C   
1715 O O   . SER   B 81  ? 0.3362 0.2584 0.3492 -0.0174 0.0171  0.0514  87  SER   C O   
1716 C CB  . SER   B 81  ? 0.2895 0.2292 0.2837 -0.0145 0.0173  0.0440  87  SER   C CB  
1717 O OG  . SER   B 81  ? 0.2765 0.2235 0.2822 -0.0143 0.0096  0.0383  87  SER   C OG  
1718 N N   . GLU   B 82  ? 0.3390 0.2534 0.3177 -0.0113 0.0125  0.0559  88  GLU   C N   
1719 C CA  . GLU   B 82  ? 0.3596 0.2664 0.3366 -0.0091 0.0052  0.0580  88  GLU   C CA  
1720 C C   . GLU   B 82  ? 0.3481 0.2658 0.3399 -0.0088 -0.0029 0.0503  88  GLU   C C   
1721 O O   . GLU   B 82  ? 0.3523 0.2664 0.3494 -0.0076 -0.0081 0.0505  88  GLU   C O   
1722 C CB  . GLU   B 82  ? 0.4388 0.3353 0.3930 -0.0042 -0.0001 0.0623  88  GLU   C CB  
1723 C CG  . GLU   B 82  ? 0.5709 0.4606 0.5051 -0.0027 0.0063  0.0667  88  GLU   C CG  
1724 C CD  . GLU   B 82  ? 0.6600 0.5598 0.5914 -0.0022 0.0049  0.0609  88  GLU   C CD  
1725 O OE1 . GLU   B 82  ? 0.6234 0.5311 0.5627 -0.0052 0.0124  0.0587  88  GLU   C OE1 
1726 O OE2 . GLU   B 82  ? 0.7188 0.6192 0.6429 0.0010  -0.0044 0.0581  88  GLU   C OE2 
1727 N N   . TYR   B 83  ? 0.3304 0.2608 0.3287 -0.0097 -0.0033 0.0439  89  TYR   C N   
1728 C CA  . TYR   B 83  ? 0.3305 0.2706 0.3396 -0.0088 -0.0093 0.0372  89  TYR   C CA  
1729 C C   . TYR   B 83  ? 0.3223 0.2694 0.3493 -0.0113 -0.0074 0.0320  89  TYR   C C   
1730 O O   . TYR   B 83  ? 0.3428 0.2938 0.3788 -0.0101 -0.0119 0.0277  89  TYR   C O   
1731 C CB  . TYR   B 83  ? 0.3270 0.2751 0.3305 -0.0076 -0.0110 0.0339  89  TYR   C CB  
1732 C CG  . TYR   B 83  ? 0.3485 0.2899 0.3350 -0.0050 -0.0141 0.0376  89  TYR   C CG  
1733 C CD1 . TYR   B 83  ? 0.3785 0.3167 0.3622 -0.0020 -0.0221 0.0379  89  TYR   C CD1 
1734 C CD2 . TYR   B 83  ? 0.3627 0.3016 0.3369 -0.0050 -0.0096 0.0396  89  TYR   C CD2 
1735 C CE1 . TYR   B 83  ? 0.4041 0.3359 0.3729 0.0009  -0.0266 0.0402  89  TYR   C CE1 
1736 C CE2 . TYR   B 83  ? 0.3905 0.3228 0.3481 -0.0019 -0.0135 0.0418  89  TYR   C CE2 
1737 C CZ  . TYR   B 83  ? 0.4240 0.3523 0.3787 0.0011  -0.0225 0.0420  89  TYR   C CZ  
1738 O OH  . TYR   B 83  ? 0.4873 0.4090 0.4264 0.0045  -0.0280 0.0430  89  TYR   C OH  
1739 N N   . TYR   B 84  ? 0.2992 0.2480 0.3321 -0.0145 -0.0009 0.0320  90  TYR   C N   
1740 C CA  . TYR   B 84  ? 0.2862 0.2419 0.3369 -0.0166 -0.0003 0.0259  90  TYR   C CA  
1741 C C   . TYR   B 84  ? 0.3126 0.2643 0.3727 -0.0204 0.0066  0.0286  90  TYR   C C   
1742 O O   . TYR   B 84  ? 0.3076 0.2559 0.3607 -0.0217 0.0133  0.0337  90  TYR   C O   
1743 C CB  . TYR   B 84  ? 0.2535 0.2210 0.3066 -0.0162 -0.0008 0.0197  90  TYR   C CB  
1744 C CG  . TYR   B 84  ? 0.2360 0.2088 0.2822 -0.0128 -0.0061 0.0167  90  TYR   C CG  
1745 C CD1 . TYR   B 84  ? 0.2403 0.2150 0.2749 -0.0116 -0.0057 0.0184  90  TYR   C CD1 
1746 C CD2 . TYR   B 84  ? 0.2263 0.2023 0.2786 -0.0106 -0.0109 0.0121  90  TYR   C CD2 
1747 C CE1 . TYR   B 84  ? 0.2329 0.2122 0.2635 -0.0089 -0.0100 0.0161  90  TYR   C CE1 
1748 C CE2 . TYR   B 84  ? 0.2137 0.1946 0.2610 -0.0075 -0.0142 0.0100  90  TYR   C CE2 
1749 C CZ  . TYR   B 84  ? 0.2210 0.2038 0.2585 -0.0070 -0.0136 0.0121  90  TYR   C CZ  
1750 O OH  . TYR   B 84  ? 0.2080 0.1950 0.2429 -0.0044 -0.0163 0.0107  90  TYR   C OH  
1751 N N   . PRO   B 85  ? 0.3228 0.2758 0.4006 -0.0222 0.0056  0.0244  91  PRO   C N   
1752 C CA  . PRO   B 85  ? 0.3259 0.2776 0.4178 -0.0264 0.0122  0.0255  91  PRO   C CA  
1753 C C   . PRO   B 85  ? 0.3268 0.2890 0.4240 -0.0276 0.0150  0.0213  91  PRO   C C   
1754 O O   . PRO   B 85  ? 0.3127 0.2833 0.4047 -0.0250 0.0103  0.0160  91  PRO   C O   
1755 C CB  . PRO   B 85  ? 0.3231 0.2752 0.4336 -0.0273 0.0076  0.0195  91  PRO   C CB  
1756 C CG  . PRO   B 85  ? 0.3316 0.2906 0.4381 -0.0233 -0.0006 0.0123  91  PRO   C CG  
1757 C CD  . PRO   B 85  ? 0.3230 0.2799 0.4096 -0.0203 -0.0017 0.0172  91  PRO   C CD  
1758 N N   . ALA   B 86  ? 0.3230 0.2853 0.4330 -0.0314 0.0226  0.0230  92  ALA   C N   
1759 C CA  . ALA   B 86  ? 0.3302 0.3030 0.4500 -0.0326 0.0247  0.0181  92  ALA   C CA  
1760 C C   . ALA   B 86  ? 0.3127 0.2946 0.4451 -0.0312 0.0153  0.0073  92  ALA   C C   
1761 O O   . ALA   B 86  ? 0.3199 0.2992 0.4640 -0.0318 0.0112  0.0039  92  ALA   C O   
1762 C CB  . ALA   B 86  ? 0.3420 0.3130 0.4792 -0.0372 0.0343  0.0214  92  ALA   C CB  
1763 N N   . ARG   B 87  ? 0.2868 0.2778 0.4143 -0.0285 0.0117  0.0022  93  ARG   C N   
1764 C CA  . ARG   B 87  ? 0.2632 0.2611 0.3967 -0.0257 0.0025  -0.0074 93  ARG   C CA  
1765 C C   . ARG   B 87  ? 0.2670 0.2742 0.3973 -0.0233 0.0003  -0.0119 93  ARG   C C   
1766 O O   . ARG   B 87  ? 0.2717 0.2804 0.3943 -0.0237 0.0056  -0.0077 93  ARG   C O   
1767 C CB  . ARG   B 87  ? 0.2635 0.2576 0.3828 -0.0221 -0.0029 -0.0073 93  ARG   C CB  
1768 C CG  . ARG   B 87  ? 0.2320 0.2272 0.3307 -0.0192 -0.0024 -0.0035 93  ARG   C CG  
1769 C CD  . ARG   B 87  ? 0.2435 0.2333 0.3301 -0.0169 -0.0051 -0.0004 93  ARG   C CD  
1770 N NE  . ARG   B 87  ? 0.2497 0.2437 0.3238 -0.0131 -0.0083 -0.0016 93  ARG   C NE  
1771 C CZ  . ARG   B 87  ? 0.2496 0.2450 0.3124 -0.0125 -0.0062 0.0017  93  ARG   C CZ  
1772 N NH1 . ARG   B 87  ? 0.2038 0.2024 0.2580 -0.0094 -0.0091 0.0007  93  ARG   C NH1 
1773 N NH2 . ARG   B 87  ? 0.2482 0.2415 0.3088 -0.0150 -0.0008 0.0061  93  ARG   C NH2 
1774 N N   . TYR   B 88  ? 0.2620 0.2747 0.3959 -0.0200 -0.0079 -0.0204 94  TYR   C N   
