data_7HWF
# 
_entry.id   7HWF 
# 
_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   7HWF         pdb_00007hwf 10.2210/pdb7hwf/pdb 
WWPDB D_1001408015 ?            ?                   
# 
_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                        7HWF 
_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-[(2S)-2-(methoxymethyl)oxane-2-carbonyl]piperidine-3-carboxamide' 284.351   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                      78.133    2   ?         ? ? ? 
5 water       nat water                                                                     18.015    373 ?         ? ? ? 
# 
_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-[(2S)-2-(methoxymethyl)oxane-2-carbonyl]piperidine-3-carboxamide' A1BO8 
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 
A1BO8 non-polymer         . '(3S)-1-[(2S)-2-(methoxymethyl)oxane-2-carbonyl]piperidine-3-carboxamide' ? 'C14 H24 N2 O4'  284.351 
ALA   'L-peptide linking' y ALANINE                                                                   ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                  ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                           ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                  ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                      ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                 ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                           ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                   ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                 ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                     ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                   ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                    ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                             ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                   ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                    ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                 ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                  ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                    ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                                ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 146 GLU GLU C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BO8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BO8 
_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 A1BO8 1   201 201 A1BO8 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 1   DMS   DMS A . 
F 3 ZN    1   201 1   ZN    ZN  C . 
G 4 DMS   1   202 1   DMS   DMS C . 
H 5 HOH   1   301 83  HOH   HOH A . 
H 5 HOH   2   302 97  HOH   HOH A . 
H 5 HOH   3   303 205 HOH   HOH A . 
H 5 HOH   4   304 347 HOH   HOH A . 
H 5 HOH   5   305 133 HOH   HOH A . 
H 5 HOH   6   306 94  HOH   HOH A . 
H 5 HOH   7   307 149 HOH   HOH A . 
H 5 HOH   8   308 172 HOH   HOH A . 
H 5 HOH   9   309 343 HOH   HOH A . 
H 5 HOH   10  310 333 HOH   HOH A . 
H 5 HOH   11  311 185 HOH   HOH A . 
H 5 HOH   12  312 154 HOH   HOH A . 
H 5 HOH   13  313 294 HOH   HOH A . 
H 5 HOH   14  314 87  HOH   HOH A . 
H 5 HOH   15  315 313 HOH   HOH A . 
H 5 HOH   16  316 141 HOH   HOH A . 
H 5 HOH   17  317 295 HOH   HOH A . 
H 5 HOH   18  318 70  HOH   HOH A . 
H 5 HOH   19  319 186 HOH   HOH A . 
H 5 HOH   20  320 113 HOH   HOH A . 
H 5 HOH   21  321 155 HOH   HOH A . 
H 5 HOH   22  322 363 HOH   HOH A . 
H 5 HOH   23  323 20  HOH   HOH A . 
H 5 HOH   24  324 206 HOH   HOH A . 
H 5 HOH   25  325 334 HOH   HOH A . 
H 5 HOH   26  326 211 HOH   HOH A . 
H 5 HOH   27  327 122 HOH   HOH A . 
H 5 HOH   28  328 148 HOH   HOH A . 
H 5 HOH   29  329 318 HOH   HOH A . 
H 5 HOH   30  330 100 HOH   HOH A . 
H 5 HOH   31  331 119 HOH   HOH A . 
H 5 HOH   32  332 120 HOH   HOH A . 
H 5 HOH   33  333 338 HOH   HOH A . 
H 5 HOH   34  334 297 HOH   HOH A . 
H 5 HOH   35  335 9   HOH   HOH A . 
H 5 HOH   36  336 280 HOH   HOH A . 
H 5 HOH   37  337 241 HOH   HOH A . 
H 5 HOH   38  338 12  HOH   HOH A . 
H 5 HOH   39  339 307 HOH   HOH A . 
H 5 HOH   40  340 77  HOH   HOH A . 
H 5 HOH   41  341 29  HOH   HOH A . 
H 5 HOH   42  342 102 HOH   HOH A . 
H 5 HOH   43  343 216 HOH   HOH A . 
H 5 HOH   44  344 74  HOH   HOH A . 
H 5 HOH   45  345 82  HOH   HOH A . 
H 5 HOH   46  346 43  HOH   HOH A . 
H 5 HOH   47  347 126 HOH   HOH A . 
H 5 HOH   48  348 123 HOH   HOH A . 
H 5 HOH   49  349 296 HOH   HOH A . 
H 5 HOH   50  350 28  HOH   HOH A . 
H 5 HOH   51  351 11  HOH   HOH A . 
H 5 HOH   52  352 4   HOH   HOH A . 
H 5 HOH   53  353 7   HOH   HOH A . 
H 5 HOH   54  354 2   HOH   HOH A . 
H 5 HOH   55  355 364 HOH   HOH A . 
H 5 HOH   56  356 293 HOH   HOH A . 
H 5 HOH   57  357 331 HOH   HOH A . 
H 5 HOH   58  358 248 HOH   HOH A . 
H 5 HOH   59  359 303 HOH   HOH A . 
H 5 HOH   60  360 212 HOH   HOH A . 
H 5 HOH   61  361 162 HOH   HOH A . 
H 5 HOH   62  362 90  HOH   HOH A . 
H 5 HOH   63  363 348 HOH   HOH A . 
H 5 HOH   64  364 64  HOH   HOH A . 
H 5 HOH   65  365 349 HOH   HOH A . 
H 5 HOH   66  366 279 HOH   HOH A . 
H 5 HOH   67  367 46  HOH   HOH A . 
H 5 HOH   68  368 196 HOH   HOH A . 
H 5 HOH   69  369 317 HOH   HOH A . 
H 5 HOH   70  370 302 HOH   HOH A . 
H 5 HOH   71  371 41  HOH   HOH A . 
H 5 HOH   72  372 152 HOH   HOH A . 
H 5 HOH   73  373 367 HOH   HOH A . 
H 5 HOH   74  374 268 HOH   HOH A . 
H 5 HOH   75  375 139 HOH   HOH A . 
H 5 HOH   76  376 164 HOH   HOH A . 
H 5 HOH   77  377 25  HOH   HOH A . 
H 5 HOH   78  378 116 HOH   HOH A . 
H 5 HOH   79  379 45  HOH   HOH A . 
H 5 HOH   80  380 326 HOH   HOH A . 
H 5 HOH   81  381 54  HOH   HOH A . 
H 5 HOH   82  382 35  HOH   HOH A . 
H 5 HOH   83  383 3   HOH   HOH A . 
H 5 HOH   84  384 57  HOH   HOH A . 
H 5 HOH   85  385 222 HOH   HOH A . 
H 5 HOH   86  386 143 HOH   HOH A . 
H 5 HOH   87  387 321 HOH   HOH A . 
H 5 HOH   88  388 98  HOH   HOH A . 
H 5 HOH   89  389 183 HOH   HOH A . 
H 5 HOH   90  390 253 HOH   HOH A . 
H 5 HOH   91  391 252 HOH   HOH A . 
H 5 HOH   92  392 316 HOH   HOH A . 
H 5 HOH   93  393 34  HOH   HOH A . 
H 5 HOH   94  394 352 HOH   HOH A . 
H 5 HOH   95  395 207 HOH   HOH A . 
H 5 HOH   96  396 27  HOH   HOH A . 
H 5 HOH   97  397 153 HOH   HOH A . 
H 5 HOH   98  398 68  HOH   HOH A . 
H 5 HOH   99  399 103 HOH   HOH A . 
H 5 HOH   100 400 51  HOH   HOH A . 
H 5 HOH   101 401 151 HOH   HOH A . 
H 5 HOH   102 402 67  HOH   HOH A . 
H 5 HOH   103 403 146 HOH   HOH A . 
H 5 HOH   104 404 50  HOH   HOH A . 
H 5 HOH   105 405 244 HOH   HOH A . 
H 5 HOH   106 406 96  HOH   HOH A . 
H 5 HOH   107 407 171 HOH   HOH A . 
H 5 HOH   108 408 101 HOH   HOH A . 
H 5 HOH   109 409 305 HOH   HOH A . 
H 5 HOH   110 410 189 HOH   HOH A . 
H 5 HOH   111 411 201 HOH   HOH A . 
H 5 HOH   112 412 163 HOH   HOH A . 
H 5 HOH   113 413 142 HOH   HOH A . 
H 5 HOH   114 414 200 HOH   HOH A . 
H 5 HOH   115 415 174 HOH   HOH A . 
H 5 HOH   116 416 93  HOH   HOH A . 
H 5 HOH   117 417 299 HOH   HOH A . 
H 5 HOH   118 418 15  HOH   HOH A . 
H 5 HOH   119 419 233 HOH   HOH A . 
H 5 HOH   120 420 238 HOH   HOH A . 
H 5 HOH   121 421 124 HOH   HOH A . 
H 5 HOH   122 422 230 HOH   HOH A . 
H 5 HOH   123 423 223 HOH   HOH A . 
H 5 HOH   124 424 345 HOH   HOH A . 
H 5 HOH   125 425 190 HOH   HOH A . 
H 5 HOH   126 426 104 HOH   HOH A . 
H 5 HOH   127 427 13  HOH   HOH A . 
H 5 HOH   128 428 176 HOH   HOH A . 
H 5 HOH   129 429 309 HOH   HOH A . 
H 5 HOH   130 430 39  HOH   HOH A . 
H 5 HOH   131 431 249 HOH   HOH A . 
H 5 HOH   132 432 168 HOH   HOH A . 
H 5 HOH   133 433 243 HOH   HOH A . 
H 5 HOH   134 434 328 HOH   HOH A . 
H 5 HOH   135 435 129 HOH   HOH A . 
H 5 HOH   136 436 308 HOH   HOH A . 
H 5 HOH   137 437 144 HOH   HOH A . 
H 5 HOH   138 438 73  HOH   HOH A . 
H 5 HOH   139 439 58  HOH   HOH A . 
H 5 HOH   140 440 130 HOH   HOH A . 
H 5 HOH   141 441 26  HOH   HOH A . 
H 5 HOH   142 442 31  HOH   HOH A . 
H 5 HOH   143 443 217 HOH   HOH A . 
H 5 HOH   144 444 84  HOH   HOH A . 
H 5 HOH   145 445 40  HOH   HOH A . 
H 5 HOH   146 446 341 HOH   HOH A . 
H 5 HOH   147 447 365 HOH   HOH A . 
H 5 HOH   148 448 137 HOH   HOH A . 
H 5 HOH   149 449 267 HOH   HOH A . 
H 5 HOH   150 450 261 HOH   HOH A . 
H 5 HOH   151 451 282 HOH   HOH A . 
H 5 HOH   152 452 380 HOH   HOH A . 
H 5 HOH   153 453 369 HOH   HOH A . 
H 5 HOH   154 454 358 HOH   HOH A . 
H 5 HOH   155 455 257 HOH   HOH A . 
H 5 HOH   156 456 360 HOH   HOH A . 
H 5 HOH   157 457 273 HOH   HOH A . 
H 5 HOH   158 458 289 HOH   HOH A . 
H 5 HOH   159 459 378 HOH   HOH A . 
H 5 HOH   160 460 356 HOH   HOH A . 
H 5 HOH   161 461 195 HOH   HOH A . 
H 5 HOH   162 462 224 HOH   HOH A . 
H 5 HOH   163 463 370 HOH   HOH A . 
H 5 HOH   164 464 275 HOH   HOH A . 
H 5 HOH   165 465 175 HOH   HOH A . 
H 5 HOH   166 466 361 HOH   HOH A . 
H 5 HOH   167 467 188 HOH   HOH A . 
H 5 HOH   168 468 240 HOH   HOH A . 
H 5 HOH   169 469 357 HOH   HOH A . 
H 5 HOH   170 470 109 HOH   HOH A . 
H 5 HOH   171 471 92  HOH   HOH A . 
H 5 HOH   172 472 286 HOH   HOH A . 
H 5 HOH   173 473 199 HOH   HOH A . 
H 5 HOH   174 474 169 HOH   HOH A . 
H 5 HOH   175 475 245 HOH   HOH A . 
H 5 HOH   176 476 251 HOH   HOH A . 
H 5 HOH   177 477 290 HOH   HOH A . 
H 5 HOH   178 478 337 HOH   HOH A . 
H 5 HOH   179 479 263 HOH   HOH A . 
H 5 HOH   180 480 254 HOH   HOH A . 
I 5 HOH   1   301 375 HOH   HOH C . 
I 5 HOH   2   302 319 HOH   HOH C . 
I 5 HOH   3   303 246 HOH   HOH C . 
I 5 HOH   4   304 298 HOH   HOH C . 
I 5 HOH   5   305 79  HOH   HOH C . 
I 5 HOH   6   306 371 HOH   HOH C . 
I 5 HOH   7   307 373 HOH   HOH C . 
I 5 HOH   8   308 277 HOH   HOH C . 
I 5 HOH   9   309 351 HOH   HOH C . 
I 5 HOH   10  310 86  HOH   HOH C . 
I 5 HOH   11  311 232 HOH   HOH C . 
I 5 HOH   12  312 304 HOH   HOH C . 
I 5 HOH   13  313 24  HOH   HOH C . 
I 5 HOH   14  314 18  HOH   HOH C . 
I 5 HOH   15  315 159 HOH   HOH C . 
I 5 HOH   16  316 30  HOH   HOH C . 
I 5 HOH   17  317 132 HOH   HOH C . 
I 5 HOH   18  318 65  HOH   HOH C . 
I 5 HOH   19  319 61  HOH   HOH C . 
I 5 HOH   20  320 258 HOH   HOH C . 
I 5 HOH   21  321 118 HOH   HOH C . 
I 5 HOH   22  322 250 HOH   HOH C . 
I 5 HOH   23  323 220 HOH   HOH C . 
I 5 HOH   24  324 167 HOH   HOH C . 
I 5 HOH   25  325 178 HOH   HOH C . 
I 5 HOH   26  326 114 HOH   HOH C . 
I 5 HOH   27  327 147 HOH   HOH C . 
I 5 HOH   28  328 314 HOH   HOH C . 
I 5 HOH   29  329 202 HOH   HOH C . 
I 5 HOH   30  330 325 HOH   HOH C . 
I 5 HOH   31  331 228 HOH   HOH C . 
I 5 HOH   32  332 115 HOH   HOH C . 
I 5 HOH   33  333 60  HOH   HOH C . 
I 5 HOH   34  334 182 HOH   HOH C . 
I 5 HOH   35  335 91  HOH   HOH C . 
I 5 HOH   36  336 218 HOH   HOH C . 
I 5 HOH   37  337 1   HOH   HOH C . 
I 5 HOH   38  338 323 HOH   HOH C . 
I 5 HOH   39  339 156 HOH   HOH C . 
I 5 HOH   40  340 180 HOH   HOH C . 
I 5 HOH   41  341 78  HOH   HOH C . 
I 5 HOH   42  342 36  HOH   HOH C . 
I 5 HOH   43  343 117 HOH   HOH C . 
I 5 HOH   44  344 33  HOH   HOH C . 
I 5 HOH   45  345 48  HOH   HOH C . 
I 5 HOH   46  346 8   HOH   HOH C . 
I 5 HOH   47  347 264 HOH   HOH C . 
I 5 HOH   48  348 306 HOH   HOH C . 
I 5 HOH   49  349 173 HOH   HOH C . 
I 5 HOH   50  350 225 HOH   HOH C . 
I 5 HOH   51  351 237 HOH   HOH C . 
I 5 HOH   52  352 69  HOH   HOH C . 
I 5 HOH   53  353 158 HOH   HOH C . 
I 5 HOH   54  354 49  HOH   HOH C . 
I 5 HOH   55  355 6   HOH   HOH C . 
I 5 HOH   56  356 37  HOH   HOH C . 
I 5 HOH   57  357 85  HOH   HOH C . 
I 5 HOH   58  358 187 HOH   HOH C . 
I 5 HOH   59  359 329 HOH   HOH C . 
I 5 HOH   60  360 161 HOH   HOH C . 
I 5 HOH   61  361 32  HOH   HOH C . 
I 5 HOH   62  362 138 HOH   HOH C . 
I 5 HOH   63  363 136 HOH   HOH C . 
I 5 HOH   64  364 327 HOH   HOH C . 
I 5 HOH   65  365 121 HOH   HOH C . 
I 5 HOH   66  366 112 HOH   HOH C . 
I 5 HOH   67  367 125 HOH   HOH C . 
I 5 HOH   68  368 292 HOH   HOH C . 
I 5 HOH   69  369 234 HOH   HOH C . 
I 5 HOH   70  370 320 HOH   HOH C . 
I 5 HOH   71  371 301 HOH   HOH C . 
I 5 HOH   72  372 75  HOH   HOH C . 
I 5 HOH   73  373 342 HOH   HOH C . 
I 5 HOH   74  374 81  HOH   HOH C . 
I 5 HOH   75  375 62  HOH   HOH C . 
I 5 HOH   76  376 255 HOH   HOH C . 
I 5 HOH   77  377 21  HOH   HOH C . 
I 5 HOH   78  378 165 HOH   HOH C . 
I 5 HOH   79  379 127 HOH   HOH C . 
I 5 HOH   80  380 71  HOH   HOH C . 
I 5 HOH   81  381 10  HOH   HOH C . 
I 5 HOH   82  382 47  HOH   HOH C . 
I 5 HOH   83  383 177 HOH   HOH C . 
I 5 HOH   84  384 219 HOH   HOH C . 
I 5 HOH   85  385 111 HOH   HOH C . 
I 5 HOH   86  386 315 HOH   HOH C . 
I 5 HOH   87  387 209 HOH   HOH C . 
I 5 HOH   88  388 55  HOH   HOH C . 
I 5 HOH   89  389 53  HOH   HOH C . 
I 5 HOH   90  390 311 HOH   HOH C . 
I 5 HOH   91  391 22  HOH   HOH C . 
I 5 HOH   92  392 17  HOH   HOH C . 
I 5 HOH   93  393 76  HOH   HOH C . 
I 5 HOH   94  394 80  HOH   HOH C . 
I 5 HOH   95  395 23  HOH   HOH C . 
I 5 HOH   96  396 204 HOH   HOH C . 
I 5 HOH   97  397 191 HOH   HOH C . 
I 5 HOH   98  398 210 HOH   HOH C . 
I 5 HOH   99  399 350 HOH   HOH C . 
I 5 HOH   100 400 105 HOH   HOH C . 
I 5 HOH   101 401 14  HOH   HOH C . 
I 5 HOH   102 402 88  HOH   HOH C . 
I 5 HOH   103 403 166 HOH   HOH C . 
I 5 HOH   104 404 44  HOH   HOH C . 
I 5 HOH   105 405 227 HOH   HOH C . 
I 5 HOH   106 406 181 HOH   HOH C . 
I 5 HOH   107 407 52  HOH   HOH C . 
I 5 HOH   108 408 72  HOH   HOH C . 
I 5 HOH   109 409 108 HOH   HOH C . 
I 5 HOH   110 410 38  HOH   HOH C . 
I 5 HOH   111 411 235 HOH   HOH C . 
I 5 HOH   112 412 131 HOH   HOH C . 
I 5 HOH   113 413 287 HOH   HOH C . 
I 5 HOH   114 414 59  HOH   HOH C . 
I 5 HOH   115 415 5   HOH   HOH C . 
I 5 HOH   116 416 229 HOH   HOH C . 
I 5 HOH   117 417 140 HOH   HOH C . 
I 5 HOH   118 418 374 HOH   HOH C . 
I 5 HOH   119 419 221 HOH   HOH C . 
I 5 HOH   120 420 150 HOH   HOH C . 
I 5 HOH   121 421 362 HOH   HOH C . 
I 5 HOH   122 422 226 HOH   HOH C . 
I 5 HOH   123 423 300 HOH   HOH C . 
I 5 HOH   124 424 193 HOH   HOH C . 
I 5 HOH   125 425 310 HOH   HOH C . 
I 5 HOH   126 426 66  HOH   HOH C . 
I 5 HOH   127 427 332 HOH   HOH C . 
I 5 HOH   128 428 192 HOH   HOH C . 
I 5 HOH   129 429 95  HOH   HOH C . 
I 5 HOH   130 430 170 HOH   HOH C . 
I 5 HOH   131 431 242 HOH   HOH C . 
I 5 HOH   132 432 42  HOH   HOH C . 
I 5 HOH   133 433 247 HOH   HOH C . 
I 5 HOH   134 434 16  HOH   HOH C . 
I 5 HOH   135 435 214 HOH   HOH C . 
I 5 HOH   136 436 19  HOH   HOH C . 
I 5 HOH   137 437 63  HOH   HOH C . 
I 5 HOH   138 438 106 HOH   HOH C . 
I 5 HOH   139 439 376 HOH   HOH C . 
I 5 HOH   140 440 56  HOH   HOH C . 
I 5 HOH   141 441 354 HOH   HOH C . 
I 5 HOH   142 442 107 HOH   HOH C . 
I 5 HOH   143 443 285 HOH   HOH C . 
I 5 HOH   144 444 340 HOH   HOH C . 
I 5 HOH   145 445 184 HOH   HOH C . 
I 5 HOH   146 446 322 HOH   HOH C . 
I 5 HOH   147 447 231 HOH   HOH C . 
I 5 HOH   148 448 157 HOH   HOH C . 
I 5 HOH   149 449 372 HOH   HOH C . 
I 5 HOH   150 450 366 HOH   HOH C . 
I 5 HOH   151 451 134 HOH   HOH C . 
I 5 HOH   152 452 262 HOH   HOH C . 
I 5 HOH   153 453 335 HOH   HOH C . 
I 5 HOH   154 454 324 HOH   HOH C . 
I 5 HOH   155 455 336 HOH   HOH C . 
I 5 HOH   156 456 99  HOH   HOH C . 
I 5 HOH   157 457 270 HOH   HOH C . 
I 5 HOH   158 458 283 HOH   HOH C . 
I 5 HOH   159 459 135 HOH   HOH C . 
I 5 HOH   160 460 213 HOH   HOH C . 
I 5 HOH   161 461 179 HOH   HOH C . 
I 5 HOH   162 462 368 HOH   HOH C . 
I 5 HOH   163 463 269 HOH   HOH C . 
I 5 HOH   164 464 145 HOH   HOH C . 
I 5 HOH   165 465 377 HOH   HOH C . 
I 5 HOH   166 466 353 HOH   HOH C . 
I 5 HOH   167 467 236 HOH   HOH C . 
I 5 HOH   168 468 208 HOH   HOH C . 
I 5 HOH   169 469 271 HOH   HOH C . 
I 5 HOH   170 470 265 HOH   HOH C . 
I 5 HOH   171 471 359 HOH   HOH C . 
I 5 HOH   172 472 215 HOH   HOH C . 
I 5 HOH   173 473 291 HOH   HOH C . 
I 5 HOH   174 474 256 HOH   HOH C . 
I 5 HOH   175 475 110 HOH   HOH C . 
I 5 HOH   176 476 355 HOH   HOH C . 
I 5 HOH   177 477 259 HOH   HOH C . 
I 5 HOH   178 478 197 HOH   HOH C . 
I 5 HOH   179 479 198 HOH   HOH C . 
I 5 HOH   180 480 203 HOH   HOH C . 
I 5 HOH   181 481 274 HOH   HOH C . 
I 5 HOH   182 482 260 HOH   HOH C . 
I 5 HOH   183 483 266 HOH   HOH C . 
I 5 HOH   184 484 284 HOH   HOH C . 
I 5 HOH   185 485 312 HOH   HOH C . 
I 5 HOH   186 486 160 HOH   HOH C . 
I 5 HOH   187 487 272 HOH   HOH C . 
I 5 HOH   188 488 288 HOH   HOH C . 
I 5 HOH   189 489 194 HOH   HOH C . 
I 5 HOH   190 490 330 HOH   HOH C . 
I 5 HOH   191 491 276 HOH   HOH C . 
I 5 HOH   192 492 379 HOH   HOH C . 
I 5 HOH   193 493 278 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           7HWF 
_cell.length_a           86.668 
_cell.length_b           57.169 
_cell.length_c           64.815 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.57 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HWF 
_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          7HWF 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.52 
_exptl_crystal.density_percent_sol   51.15 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-22 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92203 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HWF 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             43.18 
_reflns.d_resolution_high            1.25 
_reflns.number_obs                   80616 
_reflns.percent_possible_obs         92.5 
_reflns.pdbx_Rmerge_I_obs            0.054 
_reflns.pdbx_netI_over_sigmaI        19.5 
_reflns.pdbx_redundancy              5.5 
_reflns.pdbx_Rrim_I_all              0.059 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     442112 
_reflns.pdbx_chi_squared             0.85 
_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                  1.25 
_reflns_shell.d_res_low                   1.27 
_reflns_shell.number_measured_all         4288 
_reflns_shell.number_unique_obs           2130 
_reflns_shell.Rmerge_I_obs                0.790 
_reflns_shell.pdbx_chi_squared            0.22 
_reflns_shell.pdbx_redundancy             2.0 
_reflns_shell.percent_possible_obs        49.2 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.091 
_reflns_shell.pdbx_Rpim_I_all             0.749 
_reflns_shell.pdbx_CC_half                0.269 
_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                                 7HWF 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     80476 
_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                             17.96 
_refine.ls_d_res_high                            1.250 
_refine.ls_percent_reflns_obs                    92.3 
_refine.ls_R_factor_obs                          0.1778 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1769 
_refine.ls_R_factor_R_free                       0.1939 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.020 
_refine.ls_number_reflns_R_free                  4043 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.963 
_refine.B_iso_mean                               20.31 
_refine.aniso_B[1][1]                            0.07930 
_refine.aniso_B[2][2]                            -1.39110 
_refine.aniso_B[3][3]                            1.31180 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.72980 
_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             0.044 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.045 
_refine.pdbx_overall_SU_R_Blow_DPI               0.046 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.047 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HWF 
_refine_analyze.Luzzati_coordinate_error_obs    0.15 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             373 
_refine_hist.number_atoms_total               2569 
_refine_hist.d_res_high                       1.250 
_refine_hist.d_res_low                        17.96 
# 
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                  0.013 ? 2.00  2274 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.10  ? 2.00  3101 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  771  '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  400  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2274 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.92  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.96 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  282  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  2105 '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                       1.25 
_refine_ls_shell.d_res_low                        1.27 
_refine_ls_shell.number_reflns_R_work             1527 
_refine_ls_shell.R_factor_R_work                  0.2945 
_refine_ls_shell.percent_reflns_obs               47.48 
_refine_ls_shell.R_factor_R_free                  0.2901 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.16 
_refine_ls_shell.number_reflns_R_free             83 
_refine_ls_shell.number_reflns_all                1610 
_refine_ls_shell.R_factor_all                     0.2943 
# 
_struct.entry_id                  7HWF 
_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-0034437-001 (A71EV2A-x3936)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HWF 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HWF A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HWF C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,H 
2 1 B,F,G,I   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P6  AA6 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P7  AA7 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P8  AA8 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P9  AA9 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P10 AB1 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P11 AB2 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.264 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
# 
_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_555 111.3 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 105.7 ? 
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_555 116.7 ? 
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_555 103.1 ? 
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_555 102.9 ? 
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_555 116.4 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 110.0 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.0 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.7 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 104.5 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.9 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.9 ? 
# 
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 ? THR A 120 ? GLY A 119 THR A 126 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7HWF 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 363 ? ? O A HOH 442 ? ? 1.67 
2 1 O A HOH 333 ? ? O A HOH 451 ? ? 1.86 
3 1 O C HOH 389 ? ? O C HOH 427 ? ? 1.89 
4 1 O C HOH 343 ? ? O C HOH 386 ? ? 1.92 
5 1 O C HOH 450 ? ? O C HOH 458 ? ? 2.04 
6 1 O C HOH 397 ? ? O C HOH 455 ? ? 2.05 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 14.8587 8.1587   14.3952 -0.0214 -0.0171 0.0000 0.0161 0.0007 0.0053 1.2344 0.6932 0.6686 0.7478  
-0.4755 -0.2719 -0.0176 0.0485 0.1039 0.0165 0.0491 0.0061 -0.0245 -0.0810 -0.0315 
'X-RAY DIFFRACTION' 2 ? refined 25.8041 -20.1945 17.7693 -0.0274 -0.0150 0.0151 0.0073 0.0018 0.0171 0.5622 0.8236 0.3087 -0.1623 
-0.0912 -0.0877 0.0042  0.0039 0.0991 0.0087 0.0301 0.0144 0.0403  0.0018  -0.0342 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BO8 N1   N  N N 1   
A1BO8 C4   C  N N 2   
A1BO8 C5   C  N N 3   
A1BO8 C6   C  N N 4   
A1BO8 C7   C  N S 5   
A1BO8 C8   C  N N 6   
A1BO8 C10  C  N N 7   
A1BO8 C13  C  N N 8   
A1BO8 O2   O  N N 9   
A1BO8 C9   C  N N 10  
A1BO8 N    N  N N 11  
A1BO8 C3   C  N N 12  
A1BO8 O1   O  N N 13  
A1BO8 C2   C  N S 14  
A1BO8 C1   C  N N 15  
A1BO8 O    O  N N 16  
A1BO8 C    C  N N 17  
A1BO8 O3   O  N N 18  
A1BO8 C12  C  N N 19  
A1BO8 C11  C  N N 20  
A1BO8 H13  H  N N 21  
A1BO8 H12  H  N N 22  
A1BO8 H7   H  N N 23  
A1BO8 H6   H  N N 24  
A1BO8 H8   H  N N 25  
A1BO8 H9   H  N N 26  
A1BO8 H10  H  N N 27  
A1BO8 H11  H  N N 28  
A1BO8 H    H  N N 29  
A1BO8 H16  H  N N 30  
A1BO8 H17  H  N N 31  
A1BO8 H22  H  N N 32  
A1BO8 H23  H  N N 33  
A1BO8 H14  H  N N 34  
A1BO8 H15  H  N N 35  
A1BO8 H4   H  N N 36  
A1BO8 H5   H  N N 37  
A1BO8 H1   H  N N 38  
A1BO8 H2   H  N N 39  
A1BO8 H3   H  N N 40  
A1BO8 H20  H  N N 41  
A1BO8 H21  H  N N 42  
A1BO8 H18  H  N N 43  
A1BO8 H19  H  N N 44  
ALA   N    N  N N 45  
ALA   CA   C  N S 46  
ALA   C    C  N N 47  
ALA   O    O  N N 48  
ALA   CB   C  N N 49  
ALA   OXT  O  N N 50  
ALA   H    H  N N 51  
ALA   H2   H  N N 52  
ALA   HA   H  N N 53  
ALA   HB1  H  N N 54  
ALA   HB2  H  N N 55  
ALA   HB3  H  N N 56  
ALA   HXT  H  N N 57  
ARG   N    N  N N 58  
ARG   CA   C  N S 59  
ARG   C    C  N N 60  
ARG   O    O  N N 61  
ARG   CB   C  N N 62  
ARG   CG   C  N N 63  
ARG   CD   C  N N 64  
ARG   NE   N  N N 65  
ARG   CZ   C  N N 66  
ARG   NH1  N  N N 67  
ARG   NH2  N  N N 68  
ARG   OXT  O  N N 69  
ARG   H    H  N N 70  
ARG   H2   H  N N 71  
ARG   HA   H  N N 72  
ARG   HB2  H  N N 73  
ARG   HB3  H  N N 74  
ARG   HG2  H  N N 75  
ARG   HG3  H  N N 76  
ARG   HD2  H  N N 77  
ARG   HD3  H  N N 78  
ARG   HE   H  N N 79  
ARG   HH11 H  N N 80  
ARG   HH12 H  N N 81  
ARG   HH21 H  N N 82  
ARG   HH22 H  N N 83  
ARG   HXT  H  N N 84  
ASN   N    N  N N 85  
ASN   CA   C  N S 86  
ASN   C    C  N N 87  
ASN   O    O  N N 88  
ASN   CB   C  N N 89  
ASN   CG   C  N N 90  
ASN   OD1  O  N N 91  
ASN   ND2  N  N N 92  
ASN   OXT  O  N N 93  
ASN   H    H  N N 94  
ASN   H2   H  N N 95  
ASN   HA   H  N N 96  
ASN   HB2  H  N N 97  
ASN   HB3  H  N N 98  
ASN   HD21 H  N N 99  
ASN   HD22 H  N N 100 
ASN   HXT  H  N N 101 
ASP   N    N  N N 102 
ASP   CA   C  N S 103 
ASP   C    C  N N 104 
ASP   O    O  N N 105 
ASP   CB   C  N N 106 
ASP   CG   C  N N 107 
ASP   OD1  O  N N 108 
ASP   OD2  O  N N 109 
ASP   OXT  O  N N 110 
ASP   H    H  N N 111 
ASP   H2   H  N N 112 
ASP   HA   H  N N 113 
ASP   HB2  H  N N 114 
ASP   HB3  H  N N 115 
ASP   HD2  H  N N 116 
ASP   HXT  H  N N 117 
CYS   N    N  N N 118 
CYS   CA   C  N R 119 
CYS   C    C  N N 120 
CYS   O    O  N N 121 
CYS   CB   C  N N 122 
CYS   SG   S  N N 123 
CYS   OXT  O  N N 124 
CYS   H    H  N N 125 
CYS   H2   H  N N 126 
CYS   HA   H  N N 127 
CYS   HB2  H  N N 128 
CYS   HB3  H  N N 129 
CYS   HG   H  N N 130 
CYS   HXT  H  N N 131 
DMS   S    S  N N 132 
DMS   O    O  N N 133 
DMS   C1   C  N N 134 
DMS   C2   C  N N 135 
DMS   H11  H  N N 136 
DMS   H12  H  N N 137 
DMS   H13  H  N N 138 
DMS   H21  H  N N 139 
DMS   H22  H  N N 140 
DMS   H23  H  N N 141 
GLN   N    N  N N 142 
GLN   CA   C  N S 143 
GLN   C    C  N N 144 
GLN   O    O  N N 145 
GLN   CB   C  N N 146 
GLN   CG   C  N N 147 
GLN   CD   C  N N 148 
GLN   OE1  O  N N 149 
GLN   NE2  N  N N 150 
GLN   OXT  O  N N 151 
GLN   H    H  N N 152 
GLN   H2   H  N N 153 
GLN   HA   H  N N 154 
GLN   HB2  H  N N 155 
GLN   HB3  H  N N 156 
GLN   HG2  H  N N 157 
GLN   HG3  H  N N 158 
GLN   HE21 H  N N 159 
GLN   HE22 H  N N 160 
GLN   HXT  H  N N 161 
GLU   N    N  N N 162 
GLU   CA   C  N S 163 
GLU   C    C  N N 164 
GLU   O    O  N N 165 
GLU   CB   C  N N 166 
GLU   CG   C  N N 167 
GLU   CD   C  N N 168 
GLU   OE1  O  N N 169 
GLU   OE2  O  N N 170 
GLU   OXT  O  N N 171 
GLU   H    H  N N 172 
GLU   H2   H  N N 173 
GLU   HA   H  N N 174 
GLU   HB2  H  N N 175 
GLU   HB3  H  N N 176 
GLU   HG2  H  N N 177 
GLU   HG3  H  N N 178 
GLU   HE2  H  N N 179 
GLU   HXT  H  N N 180 
GLY   N    N  N N 181 
GLY   CA   C  N N 182 
GLY   C    C  N N 183 
GLY   O    O  N N 184 
GLY   OXT  O  N N 185 
GLY   H    H  N N 186 
GLY   H2   H  N N 187 
GLY   HA2  H  N N 188 
GLY   HA3  H  N N 189 
GLY   HXT  H  N N 190 
HIS   N    N  N N 191 
HIS   CA   C  N S 192 
HIS   C    C  N N 193 
HIS   O    O  N N 194 
HIS   CB   C  N N 195 
HIS   CG   C  Y N 196 
HIS   ND1  N  Y N 197 
HIS   CD2  C  Y N 198 
HIS   CE1  C  Y N 199 
HIS   NE2  N  Y N 200 
HIS   OXT  O  N N 201 
HIS   H    H  N N 202 
HIS   H2   H  N N 203 
HIS   HA   H  N N 204 
HIS   HB2  H  N N 205 
HIS   HB3  H  N N 206 
HIS   HD1  H  N N 207 
HIS   HD2  H  N N 208 
HIS   HE1  H  N N 209 
HIS   HE2  H  N N 210 
HIS   HXT  H  N N 211 
HOH   O    O  N N 212 
HOH   H1   H  N N 213 
HOH   H2   H  N N 214 
ILE   N    N  N N 215 
ILE   CA   C  N S 216 
ILE   C    C  N N 217 
ILE   O    O  N N 218 
ILE   CB   C  N S 219 
ILE   CG1  C  N N 220 
ILE   CG2  C  N N 221 
ILE   CD1  C  N N 222 
ILE   OXT  O  N N 223 
ILE   H    H  N N 224 
ILE   H2   H  N N 225 
ILE   HA   H  N N 226 
ILE   HB   H  N N 227 
ILE   HG12 H  N N 228 
ILE   HG13 H  N N 229 
ILE   HG21 H  N N 230 
ILE   HG22 H  N N 231 
ILE   HG23 H  N N 232 
ILE   HD11 H  N N 233 
ILE   HD12 H  N N 234 
ILE   HD13 H  N N 235 
ILE   HXT  H  N N 236 
LEU   N    N  N N 237 
LEU   CA   C  N S 238 
LEU   C    C  N N 239 
LEU   O    O  N N 240 
LEU   CB   C  N N 241 
LEU   CG   C  N N 242 
LEU   CD1  C  N N 243 
LEU   CD2  C  N N 244 
LEU   OXT  O  N N 245 
LEU   H    H  N N 246 
LEU   H2   H  N N 247 
LEU   HA   H  N N 248 
LEU   HB2  H  N N 249 
LEU   HB3  H  N N 250 
LEU   HG   H  N N 251 
LEU   HD11 H  N N 252 
LEU   HD12 H  N N 253 
LEU   HD13 H  N N 254 
LEU   HD21 H  N N 255 
LEU   HD22 H  N N 256 
LEU   HD23 H  N N 257 
LEU   HXT  H  N N 258 
LYS   N    N  N N 259 
LYS   CA   C  N S 260 
LYS   C    C  N N 261 
LYS   O    O  N N 262 
LYS   CB   C  N N 263 
LYS   CG   C  N N 264 
LYS   CD   C  N N 265 
LYS   CE   C  N N 266 
LYS   NZ   N  N N 267 
LYS   OXT  O  N N 268 
LYS   H    H  N N 269 
LYS   H2   H  N N 270 
LYS   HA   H  N N 271 
LYS   HB2  H  N N 272 
LYS   HB3  H  N N 273 
LYS   HG2  H  N N 274 
LYS   HG3  H  N N 275 
LYS   HD2  H  N N 276 
LYS   HD3  H  N N 277 
LYS   HE2  H  N N 278 
LYS   HE3  H  N N 279 
LYS   HZ1  H  N N 280 
LYS   HZ2  H  N N 281 
LYS   HZ3  H  N N 282 
LYS   HXT  H  N N 283 
MET   N    N  N N 284 
MET   CA   C  N S 285 
MET   C    C  N N 286 
MET   O    O  N N 287 
MET   CB   C  N N 288 
MET   CG   C  N N 289 
MET   SD   S  N N 290 
MET   CE   C  N N 291 
MET   OXT  O  N N 292 
MET   H    H  N N 293 
MET   H2   H  N N 294 
MET   HA   H  N N 295 
MET   HB2  H  N N 296 
MET   HB3  H  N N 297 
MET   HG2  H  N N 298 
MET   HG3  H  N N 299 
MET   HE1  H  N N 300 
MET   HE2  H  N N 301 
MET   HE3  H  N N 302 
MET   HXT  H  N N 303 
PHE   N    N  N N 304 
PHE   CA   C  N S 305 
PHE   C    C  N N 306 
PHE   O    O  N N 307 
PHE   CB   C  N N 308 
PHE   CG   C  Y N 309 
PHE   CD1  C  Y N 310 
PHE   CD2  C  Y N 311 
PHE   CE1  C  Y N 312 
PHE   CE2  C  Y N 313 
PHE   CZ   C  Y N 314 
PHE   OXT  O  N N 315 
PHE   H    H  N N 316 
PHE   H2   H  N N 317 
PHE   HA   H  N N 318 
PHE   HB2  H  N N 319 
PHE   HB3  H  N N 320 
PHE   HD1  H  N N 321 
PHE   HD2  H  N N 322 
PHE   HE1  H  N N 323 
PHE   HE2  H  N N 324 
PHE   HZ   H  N N 325 
PHE   HXT  H  N N 326 
PRO   N    N  N N 327 
PRO   CA   C  N S 328 
PRO   C    C  N N 329 
PRO   O    O  N N 330 
PRO   CB   C  N N 331 
PRO   CG   C  N N 332 
PRO   CD   C  N N 333 
PRO   OXT  O  N N 334 
PRO   H    H  N N 335 
PRO   HA   H  N N 336 
PRO   HB2  H  N N 337 
PRO   HB3  H  N N 338 
PRO   HG2  H  N N 339 
PRO   HG3  H  N N 340 
PRO   HD2  H  N N 341 
PRO   HD3  H  N N 342 
PRO   HXT  H  N N 343 
SER   N    N  N N 344 
SER   CA   C  N S 345 
SER   C    C  N N 346 
SER   O    O  N N 347 
SER   CB   C  N N 348 
SER   OG   O  N N 349 
SER   OXT  O  N N 350 
SER   H    H  N N 351 
SER   H2   H  N N 352 
SER   HA   H  N N 353 
SER   HB2  H  N N 354 
SER   HB3  H  N N 355 
SER   HG   H  N N 356 
SER   HXT  H  N N 357 
THR   N    N  N N 358 
THR   CA   C  N S 359 
THR   C    C  N N 360 
THR   O    O  N N 361 
THR   CB   C  N R 362 
THR   OG1  O  N N 363 
THR   CG2  C  N N 364 
THR   OXT  O  N N 365 
THR   H    H  N N 366 
THR   H2   H  N N 367 
THR   HA   H  N N 368 
THR   HB   H  N N 369 
THR   HG1  H  N N 370 
THR   HG21 H  N N 371 
THR   HG22 H  N N 372 
THR   HG23 H  N N 373 
THR   HXT  H  N N 374 
TRP   N    N  N N 375 
TRP   CA   C  N S 376 
TRP   C    C  N N 377 
TRP   O    O  N N 378 
TRP   CB   C  N N 379 
TRP   CG   C  Y N 380 
TRP   CD1  C  Y N 381 
TRP   CD2  C  Y N 382 
TRP   NE1  N  Y N 383 
TRP   CE2  C  Y N 384 
TRP   CE3  C  Y N 385 
TRP   CZ2  C  Y N 386 
TRP   CZ3  C  Y N 387 
TRP   CH2  C  Y N 388 
TRP   OXT  O  N N 389 
TRP   H    H  N N 390 
TRP   H2   H  N N 391 
TRP   HA   H  N N 392 
TRP   HB2  H  N N 393 
TRP   HB3  H  N N 394 
TRP   HD1  H  N N 395 
TRP   HE1  H  N N 396 
TRP   HE3  H  N N 397 
TRP   HZ2  H  N N 398 
TRP   HZ3  H  N N 399 
TRP   HH2  H  N N 400 
TRP   HXT  H  N N 401 
TYR   N    N  N N 402 
TYR   CA   C  N S 403 
TYR   C    C  N N 404 
TYR   O    O  N N 405 
TYR   CB   C  N N 406 
TYR   CG   C  Y N 407 
TYR   CD1  C  Y N 408 
TYR   CD2  C  Y N 409 
TYR   CE1  C  Y N 410 
TYR   CE2  C  Y N 411 
TYR   CZ   C  Y N 412 
TYR   OH   O  N N 413 
TYR   OXT  O  N N 414 
TYR   H    H  N N 415 
TYR   H2   H  N N 416 
TYR   HA   H  N N 417 
TYR   HB2  H  N N 418 
TYR   HB3  H  N N 419 
TYR   HD1  H  N N 420 
TYR   HD2  H  N N 421 
TYR   HE1  H  N N 422 
TYR   HE2  H  N N 423 
TYR   HH   H  N N 424 
TYR   HXT  H  N N 425 
VAL   N    N  N N 426 
VAL   CA   C  N S 427 
VAL   C    C  N N 428 
VAL   O    O  N N 429 
VAL   CB   C  N N 430 
VAL   CG1  C  N N 431 
VAL   CG2  C  N N 432 
VAL   OXT  O  N N 433 
VAL   H    H  N N 434 
VAL   H2   H  N N 435 
VAL   HA   H  N N 436 
VAL   HB   H  N N 437 
VAL   HG11 H  N N 438 
VAL   HG12 H  N N 439 
VAL   HG13 H  N N 440 
VAL   HG21 H  N N 441 
VAL   HG22 H  N N 442 
VAL   HG23 H  N N 443 
VAL   HXT  H  N N 444 
ZN    ZN   ZN N N 445 
# 
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 
A1BO8 C   O    sing N N 1   
A1BO8 O   C1   sing N N 2   
A1BO8 C1  C2   sing N N 3   
A1BO8 C2  C3   sing N N 4   
A1BO8 O1  C3   doub N N 5   
A1BO8 C3  N    sing N N 6   
A1BO8 N   C4   sing N N 7   
A1BO8 C4  C5   sing N N 8   
A1BO8 C5  C6   sing N N 9   
A1BO8 C6  C7   sing N N 10  
A1BO8 C7  C8   sing N N 11  
A1BO8 N1  C8   sing N N 12  
A1BO8 C8  O2   doub N N 13  
A1BO8 C9  C7   sing N N 14  
A1BO8 N   C9   sing N N 15  
A1BO8 C2  C10  sing N N 16  
A1BO8 C10 C11  sing N N 17  
A1BO8 C11 C12  sing N N 18  
A1BO8 C12 C13  sing N N 19  
A1BO8 C13 O3   sing N N 20  
A1BO8 O3  C2   sing N N 21  
A1BO8 N1  H13  sing N N 22  
A1BO8 N1  H12  sing N N 23  
A1BO8 C4  H7   sing N N 24  
A1BO8 C4  H6   sing N N 25  
A1BO8 C5  H8   sing N N 26  
A1BO8 C5  H9   sing N N 27  
A1BO8 C6  H10  sing N N 28  
A1BO8 C6  H11  sing N N 29  
A1BO8 C7  H    sing N N 30  
A1BO8 C10 H16  sing N N 31  
A1BO8 C10 H17  sing N N 32  
A1BO8 C13 H22  sing N N 33  
A1BO8 C13 H23  sing N N 34  
A1BO8 C9  H14  sing N N 35  
A1BO8 C9  H15  sing N N 36  
A1BO8 C1  H4   sing N N 37  
A1BO8 C1  H5   sing N N 38  
A1BO8 C   H1   sing N N 39  
A1BO8 C   H2   sing N N 40  
A1BO8 C   H3   sing N N 41  
A1BO8 C12 H20  sing N N 42  
A1BO8 C12 H21  sing N N 43  
A1BO8 C11 H18  sing N N 44  
A1BO8 C11 H19  sing N N 45  
ALA   N   CA   sing N N 46  
ALA   N   H    sing N N 47  
ALA   N   H2   sing N N 48  
ALA   CA  C    sing N N 49  
ALA   CA  CB   sing N N 50  
ALA   CA  HA   sing N N 51  
ALA   C   O    doub N N 52  
ALA   C   OXT  sing N N 53  
ALA   CB  HB1  sing N N 54  
ALA   CB  HB2  sing N N 55  
ALA   CB  HB3  sing N N 56  
ALA   OXT HXT  sing N N 57  
ARG   N   CA   sing N N 58  
ARG   N   H    sing N N 59  
ARG   N   H2   sing N N 60  
ARG   CA  C    sing N N 61  
ARG   CA  CB   sing N N 62  
ARG   CA  HA   sing N N 63  
ARG   C   O    doub N N 64  
ARG   C   OXT  sing N N 65  
ARG   CB  CG   sing N N 66  
ARG   CB  HB2  sing N N 67  
ARG   CB  HB3  sing N N 68  
ARG   CG  CD   sing N N 69  
ARG   CG  HG2  sing N N 70  
ARG   CG  HG3  sing N N 71  
ARG   CD  NE   sing N N 72  
ARG   CD  HD2  sing N N 73  
ARG   CD  HD3  sing N N 74  
ARG   NE  CZ   sing N N 75  
ARG   NE  HE   sing N N 76  
ARG   CZ  NH1  sing N N 77  
ARG   CZ  NH2  doub N N 78  
ARG   NH1 HH11 sing N N 79  
ARG   NH1 HH12 sing N N 80  
ARG   NH2 HH21 sing N N 81  
ARG   NH2 HH22 sing N N 82  
ARG   OXT HXT  sing N N 83  
ASN   N   CA   sing N N 84  
ASN   N   H    sing N N 85  
ASN   N   H2   sing N N 86  
ASN   CA  C    sing N N 87  
ASN   CA  CB   sing N N 88  
ASN   CA  HA   sing N N 89  
ASN   C   O    doub N N 90  
ASN   C   OXT  sing N N 91  
ASN   CB  CG   sing N N 92  
ASN   CB  HB2  sing N N 93  
ASN   CB  HB3  sing N N 94  
ASN   CG  OD1  doub N N 95  
ASN   CG  ND2  sing N N 96  
ASN   ND2 HD21 sing N N 97  
ASN   ND2 HD22 sing N N 98  
ASN   OXT HXT  sing N N 99  
ASP   N   CA   sing N N 100 
ASP   N   H    sing N N 101 
ASP   N   H2   sing N N 102 
ASP   CA  C    sing N N 103 
ASP   CA  CB   sing N N 104 
ASP   CA  HA   sing N N 105 
ASP   C   O    doub N N 106 
ASP   C   OXT  sing N N 107 
ASP   CB  CG   sing N N 108 
ASP   CB  HB2  sing N N 109 
ASP   CB  HB3  sing N N 110 
ASP   CG  OD1  doub N N 111 
ASP   CG  OD2  sing N N 112 
ASP   OD2 HD2  sing N N 113 
ASP   OXT HXT  sing N N 114 
CYS   N   CA   sing N N 115 
CYS   N   H    sing N N 116 
CYS   N   H2   sing N N 117 
CYS   CA  C    sing N N 118 
CYS   CA  CB   sing N N 119 
CYS   CA  HA   sing N N 120 
CYS   C   O    doub N N 121 
CYS   C   OXT  sing N N 122 
CYS   CB  SG   sing N N 123 
CYS   CB  HB2  sing N N 124 
CYS   CB  HB3  sing N N 125 
CYS   SG  HG   sing N N 126 
CYS   OXT HXT  sing N N 127 
DMS   S   O    doub N N 128 
DMS   S   C1   sing N N 129 
DMS   S   C2   sing N N 130 
DMS   C1  H11  sing N N 131 
DMS   C1  H12  sing N N 132 
DMS   C1  H13  sing N N 133 
DMS   C2  H21  sing N N 134 
DMS   C2  H22  sing N N 135 
DMS   C2  H23  sing N N 136 
GLN   N   CA   sing N N 137 
GLN   N   H    sing N N 138 
GLN   N   H2   sing N N 139 
GLN   CA  C    sing N N 140 
GLN   CA  CB   sing N N 141 
GLN   CA  HA   sing N N 142 
GLN   C   O    doub N N 143 
GLN   C   OXT  sing N N 144 
GLN   CB  CG   sing N N 145 
GLN   CB  HB2  sing N N 146 
GLN   CB  HB3  sing N N 147 
GLN   CG  CD   sing N N 148 
GLN   CG  HG2  sing N N 149 
GLN   CG  HG3  sing N N 150 
GLN   CD  OE1  doub N N 151 
GLN   CD  NE2  sing N N 152 
GLN   NE2 HE21 sing N N 153 
GLN   NE2 HE22 sing N N 154 
GLN   OXT HXT  sing N N 155 
GLU   N   CA   sing N N 156 
GLU   N   H    sing N N 157 
GLU   N   H2   sing N N 158 
GLU   CA  C    sing N N 159 
GLU   CA  CB   sing N N 160 
GLU   CA  HA   sing N N 161 
GLU   C   O    doub N N 162 
GLU   C   OXT  sing N N 163 
GLU   CB  CG   sing N N 164 
GLU   CB  HB2  sing N N 165 
GLU   CB  HB3  sing N N 166 
GLU   CG  CD   sing N N 167 
GLU   CG  HG2  sing N N 168 
GLU   CG  HG3  sing N N 169 
GLU   CD  OE1  doub N N 170 
GLU   CD  OE2  sing N N 171 
GLU   OE2 HE2  sing N N 172 
GLU   OXT HXT  sing N N 173 
GLY   N   CA   sing N N 174 
GLY   N   H    sing N N 175 
GLY   N   H2   sing N N 176 
GLY   CA  C    sing N N 177 
GLY   CA  HA2  sing N N 178 
GLY   CA  HA3  sing N N 179 
GLY   C   O    doub N N 180 
GLY   C   OXT  sing N N 181 
GLY   OXT HXT  sing N N 182 
HIS   N   CA   sing N N 183 
HIS   N   H    sing N N 184 
HIS   N   H2   sing N N 185 
HIS   CA  C    sing N N 186 
HIS   CA  CB   sing N N 187 
HIS   CA  HA   sing N N 188 
HIS   C   O    doub N N 189 
HIS   C   OXT  sing N N 190 
HIS   CB  CG   sing N N 191 
HIS   CB  HB2  sing N N 192 
HIS   CB  HB3  sing N N 193 
HIS   CG  ND1  sing Y N 194 
HIS   CG  CD2  doub Y N 195 
HIS   ND1 CE1  doub Y N 196 
HIS   ND1 HD1  sing N N 197 
HIS   CD2 NE2  sing Y N 198 
HIS   CD2 HD2  sing N N 199 
HIS   CE1 NE2  sing Y N 200 
HIS   CE1 HE1  sing N N 201 
HIS   NE2 HE2  sing N N 202 
HIS   OXT HXT  sing N N 203 
HOH   O   H1   sing N N 204 
HOH   O   H2   sing N N 205 
ILE   N   CA   sing N N 206 
ILE   N   H    sing N N 207 
ILE   N   H2   sing N N 208 
ILE   CA  C    sing N N 209 
ILE   CA  CB   sing N N 210 
ILE   CA  HA   sing N N 211 
ILE   C   O    doub N N 212 
ILE   C   OXT  sing N N 213 
ILE   CB  CG1  sing N N 214 
ILE   CB  CG2  sing N N 215 
ILE   CB  HB   sing N N 216 
ILE   CG1 CD1  sing N N 217 
ILE   CG1 HG12 sing N N 218 
ILE   CG1 HG13 sing N N 219 
ILE   CG2 HG21 sing N N 220 
ILE   CG2 HG22 sing N N 221 
ILE   CG2 HG23 sing N N 222 
ILE   CD1 HD11 sing N N 223 
ILE   CD1 HD12 sing N N 224 
ILE   CD1 HD13 sing N N 225 
ILE   OXT HXT  sing N N 226 
LEU   N   CA   sing N N 227 
LEU   N   H    sing N N 228 
LEU   N   H2   sing N N 229 
LEU   CA  C    sing N N 230 
LEU   CA  CB   sing N N 231 
LEU   CA  HA   sing N N 232 
LEU   C   O    doub N N 233 
LEU   C   OXT  sing N N 234 
LEU   CB  CG   sing N N 235 
LEU   CB  HB2  sing N N 236 
LEU   CB  HB3  sing N N 237 
LEU   CG  CD1  sing N N 238 
LEU   CG  CD2  sing N N 239 
LEU   CG  HG   sing N N 240 
LEU   CD1 HD11 sing N N 241 
LEU   CD1 HD12 sing N N 242 
LEU   CD1 HD13 sing N N 243 
LEU   CD2 HD21 sing N N 244 
LEU   CD2 HD22 sing N N 245 
LEU   CD2 HD23 sing N N 246 
LEU   OXT HXT  sing N N 247 
LYS   N   CA   sing N N 248 
LYS   N   H    sing N N 249 
LYS   N   H2   sing N N 250 
LYS   CA  C    sing N N 251 
LYS   CA  CB   sing N N 252 
LYS   CA  HA   sing N N 253 
LYS   C   O    doub N N 254 
LYS   C   OXT  sing N N 255 
LYS   CB  CG   sing N N 256 
LYS   CB  HB2  sing N N 257 
LYS   CB  HB3  sing N N 258 
LYS   CG  CD   sing N N 259 
LYS   CG  HG2  sing N N 260 
LYS   CG  HG3  sing N N 261 
LYS   CD  CE   sing N N 262 
LYS   CD  HD2  sing N N 263 
LYS   CD  HD3  sing N N 264 
LYS   CE  NZ   sing N N 265 
LYS   CE  HE2  sing N N 266 
LYS   CE  HE3  sing N N 267 
LYS   NZ  HZ1  sing N N 268 
LYS   NZ  HZ2  sing N N 269 
LYS   NZ  HZ3  sing N N 270 
LYS   OXT HXT  sing N N 271 
MET   N   CA   sing N N 272 
MET   N   H    sing N N 273 
MET   N   H2   sing N N 274 
MET   CA  C    sing N N 275 
MET   CA  CB   sing N N 276 
MET   CA  HA   sing N N 277 
MET   C   O    doub N N 278 
MET   C   OXT  sing N N 279 
MET   CB  CG   sing N N 280 
MET   CB  HB2  sing N N 281 
MET   CB  HB3  sing N N 282 
MET   CG  SD   sing N N 283 
MET   CG  HG2  sing N N 284 
MET   CG  HG3  sing N N 285 
MET   SD  CE   sing N N 286 
MET   CE  HE1  sing N N 287 
MET   CE  HE2  sing N N 288 
MET   CE  HE3  sing N N 289 
MET   OXT HXT  sing N N 290 
PHE   N   CA   sing N N 291 
PHE   N   H    sing N N 292 
PHE   N   H2   sing N N 293 
PHE   CA  C    sing N N 294 
PHE   CA  CB   sing N N 295 
PHE   CA  HA   sing N N 296 
PHE   C   O    doub N N 297 
PHE   C   OXT  sing N N 298 
PHE   CB  CG   sing N N 299 
PHE   CB  HB2  sing N N 300 
PHE   CB  HB3  sing N N 301 
PHE   CG  CD1  doub Y N 302 
PHE   CG  CD2  sing Y N 303 
PHE   CD1 CE1  sing Y N 304 
PHE   CD1 HD1  sing N N 305 
PHE   CD2 CE2  doub Y N 306 
PHE   CD2 HD2  sing N N 307 
PHE   CE1 CZ   doub Y N 308 
PHE   CE1 HE1  sing N N 309 
PHE   CE2 CZ   sing Y N 310 
PHE   CE2 HE2  sing N N 311 
PHE   CZ  HZ   sing N N 312 
PHE   OXT HXT  sing N N 313 
PRO   N   CA   sing N N 314 
PRO   N   CD   sing N N 315 
PRO   N   H    sing N N 316 
PRO   CA  C    sing N N 317 
PRO   CA  CB   sing N N 318 
PRO   CA  HA   sing N N 319 
PRO   C   O    doub N N 320 
PRO   C   OXT  sing N N 321 
PRO   CB  CG   sing N N 322 
PRO   CB  HB2  sing N N 323 
PRO   CB  HB3  sing N N 324 
PRO   CG  CD   sing N N 325 
PRO   CG  HG2  sing N N 326 
PRO   CG  HG3  sing N N 327 
PRO   CD  HD2  sing N N 328 
PRO   CD  HD3  sing N N 329 
PRO   OXT HXT  sing N N 330 
SER   N   CA   sing N N 331 
SER   N   H    sing N N 332 
SER   N   H2   sing N N 333 
SER   CA  C    sing N N 334 
SER   CA  CB   sing N N 335 
SER   CA  HA   sing N N 336 
SER   C   O    doub N N 337 
SER   C   OXT  sing N N 338 
SER   CB  OG   sing N N 339 
SER   CB  HB2  sing N N 340 
SER   CB  HB3  sing N N 341 
SER   OG  HG   sing N N 342 
SER   OXT HXT  sing N N 343 
THR   N   CA   sing N N 344 
THR   N   H    sing N N 345 
THR   N   H2   sing N N 346 
THR   CA  C    sing N N 347 
THR   CA  CB   sing N N 348 
THR   CA  HA   sing N N 349 
THR   C   O    doub N N 350 
THR   C   OXT  sing N N 351 
THR   CB  OG1  sing N N 352 
THR   CB  CG2  sing N N 353 
THR   CB  HB   sing N N 354 
THR   OG1 HG1  sing N N 355 
THR   CG2 HG21 sing N N 356 
THR   CG2 HG22 sing N N 357 
THR   CG2 HG23 sing N N 358 
THR   OXT HXT  sing N N 359 
TRP   N   CA   sing N N 360 
TRP   N   H    sing N N 361 
TRP   N   H2   sing N N 362 
TRP   CA  C    sing N N 363 
TRP   CA  CB   sing N N 364 
TRP   CA  HA   sing N N 365 
TRP   C   O    doub N N 366 
TRP   C   OXT  sing N N 367 
TRP   CB  CG   sing N N 368 
TRP   CB  HB2  sing N N 369 
TRP   CB  HB3  sing N N 370 
TRP   CG  CD1  doub Y N 371 
TRP   CG  CD2  sing Y N 372 
TRP   CD1 NE1  sing Y N 373 
TRP   CD1 HD1  sing N N 374 
TRP   CD2 CE2  doub Y N 375 
TRP   CD2 CE3  sing Y N 376 
TRP   NE1 CE2  sing Y N 377 
TRP   NE1 HE1  sing N N 378 
TRP   CE2 CZ2  sing Y N 379 
TRP   CE3 CZ3  doub Y N 380 
TRP   CE3 HE3  sing N N 381 
TRP   CZ2 CH2  doub Y N 382 
TRP   CZ2 HZ2  sing N N 383 
TRP   CZ3 CH2  sing Y N 384 
TRP   CZ3 HZ3  sing N N 385 
TRP   CH2 HH2  sing N N 386 
TRP   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_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                    7HWF 
_atom_sites.fract_transf_matrix[1][1]   0.011538 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000922 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017492 