1775 C CA  . TYR   B 88  ? 0.2750 0.2951 0.4028 -0.0166 -0.0109 -0.0243 94  TYR   C CA  
1776 C C   . TYR   B 88  ? 0.2366 0.2553 0.3440 -0.0124 -0.0134 -0.0226 94  TYR   C C   
1777 O O   . TYR   B 88  ? 0.2378 0.2536 0.3418 -0.0102 -0.0175 -0.0248 94  TYR   C O   
1778 C CB  . TYR   B 88  ? 0.2991 0.3247 0.4399 -0.0144 -0.0188 -0.0344 94  TYR   C CB  
1779 C CG  . TYR   B 88  ? 0.3427 0.3722 0.5067 -0.0182 -0.0169 -0.0369 94  TYR   C CG  
1780 C CD1 . TYR   B 88  ? 0.3680 0.4042 0.5362 -0.0182 -0.0148 -0.0375 94  TYR   C CD1 
1781 C CD2 . TYR   B 88  ? 0.3768 0.4031 0.5602 -0.0221 -0.0165 -0.0384 94  TYR   C CD2 
1782 C CE1 . TYR   B 88  ? 0.3931 0.4337 0.5855 -0.0219 -0.0121 -0.0397 94  TYR   C CE1 
1783 C CE2 . TYR   B 88  ? 0.3902 0.4204 0.5983 -0.0261 -0.0139 -0.0406 94  TYR   C CE2 
1784 C CZ  . TYR   B 88  ? 0.4084 0.4461 0.6213 -0.0260 -0.0114 -0.0411 94  TYR   C CZ  
1785 O OH  . TYR   B 88  ? 0.4465 0.4888 0.6865 -0.0299 -0.0083 -0.0434 94  TYR   C OH  
1786 N N   . GLN   B 89  ? 0.1950 0.2155 0.2900 -0.0114 -0.0106 -0.0188 95  GLN   C N   
1787 C CA  . GLN   B 89  ? 0.1812 0.2011 0.2598 -0.0077 -0.0128 -0.0174 95  GLN   C CA  
1788 C C   . GLN   B 89  ? 0.1684 0.1945 0.2445 -0.0033 -0.0174 -0.0231 95  GLN   C C   
1789 O O   . GLN   B 89  ? 0.1806 0.2112 0.2615 -0.0035 -0.0171 -0.0250 95  GLN   C O   
1790 C CB  . GLN   B 89  ? 0.1779 0.1949 0.2447 -0.0088 -0.0079 -0.0102 95  GLN   C CB  
1791 C CG  . GLN   B 89  ? 0.1936 0.2107 0.2467 -0.0054 -0.0101 -0.0089 95  GLN   C CG  
1792 C CD  . GLN   B 89  ? 0.1947 0.2072 0.2377 -0.0065 -0.0072 -0.0024 95  GLN   C CD  
1793 O OE1 . GLN   B 89  ? 0.1864 0.1929 0.2289 -0.0088 -0.0049 0.0017  95  GLN   C OE1 
1794 N NE2 . GLN   B 89  ? 0.1800 0.1943 0.2141 -0.0044 -0.0078 -0.0015 95  GLN   C NE2 
1795 N N   . SER   B 90  ? 0.1601 0.1857 0.2287 0.0010  -0.0215 -0.0260 96  SER   C N   
1796 C CA  . SER   B 90  ? 0.1590 0.1887 0.2222 0.0061  -0.0258 -0.0309 96  SER   C CA  
1797 C C   . SER   B 90  ? 0.1619 0.1920 0.2110 0.0083  -0.0234 -0.0263 96  SER   C C   
1798 O O   . SER   B 90  ? 0.1666 0.1939 0.2103 0.0062  -0.0195 -0.0203 96  SER   C O   
1799 C CB  . SER   B 90  ? 0.1970 0.2250 0.2576 0.0106  -0.0308 -0.0365 96  SER   C CB  
1800 O OG  . SER   B 90  ? 0.2184 0.2425 0.2712 0.0111  -0.0282 -0.0325 96  SER   C OG  
1801 N N   . HIS   B 91  ? 0.1528 0.1860 0.1964 0.0127  -0.0263 -0.0294 97  HIS   C N   
1802 C CA  . HIS   B 91  ? 0.1595 0.1927 0.1909 0.0153  -0.0244 -0.0255 97  HIS   C CA  
1803 C C   . HIS   B 91  ? 0.1656 0.1989 0.1976 0.0112  -0.0198 -0.0201 97  HIS   C C   
1804 O O   . HIS   B 91  ? 0.1730 0.2045 0.1968 0.0116  -0.0173 -0.0155 97  HIS   C O   
1805 C CB  . HIS   B 91  ? 0.1579 0.1878 0.1799 0.0179  -0.0228 -0.0230 97  HIS   C CB  
1806 C CG  . HIS   B 91  ? 0.1901 0.2188 0.2084 0.0231  -0.0265 -0.0285 97  HIS   C CG  
1807 N ND1 . HIS   B 91  ? 0.2250 0.2535 0.2319 0.0295  -0.0281 -0.0302 97  HIS   C ND1 
1808 C CD2 . HIS   B 91  ? 0.1983 0.2255 0.2222 0.0233  -0.0291 -0.0330 97  HIS   C CD2 
1809 C CE1 . HIS   B 91  ? 0.2343 0.2608 0.2384 0.0337  -0.0316 -0.0357 97  HIS   C CE1 
1810 N NE2 . HIS   B 91  ? 0.2314 0.2574 0.2462 0.0301  -0.0325 -0.0379 97  HIS   C NE2 
1811 N N   . LEU   B 92  ? 0.1584 0.1936 0.2004 0.0076  -0.0186 -0.0209 98  LEU   C N   
1812 C CA  . LEU   B 92  ? 0.1579 0.1923 0.1991 0.0043  -0.0138 -0.0162 98  LEU   C CA  
1813 C C   . LEU   B 92  ? 0.1604 0.1990 0.2034 0.0058  -0.0140 -0.0180 98  LEU   C C   
1814 O O   . LEU   B 92  ? 0.1631 0.2059 0.2151 0.0072  -0.0171 -0.0231 98  LEU   C O   
1815 C CB  . LEU   B 92  ? 0.1623 0.1946 0.2124 -0.0004 -0.0103 -0.0147 98  LEU   C CB  
1816 C CG  . LEU   B 92  ? 0.2005 0.2300 0.2469 -0.0033 -0.0046 -0.0095 98  LEU   C CG  
1817 C CD1 . LEU   B 92  ? 0.2003 0.2244 0.2336 -0.0030 -0.0043 -0.0047 98  LEU   C CD1 
1818 C CD2 . LEU   B 92  ? 0.2286 0.2553 0.2836 -0.0074 -0.0002 -0.0076 98  LEU   C CD2 
1819 N N   . MET   B 93  ? 0.1488 0.1861 0.1844 0.0057  -0.0111 -0.0142 99  MET   C N   
1820 C CA  . MET   B 93  ? 0.1538 0.1945 0.1908 0.0074  -0.0109 -0.0156 99  MET   C CA  
1821 C C   . MET   B 93  ? 0.1717 0.2110 0.2096 0.0042  -0.0052 -0.0128 99  MET   C C   
1822 O O   . MET   B 93  ? 0.1865 0.2207 0.2161 0.0026  -0.0028 -0.0086 99  MET   C O   
1823 C CB  . MET   B 93  ? 0.1443 0.1832 0.1700 0.0110  -0.0125 -0.0137 99  MET   C CB  
1824 C CG  . MET   B 93  ? 0.1991 0.2382 0.2211 0.0151  -0.0169 -0.0160 99  MET   C CG  
1825 S SD  . MET   B 93  ? 0.2103 0.2459 0.2195 0.0189  -0.0166 -0.0120 99  MET   C SD  
1826 C CE  . MET   B 93  ? 0.2146 0.2457 0.2212 0.0145  -0.0126 -0.0065 99  MET   C CE  
1827 N N   . LEU   B 94  ? 0.1411 0.1847 0.1886 0.0039  -0.0032 -0.0152 100 LEU   C N   
1828 C CA  . LEU   B 94  ? 0.1477 0.1895 0.1948 0.0015  0.0037  -0.0125 100 LEU   C CA  
1829 C C   . LEU   B 94  ? 0.1453 0.1881 0.1881 0.0041  0.0043  -0.0129 100 LEU   C C   
1830 O O   . LEU   B 94  ? 0.1420 0.1891 0.1887 0.0073  0.0003  -0.0162 100 LEU   C O   
1831 C CB  . LEU   B 94  ? 0.1630 0.2086 0.2264 -0.0013 0.0082  -0.0142 100 LEU   C CB  
1832 C CG  . LEU   B 94  ? 0.1837 0.2276 0.2538 -0.0043 0.0083  -0.0138 100 LEU   C CG  
1833 C CD1 . LEU   B 94  ? 0.1996 0.2466 0.2876 -0.0076 0.0144  -0.0145 100 LEU   C CD1 
1834 C CD2 . LEU   B 94  ? 0.1971 0.2326 0.2534 -0.0060 0.0104  -0.0081 100 LEU   C CD2 
1835 N N   . ALA   B 95  ? 0.1539 0.1922 0.1888 0.0032  0.0095  -0.0098 101 ALA   C N   
1836 C CA  . ALA   B 95  ? 0.1548 0.1933 0.1863 0.0056  0.0110  -0.0106 101 ALA   C CA  
1837 C C   . ALA   B 95  ? 0.1523 0.1878 0.1817 0.0040  0.0193  -0.0089 101 ALA   C C   
1838 O O   . ALA   B 95  ? 0.1755 0.2064 0.2008 0.0015  0.0228  -0.0057 101 ALA   C O   
1839 C CB  . ALA   B 95  ? 0.1652 0.1983 0.1831 0.0073  0.0074  -0.0087 101 ALA   C CB  
1840 N N   . VAL   B 96  ? 0.1473 0.1846 0.1785 0.0061  0.0227  -0.0107 102 VAL   C N   
1841 C CA  . VAL   B 96  ? 0.1573 0.1907 0.1831 0.0058  0.0312  -0.0090 102 VAL   C CA  
1842 C C   . VAL   B 96  ? 0.2011 0.2251 0.2068 0.0073  0.0294  -0.0069 102 VAL   C C   
1843 O O   . VAL   B 96  ? 0.2236 0.2469 0.2252 0.0099  0.0251  -0.0087 102 VAL   C O   
1844 C CB  . VAL   B 96  ? 0.1663 0.2057 0.2034 0.0080  0.0357  -0.0126 102 VAL   C CB  
1845 C CG1 . VAL   B 96  ? 0.1826 0.2170 0.2119 0.0085  0.0460  -0.0107 102 VAL   C CG1 
1846 C CG2 . VAL   B 96  ? 0.1754 0.2245 0.2354 0.0064  0.0361  -0.0153 102 VAL   C CG2 
1847 N N   . GLY   B 97  ? 0.2261 0.2425 0.2202 0.0059  0.0322  -0.0032 103 GLY   C N   
1848 C CA  . GLY   B 97  ? 0.2616 0.2687 0.2374 0.0076  0.0289  -0.0019 103 GLY   C CA  
1849 C C   . GLY   B 97  ? 0.2818 0.2806 0.2457 0.0064  0.0310  0.0022  103 GLY   C C   
1850 O O   . GLY   B 97  ? 0.2803 0.2803 0.2505 0.0038  0.0350  0.0047  103 GLY   C O   
1851 N N   . HIS   B 98  ? 0.2790 0.2685 0.2255 0.0087  0.0286  0.0028  104 HIS   C N   
1852 C CA  . HIS   B 98  ? 0.2964 0.2762 0.2283 0.0088  0.0295  0.0067  104 HIS   C CA  
1853 C C   . HIS   B 98  ? 0.3060 0.2849 0.2397 0.0069  0.0215  0.0084  104 HIS   C C   
1854 O O   . HIS   B 98  ? 0.2877 0.2691 0.2254 0.0069  0.0138  0.0063  104 HIS   C O   
1855 C CB  . HIS   B 98  ? 0.3103 0.2796 0.2216 0.0130  0.0284  0.0055  104 HIS   C CB  
1856 C CG  . HIS   B 98  ? 0.3367 0.2944 0.2299 0.0144  0.0281  0.0093  104 HIS   C CG  
1857 N ND1 . HIS   B 98  ? 0.3562 0.3095 0.2433 0.0142  0.0380  0.0138  104 HIS   C ND1 
1858 C CD2 . HIS   B 98  ? 0.3614 0.3113 0.2434 0.0157  0.0186  0.0095  104 HIS   C CD2 
1859 C CE1 . HIS   B 98  ? 0.3745 0.3166 0.2443 0.0160  0.0340  0.0168  104 HIS   C CE1 
1860 N NE2 . HIS   B 98  ? 0.3889 0.3288 0.2553 0.0171  0.0219  0.0139  104 HIS   C NE2 
1861 N N   . SER   B 99  ? 0.3155 0.2900 0.2459 0.0054  0.0237  0.0125  105 SER   C N   
1862 C CA  . SER   B 99  ? 0.3421 0.3145 0.2734 0.0039  0.0171  0.0145  105 SER   C CA  
1863 C C   . SER   B 99  ? 0.3572 0.3186 0.2739 0.0047  0.0203  0.0194  105 SER   C C   
1864 O O   . SER   B 99  ? 0.3689 0.3278 0.2826 0.0047  0.0298  0.0220  105 SER   C O   
1865 C CB  . SER   B 99  ? 0.3751 0.3568 0.3254 0.0006  0.0176  0.0142  105 SER   C CB  
1866 O OG  . SER   B 99  ? 0.4838 0.4653 0.4375 -0.0005 0.0111  0.0152  105 SER   C OG  
1867 N N   . GLU   B 100 ? 0.3463 0.3010 0.2549 0.0057  0.0126  0.0209  106 GLU   C N   
1868 C CA  . GLU   B 100 ? 0.3583 0.3019 0.2535 0.0069  0.0132  0.0259  106 GLU   C CA  
1869 C C   . GLU   B 100 ? 0.3531 0.2983 0.2575 0.0051  0.0055  0.0267  106 GLU   C C   
1870 O O   . GLU   B 100 ? 0.3460 0.2990 0.2624 0.0041  -0.0003 0.0232  106 GLU   C O   
1871 C CB  . GLU   B 100 ? 0.3889 0.3204 0.2607 0.0117  0.0097  0.0259  106 GLU   C CB  
1872 C CG  . GLU   B 100 ? 0.4776 0.4053 0.3380 0.0139  0.0201  0.0266  106 GLU   C CG  
1873 C CD  . GLU   B 100 ? 0.5463 0.4615 0.3815 0.0197  0.0162  0.0254  106 GLU   C CD  
1874 O OE1 . GLU   B 100 ? 0.5941 0.4995 0.4160 0.0223  0.0081  0.0269  106 GLU   C OE1 
1875 O OE2 . GLU   B 100 ? 0.5574 0.4726 0.3866 0.0220  0.0203  0.0222  106 GLU   C OE2 
1876 N N   . PRO   B 101 ? 0.3560 0.2941 0.2562 0.0049  0.0057  0.0314  107 PRO   C N   
1877 C CA  . PRO   B 101 ? 0.3494 0.2909 0.2622 0.0032  -0.0010 0.0313  107 PRO   C CA  
1878 C C   . PRO   B 101 ? 0.3259 0.2688 0.2403 0.0048  -0.0120 0.0280  107 PRO   C C   
1879 O O   . PRO   B 101 ? 0.3235 0.2750 0.2540 0.0029  -0.0152 0.0257  107 PRO   C O   
1880 C CB  . PRO   B 101 ? 0.3774 0.3083 0.2816 0.0038  0.0005  0.0371  107 PRO   C CB  
1881 C CG  . PRO   B 101 ? 0.3922 0.3183 0.2877 0.0038  0.0123  0.0408  107 PRO   C CG  
1882 C CD  . PRO   B 101 ? 0.3745 0.3021 0.2613 0.0060  0.0135  0.0372  107 PRO   C CD  
1883 N N   . GLY   B 102 ? 0.3188 0.2531 0.2172 0.0085  -0.0173 0.0274  108 GLY   C N   
1884 C CA  . GLY   B 102 ? 0.3103 0.2454 0.2119 0.0100  -0.0281 0.0239  108 GLY   C CA  
1885 C C   . GLY   B 102 ? 0.2960 0.2416 0.2110 0.0083  -0.0283 0.0195  108 GLY   C C   
1886 O O   . GLY   B 102 ? 0.2988 0.2468 0.2216 0.0087  -0.0358 0.0168  108 GLY   C O   
1887 N N   . ASP   B 103 ? 0.2650 0.2169 0.1840 0.0066  -0.0200 0.0188  109 ASP   C N   
1888 C CA  . ASP   B 103 ? 0.2463 0.2075 0.1771 0.0054  -0.0198 0.0152  109 ASP   C CA  
1889 C C   . ASP   B 103 ? 0.2230 0.1935 0.1714 0.0030  -0.0200 0.0150  109 ASP   C C   
1890 O O   . ASP   B 103 ? 0.2157 0.1926 0.1730 0.0026  -0.0207 0.0128  109 ASP   C O   
1891 C CB  . ASP   B 103 ? 0.2539 0.2182 0.1826 0.0053  -0.0118 0.0141  109 ASP   C CB  
1892 C CG  . ASP   B 103 ? 0.2762 0.2323 0.1883 0.0085  -0.0120 0.0129  109 ASP   C CG  
1893 O OD1 . ASP   B 103 ? 0.2685 0.2194 0.1750 0.0106  -0.0200 0.0109  109 ASP   C OD1 