_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]   0.015478 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.655 8.027   24.862 1.00 17.12 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.884 8.145   24.065 1.00 16.74 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.045 6.934   23.149 1.00 16.45 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.351 5.906   23.331 1.00 16.93 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.094 8.263   25.002 1.00 19.55 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.227 7.066   25.742 1.00 21.60 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.945 7.040   22.168 1.00 14.86 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.212 5.935   21.255 1.00 14.28 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.636 6.411   19.885 1.00 13.72 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.293 7.513   19.477 1.00 15.26 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.307 5.566   19.159 1.00 12.60 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.786 5.915   17.821 1.00 12.87 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.767 4.695   16.921 1.00 13.04 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.691 3.545   17.390 1.00 13.92 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.230 6.466   17.946 1.00 14.43 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.835 4.935   15.609 1.00 12.15 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.062 3.890   14.597 1.00 11.53 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.535 3.978   14.218 1.00 12.58 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.037 5.087   13.928 1.00 12.77 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.207 4.086   13.330 1.00 11.78 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.727 4.248   13.681 1.00 13.67 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.418 2.887   12.362 1.00 13.00 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.920 4.788   12.454 1.00 14.50 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.245 2.833   14.178 1.00 12.60 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.650 2.823   13.774 1.00 13.67 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.759 1.982   12.507 1.00 14.29 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.754 0.746   12.572 1.00 14.72 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.543 2.240   14.894 1.00 14.76 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.586 3.126   16.111 1.00 14.19 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.461 4.212   16.180 1.00 15.09 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.737 2.906   17.186 1.00 15.78 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.440 5.095   17.269 1.00 15.24 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.739 3.756   18.299 1.00 16.47 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.576 4.864   18.317 1.00 15.98 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.586 5.722   19.423 1.00 18.73 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.820 2.645   11.350 1.00 14.39 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.915 2.016   10.048 1.00 14.50 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.142 2.507   9.327  1.00 15.73 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.378 3.722   9.274  1.00 14.89 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.611 2.257   9.212  1.00 15.83 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.259 3.762   9.113  1.00 16.74 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.777 1.648   7.832  1.00 17.23 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.013 1.593   8.866  1.00 17.16 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.248 2.029   8.219  1.00 17.04 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.082 2.904   9.141  1.00 16.19 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.182 2.603   10.345 1.00 16.05 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.532 4.062   8.617  1.00 15.77 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.233 5.031   9.452  1.00 15.61 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.325 6.220   9.776  1.00 14.65 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.813 7.361   9.908  1.00 15.36 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.575 5.484   8.867  1.00 16.90 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.650 4.438   9.002  1.00 21.21 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.404 4.390   9.989  1.00 23.47 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.703 3.567   8.044  1.00 19.22 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.043 5.938   10.015 1.00 13.46 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.082 6.986   10.379 1.00 13.36 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.414 6.649   11.706 1.00 12.61 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.144 5.475   12.024 1.00 13.90 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.970 7.056   9.299  1.00 14.08 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.463 7.460   7.925  1.00 14.44 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.110 8.676   7.719  1.00 16.40 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.285 6.623   6.830  1.00 16.79 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.586 9.039   6.462  1.00 17.30 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.720 6.997   5.560  1.00 17.37 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.351 8.212   5.379  1.00 18.59 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.801 8.611   4.124  1.00 21.89 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.052 7.707   12.440 1.00 12.29 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.248 7.650   13.671 1.00 12.37 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.024 8.507   13.427 1.00 12.75 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.158 9.715   13.141 1.00 13.24 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.072 8.194   14.867 1.00 13.02 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.292 8.506   16.147 1.00 13.49 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.227 8.903   17.315 1.00 14.57 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.662 9.973   18.142 1.00 15.47 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.995 9.773   19.279 1.00 17.28 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.702 8.535   19.678 1.00 18.34 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.529 10.808  19.970 1.00 17.38 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.840 7.894   13.487 1.00 11.91 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.566 8.618   13.237 1.00 11.82 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.885 8.844   14.587 1.00 12.53 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.579 7.849   15.290 1.00 13.38 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.624 7.806   12.324 1.00 12.59 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.411 8.666   11.931 1.00 12.59 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.328 7.323   11.063 1.00 13.33 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.624 10.100  14.955 1.00 11.67 ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.008 10.429  16.250 0.50 11.70 ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.053 10.407  16.263 0.50 13.69 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.909 11.418  16.060 1.00 12.41 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.750 12.042  14.971 1.00 13.57 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.020 11.051  17.253 0.50 10.95 ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.208 11.026  17.129 0.50 17.29 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 22.933 9.980   17.798 0.50 12.01 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.772 11.391  18.528 0.50 17.59 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.769 12.277  16.644 0.50 8.55  ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.398 10.103  17.210 0.50 19.83 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.068 11.602  17.099 1.00 12.32 ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.056 12.659  17.045 1.00 12.51 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.840 13.987  17.059 1.00 12.93 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.755 14.165  17.884 1.00 13.38 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.198 12.629  18.315 1.00 12.76 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.326 11.383  18.411 1.00 13.34 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.752 10.360  18.998 1.00 14.07 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.157 11.422  17.744 1.00 14.02 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.468 14.921  16.163 1.00 12.63 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.219 16.213  16.123 1.00 13.19 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.174 16.904  17.472 1.00 14.98 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.180 17.460  17.906 1.00 15.44 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.605 17.093  15.045 1.00 13.94 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.399 18.411  14.802 1.00 14.55 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.654 19.304  13.815 1.00 16.58 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.396 20.495  13.380 1.00 16.89 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.382 21.661  14.013 1.00 19.73 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.818 21.768  15.206 1.00 19.76 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 19.996 22.723  13.481 1.00 20.59 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.032 16.808  18.179 1.00 14.59 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 17.904 17.511  19.457 1.00 16.21 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.760 16.914  20.583 1.00 16.59 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 18.890 17.544  21.637 1.00 18.34 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.415 17.667  19.880 1.00 17.22 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.762 16.420  20.392 1.00 15.29 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.134 15.529  19.543 1.00 16.11 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.536 16.022  21.673 1.00 16.94 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.614 14.579  20.322 1.00 16.06 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.841 14.828  21.599 1.00 17.07 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.296 15.696  20.401 1.00 15.84 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.169 15.036  21.372 1.00 16.00 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.631 14.977  20.911 1.00 16.80 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.470 14.378  21.589 1.00 17.18 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.655 13.633  21.699 1.00 15.73 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.259 13.597  22.296 1.00 16.47 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.850 12.127  22.569 1.00 17.09 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.160 14.424  23.627 1.00 18.22 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 21.974 15.620  19.763 1.00 16.07 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.355 15.597  19.285 1.00 15.60 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.317 16.249  20.257 1.00 17.30 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 23.992 17.269  20.884 1.00 17.99 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.431 16.278  17.913 1.00 15.55 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.489 15.626  20.377 1.00 16.17 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.543 16.129  21.287 1.00 16.03 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.460 17.131  20.577 1.00 17.01 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.435 17.264  19.334 1.00 15.87 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.407 14.959  21.801 1.00 18.10 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.156 14.419  20.694 1.00 18.95 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.596 13.869  22.496 1.00 19.28 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.378 17.811  21.341 1.00 17.39 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.362 18.666  20.714 1.00 18.04 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.228 17.860  19.748 1.00 17.07 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.511 18.343  18.642 1.00 17.09 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.289 19.343  21.774 1.00 19.49 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.525 20.009  21.165 1.00 28.05 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.444 21.220  20.494 1.00 32.68 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.792 19.528  21.026 1.00 32.19 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.667 21.507  20.085 1.00 32.99 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.520 20.504  20.347 1.00 34.59 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.625 16.615  20.124 1.00 16.63 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.432 15.808  19.210 1.00 17.04 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.674 15.510  17.897 1.00 15.40 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.273 15.524  16.815 1.00 16.42 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.884 14.496  19.846 1.00 18.31 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.883 13.772  18.966 1.00 26.63 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.043 14.224  18.796 1.00 30.02 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.438 12.674  18.312 1.00 29.09 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.336 15.268  17.973 1.00 14.42 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.561 15.069  16.757 1.00 14.28 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.619 16.320  15.848 1.00 13.37 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.854 16.207  14.645 1.00 14.21 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.086 14.802  17.096 1.00 14.36 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.815 13.436  17.680 1.00 15.81 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.473 12.456  17.233 1.00 15.76 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 25.981 13.340  18.612 1.00 15.76 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.410 17.512  16.418 1.00 13.82 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.456 18.758  15.628 1.00 13.87 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.872 19.035  15.077 1.00 14.66 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 29.973 19.591  13.976 1.00 15.58 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 27.978 19.934  16.517 1.00 14.37 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.482 20.006  16.639 1.00 14.38 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.723 19.707  17.736 1.00 16.02 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.561 20.454  15.630 1.00 15.31 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.386 19.925  17.466 1.00 15.60 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.260 20.384  16.174 1.00 15.43 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.721 20.914  14.316 1.00 16.79 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.120 20.776  15.442 1.00 17.12 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.603 21.249  13.583 1.00 17.72 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.335 21.211  14.143 1.00 18.23 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.926 18.608  15.803 1.00 14.60 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.286 18.819  15.348 1.00 15.25 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.722 17.826  14.260 1.00 15.99 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.757 18.002  13.627 1.00 16.81 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.243 18.774  16.549 1.00 16.85 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.921 16.751  14.052 1.00 15.54 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.212 15.706  13.030 1.00 15.68 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.963 15.520  12.167 1.00 15.40 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.578 14.394  11.848 1.00 15.22 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.605 14.371  13.738 1.00 17.24 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.945 14.551  14.418 1.00 18.73 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 34.975 14.480  13.756 1.00 20.80 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 33.951 14.869  15.734 1.00 18.68 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.308 16.605  11.831 1.00 14.72 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.017 16.570  11.173 1.00 13.52 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.079 16.120  9.739  1.00 14.96 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.938 16.586  8.957  1.00 16.43 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.434 18.001  11.232 1.00 14.32 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.038 18.148  10.652 1.00 15.30 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.011 17.348  11.482 1.00 15.14 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.590 19.619  10.598 1.00 17.83 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.160 15.238  9.351  1.00 13.65 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.003 14.827  7.954  1.00 14.45 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.747 15.532  7.365  1.00 15.28 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.795 16.077  6.246  1.00 16.45 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.869 13.295  7.847  1.00 13.58 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.503 12.876  6.411  1.00 15.85 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.161 12.615  8.336  1.00 15.54 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.593 15.487  8.087  1.00 14.77 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.341 16.024  7.574  1.00 14.87 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.377 16.239  8.726  1.00 15.05 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.407 15.458  9.690  1.00 14.26 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.736 15.015  6.555  1.00 15.80 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.324 15.279  6.102  1.00 16.67 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.922 16.107  5.089  1.00 19.30 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.129 14.656  6.609  1.00 15.93 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.548 16.034  4.942  1.00 20.38 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.042 15.136  5.850  1.00 17.85 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.871 13.747  7.638  1.00 16.00 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.712 14.700  6.074  1.00 18.84 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.577 13.292  7.828  1.00 17.58 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.509 13.796  7.087  1.00 18.83 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.527 17.278  8.654  1.00 15.75 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.519 17.473  9.692  1.00 15.27 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.285 18.105  9.057  1.00 16.66 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.393 18.886  8.076  1.00 16.94 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.057 18.308  10.848 1.00 16.56 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.641 19.673  10.460 1.00 17.10 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.666 20.829  10.262 1.00 19.35 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.003 21.791  9.517  1.00 20.09 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.567 20.802  10.860 1.00 18.62 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.114 17.807  9.608  1.00 15.11 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.859 18.362  9.102  1.00 14.86 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.904 18.529  10.284 1.00 15.93 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.370 17.545  10.832 1.00 15.55 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.272 17.438  8.024  1.00 17.00 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.010 17.936  7.368  1.00 20.09 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.188 18.542  8.064  1.00 23.36 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.834 17.695  6.163  1.00 24.19 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.686 19.787  10.691 1.00 16.63 ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.818 20.110  11.809 0.50 17.26 ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.827 20.050  11.837 0.50 18.00 ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.369 19.668  11.557 1.00 17.82 ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.716 19.163  12.471 1.00 17.85 ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.883 21.618  12.061 0.50 17.79 ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 15.963 21.504  12.287 0.50 21.13 ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 14.908 22.019  13.001 0.50 17.97 ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.589 22.361  11.229 0.50 26.11 ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.885 19.812  10.324 1.00 17.34 ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.505 19.408  10.011 1.00 17.50 ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.255 17.927  10.189 1.00 16.87 ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.114 17.538  10.422 1.00 18.84 ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.090 19.847  8.604  1.00 20.05 ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.621 19.004  7.595  1.00 26.30 ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.300 17.097  10.166 1.00 15.28 ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.190 15.639  10.354 1.00 15.90 ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.672 15.186  11.739 1.00 14.93 ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.606 13.973  12.046 1.00 14.01 ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.055 14.918  9.295  1.00 16.40 ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.526 15.094  7.867  1.00 17.47 ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.407 14.415  6.826  1.00 17.84 ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.329 12.952  6.966  1.00 15.28 ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.501 12.105  5.957  1.00 16.56 ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.737 12.558  4.731  1.00 18.68 ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.375 10.795  6.149  1.00 15.92 ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.235 16.102  12.564 1.00 14.19 ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.866 15.750  13.827 1.00 13.18 ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.018 14.745  13.666 1.00 13.54 ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.223 13.907  14.553 1.00 13.98 ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.859 15.258  14.900 1.00 13.98 ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.463 15.020  16.280 1.00 14.48 ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.295 15.859  16.738 1.00 15.85 ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.066 14.023  16.946 1.00 15.19 ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.825 14.877  12.593 1.00 13.30 ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.920 13.931  12.380 1.00 12.21 ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.267 14.653  12.266 1.00 13.22 ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.339 15.766  11.688 1.00 13.42 ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.710 13.128  11.098 1.00 12.36 ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.624 12.004  11.153 1.00 14.60 ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.554 11.295  9.835  1.00 16.26 ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.901 11.011  12.290 1.00 14.83 ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.324 14.004  12.747 1.00 12.58 ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.691 14.467  12.524 1.00 12.24 ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.560 13.222  12.384 1.00 12.53 ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.352 12.194  13.067 1.00 12.59 ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.158 15.313  13.755 1.00 13.02 ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.594 15.882  13.666 1.00 13.17 ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.685 17.264  14.336 1.00 14.40 ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.630 14.930  14.286 1.00 13.76 ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.519 13.283  11.448 1.00 12.58 ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.471 12.200  11.194 1.00 11.71 ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.869 12.733  11.359 1.00 12.05 ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.207 13.796  10.786 1.00 12.95 ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.246 11.613  9.785  1.00 12.23 ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.243 10.499  9.502  1.00 14.14 ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.802 11.099  9.636  1.00 13.95 ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.685 12.041  12.144 1.00 12.22 ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.100 12.391  12.348 1.00 12.27 ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 28.979 11.218  11.900 1.00 13.59 ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.512 10.075  11.675 1.00 13.79 ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.368 12.744  13.806 1.00 14.03 ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.046 11.668  14.681 1.00 14.45 ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.274 11.504  11.715 1.00 14.54 ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.207 10.459  11.280 1.00 15.41 ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.841 9.733   12.460 1.00 16.55 ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.022 10.345  13.540 1.00 18.54 ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.286 11.057  10.380 1.00 18.11 ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.002 12.036  11.123 1.00 20.14 ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.170 8.425   12.263 1.00 17.13 ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.754 7.634   13.345 1.00 18.80 ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.087 7.051   12.904 1.00 20.97 ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.320 6.822   11.701 1.00 20.16 ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.822 6.456   13.721 1.00 19.12 ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.711 5.547   12.623 1.00 19.73 ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.430 6.922   14.108 1.00 19.29 ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.943 6.764   13.894 1.00 22.06 ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.210 6.122   13.582 1.00 23.46 ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.007 4.615   13.364 1.00 23.65 ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.550 4.058   12.389 1.00 25.74 ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.260 6.433   14.664 1.00 26.98 ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.775 5.957   15.899 1.00 31.46 ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.518 7.904   14.797 1.00 27.57 ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.210 3.971   14.238 1.00 23.79 ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.948 2.534   14.082 1.00 24.73 ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.717 2.249   13.194 1.00 22.85 ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.773 3.045   13.185 1.00 21.99 ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.723 1.899   15.443 1.00 27.68 ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.713 1.118   12.478 1.00 22.22 ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.582 0.701   11.646 1.00 22.57 ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.485 0.110   12.507 1.00 21.68 ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.761 -0.646  13.441 1.00 22.56 ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.002 -0.329  10.599 1.00 24.47 ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.889 0.269   9.497  1.00 30.35 ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.261 -0.770  8.480  1.00 36.45 ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.112 -1.630  8.720  1.00 35.73 ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.598 -0.738  7.333  1.00 38.22 ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.232 0.441   12.170 1.00 18.49 ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.063 -0.040  12.890 1.00 18.57 ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.466 -1.302  12.312 1.00 16.63 ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.786 -1.692  11.174 1.00 18.17 ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.522 -1.905  13.089 1.00 16.38 ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.923 -3.197  12.703 1.00 16.68 ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.479 -3.146  12.256 1.00 16.92 ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.940 -4.184  11.837 1.00 17.72 ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.083 -4.231  13.813 1.00 17.82 ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.797 -4.643  14.187 1.00 21.40 ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.818 -2.006  12.401 1.00 15.14 ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.430 -1.908  11.957 1.00 14.10 ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.356 -1.841  10.440 1.00 15.97 ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.256 -1.287  9.791  1.00 17.21 ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.789 -0.666  12.580 1.00 13.80 ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.695 -0.718  14.096 1.00 15.50 ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.334 -1.810  14.636 1.00 15.51 ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.899 0.334   14.748 1.00 15.87 ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.325 -2.419  9.862  1.00 16.85 ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 22.059 -2.318  8.407  1.00 17.68 ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.710 -1.611  8.223  1.00 16.57 ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.803 -1.773  9.051  1.00 17.85 ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 22.033 -3.666  7.749  1.00 22.00 ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 20.971 -4.407  8.278  1.00 27.16 ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 23.378 -4.422  7.941  1.00 23.33 ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.600 -0.750  7.206  1.00 15.68 ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.377 -0.009  6.978  1.00 14.62 ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.407 -0.779  6.082  1.00 14.91 ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.792 -1.313  5.020  1.00 15.84 ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.698 1.394   6.385  1.00 14.59 ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.797 2.138   7.161  1.00 15.42 ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.433 2.287   6.234  1.00 14.95 ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.392 2.460   8.633  1.00 16.42 ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.137 -0.794  6.451  1.00 14.20 ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.065 -1.397  5.659  1.00 14.45 ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.793 -0.545  4.416  1.00 15.75 ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.782 0.692   4.470  1.00 15.78 ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.797 -1.452  6.495  1.00 14.63 ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.574 -1.218  3.274  1.00 17.19 ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.243 -0.536  2.023  1.00 18.26 ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 13.951 -1.215  1.537  1.00 19.98 ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 13.986 -2.185  0.767  1.00 22.26 ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.417 -0.630  1.006  1.00 18.49 ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.745 -0.076  1.535  1.00 18.25 ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.755 1.448   1.809  1.00 17.09 ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.073 1.922   2.317  1.00 16.34 ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.270 3.080   2.937  1.00 18.65 ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.273 3.933   3.098  1.00 17.46 ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.464 3.376   3.442  1.00 20.88 ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.821 -0.691  2.008  1.00 19.55 ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.515 -1.336  1.868  1.00 20.14 ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.373 -0.331  2.162  1.00 20.74 ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.548 0.810   2.567  1.00 22.95 ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.478 -2.485  2.873  1.00 18.57 ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.410 -1.906  4.580  1.00 18.64 ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 9.087  -0.851  2.075  1.00 23.56 ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 7.907  -0.080  2.427  1.00 26.54 ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.126  -0.836  3.535  1.00 25.51 ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.905  -0.720  3.620  1.00 26.23 ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 6.983  0.193   1.210  1.00 32.50 ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.430  -1.061  0.559  1.00 41.57 ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 6.843  -2.177  0.958  1.00 43.13 ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.594  -0.930  -0.370 1.00 46.11 ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.825  -1.560  4.435  1.00 21.71 ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.156  -2.203  5.591  1.00 19.37 ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.420  -1.167  6.422  1.00 20.26 ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.870  -0.017  6.607  1.00 20.10 ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.169  -2.929  6.477  1.00 19.80 ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.853  -4.470  5.819  1.00 20.32 ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.272  -1.598  6.951  1.00 17.68 ? 59  GLN   A N   1 
ATOM   411  C  CA  A GLN   A 1 53  ? 4.433  -0.828  7.886  0.50 16.89 ? 59  GLN   A CA  1 
ATOM   412  C  CA  B GLN   A 1 53  ? 4.541  -0.768  7.854  0.50 17.70 ? 59  GLN   A CA  1 
ATOM   413  C  C   . GLN   A 1 53  ? 4.226  -1.565  9.172  1.00 16.21 ? 59  GLN   A C   1 
ATOM   414  O  O   . GLN   A 1 53  ? 3.392  -1.178  9.957  1.00 16.25 ? 59  GLN   A O   1 
ATOM   415  C  CB  A GLN   A 1 53  ? 3.067  -0.356  7.329  0.50 17.11 ? 59  GLN   A CB  1 
ATOM   416  C  CB  B GLN   A 1 53  ? 3.379  -0.101  7.101  0.50 19.91 ? 59  GLN   A CB  1 
ATOM   417  C  CG  A GLN   A 1 53  ? 3.150  0.887   6.423  0.50 16.55 ? 59  GLN   A CG  1 
ATOM   418  C  CG  B GLN   A 1 53  ? 3.915  0.740   5.871  0.50 21.13 ? 59  GLN   A CG  1 
ATOM   419  C  CD  A GLN   A 1 53  ? 1.772  1.421   6.030  0.50 19.01 ? 59  GLN   A CD  1 
ATOM   420  C  CD  B GLN   A 1 53  ? 4.946  1.828   6.249  0.50 21.55 ? 59  GLN   A CD  1 
ATOM   421  O  OE1 A GLN   A 1 53  ? 1.274  1.211   4.911  0.50 22.00 ? 59  GLN   A OE1 1 
ATOM   422  O  OE1 B GLN   A 1 53  ? 5.935  2.191   5.524  0.50 19.65 ? 59  GLN   A OE1 1 
ATOM   423  N  NE2 A GLN   A 1 53  ? 1.120  2.124   6.936  0.50 16.93 ? 59  GLN   A NE2 1 
ATOM   424  N  NE2 B GLN   A 1 53  ? 4.752  2.392   7.429  0.50 22.34 ? 59  GLN   A NE2 1 
ATOM   425  N  N   . THR   A 1 54  ? 4.987  -2.669  9.408  1.00 14.72 ? 60  THR   A N   1 
ATOM   426  C  CA  . THR   A 1 54  ? 4.987  -3.386  10.656 1.00 15.04 ? 60  THR   A CA  1 
ATOM   427  C  C   . THR   A 1 54  ? 6.464  -3.636  11.063 1.00 13.65 ? 60  THR   A C   1 
ATOM   428  O  O   . THR   A 1 54  ? 7.327  -3.838  10.193 1.00 15.21 ? 60  THR   A O   1 
ATOM   429  C  CB  . THR   A 1 54  ? 4.228  -4.693  10.665 1.00 17.81 ? 60  THR   A CB  1 
ATOM   430  O  OG1 . THR   A 1 54  ? 4.855  -5.620  9.817  1.00 23.85 ? 60  THR   A OG1 1 
ATOM   431  C  CG2 . THR   A 1 54  ? 2.802  -4.563  10.219 1.00 18.04 ? 60  THR   A CG2 1 
ATOM   432  N  N   . GLY   A 1 55  ? 6.716  -3.561  12.346 1.00 12.74 ? 61  GLY   A N   1 
ATOM   433  C  CA  . GLY   A 1 55  ? 8.085  -3.788  12.839 1.00 12.86 ? 61  GLY   A CA  1 
ATOM   434  C  C   . GLY   A 1 55  ? 8.081  -3.835  14.353 1.00 12.56 ? 61  GLY   A C   1 
ATOM   435  O  O   . GLY   A 1 55  ? 7.050  -4.067  14.983 1.00 13.03 ? 61  GLY   A O   1 
ATOM   436  N  N   . VAL   A 1 56  ? 9.265  -3.635  14.953 1.00 11.90 ? 62  VAL   A N   1 
ATOM   437  C  CA  . VAL   A 1 56  ? 9.452  -3.711  16.397 1.00 11.36 ? 62  VAL   A CA  1 
ATOM   438  C  C   . VAL   A 1 56  ? 10.323 -2.544  16.842 1.00 10.79 ? 62  VAL   A C   1 
ATOM   439  O  O   . VAL   A 1 56  ? 11.300 -2.240  16.159 1.00 12.17 ? 62  VAL   A O   1 
ATOM   440  C  CB  . VAL   A 1 56  ? 10.165 -5.054  16.734 1.00 12.62 ? 62  VAL   A CB  1 
ATOM   441  C  CG1 . VAL   A 1 56  ? 10.533 -5.140  18.208 1.00 14.49 ? 62  VAL   A CG1 1 
ATOM   442  C  CG2 . VAL   A 1 56  ? 9.258  -6.249  16.369 1.00 13.17 ? 62  VAL   A CG2 1 
ATOM   443  N  N   . TYR   A 1 57  ? 9.940  -1.859  17.938 1.00 11.49 ? 63  TYR   A N   1 
ATOM   444  C  CA  . TYR   A 1 57  ? 10.806 -0.767  18.411 1.00 10.90 ? 63  TYR   A CA  1 
ATOM   445  C  C   . TYR   A 1 57  ? 11.231 -0.985  19.864 1.00 11.54 ? 63  TYR   A C   1 
ATOM   446  O  O   . TYR   A 1 57  ? 10.515 -1.628  20.656 1.00 12.37 ? 63  TYR   A O   1 
ATOM   447  C  CB  . TYR   A 1 57  ? 10.107 0.638   18.260 1.00 11.35 ? 63  TYR   A CB  1 
ATOM   448  C  CG  . TYR   A 1 57  ? 9.136  1.010   19.372 1.00 11.56 ? 63  TYR   A CG  1 
ATOM   449  C  CD1 . TYR   A 1 57  ? 7.845  0.494   19.393 1.00 12.86 ? 63  TYR   A CD1 1 
ATOM   450  C  CD2 . TYR   A 1 57  ? 9.490  1.923   20.355 1.00 12.13 ? 63  TYR   A CD2 1 
ATOM   451  C  CE1 . TYR   A 1 57  ? 6.933  0.845   20.393 1.00 13.44 ? 63  TYR   A CE1 1 
ATOM   452  C  CE2 . TYR   A 1 57  ? 8.583  2.299   21.360 1.00 12.77 ? 63  TYR   A CE2 1 
ATOM   453  C  CZ  . TYR   A 1 57  ? 7.307  1.757   21.355 1.00 13.48 ? 63  TYR   A CZ  1 
ATOM   454  O  OH  . TYR   A 1 57  ? 6.382  2.079   22.339 1.00 15.43 ? 63  TYR   A OH  1 
ATOM   455  N  N   . TYR   A 1 58  ? 12.357 -0.368  20.237 1.00 11.21 ? 64  TYR   A N   1 
ATOM   456  C  CA  . TYR   A 1 58  ? 12.820 -0.408  21.621 1.00 11.14 ? 64  TYR   A CA  1 
ATOM   457  C  C   . TYR   A 1 58  ? 12.354 0.802   22.425 1.00 11.45 ? 64  TYR   A C   1 
ATOM   458  O  O   . TYR   A 1 58  ? 12.583 1.951   22.024 1.00 11.51 ? 64  TYR   A O   1 
ATOM   459  C  CB  . TYR   A 1 58  ? 14.364 -0.491  21.677 1.00 12.63 ? 64  TYR   A CB  1 
ATOM   460  C  CG  . TYR   A 1 58  ? 14.839 -0.631  23.103 1.00 12.74 ? 64  TYR   A CG  1 
ATOM   461  C  CD1 . TYR   A 1 58  ? 14.518 -1.743  23.849 1.00 13.26 ? 64  TYR   A CD1 1 
ATOM   462  C  CD2 . TYR   A 1 58  ? 15.602 0.375   23.715 1.00 12.49 ? 64  TYR   A CD2 1 
ATOM   463  C  CE1 . TYR   A 1 58  ? 14.887 -1.841  25.188 1.00 14.45 ? 64  TYR   A CE1 1 
ATOM   464  C  CE2 . TYR   A 1 58  ? 15.987 0.283   25.045 1.00 13.15 ? 64  TYR   A CE2 1 
ATOM   465  C  CZ  . TYR   A 1 58  ? 15.665 -0.850  25.757 1.00 14.29 ? 64  TYR   A CZ  1 
ATOM   466  O  OH  . TYR   A 1 58  ? 16.040 -0.952  27.088 1.00 17.46 ? 64  TYR   A OH  1 
ATOM   467  N  N   . CYS   A 1 59  ? 11.727 0.509   23.565 1.00 11.44 ? 65  CYS   A N   1 
ATOM   468  C  CA  . CYS   A 1 59  ? 11.197 1.517   24.503 1.00 12.06 ? 65  CYS   A CA  1 
ATOM   469  C  C   . CYS   A 1 59  ? 12.039 1.485   25.789 1.00 12.48 ? 65  CYS   A C   1 
ATOM   470  O  O   . CYS   A 1 59  ? 11.854 0.573   26.640 1.00 12.79 ? 65  CYS   A O   1 
ATOM   471  C  CB  . CYS   A 1 59  ? 9.741  1.208   24.801 1.00 12.88 ? 65  CYS   A CB  1 
ATOM   472  S  SG  . CYS   A 1 59  ? 9.014  2.311   26.045 1.00 13.23 ? 65  CYS   A SG  1 
ATOM   473  N  N   . SER   A 1 60  ? 12.952 2.457   25.961 1.00 12.79 ? 66  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 60  ? 13.849 2.427   27.117 1.00 13.51 ? 66  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 60  ? 13.137 2.608   28.468 1.00 13.21 ? 66  SER   A C   1 
ATOM   476  O  O   . SER   A 1 60  ? 13.547 1.989   29.456 1.00 14.40 ? 66  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 60  ? 14.944 3.466   26.961 1.00 15.98 ? 66  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 60  ? 14.536 4.807   27.072 1.00 19.56 ? 66  SER   A OG  1 
ATOM   479  N  N   . SER   A 1 61  ? 11.987 3.374   28.471 1.00 12.33 ? 67  SER   A N   1 
ATOM   480  C  CA  . SER   A 1 61  ? 11.228 3.580   29.697 1.00 12.17 ? 67  SER   A CA  1 
ATOM   481  C  C   . SER   A 1 61  ? 10.417 2.354   30.140 1.00 13.00 ? 67  SER   A C   1 
ATOM   482  O  O   . SER   A 1 61  ? 9.792  2.380   31.186 1.00 13.29 ? 67  SER   A O   1 
ATOM   483  C  CB  . SER   A 1 61  ? 10.324 4.798   29.557 1.00 12.70 ? 67  SER   A CB  1 
ATOM   484  O  OG  . SER   A 1 61  ? 9.307  4.576   28.603 1.00 13.39 ? 67  SER   A OG  1 
ATOM   485  N  N   . ARG   A 1 62  ? 10.481 1.263   29.369 1.00 12.99 ? 68  ARG   A N   1 
ATOM   486  C  CA  . ARG   A 1 62  ? 9.897  -0.035  29.724 1.00 13.64 ? 68  ARG   A CA  1 
ATOM   487  C  C   . ARG   A 1 62  ? 10.924 -1.165  29.677 1.00 15.08 ? 68  ARG   A C   1 
ATOM   488  O  O   . ARG   A 1 62  ? 10.562 -2.321  29.950 1.00 15.49 ? 68  ARG   A O   1 
ATOM   489  C  CB  . ARG   A 1 62  ? 8.690  -0.367  28.824 1.00 14.17 ? 68  ARG   A CB  1 
ATOM   490  C  CG  . ARG   A 1 62  ? 7.553  0.630   28.936 1.00 13.93 ? 68  ARG   A CG  1 
ATOM   491  C  CD  . ARG   A 1 62  ? 6.796  0.357   30.222 1.00 14.43 ? 68  ARG   A CD  1 
ATOM   492  N  NE  . ARG   A 1 62  ? 5.656  1.272   30.365 1.00 16.18 ? 68  ARG   A NE  1 
ATOM   493  C  CZ  . ARG   A 1 62  ? 5.696  2.431   31.015 1.00 14.64 ? 68  ARG   A CZ  1 
ATOM   494  N  NH1 . ARG   A 1 62  ? 6.834  2.849   31.591 1.00 16.25 ? 68  ARG   A NH1 1 
ATOM   495  N  NH2 . ARG   A 1 62  ? 4.590  3.177   31.134 1.00 16.32 ? 68  ARG   A NH2 1 
ATOM   496  N  N   . ARG   A 1 63  ? 12.150 -0.904  29.213 1.00 14.63 ? 69  ARG   A N   1 
ATOM   497  C  CA  . ARG   A 1 63  ? 13.133 -1.975  28.916 1.00 14.98 ? 69  ARG   A CA  1 
ATOM   498  C  C   . ARG   A 1 63  ? 12.494 -3.099  28.053 1.00 16.58 ? 69  ARG   A C   1 
ATOM   499  O  O   . ARG   A 1 63  ? 12.640 -4.305  28.337 1.00 18.17 ? 69  ARG   A O   1 
ATOM   500  C  CB  . ARG   A 1 63  ? 13.781 -2.578  30.168 1.00 17.81 ? 69  ARG   A CB  1 
ATOM   501  C  CG  . ARG   A 1 63  ? 14.722 -1.608  30.816 1.00 17.87 ? 69  ARG   A CG  1 
ATOM   502  C  CD  . ARG   A 1 63  ? 15.596 -2.409  31.782 1.00 18.76 ? 69  ARG   A CD  1 
ATOM   503  N  NE  . ARG   A 1 63  ? 16.383 -1.480  32.575 1.00 19.68 ? 69  ARG   A NE  1 
ATOM   504  C  CZ  . ARG   A 1 63  ? 16.067 -1.084  33.807 1.00 17.74 ? 69  ARG   A CZ  1 
ATOM   505  N  NH1 . ARG   A 1 63  ? 14.996 -1.589  34.429 1.00 19.31 ? 69  ARG   A NH1 1 
ATOM   506  N  NH2 . ARG   A 1 63  ? 16.846 -0.233  34.453 1.00 19.53 ? 69  ARG   A NH2 1 
ATOM   507  N  N   . LYS   A 1 64  ? 11.772 -2.707  27.027 1.00 15.09 ? 70  LYS   A N   1 
ATOM   508  C  CA  . LYS   A 1 64  ? 11.034 -3.683  26.237 1.00 15.08 ? 70  LYS   A CA  1 
ATOM   509  C  C   . LYS   A 1 64  ? 11.016 -3.311  24.791 1.00 14.74 ? 70  LYS   A C   1 
ATOM   510  O  O   . LYS   A 1 64  ? 10.939 -2.124  24.442 1.00 14.51 ? 70  LYS   A O   1 
ATOM   511  C  CB  . LYS   A 1 64  ? 9.572  -3.779  26.760 1.00 19.50 ? 70  LYS   A CB  1 
ATOM   512  C  CG  . LYS   A 1 64  ? 9.406  -4.688  27.991 1.00 28.66 ? 70  LYS   A CG  1 
ATOM   513  C  CD  . LYS   A 1 64  ? 7.946  -5.021  28.243 1.00 38.22 ? 70  LYS   A CD  1 
ATOM   514  C  CE  . LYS   A 1 64  ? 7.771  -5.843  29.503 1.00 44.31 ? 70  LYS   A CE  1 
ATOM   515  N  NZ  . LYS   A 1 64  ? 8.420  -5.197  30.682 1.00 48.21 ? 70  LYS   A NZ  1 
ATOM   516  N  N   . HIS   A 1 65  ? 11.005 -4.331  23.928 1.00 13.84 ? 71  HIS   A N   1 
ATOM   517  C  CA  . HIS   A 1 65  ? 10.784 -4.186  22.486 1.00 13.31 ? 71  HIS   A CA  1 
ATOM   518  C  C   . HIS   A 1 65  ? 9.327  -4.541  22.198 1.00 14.33 ? 71  HIS   A C   1 
ATOM   519  O  O   . HIS   A 1 65  ? 8.828  -5.586  22.647 1.00 17.28 ? 71  HIS   A O   1 
ATOM   520  C  CB  . HIS   A 1 65  ? 11.691 -5.154  21.698 1.00 12.46 ? 71  HIS   A CB  1 
ATOM   521  C  CG  . HIS   A 1 65  ? 13.147 -4.820  21.820 1.00 13.61 ? 71  HIS   A CG  1 
ATOM   522  N  ND1 . HIS   A 1 65  ? 13.872 -4.147  20.832 1.00 16.87 ? 71  HIS   A ND1 1 
ATOM   523  C  CD2 . HIS   A 1 65  ? 13.992 -5.128  22.833 1.00 13.27 ? 71  HIS   A CD2 1 
ATOM   524  C  CE1 . HIS   A 1 65  ? 15.146 -4.099  21.277 1.00 14.64 ? 71  HIS   A CE1 1 
ATOM   525  N  NE2 . HIS   A 1 65  ? 15.238 -4.659  22.472 1.00 17.26 ? 71  HIS   A NE2 1 
ATOM   526  N  N   . TYR   A 1 66  ? 8.621  -3.662  21.481 1.00 12.38 ? 72  TYR   A N   1 
ATOM   527  C  CA  . TYR   A 1 66  ? 7.196  -3.850  21.181 1.00 13.35 ? 72  TYR   A CA  1 
ATOM   528  C  C   . TYR   A 1 66  ? 6.966  -3.958  19.697 1.00 12.46 ? 72  TYR   A C   1 
ATOM   529  O  O   . TYR   A 1 66  ? 7.457  -3.120  18.923 1.00 12.31 ? 72  TYR   A O   1 
ATOM   530  C  CB  . TYR   A 1 66  ? 6.392  -2.604  21.675 1.00 13.45 ? 72  TYR   A CB  1 
ATOM   531  C  CG  . TYR   A 1 66  ? 6.310  -2.422  23.177 1.00 14.28 ? 72  TYR   A CG  1 
ATOM   532  C  CD1 . TYR   A 1 66  ? 5.477  -3.228  23.957 1.00 15.68 ? 72  TYR   A CD1 1 
ATOM   533  C  CD2 . TYR   A 1 66  ? 7.068  -1.461  23.818 1.00 14.89 ? 72  TYR   A CD2 1 
ATOM   534  C  CE1 . TYR   A 1 66  ? 5.352  -3.031  25.326 1.00 16.28 ? 72  TYR   A CE1 1 
ATOM   535  C  CE2 . TYR   A 1 66  ? 6.972  -1.264  25.193 1.00 15.56 ? 72  TYR   A CE2 1 
ATOM   536  C  CZ  . TYR   A 1 66  ? 6.111  -2.052  25.942 1.00 16.10 ? 72  TYR   A CZ  1 
ATOM   537  O  OH  . TYR   A 1 66  ? 6.040  -1.862  27.321 1.00 18.71 ? 72  TYR   A OH  1 
ATOM   538  N  N   . PRO   A 1 67  ? 6.138  -4.932  19.277 1.00 12.77 ? 73  PRO   A N   1 
ATOM   539  C  CA  . PRO   A 1 67  ? 5.728  -4.972  17.864 1.00 13.15 ? 73  PRO   A CA  1 
ATOM   540  C  C   . PRO   A 1 67  ? 4.676  -3.894  17.584 1.00 13.92 ? 73  PRO   A C   1 
ATOM   541  O  O   . PRO   A 1 67  ? 3.729  -3.742  18.396 1.00 15.99 ? 73  PRO   A O   1 
ATOM   542  C  CB  . PRO   A 1 67  ? 5.115  -6.380  17.684 1.00 15.45 ? 73  PRO   A CB  1 
ATOM   543  C  CG  . PRO   A 1 67  ? 4.696  -6.787  19.082 1.00 16.45 ? 73  PRO   A CG  1 
ATOM   544  C  CD  . PRO   A 1 67  ? 5.587  -6.045  20.084 1.00 13.61 ? 73  PRO   A CD  1 
ATOM   545  N  N   . VAL   A 1 68  ? 4.812  -3.217  16.480 1.00 12.92 ? 74  VAL   A N   1 
ATOM   546  C  CA  . VAL   A 1 68  ? 3.850  -2.157  16.117 1.00 14.06 ? 74  VAL   A CA  1 
ATOM   547  C  C   . VAL   A 1 68  ? 3.556  -2.127  14.654 1.00 13.41 ? 74  VAL   A C   1 
ATOM   548  O  O   . VAL   A 1 68  ? 4.357  -2.488  13.814 1.00 13.95 ? 74  VAL   A O   1 
ATOM   549  C  CB  . VAL   A 1 68  ? 4.430  -0.763  16.489 1.00 16.26 ? 74  VAL   A CB  1 
ATOM   550  C  CG1 . VAL   A 1 68  ? 4.386  -0.525  18.002 1.00 17.10 ? 74  VAL   A CG1 1 
ATOM   551  C  CG2 . VAL   A 1 68  ? 5.851  -0.542  15.944 1.00 17.43 ? 74  VAL   A CG2 1 
ATOM   552  N  N   . SER   A 1 69  ? 2.360  -1.572  14.321 1.00 14.12 ? 75  SER   A N   1 
ATOM   553  C  CA  A SER   A 1 69  ? 1.995  -1.168  12.973 0.50 14.38 ? 75  SER   A CA  1 
ATOM   554  C  CA  B SER   A 1 69  ? 1.912  -1.169  13.005 0.50 14.54 ? 75  SER   A CA  1 
ATOM   555  C  C   . SER   A 1 69  ? 2.191  0.349   12.950 1.00 13.77 ? 75  SER   A C   1 
ATOM   556  O  O   . SER   A 1 69  ? 1.825  1.040   13.907 1.00 14.44 ? 75  SER   A O   1 
ATOM   557  C  CB  A SER   A 1 69  ? 0.532  -1.465  12.667 0.50 16.57 ? 75  SER   A CB  1 
ATOM   558  C  CB  B SER   A 1 69  ? 0.402  -1.378  12.898 0.50 17.40 ? 75  SER   A CB  1 
ATOM   559  O  OG  A SER   A 1 69  ? 0.250  -2.838  12.837 0.50 20.55 ? 75  SER   A OG  1 
ATOM   560  O  OG  B SER   A 1 69  ? -0.087 -0.883  11.664 0.50 21.76 ? 75  SER   A OG  1 
ATOM   561  N  N   . PHE   A 1 70  ? 2.777  0.881   11.870 1.00 14.30 ? 76  PHE   A N   1 
ATOM   562  C  CA  . PHE   A 1 70  ? 3.085  2.305   11.807 1.00 15.01 ? 76  PHE   A CA  1 
ATOM   563  C  C   . PHE   A 1 70  ? 2.697  2.897   10.478 1.00 15.15 ? 76  PHE   A C   1 
ATOM   564  O  O   . PHE   A 1 70  ? 2.626  2.190   9.462  1.00 16.16 ? 76  PHE   A O   1 
ATOM   565  C  CB  . PHE   A 1 70  ? 4.594  2.580   12.186 1.00 14.83 ? 76  PHE   A CB  1 
ATOM   566  C  CG  . PHE   A 1 70  ? 5.612  1.773   11.380 1.00 14.19 ? 76  PHE   A CG  1 
ATOM   567  C  CD1 . PHE   A 1 70  ? 6.029  0.523   11.806 1.00 14.54 ? 76  PHE   A CD1 1 
ATOM   568  C  CD2 . PHE   A 1 70  ? 6.186  2.294   10.232 1.00 14.17 ? 76  PHE   A CD2 1 
ATOM   569  C  CE1 . PHE   A 1 70  ? 6.965  -0.195  11.084 1.00 14.30 ? 76  PHE   A CE1 1 
ATOM   570  C  CE2 . PHE   A 1 70  ? 7.123  1.547   9.493  1.00 14.71 ? 76  PHE   A CE2 1 
ATOM   571  C  CZ  . PHE   A 1 70  ? 7.484  0.299   9.920  1.00 14.50 ? 76  PHE   A CZ  1 
ATOM   572  N  N   . SER   A 1 71  ? 2.392  4.207   10.456 1.00 15.64 ? 77  SER   A N   1 
ATOM   573  C  CA  . SER   A 1 71  ? 1.999  4.908   9.239  1.00 15.66 ? 77  SER   A CA  1 
ATOM   574  C  C   . SER   A 1 71  ? 3.176  5.139   8.295  1.00 15.85 ? 77  SER   A C   1 
ATOM   575  O  O   . SER   A 1 71  ? 4.346  5.006   8.689  1.00 15.71 ? 77  SER   A O   1 
ATOM   576  C  CB  . SER   A 1 71  ? 1.292  6.230   9.607  1.00 17.67 ? 77  SER   A CB  1 
ATOM   577  O  OG  . SER   A 1 71  ? 2.165  7.122   10.288 1.00 19.45 ? 77  SER   A OG  1 
ATOM   578  N  N   . LYS   A 1 72  ? 2.889  5.461   7.059  1.00 16.02 ? 78  LYS   A N   1 
ATOM   579  C  CA  . LYS   A 1 72  ? 3.933  5.780   6.098  1.00 15.95 ? 78  LYS   A CA  1 
ATOM   580  C  C   . LYS   A 1 72  ? 4.575  7.145   6.444  1.00 17.34 ? 78  LYS   A C   1 
ATOM   581  O  O   . LYS   A 1 72  ? 3.888  8.018   7.000  1.00 17.85 ? 78  LYS   A O   1 
ATOM   582  C  CB  . LYS   A 1 72  ? 3.343  5.778   4.682  1.00 18.93 ? 78  LYS   A CB  1 
ATOM   583  C  CG  . LYS   A 1 72  ? 2.919  4.378   4.264  1.00 22.65 ? 78  LYS   A CG  1 
ATOM   584  C  CD  . LYS   A 1 72  ? 2.539  4.309   2.798  1.00 29.50 ? 78  LYS   A CD  1 
ATOM   585  C  CE  . LYS   A 1 72  ? 2.224  2.900   2.354  1.00 35.48 ? 78  LYS   A CE  1 
ATOM   586  N  NZ  . LYS   A 1 72  ? 2.058  2.839   0.873  1.00 40.26 ? 78  LYS   A NZ  1 
ATOM   587  N  N   . PRO   A 1 73  ? 5.841  7.380   6.112  1.00 17.17 ? 79  PRO   A N   1 
ATOM   588  C  CA  . PRO   A 1 73  ? 6.474  8.677   6.430  1.00 16.88 ? 79  PRO   A CA  1 
ATOM   589  C  C   . PRO   A 1 73  ? 5.673  9.852   5.880  1.00 17.82 ? 79  PRO   A C   1 
ATOM   590  O  O   . PRO   A 1 73  ? 5.307  9.864   4.707  1.00 20.42 ? 79  PRO   A O   1 
ATOM   591  C  CB  . PRO   A 1 73  ? 7.865  8.568   5.785  1.00 19.38 ? 79  PRO   A CB  1 
ATOM   592  C  CG  . PRO   A 1 73  ? 8.098  7.124   5.536  1.00 22.62 ? 79  PRO   A CG  1 
ATOM   593  C  CD  . PRO   A 1 73  ? 6.763  6.451   5.412  1.00 18.24 ? 79  PRO   A CD  1 
ATOM   594  N  N   . SER   A 1 74  ? 5.403  10.817  6.735  1.00 17.69 ? 80  SER   A N   1 
ATOM   595  C  CA  . SER   A 1 74  ? 4.511  11.932  6.367  1.00 19.34 ? 80  SER   A CA  1 
ATOM   596  C  C   . SER   A 1 74  ? 4.900  13.202  7.122  1.00 18.62 ? 80  SER   A C   1 
ATOM   597  O  O   . SER   A 1 74  ? 5.726  13.176  8.031  1.00 17.88 ? 80  SER   A O   1 
ATOM   598  C  CB  . SER   A 1 74  ? 3.041  11.588  6.717  1.00 25.73 ? 80  SER   A CB  1 
ATOM   599  O  OG  . SER   A 1 74  ? 2.657  10.256  6.419  1.00 35.93 ? 80  SER   A OG  1 
ATOM   600  N  N   . LEU   A 1 75  ? 4.188  14.302  6.802  1.00 20.49 ? 81  LEU   A N   1 
ATOM   601  C  CA  . LEU   A 1 75  ? 4.357  15.597  7.422  1.00 22.54 ? 81  LEU   A CA  1 
ATOM   602  C  C   . LEU   A 1 75  ? 3.274  15.662  8.507  1.00 23.50 ? 81  LEU   A C   1 
ATOM   603  O  O   . LEU   A 1 75  ? 2.068  15.685  8.185  1.00 25.06 ? 81  LEU   A O   1 
ATOM   604  C  CB  . LEU   A 1 75  ? 4.158  16.695  6.349  1.00 24.32 ? 81  LEU   A CB  1 
ATOM   605  C  CG  . LEU   A 1 75  ? 4.475  18.112  6.736  1.00 27.54 ? 81  LEU   A CG  1 
ATOM   606  C  CD1 . LEU   A 1 75  ? 5.947  18.290  7.029  1.00 28.38 ? 81  LEU   A CD1 1 
ATOM   607  C  CD2 . LEU   A 1 75  ? 4.084  19.076  5.597  1.00 29.14 ? 81  LEU   A CD2 1 
ATOM   608  N  N   . ILE   A 1 76  ? 3.673  15.654  9.764  1.00 21.96 ? 82  ILE   A N   1 
ATOM   609  C  CA  . ILE   A 1 76  ? 2.792  15.597  10.931 1.00 23.91 ? 82  ILE   A CA  1 
ATOM   610  C  C   . ILE   A 1 76  ? 3.027  16.760  11.854 1.00 24.06 ? 82  ILE   A C   1 
ATOM   611  O  O   . ILE   A 1 76  ? 4.186  17.096  12.143 1.00 23.19 ? 82  ILE   A O   1 
ATOM   612  C  CB  . ILE   A 1 76  ? 3.081  14.297  11.691 1.00 25.28 ? 82  ILE   A CB  1 
ATOM   613  C  CG1 . ILE   A 1 76  ? 2.907  13.057  10.752 1.00 27.74 ? 82  ILE   A CG1 1 
ATOM   614  C  CG2 . ILE   A 1 76  ? 2.294  14.202  13.044 1.00 26.79 ? 82  ILE   A CG2 1 
ATOM   615  C  CD1 . ILE   A 1 76  ? 2.804  11.921  11.249 1.00 28.90 ? 82  ILE   A CD1 1 
ATOM   616  N  N   . PHE   A 1 77  ? 1.951  17.340  12.390 1.00 24.43 ? 83  PHE   A N   1 
ATOM   617  C  CA  . PHE   A 1 77  ? 2.062  18.420  13.355 1.00 25.10 ? 83  PHE   A CA  1 
ATOM   618  C  C   . PHE   A 1 77  ? 2.445  17.837  14.725 1.00 26.91 ? 83  PHE   A C   1 
ATOM   619  O  O   . PHE   A 1 77  ? 1.851  16.867  15.206 1.00 29.69 ? 83  PHE   A O   1 
ATOM   620  C  CB  . PHE   A 1 77  ? 0.718  19.171  13.492 1.00 26.35 ? 83  PHE   A CB  1 
ATOM   621  C  CG  . PHE   A 1 77  ? 0.951  20.520  14.099 1.00 28.99 ? 83  PHE   A CG  1 
ATOM   622  C  CD1 . PHE   A 1 77  ? 1.629  21.503  13.400 1.00 31.71 ? 83  PHE   A CD1 1 
ATOM   623  C  CD2 . PHE   A 1 77  ? 0.555  20.785  15.390 1.00 32.37 ? 83  PHE   A CD2 1 
ATOM   624  C  CE1 . PHE   A 1 77  ? 1.868  22.739  13.966 1.00 34.31 ? 83  PHE   A CE1 1 
ATOM   625  C  CE2 . PHE   A 1 77  ? 0.775  22.032  15.952 1.00 33.34 ? 83  PHE   A CE2 1 
ATOM   626  C  CZ  . PHE   A 1 77  ? 1.420  23.006  15.233 1.00 34.42 ? 83  PHE   A CZ  1 
ATOM   627  N  N   . VAL   A 1 78  ? 3.527  18.359  15.303 1.00 24.17 ? 84  VAL   A N   1 
ATOM   628  C  CA  . VAL   A 1 78  ? 4.024  17.922  16.597 1.00 22.59 ? 84  VAL   A CA  1 
ATOM   629  C  C   . VAL   A 1 78  ? 3.931  19.119  17.563 1.00 21.99 ? 84  VAL   A C   1 
ATOM   630  O  O   . VAL   A 1 78  ? 4.421  20.196  17.234 1.00 22.54 ? 84  VAL   A O   1 
ATOM   631  C  CB  . VAL   A 1 78  ? 5.490  17.415  16.472 1.00 21.47 ? 84  VAL   A CB  1 
ATOM   632  C  CG1 . VAL   A 1 78  ? 6.036  17.007  17.845 1.00 21.79 ? 84  VAL   A CG1 1 
ATOM   633  C  CG2 . VAL   A 1 78  ? 5.564  16.255  15.455 1.00 21.26 ? 84  VAL   A CG2 1 
ATOM   634  N  N   . GLU   A 1 79  ? 3.395  18.893  18.757 1.00 22.12 ? 85  GLU   A N   1 
ATOM   635  C  CA  . GLU   A 1 79  ? 3.244  19.968  19.733 1.00 24.20 ? 85  GLU   A CA  1 
ATOM   636  C  C   . GLU   A 1 79  ? 4.571  20.513  20.210 1.00 24.40 ? 85  GLU   A C   1 
ATOM   637  O  O   . GLU   A 1 79  ? 5.572  19.801  20.188 1.00 23.95 ? 85  GLU   A O   1 
ATOM   638  C  CB  . GLU   A 1 79  ? 2.427  19.459  20.938 1.00 28.77 ? 85  GLU   A CB  1 
ATOM   639  C  CG  . GLU   A 1 79  ? 0.970  19.177  20.598 1.00 36.52 ? 85  GLU   A CG  1 
ATOM   640  C  CD  . GLU   A 1 79  ? 0.235  20.361  20.000 1.00 46.73 ? 85  GLU   A CD  1 
ATOM   641  O  OE1 . GLU   A 1 79  ? 0.322  21.470  20.576 1.00 46.89 ? 85  GLU   A OE1 1 
ATOM   642  O  OE2 . GLU   A 1 79  ? -0.410 20.190  18.940 1.00 51.27 ? 85  GLU   A OE2 1 
ATOM   643  N  N   . ALA   A 1 80  ? 4.548  21.745  20.730 1.00 25.69 ? 86  ALA   A N   1 
ATOM   644  C  CA  . ALA   A 1 80  ? 5.730  22.417  21.278 1.00 27.31 ? 86  ALA   A CA  1 
ATOM   645  C  C   . ALA   A 1 80  ? 6.288  21.616  22.409 1.00 28.68 ? 86  ALA   A C   1 
ATOM   646  O  O   . ALA   A 1 80  ? 5.538  21.054  23.211 1.00 30.76 ? 86  ALA   A O   1 
ATOM   647  C  CB  . ALA   A 1 80  ? 5.366  23.804  21.794 1.00 28.58 ? 86  ALA   A CB  1 
ATOM   648  N  N   . SER   A 1 81  ? 7.610  21.540  22.467 1.00 27.54 ? 87  SER   A N   1 
ATOM   649  C  CA  . SER   A 1 81  ? 8.316  20.843  23.536 1.00 26.55 ? 87  SER   A CA  1 
ATOM   650  C  C   . SER   A 1 81  ? 9.481  21.774  23.967 1.00 26.12 ? 87  SER   A C   1 
ATOM   651  O  O   . SER   A 1 81  ? 9.597  22.906  23.480 1.00 28.43 ? 87  SER   A O   1 
ATOM   652  C  CB  . SER   A 1 81  ? 8.890  19.529  23.025 1.00 26.35 ? 87  SER   A CB  1 
ATOM   653  O  OG  . SER   A 1 81  ? 9.936  19.761  22.082 1.00 24.82 ? 87  SER   A OG  1 
ATOM   654  N  N   . GLU   A 1 82  ? 10.343 21.294  24.868 1.00 26.88 ? 88  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 82  ? 11.527 22.074  25.247 1.00 27.05 ? 88  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 82  ? 12.589 22.052  24.133 1.00 24.13 ? 88  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 82  ? 13.490 22.881  24.196 1.00 23.79 ? 88  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 82  ? 12.116 21.629  26.596 1.00 31.09 ? 88  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 82  ? 12.857 20.313  26.561 1.00 36.05 ? 88  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 82  ? 13.564 20.019  27.867 1.00 47.41 ? 88  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 82  ? 12.982 19.291  28.703 1.00 49.58 ? 88  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 82  ? 14.697 20.521  28.060 1.00 50.80 ? 88  GLU   A OE2 1 
ATOM   663  N  N   . TYR   A 1 83  ? 12.441 21.202  23.077 1.00 22.38 ? 89  TYR   A N   1 
ATOM   664  C  CA  . TYR   A 1 83  ? 13.425 21.136  21.973 1.00 20.38 ? 89  TYR   A CA  1 
ATOM   665  C  C   . TYR   A 1 83  ? 12.997 21.804  20.692 1.00 19.75 ? 89  TYR   A C   1 
ATOM   666  O  O   . TYR   A 1 83  ? 13.871 22.254  19.929 1.00 19.97 ? 89  TYR   A O   1 
ATOM   667  C  CB  . TYR   A 1 83  ? 13.760 19.679  21.675 1.00 20.29 ? 89  TYR   A CB  1 
ATOM   668  C  CG  . TYR   A 1 83  ? 14.426 19.020  22.856 1.00 20.21 ? 89  TYR   A CG  1 
ATOM   669  C  CD1 . TYR   A 1 83  ? 15.745 19.295  23.175 1.00 21.62 ? 89  TYR   A CD1 1 
ATOM   670  C  CD2 . TYR   A 1 83  ? 13.713 18.183  23.705 1.00 23.87 ? 89  TYR   A CD2 1 
ATOM   671  C  CE1 . TYR   A 1 83  ? 16.381 18.659  24.232 1.00 24.15 ? 89  TYR   A CE1 1 
ATOM   672  C  CE2 . TYR   A 1 83  ? 14.334 17.550  24.780 1.00 25.75 ? 89  TYR   A CE2 1 
ATOM   673  C  CZ  . TYR   A 1 83  ? 15.659 17.816  25.060 1.00 26.96 ? 89  TYR   A CZ  1 
ATOM   674  O  OH  . TYR   A 1 83  ? 16.297 17.183  26.109 1.00 31.06 ? 89  TYR   A OH  1 
ATOM   675  N  N   . TYR   A 1 84  ? 11.668 21.853  20.412 1.00 20.49 ? 90  TYR   A N   1 
ATOM   676  C  CA  . TYR   A 1 84  ? 11.172 22.490  19.186 1.00 20.56 ? 90  TYR   A CA  1 
ATOM   677  C  C   . TYR   A 1 84  ? 9.852  23.220  19.492 1.00 22.12 ? 90  TYR   A C   1 
ATOM   678  O  O   . TYR   A 1 84  ? 9.071  22.718  20.315 1.00 22.72 ? 90  TYR   A O   1 
ATOM   679  C  CB  . TYR   A 1 84  ? 10.829 21.431  18.101 1.00 19.28 ? 90  TYR   A CB  1 
ATOM   680  C  CG  . TYR   A 1 84  ? 12.008 20.622  17.577 1.00 17.40 ? 90  TYR   A CG  1 
ATOM   681  C  CD1 . TYR   A 1 84  ? 12.952 21.196  16.739 1.00 17.93 ? 90  TYR   A CD1 1 
ATOM   682  C  CD2 . TYR   A 1 84  ? 12.183 19.293  17.943 1.00 17.11 ? 90  TYR   A CD2 1 
ATOM   683  C  CE1 . TYR   A 1 84  ? 14.020 20.453  16.242 1.00 16.84 ? 90  TYR   A CE1 1 
ATOM   684  C  CE2 . TYR   A 1 84  ? 13.256 18.549  17.480 1.00 16.79 ? 90  TYR   A CE2 1 
ATOM   685  C  CZ  . TYR   A 1 84  ? 14.193 19.146  16.663 1.00 16.25 ? 90  TYR   A CZ  1 
ATOM   686  O  OH  . TYR   A 1 84  ? 15.264 18.421  16.189 1.00 16.68 ? 90  TYR   A OH  1 
ATOM   687  N  N   . PRO   A 1 85  ? 9.558  24.317  18.768 1.00 23.80 ? 91  PRO   A N   1 
ATOM   688  C  CA  . PRO   A 1 85  ? 8.213  24.920  18.861 1.00 24.81 ? 91  PRO   A CA  1 
ATOM   689  C  C   . PRO   A 1 85  ? 7.201  23.972  18.180 1.00 26.26 ? 91  PRO   A C   1 
ATOM   690  O  O   . PRO   A 1 85  ? 7.597  22.985  17.509 1.00 26.45 ? 91  PRO   A O   1 
ATOM   691  C  CB  . PRO   A 1 85  ? 8.367  26.240  18.077 1.00 26.63 ? 91  PRO   A CB  1 
ATOM   692  C  CG  . PRO   A 1 85  ? 9.393  25.946  17.072 1.00 26.72 ? 91  PRO   A CG  1 
ATOM   693  C  CD  . PRO   A 1 85  ? 10.381 24.971  17.727 1.00 24.50 ? 91  PRO   A CD  1 
ATOM   694  N  N   . ALA   A 1 86  ? 5.891  24.268  18.279 1.00 27.32 ? 92  ALA   A N   1 
ATOM   695  C  CA  . ALA   A 1 86  ? 4.883  23.431  17.600 1.00 27.62 ? 92  ALA   A CA  1 
ATOM   696  C  C   . ALA   A 1 86  ? 5.124  23.652  16.097 1.00 27.38 ? 92  ALA   A C   1 
ATOM   697  O  O   . ALA   A 1 86  ? 5.399  24.778  15.670 1.00 29.42 ? 92  ALA   A O   1 
ATOM   698  C  CB  . ALA   A 1 86  ? 3.470  23.872  18.013 1.00 28.00 ? 92  ALA   A CB  1 
ATOM   699  N  N   . ARG   A 1 87  ? 5.220  22.562  15.338 1.00 25.55 ? 93  ARG   A N   1 
ATOM   700  C  CA  . ARG   A 1 87  ? 5.618  22.663  13.943 1.00 24.98 ? 93  ARG   A CA  1 
ATOM   701  C  C   . ARG   A 1 87  ? 5.259  21.381  13.213 1.00 25.76 ? 93  ARG   A C   1 
ATOM   702  O  O   . ARG   A 1 87  ? 4.833  20.399  13.836 1.00 26.39 ? 93  ARG   A O   1 
ATOM   703  C  CB  . ARG   A 1 87  ? 7.138  22.860  13.884 1.00 25.22 ? 93  ARG   A CB  1 
ATOM   704  C  CG  . ARG   A 1 87  ? 7.899  21.502  14.108 1.00 25.62 ? 93  ARG   A CG  1 
ATOM   705  C  CD  . ARG   A 1 87  ? 9.276  21.702  14.617 1.00 25.38 ? 93  ARG   A CD  1 
ATOM   706  N  NE  . ARG   A 1 87  ? 10.215 20.628  14.263 1.00 24.31 ? 93  ARG   A NE  1 
ATOM   707  C  CZ  . ARG   A 1 87  ? 10.273 19.409  14.773 1.00 26.91 ? 93  ARG   A CZ  1 
ATOM   708  N  NH1 . ARG   A 1 87  ? 9.330  18.985  15.638 1.00 25.57 ? 93  ARG   A NH1 1 
ATOM   709  N  NH2 . ARG   A 1 87  ? 11.247 18.576  14.393 1.00 21.55 ? 93  ARG   A NH2 1 
ATOM   710  N  N   . TYR   A 1 88  ? 5.497  21.373  11.896 1.00 25.74 ? 94  TYR   A N   1 
ATOM   711  C  CA  . TYR   A 1 88  ? 5.324  20.181  11.118 1.00 26.01 ? 94  TYR   A CA  1 
ATOM   712  C  C   . TYR   A 1 88  ? 6.668  19.496  11.013 1.00 22.98 ? 94  TYR   A C   1 
ATOM   713  O  O   . TYR   A 1 88  ? 7.652  20.094  10.563 1.00 23.96 ? 94  TYR   A O   1 
ATOM   714  C  CB  . TYR   A 1 88  ? 4.846  20.529  9.729  1.00 26.60 ? 94  TYR   A CB  1 
ATOM   715  C  CG  . TYR   A 1 88  ? 3.371  20.833  9.741  1.00 28.07 ? 94  TYR   A CG  1 
ATOM   716  C  CD1 . TYR   A 1 88  ? 2.431  19.812  9.765  1.00 28.73 ? 94  TYR   A CD1 1 
ATOM   717  C  CD2 . TYR   A 1 88  ? 2.911  22.141  9.835  1.00 30.17 ? 94  TYR   A CD2 1 
ATOM   718  C  CE1 . TYR   A 1 88  ? 1.072  20.086  9.808  1.00 30.92 ? 94  TYR   A CE1 1 
ATOM   719  C  CE2 . TYR   A 1 88  ? 1.553  22.424  9.882  1.00 31.48 ? 94  TYR   A CE2 1 
ATOM   720  C  CZ  . TYR   A 1 88  ? 0.640  21.391  9.910  1.00 32.57 ? 94  TYR   A CZ  1 
ATOM   721  O  OH  . TYR   A 1 88  ? -0.702 21.656  9.950  1.00 35.70 ? 94  TYR   A OH  1 
ATOM   722  N  N   . GLN   A 1 89  ? 6.724  18.236  11.467 1.00 20.08 ? 95  GLN   A N   1 
ATOM   723  C  CA  . GLN   A 1 89  ? 7.941  17.414  11.343 1.00 18.65 ? 95  GLN   A CA  1 
ATOM   724  C  C   . GLN   A 1 89  ? 7.734  16.522  10.111 1.00 18.54 ? 95  GLN   A C   1 
ATOM   725  O  O   . GLN   A 1 89  ? 6.653  15.926  9.938  1.00 19.12 ? 95  GLN   A O   1 
ATOM   726  C  CB  . GLN   A 1 89  ? 8.180  16.577  12.608 1.00 17.51 ? 95  GLN   A CB  1 
ATOM   727  C  CG  . GLN   A 1 89  ? 9.449  15.753  12.490 1.00 17.18 ? 95  GLN   A CG  1 
ATOM   728  C  CD  . GLN   A 1 89  ? 9.993  15.295  13.835 1.00 15.51 ? 95  GLN   A CD  1 
ATOM   729  O  OE1 . GLN   A 1 89  ? 10.028 16.009  14.840 1.00 17.88 ? 95  GLN   A OE1 1 
ATOM   730  N  NE2 . GLN   A 1 89  ? 10.473 14.072  13.820 1.00 16.83 ? 95  GLN   A NE2 1 
ATOM   731  N  N   . SER   A 1 90  ? 8.729  16.460  9.215  1.00 16.86 ? 96  SER   A N   1 
ATOM   732  C  CA  . SER   A 1 90  ? 8.627  15.667  8.013  1.00 16.46 ? 96  SER   A CA  1 
ATOM   733  C  C   . SER   A 1 90  ? 9.221  14.262  8.196  1.00 16.01 ? 96  SER   A C   1 
ATOM   734  O  O   . SER   A 1 90  ? 9.993  14.021  9.134  1.00 16.82 ? 96  SER   A O   1 
ATOM   735  C  CB  . SER   A 1 90  ? 9.304  16.377  6.845  1.00 19.14 ? 96  SER   A CB  1 
ATOM   736  O  OG  . SER   A 1 90  ? 10.679 16.520  7.168  1.00 21.76 ? 96  SER   A OG  1 
ATOM   737  N  N   . HIS   A 1 91  ? 8.805  13.343  7.310  1.00 16.40 ? 97  HIS   A N   1 
ATOM   738  C  CA  . HIS   A 1 91  ? 9.328  11.969  7.264  1.00 16.06 ? 97  HIS   A CA  1 
ATOM   739  C  C   . HIS   A 1 91  ? 9.080  11.267  8.611  1.00 14.66 ? 97  HIS   A C   1 
ATOM   740  O  O   . HIS   A 1 91  ? 9.889  10.403  9.022  1.00 15.32 ? 97  HIS   A O   1 
ATOM   741  C  CB  . HIS   A 1 91  ? 10.844 11.935  6.878  1.00 17.34 ? 97  HIS   A CB  1 
ATOM   742  C  CG  . HIS   A 1 91  ? 11.135 12.524  5.511  1.00 19.05 ? 97  HIS   A CG  1 
ATOM   743  N  ND1 . HIS   A 1 91  ? 11.254 11.722  4.392  1.00 21.43 ? 97  HIS   A ND1 1 
ATOM   744  C  CD2 . HIS   A 1 91  ? 11.250 13.817  5.133  1.00 21.05 ? 97  HIS   A CD2 1 
ATOM   745  C  CE1 . HIS   A 1 91  ? 11.490 12.543  3.368  1.00 22.00 ? 97  HIS   A CE1 1 
ATOM   746  N  NE2 . HIS   A 1 91  ? 11.501 13.813  3.760  1.00 22.38 ? 97  HIS   A NE2 1 
ATOM   747  N  N   . LEU   A 1 92  ? 7.956  11.555  9.255  1.00 14.30 ? 98  LEU   A N   1 
ATOM   748  C  CA  . LEU   A 1 92  ? 7.613  11.004  10.564 1.00 14.25 ? 98  LEU   A CA  1 
ATOM   749  C  C   . LEU   A 1 92  ? 6.545  9.900   10.372 1.00 14.36 ? 98  LEU   A C   1 
ATOM   750  O  O   . LEU   A 1 92  ? 5.609  10.071  9.579  1.00 15.28 ? 98  LEU   A O   1 
ATOM   751  C  CB  . LEU   A 1 92  ? 7.061  12.126  11.472 1.00 16.30 ? 98  LEU   A CB  1 
ATOM   752  C  CG  . LEU   A 1 92  ? 6.778  11.703  12.967 1.00 17.67 ? 98  LEU   A CG  1 
ATOM   753  C  CD1 . LEU   A 1 92  ? 8.039  11.394  13.686 1.00 17.96 ? 98  LEU   A CD1 1 
ATOM   754  C  CD2 . LEU   A 1 92  ? 6.076  12.845  13.743 1.00 19.73 ? 98  LEU   A CD2 1 
ATOM   755  N  N   . MET   A 1 93  ? 6.661  8.812   11.118 1.00 14.87 ? 99  MET   A N   1 
ATOM   756  C  CA  . MET   A 1 93  ? 5.710  7.697   11.082 1.00 14.88 ? 99  MET   A CA  1 
ATOM   757  C  C   . MET   A 1 93  ? 5.124  7.540   12.496 1.00 14.87 ? 99  MET   A C   1 
ATOM   758  O  O   . MET   A 1 93  ? 5.893  7.564   13.468 1.00 15.54 ? 99  MET   A O   1 
ATOM   759  C  CB  . MET   A 1 93  ? 6.468  6.421   10.730 1.00 15.05 ? 99  MET   A CB  1 
ATOM   760  C  CG  . MET   A 1 93  ? 7.112  6.537   9.335  1.00 15.81 ? 99  MET   A CG  1 
ATOM   761  S  SD  . MET   A 1 93  ? 8.201  5.156   8.862  1.00 18.68 ? 99  MET   A SD  1 
ATOM   762  C  CE  . MET   A 1 93  ? 9.477  5.349   10.070 1.00 21.49 ? 99  MET   A CE  1 
ATOM   763  N  N   . LEU   A 1 94  ? 3.809  7.341   12.640 1.00 14.04 ? 100 LEU   A N   1 
ATOM   764  C  CA  . LEU   A 1 94  ? 3.216  7.191   13.967 1.00 14.79 ? 100 LEU   A CA  1 
ATOM   765  C  C   . LEU   A 1 94  ? 2.722  5.785   14.191 1.00 13.60 ? 100 LEU   A C   1 
ATOM   766  O  O   . LEU   A 1 94  ? 2.269  5.091   13.265 1.00 15.46 ? 100 LEU   A O   1 
ATOM   767  C  CB  . LEU   A 1 94  ? 1.975  8.118   14.116 1.00 17.38 ? 100 LEU   A CB  1 
ATOM   768  C  CG  . LEU   A 1 94  ? 2.210  9.591   14.058 1.00 21.32 ? 100 LEU   A CG  1 
ATOM   769  C  CD1 . LEU   A 1 94  ? 0.908  10.368  14.426 1.00 23.21 ? 100 LEU   A CD1 1 
ATOM   770  C  CD2 . LEU   A 1 94  ? 3.293  10.038  15.077 1.00 23.52 ? 100 LEU   A CD2 1 
ATOM   771  N  N   . ALA   A 1 95  ? 2.753  5.369   15.464 1.00 13.82 ? 101 ALA   A N   1 
ATOM   772  C  CA  . ALA   A 1 95  ? 2.193  4.086   15.901 1.00 13.45 ? 101 ALA   A CA  1 
ATOM   773  C  C   . ALA   A 1 95  ? 1.586  4.298   17.289 1.00 13.21 ? 101 ALA   A C   1 
ATOM   774  O  O   . ALA   A 1 95  ? 1.873  5.287   17.967 1.00 14.44 ? 101 ALA   A O   1 
ATOM   775  C  CB  . ALA   A 1 95  ? 3.313  3.009   16.022 1.00 14.37 ? 101 ALA   A CB  1 
ATOM   776  N  N   . VAL   A 1 96  ? 0.782  3.317   17.719 1.00 12.89 ? 102 VAL   A N   1 
ATOM   777  C  CA  . VAL   A 1 96  ? 0.282  3.282   19.076 1.00 13.10 ? 102 VAL   A CA  1 
ATOM   778  C  C   . VAL   A 1 96  ? 1.309  2.529   19.958 1.00 14.47 ? 102 VAL   A C   1 
ATOM   779  O  O   . VAL   A 1 96  ? 1.649  1.388   19.704 1.00 15.98 ? 102 VAL   A O   1 
ATOM   780  C  CB  . VAL   A 1 96  ? -1.066 2.574   19.119 1.00 13.56 ? 102 VAL   A CB  1 
ATOM   781  C  CG1 . VAL   A 1 96  ? -1.559 2.422   20.570 1.00 15.13 ? 102 VAL   A CG1 1 
ATOM   782  C  CG2 . VAL   A 1 96  ? -2.088 3.347   18.258 1.00 14.05 ? 102 VAL   A CG2 1 
ATOM   783  N  N   . GLY   A 1 97  ? 1.809  3.231   20.953 1.00 15.15 ? 103 GLY   A N   1 
ATOM   784  C  CA  . GLY   A 1 97  ? 2.816  2.654   21.846 1.00 16.06 ? 103 GLY   A CA  1 
ATOM   785  C  C   . GLY   A 1 97  ? 3.272  3.655   22.856 1.00 16.08 ? 103 GLY   A C   1 
ATOM   786  O  O   . GLY   A 1 97  ? 2.970  4.844   22.765 1.00 17.23 ? 103 GLY   A O   1 
ATOM   787  N  N   . HIS   A 1 98  ? 3.980  3.156   23.882 1.00 16.90 ? 104 HIS   A N   1 
ATOM   788  C  CA  . HIS   A 1 98  ? 4.478  4.022   24.921 1.00 17.70 ? 104 HIS   A CA  1 
ATOM   789  C  C   . HIS   A 1 98  ? 5.774  4.747   24.523 1.00 15.78 ? 104 HIS   A C   1 
ATOM   790  O  O   . HIS   A 1 98  ? 6.715  4.085   24.024 1.00 15.78 ? 104 HIS   A O   1 
ATOM   791  C  CB  . HIS   A 1 98  ? 4.695  3.209   26.231 1.00 17.52 ? 104 HIS   A CB  1 
ATOM   792  C  CG  . HIS   A 1 98  ? 5.085  4.092   27.359 1.00 16.61 ? 104 HIS   A CG  1 
ATOM   793  N  ND1 . HIS   A 1 98  ? 4.183  4.959   27.935 1.00 17.48 ? 104 HIS   A ND1 1 
ATOM   794  C  CD2 . HIS   A 1 98  ? 6.287  4.253   27.968 1.00 16.84 ? 104 HIS   A CD2 1 
ATOM   795  C  CE1 . HIS   A 1 98  ? 4.872  5.641   28.841 1.00 18.23 ? 104 HIS   A CE1 1 
ATOM   796  N  NE2 . HIS   A 1 98  ? 6.139  5.235   28.892 1.00 17.28 ? 104 HIS   A NE2 1 
ATOM   797  N  N   . SER   A 1 99  ? 5.872  6.047   24.741 1.00 15.76 ? 105 SER   A N   1 
ATOM   798  C  CA  . SER   A 1 99  ? 7.050  6.851   24.439 1.00 16.03 ? 105 SER   A CA  1 
ATOM   799  C  C   . SER   A 1 99  ? 6.977  8.034   25.342 1.00 19.23 ? 105 SER   A C   1 
ATOM   800  O  O   . SER   A 1 99  ? 5.989  8.795   25.259 1.00 21.06 ? 105 SER   A O   1 
ATOM   801  C  CB  . SER   A 1 99  ? 7.096  7.228   22.944 1.00 16.47 ? 105 SER   A CB  1 
ATOM   802  O  OG  . SER   A 1 99  ? 8.149  8.118   22.613 1.00 17.45 ? 105 SER   A OG  1 
ATOM   803  N  N   . GLU   A 1 100 ? 7.964  8.197   26.211 1.00 17.12 ? 106 GLU   A N   1 
ATOM   804  C  CA  . GLU   A 1 100 ? 7.942  9.310   27.136 1.00 19.26 ? 106 GLU   A CA  1 
ATOM   805  C  C   . GLU   A 1 100 ? 9.327  9.927   27.034 1.00 21.09 ? 106 GLU   A C   1 
ATOM   806  O  O   . GLU   A 1 100 ? 10.270 9.378   26.421 1.00 22.17 ? 106 GLU   A O   1 
ATOM   807  C  CB  . GLU   A 1 100 ? 7.483  8.839   28.590 1.00 19.62 ? 106 GLU   A CB  1 
ATOM   808  C  CG  . GLU   A 1 100 ? 8.478  7.903   29.192 1.00 20.31 ? 106 GLU   A CG  1 
ATOM   809  C  CD  . GLU   A 1 100 ? 8.192  7.515   30.616 1.00 19.66 ? 106 GLU   A CD  1 
ATOM   810  O  OE1 . GLU   A 1 100 ? 8.699  8.192   31.535 1.00 24.47 ? 106 GLU   A OE1 1 
ATOM   811  O  OE2 . GLU   A 1 100 ? 7.436  6.547   30.814 1.00 18.10 ? 106 GLU   A OE2 1 
ATOM   812  N  N   . PRO   A 1 101 ? 9.513  11.133  27.586 1.00 24.52 ? 107 PRO   A N   1 
ATOM   813  C  CA  . PRO   A 1 101 ? 10.824 11.771  27.519 1.00 24.24 ? 107 PRO   A CA  1 
ATOM   814  C  C   . PRO   A 1 101 ? 11.931 10.839  28.017 1.00 22.93 ? 107 PRO   A C   1 
ATOM   815  O  O   . PRO   A 1 101 ? 11.773 10.226  29.099 1.00 24.13 ? 107 PRO   A O   1 
ATOM   816  C  CB  . PRO   A 1 101 ? 10.643 12.981  28.441 1.00 25.67 ? 107 PRO   A CB  1 
ATOM   817  C  CG  . PRO   A 1 101 ? 9.222  13.328  28.271 1.00 27.01 ? 107 PRO   A CG  1 
ATOM   818  C  CD  . PRO   A 1 101 ? 8.523  11.997  28.251 1.00 25.01 ? 107 PRO   A CD  1 
ATOM   819  N  N   . GLY   A 1 102 ? 12.966 10.672  27.178 1.00 18.94 ? 108 GLY   A N   1 
ATOM   820  C  CA  . GLY   A 1 102 ? 14.099 9.757   27.349 1.00 19.06 ? 108 GLY   A CA  1 
ATOM   821  C  C   . GLY   A 1 102 ? 14.101 8.619   26.336 1.00 16.17 ? 108 GLY   A C   1 
ATOM   822  O  O   . GLY   A 1 102 ? 15.135 7.996   26.143 1.00 17.13 ? 108 GLY   A O   1 
ATOM   823  N  N   . ASP   A 1 103 ? 12.943 8.310   25.713 1.00 14.32 ? 109 ASP   A N   1 
ATOM   824  C  CA  . ASP   A 1 103 ? 12.849 7.200   24.757 1.00 13.87 ? 109 ASP   A CA  1 
ATOM   825  C  C   . ASP   A 1 103 ? 13.344 7.529   23.352 1.00 13.73 ? 109 ASP   A C   1 
ATOM   826  O  O   . ASP   A 1 103 ? 13.555 6.606   22.538 1.00 13.60 ? 109 ASP   A O   1 
ATOM   827  C  CB  . ASP   A 1 103 ? 11.386 6.656   24.652 1.00 13.60 ? 109 ASP   A CB  1 
ATOM   828  C  CG  . ASP   A 1 103 ? 11.013 5.921   25.934 1.00 14.28 ? 109 ASP   A CG  1 
ATOM   829  O  OD1 . ASP   A 1 103 ? 11.885 5.232   26.475 1.00 14.56 ? 109 ASP   A OD1 1 
ATOM   830  O  OD2 . ASP   A 1 103 ? 9.820  5.996   26.361 1.00 14.20 ? 109 ASP   A OD2 1 
ATOM   831  N  N   . CYS   A 1 104 ? 13.597 8.820   23.056 1.00 13.10 ? 110 CYS   A N   1 
ATOM   832  C  CA  . CYS   A 1 104 ? 14.134 9.159   21.707 1.00 13.68 ? 110 CYS   A CA  1 
ATOM   833  C  C   . CYS   A 1 104 ? 15.437 8.428   21.483 1.00 13.21 ? 110 CYS   A C   1 
ATOM   834  O  O   . CYS   A 1 104 ? 16.276 8.310   22.374 1.00 13.37 ? 110 CYS   A O   1 
ATOM   835  C  CB  . CYS   A 1 104 ? 14.338 10.661  21.570 1.00 13.70 ? 110 CYS   A CB  1 
ATOM   836  S  SG  . CYS   A 1 104 ? 12.786 11.582  21.368 1.00 16.69 ? 110 CYS   A SG  1 
ATOM   837  N  N   . GLY   A 1 105 ? 15.619 7.922   20.263 1.00 12.53 ? 111 GLY   A N   1 
ATOM   838  C  CA  . GLY   A 1 105 ? 16.836 7.214   19.895 1.00 12.65 ? 111 GLY   A CA  1 
ATOM   839  C  C   . GLY   A 1 105 ? 16.646 5.717   19.802 1.00 12.01 ? 111 GLY   A C   1 
ATOM   840  O  O   . GLY   A 1 105 ? 17.508 5.019   19.253 1.00 12.65 ? 111 GLY   A O   1 
ATOM   841  N  N   . GLY   A 1 106 ? 15.575 5.197   20.398 1.00 12.41 ? 112 GLY   A N   1 
ATOM   842  C  CA  . GLY   A 1 106 ? 15.318 3.766   20.301 1.00 12.16 ? 112 GLY   A CA  1 
ATOM   843  C  C   . GLY   A 1 106 ? 15.099 3.341   18.849 1.00 11.39 ? 112 GLY   A C   1 
ATOM   844  O  O   . GLY   A 1 106 ? 14.397 4.047   18.113 1.00 11.52 ? 112 GLY   A O   1 
ATOM   845  N  N   . ILE   A 1 107 ? 15.607 2.163   18.457 1.00 11.48 ? 113 ILE   A N   1 
ATOM   846  C  CA  . ILE   A 1 107 ? 15.444 1.746   17.058 1.00 11.45 ? 113 ILE   A CA  1 
ATOM   847  C  C   . ILE   A 1 107 ? 14.117 1.093   16.773 1.00 11.40 ? 113 ILE   A C   1 
ATOM   848  O  O   . ILE   A 1 107 ? 13.654 0.262   17.564 1.00 11.85 ? 113 ILE   A O   1 
ATOM   849  C  CB  . ILE   A 1 107 ? 16.621 0.788   16.733 1.00 11.75 ? 113 ILE   A CB  1 
ATOM   850  C  CG1 . ILE   A 1 107 ? 17.909 1.639   16.488 1.00 13.44 ? 113 ILE   A CG1 1 
ATOM   851  C  CG2 . ILE   A 1 107 ? 16.335 -0.100  15.479 1.00 13.20 ? 113 ILE   A CG2 1 
ATOM   852  C  CD1 . ILE   A 1 107 ? 19.178 0.812   16.296 1.00 15.93 ? 113 ILE   A CD1 1 
ATOM   853  N  N   . LEU   A 1 108 ? 13.540 1.425   15.634 1.00 10.60 ? 114 LEU   A N   1 
ATOM   854  C  CA  . LEU   A 1 108 ? 12.447 0.701   14.993 1.00 10.77 ? 114 LEU   A CA  1 
ATOM   855  C  C   . LEU   A 1 108 ? 13.072 -0.138  13.870 1.00 10.72 ? 114 LEU   A C   1 
ATOM   856  O  O   . LEU   A 1 108 ? 13.828 0.419   13.040 1.00 11.40 ? 114 LEU   A O   1 
ATOM   857  C  CB  . LEU   A 1 108 ? 11.438 1.710   14.364 1.00 11.43 ? 114 LEU   A CB  1 
ATOM   858  C  CG  . LEU   A 1 108 ? 10.335 1.080   13.471 1.00 12.24 ? 114 LEU   A CG  1 
ATOM   859  C  CD1 . LEU   A 1 108 ? 9.357  0.281   14.322 1.00 13.29 ? 114 LEU   A CD1 1 
ATOM   860  C  CD2 . LEU   A 1 108 ? 9.529  2.189   12.734 1.00 14.21 ? 114 LEU   A CD2 1 
ATOM   861  N  N   . ARG   A 1 109 ? 12.750 -1.431  13.820 1.00 11.13 ? 115 ARG   A N   1 
ATOM   862  C  CA  . ARG   A 1 109 ? 13.310 -2.334  12.782 1.00 11.44 ? 115 ARG   A CA  1 
ATOM   863  C  C   . ARG   A 1 109 ? 12.229 -3.231  12.235 1.00 12.41 ? 115 ARG   A C   1 
ATOM   864  O  O   . ARG   A 1 109 ? 11.225 -3.533  12.892 1.00 12.65 ? 115 ARG   A O   1 
ATOM   865  C  CB  . ARG   A 1 109 ? 14.466 -3.166  13.375 1.00 13.11 ? 115 ARG   A CB  1 
ATOM   866  C  CG  . ARG   A 1 109 ? 14.010 -4.125  14.475 1.00 13.18 ? 115 ARG   A CG  1 
ATOM   867  C  CD  . ARG   A 1 109 ? 15.268 -4.838  15.005 1.00 15.06 ? 115 ARG   A CD  1 
ATOM   868  N  NE  . ARG   A 1 109 ? 16.036 -3.976  15.886 1.00 16.67 ? 115 ARG   A NE  1 
ATOM   869  C  CZ  . ARG   A 1 109 ? 17.340 -3.766  15.790 1.00 16.00 ? 115 ARG   A CZ  1 
ATOM   870  N  NH1 . ARG   A 1 109 ? 18.018 -4.193  14.720 1.00 16.54 ? 115 ARG   A NH1 1 
ATOM   871  N  NH2 . ARG   A 1 109 ? 17.966 -3.032  16.699 1.00 16.87 ? 115 ARG   A NH2 1 
ATOM   872  N  N   . CYS   A 1 110 ? 12.472 -3.687  11.006 1.00 13.99 ? 116 CYS   A N   1 
ATOM   873  C  CA  . CYS   A 1 110 ? 11.565 -4.624  10.332 1.00 16.83 ? 116 CYS   A CA  1 
ATOM   874  C  C   . CYS   A 1 110 ? 12.414 -5.828  9.919  1.00 19.50 ? 116 CYS   A C   1 
ATOM   875  O  O   . CYS   A 1 110 ? 13.605 -5.948  10.273 1.00 18.96 ? 116 CYS   A O   1 
ATOM   876  C  CB  . CYS   A 1 110 ? 10.903 -3.955  9.127  1.00 16.38 ? 116 CYS   A CB  1 
ATOM   877  S  SG  . CYS   A 1 110 ? 12.066 -3.593  7.788  1.00 16.13 ? 116 CYS   A SG  1 
ATOM   878  N  N   . GLN   A 1 111 ? 11.790 -6.740  9.112  1.00 21.36 ? 117 GLN   A N   1 
ATOM   879  C  CA  . GLN   A 1 111 ? 12.525 -7.897  8.644  1.00 24.21 ? 117 GLN   A CA  1 
ATOM   880  C  C   . GLN   A 1 111 ? 13.770 -7.543  7.777  1.00 24.73 ? 117 GLN   A C   1 
ATOM   881  O  O   . GLN   A 1 111 ? 14.727 -8.325  7.712  1.00 27.39 ? 117 GLN   A O   1 
ATOM   882  C  CB  . GLN   A 1 111 ? 11.588 -8.876  7.888  1.00 28.80 ? 117 GLN   A CB  1 
ATOM   883  C  CG  . GLN   A 1 111 ? 11.177 -8.367  6.522  1.00 33.98 ? 117 GLN   A CG  1 
ATOM   884  C  CD  . GLN   A 1 111 ? 10.210 -9.285  5.809  1.00 40.13 ? 117 GLN   A CD  1 
ATOM   885  O  OE1 . GLN   A 1 111 ? 8.985  -9.115  5.891  1.00 42.21 ? 117 GLN   A OE1 1 
ATOM   886  N  NE2 . GLN   A 1 111 ? 10.740 -10.249 5.076  1.00 39.02 ? 117 GLN   A NE2 1 
ATOM   887  N  N   . HIS   A 1 112 ? 13.800 -6.342  7.194  1.00 20.85 ? 118 HIS   A N   1 
ATOM   888  C  CA  . HIS   A 1 112 ? 14.906 -5.932  6.295  1.00 19.79 ? 118 HIS   A CA  1 
ATOM   889  C  C   . HIS   A 1 112 ? 16.047 -5.183  6.991  1.00 20.04 ? 118 HIS   A C   1 
ATOM   890  O  O   . HIS   A 1 112 ? 17.081 -4.924  6.369  1.00 22.05 ? 118 HIS   A O   1 
ATOM   891  C  CB  . HIS   A 1 112 ? 14.334 -5.076  5.164  1.00 20.06 ? 118 HIS   A CB  1 
ATOM   892  C  CG  . HIS   A 1 112 ? 13.193 -5.763  4.445  1.00 23.75 ? 118 HIS   A CG  1 
ATOM   893  N  ND1 . HIS   A 1 112 ? 11.884 -5.332  4.560  1.00 23.88 ? 118 HIS   A ND1 1 
ATOM   894  C  CD2 . HIS   A 1 112 ? 13.240 -6.766  3.529  1.00 26.22 ? 118 HIS   A CD2 1 
ATOM   895  C  CE1 . HIS   A 1 112 ? 11.156 -6.159  3.817  1.00 27.37 ? 118 HIS   A CE1 1 
ATOM   896  N  NE2 . HIS   A 1 112 ? 11.939 -7.020  3.147  1.00 28.25 ? 118 HIS   A NE2 1 
ATOM   897  N  N   . GLY   A 1 113 ? 15.831 -4.738  8.247  1.00 18.16 ? 119 GLY   A N   1 
ATOM   898  C  CA  . GLY   A 1 113 ? 16.867 -3.950  8.911  1.00 16.31 ? 119 GLY   A CA  1 
ATOM   899  C  C   . GLY   A 1 113 ? 16.271 -2.783  9.694  1.00 14.28 ? 119 GLY   A C   1 
ATOM   900  O  O   . GLY   A 1 113 ? 15.084 -2.788  10.024 1.00 14.11 ? 119 GLY   A O   1 
ATOM   901  N  N   . VAL   A 1 114 ? 17.120 -1.751  9.960  1.00 13.35 ? 120 VAL   A N   1 
ATOM   902  C  CA  . VAL   A 1 114 ? 16.674 -0.556  10.730 1.00 13.27 ? 120 VAL   A CA  1 
ATOM   903  C  C   . VAL   A 1 114 ? 15.814 0.362   9.876  1.00 12.61 ? 120 VAL   A C   1 
ATOM   904  O  O   . VAL   A 1 114 ? 16.228 0.724   8.757  1.00 12.68 ? 120 VAL   A O   1 
ATOM   905  C  CB  . VAL   A 1 114 ? 17.882 0.209   11.294 1.00 13.16 ? 120 VAL   A CB  1 
ATOM   906  C  CG1 . VAL   A 1 114 ? 17.445 1.509   11.969 1.00 13.71 ? 120 VAL   A CG1 1 
ATOM   907  C  CG2 . VAL   A 1 114 ? 18.673 -0.669  12.246 1.00 14.02 ? 120 VAL   A CG2 1 
ATOM   908  N  N   . VAL   A 1 115 ? 14.681 0.768   10.396 1.00 12.14 ? 121 VAL   A N   1 
ATOM   909  C  CA  . VAL   A 1 115 ? 13.719 1.591   9.695  1.00 12.56 ? 121 VAL   A CA  1 
ATOM   910  C  C   . VAL   A 1 115 ? 13.874 3.041   10.111 1.00 12.78 ? 121 VAL   A C   1 
ATOM   911  O  O   . VAL   A 1 115 ? 13.726 3.965   9.304  1.00 13.66 ? 121 VAL   A O   1 
ATOM   912  C  CB  . VAL   A 1 115 ? 12.272 1.084   9.974  1.00 13.40 ? 121 VAL   A CB  1 
ATOM   913  C  CG1 . VAL   A 1 115 ? 11.181 2.060   9.447  1.00 15.19 ? 121 VAL   A CG1 1 
ATOM   914  C  CG2 . VAL   A 1 115 ? 12.062 -0.304  9.404  1.00 14.66 ? 121 VAL   A CG2 1 
ATOM   915  N  N   . GLY   A 1 116 ? 14.082 3.279   11.421 1.00 12.45 ? 122 GLY   A N   1 
ATOM   916  C  CA  . GLY   A 1 116 ? 14.189 4.651   11.939 1.00 13.14 ? 122 GLY   A CA  1 
ATOM   917  C  C   . GLY   A 1 116 ? 14.400 4.654   13.437 1.00 11.82 ? 122 GLY   A C   1 
ATOM   918  O  O   . GLY   A 1 116 ? 14.729 3.599   14.012 1.00 11.97 ? 122 GLY   A O   1 
ATOM   919  N  N   . ILE   A 1 117 ? 14.265 5.831   14.049 1.00 11.24 ? 123 ILE   A N   1 
ATOM   920  C  CA  . ILE   A 1 117 ? 14.474 5.971   15.497 1.00 10.87 ? 123 ILE   A CA  1 
ATOM   921  C  C   . ILE   A 1 117 ? 13.326 6.736   16.126 1.00 11.30 ? 123 ILE   A C   1 
ATOM   922  O  O   . ILE   A 1 117 ? 12.704 7.616   15.492 1.00 12.20 ? 123 ILE   A O   1 
ATOM   923  C  CB  . ILE   A 1 117 ? 15.818 6.666   15.877 1.00 11.71 ? 123 ILE   A CB  1 
ATOM   924  C  CG1 . ILE   A 1 117 ? 15.977 7.997   15.144 1.00 13.00 ? 123 ILE   A CG1 1 
ATOM   925  C  CG2 . ILE   A 1 117 ? 16.990 5.704   15.663 1.00 13.04 ? 123 ILE   A CG2 1 
ATOM   926  C  CD1 . ILE   A 1 117 ? 17.242 8.821   15.637 1.00 14.55 ? 123 ILE   A CD1 1 
ATOM   927  N  N   . VAL   A 1 118 ? 13.031 6.435   17.398 1.00 11.11 ? 124 VAL   A N   1 
ATOM   928  C  CA  . VAL   A 1 118 ? 12.002 7.177   18.132 1.00 11.17 ? 124 VAL   A CA  1 
ATOM   929  C  C   . VAL   A 1 118 ? 12.348 8.680   18.132 1.00 11.90 ? 124 VAL   A C   1 
ATOM   930  O  O   . VAL   A 1 118 ? 13.493 9.049   18.437 1.00 12.15 ? 124 VAL   A O   1 
ATOM   931  C  CB  . VAL   A 1 118 ? 11.863 6.683   19.585 1.00 12.48 ? 124 VAL   A CB  1 
ATOM   932  C  CG1 . VAL   A 1 118 ? 10.878 7.562   20.397 1.00 12.94 ? 124 VAL   A CG1 1 
ATOM   933  C  CG2 . VAL   A 1 118 ? 11.417 5.212   19.653 1.00 13.31 ? 124 VAL   A CG2 1 
ATOM   934  N  N   . SER   A 1 119 ? 11.368 9.540   17.800 1.00 12.64 ? 125 SER   A N   1 
ATOM   935  C  CA  . SER   A 1 119 ? 11.536 10.986  17.770 1.00 14.24 ? 125 SER   A CA  1 
ATOM   936  C  C   . SER   A 1 119 ? 10.431 11.717  18.543 1.00 15.53 ? 125 SER   A C   1 
ATOM   937  O  O   . SER   A 1 119 ? 10.712 12.792  19.061 1.00 18.09 ? 125 SER   A O   1 
ATOM   938  C  CB  . SER   A 1 119 ? 11.645 11.455  16.333 1.00 15.80 ? 125 SER   A CB  1 
ATOM   939  O  OG  . SER   A 1 119 ? 11.721 12.869  16.202 1.00 16.61 ? 125 SER   A OG  1 
ATOM   940  N  N   . THR   A 1 120 ? 9.223  11.121  18.699 1.00 14.73 ? 126 THR   A N   1 
ATOM   941  C  CA  . THR   A 1 120 ? 8.117  11.815  19.410 1.00 15.85 ? 126 THR   A CA  1 
ATOM   942  C  C   . THR   A 1 120 ? 7.366  10.838  20.325 1.00 16.45 ? 126 THR   A C   1 
ATOM   943  O  O   . THR   A 1 120 ? 7.467  9.628   20.167 1.00 15.90 ? 126 THR   A O   1 
ATOM   944  C  CB  . THR   A 1 120 ? 7.123  12.502  18.411 1.00 17.96 ? 126 THR   A CB  1 
ATOM   945  O  OG1 . THR   A 1 120 ? 6.324  11.506  17.763 1.00 18.76 ? 126 THR   A OG1 1 
ATOM   946  C  CG2 . THR   A 1 120 ? 7.797  13.390  17.412 1.00 18.49 ? 126 THR   A CG2 1 
ATOM   947  N  N   . GLY   A 1 121 ? 6.543  11.366  21.265 1.00 16.91 ? 127 GLY   A N   1 
ATOM   948  C  CA  . GLY   A 1 121 ? 5.767  10.518  22.168 1.00 18.48 ? 127 GLY   A CA  1 
ATOM   949  C  C   . GLY   A 1 121 ? 4.536  11.196  22.760 1.00 20.06 ? 127 GLY   A C   1 
ATOM   950  O  O   . GLY   A 1 121 ? 3.997  12.075  22.158 1.00 21.58 ? 127 GLY   A O   1 
ATOM   951  N  N   . GLY   A 1 122 ? 3.998  10.608  23.826 1.00 19.33 ? 128 GLY   A N   1 
ATOM   952  C  CA  . GLY   A 1 122 ? 2.825  11.146  24.526 1.00 19.59 ? 128 GLY   A CA  1 
ATOM   953  C  C   . GLY   A 1 122 ? 1.507  10.584  24.038 1.00 21.18 ? 128 GLY   A C   1 
ATOM   954  O  O   . GLY   A 1 122 ? 1.382  10.205  22.859 1.00 21.64 ? 128 GLY   A O   1 
ATOM   955  N  N   . ASN   A 1 123 ? 0.500  10.626  24.908 1.00 21.26 ? 129 ASN   A N   1 
ATOM   956  C  CA  . ASN   A 1 123 ? -0.879 10.298  24.516 1.00 23.72 ? 129 ASN   A CA  1 
ATOM   957  C  C   . ASN   A 1 123 ? -1.045 8.889   24.009 1.00 21.11 ? 129 ASN   A C   1 
ATOM   958  O  O   . ASN   A 1 123 ? -2.051 8.615   23.341 1.00 20.65 ? 129 ASN   A O   1 
ATOM   959  C  CB  . ASN   A 1 123 ? -1.367 11.328  23.438 1.00 26.38 ? 129 ASN   A CB  1 
ATOM   960  C  CG  . ASN   A 1 123 ? -1.463 12.740  23.943 1.00 32.50 ? 129 ASN   A CG  1 
ATOM   961  O  OD1 . ASN   A 1 123 ? -1.632 12.955  25.142 1.00 33.36 ? 129 ASN   A OD1 1 
ATOM   962  N  ND2 . ASN   A 1 123 ? -1.428 13.730  23.045 1.00 34.64 ? 129 ASN   A ND2 1 
ATOM   963  N  N   . GLY   A 1 124 ? -0.145 7.977   24.359 1.00 18.70 ? 130 GLY   A N   1 
ATOM   964  C  CA  . GLY   A 1 124 ? -0.250 6.620   23.878 1.00 17.61 ? 130 GLY   A CA  1 
ATOM   965  C  C   . GLY   A 1 124 ? 0.200  6.475   22.439 1.00 15.36 ? 130 GLY   A C   1 
ATOM   966  O  O   . GLY   A 1 124 ? -0.021 5.416   21.885 1.00 16.92 ? 130 GLY   A O   1 
ATOM   967  N  N   . LEU   A 1 125 ? 0.887  7.485   21.867 1.00 14.51 ? 131 LEU   A N   1 
ATOM   968  C  CA  . LEU   A 1 125 ? 1.454  7.415   20.506 1.00 14.55 ? 131 LEU   A CA  1 
ATOM   969  C  C   . LEU   A 1 125 ? 2.964  7.488   20.573 1.00 15.77 ? 131 LEU   A C   1 
ATOM   970  O  O   . LEU   A 1 125 ? 3.548  8.076   21.499 1.00 17.02 ? 131 LEU   A O   1 
ATOM   971  C  CB  . LEU   A 1 125 ? 0.953  8.593   19.677 1.00 15.51 ? 131 LEU   A CB  1 
ATOM   972  C  CG  . LEU   A 1 125 ? -0.574 8.585   19.444 1.00 16.74 ? 131 LEU   A CG  1 
ATOM   973  C  CD1 . LEU   A 1 125 ? -1.087 9.987   19.102 1.00 19.26 ? 131 LEU   A CD1 1 
ATOM   974  C  CD2 . LEU   A 1 125 ? -0.969 7.509   18.414 1.00 16.90 ? 131 LEU   A CD2 1 
ATOM   975  N  N   . VAL   A 1 126 ? 3.602  6.864   19.578 1.00 13.73 ? 132 VAL   A N   1 
ATOM   976  C  CA  . VAL   A 1 126 ? 5.064  6.954   19.434 1.00 14.30 ? 132 VAL   A CA  1 
ATOM   977  C  C   . VAL   A 1 126 ? 5.331  7.346   17.968 1.00 13.82 ? 132 VAL   A C   1 
ATOM   978  O  O   . VAL   A 1 126 ? 4.712  6.795   17.061 1.00 14.80 ? 132 VAL   A O   1 
ATOM   979  C  CB  . VAL   A 1 126 ? 5.771  5.648   19.853 1.00 14.05 ? 132 VAL   A CB  1 
ATOM   980  C  CG1 . VAL   A 1 126 ? 5.189  4.419   19.156 1.00 15.51 ? 132 VAL   A CG1 1 
ATOM   981  C  CG2 . VAL   A 1 126 ? 7.297  5.767   19.667 1.00 14.32 ? 132 VAL   A CG2 1 
ATOM   982  N  N   . GLY   A 1 127 ? 6.218  8.310   17.745 1.00 13.41 ? 133 GLY   A N   1 
ATOM   983  C  CA  . GLY   A 1 127 ? 6.568  8.712   16.380 1.00 14.02 ? 133 GLY   A CA  1 
ATOM   984  C  C   . GLY   A 1 127 ? 8.027  8.390   16.095 1.00 13.67 ? 133 GLY   A C   1 
ATOM   985  O  O   . GLY   A 1 127 ? 8.904  8.542   16.966 1.00 14.80 ? 133 GLY   A O   1 
ATOM   986  N  N   . PHE   A 1 128 ? 8.276  7.919   14.879 1.00 12.62 ? 134 PHE   A N   1 
ATOM   987  C  CA  . PHE   A 1 128 ? 9.625  7.506   14.421 1.00 12.63 ? 134 PHE   A CA  1 
ATOM   988  C  C   . PHE   A 1 128 ? 10.098 8.327   13.239 1.00 12.78 ? 134 PHE   A C   1 
ATOM   989  O  O   . PHE   A 1 128 ? 9.331  8.518   12.287 1.00 13.27 ? 134 PHE   A O   1 
ATOM   990  C  CB  . PHE   A 1 128 ? 9.594  6.032   13.984 1.00 13.08 ? 134 PHE   A CB  1 
ATOM   991  C  CG  . PHE   A 1 128 ? 8.981  5.088   15.008 1.00 12.50 ? 134 PHE   A CG  1 
ATOM   992  C  CD1 . PHE   A 1 128 ? 9.723  4.621   16.080 1.00 12.04 ? 134 PHE   A CD1 1 
ATOM   993  C  CD2 . PHE   A 1 128 ? 7.663  4.683   14.884 1.00 13.82 ? 134 PHE   A CD2 1 
ATOM   994  C  CE1 . PHE   A 1 128 ? 9.154  3.747   17.015 1.00 12.57 ? 134 PHE   A CE1 1 
ATOM   995  C  CE2 . PHE   A 1 128 ? 7.098  3.825   15.826 1.00 14.02 ? 134 PHE   A CE2 1 
ATOM   996  C  CZ  . PHE   A 1 128 ? 7.867  3.344   16.874 1.00 13.16 ? 134 PHE   A CZ  1 
ATOM   997  N  N   . ALA   A 1 129 ? 11.351 8.815   13.321 1.00 12.64 ? 135 ALA   A N   1 
ATOM   998  C  CA  . ALA   A 1 129 ? 11.971 9.496   12.169 1.00 12.56 ? 135 ALA   A CA  1 
ATOM   999  C  C   . ALA   A 1 129 ? 12.461 8.427   11.206 1.00 12.31 ? 135 ALA   A C   1 
ATOM   1000 O  O   . ALA   A 1 129 ? 13.342 7.621   11.576 1.00 12.76 ? 135 ALA   A O   1 
ATOM   1001 C  CB  . ALA   A 1 129 ? 13.121 10.350  12.676 1.00 12.92 ? 135 ALA   A CB  1 
ATOM   1002 N  N   . ASP   A 1 130 ? 11.916 8.381   9.995  1.00 12.71 ? 136 ASP   A N   1 
ATOM   1003 C  CA  . ASP   A 1 130 ? 12.336 7.380   9.004  1.00 13.23 ? 136 ASP   A CA  1 
ATOM   1004 C  C   . ASP   A 1 130 ? 13.744 7.691   8.493  1.00 13.51 ? 136 ASP   A C   1 
ATOM   1005 O  O   . ASP   A 1 130 ? 14.130 8.853   8.339  1.00 14.74 ? 136 ASP   A O   1 
ATOM   1006 C  CB  . ASP   A 1 130 ? 11.372 7.461   7.792  1.00 15.59 ? 136 ASP   A CB  1 
ATOM   1007 C  CG  . ASP   A 1 130 ? 11.655 6.460   6.721  1.00 20.01 ? 136 ASP   A CG  1 
ATOM   1008 O  OD1 . ASP   A 1 130 ? 11.745 5.253   7.033  1.00 18.49 ? 136 ASP   A OD1 1 
ATOM   1009 O  OD2 . ASP   A 1 130 ? 11.886 6.894   5.557  1.00 25.48 ? 136 ASP   A OD2 1 
ATOM   1010 N  N   . VAL   A 1 131 ? 14.508 6.631   8.203  1.00 12.78 ? 137 VAL   A N   1 
ATOM   1011 C  CA  . VAL   A 1 131 ? 15.830 6.760   7.556  1.00 12.97 ? 137 VAL   A CA  1 
ATOM   1012 C  C   . VAL   A 1 131 ? 15.951 5.943   6.268  1.00 14.31 ? 137 VAL   A C   1 
ATOM   1013 O  O   . VAL   A 1 131 ? 17.009 5.998   5.621  1.00 13.61 ? 137 VAL   A O   1 
ATOM   1014 C  CB  . VAL   A 1 131 ? 17.014 6.422   8.498  1.00 12.43 ? 137 VAL   A CB  1 
ATOM   1015 C  CG1 . VAL   A 1 131 ? 17.037 7.346   9.729  1.00 13.23 ? 137 VAL   A CG1 1 
ATOM   1016 C  CG2 . VAL   A 1 131 ? 17.005 4.948   8.907  1.00 13.76 ? 137 VAL   A CG2 1 
ATOM   1017 N  N   . ARG   A 1 132 ? 14.879 5.272   5.828  1.00 13.87 ? 138 ARG   A N   1 
ATOM   1018 C  CA  . ARG   A 1 132 ? 14.971 4.372   4.680  1.00 13.52 ? 138 ARG   A CA  1 
ATOM   1019 C  C   . ARG   A 1 132 ? 15.229 5.052   3.360  1.00 14.74 ? 138 ARG   A C   1 
ATOM   1020 O  O   . ARG   A 1 132 ? 15.679 4.390   2.380  1.00 15.83 ? 138 ARG   A O   1 
ATOM   1021 C  CB  . ARG   A 1 132 ? 13.704 3.491   4.580  1.00 14.36 ? 138 ARG   A CB  1 
ATOM   1022 C  CG  . ARG   A 1 132 ? 13.582 2.519   5.787  1.00 14.23 ? 138 ARG   A CG  1 
ATOM   1023 C  CD  . ARG   A 1 132 ? 12.258 1.750   5.671  1.00 15.28 ? 138 ARG   A CD  1 
ATOM   1024 N  NE  . ARG   A 1 132 ? 11.120 2.657   5.890  1.00 15.68 ? 138 ARG   A NE  1 
ATOM   1025 C  CZ  . ARG   A 1 132 ? 9.855  2.262   5.992  1.00 17.42 ? 138 ARG   A CZ  1 
ATOM   1026 N  NH1 . ARG   A 1 132 ? 9.521  1.003   5.702  1.00 17.51 ? 138 ARG   A NH1 1 
ATOM   1027 N  NH2 . ARG   A 1 132 ? 8.904  3.147   6.280  1.00 18.35 ? 138 ARG   A NH2 1 
ATOM   1028 N  N   . ASP   A 1 133 ? 14.920 6.367   3.249  1.00 14.66 ? 139 ASP   A N   1 
ATOM   1029 C  CA  . ASP   A 1 133 ? 15.182 7.082   1.998  1.00 15.38 ? 139 ASP   A CA  1 
ATOM   1030 C  C   . ASP   A 1 133 ? 16.615 7.613   1.912  1.00 15.38 ? 139 ASP   A C   1 
ATOM   1031 O  O   . ASP   A 1 133 ? 17.014 8.094   0.850  1.00 16.82 ? 139 ASP   A O   1 
ATOM   1032 C  CB  . ASP   A 1 133 ? 14.175 8.257   1.879  1.00 17.51 ? 139 ASP   A CB  1 
ATOM   1033 C  CG  . ASP   A 1 133 ? 14.391 9.319   2.976  1.00 20.40 ? 139 ASP   A CG  1 
ATOM   1034 O  OD1 . ASP   A 1 133 ? 14.527 8.944   4.169  1.00 19.98 ? 139 ASP   A OD1 1 
ATOM   1035 O  OD2 . ASP   A 1 133 ? 14.386 10.514  2.662  1.00 23.07 ? 139 ASP   A OD2 1 
ATOM   1036 N  N   . LEU   A 1 134 ? 17.413 7.537   2.997  1.00 14.10 ? 140 LEU   A N   1 
ATOM   1037 C  CA  . LEU   A 1 134 ? 18.783 8.079   3.046  1.00 14.57 ? 140 LEU   A CA  1 
ATOM   1038 C  C   . LEU   A 1 134 ? 19.738 7.023   2.501  1.00 14.71 ? 140 LEU   A C   1 
ATOM   1039 O  O   . LEU   A 1 134 ? 20.451 6.334   3.240  1.00 14.90 ? 140 LEU   A O   1 
ATOM   1040 C  CB  . LEU   A 1 134 ? 19.122 8.474   4.500  1.00 14.51 ? 140 LEU   A CB  1 
ATOM   1041 C  CG  . LEU   A 1 134 ? 18.152 9.498   5.141  1.00 16.17 ? 140 LEU   A CG  1 
ATOM   1042 C  CD1 . LEU   A 1 134 ? 18.538 9.747   6.607  1.00 16.53 ? 140 LEU   A CD1 1 
ATOM   1043 C  CD2 . LEU   A 1 134 ? 18.152 10.801  4.376  1.00 18.19 ? 140 LEU   A CD2 1 
ATOM   1044 N  N   . LEU   A 1 135 ? 19.751 6.907   1.171  1.00 14.52 ? 141 LEU   A N   1 
ATOM   1045 C  CA  . LEU   A 1 135 ? 20.501 5.824   0.532  1.00 15.44 ? 141 LEU   A CA  1 
ATOM   1046 C  C   . LEU   A 1 135 ? 21.988 5.937   0.723  1.00 15.30 ? 141 LEU   A C   1 
ATOM   1047 O  O   . LEU   A 1 135 ? 22.705 4.912   0.773  1.00 16.77 ? 141 LEU   A O   1 
ATOM   1048 C  CB  . LEU   A 1 135 ? 20.157 5.708   -0.982 1.00 16.91 ? 141 LEU   A CB  1 
ATOM   1049 C  CG  . LEU   A 1 135 ? 18.642 5.675   -1.319 1.00 18.18 ? 141 LEU   A CG  1 
ATOM   1050 C  CD1 . LEU   A 1 135 ? 18.449 5.320   -2.823 1.00 19.55 ? 141 LEU   A CD1 1 
ATOM   1051 C  CD2 . LEU   A 1 135 ? 17.830 4.692   -0.448 1.00 19.72 ? 141 LEU   A CD2 1 
ATOM   1052 N  N   . TRP   A 1 136 ? 22.475 7.183   0.870  1.00 14.37 ? 142 TRP   A N   1 
ATOM   1053 C  CA  . TRP   A 1 136 ? 23.883 7.420   1.064  1.00 15.13 ? 142 TRP   A CA  1 
ATOM   1054 C  C   . TRP   A 1 136 ? 24.431 6.819   2.355  1.00 15.79 ? 142 TRP   A C   1 
ATOM   1055 O  O   . TRP   A 1 136 ? 25.654 6.704   2.489  1.00 16.71 ? 142 TRP   A O   1 
ATOM   1056 C  CB  . TRP   A 1 136 ? 24.191 8.933   0.941  1.00 15.47 ? 142 TRP   A CB  1 
ATOM   1057 C  CG  . TRP   A 1 136 ? 23.379 9.767   1.885  1.00 14.73 ? 142 TRP   A CG  1 
ATOM   1058 C  CD1 . TRP   A 1 136 ? 22.231 10.444  1.592  1.00 16.12 ? 142 TRP   A CD1 1 
ATOM   1059 C  CD2 . TRP   A 1 136 ? 23.696 10.072  3.257  1.00 15.45 ? 142 TRP   A CD2 1 
ATOM   1060 N  NE1 . TRP   A 1 136 ? 21.760 11.086  2.732  1.00 17.27 ? 142 TRP   A NE1 1 
ATOM   1061 C  CE2 . TRP   A 1 136 ? 22.685 10.928  3.736  1.00 16.11 ? 142 TRP   A CE2 1 
ATOM   1062 C  CE3 . TRP   A 1 136 ? 24.779 9.772   4.094  1.00 16.03 ? 142 TRP   A CE3 1 
ATOM   1063 C  CZ2 . TRP   A 1 136 ? 22.688 11.405  5.058  1.00 16.91 ? 142 TRP   A CZ2 1 
ATOM   1064 C  CZ3 . TRP   A 1 136 ? 24.789 10.262  5.387  1.00 18.06 ? 142 TRP   A CZ3 1 
ATOM   1065 C  CH2 . TRP   A 1 136 ? 23.774 11.094  5.840  1.00 17.47 ? 142 TRP   A CH2 1 
ATOM   1066 N  N   . LEU   A 1 137 ? 23.566 6.471   3.342  1.00 15.01 ? 143 LEU   A N   1 
ATOM   1067 C  CA  . LEU   A 1 137 ? 24.075 5.823   4.563  1.00 16.08 ? 143 LEU   A CA  1 
ATOM   1068 C  C   . LEU   A 1 137 ? 24.779 4.496   4.244  1.00 18.13 ? 143 LEU   A C   1 
ATOM   1069 O  O   . LEU   A 1 137 ? 25.613 4.049   5.052  1.00 19.57 ? 143 LEU   A O   1 
ATOM   1070 C  CB  . LEU   A 1 137 ? 22.942 5.561   5.556  1.00 15.20 ? 143 LEU   A CB  1 
ATOM   1071 C  CG  . LEU   A 1 137 ? 22.375 6.786   6.232  1.00 15.35 ? 143 LEU   A CG  1 
ATOM   1072 C  CD1 . LEU   A 1 137 ? 21.138 6.415   7.017  1.00 17.54 ? 143 LEU   A CD1 1 
ATOM   1073 C  CD2 . LEU   A 1 137 ? 23.461 7.429   7.182  1.00 16.46 ? 143 LEU   A CD2 1 
ATOM   1074 N  N   . ASP   A 1 138 ? 24.453 3.860   3.083  1.00 20.89 ? 144 ASP   A N   1 
ATOM   1075 C  CA  . ASP   A 1 138 ? 25.029 2.553   2.689  1.00 23.17 ? 144 ASP   A CA  1 
ATOM   1076 C  C   . ASP   A 1 138 ? 26.355 2.631   1.964  1.00 27.47 ? 144 ASP   A C   1 
ATOM   1077 O  O   . ASP   A 1 138 ? 26.893 1.577   1.579  1.00 29.25 ? 144 ASP   A O   1 
ATOM   1078 C  CB  . ASP   A 1 138 ? 24.058 1.804   1.734  1.00 24.03 ? 144 ASP   A CB  1 
ATOM   1079 C  CG  . ASP   A 1 138 ? 22.693 1.508   2.292  1.00 27.02 ? 144 ASP   A CG  1 
ATOM   1080 O  OD1 . ASP   A 1 138 ? 22.528 1.581   3.537  1.00 28.56 ? 144 ASP   A OD1 1 
ATOM   1081 O  OD2 . ASP   A 1 138 ? 21.760 1.207   1.489  1.00 33.29 ? 144 ASP   A OD2 1 
ATOM   1082 N  N   . GLU   A 1 139 ? 26.906 3.840   1.760  1.00 28.86 ? 145 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 139 ? 28.154 3.966   0.993  1.00 32.37 ? 145 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 139 ? 29.128 4.977   1.612  1.00 34.87 ? 145 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 139 ? 28.795 5.632   2.603  1.00 34.35 ? 145 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 139 ? 27.783 4.355   -0.447 1.00 35.83 ? 145 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 139 ? 27.077 5.693   -0.503 1.00 43.54 ? 145 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 139 ? 26.253 5.992   -1.741 1.00 51.44 ? 145 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 139 ? 26.003 7.193   -2.002 1.00 51.24 ? 145 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 139 ? 25.853 5.035   -2.446 1.00 54.80 ? 145 GLU   A OE2 1 
ATOM   1091 N  N   . GLU   A 1 140 ? 30.342 5.069   1.036  1.00 37.79 ? 146 GLU   A N   1 
ATOM   1092 C  CA  . GLU   A 1 140 ? 31.456 5.953   1.399  1.00 41.22 ? 146 GLU   A CA  1 
ATOM   1093 C  C   . GLU   A 1 140 ? 32.155 5.481   2.666  1.00 43.46 ? 146 GLU   A C   1 
ATOM   1094 O  O   . GLU   A 1 140 ? 33.369 5.249   2.633  1.00 44.78 ? 146 GLU   A O   1 
ATOM   1095 C  CB  . GLU   A 1 140 ? 31.023 7.429   1.452  1.00 44.71 ? 146 GLU   A CB  1 
ATOM   1096 C  CG  . GLU   A 1 140 ? 31.922 8.363   2.241  1.00 51.35 ? 146 GLU   A CG  1 
ATOM   1097 C  CD  . GLU   A 1 140 ? 32.406 9.543   1.424  1.00 60.17 ? 146 GLU   A CD  1 
ATOM   1098 O  OE1 . GLU   A 1 140 ? 31.556 10.228  0.808  1.00 63.22 ? 146 GLU   A OE1 1 
ATOM   1099 O  OE2 . GLU   A 1 140 ? 33.638 9.769   1.382  1.00 61.31 ? 146 GLU   A OE2 1 
ATOM   1100 N  N   . SER   B 1 1   ? 21.905 -21.313 7.611  1.00 18.67 ? 7   SER   C N   1 
ATOM   1101 C  CA  . SER   B 1 1   ? 20.770 -21.118 8.546  1.00 18.28 ? 7   SER   C CA  1 
ATOM   1102 C  C   . SER   B 1 1   ? 20.731 -22.219 9.621  1.00 17.54 ? 7   SER   C C   1 
ATOM   1103 O  O   . SER   B 1 1   ? 21.388 -23.258 9.469  1.00 19.03 ? 7   SER   C O   1 
ATOM   1104 C  CB  . SER   B 1 1   ? 19.457 -21.140 7.765  1.00 21.70 ? 7   SER   C CB  1 
ATOM   1105 O  OG  . SER   B 1 1   ? 19.287 -22.423 7.191  1.00 25.54 ? 7   SER   C OG  1 
ATOM   1106 N  N   . GLY   B 1 2   ? 19.967 -21.993 10.695 1.00 17.30 ? 8   GLY   C N   1 
ATOM   1107 C  CA  . GLY   B 1 2   ? 19.815 -22.975 11.760 1.00 16.63 ? 8   GLY   C CA  1 
ATOM   1108 C  C   . GLY   B 1 2   ? 19.518 -22.347 13.105 1.00 15.36 ? 8   GLY   C C   1 
ATOM   1109 O  O   . GLY   B 1 2   ? 19.934 -21.224 13.377 1.00 16.30 ? 8   GLY   C O   1 
ATOM   1110 N  N   . ALA   B 1 3   ? 18.854 -23.096 13.973 1.00 14.63 ? 9   ALA   C N   1 
ATOM   1111 C  CA  . ALA   B 1 3   ? 18.539 -22.614 15.317 1.00 14.29 ? 9   ALA   C CA  1 
ATOM   1112 C  C   . ALA   B 1 3   ? 18.648 -23.735 16.346 1.00 13.63 ? 9   ALA   C C   1 
ATOM   1113 O  O   . ALA   B 1 3   ? 18.713 -24.918 15.972 1.00 15.36 ? 9   ALA   C O   1 
ATOM   1114 C  CB  . ALA   B 1 3   ? 17.107 -22.052 15.332 1.00 16.67 ? 9   ALA   C CB  1 
ATOM   1115 N  N   . ILE   B 1 4   ? 18.682 -23.350 17.639 1.00 13.51 ? 10  ILE   C N   1 
ATOM   1116 C  CA  . ILE   B 1 4   ? 18.597 -24.286 18.753 1.00 13.78 ? 10  ILE   C CA  1 
ATOM   1117 C  C   . ILE   B 1 4   ? 17.198 -24.106 19.352 1.00 13.71 ? 10  ILE   C C   1 
ATOM   1118 O  O   . ILE   B 1 4   ? 16.761 -22.973 19.564 1.00 14.56 ? 10  ILE   C O   1 
ATOM   1119 C  CB  . ILE   B 1 4   ? 19.635 -23.981 19.843 1.00 13.29 ? 10  ILE   C CB  1 
ATOM   1120 C  CG1 . ILE   B 1 4   ? 21.054 -23.827 19.254 1.00 14.76 ? 10  ILE   C CG1 1 
ATOM   1121 C  CG2 . ILE   B 1 4   ? 19.576 -25.093 20.928 1.00 15.15 ? 10  ILE   C CG2 1 
ATOM   1122 C  CD1 . ILE   B 1 4   ? 22.033 -23.212 20.265 1.00 15.94 ? 10  ILE   C CD1 1 
ATOM   1123 N  N   . TYR   B 1 5   ? 16.504 -25.204 19.666 1.00 13.47 ? 11  TYR   C N   1 
ATOM   1124 C  CA  . TYR   B 1 5   ? 15.160 -25.152 20.238 1.00 14.55 ? 11  TYR   C CA  1 
ATOM   1125 C  C   . TYR   B 1 5   ? 15.209 -25.827 21.601 1.00 15.27 ? 11  TYR   C C   1 
ATOM   1126 O  O   . TYR   B 1 5   ? 15.282 -27.057 21.670 1.00 16.99 ? 11  TYR   C O   1 
ATOM   1127 C  CB  . TYR   B 1 5   ? 14.113 -25.854 19.321 1.00 15.42 ? 11  TYR   C CB  1 
ATOM   1128 C  CG  . TYR   B 1 5   ? 13.920 -25.092 18.025 1.00 15.60 ? 11  TYR   C CG  1 
ATOM   1129 C  CD1 . TYR   B 1 5   ? 13.083 -23.976 17.963 1.00 15.69 ? 11  TYR   C CD1 1 
ATOM   1130 C  CD2 . TYR   B 1 5   ? 14.630 -25.436 16.881 1.00 16.13 ? 11  TYR   C CD2 1 
ATOM   1131 C  CE1 . TYR   B 1 5   ? 12.964 -23.237 16.793 1.00 17.18 ? 11  TYR   C CE1 1 
ATOM   1132 C  CE2 . TYR   B 1 5   ? 14.507 -24.712 15.701 1.00 18.27 ? 11  TYR   C CE2 1 
ATOM   1133 C  CZ  . TYR   B 1 5   ? 13.668 -23.620 15.664 1.00 18.32 ? 11  TYR   C CZ  1 
ATOM   1134 O  OH  . TYR   B 1 5   ? 13.571 -22.883 14.504 1.00 20.01 ? 11  TYR   C OH  1 
ATOM   1135 N  N   . VAL   B 1 6   ? 15.244 -25.072 22.686 1.00 15.16 ? 12  VAL   C N   1 
ATOM   1136 C  CA  . VAL   B 1 6   ? 15.322 -25.599 24.062 1.00 16.24 ? 12  VAL   C CA  1 
ATOM   1137 C  C   . VAL   B 1 6   ? 14.200 -25.005 24.902 1.00 16.13 ? 12  VAL   C C   1 
ATOM   1138 O  O   . VAL   B 1 6   ? 14.008 -23.798 24.898 1.00 15.79 ? 12  VAL   C O   1 
ATOM   1139 C  CB  . VAL   B 1 6   ? 16.727 -25.352 24.676 1.00 17.57 ? 12  VAL   C CB  1 
ATOM   1140 C  CG1 . VAL   B 1 6   ? 17.108 -23.851 24.605 1.00 17.32 ? 12  VAL   C CG1 1 
ATOM   1141 C  CG2 . VAL   B 1 6   ? 16.751 -25.867 26.108 1.00 18.93 ? 12  VAL   C CG2 1 
ATOM   1142 N  N   . GLY   B 1 7   ? 13.374 -25.837 25.562 1.00 17.32 ? 13  GLY   C N   1 
ATOM   1143 C  CA  . GLY   B 1 7   ? 12.255 -25.299 26.338 1.00 18.02 ? 13  GLY   C CA  1 
ATOM   1144 C  C   . GLY   B 1 7   ? 11.318 -24.459 25.465 1.00 17.76 ? 13  GLY   C C   1 
ATOM   1145 O  O   . GLY   B 1 7   ? 11.039 -24.840 24.319 1.00 18.71 ? 13  GLY   C O   1 
ATOM   1146 N  N   . ASN   B 1 8   ? 10.982 -23.261 25.904 1.00 17.36 ? 14  ASN   C N   1 
ATOM   1147 C  CA  . ASN   B 1 8   ? 10.179 -22.351 25.069 1.00 17.67 ? 14  ASN   C CA  1 
ATOM   1148 C  C   . ASN   B 1 8   ? 11.077 -21.249 24.490 1.00 17.31 ? 14  ASN   C C   1 
ATOM   1149 O  O   . ASN   B 1 8   ? 10.622 -20.119 24.321 1.00 18.00 ? 14  ASN   C O   1 
ATOM   1150 C  CB  . ASN   B 1 8   ? 8.950  -21.769 25.816 1.00 19.53 ? 14  ASN   C CB  1 
ATOM   1151 C  CG  . ASN   B 1 8   ? 7.851  -22.804 25.950 1.00 26.27 ? 14  ASN   C CG  1 
ATOM   1152 O  OD1 . ASN   B 1 8   ? 6.976  -22.931 25.092 1.00 29.06 ? 14  ASN   C OD1 1 
ATOM   1153 N  ND2 . ASN   B 1 8   ? 7.939  -23.609 26.984 1.00 27.84 ? 14  ASN   C ND2 1 
ATOM   1154 N  N   . TYR   B 1 9   ? 12.298 -21.616 24.107 1.00 14.73 ? 15  TYR   C N   1 
ATOM   1155 C  CA  . TYR   B 1 9   ? 13.253 -20.650 23.518 1.00 14.50 ? 15  TYR   C CA  1 
ATOM   1156 C  C   . TYR   B 1 9   ? 13.731 -21.128 22.148 1.00 14.61 ? 15  TYR   C C   1 
ATOM   1157 O  O   . TYR   B 1 9   ? 13.928 -22.342 21.937 1.00 15.86 ? 15  TYR   C O   1 
ATOM   1158 C  CB  . TYR   B 1 9   ? 14.500 -20.501 24.432 1.00 15.31 ? 15  TYR   C CB  1 
ATOM   1159 C  CG  . TYR   B 1 9   ? 14.174 -19.979 25.830 1.00 16.43 ? 15  TYR   C CG  1 
ATOM   1160 C  CD1 . TYR   B 1 9   ? 13.620 -18.718 26.011 1.00 18.73 ? 15  TYR   C CD1 1 
ATOM   1161 C  CD2 . TYR   B 1 9   ? 14.474 -20.727 26.970 1.00 17.58 ? 15  TYR   C CD2 1 
ATOM   1162 C  CE1 . TYR   B 1 9   ? 13.319 -18.236 27.286 1.00 21.35 ? 15  TYR   C CE1 1 
ATOM   1163 C  CE2 . TYR   B 1 9   ? 14.206 -20.232 28.253 1.00 20.27 ? 15  TYR   C CE2 1 
ATOM   1164 C  CZ  . TYR   B 1 9   ? 13.674 -18.969 28.396 1.00 23.12 ? 15  TYR   C CZ  1 
ATOM   1165 O  OH  . TYR   B 1 9   ? 13.379 -18.447 29.650 1.00 28.63 ? 15  TYR   C OH  1 
ATOM   1166 N  N   . ARG   B 1 10  ? 14.000 -20.178 21.262 1.00 13.86 ? 16  ARG   C N   1 
ATOM   1167 C  CA  . ARG   B 1 10  ? 14.617 -20.396 19.939 1.00 13.61 ? 16  ARG   C CA  1 
ATOM   1168 C  C   . ARG   B 1 10  ? 15.871 -19.517 19.924 1.00 13.77 ? 16  ARG   C C   1 
ATOM   1169 O  O   . ARG   B 1 10  ? 15.794 -18.302 20.137 1.00 14.16 ? 16  ARG   C O   1 
ATOM   1170 C  CB  . ARG   B 1 10  ? 13.643 -19.946 18.808 1.00 14.40 ? 16  ARG   C CB  1 
ATOM   1171 C  CG  . ARG   B 1 10  ? 14.258 -19.800 17.411 1.00 15.34 ? 16  ARG   C CG  1 
ATOM   1172 C  CD  . ARG   B 1 10  ? 13.190 -19.495 16.368 1.00 15.05 ? 16  ARG   C CD  1 
ATOM   1173 N  NE  . ARG   B 1 10  ? 13.650 -18.552 15.337 1.00 16.66 ? 16  ARG   C NE  1 
ATOM   1174 C  CZ  . ARG   B 1 10  ? 14.145 -18.866 14.136 1.00 18.39 ? 16  ARG   C CZ  1 
ATOM   1175 N  NH1 . ARG   B 1 10  ? 14.404 -20.139 13.821 1.00 19.58 ? 16  ARG   C NH1 1 
ATOM   1176 N  NH2 . ARG   B 1 10  ? 14.498 -17.909 13.288 1.00 18.64 ? 16  ARG   C NH2 1 
ATOM   1177 N  N   . VAL   B 1 11  ? 17.033 -20.137 19.706 1.00 12.94 ? 17  VAL   C N   1 
ATOM   1178 C  CA  . VAL   B 1 11  ? 18.320 -19.413 19.684 1.00 12.40 ? 17  VAL   C CA  1 
ATOM   1179 C  C   . VAL   B 1 11  ? 18.805 -19.353 18.252 1.00 13.13 ? 17  VAL   C C   1 
ATOM   1180 O  O   . VAL   B 1 11  ? 18.988 -20.417 17.617 1.00 13.88 ? 17  VAL   C O   1 
ATOM   1181 C  CB  . VAL   B 1 11  ? 19.402 -20.154 20.540 1.00 13.19 ? 17  VAL   C CB  1 
ATOM   1182 C  CG1 . VAL   B 1 11  ? 20.644 -19.275 20.657 1.00 15.22 ? 17  VAL   C CG1 1 
ATOM   1183 C  CG2 . VAL   B 1 11  ? 18.857 -20.519 21.937 1.00 14.76 ? 17  VAL   C CG2 1 