1894 O OD2 . ASP   B 103 ? 0.2921 0.2467 0.1974 0.0092  -0.0041 0.0135  109 ASP   C OD2 
1895 N N   . CYS   B 104 ? 0.2142 0.1847 0.1668 0.0017  -0.0189 0.0174  110 CYS   C N   
1896 C CA  . CYS   B 104 ? 0.2088 0.1872 0.1763 0.0002  -0.0190 0.0166  110 CYS   C CA  
1897 C C   . CYS   B 104 ? 0.2162 0.1968 0.1907 0.0009  -0.0249 0.0153  110 CYS   C C   
1898 O O   . CYS   B 104 ? 0.2297 0.2046 0.2002 0.0022  -0.0309 0.0157  110 CYS   C O   
1899 C CB  . CYS   B 104 ? 0.2287 0.2050 0.1990 -0.0008 -0.0180 0.0189  110 CYS   C CB  
1900 S SG  . CYS   B 104 ? 0.2785 0.2552 0.2490 -0.0029 -0.0094 0.0201  110 CYS   C SG  
1901 N N   . GLY   B 105 ? 0.1849 0.1732 0.1695 0.0005  -0.0231 0.0137  111 GLY   C N   
1902 C CA  . GLY   B 105 ? 0.1948 0.1857 0.1880 0.0011  -0.0267 0.0131  111 GLY   C CA  
1903 C C   . GLY   B 105 ? 0.2026 0.1948 0.1958 0.0015  -0.0267 0.0117  111 GLY   C C   
1904 O O   . GLY   B 105 ? 0.2009 0.1963 0.2033 0.0017  -0.0274 0.0117  111 GLY   C O   
1905 N N   . GLY   B 106 ? 0.1833 0.1727 0.1669 0.0019  -0.0253 0.0108  112 GLY   C N   
1906 C CA  . GLY   B 106 ? 0.1722 0.1625 0.1559 0.0026  -0.0252 0.0091  112 GLY   C CA  
1907 C C   . GLY   B 106 ? 0.1680 0.1654 0.1594 0.0026  -0.0210 0.0091  112 GLY   C C   
1908 O O   . GLY   B 106 ? 0.1798 0.1810 0.1716 0.0025  -0.0173 0.0091  112 GLY   C O   
1909 N N   . ILE   B 107 ? 0.1652 0.1637 0.1625 0.0032  -0.0219 0.0092  113 ILE   C N   
1910 C CA  . ILE   B 107 ? 0.1645 0.1681 0.1669 0.0041  -0.0180 0.0100  113 ILE   C CA  
1911 C C   . ILE   B 107 ? 0.1649 0.1698 0.1625 0.0053  -0.0155 0.0085  113 ILE   C C   
1912 O O   . ILE   B 107 ? 0.1730 0.1745 0.1666 0.0056  -0.0169 0.0071  113 ILE   C O   
1913 C CB  . ILE   B 107 ? 0.2084 0.2119 0.2205 0.0041  -0.0187 0.0118  113 ILE   C CB  
1914 C CG1 . ILE   B 107 ? 0.2325 0.2373 0.2524 0.0035  -0.0194 0.0132  113 ILE   C CG1 
1915 C CG2 . ILE   B 107 ? 0.2329 0.2389 0.2468 0.0059  -0.0144 0.0132  113 ILE   C CG2 
1916 C CD1 . ILE   B 107 ? 0.2596 0.2649 0.2924 0.0032  -0.0191 0.0152  113 ILE   C CD1 
1917 N N   . LEU   B 108 ? 0.1496 0.1591 0.1479 0.0066  -0.0125 0.0084  114 LEU   C N   
1918 C CA  . LEU   B 108 ? 0.1408 0.1524 0.1370 0.0085  -0.0109 0.0070  114 LEU   C CA  
1919 C C   . LEU   B 108 ? 0.1518 0.1640 0.1507 0.0107  -0.0098 0.0092  114 LEU   C C   
1920 O O   . LEU   B 108 ? 0.1583 0.1721 0.1591 0.0115  -0.0084 0.0106  114 LEU   C O   
1921 C CB  . LEU   B 108 ? 0.1339 0.1499 0.1299 0.0090  -0.0094 0.0050  114 LEU   C CB  
1922 C CG  . LEU   B 108 ? 0.1568 0.1759 0.1527 0.0117  -0.0088 0.0030  114 LEU   C CG  
1923 C CD1 . LEU   B 108 ? 0.1746 0.1922 0.1688 0.0118  -0.0083 0.0016  114 LEU   C CD1 
1924 C CD2 . LEU   B 108 ? 0.1562 0.1800 0.1550 0.0120  -0.0086 0.0002  114 LEU   C CD2 
1925 N N   . ARG   B 109 ? 0.1484 0.1584 0.1470 0.0120  -0.0098 0.0096  115 ARG   C N   
1926 C CA  . ARG   B 109 ? 0.1488 0.1578 0.1492 0.0143  -0.0079 0.0127  115 ARG   C CA  
1927 C C   . ARG   B 109 ? 0.1598 0.1691 0.1563 0.0175  -0.0078 0.0117  115 ARG   C C   
1928 O O   . ARG   B 109 ? 0.1880 0.1969 0.1835 0.0173  -0.0092 0.0091  115 ARG   C O   
1929 C CB  . ARG   B 109 ? 0.1790 0.1834 0.1855 0.0127  -0.0088 0.0146  115 ARG   C CB  
1930 C CG  . ARG   B 109 ? 0.2492 0.2528 0.2621 0.0099  -0.0102 0.0154  115 ARG   C CG  
1931 C CD  . ARG   B 109 ? 0.3133 0.3125 0.3348 0.0084  -0.0123 0.0163  115 ARG   C CD  
1932 N NE  . ARG   B 109 ? 0.3976 0.3964 0.4249 0.0097  -0.0076 0.0208  115 ARG   C NE  
1933 C CZ  . ARG   B 109 ? 0.4233 0.4233 0.4590 0.0091  -0.0045 0.0240  115 ARG   C CZ  
1934 N NH1 . ARG   B 109 ? 0.4473 0.4488 0.4890 0.0068  -0.0073 0.0227  115 ARG   C NH1 
1935 N NH2 . ARG   B 109 ? 0.4276 0.4269 0.4660 0.0110  0.0015  0.0288  115 ARG   C NH2 
1936 N N   . CYS   B 110 ? 0.1495 0.1586 0.1436 0.0208  -0.0059 0.0141  116 CYS   C N   
1937 C CA  . CYS   B 110 ? 0.1605 0.1686 0.1506 0.0248  -0.0064 0.0141  116 CYS   C CA  
1938 C C   . CYS   B 110 ? 0.2022 0.2048 0.1933 0.0263  -0.0037 0.0193  116 CYS   C C   
1939 O O   . CYS   B 110 ? 0.1902 0.1907 0.1870 0.0238  -0.0015 0.0223  116 CYS   C O   
1940 C CB  . CYS   B 110 ? 0.1535 0.1649 0.1379 0.0287  -0.0072 0.0124  116 CYS   C CB  
1941 S SG  . CYS   B 110 ? 0.1772 0.1867 0.1559 0.0318  -0.0038 0.0164  116 CYS   C SG  
1942 N N   . GLN   B 111 ? 0.2256 0.2255 0.2121 0.0307  -0.0038 0.0207  117 GLN   C N   
1943 C CA  . GLN   B 111 ? 0.2499 0.2434 0.2371 0.0323  -0.0004 0.0265  117 GLN   C CA  
1944 C C   . GLN   B 111 ? 0.2689 0.2608 0.2538 0.0336  0.0050  0.0318  117 GLN   C C   
1945 O O   . GLN   B 111 ? 0.2982 0.2850 0.2870 0.0336  0.0095  0.0374  117 GLN   C O   
1946 C CB  . GLN   B 111 ? 0.2730 0.2634 0.2539 0.0376  -0.0020 0.0271  117 GLN   C CB  
1947 C CG  . GLN   B 111 ? 0.3087 0.3004 0.2785 0.0433  -0.0028 0.0269  117 GLN   C CG  
1948 C CD  . GLN   B 111 ? 0.4442 0.4323 0.4078 0.0491  -0.0055 0.0274  117 GLN   C CD  
1949 O OE1 . GLN   B 111 ? 0.4970 0.4893 0.4608 0.0509  -0.0107 0.0220  117 GLN   C OE1 
1950 N NE2 . GLN   B 111 ? 0.4534 0.4334 0.4126 0.0524  -0.0019 0.0341  117 GLN   C NE2 
1951 N N   . HIS   B 112 ? 0.2424 0.2385 0.2223 0.0346  0.0051  0.0298  118 HIS   C N   
1952 C CA  . HIS   B 112 ? 0.2329 0.2275 0.2092 0.0367  0.0108  0.0341  118 HIS   C CA  
1953 C C   . HIS   B 112 ? 0.2398 0.2372 0.2265 0.0318  0.0130  0.0343  118 HIS   C C   