ATOM   1184 N  N   . VAL   B 1 12  ? 19.056 -18.144 17.724 1.00 12.55 ? 18  VAL   C N   1 
ATOM   1185 C  CA  A VAL   B 1 12  ? 19.512 -17.967 16.341 0.50 12.10 ? 18  VAL   C CA  1 
ATOM   1186 C  CA  B VAL   B 1 12  ? 19.465 -17.990 16.336 0.50 14.12 ? 18  VAL   C CA  1 
ATOM   1187 C  C   . VAL   B 1 12  ? 20.636 -16.972 16.264 1.00 12.84 ? 18  VAL   C C   1 
ATOM   1188 O  O   . VAL   B 1 12  ? 20.896 -16.219 17.223 1.00 13.71 ? 18  VAL   C O   1 
ATOM   1189 C  CB  A VAL   B 1 12  ? 18.362 -17.441 15.428 0.50 12.10 ? 18  VAL   C CB  1 
ATOM   1190 C  CB  B VAL   B 1 12  ? 18.194 -17.455 15.577 0.50 18.24 ? 18  VAL   C CB  1 
ATOM   1191 C  CG1 A VAL   B 1 12  ? 17.385 -18.558 15.122 0.50 13.07 ? 18  VAL   C CG1 1 
ATOM   1192 C  CG1 B VAL   B 1 12  ? 18.443 -17.248 14.107 0.50 19.23 ? 18  VAL   C CG1 1 
ATOM   1193 C  CG2 A VAL   B 1 12  ? 17.701 -16.156 15.996 0.50 9.09  ? 18  VAL   C CG2 1 
ATOM   1194 C  CG2 B VAL   B 1 12  ? 17.012 -18.393 15.749 0.50 20.95 ? 18  VAL   C CG2 1 
ATOM   1195 N  N   . ASN   B 1 13  ? 21.339 -16.923 15.119 1.00 12.06 ? 19  ASN   C N   1 
ATOM   1196 C  CA  . ASN   B 1 13  ? 22.324 -15.873 14.907 1.00 11.77 ? 19  ASN   C CA  1 
ATOM   1197 C  C   . ASN   B 1 13  ? 21.518 -14.528 14.854 1.00 12.89 ? 19  ASN   C C   1 
ATOM   1198 O  O   . ASN   B 1 13  ? 20.520 -14.441 14.147 1.00 13.11 ? 19  ASN   C O   1 
ATOM   1199 C  CB  . ASN   B 1 13  ? 23.029 -16.031 13.549 1.00 12.39 ? 19  ASN   C CB  1 
ATOM   1200 C  CG  . ASN   B 1 13  ? 23.882 -17.296 13.485 1.00 12.38 ? 19  ASN   C CG  1 
ATOM   1201 O  OD1 . ASN   B 1 13  ? 23.430 -18.360 13.048 1.00 13.49 ? 19  ASN   C OD1 1 
ATOM   1202 N  ND2 . ASN   B 1 13  ? 25.125 -17.188 13.943 1.00 13.35 ? 19  ASN   C ND2 1 
ATOM   1203 N  N   . ARG   B 1 14  ? 22.026 -13.492 15.558 1.00 12.69 ? 20  ARG   C N   1 
ATOM   1204 C  CA  . ARG   B 1 14  ? 21.282 -12.201 15.569 1.00 12.50 ? 20  ARG   C CA  1 
ATOM   1205 C  C   . ARG   B 1 14  ? 21.133 -11.661 14.148 1.00 14.29 ? 20  ARG   C C   1 
ATOM   1206 O  O   . ARG   B 1 14  ? 20.067 -11.127 13.798 1.00 14.20 ? 20  ARG   C O   1 
ATOM   1207 C  CB  . ARG   B 1 14  ? 22.030 -11.210 16.461 1.00 12.64 ? 20  ARG   C CB  1 
ATOM   1208 C  CG  . ARG   B 1 14  ? 21.236 -9.887  16.660 1.00 13.98 ? 20  ARG   C CG  1 
ATOM   1209 C  CD  . ARG   B 1 14  ? 22.103 -8.906  17.444 1.00 14.25 ? 20  ARG   C CD  1 
ATOM   1210 N  NE  . ARG   B 1 14  ? 21.429 -7.654  17.882 1.00 14.65 ? 20  ARG   C NE  1 
ATOM   1211 C  CZ  . ARG   B 1 14  ? 21.340 -6.566  17.133 1.00 14.16 ? 20  ARG   C CZ  1 
ATOM   1212 N  NH1 . ARG   B 1 14  ? 21.708 -6.598  15.858 1.00 15.78 ? 20  ARG   C NH1 1 
ATOM   1213 N  NH2 . ARG   B 1 14  ? 20.829 -5.447  17.636 1.00 15.61 ? 20  ARG   C NH2 1 
ATOM   1214 N  N   . HIS   B 1 15  ? 22.149 -11.867 13.284 1.00 13.76 ? 21  HIS   C N   1 
ATOM   1215 C  CA  . HIS   B 1 15  ? 22.066 -11.326 11.913 1.00 14.29 ? 21  HIS   C CA  1 
ATOM   1216 C  C   . HIS   B 1 15  ? 21.063 -12.073 11.020 1.00 15.29 ? 21  HIS   C C   1 
ATOM   1217 O  O   . HIS   B 1 15  ? 20.764 -11.574 9.949  1.00 16.77 ? 21  HIS   C O   1 
ATOM   1218 C  CB  . HIS   B 1 15  ? 23.465 -11.227 11.245 1.00 14.08 ? 21  HIS   C CB  1 
ATOM   1219 C  CG  . HIS   B 1 15  ? 24.053 -12.548 10.808 1.00 13.76 ? 21  HIS   C CG  1 
ATOM   1220 N  ND1 . HIS   B 1 15  ? 24.794 -13.370 11.680 1.00 15.06 ? 21  HIS   C ND1 1 
ATOM   1221 C  CD2 . HIS   B 1 15  ? 24.054 -13.110 9.574  1.00 14.65 ? 21  HIS   C CD2 1 
ATOM   1222 C  CE1 . HIS   B 1 15  ? 25.200 -14.403 10.942 1.00 15.55 ? 21  HIS   C CE1 1 
ATOM   1223 N  NE2 . HIS   B 1 15  ? 24.767 -14.299 9.681  1.00 15.36 ? 21  HIS   C NE2 1 
ATOM   1224 N  N   . LEU   B 1 16  ? 20.537 -13.222 11.458 1.00 14.30 ? 22  LEU   C N   1 
ATOM   1225 C  CA  . LEU   B 1 16  ? 19.531 -13.978 10.709 1.00 15.52 ? 22  LEU   C CA  1 
ATOM   1226 C  C   . LEU   B 1 16  ? 18.144 -13.919 11.389 1.00 15.41 ? 22  LEU   C C   1 
ATOM   1227 O  O   . LEU   B 1 16  ? 17.208 -14.629 10.956 1.00 16.68 ? 22  LEU   C O   1 
ATOM   1228 C  CB  . LEU   B 1 16  ? 19.994 -15.428 10.515 1.00 15.55 ? 22  LEU   C CB  1 
ATOM   1229 C  CG  . LEU   B 1 16  ? 21.276 -15.586 9.699  1.00 15.89 ? 22  LEU   C CG  1 
ATOM   1230 C  CD1 . LEU   B 1 16  ? 21.666 -17.062 9.612  1.00 17.05 ? 22  LEU   C CD1 1 
ATOM   1231 C  CD2 . LEU   B 1 16  ? 21.171 -14.971 8.306  1.00 15.65 ? 22  LEU   C CD2 1 
ATOM   1232 N  N   . ALA   B 1 17  ? 17.989 -13.149 12.486 1.00 15.58 ? 23  ALA   C N   1 
ATOM   1233 C  CA  . ALA   B 1 17  ? 16.702 -13.094 13.196 1.00 15.23 ? 23  ALA   C CA  1 
ATOM   1234 C  C   . ALA   B 1 17  ? 15.592 -12.534 12.314 1.00 15.92 ? 23  ALA   C C   1 
ATOM   1235 O  O   . ALA   B 1 17  ? 15.831 -11.615 11.506 1.00 17.12 ? 23  ALA   C O   1 
ATOM   1236 C  CB  . ALA   B 1 17  ? 16.837 -12.253 14.468 1.00 16.54 ? 23  ALA   C CB  1 
ATOM   1237 N  N   . THR   B 1 18  ? 14.406 -13.104 12.468 1.00 16.65 ? 24  THR   C N   1 
ATOM   1238 C  CA  . THR   B 1 18  ? 13.244 -12.699 11.683 1.00 16.74 ? 24  THR   C CA  1 
ATOM   1239 C  C   . THR   B 1 18  ? 12.441 -11.622 12.438 1.00 16.82 ? 24  THR   C C   1 
ATOM   1240 O  O   . THR   B 1 18  ? 12.661 -11.338 13.629 1.00 17.30 ? 24  THR   C O   1 
ATOM   1241 C  CB  . THR   B 1 18  ? 12.319 -13.939 11.421 1.00 17.70 ? 24  THR   C CB  1 
ATOM   1242 O  OG1 . THR   B 1 18  ? 11.782 -14.358 12.655 1.00 18.10 ? 24  THR   C OG1 1 
ATOM   1243 C  CG2 . THR   B 1 18  ? 13.037 -15.098 10.712 1.00 18.40 ? 24  THR   C CG2 1 
ATOM   1244 N  N   . HIS   B 1 19  ? 11.409 -11.032 11.746 1.00 17.66 ? 25  HIS   C N   1 
ATOM   1245 C  CA  . HIS   B 1 19  ? 10.489 -10.109 12.426 1.00 18.84 ? 25  HIS   C CA  1 
ATOM   1246 C  C   . HIS   B 1 19  ? 9.796  -10.855 13.571 1.00 17.13 ? 25  HIS   C C   1 
ATOM   1247 O  O   . HIS   B 1 19  ? 9.698  -10.282 14.654 1.00 18.29 ? 25  HIS   C O   1 
ATOM   1248 C  CB  . HIS   B 1 19  ? 9.375  -9.604  11.464 1.00 20.06 ? 25  HIS   C CB  1 
ATOM   1249 C  CG  . HIS   B 1 19  ? 8.233  -8.891  12.168 1.00 22.20 ? 25  HIS   C CG  1 
ATOM   1250 N  ND1 . HIS   B 1 19  ? 8.379  -7.620  12.681 1.00 24.90 ? 25  HIS   C ND1 1 
ATOM   1251 C  CD2 . HIS   B 1 19  ? 7.023  -9.364  12.533 1.00 23.94 ? 25  HIS   C CD2 1 
ATOM   1252 C  CE1 . HIS   B 1 19  ? 7.203  -7.297  13.209 1.00 24.80 ? 25  HIS   C CE1 1 
ATOM   1253 N  NE2 . HIS   B 1 19  ? 6.362  -8.331  13.176 1.00 24.34 ? 25  HIS   C NE2 1 
ATOM   1254 N  N   . ASN   B 1 20  ? 9.355  -12.112 13.373 1.00 17.62 ? 26  ASN   C N   1 
ATOM   1255 C  CA  . ASN   B 1 20  ? 8.725  -12.845 14.472 1.00 18.75 ? 26  ASN   C CA  1 
ATOM   1256 C  C   . ASN   B 1 20  ? 9.658  -13.006 15.675 1.00 17.18 ? 26  ASN   C C   1 
ATOM   1257 O  O   . ASN   B 1 20  ? 9.229  -12.907 16.825 1.00 16.52 ? 26  ASN   C O   1 
ATOM   1258 C  CB  . ASN   B 1 20  ? 8.195  -14.213 14.034 1.00 20.00 ? 26  ASN   C CB  1 
ATOM   1259 C  CG  . ASN   B 1 20  ? 7.374  -14.895 15.132 1.00 26.65 ? 26  ASN   C CG  1 
ATOM   1260 O  OD1 . ASN   B 1 20  ? 6.249  -14.473 15.439 1.00 29.80 ? 26  ASN   C OD1 1 
ATOM   1261 N  ND2 . ASN   B 1 20  ? 7.930  -15.912 15.796 1.00 28.32 ? 26  ASN   C ND2 1 
ATOM   1262 N  N   . ASP   B 1 21  ? 10.980 -13.221 15.417 1.00 15.98 ? 27  ASP   C N   1 
ATOM   1263 C  CA  . ASP   B 1 21  ? 11.926 -13.319 16.515 1.00 15.85 ? 27  ASP   C CA  1 
ATOM   1264 C  C   . ASP   B 1 21  ? 11.968 -12.010 17.320 1.00 15.67 ? 27  ASP   C C   1 
ATOM   1265 O  O   . ASP   B 1 21  ? 11.899 -12.028 18.547 1.00 17.15 ? 27  ASP   C O   1 
ATOM   1266 C  CB  . ASP   B 1 21  ? 13.344 -13.628 16.001 1.00 15.41 ? 27  ASP   C CB  1 
ATOM   1267 C  CG  . ASP   B 1 21  ? 13.553 -15.050 15.525 1.00 16.03 ? 27  ASP   C CG  1 
ATOM   1268 O  OD1 . ASP   B 1 21  ? 12.974 -15.972 16.139 1.00 17.54 ? 27  ASP   C OD1 1 
ATOM   1269 O  OD2 . ASP   B 1 21  ? 14.252 -15.239 14.491 1.00 15.71 ? 27  ASP   C OD2 1 
ATOM   1270 N  N   . TRP   B 1 22  ? 12.085 -10.856 16.621 1.00 16.24 ? 28  TRP   C N   1 
ATOM   1271 C  CA  . TRP   B 1 22  ? 12.117 -9.559  17.293 1.00 16.81 ? 28  TRP   C CA  1 
ATOM   1272 C  C   . TRP   B 1 22  ? 10.787 -9.219  18.001 1.00 16.18 ? 28  TRP   C C   1 
ATOM   1273 O  O   . TRP   B 1 22  ? 10.806 -8.594  19.077 1.00 16.92 ? 28  TRP   C O   1 
ATOM   1274 C  CB  . TRP   B 1 22  ? 12.497 -8.468  16.304 1.00 16.95 ? 28  TRP   C CB  1 
ATOM   1275 C  CG  . TRP   B 1 22  ? 13.976 -8.425  16.057 1.00 16.42 ? 28  TRP   C CG  1 
ATOM   1276 C  CD1 . TRP   B 1 22  ? 14.640 -8.918  14.969 1.00 17.03 ? 28  TRP   C CD1 1 
ATOM   1277 C  CD2 . TRP   B 1 22  ? 14.983 -7.833  16.910 1.00 15.34 ? 28  TRP   C CD2 1 
ATOM   1278 N  NE1 . TRP   B 1 22  ? 15.993 -8.636  15.067 1.00 16.92 ? 28  TRP   C NE1 1 
ATOM   1279 C  CE2 . TRP   B 1 22  ? 16.222 -7.953  16.241 1.00 17.03 ? 28  TRP   C CE2 1 
ATOM   1280 C  CE3 . TRP   B 1 22  ? 14.935 -7.107  18.115 1.00 17.36 ? 28  TRP   C CE3 1 
ATOM   1281 C  CZ2 . TRP   B 1 22  ? 17.405 -7.419  16.746 1.00 16.52 ? 28  TRP   C CZ2 1 
ATOM   1282 C  CZ3 . TRP   B 1 22  ? 16.133 -6.622  18.637 1.00 17.84 ? 28  TRP   C CZ3 1 
ATOM   1283 C  CH2 . TRP   B 1 22  ? 17.344 -6.773  17.938 1.00 17.60 ? 28  TRP   C CH2 1 
ATOM   1284 N  N   . ALA   B 1 23  ? 9.663  -9.696  17.451 1.00 16.23 ? 29  ALA   C N   1 
ATOM   1285 C  CA  . ALA   B 1 23  ? 8.336  -9.475  18.056 1.00 17.24 ? 29  ALA   C CA  1 
ATOM   1286 C  C   . ALA   B 1 23  ? 8.090  -10.356 19.290 1.00 18.76 ? 29  ALA   C C   1 
ATOM   1287 O  O   . ALA   B 1 23  ? 7.124  -10.126 20.026 1.00 19.99 ? 29  ALA   C O   1 
ATOM   1288 C  CB  . ALA   B 1 23  ? 7.232  -9.728  17.026 1.00 17.90 ? 29  ALA   C CB  1 
ATOM   1289 N  N   . ASN   B 1 24  ? 8.938  -11.388 19.514 1.00 18.16 ? 30  ASN   C N   1 
ATOM   1290 C  CA  . ASN   B 1 24  ? 8.833  -12.292 20.668 1.00 17.25 ? 30  ASN   C CA  1 
ATOM   1291 C  C   . ASN   B 1 24  ? 10.203 -12.363 21.363 1.00 17.07 ? 30  ASN   C C   1 
ATOM   1292 O  O   . ASN   B 1 24  ? 10.628 -13.425 21.786 1.00 16.77 ? 30  ASN   C O   1 
ATOM   1293 C  CB  . ASN   B 1 24  ? 8.366  -13.677 20.173 1.00 18.83 ? 30  ASN   C CB  1 
ATOM   1294 C  CG  . ASN   B 1 24  ? 6.943  -13.613 19.677 1.00 19.92 ? 30  ASN   C CG  1 
ATOM   1295 O  OD1 . ASN   B 1 24  ? 5.995  -13.625 20.506 1.00 22.06 ? 30  ASN   C OD1 1 
ATOM   1296 N  ND2 . ASN   B 1 24  ? 6.768  -13.507 18.359 1.00 19.91 ? 30  ASN   C ND2 1 
ATOM   1297 N  N   . LEU   B 1 25  ? 10.906 -11.251 21.451 1.00 17.05 ? 31  LEU   C N   1 
ATOM   1298 C  CA  . LEU   B 1 25  ? 12.277 -11.215 21.936 1.00 16.28 ? 31  LEU   C CA  1 
ATOM   1299 C  C   . LEU   B 1 25  ? 12.412 -11.533 23.402 1.00 17.75 ? 31  LEU   C C   1 
ATOM   1300 O  O   . LEU   B 1 25  ? 11.657 -11.014 24.238 1.00 18.75 ? 31  LEU   C O   1 
ATOM   1301 C  CB  . LEU   B 1 25  ? 12.820 -9.801  21.669 1.00 17.28 ? 31  LEU   C CB  1 
ATOM   1302 C  CG  . LEU   B 1 25  ? 14.296 -9.636  22.012 1.00 17.66 ? 31  LEU   C CG  1 
ATOM   1303 C  CD1 . LEU   B 1 25  ? 15.191 -10.533 21.114 1.00 17.94 ? 31  LEU   C CD1 1 
ATOM   1304 C  CD2 . LEU   B 1 25  ? 14.729 -8.197  21.870 1.00 19.91 ? 31  LEU   C CD2 1 
ATOM   1305 N  N   . VAL   B 1 26  ? 13.398 -12.363 23.735 1.00 16.93 ? 32  VAL   C N   1 
ATOM   1306 C  CA  . VAL   B 1 26  ? 13.746 -12.642 25.127 1.00 17.52 ? 32  VAL   C CA  1 
ATOM   1307 C  C   . VAL   B 1 26  ? 15.085 -11.918 25.452 1.00 18.02 ? 32  VAL   C C   1 
ATOM   1308 O  O   . VAL   B 1 26  ? 15.212 -11.244 26.492 1.00 19.45 ? 32  VAL   C O   1 
ATOM   1309 C  CB  . VAL   B 1 26  ? 13.901 -14.157 25.357 1.00 17.57 ? 32  VAL   C CB  1 
ATOM   1310 C  CG1 . VAL   B 1 26  ? 14.451 -14.433 26.763 1.00 19.25 ? 32  VAL   C CG1 1 
ATOM   1311 C  CG2 . VAL   B 1 26  ? 12.562 -14.872 25.144 1.00 17.14 ? 32  VAL   C CG2 1 
ATOM   1312 N  N   . TRP   B 1 27  ? 16.110 -12.071 24.576 1.00 16.00 ? 33  TRP   C N   1 
ATOM   1313 C  CA  . TRP   B 1 27  ? 17.431 -11.489 24.840 1.00 15.93 ? 33  TRP   C CA  1 
ATOM   1314 C  C   . TRP   B 1 27  ? 18.223 -11.431 23.530 1.00 16.23 ? 33  TRP   C C   1 
ATOM   1315 O  O   . TRP   B 1 27  ? 18.025 -12.297 22.667 1.00 16.16 ? 33  TRP   C O   1 
ATOM   1316 C  CB  . TRP   B 1 27  ? 18.162 -12.372 25.880 1.00 16.90 ? 33  TRP   C CB  1 
ATOM   1317 C  CG  . TRP   B 1 27  ? 19.640 -12.118 26.079 1.00 17.50 ? 33  TRP   C CG  1 
ATOM   1318 C  CD1 . TRP   B 1 27  ? 20.223 -11.177 26.883 1.00 19.93 ? 33  TRP   C CD1 1 
ATOM   1319 C  CD2 . TRP   B 1 27  ? 20.719 -12.821 25.442 1.00 16.83 ? 33  TRP   C CD2 1 
ATOM   1320 N  NE1 . TRP   B 1 27  ? 21.607 -11.291 26.826 1.00 21.08 ? 33  TRP   C NE1 1 
ATOM   1321 C  CE2 . TRP   B 1 27  ? 21.931 -12.300 25.955 1.00 18.48 ? 33  TRP   C CE2 1 
ATOM   1322 C  CE3 . TRP   B 1 27  ? 20.782 -13.838 24.477 1.00 16.65 ? 33  TRP   C CE3 1 
ATOM   1323 C  CZ2 . TRP   B 1 27  ? 23.183 -12.786 25.560 1.00 18.14 ? 33  TRP   C CZ2 1 
ATOM   1324 C  CZ3 . TRP   B 1 27  ? 22.027 -14.340 24.132 1.00 18.05 ? 33  TRP   C CZ3 1 
ATOM   1325 C  CH2 . TRP   B 1 27  ? 23.196 -13.766 24.616 1.00 18.08 ? 33  TRP   C CH2 1 
ATOM   1326 N  N   . GLU   B 1 28  ? 19.071 -10.425 23.371 1.00 15.11 ? 34  GLU   C N   1 
ATOM   1327 C  CA  . GLU   B 1 28  ? 19.928 -10.337 22.197 1.00 16.08 ? 34  GLU   C CA  1 
ATOM   1328 C  C   . GLU   B 1 28  ? 21.236 -9.652  22.550 1.00 16.33 ? 34  GLU   C C   1 
ATOM   1329 O  O   . GLU   B 1 28  ? 21.265 -8.781  23.462 1.00 16.93 ? 34  GLU   C O   1 
ATOM   1330 C  CB  . GLU   B 1 28  ? 19.216 -9.650  21.031 1.00 16.65 ? 34  GLU   C CB  1 
ATOM   1331 C  CG  . GLU   B 1 28  ? 18.669 -8.266  21.309 1.00 17.56 ? 34  GLU   C CG  1 
ATOM   1332 C  CD  . GLU   B 1 28  ? 19.651 -7.106  21.247 1.00 19.39 ? 34  GLU   C CD  1 
ATOM   1333 O  OE1 . GLU   B 1 28  ? 19.387 -6.075  21.912 1.00 22.11 ? 34  GLU   C OE1 1 
ATOM   1334 O  OE2 . GLU   B 1 28  ? 20.664 -7.192  20.507 1.00 18.14 ? 34  GLU   C OE2 1 
ATOM   1335 N  N   . ASP   B 1 29  ? 22.315 -10.031 21.843 1.00 14.80 ? 35  ASP   C N   1 
ATOM   1336 C  CA  . ASP   B 1 29  ? 23.609 -9.400  22.090 1.00 15.23 ? 35  ASP   C CA  1 
ATOM   1337 C  C   . ASP   B 1 29  ? 24.373 -9.359  20.766 1.00 15.20 ? 35  ASP   C C   1 
ATOM   1338 O  O   . ASP   B 1 29  ? 24.811 -10.400 20.264 1.00 14.96 ? 35  ASP   C O   1 
ATOM   1339 C  CB  . ASP   B 1 29  ? 24.352 -10.183 23.182 1.00 15.91 ? 35  ASP   C CB  1 
ATOM   1340 C  CG  . ASP   B 1 29  ? 25.684 -9.618  23.578 1.00 20.03 ? 35  ASP   C CG  1 
ATOM   1341 O  OD1 . ASP   B 1 29  ? 26.415 -9.149  22.689 1.00 20.05 ? 35  ASP   C OD1 1 
ATOM   1342 O  OD2 . ASP   B 1 29  ? 26.049 -9.750  24.756 1.00 22.85 ? 35  ASP   C OD2 1 
ATOM   1343 N  N   . SER   B 1 30  ? 24.531 -8.152  20.186 1.00 14.49 ? 36  SER   C N   1 
ATOM   1344 C  CA  A SER   B 1 30  ? 25.228 -7.992  18.918 0.50 14.80 ? 36  SER   C CA  1 
ATOM   1345 C  CA  B SER   B 1 30  ? 25.211 -8.052  18.903 0.50 15.18 ? 36  SER   C CA  1 
ATOM   1346 C  C   . SER   B 1 30  ? 26.695 -8.429  19.005 1.00 15.43 ? 36  SER   C C   1 
ATOM   1347 O  O   . SER   B 1 30  ? 27.216 -9.040  18.052 1.00 14.85 ? 36  SER   C O   1 
ATOM   1348 C  CB  A SER   B 1 30  ? 25.153 -6.537  18.458 0.50 16.06 ? 36  SER   C CB  1 
ATOM   1349 C  CB  B SER   B 1 30  ? 25.025 -6.672  18.292 0.50 17.84 ? 36  SER   C CB  1 
ATOM   1350 O  OG  A SER   B 1 30  ? 26.057 -6.273  17.395 0.50 16.29 ? 36  SER   C OG  1 
ATOM   1351 O  OG  B SER   B 1 30  ? 25.515 -5.700  19.194 0.50 19.99 ? 36  SER   C OG  1 
ATOM   1352 N  N   . SER   B 1 31  ? 27.364 -8.148  20.153 1.00 15.26 ? 37  SER   C N   1 
ATOM   1353 C  CA  . SER   B 1 31  ? 28.771 -8.542  20.268 1.00 16.21 ? 37  SER   C CA  1 
ATOM   1354 C  C   . SER   B 1 31  ? 28.964 -10.053 20.216 1.00 15.17 ? 37  SER   C C   1 
ATOM   1355 O  O   . SER   B 1 31  ? 30.062 -10.508 19.871 1.00 15.97 ? 37  SER   C O   1 
ATOM   1356 C  CB  . SER   B 1 31  ? 29.401 -7.980  21.531 1.00 19.25 ? 37  SER   C CB  1 
ATOM   1357 O  OG  . SER   B 1 31  ? 29.039 -8.697  22.690 1.00 23.47 ? 37  SER   C OG  1 
ATOM   1358 N  N   . ARG   B 1 32  ? 27.923 -10.853 20.536 1.00 14.40 ? 38  ARG   C N   1 
ATOM   1359 C  CA  . ARG   B 1 32  ? 28.019 -12.317 20.471 1.00 14.62 ? 38  ARG   C CA  1 
ATOM   1360 C  C   . ARG   B 1 32  ? 27.368 -12.893 19.205 1.00 13.87 ? 38  ARG   C C   1 
ATOM   1361 O  O   . ARG   B 1 32  ? 27.387 -14.111 19.003 1.00 12.98 ? 38  ARG   C O   1 
ATOM   1362 C  CB  . ARG   B 1 32  ? 27.278 -12.916 21.695 1.00 16.61 ? 38  ARG   C CB  1 
ATOM   1363 C  CG  . ARG   B 1 32  ? 27.949 -12.552 23.026 1.00 16.95 ? 38  ARG   C CG  1 
ATOM   1364 C  CD  . ARG   B 1 32  ? 27.195 -13.128 24.230 1.00 14.70 ? 38  ARG   C CD  1 
ATOM   1365 N  NE  . ARG   B 1 32  ? 27.253 -14.603 24.268 1.00 13.97 ? 38  ARG   C NE  1 
ATOM   1366 C  CZ  . ARG   B 1 32  ? 27.202 -15.331 25.379 1.00 13.86 ? 38  ARG   C CZ  1 
ATOM   1367 N  NH1 . ARG   B 1 32  ? 27.091 -14.747 26.561 1.00 15.36 ? 38  ARG   C NH1 1 
ATOM   1368 N  NH2 . ARG   B 1 32  ? 27.371 -16.654 25.322 1.00 14.82 ? 38  ARG   C NH2 1 
ATOM   1369 N  N   . ASP   B 1 33  ? 26.683 -12.060 18.389 1.00 12.48 ? 39  ASP   C N   1 
ATOM   1370 C  CA  . ASP   B 1 33  ? 25.894 -12.501 17.247 1.00 12.60 ? 39  ASP   C CA  1 
ATOM   1371 C  C   . ASP   B 1 33  ? 24.789 -13.474 17.693 1.00 12.61 ? 39  ASP   C C   1 
ATOM   1372 O  O   . ASP   B 1 33  ? 24.489 -14.399 16.943 1.00 12.93 ? 39  ASP   C O   1 
ATOM   1373 C  CB  . ASP   B 1 33  ? 26.739 -13.110 16.126 1.00 12.85 ? 39  ASP   C CB  1 
ATOM   1374 C  CG  . ASP   B 1 33  ? 25.948 -13.459 14.864 1.00 13.70 ? 39  ASP   C CG  1 
ATOM   1375 O  OD1 . ASP   B 1 33  ? 25.064 -12.659 14.458 1.00 14.45 ? 39  ASP   C OD1 1 
ATOM   1376 O  OD2 . ASP   B 1 33  ? 26.274 -14.474 14.211 1.00 13.37 ? 39  ASP   C OD2 1 
ATOM   1377 N  N   . LEU   B 1 34  ? 24.131 -13.244 18.858 1.00 12.02 ? 40  LEU   C N   1 
ATOM   1378 C  CA  . LEU   B 1 34  ? 23.054 -14.141 19.300 1.00 12.96 ? 40  LEU   C CA  1 
ATOM   1379 C  C   . LEU   B 1 34  ? 21.758 -13.384 19.546 1.00 13.41 ? 40  LEU   C C   1 
ATOM   1380 O  O   . LEU   B 1 34  ? 21.770 -12.233 20.009 1.00 13.63 ? 40  LEU   C O   1 
ATOM   1381 C  CB  . LEU   B 1 34  ? 23.440 -14.857 20.616 1.00 13.57 ? 40  LEU   C CB  1 
ATOM   1382 C  CG  . LEU   B 1 34  ? 24.527 -15.958 20.502 1.00 14.29 ? 40  LEU   C CG  1 
ATOM   1383 C  CD1 . LEU   B 1 34  ? 24.765 -16.564 21.898 1.00 14.95 ? 40  LEU   C CD1 1 
ATOM   1384 C  CD2 . LEU   B 1 34  ? 24.084 -17.062 19.525 1.00 15.25 ? 40  LEU   C CD2 1 
ATOM   1385 N  N   . LEU   B 1 35  ? 20.653 -14.085 19.312 1.00 12.45 ? 41  LEU   C N   1 
ATOM   1386 C  CA  . LEU   B 1 35  ? 19.330 -13.564 19.685 1.00 12.86 ? 41  LEU   C CA  1 
ATOM   1387 C  C   . LEU   B 1 35  ? 18.481 -14.790 20.086 1.00 13.10 ? 41  LEU   C C   1 
ATOM   1388 O  O   . LEU   B 1 35  ? 18.582 -15.860 19.475 1.00 13.86 ? 41  LEU   C O   1 
ATOM   1389 C  CB  . LEU   B 1 35  ? 18.669 -12.839 18.461 1.00 13.19 ? 41  LEU   C CB  1 
ATOM   1390 C  CG  . LEU   B 1 35  ? 17.270 -12.255 18.716 1.00 14.89 ? 41  LEU   C CG  1 
ATOM   1391 C  CD1 . LEU   B 1 35  ? 17.061 -10.947 17.951 1.00 16.63 ? 41  LEU   C CD1 1 
ATOM   1392 C  CD2 . LEU   B 1 35  ? 16.181 -13.286 18.384 1.00 14.60 ? 41  LEU   C CD2 1 
ATOM   1393 N  N   . VAL   B 1 36  ? 17.687 -14.623 21.143 1.00 13.49 ? 42  VAL   C N   1 
ATOM   1394 C  CA  . VAL   B 1 36  ? 16.773 -15.646 21.652 1.00 13.44 ? 42  VAL   C CA  1 
ATOM   1395 C  C   . VAL   B 1 36  ? 15.361 -15.088 21.655 1.00 14.16 ? 42  VAL   C C   1 
ATOM   1396 O  O   . VAL   B 1 36  ? 15.126 -13.955 22.141 1.00 15.05 ? 42  VAL   C O   1 
ATOM   1397 C  CB  . VAL   B 1 36  ? 17.186 -16.082 23.073 1.00 14.11 ? 42  VAL   C CB  1 
ATOM   1398 C  CG1 . VAL   B 1 36  ? 16.228 -17.149 23.611 1.00 15.65 ? 42  VAL   C CG1 1 
ATOM   1399 C  CG2 . VAL   B 1 36  ? 18.625 -16.624 23.076 1.00 14.68 ? 42  VAL   C CG2 1 
ATOM   1400 N  N   . SER   B 1 37  ? 14.440 -15.844 21.096 1.00 13.52 ? 43  SER   C N   1 
ATOM   1401 C  CA  . SER   B 1 37  ? 13.016 -15.505 21.059 1.00 13.50 ? 43  SER   C CA  1 
ATOM   1402 C  C   . SER   B 1 37  ? 12.207 -16.605 21.737 1.00 14.72 ? 43  SER   C C   1 
ATOM   1403 O  O   . SER   B 1 37  ? 12.693 -17.719 21.986 1.00 15.71 ? 43  SER   C O   1 
ATOM   1404 C  CB  . SER   B 1 37  ? 12.539 -15.313 19.624 1.00 14.97 ? 43  SER   C CB  1 
ATOM   1405 O  OG  . SER   B 1 37  ? 12.697 -16.481 18.820 1.00 16.63 ? 43  SER   C OG  1 
ATOM   1406 N  N   . SER   B 1 38  ? 10.971 -16.278 22.103 1.00 15.57 ? 44  SER   C N   1 
ATOM   1407 C  CA  . SER   B 1 38  ? 10.079 -17.240 22.766 1.00 16.24 ? 44  SER   C CA  1 
ATOM   1408 C  C   . SER   B 1 38  ? 9.257  -18.027 21.757 1.00 18.35 ? 44  SER   C C   1 
ATOM   1409 O  O   . SER   B 1 38  ? 8.949  -17.523 20.673 1.00 20.05 ? 44  SER   C O   1 
ATOM   1410 C  CB  . SER   B 1 38  ? 9.189  -16.527 23.782 1.00 19.30 ? 44  SER   C CB  1 
ATOM   1411 O  OG  . SER   B 1 38  ? 8.343  -15.621 23.100 1.00 23.71 ? 44  SER   C OG  1 
ATOM   1412 N  N   . THR   B 1 39  ? 8.914  -19.269 22.094 1.00 18.49 ? 45  THR   C N   1 
ATOM   1413 C  CA  . THR   B 1 39  ? 8.164  -20.134 21.185 1.00 19.99 ? 45  THR   C CA  1 
ATOM   1414 C  C   . THR   B 1 39  ? 6.878  -20.607 21.880 1.00 22.41 ? 45  THR   C C   1 
ATOM   1415 O  O   . THR   B 1 39  ? 6.818  -20.692 23.101 1.00 21.68 ? 45  THR   C O   1 
ATOM   1416 C  CB  . THR   B 1 39  ? 9.007  -21.393 20.813 1.00 20.22 ? 45  THR   C CB  1 
ATOM   1417 O  OG1 . THR   B 1 39  ? 9.248  -22.166 21.986 1.00 21.58 ? 45  THR   C OG1 1 
ATOM   1418 C  CG2 . THR   B 1 39  ? 10.383 -21.040 20.207 1.00 19.93 ? 45  THR   C CG2 1 
ATOM   1419 N  N   . THR   B 1 40  ? 5.883  -20.980 21.078 1.00 23.90 ? 46  THR   C N   1 
ATOM   1420 C  CA  . THR   B 1 40  ? 4.646  -21.538 21.645 1.00 25.96 ? 46  THR   C CA  1 
ATOM   1421 C  C   . THR   B 1 40  ? 4.855  -23.015 21.997 1.00 26.45 ? 46  THR   C C   1 
ATOM   1422 O  O   . THR   B 1 40  ? 4.450  -23.466 23.081 1.00 28.36 ? 46  THR   C O   1 
ATOM   1423 C  CB  . THR   B 1 40  ? 3.463  -21.311 20.708 1.00 30.13 ? 46  THR   C CB  1 
ATOM   1424 O  OG1 . THR   B 1 40  ? 3.771  -21.921 19.464 1.00 34.29 ? 46  THR   C OG1 1 
ATOM   1425 C  CG2 . THR   B 1 40  ? 3.212  -19.859 20.468 1.00 29.14 ? 46  THR   C CG2 1 
ATOM   1426 N  N   . ALA   B 1 41  ? 5.499  -23.772 21.087 1.00 24.65 ? 47  ALA   C N   1 
ATOM   1427 C  CA  . ALA   B 1 41  ? 5.755  -25.184 21.336 1.00 24.93 ? 47  ALA   C CA  1 
ATOM   1428 C  C   . ALA   B 1 41  ? 7.090  -25.415 22.054 1.00 22.80 ? 47  ALA   C C   1 
ATOM   1429 O  O   . ALA   B 1 41  ? 8.017  -24.634 21.881 1.00 22.32 ? 47  ALA   C O   1 
ATOM   1430 C  CB  . ALA   B 1 41  ? 5.752  -25.948 20.020 1.00 26.69 ? 47  ALA   C CB  1 
ATOM   1431 N  N   . GLN   B 1 42  ? 7.210  -26.470 22.840 1.00 22.83 ? 48  GLN   C N   1 
ATOM   1432 C  CA  . GLN   B 1 42  ? 8.446  -26.819 23.532 1.00 23.61 ? 48  GLN   C CA  1 
ATOM   1433 C  C   . GLN   B 1 42  ? 9.425  -27.476 22.556 1.00 22.79 ? 48  GLN   C C   1 
ATOM   1434 O  O   . GLN   B 1 42  ? 9.020  -28.255 21.690 1.00 24.25 ? 48  GLN   C O   1 
ATOM   1435 C  CB  . GLN   B 1 42  ? 8.157  -27.771 24.702 1.00 28.67 ? 48  GLN   C CB  1 
ATOM   1436 C  CG  . GLN   B 1 42  ? 7.497  -27.050 25.873 1.00 36.27 ? 48  GLN   C CG  1 
ATOM   1437 C  CD  . GLN   B 1 42  ? 7.294  -28.001 27.012 1.00 47.22 ? 48  GLN   C CD  1 
ATOM   1438 O  OE1 . GLN   B 1 42  ? 6.376  -28.834 27.006 1.00 51.43 ? 48  GLN   C OE1 1 
ATOM   1439 N  NE2 . GLN   B 1 42  ? 8.147  -27.906 28.017 1.00 49.90 ? 48  GLN   C NE2 1 
ATOM   1440 N  N   . GLY   B 1 43  ? 10.698 -27.126 22.695 1.00 20.17 ? 49  GLY   C N   1 
ATOM   1441 C  CA  . GLY   B 1 43  ? 11.798 -27.696 21.912 1.00 19.49 ? 49  GLY   C CA  1 
ATOM   1442 C  C   . GLY   B 1 43  ? 12.463 -28.851 22.638 1.00 19.18 ? 49  GLY   C C   1 
ATOM   1443 O  O   . GLY   B 1 43  ? 12.229 -29.052 23.840 1.00 21.97 ? 49  GLY   C O   1 
ATOM   1444 N  N   . CYS   B 1 44  ? 13.280 -29.578 21.924 1.00 18.10 ? 50  CYS   C N   1 
ATOM   1445 C  CA  . CYS   B 1 44  ? 13.849 -30.813 22.474 1.00 18.68 ? 50  CYS   C CA  1 
ATOM   1446 C  C   . CYS   B 1 44  ? 15.348 -30.857 22.544 1.00 19.39 ? 50  CYS   C C   1 
ATOM   1447 O  O   . CYS   B 1 44  ? 15.892 -31.896 22.960 1.00 22.03 ? 50  CYS   C O   1 
ATOM   1448 C  CB  . CYS   B 1 44  ? 13.307 -32.004 21.684 1.00 18.76 ? 50  CYS   C CB  1 
ATOM   1449 S  SG  . CYS   B 1 44  ? 11.488 -32.023 21.581 1.00 25.79 ? 50  CYS   C SG  1 
ATOM   1450 N  N   . ASP   B 1 45  ? 16.045 -29.777 22.190 1.00 16.43 ? 51  ASP   C N   1 
ATOM   1451 C  CA  . ASP   B 1 45  ? 17.509 -29.778 22.247 1.00 16.38 ? 51  ASP   C CA  1 
ATOM   1452 C  C   . ASP   B 1 45  ? 17.914 -29.572 23.699 1.00 16.94 ? 51  ASP   C C   1 
ATOM   1453 O  O   . ASP   B 1 45  ? 17.198 -28.921 24.490 1.00 18.66 ? 51  ASP   C O   1 
ATOM   1454 C  CB  . ASP   B 1 45  ? 18.070 -28.626 21.386 1.00 16.06 ? 51  ASP   C CB  1 
ATOM   1455 C  CG  . ASP   B 1 45  ? 17.876 -28.802 19.894 1.00 20.10 ? 51  ASP   C CG  1 
ATOM   1456 O  OD1 . ASP   B 1 45  ? 17.905 -29.946 19.423 1.00 20.97 ? 51  ASP   C OD1 1 
ATOM   1457 O  OD2 . ASP   B 1 45  ? 17.728 -27.777 19.180 1.00 18.03 ? 51  ASP   C OD2 1 
ATOM   1458 N  N   . THR   B 1 46  ? 19.027 -30.168 24.065 1.00 15.02 ? 52  THR   C N   1 
ATOM   1459 C  CA  . THR   B 1 46  ? 19.635 -30.009 25.389 1.00 15.18 ? 52  THR   C CA  1 
ATOM   1460 C  C   . THR   B 1 46  ? 20.920 -29.175 25.241 1.00 14.75 ? 52  THR   C C   1 
ATOM   1461 O  O   . THR   B 1 46  ? 21.723 -29.454 24.330 1.00 14.92 ? 52  THR   C O   1 
ATOM   1462 C  CB  . THR   B 1 46  ? 20.047 -31.379 25.957 1.00 17.37 ? 52  THR   C CB  1 
ATOM   1463 O  OG1 . THR   B 1 46  ? 18.865 -32.183 26.165 1.00 19.90 ? 52  THR   C OG1 1 
ATOM   1464 C  CG2 . THR   B 1 46  ? 20.841 -31.254 27.282 1.00 19.26 ? 52  THR   C CG2 1 
ATOM   1465 N  N   . ILE   B 1 47  ? 21.090 -28.123 26.049 1.00 14.26 ? 53  ILE   C N   1 
ATOM   1466 C  CA  . ILE   B 1 47  ? 22.283 -27.305 25.992 1.00 13.54 ? 53  ILE   C CA  1 
ATOM   1467 C  C   . ILE   B 1 47  ? 23.386 -27.973 26.840 1.00 13.64 ? 53  ILE   C C   1 
ATOM   1468 O  O   . ILE   B 1 47  ? 23.140 -28.413 27.972 1.00 14.69 ? 53  ILE   C O   1 
ATOM   1469 C  CB  . ILE   B 1 47  ? 22.013 -25.903 26.555 1.00 14.48 ? 53  ILE   C CB  1 
ATOM   1470 C  CG1 . ILE   B 1 47  ? 20.815 -25.226 25.908 1.00 15.35 ? 53  ILE   C CG1 1 
ATOM   1471 C  CG2 . ILE   B 1 47  ? 23.271 -25.022 26.476 1.00 15.63 ? 53  ILE   C CG2 1 
ATOM   1472 C  CD1 . ILE   B 1 47  ? 21.035 -25.073 24.360 1.00 17.92 ? 53  ILE   C CD1 1 
ATOM   1473 N  N   . ALA   B 1 48  ? 24.594 -28.055 26.273 1.00 12.51 ? 54  ALA   C N   1 
ATOM   1474 C  CA  . ALA   B 1 48  ? 25.727 -28.628 27.013 1.00 12.72 ? 54  ALA   C CA  1 
ATOM   1475 C  C   . ALA   B 1 48  ? 26.059 -27.693 28.198 1.00 13.00 ? 54  ALA   C C   1 
ATOM   1476 O  O   . ALA   B 1 48  ? 26.009 -26.454 28.062 1.00 13.09 ? 54  ALA   C O   1 
ATOM   1477 C  CB  . ALA   B 1 48  ? 26.936 -28.685 26.087 1.00 13.10 ? 54  ALA   C CB  1 
ATOM   1478 N  N   . ARG   B 1 49  ? 26.453 -28.277 29.352 1.00 12.45 ? 55  ARG   C N   1 
ATOM   1479 C  CA  . ARG   B 1 49  ? 26.913 -27.533 30.531 1.00 12.33 ? 55  ARG   C CA  1 
ATOM   1480 C  C   . ARG   B 1 49  ? 28.231 -28.198 30.906 1.00 13.84 ? 55  ARG   C C   1 
ATOM   1481 O  O   . ARG   B 1 49  ? 28.256 -29.230 31.581 1.00 14.72 ? 55  ARG   C O   1 
ATOM   1482 C  CB  . ARG   B 1 49  ? 25.872 -27.540 31.671 1.00 13.05 ? 55  ARG   C CB  1 
ATOM   1483 C  CG  . ARG   B 1 49  ? 24.518 -26.991 31.207 1.00 12.44 ? 55  ARG   C CG  1 
ATOM   1484 C  CD  . ARG   B 1 49  ? 24.528 -25.503 30.892 1.00 14.69 ? 55  ARG   C CD  1 
ATOM   1485 N  NE  . ARG   B 1 49  ? 23.179 -25.068 30.487 1.00 15.33 ? 55  ARG   C NE  1 
ATOM   1486 C  CZ  . ARG   B 1 49  ? 22.933 -23.973 29.772 1.00 15.13 ? 55  ARG   C CZ  1 
ATOM   1487 N  NH1 . ARG   B 1 49  ? 23.921 -23.155 29.437 1.00 15.04 ? 55  ARG   C NH1 1 
ATOM   1488 N  NH2 . ARG   B 1 49  ? 21.682 -23.696 29.357 1.00 14.88 ? 55  ARG   C NH2 1 
ATOM   1489 N  N   . CYS   B 1 50  ? 29.333 -27.628 30.366 1.00 13.10 ? 56  CYS   C N   1 
ATOM   1490 C  CA  . CYS   B 1 50  ? 30.654 -28.286 30.413 1.00 13.28 ? 56  CYS   C CA  1 
ATOM   1491 C  C   . CYS   B 1 50  ? 31.714 -27.329 29.898 1.00 13.07 ? 56  CYS   C C   1 
ATOM   1492 O  O   . CYS   B 1 50  ? 31.417 -26.214 29.445 1.00 13.87 ? 56  CYS   C O   1 
ATOM   1493 C  CB  . CYS   B 1 50  ? 30.591 -29.501 29.476 1.00 13.52 ? 56  CYS   C CB  1 
ATOM   1494 S  SG  . CYS   B 1 50  ? 30.454 -29.059 27.706 1.00 13.00 ? 56  CYS   C SG  1 
ATOM   1495 N  N   . ASP   B 1 51  ? 32.994 -27.796 29.918 1.00 14.29 ? 57  ASP   C N   1 
ATOM   1496 C  CA  . ASP   B 1 51  ? 34.143 -27.074 29.342 1.00 15.14 ? 57  ASP   C CA  1 
ATOM   1497 C  C   . ASP   B 1 51  ? 34.812 -27.947 28.241 1.00 15.69 ? 57  ASP   C C   1 
ATOM   1498 O  O   . ASP   B 1 51  ? 36.011 -27.813 27.993 1.00 16.30 ? 57  ASP   C O   1 
ATOM   1499 C  CB  . ASP   B 1 51  ? 35.155 -26.642 30.412 1.00 17.66 ? 57  ASP   C CB  1 
ATOM   1500 C  CG  . ASP   B 1 51  ? 35.826 -27.767 31.119 1.00 20.90 ? 57  ASP   C CG  1 
ATOM   1501 O  OD1 . ASP   B 1 51  ? 35.484 -28.925 30.859 1.00 20.33 ? 57  ASP   C OD1 1 
ATOM   1502 O  OD2 . ASP   B 1 51  ? 36.782 -27.488 31.909 1.00 26.69 ? 57  ASP   C OD2 1 
ATOM   1503 N  N   . CYS   B 1 52  ? 34.025 -28.783 27.539 1.00 14.63 ? 58  CYS   C N   1 
ATOM   1504 C  CA  . CYS   B 1 52  ? 34.575 -29.568 26.396 1.00 13.49 ? 58  CYS   C CA  1 
ATOM   1505 C  C   . CYS   B 1 52  ? 35.252 -28.653 25.380 1.00 12.83 ? 58  CYS   C C   1 
ATOM   1506 O  O   . CYS   B 1 52  ? 34.804 -27.507 25.136 1.00 13.59 ? 58  CYS   C O   1 
ATOM   1507 C  CB  . CYS   B 1 52  ? 33.482 -30.371 25.684 1.00 13.54 ? 58  CYS   C CB  1 
ATOM   1508 S  SG  . CYS   B 1 52  ? 32.863 -31.804 26.602 1.00 14.00 ? 58  CYS   C SG  1 
ATOM   1509 N  N   . GLN   B 1 53  ? 36.285 -29.185 24.747 1.00 12.72 ? 59  GLN   C N   1 
ATOM   1510 C  CA  . GLN   B 1 53  ? 36.978 -28.574 23.617 1.00 13.41 ? 59  GLN   C CA  1 
ATOM   1511 C  C   . GLN   B 1 53  ? 37.045 -29.513 22.449 1.00 13.14 ? 59  GLN   C C   1 
ATOM   1512 O  O   . GLN   B 1 53  ? 37.799 -29.270 21.492 1.00 13.57 ? 59  GLN   C O   1 
ATOM   1513 C  CB  . GLN   B 1 53  ? 38.397 -28.121 24.014 1.00 14.28 ? 59  GLN   C CB  1 
ATOM   1514 C  CG  . GLN   B 1 53  ? 38.359 -26.888 24.894 1.00 18.26 ? 59  GLN   C CG  1 
ATOM   1515 C  CD  . GLN   B 1 53  ? 39.726 -26.334 25.121 1.00 19.73 ? 59  GLN   C CD  1 
ATOM   1516 O  OE1 . GLN   B 1 53  ? 40.228 -26.363 26.274 1.00 21.55 ? 59  GLN   C OE1 1 
ATOM   1517 N  NE2 . GLN   B 1 53  ? 40.368 -25.795 24.056 1.00 17.74 ? 59  GLN   C NE2 1 
ATOM   1518 N  N   . THR   B 1 54  ? 36.257 -30.621 22.451 1.00 13.30 ? 60  THR   C N   1 
ATOM   1519 C  CA  . THR   B 1 54  ? 36.130 -31.462 21.268 1.00 14.15 ? 60  THR   C CA  1 
ATOM   1520 C  C   . THR   B 1 54  ? 34.629 -31.726 21.033 1.00 13.57 ? 60  THR   C C   1 
ATOM   1521 O  O   . THR   B 1 54  ? 33.847 -31.832 21.990 1.00 13.92 ? 60  THR   C O   1 
ATOM   1522 C  CB  . THR   B 1 54  ? 36.871 -32.768 21.330 1.00 17.41 ? 60  THR   C CB  1 
ATOM   1523 O  OG1 . THR   B 1 54  ? 36.324 -33.562 22.327 1.00 21.45 ? 60  THR   C OG1 1 
ATOM   1524 C  CG2 . THR   B 1 54  ? 38.365 -32.591 21.633 1.00 17.01 ? 60  THR   C CG2 1 
ATOM   1525 N  N   . GLY   B 1 55  ? 34.226 -31.784 19.769 1.00 12.47 ? 61  GLY   C N   1 
ATOM   1526 C  CA  . GLY   B 1 55  ? 32.828 -32.028 19.426 1.00 12.89 ? 61  GLY   C CA  1 
ATOM   1527 C  C   . GLY   B 1 55  ? 32.698 -32.225 17.934 1.00 12.14 ? 61  GLY   C C   1 
ATOM   1528 O  O   . GLY   B 1 55  ? 33.682 -32.541 17.240 1.00 13.18 ? 61  GLY   C O   1 
ATOM   1529 N  N   . VAL   B 1 56  ? 31.459 -32.101 17.447 1.00 11.76 ? 62  VAL   C N   1 
ATOM   1530 C  CA  . VAL   B 1 56  ? 31.160 -32.305 16.015 1.00 11.18 ? 62  VAL   C CA  1 
ATOM   1531 C  C   . VAL   B 1 56  ? 30.261 -31.159 15.578 1.00 11.06 ? 62  VAL   C C   1 
ATOM   1532 O  O   . VAL   B 1 56  ? 29.312 -30.837 16.298 1.00 12.35 ? 62  VAL   C O   1 
ATOM   1533 C  CB  . VAL   B 1 56  ? 30.418 -33.667 15.852 1.00 12.12 ? 62  VAL   C CB  1 
ATOM   1534 C  CG1 . VAL   B 1 56  ? 29.894 -33.851 14.412 1.00 13.44 ? 62  VAL   C CG1 1 
ATOM   1535 C  CG2 . VAL   B 1 56  ? 31.322 -34.869 16.262 1.00 12.65 ? 62  VAL   C CG2 1 
ATOM   1536 N  N   . TYR   B 1 57  ? 30.517 -30.592 14.390 1.00 11.43 ? 63  TYR   C N   1 
ATOM   1537 C  CA  . TYR   B 1 57  ? 29.623 -29.511 13.905 1.00 10.44 ? 63  TYR   C CA  1 
ATOM   1538 C  C   . TYR   B 1 57  ? 29.056 -29.853 12.538 1.00 11.26 ? 63  TYR   C C   1 
ATOM   1539 O  O   . TYR   B 1 57  ? 29.729 -30.546 11.757 1.00 12.32 ? 63  TYR   C O   1 
ATOM   1540 C  CB  . TYR   B 1 57  ? 30.310 -28.096 13.885 1.00 11.42 ? 63  TYR   C CB  1 
ATOM   1541 C  CG  . TYR   B 1 57  ? 31.179 -27.789 12.660 1.00 11.89 ? 63  TYR   C CG  1 
ATOM   1542 C  CD1 . TYR   B 1 57  ? 32.467 -28.287 12.551 1.00 13.09 ? 63  TYR   C CD1 1 
ATOM   1543 C  CD2 . TYR   B 1 57  ? 30.719 -26.942 11.654 1.00 12.46 ? 63  TYR   C CD2 1 
ATOM   1544 C  CE1 . TYR   B 1 57  ? 33.284 -27.974 11.455 1.00 13.56 ? 63  TYR   C CE1 1 
ATOM   1545 C  CE2 . TYR   B 1 57  ? 31.528 -26.613 10.556 1.00 13.46 ? 63  TYR   C CE2 1 
ATOM   1546 C  CZ  . TYR   B 1 57  ? 32.808 -27.136 10.468 1.00 13.29 ? 63  TYR   C CZ  1 
ATOM   1547 O  OH  . TYR   B 1 57  ? 33.673 -26.833 9.404  1.00 15.18 ? 63  TYR   C OH  1 
ATOM   1548 N  N   . TYR   B 1 58  ? 27.907 -29.276 12.243 1.00 11.82 ? 64  TYR   C N   1 
ATOM   1549 C  CA  . TYR   B 1 58  ? 27.299 -29.452 10.915 1.00 11.73 ? 64  TYR   C CA  1 
ATOM   1550 C  C   . TYR   B 1 58  ? 27.677 -28.307 9.985  1.00 11.61 ? 64  TYR   C C   1 
ATOM   1551 O  O   . TYR   B 1 58  ? 27.434 -27.127 10.289 1.00 12.51 ? 64  TYR   C O   1 
ATOM   1552 C  CB  . TYR   B 1 58  ? 25.768 -29.569 10.999 1.00 12.58 ? 64  TYR   C CB  1 
ATOM   1553 C  CG  . TYR   B 1 58  ? 25.164 -29.834 9.627  1.00 13.74 ? 64  TYR   C CG  1 
ATOM   1554 C  CD1 . TYR   B 1 58  ? 25.485 -30.991 8.920  1.00 14.61 ? 64  TYR   C CD1 1 
ATOM   1555 C  CD2 . TYR   B 1 58  ? 24.314 -28.925 9.034  1.00 14.06 ? 64  TYR   C CD2 1 
ATOM   1556 C  CE1 . TYR   B 1 58  ? 25.007 -31.214 7.622  1.00 14.91 ? 64  TYR   C CE1 1 
ATOM   1557 C  CE2 . TYR   B 1 58  ? 23.797 -29.160 7.749  1.00 14.43 ? 64  TYR   C CE2 1 
ATOM   1558 C  CZ  . TYR   B 1 58  ? 24.118 -30.328 7.079  1.00 15.21 ? 64  TYR   C CZ  1 
ATOM   1559 O  OH  . TYR   B 1 58  ? 23.654 -30.553 5.778  1.00 18.78 ? 64  TYR   C OH  1 
ATOM   1560 N  N   . CYS   B 1 59  ? 28.214 -28.673 8.827  1.00 11.69 ? 65  CYS   C N   1 
ATOM   1561 C  CA  . CYS   B 1 59  ? 28.624 -27.729 7.755  1.00 12.26 ? 65  CYS   C CA  1 
ATOM   1562 C  C   . CYS   B 1 59  ? 27.670 -27.916 6.553  1.00 13.35 ? 65  CYS   C C   1 
ATOM   1563 O  O   . CYS   B 1 59  ? 27.829 -28.870 5.757  1.00 13.72 ? 65  CYS   C O   1 
ATOM   1564 C  CB  . CYS   B 1 59  ? 30.067 -28.003 7.367  1.00 12.25 ? 65  CYS   C CB  1 
ATOM   1565 S  SG  . CYS   B 1 59  ? 30.652 -26.946 6.020  1.00 14.57 ? 65  CYS   C SG  1 
ATOM   1566 N  N   . SER   B 1 60  ? 26.688 -27.018 6.420  1.00 13.87 ? 66  SER   C N   1 
ATOM   1567 C  CA  . SER   B 1 60  ? 25.700 -27.161 5.351  1.00 14.56 ? 66  SER   C CA  1 
ATOM   1568 C  C   . SER   B 1 60  ? 26.317 -27.073 3.950  1.00 15.40 ? 66  SER   C C   1 
ATOM   1569 O  O   . SER   B 1 60  ? 25.876 -27.816 3.072  1.00 16.78 ? 66  SER   C O   1 
ATOM   1570 C  CB  . SER   B 1 60  ? 24.597 -26.128 5.516  1.00 17.34 ? 66  SER   C CB  1 
ATOM   1571 O  OG  . SER   B 1 60  ? 23.683 -26.316 4.445  1.00 22.31 ? 66  SER   C OG  1 
ATOM   1572 N  N   . SER   B 1 61  ? 27.353 -26.233 3.760  1.00 13.99 ? 67  SER   C N   1 
ATOM   1573 C  CA  . SER   B 1 61  ? 27.987 -26.093 2.440  1.00 14.18 ? 67  SER   C CA  1 
ATOM   1574 C  C   . SER   B 1 61  ? 28.806 -27.304 2.034  1.00 15.98 ? 67  SER   C C   1 
ATOM   1575 O  O   . SER   B 1 61  ? 29.298 -27.334 0.894  1.00 17.75 ? 67  SER   C O   1 
ATOM   1576 C  CB  . SER   B 1 61  ? 28.843 -24.841 2.404  1.00 15.20 ? 67  SER   C CB  1 
ATOM   1577 O  OG  . SER   B 1 61  ? 29.955 -24.941 3.272  1.00 15.91 ? 67  SER   C OG  1 
ATOM   1578 N  N   . ARG   B 1 62  ? 28.968 -28.310 2.906  1.00 15.17 ? 68  ARG   C N   1 
ATOM   1579 C  CA  . ARG   B 1 62  ? 29.585 -29.580 2.546  1.00 15.18 ? 68  ARG   C CA  1 
ATOM   1580 C  C   . ARG   B 1 62  ? 28.637 -30.778 2.761  1.00 15.26 ? 68  ARG   C C   1 
ATOM   1581 O  O   . ARG   B 1 62  ? 29.053 -31.924 2.589  1.00 16.79 ? 68  ARG   C O   1 
ATOM   1582 C  CB  . ARG   B 1 62  ? 30.883 -29.811 3.316  1.00 15.47 ? 68  ARG   C CB  1 
ATOM   1583 C  CG  . ARG   B 1 62  ? 31.932 -28.710 3.120  1.00 19.36 ? 68  ARG   C CG  1 
ATOM   1584 C  CD  . ARG   B 1 62  ? 32.595 -28.940 1.788  1.00 19.90 ? 68  ARG   C CD  1 
ATOM   1585 N  NE  . ARG   B 1 62  ? 33.630 -27.909 1.496  1.00 21.65 ? 68  ARG   C NE  1 
ATOM   1586 C  CZ  . ARG   B 1 62  ? 33.405 -26.760 0.874  1.00 24.43 ? 68  ARG   C CZ  1 
ATOM   1587 N  NH1 . ARG   B 1 62  ? 32.203 -26.490 0.378  1.00 25.33 ? 68  ARG   C NH1 1 
ATOM   1588 N  NH2 . ARG   B 1 62  ? 34.420 -25.931 0.598  1.00 26.24 ? 68  ARG   C NH2 1 
ATOM   1589 N  N   . ARG   B 1 63  ? 27.431 -30.530 3.302  1.00 16.38 ? 69  ARG   C N   1 
ATOM   1590 C  CA  . ARG   B 1 63  ? 26.461 -31.583 3.732  1.00 17.98 ? 69  ARG   C CA  1 
ATOM   1591 C  C   . ARG   B 1 63  ? 27.172 -32.614 4.605  1.00 18.42 ? 69  ARG   C C   1 
ATOM   1592 O  O   . ARG   B 1 63  ? 27.049 -33.826 4.397  1.00 20.44 ? 69  ARG   C O   1 
ATOM   1593 C  CB  . ARG   B 1 63  ? 25.796 -32.272 2.517  1.00 18.49 ? 69  ARG   C CB  1 
ATOM   1594 C  CG  . ARG   B 1 63  ? 24.962 -31.384 1.635  1.00 22.05 ? 69  ARG   C CG  1 
ATOM   1595 C  CD  . ARG   B 1 63  ? 23.710 -30.983 2.327  1.00 27.03 ? 69  ARG   C CD  1 
ATOM   1596 N  NE  . ARG   B 1 63  ? 22.743 -30.511 1.348  1.00 29.42 ? 69  ARG   C NE  1 
ATOM   1597 C  CZ  . ARG   B 1 63  ? 22.550 -29.239 1.037  1.00 31.38 ? 69  ARG   C CZ  1 
ATOM   1598 N  NH1 . ARG   B 1 63  ? 23.291 -28.288 1.599  1.00 30.03 ? 69  ARG   C NH1 1 
ATOM   1599 N  NH2 . ARG   B 1 63  ? 21.616 -28.903 0.164  1.00 31.06 ? 69  ARG   C NH2 1 
ATOM   1600 N  N   . LYS   B 1 64  ? 28.003 -32.126 5.558  1.00 15.91 ? 70  LYS   C N   1 
ATOM   1601 C  CA  . LYS   B 1 64  ? 28.805 -33.028 6.358  1.00 16.54 ? 70  LYS   C CA  1 
ATOM   1602 C  C   . LYS   B 1 64  ? 28.906 -32.554 7.784  1.00 15.01 ? 70  LYS   C C   1 
ATOM   1603 O  O   . LYS   B 1 64  ? 28.941 -31.349 8.054  1.00 15.15 ? 70  LYS   C O   1 
ATOM   1604 C  CB  . LYS   B 1 64  ? 30.229 -33.093 5.763  1.00 20.68 ? 70  LYS   C CB  1 
ATOM   1605 C  CG  . LYS   B 1 64  ? 30.373 -34.081 4.602  1.00 31.85 ? 70  LYS   C CG  1 
ATOM   1606 C  CD  . LYS   B 1 64  ? 31.840 -34.373 4.302  1.00 39.71 ? 70  LYS   C CD  1 
ATOM   1607 C  CE  . LYS   B 1 64  ? 31.980 -35.291 3.116  1.00 44.89 ? 70  LYS   C CE  1 
ATOM   1608 N  NZ  . LYS   B 1 64  ? 31.256 -34.764 1.930  1.00 48.74 ? 70  LYS   C NZ  1 
ATOM   1609 N  N   . HIS   B 1 65  ? 29.006 -33.523 8.695  1.00 14.65 ? 71  HIS   C N   1 
ATOM   1610 C  CA  . HIS   B 1 65  ? 29.304 -33.251 10.102 1.00 14.44 ? 71  HIS   C CA  1 
ATOM   1611 C  C   . HIS   B 1 65  ? 30.770 -33.533 10.294 1.00 15.63 ? 71  HIS   C C   1 
ATOM   1612 O  O   . HIS   B 1 65  ? 31.253 -34.626 9.952  1.00 18.70 ? 71  HIS   C O   1 
ATOM   1613 C  CB  . HIS   B 1 65  ? 28.493 -34.166 11.020 1.00 14.59 ? 71  HIS   C CB  1 
ATOM   1614 C  CG  . HIS   B 1 65  ? 27.018 -33.884 10.988 1.00 13.27 ? 71  HIS   C CG  1 
ATOM   1615 N  ND1 . HIS   B 1 65  ? 26.356 -33.113 11.944 1.00 16.53 ? 71  HIS   C ND1 1 
ATOM   1616 C  CD2 . HIS   B 1 65  ? 26.121 -34.292 10.072 1.00 14.18 ? 71  HIS   C CD2 1 
ATOM   1617 C  CE1 . HIS   B 1 65  ? 25.064 -33.138 11.605 1.00 14.86 ? 71  HIS   C CE1 1 
ATOM   1618 N  NE2 . HIS   B 1 65  ? 24.878 -33.833 10.491 1.00 16.77 ? 71  HIS   C NE2 1 
ATOM   1619 N  N   . TYR   B 1 66  ? 31.532 -32.579 10.866 1.00 13.70 ? 72  TYR   C N   1 
ATOM   1620 C  CA  . TYR   B 1 66  ? 32.974 -32.771 11.025 1.00 13.29 ? 72  TYR   C CA  1 
ATOM   1621 C  C   . TYR   B 1 66  ? 33.343 -32.815 12.502 1.00 13.05 ? 72  TYR   C C   1 
ATOM   1622 O  O   . TYR   B 1 66  ? 32.925 -31.938 13.270 1.00 13.21 ? 72  TYR   C O   1 
ATOM   1623 C  CB  . TYR   B 1 66  ? 33.706 -31.537 10.449 1.00 14.24 ? 72  TYR   C CB  1 
ATOM   1624 C  CG  . TYR   B 1 66  ? 33.687 -31.432 8.936  1.00 14.57 ? 72  TYR   C CG  1 
ATOM   1625 C  CD1 . TYR   B 1 66  ? 34.524 -32.211 8.154  1.00 16.34 ? 72  TYR   C CD1 1 
ATOM   1626 C  CD2 . TYR   B 1 66  ? 32.863 -30.521 8.288  1.00 15.33 ? 72  TYR   C CD2 1 
ATOM   1627 C  CE1 . TYR   B 1 66  ? 34.558 -32.071 6.768  1.00 17.75 ? 72  TYR   C CE1 1 
ATOM   1628 C  CE2 . TYR   B 1 66  ? 32.882 -30.375 6.906  1.00 16.66 ? 72  TYR   C CE2 1 
ATOM   1629 C  CZ  . TYR   B 1 66  ? 33.730 -31.156 6.150  1.00 17.43 ? 72  TYR   C CZ  1 
ATOM   1630 O  OH  . TYR   B 1 66  ? 33.723 -30.994 4.772  1.00 19.19 ? 72  TYR   C OH  1 
ATOM   1631 N  N   . PRO   B 1 67  ? 34.157 -33.788 12.914 1.00 12.79 ? 73  PRO   C N   1 
ATOM   1632 C  CA  . PRO   B 1 67  ? 34.690 -33.757 14.293 1.00 12.57 ? 73  PRO   C CA  1 
ATOM   1633 C  C   . PRO   B 1 67  ? 35.811 -32.706 14.400 1.00 13.93 ? 73  PRO   C C   1 
ATOM   1634 O  O   . PRO   B 1 67  ? 36.686 -32.625 13.500 1.00 15.86 ? 73  PRO   C O   1 
ATOM   1635 C  CB  . PRO   B 1 67  ? 35.274 -35.162 14.503 1.00 14.98 ? 73  PRO   C CB  1 
ATOM   1636 C  CG  . PRO   B 1 67  ? 35.473 -35.715 13.124 1.00 17.68 ? 73  PRO   C CG  1 
ATOM   1637 C  CD  . PRO   B 1 67  ? 34.644 -34.958 12.131 1.00 14.03 ? 73  PRO   C CD  1 
ATOM   1638 N  N   . VAL   B 1 68  ? 35.783 -31.886 15.436 1.00 12.82 ? 74  VAL   C N   1 
ATOM   1639 C  CA  . VAL   B 1 68  ? 36.755 -30.796 15.571 1.00 12.93 ? 74  VAL   C CA  1 
ATOM   1640 C  C   . VAL   B 1 68  ? 37.160 -30.624 17.014 1.00 12.34 ? 74  VAL   C C   1 
ATOM   1641 O  O   . VAL   B 1 68  ? 36.411 -30.908 17.949 1.00 13.05 ? 74  VAL   C O   1 
ATOM   1642 C  CB  . VAL   B 1 68  ? 36.150 -29.423 15.085 1.00 15.07 ? 74  VAL   C CB  1 
ATOM   1643 C  CG1 . VAL   B 1 68  ? 36.082 -29.318 13.560 1.00 17.71 ? 74  VAL   C CG1 1 
ATOM   1644 C  CG2 . VAL   B 1 68  ? 34.803 -29.122 15.757 1.00 15.70 ? 74  VAL   C CG2 1 
ATOM   1645 N  N   . SER   B 1 69  ? 38.374 -30.069 17.179 1.00 12.34 ? 75  SER   C N   1 
ATOM   1646 C  CA  . SER   B 1 69  ? 38.847 -29.451 18.422 1.00 13.30 ? 75  SER   C CA  1 
ATOM   1647 C  C   . SER   B 1 69  ? 38.542 -27.958 18.316 1.00 12.63 ? 75  SER   C C   1 
ATOM   1648 O  O   . SER   B 1 69  ? 38.693 -27.352 17.233 1.00 13.23 ? 75  SER   C O   1 
ATOM   1649 C  CB  . SER   B 1 69  ? 40.352 -29.640 18.619 1.00 16.17 ? 75  SER   C CB  1 
ATOM   1650 O  OG  . SER   B 1 69  ? 40.621 -31.021 18.705 1.00 20.92 ? 75  SER   C OG  1 
ATOM   1651 N  N   . PHE   B 1 70  ? 38.078 -27.343 19.399 1.00 12.22 ? 76  PHE   C N   1 
ATOM   1652 C  CA  . PHE   B 1 70  ? 37.739 -25.922 19.367 1.00 12.22 ? 76  PHE   C CA  1 
ATOM   1653 C  C   . PHE   B 1 70  ? 38.245 -25.181 20.612 1.00 12.67 ? 76  PHE   C C   1 
ATOM   1654 O  O   . PHE   B 1 70  ? 38.414 -25.782 21.674 1.00 12.94 ? 76  PHE   C O   1 
ATOM   1655 C  CB  . PHE   B 1 70  ? 36.214 -25.671 19.108 1.00 12.49 ? 76  PHE   C CB  1 
ATOM   1656 C  CG  . PHE   B 1 70  ? 35.319 -26.383 20.119 1.00 11.84 ? 76  PHE   C CG  1 
ATOM   1657 C  CD1 . PHE   B 1 70  ? 34.878 -27.684 19.895 1.00 12.54 ? 76  PHE   C CD1 1 
ATOM   1658 C  CD2 . PHE   B 1 70  ? 34.877 -25.728 21.255 1.00 12.71 ? 76  PHE   C CD2 1 
ATOM   1659 C  CE1 . PHE   B 1 70  ? 34.067 -28.334 20.823 1.00 12.14 ? 76  PHE   C CE1 1 
ATOM   1660 C  CE2 . PHE   B 1 70  ? 34.044 -26.379 22.165 1.00 12.61 ? 76  PHE   C CE2 1 
ATOM   1661 C  CZ  . PHE   B 1 70  ? 33.666 -27.682 21.962 1.00 13.04 ? 76  PHE   C CZ  1 
ATOM   1662 N  N   . SER   B 1 71  ? 38.494 -23.895 20.472 1.00 11.80 ? 77  SER   C N   1 
ATOM   1663 C  CA  . SER   B 1 71  ? 39.113 -23.084 21.518 1.00 13.01 ? 77  SER   C CA  1 
ATOM   1664 C  C   . SER   B 1 71  ? 38.136 -22.693 22.630 1.00 14.16 ? 77  SER   C C   1 
ATOM   1665 O  O   . SER   B 1 71  ? 36.935 -22.994 22.569 1.00 15.10 ? 77  SER   C O   1 
ATOM   1666 C  CB  . SER   B 1 71  ? 39.842 -21.890 20.910 1.00 14.52 ? 77  SER   C CB  1 
ATOM   1667 O  OG  . SER   B 1 71  ? 38.915 -20.996 20.300 1.00 16.22 ? 77  SER   C OG  1 
ATOM   1668 N  N   . LYS   B 1 72  ? 38.642 -22.032 23.656 1.00 15.00 ? 78  LYS   C N   1 
ATOM   1669 C  CA  . LYS   B 1 72  ? 37.793 -21.619 24.784 1.00 14.56 ? 78  LYS   C CA  1 
ATOM   1670 C  C   . LYS   B 1 72  ? 37.035 -20.342 24.374 1.00 15.69 ? 78  LYS   C C   1 
ATOM   1671 O  O   . LYS   B 1 72  ? 37.581 -19.532 23.623 1.00 16.96 ? 78  LYS   C O   1 
ATOM   1672 C  CB  . LYS   B 1 72  ? 38.709 -21.264 25.986 1.00 19.12 ? 78  LYS   C CB  1 
ATOM   1673 C  CG  . LYS   B 1 72  ? 39.508 -22.459 26.464 1.00 21.37 ? 78  LYS   C CG  1 
ATOM   1674 C  CD  . LYS   B 1 72  ? 40.460 -22.101 27.615 1.00 32.24 ? 78  LYS   C CD  1 
ATOM   1675 C  CE  . LYS   B 1 72  ? 40.976 -23.366 28.278 1.00 40.70 ? 78  LYS   C CE  1 
ATOM   1676 N  NZ  . LYS   B 1 72  ? 39.845 -24.238 28.749 1.00 45.66 ? 78  LYS   C NZ  1 
ATOM   1677 N  N   . PRO   B 1 73  ? 35.802 -20.101 24.857 1.00 14.26 ? 79  PRO   C N   1 
ATOM   1678 C  CA  . PRO   B 1 73  ? 35.053 -18.861 24.464 1.00 15.00 ? 79  PRO   C CA  1 
ATOM   1679 C  C   . PRO   B 1 73  ? 35.832 -17.615 24.827 1.00 15.29 ? 79  PRO   C C   1 
ATOM   1680 O  O   . PRO   B 1 73  ? 36.271 -17.463 25.986 1.00 17.93 ? 79  PRO   C O   1 
ATOM   1681 C  CB  . PRO   B 1 73  ? 33.775 -18.907 25.302 1.00 17.14 ? 79  PRO   C CB  1 
ATOM   1682 C  CG  . PRO   B 1 73  ? 33.637 -20.338 25.701 1.00 18.69 ? 79  PRO   C CG  1 
ATOM   1683 C  CD  . PRO   B 1 73  ? 35.028 -20.959 25.785 1.00 15.43 ? 79  PRO   C CD  1 
ATOM   1684 N  N   . SER   B 1 74  ? 36.065 -16.745 23.839 1.00 14.17 ? 80  SER   C N   1 
ATOM   1685 C  CA  . SER   B 1 74  ? 36.952 -15.587 24.050 1.00 14.97 ? 80  SER   C CA  1 
ATOM   1686 C  C   . SER   B 1 74  ? 36.535 -14.415 23.171 1.00 14.60 ? 80  SER   C C   1 
ATOM   1687 O  O   . SER   B 1 74  ? 35.650 -14.545 22.333 1.00 14.72 ? 80  SER   C O   1 
ATOM   1688 C  CB  . SER   B 1 74  ? 38.379 -15.973 23.655 1.00 18.38 ? 80  SER   C CB  1 
ATOM   1689 O  OG  . SER   B 1 74  ? 38.828 -17.166 24.307 1.00 22.42 ? 80  SER   C OG  1 
ATOM   1690 N  N   . LEU   B 1 75  ? 37.227 -13.279 23.353 1.00 15.92 ? 81  LEU   C N   1 
ATOM   1691 C  CA  . LEU   B 1 75  ? 37.035 -12.052 22.581 1.00 17.05 ? 81  LEU   C CA  1 
ATOM   1692 C  C   . LEU   B 1 75  ? 38.049 -12.120 21.420 1.00 17.51 ? 81  LEU   C C   1 
ATOM   1693 O  O   . LEU   B 1 75  ? 39.278 -12.070 21.652 1.00 19.35 ? 81  LEU   C O   1 
ATOM   1694 C  CB  . LEU   B 1 75  ? 37.276 -10.820 23.491 1.00 19.14 ? 81  LEU   C CB  1 
ATOM   1695 C  CG  . LEU   B 1 75  ? 37.008 -9.469  22.879 1.00 22.16 ? 81  LEU   C CG  1 
ATOM   1696 C  CD1 . LEU   B 1 75  ? 35.515 -9.270  22.631 1.00 21.10 ? 81  LEU   C CD1 1 
ATOM   1697 C  CD2 . LEU   B 1 75  ? 37.510 -8.340  23.824 1.00 24.71 ? 81  LEU   C CD2 1 
ATOM   1698 N  N   . ILE   B 1 76  ? 37.571 -12.304 20.196 1.00 18.52 ? 82  ILE   C N   1 
ATOM   1699 C  CA  . ILE   B 1 76  ? 38.393 -12.536 19.017 1.00 19.87 ? 82  ILE   C CA  1 
ATOM   1700 C  C   . ILE   B 1 76  ? 38.120 -11.484 17.971 1.00 19.33 ? 82  ILE   C C   1 
ATOM   1701 O  O   . ILE   B 1 76  ? 36.938 -11.184 17.726 1.00 18.02 ? 82  ILE   C O   1 
ATOM   1702 C  CB  . ILE   B 1 76  ? 38.024 -13.933 18.444 1.00 21.97 ? 82  ILE   C CB  1 
ATOM   1703 C  CG1 . ILE   B 1 76  ? 38.231 -15.085 19.479 1.00 24.91 ? 82  ILE   C CG1 1 
ATOM   1704 C  CG2 . ILE   B 1 76  ? 38.717 -14.237 17.101 1.00 23.89 ? 82  ILE   C CG2 1 
ATOM   1705 C  CD1 . ILE   B 1 76  ? 39.550 -15.842 19.490 1.00 28.22 ? 82  ILE   C CD1 1 
ATOM   1706 N  N   . PHE   B 1 77  ? 39.178 -10.984 17.287 1.00 19.63 ? 83  PHE   C N   1 
ATOM   1707 C  CA  . PHE   B 1 77  ? 38.981 -10.053 16.178 1.00 20.60 ? 83  PHE   C CA  1 
ATOM   1708 C  C   . PHE   B 1 77  ? 38.596 -10.906 14.959 1.00 21.11 ? 83  PHE   C C   1 
ATOM   1709 O  O   . PHE   B 1 77  ? 39.275 -11.892 14.613 1.00 23.60 ? 83  PHE   C O   1 
ATOM   1710 C  CB  . PHE   B 1 77  ? 40.275 -9.267  15.876 1.00 21.22 ? 83  PHE   C CB  1 
ATOM   1711 C  CG  . PHE   B 1 77  ? 39.982 -8.070  14.976 1.00 21.60 ? 83  PHE   C CG  1 
ATOM   1712 C  CD1 . PHE   B 1 77  ? 39.234 -7.001  15.440 1.00 22.76 ? 83  PHE   C CD1 1 
ATOM   1713 C  CD2 . PHE   B 1 77  ? 40.336 -8.088  13.624 1.00 23.57 ? 83  PHE   C CD2 1 
ATOM   1714 C  CE1 . PHE   B 1 77  ? 38.913 -5.933  14.596 1.00 24.49 ? 83  PHE   C CE1 1 
ATOM   1715 C  CE2 . PHE   B 1 77  ? 40.022 -7.015  12.790 1.00 23.48 ? 83  PHE   C CE2 1 
ATOM   1716 C  CZ  . PHE   B 1 77  ? 39.332 -5.937  13.287 1.00 24.16 ? 83  PHE   C CZ  1 
ATOM   1717 N  N   . VAL   B 1 78  ? 37.481 -10.538 14.310 1.00 17.94 ? 84  VAL   C N   1 
ATOM   1718 C  CA  . VAL   B 1 78  ? 36.956 -11.261 13.163 1.00 18.45 ? 84  VAL   C CA  1 
ATOM   1719 C  C   . VAL   B 1 78  ? 37.050 -10.353 11.943 1.00 17.99 ? 84  VAL   C C   1 
ATOM   1720 O  O   . VAL   B 1 78  ? 36.572 -9.223  12.012 1.00 17.63 ? 84  VAL   C O   1 
ATOM   1721 C  CB  . VAL   B 1 78  ? 35.474 -11.660 13.458 1.00 19.24 ? 84  VAL   C CB  1 
ATOM   1722 C  CG1 . VAL   B 1 78  ? 34.908 -12.438 12.290 1.00 20.02 ? 84  VAL   C CG1 1 
ATOM   1723 C  CG2 . VAL   B 1 78  ? 35.371 -12.477 14.744 1.00 20.22 ? 84  VAL   C CG2 1 
ATOM   1724 N  N   . GLU   B 1 79  ? 37.558 -10.840 10.803 1.00 17.17 ? 85  GLU   C N   1 
ATOM   1725 C  CA  . GLU   B 1 79  ? 37.578 -10.040 9.580  1.00 17.38 ? 85  GLU   C CA  1 
ATOM   1726 C  C   . GLU   B 1 79  ? 36.170 -9.781  9.044  1.00 16.99 ? 85  GLU   C C   1 
ATOM   1727 O  O   . GLU   B 1 79  ? 35.205 -10.465 9.413  1.00 16.63 ? 85  GLU   C O   1 
ATOM   1728 C  CB  . GLU   B 1 79  ? 38.430 -10.734 8.496  1.00 20.39 ? 85  GLU   C CB  1 
ATOM   1729 C  CG  . GLU   B 1 79  ? 39.916 -10.792 8.857  1.00 24.32 ? 85  GLU   C CG  1 
ATOM   1730 C  CD  . GLU   B 1 79  ? 40.546 -9.433  9.124  1.00 34.17 ? 85  GLU   C CD  1 
ATOM   1731 O  OE1 . GLU   B 1 79  ? 40.314 -8.485  8.336  1.00 38.11 ? 85  GLU   C OE1 1 
ATOM   1732 O  OE2 . GLU   B 1 79  ? 41.248 -9.300  10.154 1.00 37.36 ? 85  GLU   C OE2 1 
ATOM   1733 N  N   . ALA   B 1 80  ? 36.032 -8.767  8.197  1.00 17.61 ? 86  ALA   C N   1 
ATOM   1734 C  CA  . ALA   B 1 80  ? 34.758 -8.403  7.619  1.00 18.75 ? 86  ALA   C CA  1 
ATOM   1735 C  C   . ALA   B 1 80  ? 34.136 -9.580  6.878  1.00 19.23 ? 86  ALA   C C   1 
ATOM   1736 O  O   . ALA   B 1 80  ? 34.863 -10.379 6.263  1.00 20.42 ? 86  ALA   C O   1 
ATOM   1737 C  CB  . ALA   B 1 80  ? 34.982 -7.246  6.634  1.00 20.27 ? 86  ALA   C CB  1 
ATOM   1738 N  N   . SER   B 1 81  ? 32.843 -9.746  7.041  1.00 18.20 ? 87  SER   C N   1 
ATOM   1739 C  CA  . SER   B 1 81  ? 32.113 -10.766 6.341  1.00 18.72 ? 87  SER   C CA  1 
ATOM   1740 C  C   . SER   B 1 81  ? 30.987 -10.104 5.555  1.00 20.10 ? 87  SER   C C   1 
ATOM   1741 O  O   . SER   B 1 81  ? 30.832 -8.860  5.568  1.00 20.59 ? 87  SER   C O   1 
ATOM   1742 C  CB  . SER   B 1 81  ? 31.555 -11.773 7.346  1.00 17.60 ? 87  SER   C CB  1 
ATOM   1743 O  OG  . SER   B 1 81  ? 30.516 -11.148 8.099  1.00 18.32 ? 87  SER   C OG  1 
ATOM   1744 N  N   . GLU   B 1 82  ? 30.173 -10.930 4.893  1.00 21.28 ? 88  GLU   C N   1 
ATOM   1745 C  CA  . GLU   B 1 82  ? 29.058 -10.320 4.166  1.00 21.96 ? 88  GLU   C CA  1 
ATOM   1746 C  C   . GLU   B 1 82  ? 28.006 -9.679  5.098  1.00 21.63 ? 88  GLU   C C   1 
ATOM   1747 O  O   . GLU   B 1 82  ? 27.252 -8.815  4.662  1.00 23.75 ? 88  GLU   C O   1 
ATOM   1748 C  CB  . GLU   B 1 82  ? 28.450 -11.313 3.176  1.00 26.83 ? 88  GLU   C CB  1 
ATOM   1749 C  CG  . GLU   B 1 82  ? 27.645 -12.449 3.753  1.00 35.30 ? 88  GLU   C CG  1 
ATOM   1750 C  CD  . GLU   B 1 82  ? 26.942 -13.208 2.641  1.00 41.50 ? 88  GLU   C CD  1 
ATOM   1751 O  OE1 . GLU   B 1 82  ? 27.569 -13.396 1.571  1.00 42.59 ? 88  GLU   C OE1 1 
ATOM   1752 O  OE2 . GLU   B 1 82  ? 25.770 -13.606 2.836  1.00 42.76 ? 88  GLU   C OE2 1 
ATOM   1753 N  N   . TYR   B 1 83  ? 28.021 -10.008 6.396  1.00 19.03 ? 89  TYR   C N   1 
ATOM   1754 C  CA  . TYR   B 1 83  ? 26.989 -9.539  7.312  1.00 18.34 ? 89  TYR   C CA  1 
ATOM   1755 C  C   . TYR   B 1 83  ? 27.495 -8.689  8.512  1.00 19.69 ? 89  TYR   C C   1 
ATOM   1756 O  O   . TYR   B 1 83  ? 26.660 -8.085  9.202  1.00 20.94 ? 89  TYR   C O   1 
ATOM   1757 C  CB  . TYR   B 1 83  ? 26.152 -10.754 7.795  1.00 18.11 ? 89  TYR   C CB  1 
ATOM   1758 C  CG  . TYR   B 1 83  ? 26.981 -11.951 8.264  1.00 18.03 ? 89  TYR   C CG  1 
ATOM   1759 C  CD1 . TYR   B 1 83  ? 27.394 -12.942 7.367  1.00 18.05 ? 89  TYR   C CD1 1 
ATOM   1760 C  CD2 . TYR   B 1 83  ? 27.388 -12.067 9.590  1.00 17.12 ? 89  TYR   C CD2 1 
ATOM   1761 C  CE1 . TYR   B 1 83  ? 28.169 -14.028 7.790  1.00 17.38 ? 89  TYR   C CE1 1 
ATOM   1762 C  CE2 . TYR   B 1 83  ? 28.161 -13.146 10.024 1.00 16.60 ? 89  TYR   C CE2 1 
ATOM   1763 C  CZ  . TYR   B 1 83  ? 28.552 -14.129 9.118  1.00 16.61 ? 89  TYR   C CZ  1 
ATOM   1764 O  OH  . TYR   B 1 83  ? 29.372 -15.168 9.521  1.00 17.57 ? 89  TYR   C OH  1 
ATOM   1765 N  N   . TYR   B 1 84  ? 28.821 -8.562  8.759  1.00 17.33 ? 90  TYR   C N   1 
ATOM   1766 C  CA  . TYR   B 1 84  ? 29.351 -7.632  9.773  1.00 17.30 ? 90  TYR   C CA  1 
ATOM   1767 C  C   . TYR   B 1 84  ? 30.681 -7.028  9.238  1.00 16.96 ? 90  TYR   C C   1 
ATOM   1768 O  O   . TYR   B 1 84  ? 31.404 -7.688  8.494  1.00 16.80 ? 90  TYR   C O   1 
ATOM   1769 C  CB  . TYR   B 1 84  ? 29.715 -8.354  11.106 1.00 16.86 ? 90  TYR   C CB  1 
ATOM   1770 C  CG  . TYR   B 1 84  ? 28.538 -8.794  11.947 1.00 15.18 ? 90  TYR   C CG  1 
ATOM   1771 C  CD1 . TYR   B 1 84  ? 27.630 -7.870  12.476 1.00 15.88 ? 90  TYR   C CD1 1 
ATOM   1772 C  CD2 . TYR   B 1 84  ? 28.364 -10.110 12.261 1.00 14.65 ? 90  TYR   C CD2 1 
ATOM   1773 C  CE1 . TYR   B 1 84  ? 26.561 -8.282  13.280 1.00 16.50 ? 90  TYR   C CE1 1 
ATOM   1774 C  CE2 . TYR   B 1 84  ? 27.297 -10.538 13.050 1.00 15.05 ? 90  TYR   C CE2 1 
ATOM   1775 C  CZ  . TYR   B 1 84  ? 26.410 -9.618  13.589 1.00 15.96 ? 90  TYR   C CZ  1 
ATOM   1776 O  OH  . TYR   B 1 84  ? 25.339 -10.033 14.385 1.00 15.22 ? 90  TYR   C OH  1 
ATOM   1777 N  N   . PRO   B 1 85  ? 31.057 -5.824  9.700  1.00 17.82 ? 91  PRO   C N   1 
ATOM   1778 C  CA  . PRO   B 1 85  ? 32.406 -5.313  9.401  1.00 17.44 ? 91  PRO   C CA  1 
ATOM   1779 C  C   . PRO   B 1 85  ? 33.448 -6.085  10.238 1.00 17.10 ? 91  PRO   C C   1 
ATOM   1780 O  O   . PRO   B 1 85  ? 33.094 -6.900  11.133 1.00 17.25 ? 91  PRO   C O   1 
ATOM   1781 C  CB  . PRO   B 1 85  ? 32.288 -3.837  9.849  1.00 18.56 ? 91  PRO   C CB  1 
ATOM   1782 C  CG  . PRO   B 1 85  ? 31.364 -3.916  11.047 1.00 19.09 ? 91  PRO   C CG  1 
ATOM   1783 C  CD  . PRO   B 1 85  ? 30.331 -4.983  10.695 1.00 18.30 ? 91  PRO   C CD  1 
ATOM   1784 N  N   . ALA   B 1 86  ? 34.735 -5.795  10.028 1.00 16.96 ? 92  ALA   C N   1 
ATOM   1785 C  CA  . ALA   B 1 86  ? 35.791 -6.349  10.864 1.00 18.64 ? 92  ALA   C CA  1 
ATOM   1786 C  C   . ALA   B 1 86  ? 35.597 -5.778  12.276 1.00 19.48 ? 92  ALA   C C   1 
ATOM   1787 O  O   . ALA   B 1 86  ? 35.295 -4.578  12.422 1.00 21.09 ? 92  ALA   C O   1 
ATOM   1788 C  CB  . ALA   B 1 86  ? 37.153 -5.924  10.310 1.00 18.77 ? 92  ALA   C CB  1 
ATOM   1789 N  N   . ARG   B 1 87  ? 35.595 -6.667  13.276 1.00 18.46 ? 93  ARG   C N   1 
ATOM   1790 C  CA  . ARG   B 1 87  ? 35.290 -6.230  14.631 1.00 18.80 ? 93  ARG   C CA  1 
ATOM   1791 C  C   . ARG   B 1 87  ? 35.685 -7.315  15.622 1.00 18.90 ? 93  ARG   C C   1 
ATOM   1792 O  O   . ARG   B 1 87  ? 35.905 -8.460  15.249 1.00 17.95 ? 93  ARG   C O   1 
ATOM   1793 C  CB  . ARG   B 1 87  ? 33.764 -5.957  14.786 1.00 19.29 ? 93  ARG   C CB  1 
ATOM   1794 C  CG  . ARG   B 1 87  ? 32.945 -7.262  14.692 1.00 17.79 ? 93  ARG   C CG  1 
ATOM   1795 C  CD  . ARG   B 1 87  ? 31.459 -6.984  14.805 1.00 18.41 ? 93  ARG   C CD  1 
ATOM   1796 N  NE  . ARG   B 1 87  ? 30.747 -8.252  15.028 1.00 17.44 ? 93  ARG   C NE  1 
ATOM   1797 C  CZ  . ARG   B 1 87  ? 29.683 -8.431  15.799 1.00 18.99 ? 93  ARG   C CZ  1 
ATOM   1798 N  NH1 . ARG   B 1 87  ? 29.063 -7.388  16.352 1.00 19.02 ? 93  ARG   C NH1 1 
ATOM   1799 N  NH2 . ARG   B 1 87  ? 29.209 -9.652  16.003 1.00 18.37 ? 93  ARG   C NH2 1 
ATOM   1800 N  N   . TYR   B 1 88  ? 35.660 -6.965  16.919 1.00 19.60 ? 94  TYR   C N   1 
ATOM   1801 C  CA  . TYR   B 1 88  ? 35.810 -7.947  17.989 1.00 20.87 ? 94  TYR   C CA  1 
ATOM   1802 C  C   . TYR   B 1 88  ? 34.426 -8.613  18.245 1.00 19.18 ? 94  TYR   C C   1 
ATOM   1803 O  O   . TYR   B 1 88  ? 33.400 -7.925  18.289 1.00 20.64 ? 94  TYR   C O   1 
ATOM   1804 C  CB  . TYR   B 1 88  ? 36.202 -7.203  19.278 1.00 23.44 ? 94  TYR   C CB  1 
ATOM   1805 C  CG  . TYR   B 1 88  ? 37.665 -6.830  19.277 1.00 26.27 ? 94  TYR   C CG  1 
ATOM   1806 C  CD1 . TYR   B 1 88  ? 38.637 -7.778  19.540 1.00 26.86 ? 94  TYR   C CD1 1 
ATOM   1807 C  CD2 . TYR   B 1 88  ? 38.080 -5.553  18.904 1.00 27.48 ? 94  TYR   C CD2 1 
ATOM   1808 C  CE1 . TYR   B 1 88  ? 39.992 -7.453  19.506 1.00 27.79 ? 94  TYR   C CE1 1 
ATOM   1809 C  CE2 . TYR   B 1 88  ? 39.423 -5.217  18.867 1.00 28.56 ? 94  TYR   C CE2 1 
ATOM   1810 C  CZ  . TYR   B 1 88  ? 40.377 -6.175  19.147 1.00 29.46 ? 94  TYR   C CZ  1 
ATOM   1811 O  OH  . TYR   B 1 88  ? 41.711 -5.819  19.117 1.00 31.97 ? 94  TYR   C OH  1 
ATOM   1812 N  N   . GLN   B 1 89  ? 34.403 -9.953  18.348 1.00 16.94 ? 95  GLN   C N   1 
ATOM   1813 C  CA  . GLN   B 1 89  ? 33.185 -10.706 18.704 1.00 15.93 ? 95  GLN   C CA  1 
ATOM   1814 C  C   . GLN   B 1 89  ? 33.501 -11.441 20.006 1.00 14.98 ? 95  GLN   C C   1 
ATOM   1815 O  O   . GLN   B 1 89  ? 34.596 -12.010 20.149 1.00 15.72 ? 95  GLN   C O   1 
ATOM   1816 C  CB  . GLN   B 1 89  ? 32.805 -11.647 17.566 1.00 16.46 ? 95  GLN   C CB  1 
ATOM   1817 C  CG  . GLN   B 1 89  ? 31.530 -12.430 17.877 1.00 17.69 ? 95  GLN   C CG  1 
ATOM   1818 C  CD  . GLN   B 1 89  ? 30.837 -13.011 16.655 1.00 16.35 ? 95  GLN   C CD  1 
ATOM   1819 O  OE1 . GLN   B 1 89  ? 30.817 -12.429 15.555 1.00 16.87 ? 95  GLN   C OE1 1 
ATOM   1820 N  NE2 . GLN   B 1 89  ? 30.292 -14.178 16.852 1.00 15.14 ? 95  GLN   C NE2 1 
ATOM   1821 N  N   . SER   B 1 90  ? 32.586 -11.413 20.958 1.00 14.35 ? 96  SER   C N   1 
ATOM   1822 C  CA  . SER   B 1 90  ? 32.788 -12.045 22.244 1.00 14.76 ? 96  SER   C CA  1 
ATOM   1823 C  C   . SER   B 1 90  ? 32.181 -13.446 22.297 1.00 13.94 ? 96  SER   C C   1 
ATOM   1824 O  O   . SER   B 1 90  ? 31.333 -13.813 21.485 1.00 14.00 ? 96  SER   C O   1 
ATOM   1825 C  CB  . SER   B 1 90  ? 32.224 -11.175 23.381 1.00 17.12 ? 96  SER   C CB  1 
ATOM   1826 O  OG  . SER   B 1 90  ? 30.823 -11.093 23.235 1.00 17.56 ? 96  SER   C OG  1 
ATOM   1827 N  N   . HIS   B 1 91  ? 32.647 -14.234 23.277 1.00 14.00 ? 97  HIS   C N   1 
ATOM   1828 C  CA  . HIS   B 1 91  ? 32.147 -15.593 23.544 1.00 13.30 ? 97  HIS   C CA  1 
ATOM   1829 C  C   . HIS   B 1 91  ? 32.244 -16.463 22.280 1.00 13.85 ? 97  HIS   C C   1 
ATOM   1830 O  O   . HIS   B 1 91  ? 31.352 -17.293 22.029 1.00 14.48 ? 97  HIS   C O   1 
ATOM   1831 C  CB  . HIS   B 1 91  ? 30.692 -15.556 24.106 1.00 14.83 ? 97  HIS   C CB  1 
ATOM   1832 C  CG  . HIS   B 1 91  ? 30.560 -14.793 25.406 1.00 16.23 ? 97  HIS   C CG  1 
ATOM   1833 N  ND1 . HIS   B 1 91  ? 30.552 -15.440 26.621 1.00 18.63 ? 97  HIS   C ND1 1 
ATOM   1834 C  CD2 . HIS   B 1 91  ? 30.488 -13.443 25.627 1.00 16.94 ? 97  HIS   C CD2 1 
ATOM   1835 C  CE1 . HIS   B 1 91  ? 30.421 -14.490 27.548 1.00 18.23 ? 97  HIS   C CE1 1 
ATOM   1836 N  NE2 . HIS   B 1 91  ? 30.371 -13.269 27.002 1.00 18.41 ? 97  HIS   C NE2 1 
ATOM   1837 N  N   . LEU   B 1 92  ? 33.324 -16.310 21.534 1.00 13.17 ? 98  LEU   C N   1 
ATOM   1838 C  CA  . LEU   B 1 92  ? 33.532 -17.005 20.272 1.00 12.98 ? 98  LEU   C CA  1 
ATOM   1839 C  C   . LEU   B 1 92  ? 34.611 -18.074 20.462 1.00 12.94 ? 98  LEU   C C   1 
ATOM   1840 O  O   . LEU   B 1 92  ? 35.591 -17.861 21.169 1.00 13.21 ? 98  LEU   C O   1 
ATOM   1841 C  CB  . LEU   B 1 92  ? 34.007 -15.983 19.187 1.00 14.55 ? 98  LEU   C CB  1 
ATOM   1842 C  CG  . LEU   B 1 92  ? 34.101 -16.541 17.770 1.00 15.25 ? 98  LEU   C CG  1 
ATOM   1843 C  CD1 . LEU   B 1 92  ? 32.730 -16.877 17.213 1.00 16.80 ? 98  LEU   C CD1 1 
ATOM   1844 C  CD2 . LEU   B 1 92  ? 34.772 -15.516 16.833 1.00 16.16 ? 98  LEU   C CD2 1 
ATOM   1845 N  N   . MET   B 1 93  ? 34.417 -19.220 19.827 1.00 12.64 ? 99  MET   C N   1 
ATOM   1846 C  CA  . MET   B 1 93  ? 35.356 -20.355 19.859 1.00 11.81 ? 99  MET   C CA  1 
ATOM   1847 C  C   . MET   B 1 93  ? 35.766 -20.668 18.424 1.00 12.42 ? 99  MET   C C   1 
ATOM   1848 O  O   . MET   B 1 93  ? 34.885 -20.708 17.561 1.00 12.93 ? 99  MET   C O   1 
ATOM   1849 C  CB  . MET   B 1 93  ? 34.629 -21.578 20.439 1.00 13.63 ? 99  MET   C CB  1 
ATOM   1850 C  CG  . MET   B 1 93  ? 34.178 -21.316 21.876 1.00 14.13 ? 99  MET   C CG  1 
ATOM   1851 S  SD  . MET   B 1 93  ? 33.160 -22.627 22.523 1.00 15.84 ? 99  MET   C SD  1 
ATOM   1852 C  CE  . MET   B 1 93  ? 31.730 -22.487 21.470 1.00 15.81 ? 99  MET   C CE  1 
ATOM   1853 N  N   . LEU   B 1 94  ? 37.033 -20.943 18.158 1.00 12.68 ? 100 LEU   C N   1 
ATOM   1854 C  CA  . LEU   B 1 94  ? 37.461 -21.228 16.784 1.00 13.29 ? 100 LEU   C CA  1 
ATOM   1855 C  C   . LEU   B 1 94  ? 37.910 -22.680 16.652 1.00 12.62 ? 100 LEU   C C   1 
ATOM   1856 O  O   . LEU   B 1 94  ? 38.429 -23.277 17.596 1.00 14.25 ? 100 LEU   C O   1 
ATOM   1857 C  CB  . LEU   B 1 94  ? 38.718 -20.386 16.397 1.00 14.18 ? 100 LEU   C CB  1 
ATOM   1858 C  CG  . LEU   B 1 94  ? 38.539 -18.883 16.385 1.00 15.70 ? 100 LEU   C CG  1 
ATOM   1859 C  CD1 . LEU   B 1 94  ? 39.834 -18.211 15.945 1.00 19.08 ? 100 LEU   C CD1 1 
ATOM   1860 C  CD2 . LEU   B 1 94  ? 37.369 -18.437 15.507 1.00 17.35 ? 100 LEU   C CD2 1 
ATOM   1861 N  N   . ALA   B 1 95  ? 37.736 -23.217 15.441 1.00 13.33 ? 101 ALA   C N   1 
ATOM   1862 C  CA  . ALA   B 1 95  ? 38.295 -24.510 15.049 1.00 13.10 ? 101 ALA   C CA  1 
ATOM   1863 C  C   . ALA   B 1 95  ? 38.854 -24.382 13.632 1.00 13.45 ? 101 ALA   C C   1 
ATOM   1864 O  O   . ALA   B 1 95  ? 38.486 -23.467 12.894 1.00 13.35 ? 101 ALA   C O   1 
ATOM   1865 C  CB  . ALA   B 1 95  ? 37.210 -25.618 15.064 1.00 13.67 ? 101 ALA   C CB  1 
ATOM   1866 N  N   . VAL   B 1 96  ? 39.700 -25.329 13.222 1.00 13.16 ? 102 VAL   C N   1 
ATOM   1867 C  CA  . VAL   B 1 96  ? 40.147 -25.406 11.837 1.00 13.93 ? 102 VAL   C CA  1 
ATOM   1868 C  C   . VAL   B 1 96  ? 39.099 -26.152 11.024 1.00 13.93 ? 102 VAL   C C   1 
ATOM   1869 O  O   . VAL   B 1 96  ? 38.772 -27.325 11.322 1.00 15.71 ? 102 VAL   C O   1 
ATOM   1870 C  CB  . VAL   B 1 96  ? 41.509 -26.132 11.800 1.00 15.50 ? 102 VAL   C CB  1 
ATOM   1871 C  CG1 . VAL   B 1 96  ? 41.972 -26.291 10.345 1.00 16.81 ? 102 VAL   C CG1 1 
ATOM   1872 C  CG2 . VAL   B 1 96  ? 42.540 -25.354 12.610 1.00 17.12 ? 102 VAL   C CG2 1 
ATOM   1873 N  N   . GLY   B 1 97  ? 38.498 -25.454 10.078 1.00 15.44 ? 103 GLY   C N   1 
ATOM   1874 C  CA  . GLY   B 1 97  ? 37.428 -26.059 9.302  1.00 16.41 ? 103 GLY   C CA  1 
ATOM   1875 C  C   . GLY   B 1 97  ? 36.761 -25.097 8.378  1.00 16.01 ? 103 GLY   C C   1 
ATOM   1876 O  O   . GLY   B 1 97  ? 37.070 -23.893 8.371  1.00 18.08 ? 103 GLY   C O   1 
ATOM   1877 N  N   . HIS   B 1 98  ? 35.885 -25.641 7.543  1.00 16.19 ? 104 HIS   C N   1 
ATOM   1878 C  CA  . HIS   B 1 98  ? 35.195 -24.847 6.551  1.00 15.54 ? 104 HIS   C CA  1 
ATOM   1879 C  C   . HIS   B 1 98  ? 33.910 -24.161 7.076  1.00 14.97 ? 104 HIS   C C   1 
ATOM   1880 O  O   . HIS   B 1 98  ? 33.090 -24.802 7.772  1.00 14.56 ? 104 HIS   C O   1 
ATOM   1881 C  CB  . HIS   B 1 98  ? 34.884 -25.712 5.331  1.00 18.53 ? 104 HIS   C CB  1 
ATOM   1882 C  CG  . HIS   B 1 98  ? 34.303 -24.902 4.228  1.00 21.86 ? 104 HIS   C CG  1 
ATOM   1883 N  ND1 . HIS   B 1 98  ? 35.064 -23.954 3.534  1.00 23.35 ? 104 HIS   C ND1 1 
ATOM   1884 C  CD2 . HIS   B 1 98  ? 33.027 -24.867 3.769  1.00 24.22 ? 104 HIS   C CD2 1 
ATOM   1885 C  CE1 . HIS   B 1 98  ? 34.214 -23.378 2.685  1.00 25.90 ? 104 HIS   C CE1 1 
ATOM   1886 N  NE2 . HIS   B 1 98  ? 32.994 -23.920 2.765  1.00 26.42 ? 104 HIS   C NE2 1 
ATOM   1887 N  N   . SER   B 1 99  ? 33.728 -22.879 6.732  1.00 15.11 ? 105 SER   C N   1 
ATOM   1888 C  CA  . SER   B 1 99  ? 32.510 -22.131 7.086  1.00 15.73 ? 105 SER   C CA  1 
ATOM   1889 C  C   . SER   B 1 99  ? 32.289 -20.975 6.101  1.00 16.77 ? 105 SER   C C   1 
ATOM   1890 O  O   . SER   B 1 99  ? 33.159 -20.100 5.968  1.00 19.86 ? 105 SER   C O   1 
ATOM   1891 C  CB  . SER   B 1 99  ? 32.708 -21.561 8.478  1.00 16.74 ? 105 SER   C CB  1 
ATOM   1892 O  OG  . SER   B 1 99  ? 31.615 -20.705 8.803  1.00 17.37 ? 105 SER   C OG  1 
ATOM   1893 N  N   . GLU   B 1 100 ? 31.170 -21.030 5.397  1.00 17.14 ? 106 GLU   C N   1 
ATOM   1894 C  CA  . GLU   B 1 100 ? 30.735 -19.962 4.483  1.00 18.08 ? 106 GLU   C CA  1 
ATOM   1895 C  C   . GLU   B 1 100 ? 29.564 -19.259 5.152  1.00 16.23 ? 106 GLU   C C   1 
ATOM   1896 O  O   . GLU   B 1 100 ? 28.994 -19.757 6.132  1.00 15.38 ? 106 GLU   C O   1 
ATOM   1897 C  CB  . GLU   B 1 100 ? 30.272 -20.574 3.177  1.00 22.97 ? 106 GLU   C CB  1 
ATOM   1898 C  CG  . GLU   B 1 100 ? 31.374 -20.414 2.130  1.00 35.58 ? 106 GLU   C CG  1 
ATOM   1899 C  CD  . GLU   B 1 100 ? 31.503 -21.585 1.185  1.00 39.38 ? 106 GLU   C CD  1 
ATOM   1900 O  OE1 . GLU   B 1 100 ? 32.475 -21.623 0.405  1.00 40.49 ? 106 GLU   C OE1 1 
ATOM   1901 O  OE2 . GLU   B 1 100 ? 30.648 -22.490 1.252  1.00 41.79 ? 106 GLU   C OE2 1 
ATOM   1902 N  N   . PRO   B 1 101 ? 29.161 -18.062 4.660  1.00 17.04 ? 107 PRO   C N   1 
ATOM   1903 C  CA  . PRO   B 1 101 ? 28.032 -17.371 5.309  1.00 16.57 ? 107 PRO   C CA  1 
ATOM   1904 C  C   . PRO   B 1 101 ? 26.789 -18.234 5.511  1.00 16.58 ? 107 PRO   C C   1 
ATOM   1905 O  O   . PRO   B 1 101 ? 26.168 -18.151 6.584  1.00 16.52 ? 107 PRO   C O   1 
ATOM   1906 C  CB  . PRO   B 1 101 ? 27.764 -16.168 4.365  1.00 18.92 ? 107 PRO   C CB  1 
ATOM   1907 C  CG  . PRO   B 1 101 ? 28.984 -16.030 3.557  1.00 21.86 ? 107 PRO   C CG  1 
ATOM   1908 C  CD  . PRO   B 1 101 ? 29.744 -17.287 3.529  1.00 18.80 ? 107 PRO   C CD  1 
ATOM   1909 N  N   . GLY   B 1 102 ? 26.431 -19.041 4.518  1.00 15.93 ? 108 GLY   C N   1 
ATOM   1910 C  CA  . GLY   B 1 102 ? 25.226 -19.872 4.612  1.00 15.85 ? 108 GLY   C CA  1 
ATOM   1911 C  C   . GLY   B 1 102 ? 25.319 -20.963 5.672  1.00 15.20 ? 108 GLY   C C   1 
ATOM   1912 O  O   . GLY   B 1 102 ? 24.316 -21.608 6.008  1.00 16.44 ? 108 GLY   C O   1 
ATOM   1913 N  N   . ASP   B 1 103 ? 26.548 -21.225 6.206  1.00 13.68 ? 109 ASP   C N   1 
ATOM   1914 C  CA  . ASP   B 1 103 ? 26.715 -22.241 7.244  1.00 13.23 ? 109 ASP   C CA  1 
ATOM   1915 C  C   . ASP   B 1 103 ? 26.342 -21.764 8.628  1.00 12.68 ? 109 ASP   C C   1 
ATOM   1916 O  O   . ASP   B 1 103 ? 26.224 -22.576 9.565  1.00 13.03 ? 109 ASP   C O   1 
ATOM   1917 C  CB  . ASP   B 1 103 ? 28.190 -22.742 7.280  1.00 14.32 ? 109 ASP   C CB  1 
ATOM   1918 C  CG  . ASP   B 1 103 ? 28.493 -23.523 6.041  1.00 15.53 ? 109 ASP   C CG  1 
ATOM   1919 O  OD1 . ASP   B 1 103 ? 27.632 -24.282 5.610  1.00 16.55 ? 109 ASP   C OD1 1 
ATOM   1920 O  OD2 . ASP   B 1 103 ? 29.627 -23.398 5.512  1.00 16.42 ? 109 ASP   C OD2 1 
ATOM   1921 N  N   . CYS   B 1 104 ? 26.123 -20.447 8.814  1.00 12.48 ? 110 CYS   C N   1 
ATOM   1922 C  CA  . CYS   B 1 104 ? 25.723 -19.904 10.106 1.00 12.94 ? 110 CYS   C CA  1 
ATOM   1923 C  C   . CYS   B 1 104 ? 24.477 -20.609 10.611 1.00 12.85 ? 110 CYS   C C   1 
ATOM   1924 O  O   . CYS   B 1 104 ? 23.530 -20.817 9.836  1.00 14.03 ? 110 CYS   C O   1 
ATOM   1925 C  CB  . CYS   B 1 104 ? 25.504 -18.393 10.007 1.00 13.52 ? 110 CYS   C CB  1 
ATOM   1926 S  SG  . CYS   B 1 104 ? 27.031 -17.424 9.932  1.00 14.96 ? 110 CYS   C SG  1 
ATOM   1927 N  N   . GLY   B 1 105 ? 24.462 -20.930 11.887 1.00 11.23 ? 111 GLY   C N   1 
ATOM   1928 C  CA  . GLY   B 1 105 ? 23.334 -21.619 12.509 1.00 12.46 ? 111 GLY   C CA  1 
ATOM   1929 C  C   . GLY   B 1 105 ? 23.547 -23.114 12.671 1.00 12.15 ? 111 GLY   C C   1 
ATOM   1930 O  O   . GLY   B 1 105 ? 22.772 -23.762 13.383 1.00 13.43 ? 111 GLY   C O   1 
ATOM   1931 N  N   . GLY   B 1 106 ? 24.567 -23.682 12.016 1.00 12.58 ? 112 GLY   C N   1 
ATOM   1932 C  CA  . GLY   B 1 106 ? 24.860 -25.120 12.182 1.00 13.18 ? 112 GLY   C CA  1 
ATOM   1933 C  C   . GLY   B 1 106 ? 25.266 -25.409 13.619 1.00 12.07 ? 112 GLY   C C   1 
ATOM   1934 O  O   . GLY   B 1 106 ? 26.018 -24.624 14.222 1.00 12.25 ? 112 GLY   C O   1 
ATOM   1935 N  N   . ILE   B 1 107 ? 24.815 -26.529 14.137 1.00 11.76 ? 113 ILE   C N   1 
ATOM   1936 C  CA  . ILE   B 1 107 ? 25.104 -26.856 15.534 1.00 11.86 ? 113 ILE   C CA  1 
ATOM   1937 C  C   . ILE   B 1 107 ? 26.462 -27.512 15.725 1.00 11.90 ? 113 ILE   C C   1 
ATOM   1938 O  O   . ILE   B 1 107 ? 26.877 -28.384 14.947 1.00 11.94 ? 113 ILE   C O   1 
ATOM   1939 C  CB  . ILE   B 1 107 ? 23.961 -27.785 16.072 1.00 14.68 ? 113 ILE   C CB  1 
ATOM   1940 C  CG1 . ILE   B 1 107 ? 22.736 -26.838 16.480 1.00 18.24 ? 113 ILE   C CG1 1 
ATOM   1941 C  CG2 . ILE   B 1 107 ? 24.415 -28.639 17.299 1.00 14.82 ? 113 ILE   C CG2 1 
ATOM   1942 C  CD1 . ILE   B 1 107 ? 21.431 -27.559 16.863 1.00 21.69 ? 113 ILE   C CD1 1 
ATOM   1943 N  N   . LEU   B 1 108 ? 27.146 -27.067 16.819 1.00 11.04 ? 114 LEU   C N   1 
ATOM   1944 C  CA  . LEU   B 1 108 ? 28.317 -27.744 17.367 1.00 10.40 ? 114 LEU   C CA  1 
ATOM   1945 C  C   . LEU   B 1 108 ? 27.805 -28.496 18.618 1.00 10.82 ? 114 LEU   C C   1 
ATOM   1946 O  O   . LEU   B 1 108 ? 27.193 -27.881 19.496 1.00 11.09 ? 114 LEU   C O   1 
ATOM   1947 C  CB  . LEU   B 1 108 ? 29.367 -26.693 17.770 1.00 10.81 ? 114 LEU   C CB  1 
ATOM   1948 C  CG  . LEU   B 1 108 ? 30.573 -27.217 18.568 1.00 11.42 ? 114 LEU   C CG  1 
ATOM   1949 C  CD1 . LEU   B 1 108 ? 31.442 -28.130 17.697 1.00 12.99 ? 114 LEU   C CD1 1 
ATOM   1950 C  CD2 . LEU   B 1 108 ? 31.411 -26.047 19.061 1.00 12.53 ? 114 LEU   C CD2 1 
ATOM   1951 N  N   . ARG   B 1 109 ? 28.095 -29.798 18.707 1.00 10.88 ? 115 ARG   C N   1 
ATOM   1952 C  CA  . ARG   B 1 109 ? 27.636 -30.617 19.853 1.00 11.50 ? 115 ARG   C CA  1 
ATOM   1953 C  C   . ARG   B 1 109 ? 28.766 -31.437 20.397 1.00 11.79 ? 115 ARG   C C   1 
ATOM   1954 O  O   . ARG   B 1 109 ? 29.670 -31.870 19.668 1.00 12.66 ? 115 ARG   C O   1 
ATOM   1955 C  CB  . ARG   B 1 109 ? 26.477 -31.528 19.424 1.00 15.42 ? 115 ARG   C CB  1 
ATOM   1956 C  CG  . ARG   B 1 109 ? 26.860 -32.545 18.378 1.00 19.80 ? 115 ARG   C CG  1 
ATOM   1957 C  CD  . ARG   B 1 109 ? 25.632 -33.372 17.964 1.00 26.58 ? 115 ARG   C CD  1 
ATOM   1958 N  NE  . ARG   B 1 109 ? 24.736 -32.653 17.051 1.00 32.44 ? 115 ARG   C NE  1 
ATOM   1959 C  CZ  . ARG   B 1 109 ? 23.469 -32.321 17.324 1.00 40.79 ? 115 ARG   C CZ  1 
ATOM   1960 N  NH1 . ARG   B 1 109 ? 22.946 -32.581 18.524 1.00 42.48 ? 115 ARG   C NH1 1 
ATOM   1961 N  NH2 . ARG   B 1 109 ? 22.736 -31.672 16.423 1.00 41.53 ? 115 ARG   C NH2 1 
ATOM   1962 N  N   . CYS   B 1 110 ? 28.678 -31.688 21.701 1.00 11.95 ? 116 CYS   C N   1 
ATOM   1963 C  CA  . CYS   B 1 110 ? 29.640 -32.577 22.409 1.00 12.81 ? 116 CYS   C CA  1 
ATOM   1964 C  C   . CYS   B 1 110 ? 28.777 -33.678 23.095 1.00 14.55 ? 116 CYS   C C   1 
ATOM   1965 O  O   . CYS   B 1 110 ? 27.545 -33.767 22.887 1.00 14.58 ? 116 CYS   C O   1 
ATOM   1966 C  CB  . CYS   B 1 110 ? 30.436 -31.785 23.437 1.00 12.37 ? 116 CYS   C CB  1 
ATOM   1967 S  SG  . CYS   B 1 110 ? 29.404 -31.129 24.790 1.00 12.87 ? 116 CYS   C SG  1 
ATOM   1968 N  N   . GLN   B 1 111 ? 29.407 -34.509 23.967 1.00 15.41 ? 117 GLN   C N   1 
ATOM   1969 C  CA  . GLN   B 1 111 ? 28.630 -35.546 24.653 1.00 17.42 ? 117 GLN   C CA  1 
ATOM   1970 C  C   . GLN   B 1 111 ? 27.553 -34.983 25.582 1.00 17.20 ? 117 GLN   C C   1 
ATOM   1971 O  O   . GLN   B 1 111 ? 26.579 -35.686 25.912 1.00 18.45 ? 117 GLN   C O   1 
ATOM   1972 C  CB  . GLN   B 1 111 ? 29.555 -36.493 25.465 1.00 18.75 ? 117 GLN   C CB  1 
ATOM   1973 C  CG  . GLN   B 1 111 ? 30.188 -35.818 26.685 1.00 22.17 ? 117 GLN   C CG  1 
ATOM   1974 C  CD  . GLN   B 1 111 ? 31.190 -36.677 27.416 1.00 33.18 ? 117 GLN   C CD  1 
ATOM   1975 O  OE1 . GLN   B 1 111 ? 32.404 -36.611 27.159 1.00 36.52 ? 117 GLN   C OE1 1 
ATOM   1976 N  NE2 . GLN   B 1 111 ? 30.696 -37.460 28.355 1.00 33.52 ? 117 GLN   C NE2 1 
ATOM   1977 N  N   . HIS   B 1 112 ? 27.669 -33.700 25.992 1.00 15.05 ? 118 HIS   C N   1 
ATOM   1978 C  CA  . HIS   B 1 112 ? 26.695 -33.111 26.908 1.00 14.72 ? 118 HIS   C CA  1 
ATOM   1979 C  C   . HIS   B 1 112 ? 25.528 -32.414 26.241 1.00 15.33 ? 118 HIS   C C   1 
ATOM   1980 O  O   . HIS   B 1 112 ? 24.596 -32.014 26.930 1.00 16.08 ? 118 HIS   C O   1 
ATOM   1981 C  CB  . HIS   B 1 112 ? 27.405 -32.141 27.850 1.00 15.21 ? 118 HIS   C CB  1 
ATOM   1982 C  CG  . HIS   B 1 112 ? 28.595 -32.783 28.527 1.00 14.85 ? 118 HIS   C CG  1 
ATOM   1983 N  ND1 . HIS   B 1 112 ? 29.914 -32.458 28.184 1.00 13.89 ? 118 HIS   C ND1 1 
ATOM   1984 C  CD2 . HIS   B 1 112 ? 28.617 -33.612 29.601 1.00 16.69 ? 118 HIS   C CD2 1 
ATOM   1985 C  CE1 . HIS   B 1 112 ? 30.684 -33.196 28.963 1.00 15.65 ? 118 HIS   C CE1 1 
ATOM   1986 N  NE2 . HIS   B 1 112 ? 29.948 -33.873 29.866 1.00 16.69 ? 118 HIS   C NE2 1 
ATOM   1987 N  N   . GLY   B 1 113 ? 25.597 -32.199 24.931 1.00 14.19 ? 119 GLY   C N   1 
ATOM   1988 C  CA  . GLY   B 1 113 ? 24.535 -31.486 24.234 1.00 13.48 ? 119 GLY   C CA  1 
ATOM   1989 C  C   . GLY   B 1 113 ? 25.063 -30.435 23.261 1.00 12.22 ? 119 GLY   C C   1 
ATOM   1990 O  O   . GLY   B 1 113 ? 26.193 -30.537 22.768 1.00 13.01 ? 119 GLY   C O   1 
ATOM   1991 N  N   . VAL   B 1 114 ? 24.220 -29.398 23.015 1.00 12.13 ? 120 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 114 ? 24.571 -28.344 22.068 1.00 12.12 ? 120 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 114 ? 25.512 -27.344 22.727 1.00 12.51 ? 120 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 114 ? 25.205 -26.780 23.797 1.00 12.35 ? 120 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 114 ? 23.289 -27.639 21.599 1.00 13.29 ? 120 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 114 ? 23.665 -26.429 20.714 1.00 14.48 ? 120 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 114 ? 22.359 -28.624 20.857 1.00 14.58 ? 120 VAL   C CG2 1 
ATOM   1998 N  N   . VAL   B 1 115 ? 26.670 -27.128 22.111 1.00 11.17 ? 121 VAL   C N   1 
ATOM   1999 C  CA  . VAL   B 1 115 ? 27.697 -26.202 22.625 1.00 11.39 ? 121 VAL   C CA  1 
ATOM   2000 C  C   . VAL   B 1 115 ? 27.476 -24.787 22.108 1.00 12.38 ? 121 VAL   C C   1 
ATOM   2001 O  O   . VAL   B 1 115 ? 27.725 -23.783 22.811 1.00 12.83 ? 121 VAL   C O   1 
ATOM   2002 C  CB  . VAL   B 1 115 ? 29.099 -26.732 22.217 1.00 11.32 ? 121 VAL   C CB  1 
ATOM   2003 C  CG1 . VAL   B 1 115 ? 30.180 -25.719 22.584 1.00 12.90 ? 121 VAL   C CG1 1 
ATOM   2004 C  CG2 . VAL   B 1 115 ? 29.348 -28.099 22.827 1.00 13.22 ? 121 VAL   C CG2 1 
ATOM   2005 N  N   . GLY   B 1 116 ? 27.110 -24.689 20.838 1.00 11.66 ? 122 GLY   C N   1 
ATOM   2006 C  CA  . GLY   B 1 116 ? 26.899 -23.380 20.208 1.00 12.81 ? 122 GLY   C CA  1 
ATOM   2007 C  C   . GLY   B 1 116 ? 26.547 -23.538 18.747 1.00 11.66 ? 122 GLY   C C   1 
ATOM   2008 O  O   . GLY   B 1 116 ? 26.243 -24.658 18.303 1.00 12.15 ? 122 GLY   C O   1 
ATOM   2009 N  N   . ILE   B 1 117 ? 26.539 -22.386 18.015 1.00 11.17 ? 123 ILE   C N   1 
ATOM   2010 C  CA  . ILE   B 1 117 ? 26.184 -22.421 16.616 1.00 11.22 ? 123 ILE   C CA  1 
ATOM   2011 C  C   . ILE   B 1 117 ? 27.218 -21.684 15.787 1.00 11.61 ? 123 ILE   C C   1 
ATOM   2012 O  O   . ILE   B 1 117 ? 27.868 -20.718 16.242 1.00 11.95 ? 123 ILE   C O   1 
ATOM   2013 C  CB  . ILE   B 1 117 ? 24.775 -21.796 16.332 1.00 12.43 ? 123 ILE   C CB  1 
ATOM   2014 C  CG1 . ILE   B 1 117 ? 24.661 -20.395 16.969 1.00 13.61 ? 123 ILE   C CG1 1 
ATOM   2015 C  CG2 . ILE   B 1 117 ? 23.650 -22.754 16.777 1.00 13.63 ? 123 ILE   C CG2 1 
ATOM   2016 C  CD1 . ILE   B 1 117 ? 23.312 -19.598 16.547 1.00 14.26 ? 123 ILE   C CD1 1 
ATOM   2017 N  N   . VAL   B 1 118 ? 27.395 -22.130 14.530 1.00 10.87 ? 124 VAL   C N   1 
ATOM   2018 C  CA  . VAL   B 1 118 ? 28.318 -21.430 13.612 1.00 11.21 ? 124 VAL   C CA  1 
ATOM   2019 C  C   . VAL   B 1 118 ? 27.962 -19.957 13.486 1.00 11.50 ? 124 VAL   C C   1 
ATOM   2020 O  O   . VAL   B 1 118 ? 26.772 -19.625 13.301 1.00 11.35 ? 124 VAL   C O   1 
ATOM   2021 C  CB  . VAL   B 1 118 ? 28.320 -22.092 12.220 1.00 11.02 ? 124 VAL   C CB  1 
ATOM   2022 C  CG1 . VAL   B 1 118 ? 29.165 -21.311 11.223 1.00 12.19 ? 124 VAL   C CG1 1 
ATOM   2023 C  CG2 . VAL   B 1 118 ? 28.787 -23.567 12.261 1.00 12.25 ? 124 VAL   C CG2 1 
ATOM   2024 N  N   . SER   B 1 119 ? 28.983 -19.075 13.603 1.00 11.49 ? 125 SER   C N   1 
ATOM   2025 C  CA  . SER   B 1 119 ? 28.783 -17.625 13.487 1.00 11.70 ? 125 SER   C CA  1 
ATOM   2026 C  C   . SER   B 1 119 ? 29.788 -16.941 12.568 1.00 12.98 ? 125 SER   C C   1 
ATOM   2027 O  O   . SER   B 1 119 ? 29.470 -15.865 12.028 1.00 13.25 ? 125 SER   C O   1 
ATOM   2028 C  CB  . SER   B 1 119 ? 28.814 -17.025 14.884 1.00 13.11 ? 125 SER   C CB  1 
ATOM   2029 O  OG  . SER   B 1 119 ? 28.684 -15.597 14.836 1.00 14.31 ? 125 SER   C OG  1 
ATOM   2030 N  N   . THR   B 1 120 ? 31.031 -17.485 12.444 1.00 13.01 ? 126 THR   C N   1 
ATOM   2031 C  CA  . THR   B 1 120 ? 32.066 -16.815 11.612 1.00 13.10 ? 126 THR   C CA  1 
ATOM   2032 C  C   . THR   B 1 120 ? 32.756 -17.841 10.710 1.00 12.47 ? 126 THR   C C   1 
ATOM   2033 O  O   . THR   B 1 120 ? 32.687 -19.063 10.962 1.00 12.80 ? 126 THR   C O   1 
ATOM   2034 C  CB  . THR   B 1 120 ? 33.134 -16.085 12.495 1.00 13.04 ? 126 THR   C CB  1 
ATOM   2035 O  OG1 . THR   B 1 120 ? 33.975 -17.046 13.146 1.00 13.80 ? 126 THR   C OG1 1 
ATOM   2036 C  CG2 . THR   B 1 120 ? 32.535 -15.164 13.511 1.00 14.76 ? 126 THR   C CG2 1 
ATOM   2037 N  N   . GLY   B 1 121 ? 33.460 -17.346 9.718  1.00 14.09 ? 127 GLY   C N   1 
ATOM   2038 C  CA  . GLY   B 1 121 ? 34.219 -18.220 8.807  1.00 15.51 ? 127 GLY   C CA  1 
ATOM   2039 C  C   . GLY   B 1 121 ? 35.253 -17.456 8.016  1.00 19.11 ? 127 GLY   C C   1 
ATOM   2040 O  O   . GLY   B 1 121 ? 35.166 -16.233 7.902  1.00 21.66 ? 127 GLY   C O   1 
ATOM   2041 N  N   . GLY   B 1 122 ? 36.081 -18.151 7.297  1.00 21.30 ? 128 GLY   C N   1 
ATOM   2042 C  CA  . GLY   B 1 122 ? 37.165 -17.520 6.531  1.00 23.73 ? 128 GLY   C CA  1 
ATOM   2043 C  C   . GLY   B 1 122 ? 38.551 -17.897 7.073  1.00 24.24 ? 128 GLY   C C   1 
ATOM   2044 O  O   . GLY   B 1 122 ? 38.748 -18.318 8.209  1.00 24.36 ? 128 GLY   C O   1 
ATOM   2045 N  N   . ASN   B 1 123 ? 39.569 -17.763 6.207  1.00 23.29 ? 129 ASN   C N   1 
ATOM   2046 C  CA  . ASN   B 1 123 ? 40.968 -18.115 6.509  1.00 24.65 ? 129 ASN   C CA  1 
ATOM   2047 C  C   . ASN   B 1 123 ? 41.110 -19.584 6.962  1.00 22.43 ? 129 ASN   C C   1 
ATOM   2048 O  O   . ASN   B 1 123 ? 42.085 -19.892 7.646  1.00 24.98 ? 129 ASN   C O   1 
ATOM   2049 C  CB  . ASN   B 1 123 ? 41.562 -17.177 7.585  1.00 29.90 ? 129 ASN   C CB  1 
ATOM   2050 C  CG  . ASN   B 1 123 ? 42.556 -16.113 7.090  1.00 37.73 ? 129 ASN   C CG  1 
ATOM   2051 O  OD1 . ASN   B 1 123 ? 42.991 -16.101 5.931  1.00 39.86 ? 129 ASN   C OD1 1 
ATOM   2052 N  ND2 . ASN   B 1 123 ? 42.928 -15.171 7.954  1.00 40.62 ? 129 ASN   C ND2 1 
ATOM   2053 N  N   . GLY   B 1 124 ? 40.202 -20.472 6.548  1.00 19.91 ? 130 GLY   C N   1 
ATOM   2054 C  CA  . GLY   B 1 124 ? 40.249 -21.885 6.946  1.00 18.99 ? 130 GLY   C CA  1 
ATOM   2055 C  C   . GLY   B 1 124 ? 39.863 -22.128 8.394  1.00 17.71 ? 130 GLY   C C   1 
ATOM   2056 O  O   . GLY   B 1 124 ? 40.138 -23.202 8.924  1.00 17.39 ? 130 GLY   C O   1 
ATOM   2057 N  N   . LEU   B 1 125 ? 39.222 -21.132 9.035  1.00 16.19 ? 131 LEU   C N   1 
ATOM   2058 C  CA  . LEU   B 1 125 ? 38.762 -21.268 10.410 1.00 15.55 ? 131 LEU   C CA  1 
ATOM   2059 C  C   . LEU   B 1 125 ? 37.229 -21.159 10.433 1.00 15.90 ? 131 LEU   C C   1 
ATOM   2060 O  O   . LEU   B 1 125 ? 36.600 -20.515 9.565  1.00 18.29 ? 131 LEU   C O   1 
ATOM   2061 C  CB  . LEU   B 1 125 ? 39.386 -20.179 11.301 1.00 17.70 ? 131 LEU   C CB  1 
ATOM   2062 C  CG  . LEU   B 1 125 ? 40.936 -20.195 11.379 1.00 20.49 ? 131 LEU   C CG  1 
ATOM   2063 C  CD1 . LEU   B 1 125 ? 41.507 -18.827 11.806 1.00 24.68 ? 131 LEU   C CD1 1 
ATOM   2064 C  CD2 . LEU   B 1 125 ? 41.431 -21.303 12.228 1.00 21.22 ? 131 LEU   C CD2 1 
ATOM   2065 N  N   . VAL   B 1 126 ? 36.637 -21.814 11.404 1.00 13.15 ? 132 VAL   C N   1 
ATOM   2066 C  CA  . VAL   B 1 126 ? 35.187 -21.701 11.650 1.00 12.48 ? 132 VAL   C CA  1 
ATOM   2067 C  C   . VAL   B 1 126 ? 35.033 -21.230 13.101 1.00 11.88 ? 132 VAL   C C   1 
ATOM   2068 O  O   . VAL   B 1 126 ? 35.709 -21.747 13.999 1.00 12.40 ? 132 VAL   C O   1 
ATOM   2069 C  CB  . VAL   B 1 126 ? 34.433 -23.038 11.421 1.00 13.09 ? 132 VAL   C CB  1 
ATOM   2070 C  CG1 . VAL   B 1 126 ? 35.087 -24.239 12.094 1.00 15.27 ? 132 VAL   C CG1 1 
ATOM   2071 C  CG2 . VAL   B 1 126 ? 32.939 -22.931 11.789 1.00 13.52 ? 132 VAL   C CG2 1 
ATOM   2072 N  N   . GLY   B 1 127 ? 34.151 -20.262 13.308 1.00 11.65 ? 133 GLY   C N   1 
ATOM   2073 C  CA  . GLY   B 1 127 ? 33.915 -19.746 14.649 1.00 11.81 ? 133 GLY   C CA  1 
ATOM   2074 C  C   . GLY   B 1 127 ? 32.490 -20.057 15.096 1.00 11.80 ? 133 GLY   C C   1 
ATOM   2075 O  O   . GLY   B 1 127 ? 31.537 -19.919 14.306 1.00 12.20 ? 133 GLY   C O   1 
ATOM   2076 N  N   . PHE   B 1 128 ? 32.369 -20.435 16.356 1.00 11.77 ? 134 PHE   C N   1 
ATOM   2077 C  CA  . PHE   B 1 128 ? 31.089 -20.793 16.988 1.00 11.14 ? 134 PHE   C CA  1 
ATOM   2078 C  C   . PHE   B 1 128 ? 30.752 -19.856 18.125 1.00 11.32 ? 134 PHE   C C   1 
ATOM   2079 O  O   . PHE   B 1 128 ? 31.600 -19.592 18.986 1.00 12.12 ? 134 PHE   C O   1 
ATOM   2080 C  CB  . PHE   B 1 128 ? 31.146 -22.241 17.563 1.00 11.47 ? 134 PHE   C CB  1 
ATOM   2081 C  CG  . PHE   B 1 128 ? 31.669 -23.260 16.561 1.00 11.21 ? 134 PHE   C CG  1 
ATOM   2082 C  CD1 . PHE   B 1 128 ? 30.824 -23.844 15.641 1.00 11.83 ? 134 PHE   C CD1 1 
ATOM   2083 C  CD2 . PHE   B 1 128 ? 32.999 -23.655 16.576 1.00 12.07 ? 134 PHE   C CD2 1 
ATOM   2084 C  CE1 . PHE   B 1 128 ? 31.299 -24.808 14.754 1.00 12.64 ? 134 PHE   C CE1 1 
ATOM   2085 C  CE2 . PHE   B 1 128 ? 33.483 -24.599 15.650 1.00 12.51 ? 134 PHE   C CE2 1 
ATOM   2086 C  CZ  . PHE   B 1 128 ? 32.627 -25.176 14.767 1.00 12.90 ? 134 PHE   C CZ  1 
ATOM   2087 N  N   . ALA   B 1 129 ? 29.504 -19.356 18.141 1.00 11.43 ? 135 ALA   C N   1 
ATOM   2088 C  CA  . ALA   B 1 129 ? 29.008 -18.564 19.265 1.00 10.92 ? 135 ALA   C CA  1 
ATOM   2089 C  C   . ALA   B 1 129 ? 28.613 -19.534 20.402 1.00 12.15 ? 135 ALA   C C   1 
ATOM   2090 O  O   . ALA   B 1 129 ? 27.718 -20.374 20.231 1.00 12.00 ? 135 ALA   C O   1 
ATOM   2091 C  CB  . ALA   B 1 129 ? 27.768 -17.771 18.812 1.00 11.95 ? 135 ALA   C CB  1 
ATOM   2092 N  N   . ASP   B 1 130 ? 29.314 -19.459 21.535 1.00 12.00 ? 136 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 130 ? 29.024 -20.349 22.672 1.00 12.41 ? 136 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 130 ? 27.673 -20.006 23.284 1.00 13.05 ? 136 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 130 ? 27.276 -18.831 23.360 1.00 13.34 ? 136 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 130 ? 30.115 -20.129 23.744 1.00 13.29 ? 136 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 130 ? 29.988 -21.037 24.934 1.00 15.53 ? 136 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 130 ? 29.885 -22.256 24.741 1.00 15.52 ? 136 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 130 ? 29.919 -20.504 26.074 1.00 18.53 ? 136 ASP   C OD2 1 
ATOM   2100 N  N   . VAL   B 1 131 ? 26.975 -21.026 23.765 1.00 12.22 ? 137 VAL   C N   1 
ATOM   2101 C  CA  . VAL   B 1 131 ? 25.732 -20.842 24.537 1.00 12.38 ? 137 VAL   C CA  1 
ATOM   2102 C  C   . VAL   B 1 131 ? 25.784 -21.531 25.907 1.00 12.80 ? 137 VAL   C C   1 
ATOM   2103 O  O   . VAL   B 1 131 ? 24.803 -21.445 26.670 1.00 13.20 ? 137 VAL   C O   1 
ATOM   2104 C  CB  . VAL   B 1 131 ? 24.446 -21.293 23.783 1.00 12.94 ? 137 VAL   C CB  1 
ATOM   2105 C  CG1 . VAL   B 1 131 ? 24.273 -20.478 22.488 1.00 13.09 ? 137 VAL   C CG1 1 
ATOM   2106 C  CG2 . VAL   B 1 131 ? 24.506 -22.780 23.485 1.00 13.55 ? 137 VAL   C CG2 1 
ATOM   2107 N  N   . ARG   B 1 132 ? 26.918 -22.149 26.273 1.00 12.76 ? 138 ARG   C N   1 
ATOM   2108 C  CA  . ARG   B 1 132 ? 26.992 -22.925 27.527 1.00 12.65 ? 138 ARG   C CA  1 
ATOM   2109 C  C   . ARG   B 1 132 ? 26.941 -22.097 28.788 1.00 12.61 ? 138 ARG   C C   1 
ATOM   2110 O  O   . ARG   B 1 132 ? 26.614 -22.650 29.855 1.00 14.13 ? 138 ARG   C O   1 
ATOM   2111 C  CB  . ARG   B 1 132 ? 28.237 -23.808 27.515 1.00 12.08 ? 138 ARG   C CB  1 
ATOM   2112 C  CG  . ARG   B 1 132 ? 28.231 -24.859 26.387 1.00 12.71 ? 138 ARG   C CG  1 
ATOM   2113 C  CD  . ARG   B 1 132 ? 29.553 -25.630 26.408 1.00 12.60 ? 138 ARG   C CD  1 
ATOM   2114 N  NE  . ARG   B 1 132 ? 30.653 -24.727 26.012 1.00 12.08 ? 138 ARG   C NE  1 
ATOM   2115 C  CZ  . ARG   B 1 132 ? 31.895 -25.127 25.821 1.00 13.17 ? 138 ARG   C CZ  1 
ATOM   2116 N  NH1 . ARG   B 1 132 ? 32.273 -26.366 26.182 1.00 13.92 ? 138 ARG   C NH1 1 
ATOM   2117 N  NH2 . ARG   B 1 132 ? 32.799 -24.277 25.364 1.00 13.32 ? 138 ARG   C NH2 1 
ATOM   2118 N  N   . ASP   B 1 133 ? 27.216 -20.792 28.711 1.00 12.38 ? 139 ASP   C N   1 
ATOM   2119 C  CA  . ASP   B 1 133 ? 27.131 -19.923 29.895 1.00 13.66 ? 139 ASP   C CA  1 
ATOM   2120 C  C   . ASP   B 1 133 ? 25.689 -19.376 30.093 1.00 14.12 ? 139 ASP   C C   1 
ATOM   2121 O  O   . ASP   B 1 133 ? 25.441 -18.758 31.135 1.00 15.92 ? 139 ASP   C O   1 
ATOM   2122 C  CB  . ASP   B 1 133 ? 28.105 -18.734 29.744 1.00 15.27 ? 139 ASP   C CB  1 
ATOM   2123 C  CG  . ASP   B 1 133 ? 27.747 -17.807 28.580 1.00 16.86 ? 139 ASP   C CG  1 
ATOM   2124 O  OD1 . ASP   B 1 133 ? 27.370 -18.316 27.497 1.00 15.99 ? 139 ASP   C OD1 1 
ATOM   2125 O  OD2 . ASP   B 1 133 ? 27.776 -16.549 28.771 1.00 19.68 ? 139 ASP   C OD2 1 
ATOM   2126 N  N   . LEU   B 1 134 ? 24.756 -19.622 29.141 1.00 13.61 ? 140 LEU   C N   1 
ATOM   2127 C  CA  . LEU   B 1 134 ? 23.399 -19.053 29.214 1.00 14.00 ? 140 LEU   C CA  1 
ATOM   2128 C  C   . LEU   B 1 134 ? 22.532 -20.031 29.991 1.00 14.05 ? 140 LEU   C C   1 
ATOM   2129 O  O   . LEU   B 1 134 ? 21.685 -20.736 29.432 1.00 14.36 ? 140 LEU   C O   1 
ATOM   2130 C  CB  . LEU   B 1 134 ? 22.859 -18.826 27.799 1.00 13.72 ? 140 LEU   C CB  1 
ATOM   2131 C  CG  . LEU   B 1 134 ? 23.721 -17.859 26.928 1.00 14.25 ? 140 LEU   C CG  1 
ATOM   2132 C  CD1 . LEU   B 1 134 ? 23.149 -17.763 25.478 1.00 15.60 ? 140 LEU   C CD1 1 
ATOM   2133 C  CD2 . LEU   B 1 134 ? 23.829 -16.472 27.577 1.00 15.73 ? 140 LEU   C CD2 1 
ATOM   2134 N  N   . LEU   B 1 135 ? 22.753 -20.075 31.328 1.00 15.03 ? 141 LEU   C N   1 
ATOM   2135 C  CA  . LEU   B 1 135 ? 22.117 -21.108 32.154 1.00 16.04 ? 141 LEU   C CA  1 
ATOM   2136 C  C   . LEU   B 1 135 ? 20.607 -20.968 32.212 1.00 15.36 ? 141 LEU   C C   1 
ATOM   2137 O  O   . LEU   B 1 135 ? 19.892 -21.978 32.377 1.00 16.34 ? 141 LEU   C O   1 
ATOM   2138 C  CB  . LEU   B 1 135 ? 22.682 -21.122 33.587 1.00 16.45 ? 141 LEU   C CB  1 
ATOM   2139 C  CG  . LEU   B 1 135 ? 23.930 -21.997 33.899 1.00 21.39 ? 141 LEU   C CG  1 
ATOM   2140 C  CD1 . LEU   B 1 135 ? 24.961 -22.096 32.821 1.00 19.72 ? 141 LEU   C CD1 1 
ATOM   2141 C  CD2 . LEU   B 1 135 ? 24.652 -21.519 35.167 1.00 23.21 ? 141 LEU   C CD2 1 
ATOM   2142 N  N   . TRP   B 1 136 ? 20.114 -19.741 32.033 1.00 15.25 ? 142 TRP   C N   1 
ATOM   2143 C  CA  . TRP   B 1 136 ? 18.677 -19.469 32.066 1.00 15.79 ? 142 TRP   C CA  1 
ATOM   2144 C  C   . TRP   B 1 136 ? 17.928 -20.171 30.941 1.00 16.55 ? 142 TRP   C C   1 
ATOM   2145 O  O   . TRP   B 1 136 ? 16.694 -20.295 31.013 1.00 18.17 ? 142 TRP   C O   1 
ATOM   2146 C  CB  . TRP   B 1 136 ? 18.442 -17.952 32.068 1.00 15.98 ? 142 TRP   C CB  1 
ATOM   2147 C  CG  . TRP   B 1 136 ? 19.118 -17.225 30.949 1.00 15.94 ? 142 TRP   C CG  1 
ATOM   2148 C  CD1 . TRP   B 1 136 ? 20.304 -16.550 31.005 1.00 17.20 ? 142 TRP   C CD1 1 
ATOM   2149 C  CD2 . TRP   B 1 136 ? 18.602 -17.035 29.605 1.00 16.21 ? 142 TRP   C CD2 1 
ATOM   2150 N  NE1 . TRP   B 1 136 ? 20.589 -15.988 29.761 1.00 17.62 ? 142 TRP   C NE1 1 
ATOM   2151 C  CE2 . TRP   B 1 136 ? 19.524 -16.221 28.913 1.00 17.38 ? 142 TRP   C CE2 1 
ATOM   2152 C  CE3 . TRP   B 1 136 ? 17.410 -17.394 28.973 1.00 17.24 ? 142 TRP   C CE3 1 
ATOM   2153 C  CZ2 . TRP   B 1 136 ? 19.339 -15.862 27.574 1.00 18.15 ? 142 TRP   C CZ2 1 
ATOM   2154 C  CZ3 . TRP   B 1 136 ? 17.205 -16.993 27.668 1.00 18.22 ? 142 TRP   C CZ3 1 
ATOM   2155 C  CH2 . TRP   B 1 136 ? 18.160 -16.241 26.985 1.00 18.50 ? 142 TRP   C CH2 1 
ATOM   2156 N  N   . LEU   B 1 137 ? 18.622 -20.634 29.872 1.00 15.58 ? 143 LEU   C N   1 
ATOM   2157 C  CA  . LEU   B 1 137 ? 17.929 -21.390 28.809 1.00 16.36 ? 143 LEU   C CA  1 
ATOM   2158 C  C   . LEU   B 1 137 ? 17.304 -22.678 29.367 1.00 19.33 ? 143 LEU   C C   1 
ATOM   2159 O  O   . LEU   B 1 137 ? 16.371 -23.199 28.744 1.00 21.01 ? 143 LEU   C O   1 
ATOM   2160 C  CB  . LEU   B 1 137 ? 18.875 -21.743 27.657 1.00 15.27 ? 143 LEU   C CB  1 
ATOM   2161 C  CG  . LEU   B 1 137 ? 19.328 -20.568 26.793 1.00 15.51 ? 143 LEU   C CG  1 
ATOM   2162 C  CD1 . LEU   B 1 137 ? 20.467 -21.006 25.853 1.00 16.62 ? 143 LEU   C CD1 1 
ATOM   2163 C  CD2 . LEU   B 1 137 ? 18.170 -20.019 25.935 1.00 17.24 ? 143 LEU   C CD2 1 
ATOM   2164 N  N   . ASP   B 1 138 ? 17.832 -23.209 30.503 1.00 18.47 ? 144 ASP   C N   1 
ATOM   2165 C  CA  . ASP   B 1 138 ? 17.351 -24.464 31.092 1.00 20.35 ? 144 ASP   C CA  1 
ATOM   2166 C  C   . ASP   B 1 138 ? 16.118 -24.302 31.993 1.00 23.35 ? 144 ASP   C C   1 
ATOM   2167 O  O   . ASP   B 1 138 ? 15.655 -25.320 32.529 1.00 24.48 ? 144 ASP   C O   1 
ATOM   2168 C  CB  . ASP   B 1 138 ? 18.456 -25.131 31.940 1.00 20.21 ? 144 ASP   C CB  1 
ATOM   2169 C  CG  . ASP   B 1 138 ? 19.716 -25.506 31.181 1.00 20.77 ? 144 ASP   C CG  1 
ATOM   2170 O  OD1 . ASP   B 1 138 ? 19.670 -25.542 29.935 1.00 21.66 ? 144 ASP   C OD1 1 
ATOM   2171 O  OD2 . ASP   B 1 138 ? 20.756 -25.748 31.855 1.00 22.59 ? 144 ASP   C OD2 1 
ATOM   2172 N  N   . GLU   B 1 139 ? 15.597 -23.088 32.165 1.00 24.19 ? 145 GLU   C N   1 
ATOM   2173 C  CA  . GLU   B 1 139 ? 14.471 -22.873 33.080 1.00 28.75 ? 145 GLU   C CA  1 
ATOM   2174 C  C   . GLU   B 1 139 ? 13.443 -21.841 32.551 1.00 33.02 ? 145 GLU   C C   1 
ATOM   2175 O  O   . GLU   B 1 139 ? 13.592 -21.314 31.455 1.00 33.47 ? 145 GLU   C O   1 
ATOM   2176 C  CB  . GLU   B 1 139 ? 15.089 -22.380 34.415 1.00 34.20 ? 145 GLU   C CB  1 
ATOM   2177 C  CG  . GLU   B 1 139 ? 15.765 -21.029 34.253 1.00 42.72 ? 145 GLU   C CG  1 
ATOM   2178 C  CD  . GLU   B 1 139 ? 16.759 -20.598 35.315 1.00 51.04 ? 145 GLU   C CD  1 
ATOM   2179 O  OE1 . GLU   B 1 139 ? 17.043 -19.378 35.404 1.00 52.47 ? 145 GLU   C OE1 1 
ATOM   2180 O  OE2 . GLU   B 1 139 ? 17.261 -21.478 36.052 1.00 52.35 ? 145 GLU   C OE2 1 
ATOM   2181 N  N   . GLU   B 1 140 ? 12.433 -21.506 33.401 1.00 35.89 ? 146 GLU   C N   1 
ATOM   2182 C  CA  . GLU   B 1 140 ? 11.457 -20.412 33.279 1.00 38.33 ? 146 GLU   C CA  1 
ATOM   2183 C  C   . GLU   B 1 140 ? 10.788 -20.341 31.934 1.00 39.43 ? 146 GLU   C C   1 
ATOM   2184 O  O   . GLU   B 1 140 ? 10.664 -19.264 31.351 1.00 40.08 ? 146 GLU   C O   1 
ATOM   2185 C  CB  . GLU   B 1 140 ? 12.152 -19.086 33.649 1.00 41.81 ? 146 GLU   C CB  1 
ATOM   2186 C  CG  . GLU   B 1 140 ? 11.304 -17.811 33.693 1.00 50.32 ? 146 GLU   C CG  1 
ATOM   2187 C  CD  . GLU   B 1 140 ? 9.896  -17.911 34.247 1.00 59.27 ? 146 GLU   C CD  1 
ATOM   2188 O  OE1 . GLU   B 1 140 ? 8.940  -17.818 33.442 1.00 61.24 ? 146 GLU   C OE1 1 
ATOM   2189 O  OE2 . GLU   B 1 140 ? 9.744  -18.066 35.482 1.00 62.59 ? 146 GLU   C OE2 1 
HETATM 2190 N  N1  . A1BO8 C 2 .   ? 10.640 15.413  17.583 1.00 22.25 ? 201 A1BO8 A N1  1 
HETATM 2191 C  C4  . A1BO8 C 2 .   ? 10.084 16.060  22.823 1.00 25.25 ? 201 A1BO8 A C4  1 
HETATM 2192 C  C5  . A1BO8 C 2 .   ? 11.411 15.839  22.121 1.00 24.87 ? 201 A1BO8 A C5  1 
HETATM 2193 C  C6  . A1BO8 C 2 .   ? 11.331 16.390  20.698 1.00 23.84 ? 201 A1BO8 A C6  1 
HETATM 2194 C  C7  . A1BO8 C 2 .   ? 10.164 15.724  19.931 1.00 24.26 ? 201 A1BO8 A C7  1 
HETATM 2195 C  C8  . A1BO8 C 2 .   ? 10.090 16.210  18.496 1.00 23.66 ? 201 A1BO8 A C8  1 
HETATM 2196 C  C10 . A1BO8 C 2 .   ? 8.564  14.797  24.993 1.00 31.28 ? 201 A1BO8 A C10 1 
HETATM 2197 C  C13 . A1BO8 C 2 .   ? 6.190  13.495  25.028 1.00 34.14 ? 201 A1BO8 A C13 1 
HETATM 2198 O  O2  . A1BO8 C 2 .   ? 9.576  17.300  18.222 1.00 24.82 ? 201 A1BO8 A O2  1 
HETATM 2199 C  C9  . A1BO8 C 2 .   ? 8.860  15.945  20.699 1.00 25.34 ? 201 A1BO8 A C9  1 
HETATM 2200 N  N   . A1BO8 C 2 .   ? 8.998  15.419  22.062 1.00 26.18 ? 201 A1BO8 A N   1 
HETATM 2201 C  C3  . A1BO8 C 2 .   ? 8.219  14.413  22.502 1.00 27.22 ? 201 A1BO8 A C3  1 
HETATM 2202 O  O1  . A1BO8 C 2 .   ? 7.294  14.014  21.823 1.00 24.70 ? 201 A1BO8 A O1  1 
HETATM 2203 C  C2  . A1BO8 C 2 .   ? 8.406  13.765  23.880 1.00 30.98 ? 201 A1BO8 A C2  1 
HETATM 2204 C  C1  . A1BO8 C 2 .   ? 9.529  12.749  23.912 1.00 31.90 ? 201 A1BO8 A C1  1 
HETATM 2205 O  O   . A1BO8 C 2 .   ? 9.312  11.771  22.920 1.00 31.56 ? 201 A1BO8 A O   1 
HETATM 2206 C  C   . A1BO8 C 2 .   ? 9.839  10.533  23.275 1.00 28.48 ? 201 A1BO8 A C   1 
HETATM 2207 O  O3  . A1BO8 C 2 .   ? 7.215  12.995  24.147 1.00 33.88 ? 201 A1BO8 A O3  1 
HETATM 2208 C  C12 . A1BO8 C 2 .   ? 6.038  15.015  25.058 1.00 33.80 ? 201 A1BO8 A C12 1 
HETATM 2209 C  C11 . A1BO8 C 2 .   ? 7.381  15.757  25.054 1.00 32.23 ? 201 A1BO8 A C11 1 
HETATM 2210 ZN ZN  . ZN    D 3 .   ? 11.061 -3.901  5.783  1.00 19.57 2 202 ZN    A ZN  1 
HETATM 2211 S  S   . DMS   E 4 .   ? 19.499 -1.775  24.371 1.00 81.56 ? 203 DMS   A S   1 
HETATM 2212 O  O   . DMS   E 4 .   ? 18.447 -1.953  23.311 1.00 81.47 ? 203 DMS   A O   1 
HETATM 2213 C  C1  . DMS   E 4 .   ? 19.480 -3.256  25.414 1.00 81.52 ? 203 DMS   A C1  1 
HETATM 2214 C  C2  . DMS   E 4 .   ? 21.114 -2.125  23.617 1.00 81.55 ? 203 DMS   A C2  1 
HETATM 2215 ZN ZN  . ZN    F 3 .   ? 30.628 -31.175 26.741 1.00 13.50 2 201 ZN    C ZN  1 
HETATM 2216 S  S   . DMS   G 4 .   ? 20.894 -32.398 9.516  1.00 78.03 ? 202 DMS   C S   1 
HETATM 2217 O  O   . DMS   G 4 .   ? 22.061 -32.630 8.609  1.00 78.23 ? 202 DMS   C O   1 
HETATM 2218 C  C1  . DMS   G 4 .   ? 21.493 -32.427 11.212 1.00 77.95 ? 202 DMS   C C1  1 
HETATM 2219 C  C2  . DMS   G 4 .   ? 20.532 -30.622 9.496  1.00 77.96 ? 202 DMS   C C2  1 
HETATM 2220 O  O   . HOH   H 5 .   ? 35.355 -3.828  7.881  1.00 24.26 ? 301 HOH   A O   1 
HETATM 2221 O  O   . HOH   H 5 .   ? 11.179 8.825   4.297  1.00 22.58 ? 302 HOH   A O   1 
HETATM 2222 O  O   . HOH   H 5 .   ? 1.954  23.186  21.150 1.00 33.68 ? 303 HOH   A O   1 
HETATM 2223 O  O   . HOH   H 5 .   ? 23.054 13.184  23.707 1.00 41.41 ? 304 HOH   A O   1 
HETATM 2224 O  O   . HOH   H 5 .   ? 14.056 17.415  4.311  1.00 38.73 ? 305 HOH   A O   1 
HETATM 2225 O  O   . HOH   H 5 .   ? 8.699  19.206  19.731 1.00 21.44 ? 306 HOH   A O   1 
HETATM 2226 O  O   . HOH   H 5 .   ? 8.333  25.166  23.530 1.00 31.29 ? 307 HOH   A O   1 
HETATM 2227 O  O   . HOH   H 5 .   ? 27.827 8.000   1.801  1.00 32.73 ? 308 HOH   A O   1 
HETATM 2228 O  O   . HOH   H 5 .   ? 37.497 15.076  13.881 1.00 54.03 ? 309 HOH   A O   1 
HETATM 2229 O  O   . HOH   H 5 .   ? 35.530 7.866   9.653  1.00 45.58 ? 310 HOH   A O   1 