1954 O O   . HIS   B 112 ? 0.2697 0.2659 0.2564 0.0332  0.0188  0.0382  118 HIS   C O   
1955 C CB  . HIS   B 112 ? 0.2338 0.2300 0.1971 0.0421  0.0092  0.0315  118 HIS   C CB  
1956 C CG  . HIS   B 112 ? 0.2389 0.2323 0.1922 0.0477  0.0057  0.0309  118 HIS   C CG  
1957 N ND1 . HIS   B 112 ? 0.2500 0.2478 0.2021 0.0487  -0.0013 0.0243  118 HIS   C ND1 
1958 C CD2 . HIS   B 112 ? 0.2729 0.2591 0.2171 0.0532  0.0085  0.0362  118 HIS   C CD2 
1959 C CE1 . HIS   B 112 ? 0.2845 0.2785 0.2286 0.0543  -0.0036 0.0253  118 HIS   C CE1 
1960 N NE2 . HIS   B 112 ? 0.2944 0.2808 0.2319 0.0576  0.0019  0.0325  118 HIS   C NE2 
1961 N N   . GLY   B 113 ? 0.2086 0.2093 0.2032 0.0269  0.0085  0.0302  119 GLY   C N   
1962 C CA  . GLY   B 113 ? 0.1950 0.1980 0.1990 0.0228  0.0090  0.0299  119 GLY   C CA  
1963 C C   . GLY   B 113 ? 0.1803 0.1877 0.1838 0.0204  0.0041  0.0245  119 GLY   C C   
1964 O O   . GLY   B 113 ? 0.1803 0.1887 0.1794 0.0204  0.0004  0.0208  119 GLY   C O   
1965 N N   . VAL   B 114 ? 0.1700 0.1794 0.1786 0.0184  0.0046  0.0242  120 VAL   C N   
1966 C CA  . VAL   B 114 ? 0.1610 0.1732 0.1693 0.0160  0.0005  0.0200  120 VAL   C CA  
1967 C C   . VAL   B 114 ? 0.1551 0.1700 0.1552 0.0186  -0.0001 0.0170  120 VAL   C C   
1968 O O   . VAL   B 114 ? 0.1757 0.1910 0.1719 0.0220  0.0028  0.0178  120 VAL   C O   
1969 C CB  . VAL   B 114 ? 0.1842 0.1973 0.2013 0.0136  0.0007  0.0208  120 VAL   C CB  
1970 C CG1 . VAL   B 114 ? 0.1965 0.2113 0.2119 0.0118  -0.0030 0.0172  120 VAL   C CG1 
1971 C CG2 . VAL   B 114 ? 0.1906 0.2012 0.2183 0.0107  -0.0008 0.0224  120 VAL   C CG2 
1972 N N   . VAL   B 115 ? 0.1451 0.1616 0.1431 0.0174  -0.0036 0.0133  121 VAL   C N   
1973 C CA  . VAL   B 115 ? 0.1379 0.1573 0.1317 0.0192  -0.0051 0.0096  121 VAL   C CA  
1974 C C   . VAL   B 115 ? 0.1482 0.1692 0.1453 0.0167  -0.0062 0.0075  121 VAL   C C   
1975 O O   . VAL   B 115 ? 0.1512 0.1739 0.1468 0.0186  -0.0068 0.0050  121 VAL   C O   
1976 C CB  . VAL   B 115 ? 0.1549 0.1756 0.1475 0.0193  -0.0074 0.0068  121 VAL   C CB  
1977 C CG1 . VAL   B 115 ? 0.1633 0.1876 0.1559 0.0203  -0.0096 0.0023  121 VAL   C CG1 
1978 C CG2 . VAL   B 115 ? 0.1617 0.1803 0.1506 0.0226  -0.0069 0.0086  121 VAL   C CG2 
1979 N N   . GLY   B 116 ? 0.1380 0.1578 0.1387 0.0128  -0.0073 0.0079  122 GLY   C N   
1980 C CA  . GLY   B 116 ? 0.1469 0.1669 0.1502 0.0105  -0.0084 0.0068  122 GLY   C CA  
1981 C C   . GLY   B 116 ? 0.1394 0.1563 0.1435 0.0073  -0.0100 0.0078  122 GLY   C C   
1982 O O   . GLY   B 116 ? 0.1436 0.1582 0.1477 0.0069  -0.0107 0.0093  122 GLY   C O   
1983 N N   . ILE   B 117 ? 0.1510 0.1668 0.1558 0.0054  -0.0109 0.0073  123 ILE   C N   
1984 C CA  . ILE   B 117 ? 0.1575 0.1688 0.1601 0.0032  -0.0127 0.0085  123 ILE   C CA  
1985 C C   . ILE   B 117 ? 0.1474 0.1574 0.1467 0.0017  -0.0115 0.0077  123 ILE   C C   
1986 O O   . ILE   B 117 ? 0.1448 0.1574 0.1473 0.0015  -0.0100 0.0063  123 ILE   C O   
1987 C CB  . ILE   B 117 ? 0.1806 0.1897 0.1872 0.0026  -0.0149 0.0101  123 ILE   C CB  
1988 C CG1 . ILE   B 117 ? 0.1781 0.1893 0.1884 0.0030  -0.0139 0.0093  123 ILE   C CG1 
1989 C CG2 . ILE   B 117 ? 0.2054 0.2149 0.2176 0.0034  -0.0159 0.0116  123 ILE   C CG2 
1990 C CD1 . ILE   B 117 ? 0.1922 0.2006 0.2071 0.0025  -0.0166 0.0109  123 ILE   C CD1 
1991 N N   . VAL   B 118 ? 0.1434 0.1487 0.1364 0.0009  -0.0119 0.0086  124 VAL   C N   
1992 C CA  . VAL   B 118 ? 0.1503 0.1532 0.1393 -0.0003 -0.0091 0.0089  124 VAL   C CA  
1993 C C   . VAL   B 118 ? 0.1502 0.1511 0.1418 -0.0016 -0.0092 0.0103  124 VAL   C C   
1994 O O   . VAL   B 118 ? 0.1685 0.1664 0.1600 -0.0014 -0.0127 0.0118  124 VAL   C O   
1995 C CB  . VAL   B 118 ? 0.1597 0.1558 0.1382 0.0001  -0.0096 0.0101  124 VAL   C CB  
1996 C CG1 . VAL   B 118 ? 0.1904 0.1826 0.1634 -0.0008 -0.0050 0.0116  124 VAL   C CG1 
1997 C CG2 . VAL   B 118 ? 0.1687 0.1661 0.1452 0.0015  -0.0094 0.0081  124 VAL   C CG2 
1998 N N   . SER   B 119 ? 0.1558 0.1587 0.1518 -0.0029 -0.0058 0.0096  125 SER   C N   
1999 C CA  . SER   B 119 ? 0.1633 0.1640 0.1633 -0.0042 -0.0057 0.0107  125 SER   C CA  
2000 C C   . SER   B 119 ? 0.1821 0.1792 0.1812 -0.0062 -0.0008 0.0126  125 SER   C C   
2001 O O   . SER   B 119 ? 0.1896 0.1809 0.1875 -0.0071 -0.0004 0.0155  125 SER   C O   
2002 C CB  . SER   B 119 ? 0.1535 0.1603 0.1632 -0.0036 -0.0068 0.0074  125 SER   C CB  
2003 O OG  . SER   B 119 ? 0.1672 0.1716 0.1822 -0.0049 -0.0069 0.0078  125 SER   C OG  
2004 N N   . THR   B 120 ? 0.1872 0.1872 0.1877 -0.0066 0.0036  0.0114  126 THR   C N   
2005 C CA  . THR   B 120 ? 0.2073 0.2043 0.2090 -0.0085 0.0102  0.0136  126 THR   C CA  
2006 C C   . THR   B 120 ? 0.2193 0.2152 0.2135 -0.0076 0.0148  0.0142  126 THR   C C   
2007 O O   . THR   B 120 ? 0.2017 0.2009 0.1932 -0.0058 0.0126  0.0117  126 THR   C O   
2008 C CB  . THR   B 120 ? 0.2115 0.2150 0.2301 -0.0105 0.0122  0.0105  126 THR   C CB  
2009 O OG1 . THR   B 120 ? 0.2195 0.2309 0.2444 -0.0094 0.0120  0.0062  126 THR   C OG1 
2010 C CG2 . THR   B 120 ? 0.2231 0.2281 0.2491 -0.0106 0.0072  0.0084  126 THR   C CG2 
2011 N N   . GLY   B 121 ? 0.2404 0.2314 0.2316 -0.0087 0.0220  0.0175  127 GLY   C N   
2012 C CA  . GLY   B 121 ? 0.2815 0.2714 0.2661 -0.0074 0.0281  0.0179  127 GLY   C CA  
2013 C C   . GLY   B 121 ? 0.3063 0.2927 0.2932 -0.0091 0.0382  0.0215  127 GLY   C C   