HETATM 2230 O  O   . HOH   H 5 .   ? 3.032  9.476   8.979  1.00 27.55 ? 311 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 5 .   ? 13.903 2.864   1.242  1.00 23.73 ? 312 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 5 .   ? 5.346  18.642  24.178 1.00 34.69 ? 313 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 5 .   ? 7.381  20.387  17.571 1.00 23.17 ? 314 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 5 .   ? 6.510  3.308   3.236  1.00 37.56 ? 315 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 5 .   ? 30.450 10.523  15.632 1.00 32.58 ? 316 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 13.154 11.434  24.660 1.00 26.40 ? 317 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 10.057 10.447  31.323 1.00 23.46 ? 318 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 21.902 2.420   -0.862 1.00 33.98 ? 319 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? 4.637  -3.560  28.797 1.00 28.09 ? 320 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 28.137 3.241   4.917  1.00 33.43 ? 321 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 0.451  -0.980  19.372 1.00 23.51 ? 322 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? 19.322 10.039  19.676 1.00 14.14 ? 323 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? 33.816 14.199  9.763  1.00 31.93 ? 324 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? 0.644  -1.144  9.097  1.00 35.96 ? 325 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 20.244 19.721  5.531  1.00 49.75 ? 326 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? 17.524 0.999   28.179 1.00 27.06 ? 327 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 23.446 21.744  7.253  1.00 24.95 ? 328 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 12.217 21.984  12.926 1.00 41.87 ? 329 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 2.674  -2.960  20.751 1.00 23.89 ? 330 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 33.563 11.218  15.589 1.00 38.34 ? 331 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? 24.908 5.088   21.459 1.00 29.27 ? 332 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 1.661  5.501   27.065 1.00 29.53 ? 333 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? 7.080  26.403  14.275 1.00 39.50 ? 334 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? -0.064 1.244   15.861 1.00 13.59 ? 335 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 23.452 3.753   -2.273 1.00 47.28 ? 336 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? 23.296 11.794  21.915 1.00 33.23 ? 337 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 22.650 0.867   17.418 1.00 16.66 ? 338 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? 36.795 2.535   10.128 1.00 40.85 ? 339 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 16.555 3.860   23.641 1.00 19.51 ? 340 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 20.964 -4.138  14.159 1.00 17.03 ? 341 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? 5.685  5.459   32.628 1.00 20.11 ? 342 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 33.922 -2.338  13.547 1.00 35.87 ? 343 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? 31.566 19.961  11.768 1.00 22.75 ? 344 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 10.749 5.605   3.409  1.00 24.08 ? 345 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 14.112 13.776  24.037 1.00 22.11 ? 346 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 8.289  -2.777  31.990 1.00 24.59 ? 347 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? 26.833 -1.224  8.817  1.00 25.44 ? 348 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 29.895 11.614  18.472 1.00 27.94 ? 349 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 3.144  7.189   24.210 1.00 22.56 ? 350 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 11.276 12.681  11.187 1.00 16.94 ? 351 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? 13.690 4.016   23.504 1.00 13.91 ? 352 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 28.918 3.378   12.685 1.00 17.37 ? 353 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? 29.353 11.983  21.308 1.00 32.89 ? 354 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 20.695 -0.988  3.008  1.00 29.80 ? 355 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 5.937  17.461  21.669 1.00 28.57 ? 356 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 20.195 17.973  24.070 1.00 38.59 ? 357 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 3.905  -8.249  9.896  1.00 49.36 ? 358 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 16.974 -3.469  27.871 1.00 33.92 ? 359 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 36.425 18.048  14.472 1.00 31.80 ? 360 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 28.884 15.866  4.394  1.00 31.19 ? 361 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 18.345 21.884  9.538  1.00 20.86 ? 362 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 14.976 21.842  8.541  1.00 30.30 ? 363 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? 30.498 2.972   14.831 1.00 23.83 ? 364 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 14.363 -10.933 8.691  1.00 48.37 ? 365 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 1.165  12.336  21.033 1.00 33.52 ? 366 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 20.805 -2.558  16.878 1.00 15.84 ? 367 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 17.346 -5.235  12.188 1.00 36.85 ? 368 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 14.980 11.405  0.045  1.00 38.02 ? 369 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 11.605 17.952  4.912  1.00 38.51 ? 370 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 13.231 11.376  9.250  1.00 14.62 ? 371 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? 6.596  -6.955  23.733 1.00 26.45 ? 372 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 11.576 -6.983  24.756 1.00 28.12 ? 373 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 30.076 -1.382  8.661  1.00 31.64 ? 374 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 4.890  15.338  21.069 1.00 34.41 ? 375 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 16.289 2.224   30.190 1.00 27.42 ? 376 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 17.533 19.980  17.018 1.00 18.24 ? 377 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 22.544 19.488  19.816 1.00 33.29 ? 378 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? 8.452  6.570   33.874 1.00 18.69 ? 379 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 35.839 15.223  11.136 1.00 42.64 ? 380 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? 22.862 -0.597  5.358  1.00 22.21 ? 381 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 9.752  4.066   33.496 1.00 13.94 ? 382 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 14.463 -2.460  17.932 1.00 19.39 ? 383 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 30.356 4.601   5.810  1.00 24.22 ? 384 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? 32.783 16.586  9.284  1.00 34.29 ? 385 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 35.178 10.853  12.563 1.00 46.79 ? 386 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 31.147 -2.454  15.579 1.00 49.31 ? 387 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? 17.176 5.883   26.723 1.00 26.27 ? 388 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 16.453 21.219  19.207 1.00 25.25 ? 389 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 19.160 16.975  26.278 1.00 43.42 ? 390 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 3.348  0.387   28.895 1.00 36.13 ? 391 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 21.910 4.978   24.700 1.00 41.74 ? 392 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 27.132 -1.347  15.892 1.00 27.26 ? 393 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 9.647  18.921  26.353 1.00 48.63 ? 394 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 25.204 17.797  4.560  1.00 34.77 ? 395 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 4.193  0.274   23.960 1.00 18.30 ? 396 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 0.192  5.842   6.087  1.00 25.64 ? 397 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 19.477 2.905   19.388 1.00 19.38 ? 398 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 1.076  11.726  27.521 1.00 31.80 ? 399 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 34.017 18.656  10.817 1.00 28.13 ? 400 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 2.616  16.178  19.414 1.00 29.84 ? 401 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 20.266 -4.361  11.092 1.00 33.79 ? 402 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 32.015 8.769   7.669  1.00 24.97 ? 403 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 3.965  -4.000  5.961  1.00 28.53 ? 404 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 24.253 -3.370  16.169 1.00 33.61 ? 405 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 17.353 10.650  26.094 1.00 23.98 ? 406 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 27.925 17.609  24.216 1.00 25.06 ? 407 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 15.132 15.130  3.401  1.00 31.90 ? 408 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 5.029  8.172   2.339  1.00 34.63 ? 409 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 32.192 2.157   5.968  1.00 36.96 ? 410 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 36.257 -0.341  12.668 1.00 32.84 ? 411 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 3.772  11.299  19.207 1.00 30.08 ? 412 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 23.291 -6.613  11.988 1.00 32.52 ? 413 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 18.075 17.756  4.253  1.00 36.44 ? 414 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 30.754 15.757  22.939 1.00 27.73 ? 415 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 15.319 14.408  26.383 1.00 32.03 ? 416 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 9.250  3.436   2.991  1.00 30.74 ? 417 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 17.460 0.650   20.215 1.00 19.33 ? 418 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 8.578  -6.491  9.701  1.00 30.92 ? 419 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 25.426 19.734  21.738 1.00 31.13 ? 420 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 16.691 -3.933  2.766  1.00 27.18 ? 421 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 6.105  -3.504  31.501 1.00 31.67 ? 422 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 4.135  9.352   27.533 1.00 36.76 ? 423 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 19.450 21.435  6.832  1.00 38.57 ? 424 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 2.204  14.547  17.058 1.00 35.48 ? 425 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 3.344  -0.404  21.426 1.00 22.35 ? 426 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 7.241  13.765  4.775  1.00 23.23 ? 427 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 5.253  26.853  19.700 1.00 28.77 ? 428 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 1.127  -4.958  17.467 1.00 36.87 ? 429 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 0.456  -1.350  16.653 1.00 18.36 ? 430 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 19.678 -0.473  33.423 1.00 36.09 ? 431 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 14.312 24.361  17.787 1.00 34.87 ? 432 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 6.262  23.901  10.392 1.00 41.40 ? 433 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 24.957 10.722  22.954 1.00 34.68 ? 434 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 1.751  8.033   26.736 1.00 44.84 ? 435 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? 17.691 24.401  10.373 1.00 35.84 ? 436 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 33.883 5.199   16.703 1.00 31.66 ? 437 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 22.726 3.440   20.842 1.00 20.79 ? 438 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 23.210 19.130  6.300  1.00 20.66 ? 439 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 19.706 13.306  2.180  1.00 33.56 ? 440 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 20.978 9.934   21.952 1.00 18.74 ? 441 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 15.879 21.423  7.200  1.00 25.91 ? 442 HOH   A O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? 34.134 7.826   16.677 1.00 33.34 ? 443 HOH   A O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? 23.382 8.323   21.741 1.00 25.42 ? 444 HOH   A O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? 17.151 -2.498  19.679 1.00 19.35 ? 445 HOH   A O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? 36.532 16.180  17.029 1.00 44.56 ? 446 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 19.644 9.339   -0.927 1.00 27.40 ? 447 HOH   A O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? -0.690 15.636  11.678 1.00 31.84 ? 448 HOH   A O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? 0.893  15.872  21.837 1.00 46.05 ? 449 HOH   A O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? 19.327 -3.193  33.712 1.00 45.32 ? 450 HOH   A O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? 1.178  3.906   26.250 1.00 29.48 ? 451 HOH   A O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? 2.037  -5.483  14.569 1.00 42.80 ? 452 HOH   A O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? 31.855 7.055   5.470  1.00 33.87 ? 453 HOH   A O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? 12.510 -12.515 7.532  1.00 45.92 ? 454 HOH   A O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 18.534 2.166   22.729 1.00 40.63 ? 455 HOH   A O   1 
HETATM 2375 O  O   . HOH   H 5 .   ? 7.190  21.620  27.007 1.00 43.79 ? 456 HOH   A O   1 
HETATM 2376 O  O   . HOH   H 5 .   ? 30.781 13.063  23.132 1.00 42.47 ? 457 HOH   A O   1 
HETATM 2377 O  O   . HOH   H 5 .   ? 17.023 -4.902  34.265 1.00 30.97 ? 458 HOH   A O   1 
HETATM 2378 O  O   . HOH   H 5 .   ? 2.680  -0.089  26.320 1.00 31.69 ? 459 HOH   A O   1 
HETATM 2379 O  O   . HOH   H 5 .   ? 11.612 24.303  14.370 1.00 36.73 ? 460 HOH   A O   1 
HETATM 2380 O  O   . HOH   H 5 .   ? 29.702 0.714   16.512 1.00 34.48 ? 461 HOH   A O   1 
HETATM 2381 O  O   . HOH   H 5 .   ? 18.642 3.113   26.203 1.00 46.83 ? 462 HOH   A O   1 
HETATM 2382 O  O   . HOH   H 5 .   ? 0.143  0.161   23.266 1.00 30.61 ? 463 HOH   A O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? 21.638 14.930  1.146  1.00 49.28 ? 464 HOH   A O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? 23.789 0.955   19.867 1.00 31.06 ? 465 HOH   A O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? 5.043  12.003  27.838 1.00 42.77 ? 466 HOH   A O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? 30.268 7.064   17.793 1.00 34.55 ? 467 HOH   A O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? 21.469 2.964   23.240 1.00 39.86 ? 468 HOH   A O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? 21.161 11.451  24.510 1.00 34.83 ? 469 HOH   A O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? 12.526 -4.991  33.090 1.00 26.27 ? 470 HOH   A O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 31.250 4.586   17.040 1.00 26.57 ? 471 HOH   A O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 8.657  12.612  31.766 1.00 34.22 ? 472 HOH   A O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 37.756 -4.573  6.675  1.00 30.98 ? 473 HOH   A O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? 21.322 -1.064  18.991 1.00 31.01 ? 474 HOH   A O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 2.371  -5.165  22.469 1.00 33.16 ? 475 HOH   A O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 10.367 16.019  30.471 1.00 46.87 ? 476 HOH   A O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 28.969 1.490   18.869 1.00 51.92 ? 477 HOH   A O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 9.736  25.928  13.520 1.00 52.59 ? 478 HOH   A O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 4.008  -6.807  23.502 1.00 51.07 ? 479 HOH   A O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 1.696  -4.764  25.032 1.00 45.47 ? 480 HOH   A O   1 
HETATM 2400 O  O   . HOH   I 5 .   ? 31.089 -32.725 0.793  1.00 38.21 ? 301 HOH   C O   1 
HETATM 2401 O  O   . HOH   I 5 .   ? 38.333 -26.098 28.366 1.00 33.05 ? 302 HOH   C O   1 
HETATM 2402 O  O   . HOH   I 5 .   ? 17.608 -33.207 24.138 1.00 37.96 ? 303 HOH   C O   1 
HETATM 2403 O  O   . HOH   I 5 .   ? 39.063 -18.751 21.562 1.00 26.37 ? 304 HOH   C O   1 
HETATM 2404 O  O   . HOH   I 5 .   ? 38.353 -7.374  7.078  1.00 22.81 ? 305 HOH   C O   1 
HETATM 2405 O  O   . HOH   I 5 .   ? 16.411 -17.093 11.161 1.00 44.31 ? 306 HOH   C O   1 
HETATM 2406 O  O   . HOH   I 5 .   ? 10.162 -20.114 28.946 1.00 36.14 ? 307 HOH   C O   1 
HETATM 2407 O  O   . HOH   I 5 .   ? 26.973 -7.612  2.368  1.00 53.99 ? 308 HOH   C O   1 
HETATM 2408 O  O   . HOH   I 5 .   ? 3.472  -12.907 20.424 1.00 45.92 ? 309 HOH   C O   1 
HETATM 2409 O  O   . HOH   I 5 .   ? 19.749 -4.141  20.172 1.00 21.98 ? 310 HOH   C O   1 
HETATM 2410 O  O   . HOH   I 5 .   ? 17.865 -6.029  24.064 1.00 25.28 ? 311 HOH   C O   1 
HETATM 2411 O  O   . HOH   I 5 .   ? 24.629 -5.881  15.199 1.00 28.59 ? 312 HOH   C O   1 
HETATM 2412 O  O   . HOH   I 5 .   ? 20.756 -18.764 12.835 1.00 14.77 ? 313 HOH   C O   1 
HETATM 2413 O  O   . HOH   I 5 .   ? 37.341 -32.007 10.980 1.00 26.09 ? 314 HOH   C O   1 
HETATM 2414 O  O   . HOH   I 5 .   ? 24.452 -9.553  26.895 1.00 40.37 ? 315 HOH   C O   1 
HETATM 2415 O  O   . HOH   I 5 .   ? 17.897 -27.544 16.518 1.00 19.28 ? 316 HOH   C O   1 
HETATM 2416 O  O   . HOH   I 5 .   ? 36.222 -26.208 34.194 1.00 35.15 ? 317 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 5 .   ? 30.795 -18.104 26.893 1.00 19.51 ? 318 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 5 .   ? 22.949 -5.951  21.169 1.00 20.48 ? 319 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 5 .   ? 36.273 -2.518  11.006 1.00 28.55 ? 320 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 5 .   ? 10.242 -17.519 18.318 1.00 27.31 ? 321 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 5 .   ? 18.848 -32.423 19.890 1.00 41.23 ? 322 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 5 .   ? 28.203 -5.066  18.484 1.00 37.02 ? 323 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 5 .   ? 26.575 -5.515  10.002 1.00 22.64 ? 324 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 5 .   ? 26.485 -15.080 30.624 1.00 34.99 ? 325 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 5 .   ? 22.033 -28.640 4.782  1.00 26.82 ? 326 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 5 .   ? 14.788 -23.893 12.314 1.00 31.47 ? 327 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 5 .   ? 22.660 -7.420  25.335 1.00 42.90 ? 328 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 5 .   ? 19.954 -21.670 35.898 1.00 38.72 ? 329 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 5 .   ? 16.378 -16.065 8.818  1.00 42.78 ? 330 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 5 .   ? 35.066 -32.882 3.364  1.00 35.23 ? 331 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 5 .   ? 18.629 -8.824  13.726 1.00 27.35 ? 332 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 5 .   ? 24.833 -15.749 7.384  1.00 19.29 ? 333 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 5 .   ? 14.809 -18.579 31.961 1.00 36.68 ? 334 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 5 .   ? 23.944 -8.156  9.472  1.00 24.64 ? 335 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 5 .   ? 7.204  -30.293 21.876 1.00 34.40 ? 336 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 5 .   ? 40.529 -27.290 15.205 1.00 13.05 ? 337 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 5 .   ? 16.878 -9.384  27.616 1.00 34.91 ? 338 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 5 .   ? 25.747 -37.787 24.365 1.00 35.54 ? 339 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 5 .   ? 37.254 -18.738 28.204 1.00 29.50 ? 340 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 5 .   ? 9.941  -8.891  23.983 1.00 28.64 ? 341 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 5 .   ? 31.044 -21.494 28.374 1.00 17.24 ? 342 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 5 .   ? 36.148 -17.643 11.572 1.00 28.24 ? 343 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 5 .   ? 19.252 -27.665 28.224 1.00 18.57 ? 344 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 5 .   ? 32.532 -23.700 29.164 1.00 17.25 ? 345 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 5 .   ? 26.034 -25.286 8.773  1.00 14.12 ? 346 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 5 .   ? 39.414 -16.919 26.999 1.00 47.60 ? 347 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 5 .   ? 34.221 -33.696 24.126 1.00 35.74 ? 348 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 5 .   ? 13.358 -11.255 28.557 1.00 36.02 ? 349 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 5 .   ? 14.634 -28.853 25.555 1.00 34.60 ? 350 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 35.946 -28.597 2.869  1.00 41.22 ? 351 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 9.207  -8.027  21.287 1.00 26.45 ? 352 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 17.594 -24.023 8.725  1.00 38.50 ? 353 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 40.153 -29.685 11.882 1.00 23.35 ? 354 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 29.929 -15.256 19.549 1.00 16.35 ? 355 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 35.157 -13.170 8.717  1.00 20.37 ? 356 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 36.340 -21.328 6.904  1.00 24.25 ? 357 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 6.642  -9.300  22.652 1.00 37.81 ? 358 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 37.256 -10.504 4.820  1.00 36.90 ? 359 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 13.829 -24.197 29.351 1.00 31.52 ? 360 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 11.934 -24.292 21.681 1.00 18.17 ? 361 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 41.449 -25.036 7.256  1.00 33.84 ? 362 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 27.072 -35.636 20.849 1.00 25.73 ? 363 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 5.820  -12.794 23.181 1.00 45.77 ? 364 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 20.792 -25.701 13.861 1.00 21.61 ? 365 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? 13.126 -29.492 19.112 1.00 30.15 ? 366 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 10.653 -16.933 12.465 1.00 34.10 ? 367 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 23.566 -33.535 29.068 1.00 29.29 ? 368 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 23.793 -3.461  19.149 1.00 37.74 ? 369 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 31.193 -6.059  5.715  1.00 42.33 ? 370 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 34.764 -35.011 18.111 1.00 30.06 ? 371 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 23.202 -25.369 8.906  1.00 21.50 ? 372 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 5.034  -12.071 14.524 1.00 53.84 ? 373 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 32.035 -10.454 13.764 1.00 19.95 ? 374 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 29.789 -13.104 12.985 1.00 16.26 ? 375 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 5.907  -16.886 22.311 1.00 48.66 ? 376 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 22.929 -8.531  14.038 1.00 16.23 ? 377 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 32.129 -34.638 24.838 1.00 28.90 ? 378 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 10.490 -16.967 15.036 1.00 31.52 ? 379 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 30.311 -18.174 8.426  1.00 24.58 ? 380 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 32.993 -9.830  11.134 1.00 15.63 ? 381 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 31.292 -12.165 10.673 1.00 16.25 ? 382 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 31.061 -23.797 -1.277 1.00 22.80 ? 383 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 14.713 -18.454 10.468 1.00 35.81 ? 384 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 31.562 -13.341 4.133  1.00 32.50 ? 385 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 36.656 -16.117 12.624 1.00 34.34 ? 386 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 11.023 -21.820 13.662 1.00 44.46 ? 387 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 43.216 -25.394 23.782 1.00 22.12 ? 388 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 37.744 -31.448 25.796 1.00 29.62 ? 389 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 22.287 -23.742 6.085  1.00 33.93 ? 390 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 28.889 -36.296 7.873  1.00 22.28 ? 391 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 22.910 -28.131 12.658 1.00 21.64 ? 392 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 11.472 -22.522 28.663 1.00 26.12 ? 393 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 8.814  -13.341 10.804 1.00 23.06 ? 394 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 28.147 -16.368 22.103 1.00 14.10 ? 395 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 37.806 -23.521 4.371  1.00 40.39 ? 396 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 5 .   ? 38.571 -13.556 10.895 1.00 35.72 ? 397 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 5 .   ? 11.017 -6.500  13.180 1.00 24.79 ? 398 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 5 .   ? 39.406 -33.561 13.950 1.00 49.05 ? 399 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 5 .   ? 4.264  -10.475 19.603 1.00 32.35 ? 400 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 5 .   ? 10.043 -24.830 19.791 1.00 21.59 ? 401 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 5 .   ? 36.941 -29.272 10.142 1.00 22.28 ? 402 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 5 .   ? 22.672 -13.946 29.931 1.00 33.04 ? 403 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 5 .   ? 26.630 -6.062  22.066 1.00 28.60 ? 404 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 5 .   ? 39.042 -13.135 25.642 1.00 29.54 ? 405 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 5 .   ? 37.848 -20.459 4.809  1.00 36.69 ? 406 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 5 .   ? 35.633 -24.631 24.717 1.00 18.20 ? 407 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 5 .   ? 26.787 -12.020 27.585 1.00 27.60 ? 408 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 5 .   ? 27.087 -19.186 1.666  1.00 24.16 ? 409 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 5 .   ? 26.006 -30.994 30.914 1.00 17.32 ? 410 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 5 .   ? 10.681 -11.976 9.063  1.00 30.48 ? 411 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 5 .   ? 3.870  -8.295  14.734 1.00 26.14 ? 412 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 5 .   ? 22.912 -33.377 5.439  1.00 36.13 ? 413 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 5 .   ? 26.403 -31.289 14.883 1.00 20.55 ? 414 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 5 .   ? 34.399 -13.433 25.506 1.00 20.21 ? 415 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 5 .   ? 24.501 -13.810 5.487  1.00 38.29 ? 416 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 5 .   ? 29.950 -10.451 27.781 1.00 43.77 ? 417 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 5 .   ? 4.736  -28.061 23.113 1.00 34.69 ? 418 HOH   C O   1 
HETATM 2518 O  O   . HOH   I 5 .   ? 10.421 -30.945 25.211 1.00 31.43 ? 419 HOH   C O   1 
HETATM 2519 O  O   . HOH   I 5 .   ? 21.731 -18.913 5.886  1.00 26.27 ? 420 HOH   C O   1 
HETATM 2520 O  O   . HOH   I 5 .   ? 33.014 -30.328 31.702 1.00 20.61 ? 421 HOH   C O   1 
HETATM 2521 O  O   . HOH   I 5 .   ? 30.264 -16.004 30.310 1.00 34.13 ? 422 HOH   C O   1 
HETATM 2522 O  O   . HOH   I 5 .   ? 9.754  -18.452 26.631 1.00 30.42 ? 423 HOH   C O   1 
HETATM 2523 O  O   . HOH   I 5 .   ? 4.103  -12.773 17.212 1.00 40.60 ? 424 HOH   C O   1 
HETATM 2524 O  O   . HOH   I 5 .   ? 38.813 -14.606 13.439 1.00 37.92 ? 425 HOH   C O   1 
HETATM 2525 O  O   . HOH   I 5 .   ? 35.755 -28.623 7.794  1.00 19.72 ? 426 HOH   C O   1 
HETATM 2526 O  O   . HOH   I 5 .   ? 36.327 -32.518 25.136 1.00 39.85 ? 427 HOH   C O   1 
HETATM 2527 O  O   . HOH   I 5 .   ? 34.659 -23.317 -0.851 1.00 39.66 ? 428 HOH   C O   1 
HETATM 2528 O  O   . HOH   I 5 .   ? 41.785 -12.281 18.035 1.00 26.56 ? 429 HOH   C O   1 
HETATM 2529 O  O   . HOH   I 5 .   ? 20.462 -32.137 22.289 1.00 33.12 ? 430 HOH   C O   1 
HETATM 2530 O  O   . HOH   I 5 .   ? 34.993 -4.117  17.686 1.00 31.57 ? 431 HOH   C O   1 
HETATM 2531 O  O   . HOH   I 5 .   ? 17.213 -25.316 12.730 1.00 24.28 ? 432 HOH   C O   1 
HETATM 2532 O  O   . HOH   I 5 .   ? 33.751 -20.636 -2.170 1.00 39.97 ? 433 HOH   C O   1 
HETATM 2533 O  O   . HOH   I 5 .   ? 18.858 -19.160 10.800 1.00 19.86 ? 434 HOH   C O   1 
HETATM 2534 O  O   . HOH   I 5 .   ? 38.734 -16.947 3.394  1.00 43.42 ? 435 HOH   C O   1 
HETATM 2535 O  O   . HOH   I 5 .   ? 40.004 -29.948 14.607 1.00 18.24 ? 436 HOH   C O   1 
HETATM 2536 O  O   . HOH   I 5 .   ? 32.796 -14.384 9.409  1.00 16.91 ? 437 HOH   C O   1 
HETATM 2537 O  O   . HOH   I 5 .   ? 16.440 -20.576 11.585 1.00 25.71 ? 438 HOH   C O   1 
HETATM 2538 O  O   . HOH   I 5 .   ? 15.190 -30.110 18.029 1.00 41.94 ? 439 HOH   C O   1 
HETATM 2539 O  O   . HOH   I 5 .   ? 18.626 -8.317  25.540 1.00 20.87 ? 440 HOH   C O   1 
HETATM 2540 O  O   . HOH   I 5 .   ? 17.030 -31.547 28.537 1.00 47.82 ? 441 HOH   C O   1 
HETATM 2541 O  O   . HOH   I 5 .   ? 6.518  -22.922 18.303 1.00 31.57 ? 442 HOH   C O   1 
HETATM 2542 O  O   . HOH   I 5 .   ? 6.528  -20.078 18.198 1.00 32.99 ? 443 HOH   C O   1 
HETATM 2543 O  O   . HOH   I 5 .   ? 8.596  -12.951 24.632 1.00 55.18 ? 444 HOH   C O   1 
HETATM 2544 O  O   . HOH   I 5 .   ? 30.965 -37.551 8.985  1.00 45.25 ? 445 HOH   C O   1 
HETATM 2545 O  O   . HOH   I 5 .   ? 20.474 -23.830 34.799 1.00 33.71 ? 446 HOH   C O   1 
HETATM 2546 O  O   . HOH   I 5 .   ? 24.394 -16.390 3.173  1.00 40.93 ? 447 HOH   C O   1 
HETATM 2547 O  O   . HOH   I 5 .   ? 34.030 -15.582 27.086 1.00 32.44 ? 448 HOH   C O   1 
HETATM 2548 O  O   . HOH   I 5 .   ? 23.397 -30.979 13.433 1.00 34.11 ? 449 HOH   C O   1 
HETATM 2549 O  O   . HOH   I 5 .   ? 23.560 -17.518 33.323 1.00 32.36 ? 450 HOH   C O   1 
HETATM 2550 O  O   . HOH   I 5 .   ? 35.199 -13.630 6.123  1.00 36.82 ? 451 HOH   C O   1 
HETATM 2551 O  O   . HOH   I 5 .   ? 18.564 -11.803 7.684  1.00 43.36 ? 452 HOH   C O   1 
HETATM 2552 O  O   . HOH   I 5 .   ? 21.738 -21.180 4.212  1.00 51.11 ? 453 HOH   C O   1 
HETATM 2553 O  O   . HOH   I 5 .   ? 9.752  -24.759 29.330 1.00 41.92 ? 454 HOH   C O   1 
HETATM 2554 O  O   . HOH   I 5 .   ? 37.277 -14.437 9.578  1.00 35.86 ? 455 HOH   C O   1 
HETATM 2555 O  O   . HOH   I 5 .   ? 31.555 -15.737 7.173  1.00 28.48 ? 456 HOH   C O   1 
HETATM 2556 O  O   . HOH   I 5 .   ? 33.858 -36.210 8.808  1.00 44.57 ? 457 HOH   C O   1 
HETATM 2557 O  O   . HOH   I 5 .   ? 21.652 -17.619 34.037 1.00 34.18 ? 458 HOH   C O   1 
HETATM 2558 O  O   . HOH   I 5 .   ? 41.873 -31.590 15.687 1.00 32.45 ? 459 HOH   C O   1 
HETATM 2559 O  O   . HOH   I 5 .   ? 20.428 -19.302 35.879 1.00 33.06 ? 460 HOH   C O   1 
HETATM 2560 O  O   . HOH   I 5 .   ? 23.861 -15.744 31.481 1.00 41.05 ? 461 HOH   C O   1 
HETATM 2561 O  O   . HOH   I 5 .   ? 34.207 -31.874 29.589 1.00 25.98 ? 462 HOH   C O   1 
HETATM 2562 O  O   . HOH   I 5 .   ? 36.680 -24.468 27.176 1.00 30.80 ? 463 HOH   C O   1 
HETATM 2563 O  O   . HOH   I 5 .   ? 26.163 -35.461 7.482  1.00 25.81 ? 464 HOH   C O   1 
HETATM 2564 O  O   . HOH   I 5 .   ? 8.896  -19.216 16.892 1.00 38.62 ? 465 HOH   C O   1 
HETATM 2565 O  O   . HOH   I 5 .   ? 11.645 -15.175 29.608 1.00 53.10 ? 466 HOH   C O   1 
HETATM 2566 O  O   . HOH   I 5 .   ? 12.056 -18.690 10.615 1.00 48.79 ? 467 HOH   C O   1 
HETATM 2567 O  O   . HOH   I 5 .   ? 22.983 -16.622 5.445  1.00 38.88 ? 468 HOH   C O   1 
HETATM 2568 O  O   . HOH   I 5 .   ? 21.541 -26.933 10.405 1.00 33.49 ? 469 HOH   C O   1 
HETATM 2569 O  O   . HOH   I 5 .   ? 38.789 -8.591  4.820  1.00 46.62 ? 470 HOH   C O   1 
HETATM 2570 O  O   . HOH   I 5 .   ? 40.642 -15.292 11.044 1.00 46.99 ? 471 HOH   C O   1 
HETATM 2571 O  O   . HOH   I 5 .   ? 16.417 -27.554 14.141 1.00 32.48 ? 472 HOH   C O   1 
HETATM 2572 O  O   . HOH   I 5 .   ? 6.224  -12.533 10.912 1.00 40.15 ? 473 HOH   C O   1 
HETATM 2573 O  O   . HOH   I 5 .   ? 18.599 -26.044 10.286 1.00 40.65 ? 474 HOH   C O   1 
HETATM 2574 O  O   . HOH   I 5 .   ? 32.600 -19.400 29.071 1.00 30.08 ? 475 HOH   C O   1 
HETATM 2575 O  O   . HOH   I 5 .   ? 41.462 -15.347 13.784 1.00 40.13 ? 476 HOH   C O   1 
HETATM 2576 O  O   . HOH   I 5 .   ? 10.093 -21.359 16.342 1.00 32.20 ? 477 HOH   C O   1 
HETATM 2577 O  O   . HOH   I 5 .   ? 18.538 -16.468 38.238 1.00 31.18 ? 478 HOH   C O   1 
HETATM 2578 O  O   . HOH   I 5 .   ? 18.140 -17.980 8.369  1.00 36.31 ? 479 HOH   C O   1 
HETATM 2579 O  O   . HOH   I 5 .   ? 16.932 -28.910 28.906 1.00 37.50 ? 480 HOH   C O   1 
HETATM 2580 O  O   . HOH   I 5 .   ? 8.981  -23.517 17.664 1.00 32.15 ? 481 HOH   C O   1 
HETATM 2581 O  O   . HOH   I 5 .   ? 35.268 -20.150 29.415 1.00 41.59 ? 482 HOH   C O   1 
HETATM 2582 O  O   . HOH   I 5 .   ? 40.150 -31.502 25.153 1.00 45.08 ? 483 HOH   C O   1 
HETATM 2583 O  O   . HOH   I 5 .   ? 22.794 -11.936 5.887  1.00 38.04 ? 484 HOH   C O   1 
HETATM 2584 O  O   . HOH   I 5 .   ? 37.218 -23.142 -1.677 1.00 34.20 ? 485 HOH   C O   1 
HETATM 2585 O  O   . HOH   I 5 .   ? 35.242 -23.009 29.062 1.00 26.65 ? 486 HOH   C O   1 
HETATM 2586 O  O   . HOH   I 5 .   ? 34.344 -10.915 26.735 1.00 45.09 ? 487 HOH   C O   1 
HETATM 2587 O  O   . HOH   I 5 .   ? 39.186 -2.571  10.871 1.00 38.70 ? 488 HOH   C O   1 
HETATM 2588 O  O   . HOH   I 5 .   ? 3.103  -8.699  21.875 1.00 45.28 ? 489 HOH   C O   1 
HETATM 2589 O  O   . HOH   I 5 .   ? 10.028 -15.977 27.563 1.00 41.49 ? 490 HOH   C O   1 
HETATM 2590 O  O   . HOH   I 5 .   ? 37.054 -35.246 9.340  1.00 49.77 ? 491 HOH   C O   1 
HETATM 2591 O  O   . HOH   I 5 .   ? 3.191  -9.440  17.039 1.00 36.33 ? 492 HOH   C O   1 
HETATM 2592 O  O   . HOH   I 5 .   ? 26.000 -8.472  29.667 1.00 68.09 ? 493 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   ? 0.2187 0.2198 0.2121 -0.0002 -0.0055 -0.0099 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2121 0.2131 0.2108 0.0011  -0.0077 -0.0077 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2064 0.2083 0.2104 0.0049  -0.0094 -0.0029 7   SER   A C   
4    O O   . SER   A 1   ? 0.2125 0.2155 0.2152 0.0056  -0.0097 -0.0009 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2471 0.2525 0.2432 -0.0042 -0.0112 -0.0068 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2718 0.2826 0.2663 -0.0059 -0.0149 -0.0020 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1846 0.1857 0.1943 0.0068  -0.0099 -0.0017 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1755 0.1767 0.1905 0.0095  -0.0102 0.0016  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1676 0.1665 0.1871 0.0115  -0.0084 0.0008  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1882 0.1849 0.2067 0.0118  -0.0067 -0.0016 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1516 0.1508 0.1765 0.0127  -0.0082 0.0029  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1543 0.1519 0.1829 0.0136  -0.0062 0.0019  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1555 0.1523 0.1875 0.0144  -0.0038 0.0027  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1661 0.1630 0.1998 0.0148  -0.0038 0.0046  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1719 0.1713 0.2049 0.0127  -0.0078 0.0025  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1443 0.1400 0.1772 0.0141  -0.0013 0.0012  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1358 0.1303 0.1720 0.0135  0.0023  0.0006  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1466 0.1415 0.1899 0.0137  0.0032  0.0007  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1487 0.1445 0.1919 0.0131  0.0022  0.0002  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1405 0.1350 0.1721 0.0113  0.0047  -0.0012 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1659 0.1617 0.1916 0.0113  0.0034  -0.0007 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1558 0.1488 0.1893 0.0091  0.0095  -0.0032 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1768 0.1752 0.1989 0.0089  0.0044  -0.0007 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1446 0.1387 0.1954 0.0145  0.0056  0.0016  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1548 0.1500 0.2145 0.0149  0.0073  0.0019  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1628 0.1549 0.2254 0.0134  0.0140  -0.0013 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1673 0.1568 0.2353 0.0142  0.0175  -0.0011 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1645 0.1626 0.2335 0.0173  0.0049  0.0067  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1574 0.1595 0.2224 0.0169  -0.0014 0.0092  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1673 0.1727 0.2335 0.0158  -0.0037 0.0091  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1792 0.1819 0.2387 0.0167  -0.0044 0.0110  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1700 0.1784 0.2308 0.0140  -0.0084 0.0100  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1883 0.1946 0.2427 0.0150  -0.0092 0.0120  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1811 0.1899 0.2360 0.0134  -0.0109 0.0112  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2169 0.2287 0.2659 0.0104  -0.0147 0.0112  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1653 0.1575 0.2242 0.0106  0.0162  -0.0045 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1672 0.1572 0.2265 0.0072  0.0229  -0.0086 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1804 0.1720 0.2453 0.0062  0.0253  -0.0100 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1700 0.1641 0.2318 0.0058  0.0216  -0.0089 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1878 0.1783 0.2353 0.0029  0.0234  -0.0108 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2003 0.1941 0.2416 0.0025  0.0184  -0.0088 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2064 0.1956 0.2527 -0.0025 0.0305  -0.0157 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1960 0.1857 0.2704 0.0061  0.0318  -0.0121 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1917 0.1833 0.2726 0.0052  0.0346  -0.0135 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1776 0.1737 0.2640 0.0087  0.0283  -0.0089 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1737 0.1711 0.2652 0.0124  0.0243  -0.0045 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1725 0.1710 0.2556 0.0064  0.0268  -0.0096 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1682 0.1707 0.2542 0.0082  0.0210  -0.0061 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1602 0.1621 0.2344 0.0072  0.0154  -0.0052 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1689 0.1726 0.2421 0.0063  0.0125  -0.0044 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1810 0.1866 0.2745 0.0069  0.0234  -0.0069 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2296 0.2373 0.3391 0.0096  0.0276  -0.0058 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2534 0.2660 0.3725 0.0126  0.0238  -0.0010 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2042 0.2087 0.3172 0.0083  0.0356  -0.0099 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1484 0.1479 0.2152 0.0076  0.0143  -0.0052 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1504 0.1492 0.2081 0.0073  0.0100  -0.0042 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1415 0.1400 0.1977 0.0099  0.0064  -0.0022 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1572 0.1551 0.2157 0.0112  0.0076  -0.0017 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1626 0.1602 0.2121 0.0045  0.0120  -0.0055 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1671 0.1658 0.2156 0.0005  0.0153  -0.0071 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1916 0.1911 0.2406 -0.0004 0.0137  -0.0061 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1975 0.1964 0.2441 -0.0033 0.0204  -0.0100 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2029 0.2038 0.2507 -0.0046 0.0166  -0.0072 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2051 0.2057 0.2494 -0.0082 0.0235  -0.0117 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2199 0.2217 0.2648 -0.0086 0.0214  -0.0099 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2618 0.2658 0.3041 -0.0140 0.0244  -0.0110 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1389 0.1373 0.1906 0.0100  0.0026  -0.0014 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1413 0.1394 0.1892 0.0113  -0.0004 -0.0003 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1492 0.1450 0.1901 0.0110  -0.0005 -0.0010 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1562 0.1508 0.1959 0.0101  -0.0007 -0.0014 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1480 0.1487 0.1979 0.0108  -0.0040 0.0009  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1560 0.1565 0.2000 0.0105  -0.0067 0.0009  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1680 0.1726 0.2132 0.0081  -0.0102 0.0020  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1824 0.1849 0.2203 0.0058  -0.0109 -0.0006 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2067 0.2101 0.2395 0.0045  -0.0124 -0.0008 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2189 0.2250 0.2528 0.0059  -0.0137 0.0022  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2109 0.2118 0.2375 0.0019  -0.0117 -0.0043 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1400 0.1353 0.1772 0.0117  -0.0001 -0.0009 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1408 0.1352 0.1732 0.0119  0.0000  -0.0005 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1507 0.1444 0.1807 0.0131  -0.0017 -0.0007 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1616 0.1561 0.1905 0.0136  -0.0024 -0.0005 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1508 0.1467 0.1807 0.0108  0.0018  -0.0001 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1513 0.1485 0.1786 0.0109  0.0014  0.0019  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1594 0.1562 0.1908 0.0082  0.0045  -0.0011 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1408 0.1325 0.1699 0.0134  -0.0018 -0.0013 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1425 0.1330 0.1689 0.0136  -0.0022 -0.0027 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1676 0.1582 0.1941 0.0136  -0.0022 -0.0027 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1522 0.1406 0.1788 0.0150  -0.0001 -0.0025 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1660 0.1541 0.1954 0.0156  0.0008  -0.0003 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1334 0.1231 0.1594 0.0115  -0.0033 -0.0047 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2134 0.2033 0.2400 0.0114  -0.0034 -0.0045 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1452 0.1388 0.1722 0.0104  -0.0059 -0.0035 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2189 0.2080 0.2413 0.0098  -0.0034 -0.0070 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.1030 0.0901 0.1316 0.0105  -0.0022 -0.0054 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2435 0.2370 0.2728 0.0105  -0.0056 -0.0031 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1520 0.1395 0.1766 0.0154  0.0009  -0.0042 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1544 0.1394 0.1817 0.0172  0.0038  -0.0040 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1605 0.1404 0.1902 0.0162  0.0056  -0.0057 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1677 0.1461 0.1946 0.0133  0.0051  -0.0091 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1586 0.1428 0.1833 0.0170  0.0056  -0.0069 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1652 0.1540 0.1875 0.0177  0.0043  -0.0054 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1753 0.1660 0.1933 0.0159  0.0020  -0.0060 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1720 0.1632 0.1977 0.0200  0.0055  -0.0025 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1556 0.1335 0.1908 0.0182  0.0075  -0.0028 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1636 0.1357 0.2017 0.0171  0.0097  -0.0042 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.1886 0.1554 0.2250 0.0153  0.0132  -0.0100 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.1963 0.1598 0.2307 0.0119  0.0137  -0.0135 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1711 0.1420 0.2165 0.0199  0.0115  0.0011  20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1797 0.1441 0.2289 0.0188  0.0139  0.0006  20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.2028 0.1662 0.2608 0.0220  0.0157  0.0074  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.2074 0.1647 0.2696 0.0209  0.0178  0.0084  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2448 0.1930 0.3117 0.0212  0.0232  0.0054  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2466 0.1909 0.3132 0.0216  0.0272  -0.0002 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2562 0.1987 0.3275 0.0203  0.0251  0.0073  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1838 0.1503 0.2204 0.0168  0.0158  -0.0114 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2068 0.1679 0.2413 0.0141  0.0205  -0.0179 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2139 0.1774 0.2390 0.0085  0.0179  -0.0226 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2385 0.1982 0.2600 0.0041  0.0215  -0.0286 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2185 0.1787 0.2572 0.0171  0.0251  -0.0184 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.1937 0.1603 0.2271 0.0170  0.0225  -0.0183 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2012 0.1741 0.2366 0.0203  0.0190  -0.0124 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2166 0.1839 0.2432 0.0135  0.0237  -0.0233 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2011 0.1778 0.2311 0.0191  0.0181  -0.0141 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2168 0.1906 0.2414 0.0151  0.0205  -0.0202 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2034 0.1736 0.2249 0.0080  0.0120  -0.0196 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2063 0.1808 0.2209 0.0031  0.0085  -0.0216 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2153 0.1921 0.2308 0.0012  0.0048  -0.0198 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2196 0.2017 0.2315 -0.0025 0.0011  -0.0196 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.2019 0.1823 0.2134 0.0041  0.0053  -0.0190 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2122 0.1915 0.2222 0.0051  0.0088  -0.0210 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2191 0.2043 0.2259 0.0056  0.0052  -0.0180 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2371 0.2133 0.2420 -0.0003 0.0130  -0.0277 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.2053 0.1790 0.2262 0.0035  0.0058  -0.0180 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.1981 0.1742 0.2204 0.0016  0.0029  -0.0166 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2209 0.1970 0.2396 -0.0046 0.0028  -0.0207 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2324 0.2027 0.2487 -0.0074 0.0071  -0.0255 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.1967 0.1694 0.2246 0.0044  0.0045  -0.0142 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2043 0.1871 0.2231 -0.0070 -0.0017 -0.0187 24  THR   A N   
139  C CA  . THR   A 18  ? 0.2027 0.1884 0.2180 -0.0140 -0.0030 -0.0214 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2150 0.1975 0.2336 -0.0156 -0.0016 -0.0224 24  THR   A C   
141  O O   . THR   A 18  ? 0.1997 0.1793 0.2238 -0.0112 -0.0005 -0.0199 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2252 0.2217 0.2410 -0.0159 -0.0090 -0.0171 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2324 0.2317 0.2559 -0.0121 -0.0109 -0.0127 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2400 0.2399 0.2527 -0.0146 -0.0108 -0.0151 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2204 0.2047 0.2356 -0.0230 -0.0020 -0.0258 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2282 0.2106 0.2466 -0.0252 -0.0011 -0.0264 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2113 0.2005 0.2367 -0.0218 -0.0051 -0.0207 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2113 0.1968 0.2412 -0.0196 -0.0032 -0.0197 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2473 0.2330 0.2603 -0.0350 -0.0017 -0.0307 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3542 0.3408 0.3709 -0.0380 -0.0021 -0.0305 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.4158 0.3917 0.4341 -0.0380 0.0033  -0.0336 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.4017 0.3989 0.4226 -0.0401 -0.0071 -0.0265 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.4174 0.3974 0.4386 -0.0412 0.0014  -0.0325 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.4326 0.4258 0.4560 -0.0424 -0.0048 -0.0282 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.2018 0.2008 0.2291 -0.0212 -0.0099 -0.0165 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.2023 0.2071 0.2380 -0.0176 -0.0122 -0.0116 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1824 0.1815 0.2211 -0.0110 -0.0093 -0.0103 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.1935 0.1929 0.2374 -0.0095 -0.0085 -0.0088 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2138 0.2290 0.2529 -0.0173 -0.0169 -0.0067 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.3137 0.3347 0.3635 -0.0143 -0.0180 -0.0022 26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3537 0.3792 0.4078 -0.0174 -0.0189 -0.0017 26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3436 0.3637 0.3979 -0.0084 -0.0170 0.0004  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1728 0.1673 0.2080 -0.0077 -0.0077 -0.0109 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1716 0.1620 0.2088 -0.0029 -0.0054 -0.0094 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1619 0.1461 0.2000 -0.0033 -0.0023 -0.0103 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1713 0.1559 0.2127 -0.0018 -0.0016 -0.0081 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1751 0.1622 0.2084 -0.0002 -0.0041 -0.0098 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1919 0.1841 0.2246 0.0012  -0.0066 -0.0079 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1883 0.1851 0.2256 0.0025  -0.0082 -0.0051 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.1931 0.1845 0.2212 0.0007  -0.0066 -0.0093 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1704 0.1488 0.2058 -0.0059 0.0000  -0.0136 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1726 0.1443 0.2101 -0.0063 0.0033  -0.0138 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1808 0.1554 0.2210 -0.0095 0.0022  -0.0133 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1925 0.1641 0.2354 -0.0087 0.0039  -0.0113 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1825 0.1463 0.2173 -0.0088 0.0071  -0.0182 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1841 0.1432 0.2191 -0.0047 0.0099  -0.0179 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2061 0.1651 0.2374 -0.0050 0.0108  -0.0209 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.1956 0.1504 0.2356 -0.0001 0.0124  -0.0139 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2012 0.1559 0.2355 -0.0004 0.0140  -0.0194 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.1979 0.1505 0.2380 0.0027  0.0147  -0.0145 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2132 0.1669 0.2577 0.0014  0.0127  -0.0092 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2183 0.1680 0.2643 0.0075  0.0171  -0.0100 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2242 0.1756 0.2734 0.0055  0.0145  -0.0043 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2308 0.1804 0.2814 0.0087  0.0166  -0.0045 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1777 0.1592 0.2179 -0.0130 -0.0008 -0.0144 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1833 0.1690 0.2272 -0.0161 -0.0017 -0.0137 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1889 0.1802 0.2384 -0.0128 -0.0027 -0.0101 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.1970 0.1913 0.2506 -0.0147 -0.0025 -0.0094 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.2016 0.1942 0.2444 -0.0217 -0.0048 -0.0154 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1827 0.1752 0.2324 -0.0084 -0.0030 -0.0082 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1815 0.1782 0.2360 -0.0059 -0.0026 -0.0058 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1804 0.1728 0.2318 -0.0029 -0.0005 -0.0048 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1771 0.1719 0.2294 -0.0006 -0.0002 -0.0038 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1975 0.2014 0.2562 -0.0045 -0.0050 -0.0042 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.2125 0.2232 0.2759 -0.0079 -0.0075 -0.0037 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2352 0.2499 0.3052 -0.0087 -0.0066 -0.0028 30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2124 0.2252 0.2721 -0.0110 -0.0105 -0.0043 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1748 0.1612 0.2232 -0.0032 0.0010  -0.0047 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1612 0.1450 0.2074 -0.0008 0.0022  -0.0025 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1783 0.1650 0.2251 -0.0013 0.0034  -0.0003 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1961 0.1835 0.2445 -0.0040 0.0045  0.0000  31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1739 0.1507 0.2193 -0.0009 0.0038  -0.0019 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1871 0.1621 0.2321 0.0019  0.0047  0.0017  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1855 0.1615 0.2284 0.0047  0.0039  0.0008  31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.2207 0.1885 0.2681 0.0022  0.0071  0.0035  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1617 0.1503 0.2065 0.0003  0.0035  0.0009  32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1713 0.1629 0.2147 -0.0017 0.0051  0.0026  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1831 0.1736 0.2239 -0.0015 0.0048  0.0070  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1977 0.1896 0.2377 -0.0043 0.0054  0.0102  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1594 0.1544 0.2024 -0.0013 0.0061  0.0008  32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1882 0.1863 0.2277 -0.0048 0.0084  0.0017  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1817 0.1785 0.2302 -0.0011 0.0068  -0.0020 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1773 0.1664 0.2174 0.0017  0.0037  0.0079  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1785 0.1682 0.2184 0.0025  0.0034  0.0131  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1813 0.1678 0.2226 0.0065  0.0031  0.0127  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1719 0.1582 0.2117 0.0078  0.0027  0.0087  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1893 0.1858 0.2253 0.0000  0.0032  0.0149  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1991 0.1992 0.2350 0.0005  0.0020  0.0209  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.2309 0.2343 0.2680 -0.0016 0.0011  0.0278  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1893 0.1916 0.2245 0.0028  0.0012  0.0213  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2426 0.2510 0.2807 -0.0005 -0.0004 0.0330  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.2113 0.2190 0.2479 0.0021  -0.0002 0.0287  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1911 0.1919 0.2249 0.0051  0.0013  0.0169  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2223 0.2344 0.2593 0.0036  -0.0012 0.0312  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.2101 0.2144 0.2432 0.0064  0.0006  0.0188  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2236 0.2334 0.2585 0.0058  -0.0006 0.0257  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1898 0.1740 0.2348 0.0085  0.0037  0.0170  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1839 0.1652 0.2310 0.0122  0.0046  0.0163  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1990 0.1825 0.2514 0.0142  0.0049  0.0237  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.2013 0.1855 0.2569 0.0130  0.0047  0.0295  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.2024 0.1759 0.2512 0.0128  0.0068  0.0116  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2097 0.1775 0.2627 0.0118  0.0088  0.0133  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2369 0.2006 0.2976 0.0147  0.0115  0.0186  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2459 0.2067 0.3108 0.0139  0.0125  0.0228  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.2270 0.1900 0.2906 0.0180  0.0130  0.0188  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1783 0.1634 0.2323 0.0171  0.0052  0.0244  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1717 0.1603 0.2327 0.0196  0.0053  0.0323  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1849 0.1702 0.2503 0.0238  0.0081  0.0300  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1803 0.1690 0.2416 0.0241  0.0073  0.0271  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1962 0.1959 0.2537 0.0168  0.0020  0.0373  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2306 0.2372 0.2955 0.0183  0.0010  0.0472  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2701 0.2739 0.3434 0.0231  0.0032  0.0489  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2803 0.2958 0.3430 0.0142  -0.0019 0.0533  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1933 0.1714 0.2672 0.0268  0.0120  0.0311  36  SER   A N   
245  C CA  A SER   A 30  ? 0.2009 0.1747 0.2801 0.0304  0.0163  0.0282  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.2105 0.1844 0.2891 0.0303  0.0162  0.0279  36  SER   A CA  
247  C C   . SER   A 30  ? 0.2034 0.1859 0.2877 0.0332  0.0152  0.0343  36  SER   A C   
248  O O   . SER   A 30  ? 0.2042 0.1870 0.2871 0.0345  0.0168  0.0301  36  SER   A O   
249  C CB  A SER   A 30  ? 0.2076 0.1715 0.2967 0.0326  0.0219  0.0288  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2508 0.2140 0.3382 0.0323  0.0221  0.0269  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.2089 0.1687 0.3052 0.0362  0.0273  0.0266  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.3098 0.2745 0.4077 0.0344  0.0222  0.0370  36  SER   A OG  
253  N N   . SER   A 31  ? 0.1930 0.1835 0.2824 0.0333  0.0123  0.0444  37  SER   A N   
254  C CA  . SER   A 31  ? 0.1898 0.1907 0.2846 0.0352  0.0107  0.0513  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1831 0.1908 0.2672 0.0323  0.0076  0.0470  37  SER   A C   
256  O O   . SER   A 31  ? 0.2048 0.2186 0.2923 0.0340  0.0076  0.0494  37  SER   A O   
257  C CB  . SER   A 31  ? 0.2165 0.2269 0.3183 0.0344  0.0074  0.0640  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2968 0.3149 0.3875 0.0282  0.0023  0.0651  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1676 0.1735 0.2397 0.0281  0.0056  0.0407  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1771 0.1877 0.2394 0.0253  0.0034  0.0362  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1691 0.1722 0.2261 0.0260  0.0054  0.0268  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1589 0.1645 0.2087 0.0240  0.0040  0.0232  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1849 0.1992 0.2389 0.0199  0.0004  0.0361  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1945 0.2190 0.2505 0.0168  -0.0023 0.0454  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.2010 0.2287 0.2480 0.0104  -0.0041 0.0440  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1707 0.2007 0.2092 0.0072  -0.0042 0.0382  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1874 0.2234 0.2185 0.0006  -0.0050 0.0379  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.2127 0.2543 0.2428 -0.0040 -0.0063 0.0430  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1812 0.2178 0.2058 -0.0020 -0.0041 0.0324  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1619 0.1558 0.2214 0.0277  0.0086  0.0227  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1531 0.1412 0.2065 0.0267  0.0098  0.0143  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1602 0.1493 0.2051 0.0231  0.0066  0.0112  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1677 0.1563 0.2070 0.0220  0.0060  0.0067  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1632 0.1523 0.2157 0.0280  0.0116  0.0114  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1735 0.1574 0.2194 0.0261  0.0128  0.0036  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.1930 0.1703 0.2389 0.0249  0.0149  -0.0001 39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.1832 0.1700 0.2239 0.0251  0.0118  0.0014  39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1568 0.1470 0.2014 0.0212  0.0050  0.0136  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1446 0.1358 0.1833 0.0182  0.0030  0.0107  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1587 0.1454 0.1980 0.0168  0.0034  0.0090  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1606 0.1452 0.2042 0.0171  0.0044  0.0120  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1451 0.1429 0.1815 0.0158  0.0014  0.0141  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1727 0.1758 0.2062 0.0155  0.0007  0.0146  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1928 0.2020 0.2230 0.0114  -0.0002 0.0169  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1777 0.1782 0.2075 0.0158  0.0008  0.0094  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1520 0.1381 0.1880 0.0151  0.0024  0.0049  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1481 0.1321 0.1849 0.0131  0.0023  0.0036  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1512 0.1387 0.1862 0.0115  0.0009  0.0019  41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1520 0.1411 0.1852 0.0121  0.0001  0.0006  41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1596 0.1385 0.1967 0.0126  0.0033  -0.0003 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1618 0.1390 0.1997 0.0099  0.0031  -0.0019 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1792 0.1498 0.2183 0.0089  0.0057  -0.0044 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1686 0.1496 0.2048 0.0081  0.0007  -0.0042 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1511 0.1396 0.1874 0.0095  0.0012  0.0024  42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1389 0.1302 0.1759 0.0081  0.0013  0.0009  42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1423 0.1330 0.1824 0.0067  0.0011  -0.0005 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1540 0.1430 0.1949 0.0053  0.0017  0.0004  42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1449 0.1392 0.1805 0.0060  0.0029  0.0021  42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1678 0.1638 0.2058 0.0047  0.0047  -0.0003 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1671 0.1634 0.1994 0.0065  0.0027  0.0037  42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1431 0.1356 0.1856 0.0069  0.0000  -0.0018 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1418 0.1360 0.1884 0.0051  -0.0006 -0.0026 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1553 0.1535 0.2076 0.0053  0.0006  -0.0024 43  SER   A C   
304  O O   . SER   A 37  ? 0.1575 0.1563 0.2103 0.0066  0.0020  -0.0022 43  SER   A O   
305  C CB  . SER   A 37  ? 0.1642 0.1588 0.2101 0.0045  -0.0032 -0.0034 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1687 0.1659 0.2144 0.0058  -0.0048 -0.0026 43  SER   A OG  
307  N N   . SER   A 38  ? 0.1648 0.1655 0.2223 0.0037  0.0008  -0.0025 44  SER   A N   
308  C CA  . SER   A 38  ? 0.1719 0.1764 0.2373 0.0041  0.0030  -0.0023 44  SER   A CA  
309  C C   . SER   A 38  ? 0.1825 0.1917 0.2546 0.0057  0.0004  -0.0001 44  SER   A C   
310  O O   . SER   A 38  ? 0.2077 0.2187 0.2781 0.0045  -0.0035 0.0009  44  SER   A O   
311  C CB  . SER   A 38  ? 0.2043 0.2104 0.2734 0.0016  0.0051  -0.0032 44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2292 0.2369 0.2993 0.0000  0.0021  -0.0027 44  SER   A OG  
313  N N   . THR   A 39  ? 0.1866 0.1977 0.2666 0.0077  0.0029  0.0010  45  THR   A N   
314  C CA  . THR   A 39  ? 0.2033 0.2196 0.2916 0.0096  0.0002  0.0050  45  THR   A CA  
315  C C   . THR   A 39  ? 0.2244 0.2455 0.3268 0.0105  0.0031  0.0065  45  THR   A C   
316  O O   . THR   A 39  ? 0.2141 0.2328 0.3192 0.0102  0.0088  0.0035  45  THR   A O   
317  C CB  . THR   A 39  ? 0.2084 0.2223 0.2960 0.0122  0.0008  0.0062  45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.2160 0.2264 0.3073 0.0132  0.0070  0.0039  45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.2161 0.2258 0.2911 0.0116  -0.0013 0.0046  45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2327 0.2613 0.3443 0.0113  -0.0006 0.0117  46  THR   A N   
321  C CA  . THR   A 40  ? 0.2430 0.2773 0.3710 0.0130  0.0022  0.0145  46  THR   A CA  
322  C C   . THR   A 40  ? 0.2432 0.2748 0.3807 0.0171  0.0071  0.0160  46  THR   A C   
323  O O   . THR   A 40  ? 0.2669 0.2970 0.4140 0.0183  0.0141  0.0138  46  THR   A O   
324  C CB  . THR   A 40  ? 0.2814 0.3266 0.4172 0.0118  -0.0039 0.0205  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3378 0.3859 0.4718 0.0124  -0.0090 0.0254  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.2914 0.3381 0.4180 0.0069  -0.0073 0.0179  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2463 0.2767 0.3810 0.0188  0.0042  0.0191  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2565 0.2832 0.4000 0.0224  0.0092  0.0205  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2399 0.2564 0.3719 0.0215  0.0144  0.0137  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2350 0.2487 0.3517 0.0190  0.0115  0.0105  47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2914 0.3221 0.4381 0.0243  0.0037  0.0280  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.2310 0.2425 0.3710 0.0231  0.0222  0.0116  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2417 0.2448 0.3713 0.0210  0.0275  0.0054  48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2331 0.2336 0.3570 0.0222  0.0243  0.0079  48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2402 0.2428 0.3740 0.0255  0.0225  0.0142  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.2639 0.2622 0.4038 0.0210  0.0381  0.0012  48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3369 0.3368 0.4793 0.0183  0.0427  -0.0033 48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.4128 0.4075 0.5647 0.0174  0.0545  -0.0086 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.3973 0.3923 0.5678 0.0215  0.0591  -0.0056 48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.4410 0.4308 0.5805 0.0117  0.0599  -0.0164 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.1992 0.1957 0.3075 0.0194  0.0238  0.0037  49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.2035 0.1975 0.3047 0.0199  0.0212  0.0052  49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.1807 0.1680 0.2831 0.0192  0.0284  0.0020  49  GLY   A C   
344  O O   . GLY   A 43  ? 0.2003 0.1841 0.3059 0.0171  0.0361  -0.0030 49  GLY   A O   
345  N N   . CYS   A 44  ? 0.1796 0.1649 0.2779 0.0200  0.0262  0.0043  50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.1852 0.1636 0.2851 0.0191  0.0330  0.0018  50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.1941 0.1700 0.2787 0.0149  0.0334  -0.0029 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.2063 0.1765 0.2906 0.0128  0.0395  -0.0060 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.1963 0.1739 0.3068 0.0230  0.0320  0.0086  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.2329 0.2141 0.3660 0.0280  0.0333  0.0155  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1741 0.1541 0.2470 0.0136  0.0273  -0.0030 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.1655 0.1448 0.2255 0.0097  0.0274  -0.0063 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.1910 0.1694 0.2464 0.0045  0.0330  -0.0122 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.2052 0.1850 0.2639 0.0039  0.0345  -0.0136 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1629 0.1470 0.2144 0.0105  0.0199  -0.0040 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.1833 0.1691 0.2364 0.0138  0.0145  0.0009  51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.1836 0.1668 0.2389 0.0144  0.0158  0.0026  51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.1875 0.1769 0.2386 0.0149  0.0094  0.0029  51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.2053 0.1819 0.2531 -0.0001 0.0363  -0.0156 52  THR   A N   
360  C CA  . THR   A 46  ? 0.2178 0.1955 0.2583 -0.0071 0.0410  -0.0210 52  THR   A CA  
361  C C   . THR   A 46  ? 0.2059 0.1893 0.2342 -0.0102 0.0359  -0.0198 52  THR   A C   
362  O O   . THR   A 46  ? 0.2228 0.2068 0.2484 -0.0083 0.0323  -0.0172 52  THR   A O   
363  C CB  . THR   A 46  ? 0.2741 0.2457 0.3163 -0.0117 0.0503  -0.0266 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.3414 0.3110 0.3796 -0.0123 0.0499  -0.0260 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.2878 0.2533 0.3454 -0.0077 0.0564  -0.0272 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.1951 0.1835 0.2171 -0.0146 0.0352  -0.0206 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.1825 0.1776 0.1955 -0.0171 0.0302  -0.0179 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.1881 0.1857 0.1927 -0.0254 0.0340  -0.0212 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.2011 0.1976 0.2032 -0.0322 0.0404  -0.0264 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.1809 0.1812 0.1923 -0.0175 0.0267  -0.0152 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.1896 0.1874 0.2089 -0.0108 0.0240  -0.0131 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.1850 0.1928 0.1902 -0.0187 0.0212  -0.0105 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.2018 0.1987 0.2235 -0.0043 0.0186  -0.0094 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.1794 0.1810 0.1792 -0.0258 0.0303  -0.0186 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.1839 0.1901 0.1749 -0.0344 0.0325  -0.0206 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.1995 0.2152 0.1838 -0.0411 0.0307  -0.0188 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.1976 0.2183 0.1837 -0.0374 0.0250  -0.0132 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.1857 0.1953 0.1749 -0.0321 0.0281  -0.0170 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.2194 0.2379 0.1960 -0.0517 0.0358  -0.0235 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.2319 0.2612 0.2007 -0.0601 0.0339  -0.0212 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2542 0.2912 0.2138 -0.0696 0.0343  -0.0218 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.2858 0.3214 0.2385 -0.0796 0.0413  -0.0290 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.2363 0.2628 0.2034 -0.0660 0.0402  -0.0269 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.2324 0.2516 0.2096 -0.0569 0.0402  -0.0266 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.2148 0.2393 0.1952 -0.0507 0.0320  -0.0182 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.2047 0.2222 0.1940 -0.0432 0.0324  -0.0187 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.2320 0.2501 0.2263 -0.0359 0.0265  -0.0130 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.2154 0.2399 0.2081 -0.0344 0.0203  -0.0063 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2597 0.2721 0.2617 -0.0302 0.0272  -0.0140 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.2459 0.2909 0.2060 -0.0666 0.0273  -0.0146 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.2530 0.3055 0.2066 -0.0734 0.0267  -0.0141 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.2557 0.3204 0.2121 -0.0697 0.0180  -0.0038 56  CYS   A C   
393  O O   . CYS   A 50  ? 0.2809 0.3466 0.2445 -0.0614 0.0131  0.0025  56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.2360 0.2771 0.1924 -0.0695 0.0310  -0.0195 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.2350 0.2709 0.2023 -0.0542 0.0254  -0.0140 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.2899 0.3636 0.2416 -0.0757 0.0166  -0.0021 57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.3222 0.4076 0.2785 -0.0719 0.0094  0.0074  57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.3098 0.3915 0.2680 -0.0681 0.0100  0.0056  57  ASP   A C   
399  O O   . ASP   A 51  ? 0.3149 0.4081 0.2738 -0.0696 0.0062  0.0112  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.3935 0.4977 0.3437 -0.0831 0.0055  0.0140  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.5105 0.6197 0.4492 -0.0967 0.0094  0.0082  57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.5358 0.6319 0.4712 -0.0978 0.0163  -0.0017 57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.5642 0.6905 0.4974 -0.1069 0.0057  0.0139  57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.2660 0.3325 0.2263 -0.0626 0.0146  -0.0012 58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.2370 0.2994 0.1996 -0.0583 0.0149  -0.0021 58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.2436 0.3122 0.2140 -0.0496 0.0088  0.0056  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.2395 0.3078 0.2163 -0.0426 0.0058  0.0098  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2469 0.2927 0.2126 -0.0525 0.0196  -0.0083 58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2590 0.2945 0.2187 -0.0614 0.0291  -0.0184 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.2093 0.2830 0.1795 -0.0504 0.0078  0.0071  59  GLN   A N   
411  C CA  A GLN   A 53  ? 0.1949 0.2737 0.1729 -0.0426 0.0038  0.0131  59  GLN   A CA  
412  C CA  B GLN   A 53  ? 0.2054 0.2837 0.1836 -0.0423 0.0038  0.0130  59  GLN   A CA  
413  C C   . GLN   A 53  ? 0.1890 0.2593 0.1676 -0.0384 0.0058  0.0094  59  GLN   A C   
414  O O   . GLN   A 53  ? 0.1864 0.2612 0.1699 -0.0339 0.0037  0.0130  59  GLN   A O   
415  C CB  A GLN   A 53  ? 0.1911 0.2879 0.1711 -0.0466 -0.0004 0.0208  59  GLN   A CB  
416  C CB  B GLN   A 53  ? 0.2266 0.3229 0.2070 -0.0463 -0.0007 0.0213  59  GLN   A CB  
417  C CG  A GLN   A 53  ? 0.1791 0.2858 0.1637 -0.0464 -0.0044 0.0286  59  GLN   A CG  
418  C CG  B GLN   A 53  ? 0.2401 0.3426 0.2202 -0.0496 -0.0029 0.0255  59  GLN   A CG  
419  C CD  A GLN   A 53  ? 0.2023 0.3278 0.1923 -0.0487 -0.0091 0.0383  59  GLN   A CD  
420  C CD  B GLN   A 53  ? 0.2460 0.3397 0.2332 -0.0402 -0.0036 0.0267  59  GLN   A CD  
421  O OE1 A GLN   A 53  ? 0.2373 0.3763 0.2222 -0.0589 -0.0111 0.0419  59  GLN   A OE1 
422  O OE1 B GLN   A 53  ? 0.2235 0.3142 0.2087 -0.0419 -0.0030 0.0259  59  GLN   A OE1 
423  N NE2 A GLN   A 53  ? 0.1716 0.2991 0.1727 -0.0398 -0.0106 0.0431  59  GLN   A NE2 
424  N NE2 B GLN   A 53  ? 0.2547 0.3439 0.2501 -0.0304 -0.0043 0.0282  59  GLN   A NE2 
425  N N   . THR   A 54  ? 0.1757 0.2337 0.1499 -0.0402 0.0104  0.0026  60  THR   A N   
426  C CA  . THR   A 54  ? 0.1824 0.2315 0.1576 -0.0361 0.0123  -0.0001 60  THR   A CA  
427  C C   . THR   A 54  ? 0.1688 0.2038 0.1461 -0.0316 0.0149  -0.0037 60  THR   A C   
428  O O   . THR   A 54  ? 0.1903 0.2215 0.1660 -0.0349 0.0177  -0.0068 60  THR   A O   
429  C CB  . THR   A 54  ? 0.2195 0.2684 0.1889 -0.0431 0.0154  -0.0033 60  THR   A CB  
430  O OG1 . THR   A 54  ? 0.2998 0.3425 0.2640 -0.0502 0.0205  -0.0089 60  THR   A OG1 
431  C CG2 . THR   A 54  ? 0.2181 0.2820 0.1854 -0.0487 0.0129  0.0004  60  THR   A CG2 
432  N N   . GLY   A 55  ? 0.1580 0.1870 0.1391 -0.0247 0.0139  -0.0030 61  GLY   A N   
433  C CA  . GLY   A 55  ? 0.1621 0.1799 0.1466 -0.0203 0.0156  -0.0050 61  GLY   A CA  
434  C C   . GLY   A 55  ? 0.1588 0.1726 0.1458 -0.0147 0.0139  -0.0033 61  GLY   A C   
435  O O   . GLY   A 55  ? 0.1642 0.1815 0.1493 -0.0153 0.0131  -0.0023 61  GLY   A O   
436  N N   . VAL   A 56  ? 0.1513 0.1585 0.1425 -0.0098 0.0134  -0.0030 62  VAL   A N   
437  C CA  . VAL   A 56  ? 0.1450 0.1489 0.1378 -0.0057 0.0116  -0.0012 62  VAL   A CA  
438  C C   . VAL   A 56  ? 0.1367 0.1403 0.1330 -0.0008 0.0086  0.0002  62  VAL   A C   
439  O O   . VAL   A 56  ? 0.1539 0.1554 0.1531 -0.0001 0.0091  -0.0005 62  VAL   A O   
440  C CB  . VAL   A 56  ? 0.1631 0.1584 0.1580 -0.0064 0.0145  -0.0016 62  VAL   A CB  
441  C CG1 . VAL   A 56  ? 0.1869 0.1799 0.1837 -0.0027 0.0119  0.0017  62  VAL   A CG1 
442  C CG2 . VAL   A 56  ? 0.1717 0.1659 0.1627 -0.0119 0.0183  -0.0035 62  VAL   A CG2 
443  N N   . TYR   A 57  ? 0.1450 0.1510 0.1408 0.0018  0.0061  0.0015  63  TYR   A N   
444  C CA  . TYR   A 57  ? 0.1368 0.1420 0.1352 0.0054  0.0040  0.0020  63  TYR   A CA  
445  C C   . TYR   A 57  ? 0.1459 0.1489 0.1436 0.0064  0.0023  0.0033  63  TYR   A C   
446  O O   . TYR   A 57  ? 0.1572 0.1610 0.1518 0.0049  0.0024  0.0040  63  TYR   A O   
447  C CB  . TYR   A 57  ? 0.1405 0.1509 0.1398 0.0070  0.0032  0.0020  63  TYR   A CB  
448  C CG  . TYR   A 57  ? 0.1428 0.1560 0.1405 0.0078  0.0031  0.0019  63  TYR   A CG  
449  C CD1 . TYR   A 57  ? 0.1584 0.1760 0.1542 0.0059  0.0041  0.0023  63  TYR   A CD1 
450  C CD2 . TYR   A 57  ? 0.1503 0.1623 0.1484 0.0096  0.0025  0.0010  63  TYR   A CD2 
451  C CE1 . TYR   A 57  ? 0.1650 0.1856 0.1601 0.0064  0.0048  0.0018  63  TYR   A CE1 
452  C CE2 . TYR   A 57  ? 0.1581 0.1724 0.1546 0.0096  0.0037  -0.0001 63  TYR   A CE2 
453  C CZ  . TYR   A 57  ? 0.1660 0.1847 0.1615 0.0083  0.0050  0.0004  63  TYR   A CZ  
454  O OH  . TYR   A 57  ? 0.1901 0.2115 0.1846 0.0081  0.0068  -0.0010 63  TYR   A OH  
455  N N   . TYR   A 58  ? 0.1414 0.1429 0.1415 0.0082  0.0005  0.0038  64  TYR   A N   
456  C CA  . TYR   A 58  ? 0.1411 0.1425 0.1398 0.0080  -0.0018 0.0055  64  TYR   A CA  
457  C C   . TYR   A 58  ? 0.1451 0.1493 0.1404 0.0079  -0.0024 0.0035  64  TYR   A C   
458  O O   . TYR   A 58  ? 0.1452 0.1495 0.1424 0.0093  -0.0020 0.0016  64  TYR   A O   
459  C CB  . TYR   A 58  ? 0.1590 0.1585 0.1626 0.0090  -0.0036 0.0077  64  TYR   A CB  
460  C CG  . TYR   A 58  ? 0.1603 0.1617 0.1622 0.0076  -0.0067 0.0108  64  TYR   A CG  
461  C CD1 . TYR   A 58  ? 0.1673 0.1688 0.1679 0.0060  -0.0073 0.0142  64  TYR   A CD1 
462  C CD2 . TYR   A 58  ? 0.1565 0.1603 0.1577 0.0069  -0.0091 0.0105  64  TYR   A CD2 
463  C CE1 . TYR   A 58  ? 0.1820 0.1870 0.1801 0.0036  -0.0107 0.0179  64  TYR   A CE1 
464  C CE2 . TYR   A 58  ? 0.1647 0.1720 0.1629 0.0040  -0.0123 0.0134  64  TYR   A CE2 
465  C CZ  . TYR   A 58  ? 0.1793 0.1877 0.1761 0.0024  -0.0134 0.0176  64  TYR   A CZ  
466  O OH  . TYR   A 58  ? 0.2190 0.2323 0.2122 -0.0015 -0.0171 0.0215  64  TYR   A OH  
467  N N   . CYS   A 59  ? 0.1459 0.1520 0.1366 0.0058  -0.0027 0.0038  65  CYS   A N   
468  C CA  . CYS   A 59  ? 0.1543 0.1627 0.1412 0.0046  -0.0019 0.0009  65  CYS   A CA  
469  C C   . CYS   A 59  ? 0.1606 0.1700 0.1435 0.0014  -0.0045 0.0021  65  CYS   A C   
470  O O   . CYS   A 59  ? 0.1652 0.1762 0.1443 -0.0014 -0.0059 0.0049  65  CYS   A O   
471  C CB  . CYS   A 59  ? 0.1648 0.1758 0.1488 0.0035  0.0004  -0.0002 65  CYS   A CB  
472  S SG  . CYS   A 59  ? 0.1699 0.1831 0.1498 0.0015  0.0032  -0.0046 65  CYS   A SG  
473  N N   . SER   A 60  ? 0.1645 0.1735 0.1479 0.0010  -0.0054 0.0007  66  SER   A N   
474  C CA  . SER   A 60  ? 0.1741 0.1858 0.1536 -0.0032 -0.0087 0.0025  66  SER   A CA  
475  C C   . SER   A 60  ? 0.1720 0.1869 0.1430 -0.0084 -0.0076 0.0002  66  SER   A C   
476  O O   . SER   A 60  ? 0.1873 0.2060 0.1539 -0.0128 -0.0109 0.0040  66  SER   A O   
477  C CB  . SER   A 60  ? 0.2049 0.2160 0.1864 -0.0034 -0.0095 0.0009  66  SER   A CB  
478  O OG  . SER   A 60  ? 0.2514 0.2608 0.2309 -0.0041 -0.0059 -0.0052 66  SER   A OG  
479  N N   . SER   A 61  ? 0.1618 0.1754 0.1312 -0.0079 -0.0027 -0.0054 67  SER   A N   
480  C CA  . SER   A 61  ? 0.1615 0.1777 0.1231 -0.0130 -0.0003 -0.0089 67  SER   A CA  
481  C C   . SER   A 61  ? 0.1723 0.1912 0.1305 -0.0146 -0.0010 -0.0056 67  SER   A C   
482  O O   . SER   A 61  ? 0.1773 0.1990 0.1285 -0.0195 0.0008  -0.0080 67  SER   A O   
483  C CB  . SER   A 61  ? 0.1683 0.1822 0.1319 -0.0115 0.0061  -0.0157 67  SER   A CB  
484  O OG  . SER   A 61  ? 0.1752 0.1885 0.1451 -0.0062 0.0082  -0.0149 67  SER   A OG  
485  N N   . ARG   A 62  ? 0.1710 0.1888 0.1338 -0.0112 -0.0034 -0.0004 68  ARG   A N   
486  C CA  . ARG   A 62  ? 0.1795 0.1989 0.1399 -0.0128 -0.0044 0.0036  68  ARG   A CA  
487  C C   . ARG   A 62  ? 0.1969 0.2157 0.1603 -0.0127 -0.0090 0.0111  68  ARG   A C   
488  O O   . ARG   A 62  ? 0.2024 0.2214 0.1649 -0.0139 -0.0098 0.0153  68  ARG   A O   
489  C CB  . ARG   A 62  ? 0.1855 0.2036 0.1492 -0.0095 -0.0011 0.0021  68  ARG   A CB  
490  C CG  . ARG   A 62  ? 0.1820 0.2019 0.1452 -0.0092 0.0037  -0.0038 68  ARG   A CG  
491  C CD  . ARG   A 62  ? 0.1898 0.2132 0.1453 -0.0145 0.0053  -0.0050 68  ARG   A CD  
492  N NE  . ARG   A 62  ? 0.2109 0.2361 0.1676 -0.0140 0.0110  -0.0108 68  ARG   A NE  
493  C CZ  . ARG   A 62  ? 0.1921 0.2170 0.1469 -0.0160 0.0146  -0.0164 68  ARG   A CZ  
494  N NH1 . ARG   A 62  ? 0.2145 0.2382 0.1647 -0.0194 0.0125  -0.0170 68  ARG   A NH1 
495  N NH2 . ARG   A 62  ? 0.2120 0.2382 0.1700 -0.0150 0.0209  -0.0213 68  ARG   A NH2 
496  N N   . ARG   A 63  ? 0.1899 0.2075 0.1586 -0.0106 -0.0114 0.0130  69  ARG   A N   
497  C CA  . ARG   A 63  ? 0.1924 0.2088 0.1679 -0.0088 -0.0145 0.0201  69  ARG   A CA  
498  C C   . ARG   A 63  ? 0.2128 0.2246 0.1926 -0.0059 -0.0119 0.0214  69  ARG   A C   
499  O O   . ARG   A 63  ? 0.2324 0.2432 0.2146 -0.0065 -0.0130 0.0273  69  ARG   A O   
500  C CB  . ARG   A 63  ? 0.2273 0.2489 0.2004 -0.0134 -0.0191 0.0273  69  ARG   A CB  
501  C CG  . ARG   A 63  ? 0.2273 0.2540 0.1977 -0.0168 -0.0222 0.0270  69  ARG   A CG  
502  C CD  . ARG   A 63  ? 0.2361 0.2692 0.2075 -0.0206 -0.0279 0.0370  69  ARG   A CD  
503  N NE  . ARG   A 63  ? 0.2472 0.2872 0.2135 -0.0262 -0.0312 0.0365  69  ARG   A NE  
504  C CZ  . ARG   A 63  ? 0.2244 0.2707 0.1790 -0.0344 -0.0323 0.0351  69  ARG   A CZ  
505  N NH1 . ARG   A 63  ? 0.2465 0.2932 0.1939 -0.0375 -0.0308 0.0348  69  ARG   A NH1 
506  N NH2 . ARG   A 63  ? 0.2466 0.2991 0.1962 -0.0404 -0.0349 0.0341  69  ARG   A NH2 
507  N N   . LYS   A 64  ? 0.1945 0.2037 0.1753 -0.0033 -0.0084 0.0162  70  LYS   A N   
508  C CA  . LYS   A 64  ? 0.1947 0.2007 0.1775 -0.0023 -0.0056 0.0162  70  LYS   A CA  
509  C C   . LYS   A 64  ? 0.1899 0.1934 0.1769 0.0006  -0.0032 0.0127  70  LYS   A C   
510  O O   . LYS   A 64  ? 0.1864 0.1917 0.1733 0.0019  -0.0028 0.0092  70  LYS   A O   
511  C CB  . LYS   A 64  ? 0.2520 0.2607 0.2282 -0.0050 -0.0038 0.0140  70  LYS   A CB  
512  C CG  . LYS   A 64  ? 0.3690 0.3792 0.3409 -0.0088 -0.0054 0.0186  70  LYS   A CG  
513  C CD  . LYS   A 64  ? 0.4912 0.5033 0.4577 -0.0114 -0.0028 0.0164  70  LYS   A CD  
514  C CE  . LYS   A 64  ? 0.5694 0.5834 0.5308 -0.0158 -0.0045 0.0211  70  LYS   A CE  
515  N NZ  . LYS   A 64  ? 0.6189 0.6374 0.5755 -0.0189 -0.0077 0.0223  70  LYS   A NZ  
516  N N   . HIS   A 65  ? 0.1785 0.1780 0.1693 0.0010  -0.0009 0.0135  71  HIS   A N   
517  C CA  . HIS   A 65  ? 0.1715 0.1696 0.1645 0.0018  0.0019  0.0100  71  HIS   A CA  
518  C C   . HIS   A 65  ? 0.1851 0.1855 0.1738 -0.0007 0.0041  0.0080  71  HIS   A C   
519  O O   . HIS   A 65  ? 0.2237 0.2225 0.2104 -0.0030 0.0052  0.0095  71  HIS   A O   
520  C CB  . HIS   A 65  ? 0.1606 0.1528 0.1599 0.0024  0.0041  0.0112  71  HIS   A CB  
521  C CG  . HIS   A 65  ? 0.1735 0.1645 0.1789 0.0050  0.0021  0.0136  71  HIS   A CG  
522  N ND1 . HIS   A 65  ? 0.2139 0.2043 0.2228 0.0067  0.0029  0.0112  71  HIS   A ND1 
523  C CD2 . HIS   A 65  ? 0.1680 0.1593 0.1768 0.0058  -0.0007 0.0188  71  HIS   A CD2 
524  C CE1 . HIS   A 65  ? 0.1838 0.1739 0.1987 0.0086  0.0008  0.0147  71  HIS   A CE1 
525  N NE2 . HIS   A 65  ? 0.2165 0.2076 0.2315 0.0081  -0.0017 0.0196  71  HIS   A NE2 
526  N N   . TYR   A 66  ? 0.1593 0.1640 0.1472 -0.0004 0.0048  0.0052  72  TYR   A N   
527  C CA  . TYR   A 66  ? 0.1710 0.1804 0.1559 -0.0028 0.0064  0.0039  72  TYR   A CA  
528  C C   . TYR   A 66  ? 0.1589 0.1697 0.1449 -0.0046 0.0082  0.0025  72  TYR   A C   
529  O O   . TYR   A 66  ? 0.1557 0.1676 0.1444 -0.0029 0.0075  0.0020  72  TYR   A O   
530  C CB  . TYR   A 66  ? 0.1702 0.1860 0.1548 -0.0012 0.0057  0.0031  72  TYR   A CB  
531  C CG  . TYR   A 66  ? 0.1817 0.1976 0.1631 -0.0013 0.0050  0.0032  72  TYR   A CG  
532  C CD1 . TYR   A 66  ? 0.2003 0.2177 0.1776 -0.0043 0.0057  0.0038  72  TYR   A CD1 
533  C CD2 . TYR   A 66  ? 0.1896 0.2046 0.1714 0.0005  0.0037  0.0026  72  TYR   A CD2 
534  C CE1 . TYR   A 66  ? 0.2089 0.2275 0.1822 -0.0055 0.0053  0.0038  72  TYR   A CE1 
535  C CE2 . TYR   A 66  ? 0.1992 0.2153 0.1768 -0.0012 0.0034  0.0021  72  TYR   A CE2 
536  C CZ  . TYR   A 66  ? 0.2069 0.2250 0.1800 -0.0043 0.0042  0.0027  72  TYR   A CZ  
537  O OH  . TYR   A 66  ? 0.2411 0.2608 0.2088 -0.0071 0.0040  0.0022  72  TYR   A OH  
538  N N   . PRO   A 67  ? 0.1634 0.1752 0.1467 -0.0089 0.0104  0.0017  73  PRO   A N   
539  C CA  . PRO   A 67  ? 0.1671 0.1827 0.1498 -0.0125 0.0119  0.0002  73  PRO   A CA  
540  C C   . PRO   A 67  ? 0.1730 0.1993 0.1566 -0.0119 0.0100  0.0015  73  PRO   A C   
541  O O   . PRO   A 67  ? 0.1978 0.2286 0.1810 -0.0114 0.0096  0.0025  73  PRO   A O   
542  C CB  . PRO   A 67  ? 0.1982 0.2117 0.1771 -0.0182 0.0151  -0.0012 73  PRO   A CB  
543  C CG  . PRO   A 67  ? 0.2118 0.2238 0.1893 -0.0171 0.0144  0.0005  73  PRO   A CG  
544  C CD  . PRO   A 67  ? 0.1758 0.1853 0.1560 -0.0115 0.0116  0.0024  73  PRO   A CD  
545  N N   . VAL   A 68  ? 0.1584 0.1888 0.1438 -0.0124 0.0094  0.0020  74  VAL   A N   
546  C CA  . VAL   A 68  ? 0.1681 0.2093 0.1568 -0.0115 0.0075  0.0049  74  VAL   A CA  
547  C C   . VAL   A 68  ? 0.1578 0.2063 0.1456 -0.0164 0.0072  0.0061  74  VAL   A C   
548  O O   . VAL   A 68  ? 0.1667 0.2112 0.1520 -0.0194 0.0084  0.0041  74  VAL   A O   
549  C CB  . VAL   A 68  ? 0.1945 0.2345 0.1887 -0.0051 0.0059  0.0062  74  VAL   A CB  
550  C CG1 . VAL   A 68  ? 0.2062 0.2427 0.2009 -0.0013 0.0062  0.0052  74  VAL   A CG1 
551  C CG2 . VAL   A 68  ? 0.2114 0.2448 0.2060 -0.0040 0.0057  0.0051  74  VAL   A CG2 
552  N N   . SER   A 69  ? 0.1616 0.2223 0.1525 -0.0174 0.0055  0.0100  75  SER   A N   
553  C CA  A SER   A 69  ? 0.1611 0.2323 0.1529 -0.0216 0.0038  0.0136  75  SER   A CA  
554  C CA  B SER   A 69  ? 0.1629 0.2346 0.1548 -0.0216 0.0038  0.0137  75  SER   A CA  
555  C C   . SER   A 69  ? 0.1496 0.2236 0.1499 -0.0150 0.0017  0.0180  75  SER   A C   
556  O O   . SER   A 69  ? 0.1562 0.2300 0.1626 -0.0090 0.0018  0.0193  75  SER   A O   
557  C CB  A SER   A 69  ? 0.1843 0.2690 0.1762 -0.0266 0.0029  0.0169  75  SER   A CB  
558  C CB  B SER   A 69  ? 0.1943 0.2793 0.1874 -0.0254 0.0028  0.0172  75  SER   A CB  
559  O OG  A SER   A 69  ? 0.2384 0.3198 0.2227 -0.0327 0.0054  0.0125  75  SER   A OG  
560  O OG  B SER   A 69  ? 0.2445 0.3427 0.2397 -0.0297 0.0002  0.0226  75  SER   A OG  
561  N N   . PHE   A 70  ? 0.1555 0.2316 0.1563 -0.0165 0.0003  0.0201  76  PHE   A N   
562  C CA  . PHE   A 70  ? 0.1614 0.2385 0.1705 -0.0105 -0.0013 0.0243  76  PHE   A CA  
563  C C   . PHE   A 70  ? 0.1581 0.2475 0.1700 -0.0142 -0.0041 0.0311  76  PHE   A C   
564  O O   . PHE   A 70  ? 0.1714 0.2664 0.1762 -0.0226 -0.0047 0.0309  76  PHE   A O   
565  C CB  . PHE   A 70  ? 0.1641 0.2276 0.1720 -0.0064 -0.0001 0.0200  76  PHE   A CB  
566  C CG  . PHE   A 70  ? 0.1601 0.2183 0.1606 -0.0117 0.0010  0.0160  76  PHE   A CG  
567  C CD1 . PHE   A 70  ? 0.1693 0.2193 0.1640 -0.0140 0.0037  0.0104  76  PHE   A CD1 
568  C CD2 . PHE   A 70  ? 0.1591 0.2199 0.1594 -0.0142 0.0000  0.0180  76  PHE   A CD2 
569  C CE1 . PHE   A 70  ? 0.1697 0.2141 0.1597 -0.0183 0.0060  0.0065  76  PHE   A CE1 
570  C CE2 . PHE   A 70  ? 0.1697 0.2254 0.1637 -0.0194 0.0023  0.0135  76  PHE   A CE2 
571  C CZ  . PHE   A 70  ? 0.1714 0.2188 0.1608 -0.0213 0.0056  0.0075  76  PHE   A CZ  
572  N N   . SER   A 71  ? 0.1591 0.2536 0.1817 -0.0087 -0.0057 0.0377  77  SER   A N   
573  C CA  . SER   A 71  ? 0.1534 0.2608 0.1808 -0.0115 -0.0090 0.0464  77  SER   A CA  
574  C C   . SER   A 71  ? 0.1589 0.2622 0.1813 -0.0145 -0.0098 0.0457  77  SER   A C   
575  O O   . SER   A 71  ? 0.1629 0.2527 0.1812 -0.0123 -0.0075 0.0390  77  SER   A O   
576  C CB  . SER   A 71  ? 0.1718 0.2847 0.2148 -0.0037 -0.0096 0.0542  77  SER   A CB  
577  O OG  . SER   A 71  ? 0.1971 0.2972 0.2447 0.0038  -0.0073 0.0514  77  SER   A OG  
578  N N   . LYS   A 72  ? 0.1567 0.2724 0.1796 -0.0201 -0.0129 0.0529  78  LYS   A N   
579  C CA  . LYS   A 72  ? 0.1580 0.2715 0.1765 -0.0237 -0.0136 0.0530  78  LYS   A CA  
580  C C   . LYS   A 72  ? 0.1747 0.2810 0.2031 -0.0147 -0.0136 0.0562  78  LYS   A C   
581  O O   . LYS   A 72  ? 0.1762 0.2852 0.2168 -0.0077 -0.0140 0.0619  78  LYS   A O   
582  C CB  . LYS   A 72  ? 0.1909 0.3218 0.2064 -0.0335 -0.0174 0.0609  78  LYS   A CB  
583  C CG  . LYS   A 72  ? 0.2405 0.3765 0.2437 -0.0442 -0.0163 0.0557  78  LYS   A CG  
584  C CD  . LYS   A 72  ? 0.3237 0.4765 0.3207 -0.0564 -0.0197 0.0618  78  LYS   A CD  
585  C CE  . LYS   A 72  ? 0.4032 0.5586 0.3864 -0.0683 -0.0172 0.0544  78  LYS   A CE  
586  N NZ  . LYS   A 72  ? 0.4624 0.6310 0.4363 -0.0818 -0.0191 0.0576  78  LYS   A NZ  
587  N N   . PRO   A 73  ? 0.1768 0.2743 0.2012 -0.0150 -0.0126 0.0526  79  PRO   A N   
588  C CA  . PRO   A 73  ? 0.1725 0.2628 0.2059 -0.0074 -0.0123 0.0552  79  PRO   A CA  
589  C C   . PRO   A 73  ? 0.1766 0.2783 0.2221 -0.0053 -0.0153 0.0676  79  PRO   A C   
590  O O   . PRO   A 73  ? 0.2057 0.3205 0.2496 -0.0121 -0.0187 0.0750  79  PRO   A O   
591  C CB  . PRO   A 73  ? 0.2091 0.2925 0.2347 -0.0112 -0.0114 0.0506  79  PRO   A CB  
592  C CG  . PRO   A 73  ? 0.2546 0.3368 0.2682 -0.0184 -0.0095 0.0430  79  PRO   A CG  
593  C CD  . PRO   A 73  ? 0.1958 0.2893 0.2078 -0.0228 -0.0109 0.0457  79  PRO   A CD  
594  N N   . SER   A 74  ? 0.1725 0.2694 0.2303 0.0036  -0.0136 0.0699  80  SER   A N   
595  C CA  . SER   A 74  ? 0.1849 0.2920 0.2579 0.0072  -0.0154 0.0825  80  SER   A CA  
596  C C   . SER   A 74  ? 0.1758 0.2711 0.2606 0.0165  -0.0118 0.0825  80  SER   A C   
597  O O   . SER   A 74  ? 0.1727 0.2535 0.2532 0.0196  -0.0082 0.0727  80  SER   A O   
598  C CB  . SER   A 74  ? 0.2597 0.3783 0.3395 0.0081  -0.0160 0.0868  80  SER   A CB  
599  O OG  . SER   A 74  ? 0.3908 0.5160 0.4584 0.0003  -0.0175 0.0827  80  SER   A OG  
600  N N   . LEU   A 75  ? 0.1917 0.2942 0.2928 0.0207  -0.0124 0.0942  81  LEU   A N   
601  C CA  . LEU   A 75  ? 0.2163 0.3087 0.3314 0.0292  -0.0080 0.0956  81  LEU   A CA  
602  C C   . LEU   A 75  ? 0.2248 0.3174 0.3506 0.0353  -0.0039 0.0945  81  LEU   A C   
603  O O   . LEU   A 75  ? 0.2362 0.3431 0.3727 0.0360  -0.0057 0.1041  81  LEU   A O   
604  C CB  . LEU   A 75  ? 0.2317 0.3326 0.3598 0.0300  -0.0107 0.1103  81  LEU   A CB  
605  C CG  . LEU   A 75  ? 0.2713 0.3609 0.4142 0.0378  -0.0060 0.1129  81  LEU   A CG  
606  C CD1 . LEU   A 75  ? 0.2910 0.3640 0.4232 0.0370  -0.0036 0.1024  81  LEU   A CD1 
607  C CD2 . LEU   A 75  ? 0.2831 0.3839 0.4404 0.0382  -0.0094 0.1300  81  LEU   A CD2 
608  N N   . ILE   A 76  ? 0.2111 0.2893 0.3338 0.0390  0.0015  0.0831  82  ILE   A N   
609  C CA  . ILE   A 76  ? 0.2341 0.3107 0.3637 0.0435  0.0064  0.0791  82  ILE   A CA  
610  C C   . ILE   A 76  ? 0.2369 0.2999 0.3772 0.0503  0.0137  0.0752  82  ILE   A C   
611  O O   . ILE   A 76  ? 0.2326 0.2825 0.3659 0.0498  0.0155  0.0682  82  ILE   A O   
612  C CB  . ILE   A 76  ? 0.2587 0.3308 0.3711 0.0395  0.0063  0.0674  82  ILE   A CB  
613  C CG1 . ILE   A 76  ? 0.2898 0.3738 0.3906 0.0317  0.0000  0.0697  82  ILE   A CG1 
614  C CG2 . ILE   A 76  ? 0.2774 0.3463 0.3943 0.0432  0.0118  0.0615  82  ILE   A CG2 
615  C CD1 . ILE   A 76  ? 0.3083 0.3917 0.3982 0.0285  -0.0001 0.0628  82  ILE   A CD1 
616  N N   . PHE   A 77  ? 0.2353 0.3007 0.3921 0.0560  0.0188  0.0787  83  PHE   A N   
617  C CA  . PHE   A 77  ? 0.2449 0.2966 0.4122 0.0618  0.0277  0.0735  83  PHE   A CA  
618  C C   . PHE   A 77  ? 0.2760 0.3169 0.4296 0.0598  0.0318  0.0584  83  PHE   A C   
619  O O   . PHE   A 77  ? 0.3115 0.3581 0.4585 0.0577  0.0309  0.0549  83  PHE   A O   
620  C CB  . PHE   A 77  ? 0.2506 0.3090 0.4417 0.0685  0.0329  0.0819  83  PHE   A CB  
621  C CG  . PHE   A 77  ? 0.2843 0.3280 0.4892 0.0743  0.0424  0.0791  83  PHE   A CG  
622  C CD1 . PHE   A 77  ? 0.3182 0.3563 0.5302 0.0760  0.0423  0.0851  83  PHE   A CD1 
623  C CD2 . PHE   A 77  ? 0.3285 0.3632 0.5381 0.0771  0.0519  0.0694  83  PHE   A CD2 
624  C CE1 . PHE   A 77  ? 0.3519 0.3752 0.5764 0.0807  0.0518  0.0817  83  PHE   A CE1 
625  C CE2 . PHE   A 77  ? 0.3414 0.3617 0.5634 0.0814  0.0619  0.0656  83  PHE   A CE2 
626  C CZ  . PHE   A 77  ? 0.3545 0.3688 0.5843 0.0834  0.0619  0.0718  83  PHE   A CZ  
627  N N   . VAL   A 78  ? 0.2482 0.2743 0.3959 0.0592  0.0355  0.0498  84  VAL   A N   
628  C CA  . VAL   A 78  ? 0.2359 0.2522 0.3703 0.0564  0.0389  0.0363  84  VAL   A CA  
629  C C   . VAL   A 78  ? 0.2288 0.2331 0.3737 0.0599  0.0494  0.0305  84  VAL   A C   
630  O O   . VAL   A 78  ? 0.2355 0.2323 0.3888 0.0621  0.0524  0.0326  84  VAL   A O   
631  C CB  . VAL   A 78  ? 0.2296 0.2400 0.3462 0.0511  0.0339  0.0307  84  VAL   A CB  
632  C CG1 . VAL   A 78  ? 0.2407 0.2425 0.3445 0.0476  0.0369  0.0183  84  VAL   A CG1 
633  C CG2 . VAL   A 78  ? 0.2263 0.2477 0.3337 0.0474  0.0252  0.0359  84  VAL   A CG2 
634  N N   . GLU   A 79  ? 0.2318 0.2336 0.3749 0.0593  0.0552  0.0223  85  GLU   A N   
635  C CA  . GLU   A 79  ? 0.2590 0.2493 0.4112 0.0614  0.0665  0.0151  85  GLU   A CA  
636  C C   . GLU   A 79  ? 0.2696 0.2460 0.4117 0.0574  0.0689  0.0062  85  GLU   A C   
637  O O   . GLU   A 79  ? 0.2697 0.2458 0.3946 0.0523  0.0621  0.0029  85  GLU   A O   
638  C CB  . GLU   A 79  ? 0.3175 0.3091 0.4665 0.0598  0.0719  0.0073  85  GLU   A CB  
639  C CG  . GLU   A 79  ? 0.4066 0.4112 0.5699 0.0644  0.0720  0.0157  85  GLU   A CG  
640  C CD  . GLU   A 79  ? 0.5268 0.5326 0.7161 0.0721  0.0777  0.0252  85  GLU   A CD  
641  O OE1 . GLU   A 79  ? 0.5295 0.5231 0.7291 0.0745  0.0882  0.0200  85  GLU   A OE1 
642  O OE2 . GLU   A 79  ? 0.5763 0.5954 0.7762 0.0754  0.0717  0.0383  85  GLU   A OE2 
643  N N   . ALA   A 80  ? 0.2861 0.2510 0.4391 0.0594  0.0794  0.0016  86  ALA   A N   
644  C CA  . ALA   A 80  ? 0.3140 0.2651 0.4586 0.0548  0.0834  -0.0078 86  ALA   A CA  
645  C C   . ALA   A 80  ? 0.3388 0.2885 0.4626 0.0470  0.0821  -0.0192 86  ALA   A C   
646  O O   . ALA   A 80  ? 0.3649 0.3185 0.4855 0.0456  0.0848  -0.0236 86  ALA   A O   
647  C CB  . ALA   A 80  ? 0.3288 0.2677 0.4895 0.0577  0.0970  -0.0121 86  ALA   A CB  
648  N N   . SER   A 81  ? 0.3304 0.2755 0.4403 0.0416  0.0778  -0.0234 87  SER   A N   
649  C CA  . SER   A 81  ? 0.3246 0.2690 0.4151 0.0335  0.0759  -0.0330 87  SER   A CA  
650  C C   . SER   A 81  ? 0.3247 0.2576 0.4100 0.0282  0.0800  -0.0407 87  SER   A C   
651  O O   . SER   A 81  ? 0.3527 0.2776 0.4500 0.0313  0.0853  -0.0390 87  SER   A O   
652  C CB  . SER   A 81  ? 0.3231 0.2770 0.4011 0.0316  0.0637  -0.0282 87  SER   A CB  
653  O OG  . SER   A 81  ? 0.3045 0.2569 0.3818 0.0319  0.0583  -0.0238 87  SER   A OG  
654  N N   . GLU   A 82  ? 0.3403 0.2730 0.4082 0.0198  0.0775  -0.0485 88  GLU   A N   
655  C CA  . GLU   A 82  ? 0.3474 0.2714 0.4089 0.0135  0.0801  -0.0553 88  GLU   A CA  
656  C C   . GLU   A 82  ? 0.3102 0.2354 0.3713 0.0151  0.0718  -0.0483 88  GLU   A C   
657  O O   . GLU   A 82  ? 0.3089 0.2265 0.3685 0.0113  0.0745  -0.0524 88  GLU   A O   
658  C CB  . GLU   A 82  ? 0.4043 0.3293 0.4477 0.0031  0.0799  -0.0651 88  GLU   A CB  
659  C CG  . GLU   A 82  ? 0.4681 0.4036 0.4982 0.0001  0.0678  -0.0610 88  GLU   A CG  
660  C CD  . GLU   A 82  ? 0.6169 0.5541 0.6304 -0.0109 0.0671  -0.0690 88  GLU   A CD  
661  O OE1 . GLU   A 82  ? 0.6450 0.5874 0.6514 -0.0141 0.0674  -0.0716 88  GLU   A OE1 
662  O OE2 . GLU   A 82  ? 0.6627 0.5970 0.6704 -0.0169 0.0663  -0.0724 88  GLU   A OE2 
663  N N   . TYR   A 83  ? 0.2842 0.2186 0.3476 0.0202  0.0630  -0.0383 89  TYR   A N   
664  C CA  . TYR   A 83  ? 0.2584 0.1946 0.3213 0.0212  0.0557  -0.0320 89  TYR   A CA  
665  C C   . TYR   A 83  ? 0.2458 0.1811 0.3237 0.0281  0.0564  -0.0230 89  TYR   A C   
666  O O   . TYR   A 83  ? 0.2490 0.1817 0.3280 0.0279  0.0539  -0.0199 89  TYR   A O   
667  C CB  . TYR   A 83  ? 0.2570 0.2037 0.3102 0.0203  0.0457  -0.0281 89  TYR   A CB  
668  C CG  . TYR   A 83  ? 0.2602 0.2087 0.2991 0.0131  0.0436  -0.0350 89  TYR   A CG  
669  C CD1 . TYR   A 83  ? 0.2813 0.2273 0.3129 0.0073  0.0419  -0.0388 89  TYR   A CD1 
670  C CD2 . TYR   A 83  ? 0.3068 0.2602 0.3400 0.0115  0.0435  -0.0373 89  TYR   A CD2 
671  C CE1 . TYR   A 83  ? 0.3162 0.2661 0.3354 0.0002  0.0389  -0.0434 89  TYR   A CE1 
672  C CE2 . TYR   A 83  ? 0.3339 0.2902 0.3541 0.0044  0.0408  -0.0421 89  TYR   A CE2 
673  C CZ  . TYR   A 83  ? 0.3520 0.3068 0.3655 -0.0013 0.0385  -0.0449 89  TYR   A CZ  
674  O OH  . TYR   A 83  ? 0.4063 0.3660 0.4078 -0.0088 0.0350  -0.0480 89  TYR   A OH  
675  N N   . TYR   A 84  ? 0.2501 0.1887 0.3398 0.0341  0.0592  -0.0178 90  TYR   A N   
676  C CA  . TYR   A 84  ? 0.2454 0.1852 0.3507 0.0405  0.0593  -0.0072 90  TYR   A CA  
677  C C   . TYR   A 84  ? 0.2605 0.1976 0.3824 0.0459  0.0683  -0.0059 90  TYR   A C   
678  O O   . TYR   A 84  ? 0.2678 0.2078 0.3878 0.0455  0.0711  -0.0102 90  TYR   A O   
679  C CB  . TYR   A 84  ? 0.2252 0.1783 0.3292 0.0427  0.0498  0.0026  90  TYR   A CB  
680  C CG  . TYR   A 84  ? 0.2044 0.1614 0.2951 0.0385  0.0413  0.0029  90  TYR   A CG  
681  C CD1 . TYR   A 84  ? 0.2119 0.1657 0.3037 0.0378  0.0392  0.0061  90  TYR   A CD1 
682  C CD2 . TYR   A 84  ? 0.2029 0.1661 0.2809 0.0353  0.0360  -0.0001 90  TYR   A CD2 
683  C CE1 . TYR   A 84  ? 0.2004 0.1580 0.2814 0.0341  0.0324  0.0062  90  TYR   A CE1 
684  C CE2 . TYR   A 84  ? 0.2011 0.1674 0.2693 0.0320  0.0294  0.0002  90  TYR   A CE2 
685  C CZ  . TYR   A 84  ? 0.1948 0.1582 0.2645 0.0314  0.0279  0.0028  90  TYR   A CZ  
686  O OH  . TYR   A 84  ? 0.2019 0.1685 0.2633 0.0282  0.0222  0.0028  90  TYR   A OH  
687  N N   . PRO   A 85  ? 0.2774 0.2102 0.4165 0.0510  0.0725  0.0014  91  PRO   A N   
688  C CA  . PRO   A 85  ? 0.2838 0.2164 0.4424 0.0575  0.0804  0.0056  91  PRO   A CA  
689  C C   . PRO   A 85  ? 0.2954 0.2443 0.4579 0.0612  0.0731  0.0158  91  PRO   A C   
690  O O   . PRO   A 85  ? 0.2986 0.2570 0.4493 0.0587  0.0628  0.0198  91  PRO   A O   
691  C CB  . PRO   A 85  ? 0.3036 0.2287 0.4793 0.0618  0.0846  0.0130  91  PRO   A CB  
692  C CG  . PRO   A 85  ? 0.3066 0.2358 0.4728 0.0591  0.0747  0.0185  91  PRO   A CG  
693  C CD  . PRO   A 85  ? 0.2861 0.2158 0.4288 0.0515  0.0695  0.0079  91  PRO   A CD  
694  N N   . ALA   A 86  ? 0.3019 0.2545 0.4817 0.0670  0.0788  0.0206  92  ALA   A N   
695  C CA  . ALA   A 86  ? 0.2986 0.2678 0.4830 0.0699  0.0719  0.0310  92  ALA   A CA  
696  C C   . ALA   A 86  ? 0.2911 0.2675 0.4817 0.0717  0.0642  0.0450  92  ALA   A C   
697  O O   . ALA   A 86  ? 0.3153 0.2844 0.5183 0.0746  0.0680  0.0498  92  ALA   A O   
698  C CB  . ALA   A 86  ? 0.2958 0.2676 0.5004 0.0760  0.0804  0.0339  92  ALA   A CB  
699  N N   . ARG   A 87  ? 0.2676 0.2566 0.4466 0.0685  0.0536  0.0499  93  ARG   A N   
700  C CA  . ARG   A 87  ? 0.2576 0.2535 0.4379 0.0678  0.0460  0.0613  93  ARG   A CA  
701  C C   . ARG   A 87  ? 0.2654 0.2774 0.4360 0.0643  0.0364  0.0666  93  ARG   A C   
702  O O   . ARG   A 87  ? 0.2749 0.2910 0.4367 0.0624  0.0356  0.0607  93  ARG   A O   
703  C CB  . ARG   A 87  ? 0.2687 0.2539 0.4356 0.0634  0.0446  0.0546  93  ARG   A CB  
704  C CG  . ARG   A 87  ? 0.2805 0.2685 0.4245 0.0568  0.0381  0.0462  93  ARG   A CG  
705  C CD  . ARG   A 87  ? 0.2854 0.2614 0.4176 0.0529  0.0394  0.0363  93  ARG   A CD  
706  N NE  . ARG   A 87  ? 0.2761 0.2562 0.3912 0.0475  0.0319  0.0335  93  ARG   A NE  
707  C CZ  . ARG   A 87  ? 0.3120 0.2961 0.4145 0.0444  0.0287  0.0278  93  ARG   A CZ  
708  N NH1 . ARG   A 87  ? 0.2941 0.2802 0.3974 0.0456  0.0315  0.0245  93  ARG   A NH1 
709  N NH2 . ARG   A 87  ? 0.2476 0.2337 0.3373 0.0400  0.0231  0.0257  93  ARG   A NH2 
710  N N   . TYR   A 88  ? 0.2622 0.2828 0.4328 0.0624  0.0294  0.0771  94  TYR   A N   
711  C CA  . TYR   A 88  ? 0.2647 0.2995 0.4240 0.0573  0.0209  0.0809  94  TYR   A CA  
712  C C   . TYR   A 88  ? 0.2349 0.2641 0.3741 0.0512  0.0172  0.0723  94  TYR   A C   
713  O O   . TYR   A 88  ? 0.2500 0.2727 0.3875 0.0501  0.0168  0.0727  94  TYR   A O   
714  C CB  . TYR   A 88  ? 0.2642 0.3127 0.4338 0.0571  0.0155  0.0969  94  TYR   A CB  
715  C CG  . TYR   A 88  ? 0.2728 0.3322 0.4616 0.0623  0.0172  0.1070  94  TYR   A CG  
716  C CD1 . TYR   A 88  ? 0.2777 0.3505 0.4632 0.0601  0.0139  0.1082  94  TYR   A CD1 
717  C CD2 . TYR   A 88  ? 0.2931 0.3485 0.5046 0.0696  0.0232  0.1146  94  TYR   A CD2 
718  C CE1 . TYR   A 88  ? 0.2955 0.3795 0.4999 0.0649  0.0155  0.1176  94  TYR   A CE1 
719  C CE2 . TYR   A 88  ? 0.2995 0.3654 0.5313 0.0750  0.0254  0.1243  94  TYR   A CE2 
720  C CZ  . TYR   A 88  ? 0.3096 0.3901 0.5376 0.0727  0.0215  0.1255  94  TYR   A CZ  
721  O OH  . TYR   A 88  ? 0.3385 0.4307 0.5873 0.0779  0.0235  0.1354  94  TYR   A OH  
722  N N   . GLN   A 89  ? 0.2023 0.2336 0.3270 0.0474  0.0149  0.0644  95  GLN   A N   
723  C CA  . GLN   A 89  ? 0.1913 0.2188 0.2984 0.0418  0.0114  0.0570  95  GLN   A CA  
724  C C   . GLN   A 89  ? 0.1876 0.2285 0.2882 0.0366  0.0048  0.0634  95  GLN   A C   
725  O O   . GLN   A 89  ? 0.1907 0.2426 0.2932 0.0358  0.0029  0.0676  95  GLN   A O   
726  C CB  . GLN   A 89  ? 0.1826 0.2037 0.2789 0.0407  0.0135  0.0453  95  GLN   A CB  
727  C CG  . GLN   A 89  ? 0.1847 0.2023 0.2659 0.0357  0.0102  0.0389  95  GLN   A CG  
728  C CD  . GLN   A 89  ? 0.1692 0.1783 0.2419 0.0349  0.0125  0.0283  95  GLN   A CD  
729  O OE1 . GLN   A 89  ? 0.2006 0.2018 0.2768 0.0371  0.0174  0.0235  95  GLN   A OE1 
730  N NE2 . GLN   A 89  ? 0.1890 0.2000 0.2505 0.0311  0.0092  0.0247  95  GLN   A NE2 
731  N N   . SER   A 90  ? 0.1689 0.2095 0.2621 0.0322  0.0016  0.0642  96  SER   A N   
732  C CA  . SER   A 90  ? 0.1623 0.2149 0.2482 0.0258  -0.0036 0.0691  96  SER   A CA  
733  C C   . SER   A 90  ? 0.1625 0.2132 0.2326 0.0207  -0.0046 0.0594  96  SER   A C   
734  O O   . SER   A 90  ? 0.1781 0.2179 0.2430 0.0222  -0.0021 0.0502  96  SER   A O   
735  C CB  . SER   A 90  ? 0.1953 0.2498 0.2823 0.0231  -0.0059 0.0758  96  SER   A CB  
736  O OG  . SER   A 90  ? 0.2348 0.2768 0.3151 0.0227  -0.0040 0.0675  96  SER   A OG  
737  N N   . HIS   A 91  ? 0.1660 0.2278 0.2294 0.0145  -0.0080 0.0622  97  HIS   A N   
738  C CA  . HIS   A 91  ? 0.1668 0.2272 0.2164 0.0089  -0.0082 0.0540  97  HIS   A CA  
739  C C   . HIS   A 91  ? 0.1519 0.2059 0.1993 0.0121  -0.0058 0.0463  97  HIS   A C   
740  O O   . HIS   A 91  ? 0.1654 0.2125 0.2043 0.0103  -0.0046 0.0382  97  HIS   A O   
741  C CB  . HIS   A 91  ? 0.1879 0.2404 0.2305 0.0062  -0.0075 0.0488  97  HIS   A CB  
742  C CG  . HIS   A 91  ? 0.2073 0.2664 0.2501 0.0017  -0.0098 0.0560  97  HIS   A CG  
743  N ND1 . HIS   A 91  ? 0.2380 0.3050 0.2714 -0.0070 -0.0113 0.0561  97  HIS   A ND1 
744  C CD2 . HIS   A 91  ? 0.2298 0.2890 0.2811 0.0043  -0.0105 0.0633  97  HIS   A CD2 
745  C CE1 . HIS   A 91  ? 0.2428 0.3150 0.2782 -0.0099 -0.0133 0.0635  97  HIS   A CE1 
746  N NE2 . HIS   A 91  ? 0.2453 0.3131 0.2919 -0.0030 -0.0131 0.0685  97  HIS   A NE2 
747  N N   . LEU   A 92  ? 0.1436 0.2010 0.1989 0.0162  -0.0049 0.0492  98  LEU   A N   
748  C CA  . LEU   A 92  ? 0.1452 0.1975 0.1989 0.0189  -0.0024 0.0426  98  LEU   A CA  
749  C C   . LEU   A 92  ? 0.1445 0.2069 0.1943 0.0149  -0.0039 0.0438  98  LEU   A C   
750  O O   . LEU   A 92  ? 0.1503 0.2250 0.2052 0.0131  -0.0062 0.0519  98  LEU   A O   
751  C CB  . LEU   A 92  ? 0.1684 0.2170 0.2339 0.0257  0.0010  0.0440  98  LEU   A CB  
752  C CG  . LEU   A 92  ? 0.1885 0.2310 0.2517 0.0280  0.0043  0.0363  98  LEU   A CG  
753  C CD1 . LEU   A 92  ? 0.1989 0.2305 0.2531 0.0270  0.0052  0.0279  98  LEU   A CD1 
754  C CD2 . LEU   A 92  ? 0.2113 0.2513 0.2872 0.0339  0.0090  0.0376  98  LEU   A CD2 
755  N N   . MET   A 93  ? 0.1552 0.2130 0.1969 0.0134  -0.0028 0.0366  99  MET   A N   
756  C CA  . MET   A 93  ? 0.1543 0.2196 0.1915 0.0094  -0.0035 0.0364  99  MET   A CA  
757  C C   . MET   A 93  ? 0.1547 0.2162 0.1939 0.0134  -0.0009 0.0327  99  MET   A C   
758  O O   . MET   A 93  ? 0.1677 0.2186 0.2042 0.0159  0.0010  0.0267  99  MET   A O   
759  C CB  . MET   A 93  ? 0.1617 0.2232 0.1871 0.0034  -0.0035 0.0306  99  MET   A CB  
760  C CG  . MET   A 93  ? 0.1713 0.2362 0.1934 -0.0016 -0.0051 0.0330  99  MET   A CG  
761  S SD  . MET   A 93  ? 0.2137 0.2720 0.2240 -0.0083 -0.0030 0.0251  99  MET   A SD  
762  C CE  . MET   A 93  ? 0.2536 0.2974 0.2655 -0.0017 -0.0011 0.0193  99  MET   A CE  
763  N N   . LEU   A 94  ? 0.1398 0.2105 0.1832 0.0132  -0.0009 0.0360  100 LEU   A N   
764  C CA  . LEU   A 94  ? 0.1497 0.2174 0.1947 0.0164  0.0020  0.0322  100 LEU   A CA  
765  C C   . LEU   A 94  ? 0.1366 0.2071 0.1730 0.0115  0.0016  0.0291  100 LEU   A C   