2014 O O   . GLY   B 121 ? 0.3039 0.2858 0.2935 -0.0111 0.0400  0.0250  127 GLY   C O   
2015 N N   . GLY   B 122 ? 0.3346 0.3219 0.3197 -0.0081 0.0454  0.0212  128 GLY   C N   
2016 C CA  . GLY   B 122 ? 0.3439 0.3277 0.3312 -0.0094 0.0573  0.0253  128 GLY   C CA  
2017 C C   . GLY   B 122 ? 0.3398 0.3326 0.3416 -0.0097 0.0638  0.0218  128 GLY   C C   
2018 O O   . GLY   B 122 ? 0.3319 0.3349 0.3480 -0.0100 0.0582  0.0162  128 GLY   C O   
2019 N N   . ASN   B 123 ? 0.3499 0.3386 0.3471 -0.0089 0.0757  0.0252  129 ASN   C N   
2020 C CA  . ASN   B 123 ? 0.3504 0.3480 0.3637 -0.0090 0.0832  0.0220  129 ASN   C CA  
2021 C C   . ASN   B 123 ? 0.3310 0.3353 0.3436 -0.0060 0.0770  0.0158  129 ASN   C C   
2022 O O   . ASN   B 123 ? 0.3301 0.3450 0.3624 -0.0064 0.0783  0.0113  129 ASN   C O   
2023 C CB  . ASN   B 123 ? 0.3669 0.3741 0.4101 -0.0134 0.0843  0.0199  129 ASN   C CB  
2024 C CG  . ASN   B 123 ? 0.4335 0.4346 0.4823 -0.0168 0.0927  0.0261  129 ASN   C CG  
2025 O OD1 . ASN   B 123 ? 0.4508 0.4420 0.4854 -0.0159 0.1034  0.0326  129 ASN   C OD1 
2026 N ND2 . ASN   B 123 ? 0.4536 0.4599 0.5233 -0.0206 0.0882  0.0241  129 ASN   C ND2 
2027 N N   . GLY   B 124 ? 0.3026 0.3006 0.2941 -0.0028 0.0700  0.0155  130 GLY   C N   
2028 C CA  . GLY   B 124 ? 0.2772 0.2800 0.2674 0.0000  0.0640  0.0102  130 GLY   C CA  
2029 C C   . GLY   B 124 ? 0.2440 0.2560 0.2486 -0.0011 0.0537  0.0058  130 GLY   C C   
2030 O O   . GLY   B 124 ? 0.2462 0.2637 0.2551 0.0010  0.0502  0.0016  130 GLY   C O   
2031 N N   . LEU   B 125 ? 0.2251 0.2379 0.2361 -0.0038 0.0491  0.0068  131 LEU   C N   
2032 C CA  . LEU   B 125 ? 0.2183 0.2381 0.2393 -0.0041 0.0396  0.0030  131 LEU   C CA  
2033 C C   . LEU   B 125 ? 0.2534 0.2668 0.2611 -0.0039 0.0324  0.0052  131 LEU   C C   
2034 O O   . LEU   B 125 ? 0.3032 0.3091 0.3027 -0.0051 0.0343  0.0094  131 LEU   C O   
2035 C CB  . LEU   B 125 ? 0.2189 0.2456 0.2612 -0.0070 0.0402  0.0012  131 LEU   C CB  
2036 C CG  . LEU   B 125 ? 0.2378 0.2721 0.2982 -0.0073 0.0467  -0.0016 131 LEU   C CG  
2037 C CD1 . LEU   B 125 ? 0.2550 0.2935 0.3365 -0.0111 0.0492  -0.0021 131 LEU   C CD1 
2038 C CD2 . LEU   B 125 ? 0.2322 0.2746 0.2997 -0.0043 0.0403  -0.0074 131 LEU   C CD2 
2039 N N   . VAL   B 126 ? 0.2018 0.2179 0.2082 -0.0023 0.0246  0.0027  132 VAL   C N   
2040 C CA  . VAL   B 126 ? 0.1893 0.2011 0.1875 -0.0022 0.0181  0.0043  132 VAL   C CA  
2041 C C   . VAL   B 126 ? 0.1772 0.1955 0.1867 -0.0025 0.0129  0.0016  132 VAL   C C   
2042 O O   . VAL   B 126 ? 0.1679 0.1928 0.1854 -0.0010 0.0112  -0.0020 132 VAL   C O   
2043 C CB  . VAL   B 126 ? 0.2097 0.2175 0.1956 0.0004  0.0141  0.0041  132 VAL   C CB  
2044 C CG1 . VAL   B 126 ? 0.2295 0.2429 0.2202 0.0025  0.0129  0.0006  132 VAL   C CG1 
2045 C CG2 . VAL   B 126 ? 0.2178 0.2224 0.1993 0.0003  0.0074  0.0055  132 VAL   C CG2 
2046 N N   . GLY   B 127 ? 0.1649 0.1806 0.1741 -0.0038 0.0102  0.0033  133 GLY   C N   
2047 C CA  . GLY   B 127 ? 0.1668 0.1874 0.1843 -0.0033 0.0055  0.0006  133 GLY   C CA  
2048 C C   . GLY   B 127 ? 0.1591 0.1774 0.1696 -0.0019 0.0006  0.0016  133 GLY   C C   
2049 O O   . GLY   B 127 ? 0.1716 0.1841 0.1751 -0.0025 0.0000  0.0048  133 GLY   C O   
2050 N N   . PHE   B 128 ? 0.1405 0.1633 0.1541 0.0004  -0.0028 -0.0009 134 PHE   C N   
2051 C CA  . PHE   B 128 ? 0.1536 0.1751 0.1627 0.0021  -0.0059 0.0002  134 PHE   C CA  
2052 C C   . PHE   B 128 ? 0.1578 0.1816 0.1714 0.0033  -0.0081 -0.0018 134 PHE   C C   
2053 O O   . PHE   B 128 ? 0.1561 0.1840 0.1743 0.0048  -0.0092 -0.0055 134 PHE   C O   
2054 C CB  . PHE   B 128 ? 0.1557 0.1789 0.1617 0.0047  -0.0069 -0.0003 134 PHE   C CB  
2055 C CG  . PHE   B 128 ? 0.1670 0.1881 0.1690 0.0043  -0.0051 0.0004  134 PHE   C CG  
2056 C CD1 . PHE   B 128 ? 0.1731 0.1890 0.1688 0.0038  -0.0058 0.0028  134 PHE   C CD1 
2057 C CD2 . PHE   B 128 ? 0.1762 0.2007 0.1814 0.0051  -0.0032 -0.0020 134 PHE   C CD2 
2058 C CE1 . PHE   B 128 ? 0.1827 0.1959 0.1733 0.0041  -0.0046 0.0026  134 PHE   C CE1 
2059 C CE2 . PHE   B 128 ? 0.1884 0.2108 0.1896 0.0053  -0.0011 -0.0018 134 PHE   C CE2 
2060 C CZ  . PHE   B 128 ? 0.1849 0.2012 0.1778 0.0049  -0.0018 0.0004  134 PHE   C CZ  
2061 N N   . ALA   B 129 ? 0.1449 0.1659 0.1570 0.0031  -0.0091 0.0001  135 ALA   C N   
2062 C CA  . ALA   B 129 ? 0.1353 0.1578 0.1501 0.0050  -0.0107 -0.0018 135 ALA   C CA  
2063 C C   . ALA   B 129 ? 0.1410 0.1651 0.1515 0.0087  -0.0110 -0.0019 135 ALA   C C   
2064 O O   . ALA   B 129 ? 0.1407 0.1631 0.1486 0.0089  -0.0102 0.0013  135 ALA   C O   
2065 C CB  . ALA   B 129 ? 0.1332 0.1520 0.1488 0.0038  -0.0111 0.0005  135 ALA   C CB  
2066 N N   . ASP   B 130 ? 0.1421 0.1690 0.1522 0.0119  -0.0124 -0.0055 136 ASP   C N   
2067 C CA  . ASP   B 130 ? 0.1554 0.1826 0.1591 0.0163  -0.0121 -0.0050 136 ASP   C CA  
2068 C C   . ASP   B 130 ? 0.1619 0.1873 0.1634 0.0183  -0.0103 -0.0032 136 ASP   C C   
2069 O O   . ASP   B 130 ? 0.1540 0.1790 0.1585 0.0180  -0.0109 -0.0049 136 ASP   C O   
2070 C CB  . ASP   B 130 ? 0.1705 0.2000 0.1728 0.0201  -0.0153 -0.0099 136 ASP   C CB  
2071 C CG  . ASP   B 130 ? 0.2138 0.2423 0.2068 0.0256  -0.0152 -0.0091 136 ASP   C CG  
2072 O OD1 . ASP   B 130 ? 0.2160 0.2435 0.2065 0.0255  -0.0132 -0.0055 136 ASP   C OD1 
2073 O OD2 . ASP   B 130 ? 0.2526 0.2804 0.2401 0.0303  -0.0170 -0.0119 136 ASP   C OD2 
2074 N N   . VAL   B 131 ? 0.1520 0.1761 0.1495 0.0203  -0.0075 0.0005  137 VAL   C N   
2075 C CA  . VAL   B 131 ? 0.1538 0.1766 0.1501 0.0228  -0.0043 0.0024  137 VAL   C CA  
2076 C C   . VAL   B 131 ? 0.1693 0.1908 0.1563 0.0286  -0.0018 0.0032  137 VAL   C C   
2077 O O   . VAL   B 131 ? 0.1904 0.2105 0.1751 0.0315  0.0025  0.0053  137 VAL   C O   
2078 C CB  . VAL   B 131 ? 0.1657 0.1875 0.1688 0.0198  -0.0018 0.0069  137 VAL   C CB  
2079 C CG1 . VAL   B 131 ? 0.1665 0.1880 0.1763 0.0153  -0.0048 0.0064  137 VAL   C CG1 
2080 C CG2 . VAL   B 131 ? 0.1758 0.1965 0.1786 0.0192  -0.0005 0.0104  137 VAL   C CG2 
2081 N N   . ARG   B 132 ? 0.1663 0.1879 0.1474 0.0308  -0.0041 0.0020  138 ARG   C N   
2082 C CA  . ARG   B 132 ? 0.1589 0.1777 0.1293 0.0367  -0.0020 0.0038  138 ARG   C CA  
2083 C C   . ARG   B 132 ? 0.1929 0.2100 0.1537 0.0428  -0.0019 0.0009  138 ARG   C C   
2084 O O   . ARG   B 132 ? 0.2162 0.2294 0.1663 0.0483  0.0021  0.0039  138 ARG   C O   
2085 C CB  . ARG   B 132 ? 0.1529 0.1720 0.1199 0.0381  -0.0058 0.0025  138 ARG   C CB  
2086 C CG  . ARG   B 132 ? 0.1583 0.1779 0.1323 0.0334  -0.0049 0.0057  138 ARG   C CG  
2087 C CD  . ARG   B 132 ? 0.1631 0.1835 0.1350 0.0351  -0.0088 0.0035  138 ARG   C CD  
2088 N NE  . ARG   B 132 ? 0.1706 0.1952 0.1482 0.0333  -0.0134 -0.0024 138 ARG   C NE  
2089 C CZ  . ARG   B 132 ? 0.1759 0.2029 0.1563 0.0338  -0.0169 -0.0054 138 ARG   C CZ  
2090 N NH1 . ARG   B 132 ? 0.1707 0.1959 0.1467 0.0370  -0.0174 -0.0038 138 ARG   C NH1 
2091 N NH2 . ARG   B 132 ? 0.1923 0.2235 0.1811 0.0313  -0.0198 -0.0102 138 ARG   C NH2 
2092 N N   . ASP   B 133 ? 0.1871 0.2060 0.1509 0.0423  -0.0061 -0.0049 139 ASP   C N   
2093 C CA  . ASP   B 133 ? 0.1998 0.2163 0.1539 0.0486  -0.0070 -0.0089 139 ASP   C CA  
2094 C C   . ASP   B 133 ? 0.2131 0.2281 0.1678 0.0494  -0.0008 -0.0066 139 ASP   C C   
2095 O O   . ASP   B 133 ? 0.2298 0.2418 0.1742 0.0556  0.0000  -0.0095 139 ASP   C O   
2096 C CB  . ASP   B 133 ? 0.2153 0.2339 0.1742 0.0480  -0.0147 -0.0169 139 ASP   C CB  
2097 C CG  . ASP   B 133 ? 0.2456 0.2669 0.2190 0.0412  -0.0148 -0.0176 139 ASP   C CG  
2098 O OD1 . ASP   B 133 ? 0.2328 0.2556 0.2140 0.0355  -0.0124 -0.0130 139 ASP   C OD1 
2099 O OD2 . ASP   B 133 ? 0.2487 0.2696 0.2248 0.0420  -0.0178 -0.0229 139 ASP   C OD2 
2100 N N   . LEU   B 134 ? 0.2073 0.2241 0.1734 0.0439  0.0033  -0.0021 140 LEU   C N   
2101 C CA  . LEU   B 134 ? 0.2231 0.2394 0.1935 0.0443  0.0089  -0.0002 140 LEU   C CA  
2102 C C   . LEU   B 134 ? 0.2290 0.2427 0.1935 0.0482  0.0174  0.0058  140 LEU   C C   
2103 O O   . LEU   B 134 ? 0.2189 0.2336 0.1931 0.0447  0.0220  0.0114  140 LEU   C O   
2104 C CB  . LEU   B 134 ? 0.2163 0.2355 0.2027 0.0370  0.0079  0.0015  140 LEU   C CB  
2105 C CG  . LEU   B 134 ? 0.2315 0.2521 0.2234 0.0330  0.0009  -0.0030 140 LEU   C CG  
2106 C CD1 . LEU   B 134 ? 0.2323 0.2539 0.2361 0.0268  0.0001  -0.0003 140 LEU   C CD1 
2107 C CD2 . LEU   B 134 ? 0.2363 0.2560 0.2261 0.0360  -0.0016 -0.0090 140 LEU   C CD2 
2108 N N   . LEU   B 135 ? 0.2404 0.2501 0.1886 0.0560  0.0196  0.0047  141 LEU   C N   
2109 C CA  . LEU   B 135 ? 0.2585 0.2642 0.1983 0.0605  0.0288  0.0113  141 LEU   C CA  
2110 C C   . LEU   B 135 ? 0.2727 0.2791 0.2220 0.0599  0.0383  0.0158  141 LEU   C C   
2111 O O   . LEU   B 135 ? 0.2834 0.2884 0.2356 0.0599  0.0465  0.0229  141 LEU   C O   
2112 C CB  . LEU   B 135 ? 0.2514 0.2512 0.1684 0.0700  0.0289  0.0094  141 LEU   C CB  
2113 C CG  . LEU   B 135 ? 0.2610 0.2601 0.1692 0.0719  0.0183  0.0037  141 LEU   C CG  
2114 C CD1 . LEU   B 135 ? 0.2969 0.2886 0.1809 0.0826  0.0185  0.0025  141 LEU   C CD1 
2115 C CD2 . LEU   B 135 ? 0.2607 0.2620 0.1765 0.0667  0.0154  0.0070  141 LEU   C CD2 
2116 N N   . TRP   B 136 ? 0.2582 0.2671 0.2148 0.0591  0.0373  0.0115  142 TRP   C N   
2117 C CA  . TRP   B 136 ? 0.2701 0.2804 0.2379 0.0590  0.0458  0.0146  142 TRP   C CA  
2118 C C   . TRP   B 136 ? 0.2642 0.2787 0.2534 0.0513  0.0468  0.0196  142 TRP   C C   
2119 O O   . TRP   B 136 ? 0.2710 0.2870 0.2723 0.0511  0.0545  0.0232  142 TRP   C O   
2120 C CB  . TRP   B 136 ? 0.2627 0.2742 0.2333 0.0602  0.0429  0.0082  142 TRP   C CB  
2121 C CG  . TRP   B 136 ? 0.2574 0.2717 0.2366 0.0543  0.0320  0.0031  142 TRP   C CG  
2122 C CD1 . TRP   B 136 ? 0.2667 0.2799 0.2377 0.0550  0.0234  -0.0032 142 TRP   C CD1 
2123 C CD2 . TRP   B 136 ? 0.2477 0.2658 0.2457 0.0471  0.0288  0.0043  142 TRP   C CD2 
2124 N NE1 . TRP   B 136 ? 0.2591 0.2751 0.2430 0.0483  0.0165  -0.0052 142 TRP   C NE1 
2125 C CE2 . TRP   B 136 ? 0.2519 0.2703 0.2505 0.0438  0.0195  -0.0007 142 TRP   C CE2 
2126 C CE3 . TRP   B 136 ? 0.2568 0.2777 0.2715 0.0434  0.0326  0.0088  142 TRP   C CE3 
2127 C CZ2 . TRP   B 136 ? 0.2659 0.2862 0.2782 0.0375  0.0147  -0.0005 142 TRP   C CZ2 
2128 C CZ3 . TRP   B 136 ? 0.2688 0.2918 0.2973 0.0376  0.0263  0.0080  142 TRP   C CZ3 
2129 C CH2 . TRP   B 136 ? 0.2677 0.2899 0.2934 0.0349  0.0178  0.0038  142 TRP   C CH2 
2130 N N   . LEU   B 137 ? 0.2601 0.2761 0.2545 0.0455  0.0392  0.0194  143 LEU   C N   
2131 C CA  . LEU   B 137 ? 0.2593 0.2781 0.2721 0.0390  0.0388  0.0232  143 LEU   C CA  
2132 C C   . LEU   B 137 ? 0.3107 0.3283 0.3287 0.0399  0.0482  0.0303  143 LEU   C C   
2133 O O   . LEU   B 137 ? 0.3125 0.3327 0.3494 0.0358  0.0499  0.0330  143 LEU   C O   
2134 C CB  . LEU   B 137 ? 0.2398 0.2592 0.2532 0.0339  0.0298  0.0216  143 LEU   C CB  
2135 C CG  . LEU   B 137 ? 0.2336 0.2546 0.2487 0.0308  0.0214  0.0162  143 LEU   C CG  
2136 C CD1 . LEU   B 137 ? 0.2217 0.2426 0.2351 0.0270  0.0149  0.0153  143 LEU   C CD1 
2137 C CD2 . LEU   B 137 ? 0.2210 0.2442 0.2519 0.0275  0.0202  0.0161  143 LEU   C CD2 
2138 N N   . ASP   B 138 ? 0.3497 0.3628 0.3517 0.0451  0.0534  0.0331  144 ASP   C N   
2139 C CA  . ASP   B 138 ? 0.4093 0.4191 0.4117 0.0471  0.0634  0.0407  144 ASP   C CA  
2140 C C   . ASP   B 138 ? 0.4585 0.4671 0.4621 0.0518  0.0761  0.0446  144 ASP   C C   
2141 O O   . ASP   B 138 ? 0.4775 0.4827 0.4816 0.0537  0.0860  0.0517  144 ASP   C O   
2142 C CB  . ASP   B 138 ? 0.4595 0.4634 0.4395 0.0524  0.0632  0.0418  144 ASP   C CB  
2143 C CG  . ASP   B 138 ? 0.5249 0.5287 0.5031 0.0489  0.0538  0.0401  144 ASP   C CG  
2144 O OD1 . ASP   B 138 ? 0.5254 0.5324 0.5198 0.0422  0.0498  0.0402  144 ASP   C OD1 
2145 O OD2 . ASP   B 138 ? 0.5895 0.5898 0.5497 0.0535  0.0504  0.0383  144 ASP   C OD2 
2146 N N   . GLU   B 139 ? 0.4750 0.4854 0.4769 0.0547  0.0767  0.0402  145 GLU   C N   
2147 C CA  . GLU   B 139 ? 0.5140 0.5233 0.5163 0.0600  0.0896  0.0433  145 GLU   C CA  
2148 C C   . GLU   B 139 ? 0.5325 0.5480 0.5558 0.0569  0.0893  0.0403  145 GLU   C C   
2149 O O   . GLU   B 139 ? 0.5489 0.5653 0.5799 0.0600  0.1004  0.0429  145 GLU   C O   
2150 C CB  . GLU   B 139 ? 0.5686 0.5718 0.5424 0.0694  0.0922  0.0405  145 GLU   C CB  
2151 C CG  . GLU   B 139 ? 0.6573 0.6615 0.6219 0.0701  0.0800  0.0310  145 GLU   C CG  
2152 C CD  . GLU   B 139 ? 0.7910 0.7883 0.7266 0.0791  0.0786  0.0272  145 GLU   C CD  
2153 O OE1 . GLU   B 139 ? 0.8085 0.8054 0.7370 0.0829  0.0749  0.0200  145 GLU   C OE1 
2154 O OE2 . GLU   B 139 ? 0.8329 0.8248 0.7528 0.0828  0.0805  0.0311  145 GLU   C OE2 
2155 N N1  . A1BQG C .   ? 0.2751 0.2713 0.3317 0.0043  0.0341  -0.0303 201 A1BQG A N1  
2156 N N3  . A1BQG C .   ? 0.4591 0.4573 0.4623 -0.0032 0.0229  -0.0269 201 A1BQG A N3  
2157 C C4  . A1BQG C .   ? 0.2709 0.2583 0.3170 0.0017  0.0345  -0.0381 201 A1BQG A C4  
2158 C C5  . A1BQG C .   ? 0.3127 0.3110 0.3615 0.0033  0.0354  -0.0292 201 A1BQG A C5  
2159 C C6  . A1BQG C .   ? 0.3764 0.3677 0.4012 -0.0008 0.0349  -0.0351 201 A1BQG A C6  
2160 C C7  . A1BQG C .   ? 0.4254 0.4174 0.4431 -0.0022 0.0392  -0.0345 201 A1BQG A C7  
2161 C C8  . A1BQG C .   ? 0.4438 0.4313 0.4646 -0.0027 0.0510  -0.0391 201 A1BQG A C8  
2162 C C10 . A1BQG C .   ? 0.4636 0.4534 0.4628 -0.0064 0.0478  -0.0351 201 A1BQG A C10 
2163 O O1  . A1BQG C .   ? 0.2910 0.2963 0.3506 0.0050  0.0355  -0.0230 201 A1BQG A O1  
2164 C C3  . A1BQG C .   ? 0.2681 0.2577 0.3117 0.0013  0.0248  -0.0357 201 A1BQG A C3  
2165 C C2  . A1BQG C .   ? 0.2532 0.2497 0.3153 0.0047  0.0223  -0.0280 201 A1BQG A C2  
2166 C C12 . A1BQG C .   ? 0.2481 0.2512 0.3233 0.0073  0.0306  -0.0225 201 A1BQG A C12 
2167 C C1  . A1BQG C .   ? 0.2404 0.2448 0.3088 0.0064  0.0217  -0.0205 201 A1BQG A C1  
2168 C C   . A1BQG C .   ? 0.2310 0.2415 0.3133 0.0080  0.0175  -0.0121 201 A1BQG A C   
2169 O O   . A1BQG C .   ? 0.2491 0.2639 0.3259 0.0068  0.0114  -0.0073 201 A1BQG A O   
2170 N N   . A1BQG C .   ? 0.2027 0.2127 0.3026 0.0101  0.0211  -0.0102 201 A1BQG A N   
2171 C C11 . A1BQG C .   ? 0.4529 0.4480 0.4589 -0.0035 0.0325  -0.0305 201 A1BQG A C11 
2172 N N2  . A1BQG C .   ? 0.4660 0.4600 0.4635 -0.0055 0.0366  -0.0306 201 A1BQG A N2  
2173 C C9  . A1BQG C .   ? 0.4572 0.4435 0.4682 -0.0050 0.0557  -0.0396 201 A1BQG A C9  
2179 N N1  . A1BQG F .   ? 0.2686 0.2350 0.2535 -0.0108 0.0135  0.0298  201 A1BQG C N1  
2180 N N3  . A1BQG F .   ? 0.4745 0.4457 0.4310 -0.0041 0.0108  0.0235  201 A1BQG C N3  
2181 C C4  . A1BQG F .   ? 0.2769 0.2329 0.2517 -0.0093 0.0098  0.0343  201 A1BQG C C4  
2182 C C5  . A1BQG F .   ? 0.3144 0.2824 0.2931 -0.0100 0.0176  0.0292  201 A1BQG C C5  
2183 C C6  . A1BQG F .   ? 0.3770 0.3355 0.3346 -0.0069 0.0169  0.0326  201 A1BQG C C6  
2184 C C7  . A1BQG F .   ? 0.4343 0.3937 0.3849 -0.0058 0.0226  0.0317  201 A1BQG C C7  
2185 C C8  . A1BQG F .   ? 0.4511 0.4042 0.3947 -0.0058 0.0324  0.0359  201 A1BQG C C8  
2186 C C10 . A1BQG F .   ? 0.4706 0.4295 0.4056 -0.0024 0.0327  0.0299  201 A1BQG C C10 
2187 O O1  . A1BQG F .   ? 0.2838 0.2602 0.2730 -0.0113 0.0208  0.0257  201 A1BQG C O1  
2188 C C3  . A1BQG F .   ? 0.2602 0.2197 0.2391 -0.0079 0.0008  0.0313  201 A1BQG C C3  
2189 C C2  . A1BQG F .   ? 0.2401 0.2086 0.2367 -0.0096 0.0000  0.0266  201 A1BQG C C2  
2190 C C12 . A1BQG F .   ? 0.2375 0.2125 0.2404 -0.0126 0.0116  0.0252  201 A1BQG C C12 
2191 C C1  . A1BQG F .   ? 0.2339 0.2118 0.2376 -0.0107 0.0034  0.0224  201 A1BQG C C1  
2192 C C   . A1BQG F .   ? 0.2217 0.2073 0.2408 -0.0115 0.0016  0.0173  201 A1BQG C C   
2193 O O   . A1BQG F .   ? 0.2000 0.1842 0.2289 -0.0134 0.0032  0.0171  201 A1BQG C O   
2194 N N   . A1BQG F .   ? 0.2122 0.2051 0.2328 -0.0097 -0.0016 0.0130  201 A1BQG C N   
2195 C C11 . A1BQG F .   ? 0.4627 0.4281 0.4124 -0.0042 0.0187  0.0270  201 A1BQG C C11 
2196 N N2  . A1BQG F .   ? 0.4728 0.4378 0.4151 -0.0026 0.0234  0.0261  201 A1BQG C N2  
2197 C C9  . A1BQG F .   ? 0.4667 0.4196 0.4020 -0.0040 0.0379  0.0351  201 A1BQG C C9  
# 