766  O O   . LEU   A 94  ? 0.1585 0.2376 0.1914 0.0060  -0.0006 0.0319  100 LEU   A O   
767  C CB  . LEU   A 94  ? 0.1751 0.2512 0.2341 0.0208  0.0036  0.0384  100 LEU   A CB  
768  C CG  . LEU   A 94  ? 0.2221 0.2951 0.2928 0.0265  0.0054  0.0420  100 LEU   A CG  
769  C CD1 . LEU   A 94  ? 0.2384 0.3186 0.3249 0.0315  0.0086  0.0472  100 LEU   A CD1 
770  C CD2 . LEU   A 94  ? 0.2562 0.3142 0.3234 0.0292  0.0088  0.0339  100 LEU   A CD2 
771  N N   . ALA   A 95  ? 0.1429 0.2065 0.1757 0.0129  0.0040  0.0234  101 ALA   A N   
772  C CA  . ALA   A 95  ? 0.1400 0.2053 0.1658 0.0089  0.0043  0.0207  101 ALA   A CA  
773  C C   . ALA   A 95  ? 0.1367 0.2001 0.1651 0.0121  0.0074  0.0181  101 ALA   A C   
774  O O   . ALA   A 95  ? 0.1524 0.2107 0.1857 0.0165  0.0097  0.0165  101 ALA   A O   
775  C CB  . ALA   A 95  ? 0.1584 0.2141 0.1736 0.0057  0.0039  0.0155  101 ALA   A CB  
776  N N   . VAL   A 96  ? 0.1328 0.2000 0.1571 0.0089  0.0079  0.0169  102 VAL   A N   
777  C CA  . VAL   A 96  ? 0.1362 0.2013 0.1603 0.0103  0.0110  0.0135  102 VAL   A CA  
778  C C   . VAL   A 96  ? 0.1606 0.2147 0.1743 0.0086  0.0109  0.0083  102 VAL   A C   
779  O O   . VAL   A 96  ? 0.1829 0.2347 0.1893 0.0047  0.0093  0.0076  102 VAL   A O   
780  C CB  . VAL   A 96  ? 0.1386 0.2134 0.1632 0.0073  0.0115  0.0153  102 VAL   A CB  
781  C CG1 . VAL   A 96  ? 0.1598 0.2324 0.1828 0.0078  0.0150  0.0113  102 VAL   A CG1 
782  C CG2 . VAL   A 96  ? 0.1364 0.2242 0.1733 0.0091  0.0110  0.0221  102 VAL   A CG2 
783  N N   . GLY   A 97  ? 0.1713 0.2192 0.1852 0.0112  0.0129  0.0050  103 GLY   A N   
784  C CA  . GLY   A 97  ? 0.1885 0.2279 0.1936 0.0093  0.0121  0.0015  103 GLY   A CA  
785  C C   . GLY   A 97  ? 0.1902 0.2248 0.1960 0.0112  0.0145  -0.0020 103 GLY   A C   
786  O O   . GLY   A 97  ? 0.2018 0.2374 0.2154 0.0145  0.0172  -0.0022 103 GLY   A O   
787  N N   . HIS   A 98  ? 0.2050 0.2345 0.2027 0.0085  0.0137  -0.0046 104 HIS   A N   
788  C CA  . HIS   A 98  ? 0.2170 0.2425 0.2131 0.0083  0.0159  -0.0085 104 HIS   A CA  
789  C C   . HIS   A 98  ? 0.1940 0.2143 0.1914 0.0099  0.0143  -0.0088 104 HIS   A C   
790  O O   . HIS   A 98  ? 0.1955 0.2136 0.1905 0.0093  0.0104  -0.0066 104 HIS   A O   
791  C CB  . HIS   A 98  ? 0.2184 0.2427 0.2046 0.0035  0.0151  -0.0102 104 HIS   A CB  
792  C CG  . HIS   A 98  ? 0.2088 0.2306 0.1917 0.0014  0.0178  -0.0148 104 HIS   A CG  
793  N ND1 . HIS   A 98  ? 0.2184 0.2415 0.2042 0.0014  0.0238  -0.0191 104 HIS   A ND1 
794  C CD2 . HIS   A 98  ? 0.2147 0.2330 0.1920 -0.0014 0.0156  -0.0159 104 HIS   A CD2 
795  C CE1 . HIS   A 98  ? 0.2308 0.2503 0.2117 -0.0018 0.0255  -0.0236 104 HIS   A CE1 
796  N NE2 . HIS   A 98  ? 0.2213 0.2386 0.1967 -0.0039 0.0202  -0.0215 104 HIS   A NE2 
797  N N   . SER   A 99  ? 0.1930 0.2109 0.1947 0.0116  0.0176  -0.0116 105 SER   A N   
798  C CA  . SER   A 99  ? 0.1978 0.2106 0.2008 0.0126  0.0167  -0.0124 105 SER   A CA  
799  C C   . SER   A 99  ? 0.2391 0.2485 0.2431 0.0119  0.0219  -0.0177 105 SER   A C   
800  O O   . SER   A 99  ? 0.2592 0.2697 0.2712 0.0147  0.0270  -0.0186 105 SER   A O   
801  C CB  . SER   A 99  ? 0.2003 0.2141 0.2113 0.0166  0.0154  -0.0083 105 SER   A CB  
802  O OG  . SER   A 99  ? 0.2136 0.2226 0.2268 0.0176  0.0151  -0.0090 105 SER   A OG  
803  N N   . GLU   A 100 ? 0.2159 0.2218 0.2127 0.0078  0.0213  -0.0212 106 GLU   A N   
804  C CA  . GLU   A 100 ? 0.2445 0.2467 0.2405 0.0053  0.0271  -0.0276 106 GLU   A CA  
805  C C   . GLU   A 100 ? 0.2698 0.2674 0.2640 0.0038  0.0252  -0.0287 106 GLU   A C   
806  O O   . GLU   A 100 ? 0.2836 0.2819 0.2768 0.0044  0.0193  -0.0246 106 GLU   A O   
807  C CB  . GLU   A 100 ? 0.2515 0.2561 0.2379 -0.0009 0.0293  -0.0318 106 GLU   A CB  
808  C CG  . GLU   A 100 ? 0.2631 0.2697 0.2389 -0.0062 0.0230  -0.0297 106 GLU   A CG  
809  C CD  . GLU   A 100 ? 0.2573 0.2669 0.2227 -0.0134 0.0244  -0.0330 106 GLU   A CD  
810  O OE1 . GLU   A 100 ? 0.3209 0.3291 0.2798 -0.0195 0.0268  -0.0382 106 GLU   A OE1 
811  O OE2 . GLU   A 100 ? 0.2370 0.2506 0.2002 -0.0138 0.0233  -0.0304 106 GLU   A OE2 
812  N N   . PRO   A 101 ? 0.3148 0.3074 0.3095 0.0017  0.0308  -0.0347 107 PRO   A N   
813  C CA  . PRO   A 101 ? 0.3131 0.3018 0.3060 -0.0006 0.0292  -0.0362 107 PRO   A CA  
814  C C   . PRO   A 101 ? 0.2985 0.2911 0.2816 -0.0057 0.0221  -0.0340 107 PRO   A C   
815  O O   . PRO   A 101 ? 0.3154 0.3118 0.2897 -0.0112 0.0213  -0.0354 107 PRO   A O   
816  C CB  . PRO   A 101 ? 0.3335 0.3167 0.3252 -0.0046 0.0376  -0.0447 107 PRO   A CB  
817  C CG  . PRO   A 101 ? 0.3476 0.3301 0.3486 0.0001  0.0442  -0.0455 107 PRO   A CG  
818  C CD  . PRO   A 101 ? 0.3207 0.3107 0.3189 0.0011  0.0397  -0.0408 107 PRO   A CD  
819  N N   . GLY   A 102 ? 0.2471 0.2396 0.2328 -0.0036 0.0170  -0.0297 108 GLY   A N   
820  C CA  . GLY   A 102 ? 0.2489 0.2455 0.2297 -0.0064 0.0100  -0.0256 108 GLY   A CA  
821  C C   . GLY   A 102 ? 0.2101 0.2090 0.1954 -0.0015 0.0055  -0.0189 108 GLY   A C   
822  O O   . GLY   A 102 ? 0.2216 0.2226 0.2069 -0.0020 0.0007  -0.0151 108 GLY   A O   
823  N N   . ASP   A 103 ? 0.1852 0.1843 0.1745 0.0027  0.0075  -0.0177 109 ASP   A N   
824  C CA  . ASP   A 103 ? 0.1779 0.1790 0.1702 0.0060  0.0043  -0.0124 109 ASP   A CA  
825  C C   . ASP   A 103 ? 0.1745 0.1739 0.1735 0.0097  0.0035  -0.0103 109 ASP   A C   
826  O O   . ASP   A 103 ? 0.1718 0.1724 0.1724 0.0111  0.0011  -0.0068 109 ASP   A O   
827  C CB  . ASP   A 103 ? 0.1734 0.1771 0.1664 0.0075  0.0063  -0.0118 109 ASP   A CB  
828  C CG  . ASP   A 103 ? 0.1836 0.1898 0.1692 0.0033  0.0060  -0.0125 109 ASP   A CG  
829  O OD1 . ASP   A 103 ? 0.1882 0.1955 0.1696 0.0004  0.0022  -0.0103 109 ASP   A OD1 
830  O OD2 . ASP   A 103 ? 0.1823 0.1901 0.1671 0.0030  0.0095  -0.0146 109 ASP   A OD2 
831  N N   . CYS   A 104 ? 0.1664 0.1625 0.1689 0.0108  0.0059  -0.0125 110 CYS   A N   
832  C CA  . CYS   A 104 ? 0.1722 0.1671 0.1805 0.0137  0.0049  -0.0099 110 CYS   A CA  
833  C C   . CYS   A 104 ? 0.1665 0.1620 0.1735 0.0124  0.0009  -0.0079 110 CYS   A C   
834  O O   . CYS   A 104 ? 0.1695 0.1654 0.1731 0.0093  -0.0009 -0.0088 110 CYS   A O   
835  C CB  . CYS   A 104 ? 0.1726 0.1631 0.1848 0.0144  0.0081  -0.0123 110 CYS   A CB  
836  S SG  . CYS   A 104 ? 0.2084 0.1981 0.2277 0.0180  0.0137  -0.0124 110 CYS   A SG  
837  N N   . GLY   A 105 ? 0.1565 0.1528 0.1669 0.0143  -0.0002 -0.0050 111 GLY   A N   
838  C CA  . GLY   A 105 ? 0.1575 0.1541 0.1690 0.0136  -0.0027 -0.0032 111 GLY   A CA  
839  C C   . GLY   A 105 ? 0.1491 0.1473 0.1599 0.0135  -0.0036 -0.0010 111 GLY   A C   
840  O O   . GLY   A 105 ? 0.1563 0.1543 0.1702 0.0136  -0.0044 0.0005  111 GLY   A O   
841  N N   . GLY   A 106 ? 0.1549 0.1544 0.1624 0.0130  -0.0031 -0.0011 112 GLY   A N   
842  C CA  . GLY   A 106 ? 0.1517 0.1519 0.1586 0.0125  -0.0034 0.0009  112 GLY   A CA  
843  C C   . GLY   A 106 ? 0.1412 0.1412 0.1505 0.0131  -0.0017 0.0013  112 GLY   A C   
844  O O   . GLY   A 106 ? 0.1421 0.1437 0.1518 0.0136  -0.0006 0.0008  112 GLY   A O   
845  N N   . ILE   A 107 ? 0.1421 0.1406 0.1533 0.0124  -0.0011 0.0023  113 ILE   A N   
846  C CA  . ILE   A 107 ? 0.1415 0.1397 0.1537 0.0114  0.0013  0.0016  113 ILE   A CA  
847  C C   . ILE   A 107 ? 0.1415 0.1416 0.1500 0.0094  0.0028  0.0012  113 ILE   A C   
848  O O   . ILE   A 107 ? 0.1480 0.1475 0.1547 0.0088  0.0028  0.0018  113 ILE   A O   
849  C CB  . ILE   A 107 ? 0.1450 0.1397 0.1618 0.0112  0.0028  0.0019  113 ILE   A CB  
850  C CG1 . ILE   A 107 ? 0.1650 0.1595 0.1862 0.0125  0.0018  0.0019  113 ILE   A CG1 
851  C CG2 . ILE   A 107 ? 0.1639 0.1573 0.1805 0.0084  0.0069  -0.0001 113 ILE   A CG2 
852  C CD1 . ILE   A 107 ? 0.1950 0.1871 0.2233 0.0130  0.0034  0.0028  113 ILE   A CD1 
853  N N   . LEU   A 108 ? 0.1307 0.1339 0.1382 0.0077  0.0039  0.0008  114 LEU   A N   
854  C CA  . LEU   A 108 ? 0.1329 0.1392 0.1371 0.0043  0.0055  0.0005  114 LEU   A CA  
855  C C   . LEU   A 108 ? 0.1332 0.1370 0.1373 0.0007  0.0087  -0.0016 114 LEU   A C   
856  O O   . LEU   A 108 ? 0.1412 0.1450 0.1469 0.0003  0.0091  -0.0020 114 LEU   A O   
857  C CB  . LEU   A 108 ? 0.1391 0.1525 0.1429 0.0039  0.0043  0.0024  114 LEU   A CB  
858  C CG  . LEU   A 108 ? 0.1485 0.1679 0.1489 -0.0011 0.0054  0.0029  114 LEU   A CG  
859  C CD1 . LEU   A 108 ? 0.1622 0.1824 0.1602 -0.0017 0.0058  0.0026  114 LEU   A CD1 
860  C CD2 . LEU   A 108 ? 0.1699 0.1979 0.1722 -0.0013 0.0035  0.0068  114 LEU   A CD2 
861  N N   . ARG   A 109 ? 0.1398 0.1411 0.1420 -0.0023 0.0116  -0.0032 115 ARG   A N   
862  C CA  . ARG   A 109 ? 0.1449 0.1425 0.1472 -0.0065 0.0164  -0.0064 115 ARG   A CA  
863  C C   . ARG   A 109 ? 0.1584 0.1580 0.1551 -0.0126 0.0192  -0.0085 115 ARG   A C   
864  O O   . ARG   A 109 ? 0.1616 0.1634 0.1558 -0.0128 0.0179  -0.0072 115 ARG   A O   
865  C CB  . ARG   A 109 ? 0.1666 0.1562 0.1752 -0.0038 0.0187  -0.0068 115 ARG   A CB  
866  C CG  . ARG   A 109 ? 0.1684 0.1549 0.1774 -0.0028 0.0188  -0.0051 115 ARG   A CG  
867  C CD  . ARG   A 109 ? 0.1915 0.1714 0.2092 0.0004  0.0205  -0.0036 115 ARG   A CD  
868  N NE  . ARG   A 109 ? 0.2100 0.1921 0.2313 0.0050  0.0156  0.0000  115 ARG   A NE  
869  C CZ  . ARG   A 109 ? 0.1996 0.1802 0.2282 0.0075  0.0158  0.0010  115 ARG   A CZ  
870  N NH1 . ARG   A 109 ? 0.2061 0.1832 0.2392 0.0061  0.0210  -0.0020 115 ARG   A NH1 
871  N NH2 . ARG   A 109 ? 0.2089 0.1924 0.2399 0.0106  0.0110  0.0044  115 ARG   A NH2 
872  N N   . CYS   A 110 ? 0.1793 0.1783 0.1738 -0.0185 0.0236  -0.0121 116 CYS   A N   
873  C CA  . CYS   A 110 ? 0.2169 0.2175 0.2051 -0.0263 0.0273  -0.0152 116 CYS   A CA  
874  C C   . CYS   A 110 ? 0.2532 0.2440 0.2437 -0.0294 0.0350  -0.0205 116 CYS   A C   
875  O O   . CYS   A 110 ? 0.2461 0.2297 0.2444 -0.0244 0.0367  -0.0205 116 CYS   A O   
876  C CB  . CYS   A 110 ? 0.2097 0.2208 0.1918 -0.0325 0.0258  -0.0147 116 CYS   A CB  
877  S SG  . CYS   A 110 ? 0.2070 0.2173 0.1886 -0.0364 0.0290  -0.0178 116 CYS   A SG  
878  N N   . GLN   A 111 ? 0.2790 0.2696 0.2632 -0.0382 0.0403  -0.0252 117 GLN   A N   
879  C CA  . GLN   A 111 ? 0.3176 0.2978 0.3045 -0.0420 0.0493  -0.0312 117 GLN   A CA  
880  C C   . GLN   A 111 ? 0.3237 0.3016 0.3141 -0.0425 0.0529  -0.0343 117 GLN   A C   
881  O O   . GLN   A 111 ? 0.3584 0.3263 0.3561 -0.0416 0.0601  -0.0379 117 GLN   A O   
882  C CB  . GLN   A 111 ? 0.3784 0.3591 0.3566 -0.0530 0.0550  -0.0367 117 GLN   A CB  
883  C CG  . GLN   A 111 ? 0.4440 0.4348 0.4124 -0.0626 0.0550  -0.0392 117 GLN   A CG  
884  C CD  . GLN   A 111 ? 0.5243 0.5174 0.4830 -0.0749 0.0599  -0.0445 117 GLN   A CD  
885  O OE1 . GLN   A 111 ? 0.5494 0.5526 0.5019 -0.0783 0.0550  -0.0413 117 GLN   A OE1 
886  N NE2 . GLN   A 111 ? 0.5137 0.4979 0.4710 -0.0823 0.0702  -0.0529 117 GLN   A NE2 
887  N N   . HIS   A 112 ? 0.2729 0.2597 0.2597 -0.0431 0.0481  -0.0321 118 HIS   A N   
888  C CA  . HIS   A 112 ? 0.2591 0.2450 0.2478 -0.0446 0.0513  -0.0349 118 HIS   A CA  
889  C C   . HIS   A 112 ? 0.2598 0.2430 0.2585 -0.0348 0.0478  -0.0310 118 HIS   A C   
890  O O   . HIS   A 112 ? 0.2847 0.2662 0.2867 -0.0352 0.0509  -0.0333 118 HIS   A O   
891  C CB  . HIS   A 112 ? 0.2618 0.2594 0.2408 -0.0521 0.0482  -0.0342 118 HIS   A CB  
892  C CG  . HIS   A 112 ? 0.3104 0.3131 0.2789 -0.0632 0.0509  -0.0375 118 HIS   A CG  
893  N ND1 . HIS   A 112 ? 0.3103 0.3239 0.2731 -0.0650 0.0443  -0.0324 118 HIS   A ND1 
894  C CD2 . HIS   A 112 ? 0.3448 0.3439 0.3075 -0.0737 0.0599  -0.0456 118 HIS   A CD2 
895  C CE1 . HIS   A 112 ? 0.3564 0.3731 0.3103 -0.0764 0.0487  -0.0370 118 HIS   A CE1 
896  N NE2 . HIS   A 112 ? 0.3709 0.3787 0.3236 -0.0825 0.0583  -0.0455 118 HIS   A NE2 
897  N N   . GLY   A 113 ? 0.2345 0.2186 0.2369 -0.0268 0.0411  -0.0251 119 GLY   A N   
898  C CA  . GLY   A 113 ? 0.2088 0.1918 0.2192 -0.0189 0.0373  -0.0215 119 GLY   A CA  
899  C C   . GLY   A 113 ? 0.1816 0.1711 0.1900 -0.0143 0.0289  -0.0159 119 GLY   A C   
900  O O   . GLY   A 113 ? 0.1798 0.1732 0.1831 -0.0153 0.0262  -0.0142 119 GLY   A O   
901  N N   . VAL   A 114 ? 0.1680 0.1585 0.1808 -0.0095 0.0254  -0.0134 120 VAL   A N   
902  C CA  . VAL   A 114 ? 0.1658 0.1609 0.1776 -0.0052 0.0187  -0.0090 120 VAL   A CA  
903  C C   . VAL   A 114 ? 0.1568 0.1594 0.1629 -0.0085 0.0164  -0.0075 120 VAL   A C   
904  O O   . VAL   A 114 ? 0.1575 0.1622 0.1621 -0.0122 0.0179  -0.0086 120 VAL   A O   
905  C CB  . VAL   A 114 ? 0.1628 0.1561 0.1810 -0.0002 0.0163  -0.0072 120 VAL   A CB  
906  C CG1 . VAL   A 114 ? 0.1691 0.1660 0.1859 0.0031  0.0109  -0.0040 120 VAL   A CG1 
907  C CG2 . VAL   A 114 ? 0.1732 0.1614 0.1983 0.0032  0.0174  -0.0066 120 VAL   A CG2 
908  N N   . VAL   A 115 ? 0.1501 0.1571 0.1539 -0.0072 0.0129  -0.0046 121 VAL   A N   
909  C CA  . VAL   A 115 ? 0.1538 0.1691 0.1545 -0.0097 0.0105  -0.0015 121 VAL   A CA  
910  C C   . VAL   A 115 ? 0.1547 0.1713 0.1595 -0.0045 0.0068  0.0022  121 VAL   A C   
911  O O   . VAL   A 115 ? 0.1641 0.1857 0.1692 -0.0057 0.0053  0.0053  121 VAL   A O   
912  C CB  . VAL   A 115 ? 0.1639 0.1840 0.1612 -0.0116 0.0097  -0.0003 121 VAL   A CB  
913  C CG1 . VAL   A 115 ? 0.1832 0.2137 0.1802 -0.0128 0.0063  0.0049  121 VAL   A CG1 
914  C CG2 . VAL   A 115 ? 0.1819 0.2007 0.1743 -0.0183 0.0140  -0.0044 121 VAL   A CG2 
915  N N   . GLY   A 116 ? 0.1509 0.1633 0.1589 0.0010  0.0054  0.0022  122 GLY   A N   
916  C CA  . GLY   A 116 ? 0.1585 0.1708 0.1702 0.0053  0.0030  0.0045  122 GLY   A CA  
917  C C   . GLY   A 116 ? 0.1427 0.1506 0.1557 0.0091  0.0022  0.0033  122 GLY   A C   
918  O O   . GLY   A 116 ? 0.1459 0.1508 0.1579 0.0088  0.0029  0.0016  122 GLY   A O   
919  N N   . ILE   A 117 ? 0.1346 0.1422 0.1501 0.0122  0.0011  0.0044  123 ILE   A N   
920  C CA  . ILE   A 117 ? 0.1311 0.1353 0.1465 0.0144  0.0006  0.0027  123 ILE   A CA  
921  C C   . ILE   A 117 ? 0.1356 0.1417 0.1521 0.0162  0.0011  0.0033  123 ILE   A C   
922  O O   . ILE   A 117 ? 0.1449 0.1537 0.1650 0.0173  0.0016  0.0058  123 ILE   A O   
923  C CB  . ILE   A 117 ? 0.1425 0.1428 0.1598 0.0153  -0.0001 0.0014  123 ILE   A CB  
924  C CG1 . ILE   A 117 ? 0.1578 0.1579 0.1783 0.0161  0.0002  0.0026  123 ILE   A CG1 
925  C CG2 . ILE   A 117 ? 0.1596 0.1583 0.1776 0.0141  -0.0003 0.0008  123 ILE   A CG2 
926  C CD1 . ILE   A 117 ? 0.1781 0.1743 0.2002 0.0164  -0.0002 0.0008  123 ILE   A CD1 
927  N N   . VAL   A 118 ? 0.1344 0.1393 0.1484 0.0164  0.0013  0.0015  124 VAL   A N   
928  C CA  . VAL   A 118 ? 0.1343 0.1403 0.1498 0.0179  0.0030  0.0009  124 VAL   A CA  
929  C C   . VAL   A 118 ? 0.1431 0.1461 0.1631 0.0198  0.0045  0.0003  124 VAL   A C   
930  O O   . VAL   A 118 ? 0.1479 0.1468 0.1668 0.0191  0.0039  -0.0016 124 VAL   A O   
931  C CB  . VAL   A 118 ? 0.1529 0.1577 0.1637 0.0167  0.0033  -0.0017 124 VAL   A CB  
932  C CG1 . VAL   A 118 ? 0.1581 0.1632 0.1705 0.0177  0.0064  -0.0036 124 VAL   A CG1 
933  C CG2 . VAL   A 118 ? 0.1638 0.1709 0.1709 0.0149  0.0023  -0.0007 124 VAL   A CG2 
934  N N   . SER   A 119 ? 0.1498 0.1548 0.1757 0.0221  0.0067  0.0024  125 SER   A N   
935  C CA  . SER   A 119 ? 0.1693 0.1706 0.2014 0.0243  0.0092  0.0024  125 SER   A CA  
936  C C   . SER   A 119 ? 0.1840 0.1848 0.2213 0.0265  0.0137  0.0012  125 SER   A C   
937  O O   . SER   A 119 ? 0.2173 0.2123 0.2577 0.0273  0.0172  -0.0018 125 SER   A O   
938  C CB  . SER   A 119 ? 0.1864 0.1902 0.2236 0.0253  0.0079  0.0076  125 SER   A CB  
939  O OG  . SER   A 119 ? 0.1955 0.1955 0.2402 0.0277  0.0105  0.0089  125 SER   A OG  
940  N N   . THR   A 120 ? 0.1717 0.1782 0.2099 0.0270  0.0142  0.0026  126 THR   A N   
941  C CA  . THR   A 120 ? 0.1836 0.1902 0.2285 0.0294  0.0194  0.0015  126 THR   A CA  
942  C C   . THR   A 120 ? 0.1919 0.2019 0.2311 0.0274  0.0199  -0.0012 126 THR   A C   
943  O O   . THR   A 120 ? 0.1862 0.1994 0.2184 0.0250  0.0160  -0.0003 126 THR   A O   
944  C CB  . THR   A 120 ? 0.2041 0.2165 0.2618 0.0334  0.0205  0.0088  126 THR   A CB  
945  O OG1 . THR   A 120 ? 0.2114 0.2335 0.2680 0.0324  0.0170  0.0134  126 THR   A OG1 
946  C CG2 . THR   A 120 ? 0.2097 0.2199 0.2730 0.0349  0.0194  0.0129  126 THR   A CG2 
947  N N   . GLY   A 121 ? 0.1968 0.2058 0.2398 0.0284  0.0254  -0.0045 127 GLY   A N   
948  C CA  . GLY   A 121 ? 0.2173 0.2298 0.2551 0.0261  0.0264  -0.0071 127 GLY   A CA  
949  C C   . GLY   A 121 ? 0.2338 0.2478 0.2805 0.0284  0.0333  -0.0086 127 GLY   A C   
950  O O   . GLY   A 121 ? 0.2485 0.2638 0.3078 0.0328  0.0361  -0.0049 127 GLY   A O   
951  N N   . GLY   A 122 ? 0.2262 0.2416 0.2668 0.0255  0.0354  -0.0129 128 GLY   A N   
952  C CA  . GLY   A 122 ? 0.2264 0.2434 0.2747 0.0269  0.0429  -0.0156 128 GLY   A CA  
953  C C   . GLY   A 122 ? 0.2407 0.2680 0.2961 0.0291  0.0422  -0.0100 128 GLY   A C   
954  O O   . GLY   A 122 ? 0.2434 0.2768 0.3021 0.0308  0.0369  -0.0028 128 GLY   A O   
955  N N   . ASN   A 123 ? 0.2399 0.2697 0.2983 0.0287  0.0482  -0.0134 129 ASN   A N   
956  C CA  . ASN   A 123 ? 0.2641 0.3047 0.3323 0.0312  0.0489  -0.0082 129 ASN   A CA  
957  C C   . ASN   A 123 ? 0.2316 0.2795 0.2910 0.0281  0.0414  -0.0040 129 ASN   A C   
958  O O   . ASN   A 123 ? 0.2197 0.2779 0.2872 0.0296  0.0402  0.0020  129 ASN   A O   
959  C CB  . ASN   A 123 ? 0.2901 0.3348 0.3774 0.0379  0.0504  -0.0005 129 ASN   A CB  
960  C CG  . ASN   A 123 ? 0.3659 0.4033 0.4655 0.0417  0.0597  -0.0042 129 ASN   A CG  
961  O OD1 . ASN   A 123 ? 0.3795 0.4118 0.4761 0.0394  0.0668  -0.0127 129 ASN   A OD1 
962  N ND2 . ASN   A 123 ? 0.3882 0.4253 0.5026 0.0471  0.0605  0.0021  129 ASN   A ND2 
963  N N   . GLY   A 124 ? 0.2077 0.2510 0.2517 0.0233  0.0370  -0.0070 130 GLY   A N   
964  C CA  . GLY   A 124 ? 0.1947 0.2432 0.2311 0.0202  0.0311  -0.0036 130 GLY   A CA  
965  C C   . GLY   A 124 ? 0.1648 0.2156 0.2033 0.0213  0.0256  0.0023  130 GLY   A C   
966  O O   . GLY   A 124 ? 0.1845 0.2401 0.2182 0.0184  0.0217  0.0051  130 GLY   A O   
967  N N   . LEU   A 125 ? 0.1534 0.2002 0.1977 0.0245  0.0256  0.0037  131 LEU   A N   
968  C CA  . LEU   A 125 ? 0.1531 0.2017 0.1982 0.0248  0.0206  0.0089  131 LEU   A CA  
969  C C   . LEU   A 125 ? 0.1743 0.2131 0.2118 0.0238  0.0186  0.0056  131 LEU   A C   
970  O O   . LEU   A 125 ? 0.1932 0.2246 0.2287 0.0241  0.0215  0.0006  131 LEU   A O   
971  C CB  . LEU   A 125 ? 0.1586 0.2121 0.2185 0.0294  0.0219  0.0149  131 LEU   A CB  
972  C CG  . LEU   A 125 ? 0.1666 0.2324 0.2372 0.0308  0.0233  0.0203  131 LEU   A CG  
973  C CD1 . LEU   A 125 ? 0.1915 0.2601 0.2801 0.0368  0.0270  0.0257  131 LEU   A CD1 
974  C CD2 . LEU   A 125 ? 0.1666 0.2427 0.2327 0.0265  0.0176  0.0255  131 LEU   A CD2 
975  N N   . VAL   A 126 ? 0.1496 0.1891 0.1827 0.0218  0.0140  0.0082  132 VAL   A N   
976  C CA  . VAL   A 126 ? 0.1613 0.1929 0.1893 0.0212  0.0120  0.0062  132 VAL   A CA  
977  C C   . VAL   A 126 ? 0.1525 0.1873 0.1852 0.0219  0.0096  0.0113  132 VAL   A C   
978  O O   . VAL   A 126 ? 0.1622 0.2047 0.1953 0.0199  0.0076  0.0153  132 VAL   A O   
979  C CB  . VAL   A 126 ? 0.1628 0.1908 0.1802 0.0174  0.0097  0.0034  132 VAL   A CB  
980  C CG1 . VAL   A 126 ? 0.1805 0.2140 0.1947 0.0143  0.0078  0.0058  132 VAL   A CG1 
981  C CG2 . VAL   A 126 ? 0.1694 0.1907 0.1838 0.0172  0.0077  0.0021  132 VAL   A CG2 
982  N N   . GLY   A 127 ? 0.1481 0.1776 0.1838 0.0239  0.0099  0.0111  133 GLY   A N   
983  C CA  . GLY   A 127 ? 0.1537 0.1860 0.1929 0.0239  0.0076  0.0160  133 GLY   A CA  
984  C C   . GLY   A 127 ? 0.1537 0.1797 0.1861 0.0219  0.0056  0.0133  133 GLY   A C   
985  O O   . GLY   A 127 ? 0.1715 0.1901 0.2007 0.0222  0.0065  0.0087  133 GLY   A O   
986  N N   . PHE   A 128 ? 0.1398 0.1697 0.1700 0.0190  0.0031  0.0161  134 PHE   A N   
987  C CA  . PHE   A 128 ? 0.1433 0.1683 0.1684 0.0167  0.0019  0.0138  134 PHE   A CA  
988  C C   . PHE   A 128 ? 0.1435 0.1701 0.1719 0.0164  0.0009  0.0175  134 PHE   A C   
989  O O   . PHE   A 128 ? 0.1460 0.1808 0.1774 0.0150  -0.0003 0.0230  134 PHE   A O   
990  C CB  . PHE   A 128 ? 0.1505 0.1776 0.1687 0.0122  0.0011  0.0125  134 PHE   A CB  
991  C CG  . PHE   A 128 ? 0.1445 0.1710 0.1592 0.0118  0.0019  0.0100  134 PHE   A CG  
992  C CD1 . PHE   A 128 ? 0.1421 0.1618 0.1536 0.0125  0.0023  0.0063  134 PHE   A CD1 
993  C CD2 . PHE   A 128 ? 0.1587 0.1926 0.1736 0.0102  0.0020  0.0121  134 PHE   A CD2 
994  C CE1 . PHE   A 128 ? 0.1499 0.1695 0.1580 0.0115  0.0028  0.0048  134 PHE   A CE1 
995  C CE2 . PHE   A 128 ? 0.1627 0.1959 0.1742 0.0094  0.0029  0.0099  134 PHE   A CE2 
996  C CZ  . PHE   A 128 ? 0.1555 0.1812 0.1633 0.0101  0.0033  0.0063  134 PHE   A CZ  
997  N N   . ALA   A 129 ? 0.1441 0.1639 0.1723 0.0172  0.0011  0.0152  135 ALA   A N   
998  C CA  . ALA   A 129 ? 0.1420 0.1628 0.1723 0.0162  0.0002  0.0184  135 ALA   A CA  
999  C C   . ALA   A 129 ? 0.1402 0.1634 0.1642 0.0111  -0.0006 0.0173  135 ALA   A C   
1000 O O   . ALA   A 129 ? 0.1488 0.1669 0.1689 0.0101  0.0001  0.0126  135 ALA   A O   
1001 C CB  . ALA   A 129 ? 0.1487 0.1615 0.1808 0.0183  0.0011  0.0156  135 ALA   A CB  
1002 N N   . ASP   A 130 ? 0.1427 0.1739 0.1661 0.0073  -0.0018 0.0217  136 ASP   A N   
1003 C CA  . ASP   A 130 ? 0.1509 0.1844 0.1675 0.0010  -0.0013 0.0197  136 ASP   A CA  
1004 C C   . ASP   A 130 ? 0.1562 0.1848 0.1722 0.0000  -0.0005 0.0177  136 ASP   A C   
1005 O O   . ASP   A 130 ? 0.1707 0.1982 0.1911 0.0023  -0.0013 0.0206  136 ASP   A O   
1006 C CB  . ASP   A 130 ? 0.1772 0.2223 0.1928 -0.0041 -0.0031 0.0258  136 ASP   A CB  
1007 C CG  . ASP   A 130 ? 0.2348 0.2831 0.2422 -0.0124 -0.0019 0.0230  136 ASP   A CG  
1008 O OD1 . ASP   A 130 ? 0.2184 0.2630 0.2211 -0.0145 0.0006  0.0172  136 ASP   A OD1 
1009 O OD2 . ASP   A 130 ? 0.3029 0.3568 0.3086 -0.0171 -0.0028 0.0264  136 ASP   A OD2 
1010 N N   . VAL   A 131 ? 0.1496 0.1751 0.1609 -0.0035 0.0018  0.0126  137 VAL   A N   
1011 C CA  . VAL   A 131 ? 0.1533 0.1755 0.1642 -0.0055 0.0033  0.0103  137 VAL   A CA  
1012 C C   . VAL   A 131 ? 0.1709 0.1969 0.1758 -0.0134 0.0059  0.0083  137 VAL   A C   
1013 O O   . VAL   A 131 ? 0.1629 0.1869 0.1674 -0.0159 0.0080  0.0060  137 VAL   A O   
1014 C CB  . VAL   A 131 ? 0.1483 0.1620 0.1620 -0.0018 0.0048  0.0057  137 VAL   A CB  
1015 C CG1 . VAL   A 131 ? 0.1581 0.1683 0.1762 0.0043  0.0026  0.0069  137 VAL   A CG1 
1016 C CG2 . VAL   A 131 ? 0.1667 0.1775 0.1785 -0.0028 0.0073  0.0016  137 VAL   A CG2 
1017 N N   . ARG   A 132 ? 0.1648 0.1972 0.1650 -0.0183 0.0060  0.0090  138 ARG   A N   
1018 C CA  . ARG   A 132 ? 0.1618 0.1972 0.1549 -0.0273 0.0094  0.0055  138 ARG   A CA  
1019 C C   . ARG   A 132 ? 0.1760 0.2182 0.1659 -0.0335 0.0088  0.0085  138 ARG   A C   
1020 O O   . ARG   A 132 ? 0.1915 0.2346 0.1753 -0.0416 0.0130  0.0040  138 ARG   A O   
1021 C CB  . ARG   A 132 ? 0.1722 0.2134 0.1602 -0.0321 0.0096  0.0055  138 ARG   A CB  
1022 C CG  . ARG   A 132 ? 0.1725 0.2059 0.1624 -0.0277 0.0115  0.0013  138 ARG   A CG  
1023 C CD  . ARG   A 132 ? 0.1854 0.2251 0.1702 -0.0328 0.0115  0.0016  138 ARG   A CD  
1024 N NE  . ARG   A 132 ? 0.1864 0.2353 0.1740 -0.0301 0.0062  0.0091  138 ARG   A NE  
1025 C CZ  . ARG   A 132 ? 0.2067 0.2628 0.1924 -0.0327 0.0048  0.0113  138 ARG   A CZ  
1026 N NH1 . ARG   A 132 ? 0.2101 0.2663 0.1890 -0.0397 0.0082  0.0065  138 ARG   A NH1 
1027 N NH2 . ARG   A 132 ? 0.2141 0.2781 0.2051 -0.0289 0.0006  0.0185  138 ARG   A NH2 
1028 N N   . ASP   A 133 ? 0.1720 0.2192 0.1659 -0.0306 0.0042  0.0163  139 ASP   A N   
1029 C CA  . ASP   A 133 ? 0.1796 0.2338 0.1708 -0.0366 0.0031  0.0205  139 ASP   A CA  
1030 C C   . ASP   A 133 ? 0.1812 0.2281 0.1750 -0.0345 0.0050  0.0178  139 ASP   A C   
1031 O O   . ASP   A 133 ? 0.1990 0.2505 0.1897 -0.0402 0.0050  0.0202  139 ASP   A O   
1032 C CB  . ASP   A 133 ? 0.2020 0.2651 0.1983 -0.0343 -0.0025 0.0315  139 ASP   A CB  
1033 C CG  . ASP   A 133 ? 0.2377 0.2932 0.2443 -0.0235 -0.0040 0.0339  139 ASP   A CG  
1034 O OD1 . ASP   A 133 ? 0.2344 0.2815 0.2434 -0.0175 -0.0025 0.0288  139 ASP   A OD1 
1035 O OD2 . ASP   A 133 ? 0.2690 0.3270 0.2808 -0.0217 -0.0064 0.0411  139 ASP   A OD2 
1036 N N   . LEU   A 134 ? 0.1666 0.2031 0.1659 -0.0271 0.0065  0.0133  140 LEU   A N   
1037 C CA  . LEU   A 134 ? 0.1735 0.2038 0.1764 -0.0247 0.0080  0.0111  140 LEU   A CA  
1038 C C   . LEU   A 134 ? 0.1773 0.2046 0.1770 -0.0297 0.0137  0.0035  140 LEU   A C   
1039 O O   . LEU   A 134 ? 0.1808 0.2009 0.1846 -0.0259 0.0166  -0.0017 140 LEU   A O   
1040 C CB  . LEU   A 134 ? 0.1729 0.1954 0.1831 -0.0155 0.0066  0.0104  140 LEU   A CB  
1041 C CG  . LEU   A 134 ? 0.1921 0.2161 0.2064 -0.0103 0.0026  0.0166  140 LEU   A CG  
1042 C CD1 . LEU   A 134 ? 0.1976 0.2137 0.2170 -0.0032 0.0023  0.0140  140 LEU   A CD1 
1043 C CD2 . LEU   A 134 ? 0.2156 0.2432 0.2322 -0.0113 0.0005  0.0231  140 LEU   A CD2 
1044 N N   . LEU   A 135 ? 0.1751 0.2085 0.1680 -0.0388 0.0157  0.0032  141 LEU   A N   
1045 C CA  . LEU   A 135 ? 0.1888 0.2196 0.1783 -0.0451 0.0228  -0.0049 141 LEU   A CA  
1046 C C   . LEU   A 135 ? 0.1872 0.2111 0.1830 -0.0417 0.0262  -0.0089 141 LEU   A C   
1047 O O   . LEU   A 135 ? 0.2068 0.2252 0.2052 -0.0424 0.0325  -0.0160 141 LEU   A O   
1048 C CB  . LEU   A 135 ? 0.2079 0.2478 0.1870 -0.0575 0.0247  -0.0049 141 LEU   A CB  
1049 C CG  . LEU   A 135 ? 0.2228 0.2728 0.1953 -0.0624 0.0204  0.0007  141 LEU   A CG  
1050 C CD1 . LEU   A 135 ? 0.2409 0.3004 0.2016 -0.0770 0.0233  -0.0008 141 LEU   A CD1 
1051 C CD2 . LEU   A 135 ? 0.2431 0.2899 0.2164 -0.0593 0.0210  -0.0021 141 LEU   A CD2 
1052 N N   . TRP   A 136 ? 0.1740 0.1980 0.1738 -0.0379 0.0223  -0.0043 142 TRP   A N   
1053 C CA  . TRP   A 136 ? 0.1832 0.2021 0.1895 -0.0349 0.0248  -0.0073 142 TRP   A CA  
1054 C C   . TRP   A 136 ? 0.1911 0.2029 0.2059 -0.0271 0.0257  -0.0104 142 TRP   A C   
1055 O O   . TRP   A 136 ? 0.2017 0.2103 0.2229 -0.0254 0.0287  -0.0134 142 TRP   A O   
1056 C CB  . TRP   A 136 ? 0.1864 0.2069 0.1944 -0.0333 0.0204  -0.0013 142 TRP   A CB  
1057 C CG  . TRP   A 136 ? 0.1763 0.1960 0.1874 -0.0266 0.0145  0.0047  142 TRP   A CG  
1058 C CD1 . TRP   A 136 ? 0.1930 0.2181 0.2015 -0.0275 0.0104  0.0116  142 TRP   A CD1 
1059 C CD2 . TRP   A 136 ? 0.1852 0.1987 0.2032 -0.0184 0.0125  0.0043  142 TRP   A CD2 
1060 N NE1 . TRP   A 136 ? 0.2069 0.2283 0.2209 -0.0198 0.0070  0.0147  142 TRP   A NE1 
1061 C CE2 . TRP   A 136 ? 0.1929 0.2072 0.2118 -0.0149 0.0082  0.0100  142 TRP   A CE2 
1062 C CE3 . TRP   A 136 ? 0.1922 0.2005 0.2162 -0.0144 0.0140  0.0002  142 TRP   A CE3 
1063 C CZ2 . TRP   A 136 ? 0.2031 0.2122 0.2270 -0.0082 0.0062  0.0101  142 TRP   A CZ2 
1064 C CZ3 . TRP   A 136 ? 0.2177 0.2223 0.2461 -0.0083 0.0109  0.0013  142 TRP   A CZ3 
1065 C CH2 . TRP   A 136 ? 0.2105 0.2150 0.2381 -0.0056 0.0074  0.0056  142 TRP   A CH2 
1066 N N   . LEU   A 137 ? 0.1815 0.1917 0.1970 -0.0225 0.0228  -0.0089 143 LEU   A N   
1067 C CA  . LEU   A 137 ? 0.1945 0.1990 0.2175 -0.0161 0.0234  -0.0109 143 LEU   A CA  
1068 C C   . LEU   A 137 ? 0.2202 0.2215 0.2469 -0.0183 0.0306  -0.0169 143 LEU   A C   
1069 O O   . LEU   A 137 ? 0.2367 0.2343 0.2725 -0.0133 0.0317  -0.0177 143 LEU   A O   
1070 C CB  . LEU   A 137 ? 0.1840 0.1879 0.2057 -0.0123 0.0198  -0.0087 143 LEU   A CB  
1071 C CG  . LEU   A 137 ? 0.1854 0.1906 0.2071 -0.0082 0.0140  -0.0037 143 LEU   A CG  
1072 C CD1 . LEU   A 137 ? 0.2137 0.2192 0.2334 -0.0059 0.0117  -0.0022 143 LEU   A CD1 
1073 C CD2 . LEU   A 137 ? 0.1985 0.2001 0.2269 -0.0032 0.0122  -0.0034 143 LEU   A CD2 
1074 N N   . ASP   A 138 ? 0.2568 0.2598 0.2771 -0.0261 0.0358  -0.0207 144 ASP   A N   
1075 C CA  . ASP   A 138 ? 0.2859 0.2846 0.3097 -0.0291 0.0445  -0.0275 144 ASP   A CA  
1076 C C   . ASP   A 138 ? 0.3390 0.3370 0.3679 -0.0315 0.0502  -0.0313 144 ASP   A C   
1077 O O   . ASP   A 138 ? 0.3613 0.3553 0.3948 -0.0340 0.0589  -0.0374 144 ASP   A O   
1078 C CB  . ASP   A 138 ? 0.2996 0.3003 0.3130 -0.0382 0.0488  -0.0314 144 ASP   A CB  
1079 C CG  . ASP   A 138 ? 0.3388 0.3409 0.3471 -0.0373 0.0446  -0.0286 144 ASP   A CG  
1080 O OD1 . ASP   A 138 ? 0.3573 0.3567 0.3712 -0.0292 0.0400  -0.0250 144 ASP   A OD1 
1081 O OD2 . ASP   A 138 ? 0.4200 0.4266 0.4183 -0.0455 0.0459  -0.0300 144 ASP   A OD2 
1082 N N   . GLU   A 139 ? 0.3554 0.3569 0.3843 -0.0310 0.0464  -0.0280 145 GLU   A N   
1083 C CA  . GLU   A 139 ? 0.3983 0.4001 0.4314 -0.0341 0.0520  -0.0317 145 GLU   A CA  
1084 C C   . GLU   A 139 ? 0.4272 0.4296 0.4682 -0.0282 0.0475  -0.0277 145 GLU   A C   
1085 O O   . GLU   A 139 ? 0.4203 0.4227 0.4623 -0.0224 0.0402  -0.0225 145 GLU   A O   
1086 C CB  . GLU   A 139 ? 0.4445 0.4516 0.4653 -0.0446 0.0540  -0.0332 145 GLU   A CB  
1087 C CG  . GLU   A 139 ? 0.5426 0.5552 0.5565 -0.0446 0.0451  -0.0255 145 GLU   A CG  
1088 C CD  . GLU   A 139 ? 0.6445 0.6644 0.6455 -0.0547 0.0446  -0.0239 145 GLU   A CD  
1089 O OE1 . GLU   A 139 ? 0.6414 0.6661 0.6392 -0.0553 0.0387  -0.0171 145 GLU   A OE1 
1090 O OE2 . GLU   A 139 ? 0.6889 0.7101 0.6832 -0.0625 0.0501  -0.0291 145 GLU   A OE2 
1091 N N   . GLU   A 140 ? 0.4621 0.4650 0.5088 -0.0303 0.0525  -0.0308 146 GLU   A N   
1092 C CA  . GLU   A 140 ? 0.5024 0.5068 0.5569 -0.0266 0.0499  -0.0282 146 GLU   A CA  
1093 C C   . GLU   A 140 ? 0.5268 0.5293 0.5951 -0.0185 0.0487  -0.0266 146 GLU   A C   
1094 O O   . GLU   A 140 ? 0.5395 0.5427 0.6192 -0.0172 0.0530  -0.0283 146 GLU   A O   
1095 C CB  . GLU   A 140 ? 0.5482 0.5553 0.5952 -0.0268 0.0420  -0.0225 146 GLU   A CB  
1096 C CG  . GLU   A 140 ? 0.6297 0.6372 0.6841 -0.0220 0.0376  -0.0193 146 GLU   A CG  
1097 C CD  . GLU   A 140 ? 0.7419 0.7519 0.7922 -0.0266 0.0368  -0.0178 146 GLU   A CD  
1098 O OE1 . GLU   A 140 ? 0.7833 0.7947 0.8239 -0.0302 0.0341  -0.0147 146 GLU   A OE1 
1099 O OE2 . GLU   A 140 ? 0.7535 0.7648 0.8112 -0.0265 0.0389  -0.0190 146 GLU   A OE2 
1100 N N   . SER   B 1   ? 0.2266 0.2363 0.2465 0.0034  -0.0115 0.0353  7   SER   C N   
1101 C CA  . SER   B 1   ? 0.2180 0.2304 0.2463 0.0019  -0.0125 0.0354  7   SER   C CA  
1102 C C   . SER   B 1   ? 0.2093 0.2202 0.2371 0.0009  -0.0122 0.0323  7   SER   C C   
1103 O O   . SER   B 1   ? 0.2316 0.2392 0.2522 0.0010  -0.0122 0.0302  7   SER   C O   
1104 C CB  . SER   B 1   ? 0.2606 0.2744 0.2898 0.0008  -0.0169 0.0376  7   SER   C CB  
1105 O OG  . SER   B 1   ? 0.3129 0.3236 0.3341 -0.0003 -0.0201 0.0358  7   SER   C OG  
1106 N N   . GLY   B 2   ? 0.2030 0.2161 0.2383 0.0001  -0.0115 0.0321  8   GLY   C N   
1107 C CA  . GLY   B 2   ? 0.1951 0.2067 0.2301 -0.0007 -0.0107 0.0298  8   GLY   C CA  
1108 C C   . GLY   B 2   ? 0.1759 0.1895 0.2180 -0.0004 -0.0079 0.0296  8   GLY   C C   
1109 O O   . GLY   B 2   ? 0.1860 0.2013 0.2319 0.0008  -0.0059 0.0299  8   GLY   C O   
1110 N N   . ALA   B 3   ? 0.1665 0.1795 0.2100 -0.0014 -0.0075 0.0288  9   ALA   C N   
1111 C CA  . ALA   B 3   ? 0.1600 0.1742 0.2086 -0.0008 -0.0044 0.0283  9   ALA   C CA  
1112 C C   . ALA   B 3   ? 0.1539 0.1653 0.1987 -0.0009 -0.0030 0.0266  9   ALA   C C   
1113 O O   . ALA   B 3   ? 0.1784 0.1871 0.2183 -0.0019 -0.0046 0.0261  9   ALA   C O   
1114 C CB  . ALA   B 3   ? 0.1860 0.2036 0.2436 -0.0017 -0.0046 0.0307  9   ALA   C CB  
1115 N N   . ILE   B 4   ? 0.1519 0.1633 0.1982 0.0002  0.0002  0.0257  10  ILE   C N   
1116 C CA  . ILE   B 4   ? 0.1572 0.1660 0.2002 0.0004  0.0021  0.0248  10  ILE   C CA  
1117 C C   . ILE   B 4   ? 0.1535 0.1640 0.2035 -0.0004 0.0041  0.0265  10  ILE   C C   
1118 O O   . ILE   B 4   ? 0.1614 0.1746 0.2173 0.0002  0.0056  0.0271  10  ILE   C O   
1119 C CB  . ILE   B 4   ? 0.1529 0.1603 0.1917 0.0026  0.0041  0.0225  10  ILE   C CB  
1120 C CG1 . ILE   B 4   ? 0.1731 0.1800 0.2079 0.0036  0.0024  0.0210  10  ILE   C CG1 
1121 C CG2 . ILE   B 4   ? 0.1793 0.1833 0.2130 0.0031  0.0058  0.0221  10  ILE   C CG2 
1122 C CD1 . ILE   B 4   ? 0.1886 0.1953 0.2217 0.0056  0.0037  0.0186  10  ILE   C CD1 
1123 N N   . TYR   B 5   ? 0.1510 0.1599 0.2010 -0.0017 0.0047  0.0274  11  TYR   C N   
1124 C CA  . TYR   B 5   ? 0.1616 0.1723 0.2191 -0.0025 0.0072  0.0294  11  TYR   C CA  
1125 C C   . TYR   B 5   ? 0.1732 0.1806 0.2263 -0.0014 0.0111  0.0290  11  TYR   C C   
1126 O O   . TYR   B 5   ? 0.1974 0.2016 0.2467 -0.0023 0.0108  0.0292  11  TYR   C O   
1127 C CB  . TYR   B 5   ? 0.1701 0.1822 0.2335 -0.0054 0.0043  0.0313  11  TYR   C CB  
1128 C CG  . TYR   B 5   ? 0.1698 0.1854 0.2374 -0.0061 0.0003  0.0321  11  TYR   C CG  
1129 C CD1 . TYR   B 5   ? 0.1664 0.1864 0.2433 -0.0058 0.0010  0.0340  11  TYR   C CD1 
1130 C CD2 . TYR   B 5   ? 0.1790 0.1931 0.2406 -0.0066 -0.0038 0.0312  11  TYR   C CD2 
1131 C CE1 . TYR   B 5   ? 0.1833 0.2062 0.2633 -0.0061 -0.0026 0.0351  11  TYR   C CE1 
1132 C CE2 . TYR   B 5   ? 0.2045 0.2213 0.2684 -0.0069 -0.0071 0.0323  11  TYR   C CE2 
1133 C CZ  . TYR   B 5   ? 0.2007 0.2218 0.2736 -0.0066 -0.0067 0.0344  11  TYR   C CZ  
1134 O OH  . TYR   B 5   ? 0.2206 0.2442 0.2953 -0.0065 -0.0101 0.0359  11  TYR   C OH  
1135 N N   . VAL   B 6   ? 0.1721 0.1795 0.2247 0.0007  0.0149  0.0283  12  VAL   C N   
1136 C CA  . VAL   B 6   ? 0.1887 0.1927 0.2355 0.0023  0.0189  0.0280  12  VAL   C CA  
1137 C C   . VAL   B 6   ? 0.1849 0.1903 0.2377 0.0030  0.0237  0.0294  12  VAL   C C   
1138 O O   . VAL   B 6   ? 0.1782 0.1861 0.2356 0.0038  0.0246  0.0288  12  VAL   C O   
1139 C CB  . VAL   B 6   ? 0.2097 0.2111 0.2468 0.0048  0.0184  0.0250  12  VAL   C CB  
1140 C CG1 . VAL   B 6   ? 0.2048 0.2086 0.2445 0.0060  0.0181  0.0231  12  VAL   C CG1 
1141 C CG2 . VAL   B 6   ? 0.2305 0.2281 0.2605 0.0068  0.0223  0.0250  12  VAL   C CG2 
1142 N N   . GLY   B 7   ? 0.2000 0.2039 0.2541 0.0025  0.0274  0.0316  13  GLY   C N   
1143 C CA  . GLY   B 7   ? 0.2062 0.2116 0.2668 0.0033  0.0328  0.0333  13  GLY   C CA  
1144 C C   . GLY   B 7   ? 0.1967 0.2077 0.2704 0.0018  0.0315  0.0347  13  GLY   C C   
1145 O O   . GLY   B 7   ? 0.2061 0.2195 0.2854 -0.0009 0.0271  0.0359  13  GLY   C O   
1146 N N   . ASN   B 8   ? 0.1898 0.2025 0.2674 0.0036  0.0346  0.0343  14  ASN   C N   
1147 C CA  . ASN   B 8   ? 0.1878 0.2058 0.2778 0.0027  0.0332  0.0357  14  ASN   C CA  
1148 C C   . ASN   B 8   ? 0.1838 0.2024 0.2715 0.0037  0.0298  0.0334  14  ASN   C C   
1149 O O   . ASN   B 8   ? 0.1890 0.2104 0.2844 0.0045  0.0308  0.0338  14  ASN   C O   
1150 C CB  . ASN   B 8   ? 0.2075 0.2276 0.3068 0.0038  0.0393  0.0377  14  ASN   C CB  
1151 C CG  . ASN   B 8   ? 0.2901 0.3114 0.3967 0.0019  0.0417  0.0411  14  ASN   C CG  
1152 O OD1 . ASN   B 8   ? 0.3198 0.3457 0.4384 -0.0005 0.0391  0.0436  14  ASN   C OD1 
1153 N ND2 . ASN   B 8   ? 0.3137 0.3308 0.4131 0.0028  0.0461  0.0413  14  ASN   C ND2 
1154 N N   . TYR   B 9   ? 0.1550 0.1712 0.2336 0.0035  0.0260  0.0313  15  TYR   C N   
1155 C CA  . TYR   B 9   ? 0.1525 0.1693 0.2293 0.0042  0.0229  0.0292  15  TYR   C CA  
1156 C C   . TYR   B 9   ? 0.1538 0.1716 0.2296 0.0023  0.0173  0.0299  15  TYR   C C   
1157 O O   . TYR   B 9   ? 0.1718 0.1878 0.2429 0.0010  0.0155  0.0301  15  TYR   C O   
1158 C CB  . TYR   B 9   ? 0.1677 0.1804 0.2337 0.0063  0.0239  0.0256  15  TYR   C CB  
1159 C CG  . TYR   B 9   ? 0.1831 0.1937 0.2473 0.0087  0.0292  0.0242  15  TYR   C CG  
1160 C CD1 . TYR   B 9   ? 0.2094 0.2216 0.2806 0.0098  0.0318  0.0239  15  TYR   C CD1 
1161 C CD2 . TYR   B 9   ? 0.2023 0.2089 0.2569 0.0101  0.0317  0.0231  15  TYR   C CD2 
1162 C CE1 . TYR   B 9   ? 0.2443 0.2540 0.3130 0.0122  0.0371  0.0223  15  TYR   C CE1 
1163 C CE2 . TYR   B 9   ? 0.2383 0.2425 0.2895 0.0126  0.0367  0.0216  15  TYR   C CE2 
1164 C CZ  . TYR   B 9   ? 0.2717 0.2773 0.3296 0.0136  0.0393  0.0209  15  TYR   C CZ  
1165 O OH  . TYR   B 9   ? 0.3438 0.3463 0.3977 0.0163  0.0445  0.0191  15  TYR   C OH  
1166 N N   . ARG   B 10  ? 0.1425 0.1624 0.2217 0.0023  0.0148  0.0300  16  ARG   C N   
1167 C CA  . ARG   B 10  ? 0.1400 0.1605 0.2168 0.0011  0.0100  0.0304  16  ARG   C CA  
1168 C C   . ARG   B 10  ? 0.1437 0.1630 0.2166 0.0027  0.0098  0.0282  16  ARG   C C   
1169 O O   . ARG   B 10  ? 0.1465 0.1670 0.2244 0.0039  0.0115  0.0279  16  ARG   C O   
1170 C CB  . ARG   B 10  ? 0.1455 0.1701 0.2314 -0.0001 0.0073  0.0335  16  ARG   C CB  
1171 C CG  . ARG   B 10  ? 0.1581 0.1833 0.2414 -0.0006 0.0028  0.0342  16  ARG   C CG  
1172 C CD  . ARG   B 10  ? 0.1506 0.1796 0.2418 -0.0017 -0.0003 0.0375  16  ARG   C CD  
1173 N NE  . ARG   B 10  ? 0.1706 0.2006 0.2619 -0.0009 -0.0025 0.0388  16  ARG   C NE  
1174 C CZ  . ARG   B 10  ? 0.1946 0.2239 0.2802 -0.0014 -0.0064 0.0393  16  ARG   C CZ  
1175 N NH1 . ARG   B 10  ? 0.2129 0.2399 0.2912 -0.0028 -0.0087 0.0380  16  ARG   C NH1 
1176 N NH2 . ARG   B 10  ? 0.1973 0.2275 0.2833 -0.0004 -0.0074 0.0410  16  ARG   C NH2 
1177 N N   . VAL   B 11  ? 0.1365 0.1536 0.2014 0.0027  0.0079  0.0264  17  VAL   C N   
1178 C CA  . VAL   B 11  ? 0.1310 0.1472 0.1929 0.0040  0.0076  0.0243  17  VAL   C CA  
1179 C C   . VAL   B 11  ? 0.1401 0.1573 0.2016 0.0032  0.0046  0.0257  17  VAL   C C   
1180 O O   . VAL   B 11  ? 0.1516 0.1677 0.2082 0.0023  0.0024  0.0261  17  VAL   C O   
1181 C CB  . VAL   B 11  ? 0.1450 0.1580 0.1983 0.0050  0.0080  0.0214  17  VAL   C CB  
1182 C CG1 . VAL   B 11  ? 0.1709 0.1838 0.2236 0.0062  0.0077  0.0191  17  VAL   C CG1 
1183 C CG2 . VAL   B 11  ? 0.1661 0.1774 0.2173 0.0058  0.0110  0.0205  17  VAL   C CG2 
1184 N N   . VAL   B 12  ? 0.1306 0.1493 0.1968 0.0038  0.0046  0.0265  18  VAL   C N   
1185 C CA  A VAL   B 12  ? 0.1250 0.1445 0.1904 0.0035  0.0023  0.0283  18  VAL   C CA  
1186 C CA  B VAL   B 12  ? 0.1505 0.1700 0.2160 0.0034  0.0023  0.0284  18  VAL   C CA  
1187 C C   . VAL   B 12  ? 0.1340 0.1533 0.2007 0.0045  0.0034  0.0273  18  VAL   C C   
1188 O O   . VAL   B 12  ? 0.1441 0.1630 0.2139 0.0053  0.0055  0.0252  18  VAL   C O   
1189 C CB  A VAL   B 12  ? 0.1220 0.1442 0.1937 0.0029  0.0009  0.0319  18  VAL   C CB  
1190 C CB  B VAL   B 12  ? 0.1994 0.2217 0.2718 0.0028  0.0011  0.0319  18  VAL   C CB  
1191 C CG1 A VAL   B 12  ? 0.1345 0.1571 0.2050 0.0013  -0.0014 0.0331  18  VAL   C CG1 
1192 C CG1 B VAL   B 12  ? 0.2123 0.2352 0.2832 0.0027  -0.0014 0.0344  18  VAL   C CG1 
1193 C CG2 A VAL   B 12  ? 0.0802 0.1041 0.1610 0.0038  0.0034  0.0327  18  VAL   C CG2 
1194 C CG2 B VAL   B 12  ? 0.2332 0.2563 0.3067 0.0015  0.0001  0.0328  18  VAL   C CG2 
1195 N N   . ASN   B 13  ? 0.1249 0.1442 0.1894 0.0045  0.0022  0.0287  19  ASN   C N   
1196 C CA  . ASN   B 13  ? 0.1200 0.1394 0.1877 0.0054  0.0036  0.0286  19  ASN   C CA  
1197 C C   . ASN   B 13  ? 0.1308 0.1518 0.2073 0.0057  0.0048  0.0307  19  ASN   C C   
1198 O O   . ASN   B 13  ? 0.1324 0.1548 0.2110 0.0054  0.0035  0.0339  19  ASN   C O   
1199 C CB  . ASN   B 13  ? 0.1292 0.1483 0.1931 0.0055  0.0027  0.0307  19  ASN   C CB  
1200 C CG  . ASN   B 13  ? 0.1324 0.1498 0.1883 0.0055  0.0019  0.0288  19  ASN   C CG  
1201 O OD1 . ASN   B 13  ? 0.1487 0.1651 0.1988 0.0049  0.0000  0.0292  19  ASN   C OD1 
1202 N ND2 . ASN   B 13  ? 0.1448 0.1618 0.2009 0.0062  0.0032  0.0266  19  ASN   C ND2 
1203 N N   . ARG   B 14  ? 0.1266 0.1471 0.2084 0.0063  0.0069  0.0288  20  ARG   C N   
1204 C CA  . ARG   B 14  ? 0.1210 0.1423 0.2115 0.0068  0.0084  0.0306  20  ARG   C CA  
1205 C C   . ARG   B 14  ? 0.1425 0.1649 0.2354 0.0070  0.0077  0.0353  20  ARG   C C   
1206 O O   . ARG   B 14  ? 0.1392 0.1630 0.2373 0.0073  0.0075  0.0384  20  ARG   C O   
1207 C CB  . ARG   B 14  ? 0.1217 0.1416 0.2168 0.0073  0.0106  0.0273  20  ARG   C CB  
1208 C CG  . ARG   B 14  ? 0.1357 0.1555 0.2400 0.0080  0.0126  0.0284  20  ARG   C CG  
1209 C CD  . ARG   B 14  ? 0.1384 0.1561 0.2470 0.0082  0.0144  0.0246  20  ARG   C CD  
1210 N NE  . ARG   B 14  ? 0.1410 0.1576 0.2580 0.0091  0.0168  0.0245  20  ARG   C NE  
1211 C CZ  . ARG   B 14  ? 0.1322 0.1488 0.2571 0.0094  0.0180  0.0277  20  ARG   C CZ  
1212 N NH1 . ARG   B 14  ? 0.1524 0.1702 0.2771 0.0091  0.0170  0.0320  20  ARG   C NH1 
1213 N NH2 . ARG   B 14  ? 0.1486 0.1635 0.2812 0.0103  0.0204  0.0269  20  ARG   C NH2 
1214 N N   . HIS   B 15  ? 0.1374 0.1593 0.2262 0.0069  0.0073  0.0363  21  HIS   C N   
1215 C CA  . HIS   B 15  ? 0.1436 0.1659 0.2333 0.0075  0.0070  0.0411  21  HIS   C CA  
1216 C C   . HIS   B 15  ? 0.1575 0.1810 0.2424 0.0072  0.0038  0.0441  21  HIS   C C   
1217 O O   . HIS   B 15  ? 0.1760 0.2000 0.2614 0.0079  0.0031  0.0483  21  HIS   C O   
1218 C CB  . HIS   B 15  ? 0.1421 0.1634 0.2293 0.0078  0.0084  0.0416  21  HIS   C CB  
1219 C CG  . HIS   B 15  ? 0.1417 0.1622 0.2189 0.0075  0.0070  0.0406  21  HIS   C CG  
1220 N ND1 . HIS   B 15  ? 0.1594 0.1794 0.2335 0.0071  0.0070  0.0362  21  HIS   C ND1 
1221 C CD2 . HIS   B 15  ? 0.1555 0.1755 0.2255 0.0079  0.0058  0.0434  21  HIS   C CD2 
1222 C CE1 . HIS   B 15  ? 0.1687 0.1877 0.2344 0.0073  0.0060  0.0366  21  HIS   C CE1 
1223 N NE2 . HIS   B 15  ? 0.1674 0.1862 0.2300 0.0077  0.0053  0.0406  21  HIS   C NE2 
1224 N N   . LEU   B 16  ? 0.1464 0.1701 0.2268 0.0063  0.0019  0.0420  22  LEU   C N   
1225 C CA  . LEU   B 16  ? 0.1628 0.1875 0.2396 0.0057  -0.0017 0.0442  22  LEU   C CA  
1226 C C   . LEU   B 16  ? 0.1583 0.1853 0.2420 0.0052  -0.0023 0.0445  22  LEU   C C   
1227 O O   . LEU   B 16  ? 0.1744 0.2026 0.2568 0.0043  -0.0055 0.0458  22  LEU   C O   
1228 C CB  . LEU   B 16  ? 0.1670 0.1899 0.2338 0.0049  -0.0034 0.0420  22  LEU   C CB  
1229 C CG  . LEU   B 16  ? 0.1743 0.1952 0.2343 0.0056  -0.0026 0.0421  22  LEU   C CG  
1230 C CD1 . LEU   B 16  ? 0.1928 0.2115 0.2435 0.0050  -0.0041 0.0396  22  LEU   C CD1 
1231 C CD2 . LEU   B 16  ? 0.1718 0.1928 0.2301 0.0065  -0.0035 0.0465  22  LEU   C CD2 
1232 N N   . ALA   B 17  ? 0.1579 0.1852 0.2489 0.0057  0.0007  0.0430  23  ALA   C N   
1233 C CA  . ALA   B 17  ? 0.1506 0.1798 0.2483 0.0055  0.0011  0.0432  23  ALA   C CA  
1234 C C   . ALA   B 17  ? 0.1561 0.1883 0.2604 0.0059  -0.0011 0.0478  23  ALA   C C   
1235 O O   . ALA   B 17  ? 0.1707 0.2029 0.2770 0.0070  -0.0012 0.0508  23  ALA   C O   
1236 C CB  . ALA   B 17  ? 0.1657 0.1940 0.2690 0.0065  0.0052  0.0405  23  ALA   C CB  
1237 N N   . THR   B 18  ? 0.1635 0.1981 0.2712 0.0051  -0.0028 0.0487  24  THR   C N   
1238 C CA  . THR   B 18  ? 0.1610 0.1991 0.2758 0.0054  -0.0056 0.0531  24  THR   C CA  
1239 C C   . THR   B 18  ? 0.1574 0.1974 0.2844 0.0068  -0.0023 0.0541  24  THR   C C   
1240 O O   . THR   B 18  ? 0.1634 0.2017 0.2923 0.0073  0.0022  0.0510  24  THR   C O   
1241 C CB  . THR   B 18  ? 0.1728 0.2130 0.2867 0.0035  -0.0097 0.0534  24  THR   C CB  
1242 O OG1 . THR   B 18  ? 0.1763 0.2170 0.2946 0.0029  -0.0068 0.0511  24  THR   C OG1 
1243 C CG2 . THR   B 18  ? 0.1866 0.2243 0.2883 0.0022  -0.0130 0.0518  24  THR   C CG2 
1244 N N   . HIS   B 19  ? 0.1640 0.2075 0.2994 0.0076  -0.0045 0.0586  25  HIS   C N   
1245 C CA  . HIS   B 19  ? 0.1740 0.2196 0.3220 0.0091  -0.0014 0.0599  25  HIS   C CA  
1246 C C   . HIS   B 19  ? 0.1510 0.1977 0.3021 0.0081  0.0009  0.0573  25  HIS   C C   
1247 O O   . HIS   B 19  ? 0.1645 0.2100 0.3203 0.0093  0.0061  0.0554  25  HIS   C O   
1248 C CB  . HIS   B 19  ? 0.1851 0.2351 0.3420 0.0100  -0.0051 0.0655  25  HIS   C CB  
1249 C CG  . HIS   B 19  ? 0.2064 0.2594 0.3775 0.0114  -0.0021 0.0670  25  HIS   C CG  
1250 N ND1 . HIS   B 19  ? 0.2391 0.2902 0.4166 0.0137  0.0028  0.0671  25  HIS   C ND1 
1251 C CD2 . HIS   B 19  ? 0.2242 0.2814 0.4039 0.0108  -0.0026 0.0679  25  HIS   C CD2 
1252 C CE1 . HIS   B 19  ? 0.2327 0.2871 0.4225 0.0147  0.0048  0.0685  25  HIS   C CE1 
1253 N NE2 . HIS   B 19  ? 0.2249 0.2833 0.4167 0.0131  0.0019  0.0691  25  HIS   C NE2 
1254 N N   . ASN   B 20  ? 0.1577 0.2060 0.3059 0.0060  -0.0024 0.0571  26  ASN   C N   
1255 C CA  . ASN   B 20  ? 0.1707 0.2198 0.3220 0.0051  0.0004  0.0551  26  ASN   C CA  
1256 C C   . ASN   B 20  ? 0.1548 0.1992 0.2986 0.0054  0.0054  0.0504  26  ASN   C C   
1257 O O   . ASN   B 20  ? 0.1454 0.1894 0.2931 0.0062  0.0101  0.0489  26  ASN   C O   
1258 C CB  . ASN   B 20  ? 0.1866 0.2375 0.3360 0.0025  -0.0040 0.0555  26  ASN   C CB  
1259 C CG  . ASN   B 20  ? 0.2685 0.3206 0.4235 0.0016  -0.0006 0.0545  26  ASN   C CG  
1260 O OD1 . ASN   B 20  ? 0.3029 0.3588 0.4704 0.0023  0.0012  0.0568  26  ASN   C OD1 
1261 N ND2 . ASN   B 20  ? 0.2937 0.3422 0.4400 0.0004  0.0010  0.0512  26  ASN   C ND2 
1262 N N   . ASP   B 21  ? 0.1445 0.1853 0.2772 0.0051  0.0043  0.0481  27  ASP   C N   
1263 C CA  . ASP   B 21  ? 0.1465 0.1832 0.2724 0.0056  0.0081  0.0437  27  ASP   C CA  
1264 C C   . ASP   B 21  ? 0.1428 0.1782 0.2743 0.0077  0.0128  0.0425  27  ASP   C C   
1265 O O   . ASP   B 21  ? 0.1624 0.1960 0.2933 0.0085  0.0169  0.0397  27  ASP   C O   
1266 C CB  . ASP   B 21  ? 0.1455 0.1792 0.2607 0.0051  0.0061  0.0419  27  ASP   C CB  
1267 C CG  . ASP   B 21  ? 0.1562 0.1894 0.2633 0.0033  0.0026  0.0414  27  ASP   C CG  
1268 O OD1 . ASP   B 21  ? 0.1753 0.2087 0.2823 0.0023  0.0032  0.0406  27  ASP   C OD1 
1269 O OD2 . ASP   B 21  ? 0.1544 0.1869 0.2557 0.0029  -0.0004 0.0421  27  ASP   C OD2 
1270 N N   . TRP   B 22  ? 0.1482 0.1842 0.2848 0.0089  0.0123  0.0447  28  TRP   C N   
1271 C CA  . TRP   B 22  ? 0.1539 0.1882 0.2967 0.0108  0.0165  0.0436  28  TRP   C CA  
1272 C C   . TRP   B 22  ? 0.1419 0.1782 0.2947 0.0121  0.0200  0.0446  28  TRP   C C   
1273 O O   . TRP   B 22  ? 0.1516 0.1853 0.3061 0.0136  0.0248  0.0416  28  TRP   C O   
1274 C CB  . TRP   B 22  ? 0.1544 0.1886 0.3010 0.0117  0.0153  0.0464  28  TRP   C CB  
1275 C CG  . TRP   B 22  ? 0.1514 0.1825 0.2900 0.0111  0.0145  0.0442  28  TRP   C CG  
1276 C CD1 . TRP   B 22  ? 0.1612 0.1925 0.2933 0.0101  0.0110  0.0459  28  TRP   C CD1 
1277 C CD2 . TRP   B 22  ? 0.1397 0.1669 0.2764 0.0116  0.0175  0.0397  28  TRP   C CD2 
1278 N NE1 . TRP   B 22  ? 0.1624 0.1907 0.2899 0.0100  0.0120  0.0433  28  TRP   C NE1 
1279 C CE2 . TRP   B 22  ? 0.1635 0.1893 0.2942 0.0108  0.0156  0.0395  28  TRP   C CE2 
1280 C CE3 . TRP   B 22  ? 0.1650 0.1895 0.3050 0.0128  0.0216  0.0361  28  TRP   C CE3 
1281 C CZ2 . TRP   B 22  ? 0.1586 0.1813 0.2879 0.0108  0.0173  0.0358  28  TRP   C CZ2 
1282 C CZ3 . TRP   B 22  ? 0.1734 0.1942 0.3104 0.0128  0.0227  0.0319  28  TRP   C CZ3 
1283 C CH2 . TRP   B 22  ? 0.1720 0.1922 0.3045 0.0117  0.0204  0.0319  28  TRP   C CH2 
1284 N N   . ALA   B 23  ? 0.1389 0.1797 0.2979 0.0114  0.0177  0.0484  29  ALA   C N   
1285 C CA  . ALA   B 23  ? 0.1472 0.1908 0.3172 0.0125  0.0210  0.0500  29  ALA   C CA  
1286 C C   . ALA   B 23  ? 0.1680 0.2104 0.3344 0.0121  0.0248  0.0470  29  ALA   C C   
1287 O O   . ALA   B 23  ? 0.1805 0.2242 0.3549 0.0133  0.0293  0.0476  29  ALA   C O   
1288 C CB  . ALA   B 23  ? 0.1505 0.2001 0.3295 0.0118  0.0166  0.0552  29  ALA   C CB  
1289 N N   . ASN   B 24  ? 0.1653 0.2050 0.3196 0.0105  0.0235  0.0441  30  ASN   C N   
1290 C CA  . ASN   B 24  ? 0.1563 0.1940 0.3053 0.0102  0.0269  0.0416  30  ASN   C CA  
1291 C C   . ASN   B 24  ? 0.1599 0.1923 0.2962 0.0106  0.0280  0.0367  30  ASN   C C   
1292 O O   . ASN   B 24  ? 0.1597 0.1902 0.2872 0.0096  0.0276  0.0350  30  ASN   C O   
1293 C CB  . ASN   B 24  ? 0.1756 0.2160 0.3238 0.0076  0.0234  0.0436  30  ASN   C CB  
1294 C CG  . ASN   B 24  ? 0.1829 0.2289 0.3450 0.0072  0.0225  0.0480  30  ASN   C CG  
1295 O OD1 . ASN   B 24  ? 0.2071 0.2545 0.3767 0.0080  0.0273  0.0487  30  ASN   C OD1 
1296 N ND2 . ASN   B 24  ? 0.1805 0.2298 0.3463 0.0062  0.0166  0.0510  30  ASN   C ND2 
1297 N N   . LEU   B 25  ? 0.1607 0.1906 0.2965 0.0120  0.0289  0.0347  31  LEU   C N   
1298 C CA  . LEU   B 25  ? 0.1559 0.1814 0.2814 0.0122  0.0287  0.0303  31  LEU   C CA  
1299 C C   . LEU   B 25  ? 0.1780 0.1998 0.2964 0.0133  0.0328  0.0263  31  LEU   C C   
1300 O O   . LEU   B 25  ? 0.1897 0.2106 0.3122 0.0151  0.0376  0.0257  31  LEU   C O   
1301 C CB  . LEU   B 25  ? 0.1677 0.1917 0.2974 0.0133  0.0290  0.0294  31  LEU   C CB  
1302 C CG  . LEU   B 25  ? 0.1765 0.1966 0.2978 0.0132  0.0281  0.0250  31  LEU   C CG  
1303 C CD1 . LEU   B 25  ? 0.1820 0.2031 0.2966 0.0113  0.0234  0.0259  31  LEU   C CD1 
1304 C CD2 . LEU   B 25  ? 0.2038 0.2220 0.3308 0.0142  0.0291  0.0240  31  LEU   C CD2 
1305 N N   . VAL   B 26  ? 0.1722 0.1915 0.2795 0.0126  0.0310  0.0237  32  VAL   C N   
1306 C CA  . VAL   B 26  ? 0.1840 0.1991 0.2824 0.0140  0.0341  0.0197  32  VAL   C CA  
1307 C C   . VAL   B 26  ? 0.1934 0.2050 0.2863 0.0147  0.0327  0.0151  32  VAL   C C   
1308 O O   . VAL   B 26  ? 0.2135 0.2216 0.3039 0.0165  0.0357  0.0113  32  VAL   C O   
1309 C CB  . VAL   B 26  ? 0.1877 0.2023 0.2776 0.0129  0.0329  0.0201  32  VAL   C CB  
1310 C CG1 . VAL   B 26  ? 0.2143 0.2242 0.2931 0.0147  0.0354  0.0161  32  VAL   C CG1 
1311 C CG2 . VAL   B 26  ? 0.1791 0.1969 0.2754 0.0120  0.0345  0.0243  32  VAL   C CG2 
1312 N N   . TRP   B 27  ? 0.1681 0.1806 0.2592 0.0133  0.0282  0.0152  33  TRP   C N   
1313 C CA  . TRP   B 27  ? 0.1694 0.1793 0.2567 0.0136  0.0266  0.0111  33  TRP   C CA  
1314 C C   . TRP   B 27  ? 0.1716 0.1837 0.2615 0.0120  0.0227  0.0131  33  TRP   C C   
1315 O O   . TRP   B 27  ? 0.1701 0.1847 0.2593 0.0107  0.0205  0.0164  33  TRP   C O   
1316 C CB  . TRP   B 27  ? 0.1865 0.1935 0.2620 0.0141  0.0260  0.0076  33  TRP   C CB  
1317 C CG  . TRP   B 27  ? 0.1963 0.2015 0.2673 0.0141  0.0229  0.0036  33  TRP   C CG  
1318 C CD1 . TRP   B 27  ? 0.2282 0.2304 0.2985 0.0152  0.0233  -0.0011 33  TRP   C CD1 
1319 C CD2 . TRP   B 27  ? 0.1884 0.1949 0.2562 0.0129  0.0190  0.0040  33  TRP   C CD2 
1320 N NE1 . TRP   B 27  ? 0.2440 0.2459 0.3111 0.0145  0.0194  -0.0037 33  TRP   C NE1 
1321 C CE2 . TRP   B 27  ? 0.2107 0.2153 0.2763 0.0133  0.0171  -0.0005 33  TRP   C CE2 
1322 C CE3 . TRP   B 27  ? 0.1857 0.1946 0.2523 0.0116  0.0168  0.0075  33  TRP   C CE3 
1323 C CZ2 . TRP   B 27  ? 0.2068 0.2124 0.2699 0.0125  0.0134  -0.0011 33  TRP   C CZ2 
1324 C CZ3 . TRP   B 27  ? 0.2047 0.2138 0.2675 0.0111  0.0136  0.0065  33  TRP   C CZ3 
1325 C CH2 . TRP   B 27  ? 0.2056 0.2136 0.2677 0.0115  0.0121  0.0026  33  TRP   C CH2 
1326 N N   . GLU   B 28  ? 0.1567 0.1677 0.2498 0.0120  0.0220  0.0111  34  GLU   C N   
1327 C CA  . GLU   B 28  ? 0.1677 0.1804 0.2629 0.0108  0.0190  0.0130  34  GLU   C CA  
1328 C C   . GLU   B 28  ? 0.1715 0.1821 0.2667 0.0108  0.0181  0.0090  34  GLU   C C   
1329 O O   . GLU   B 28  ? 0.1794 0.1872 0.2765 0.0117  0.0199  0.0052  34  GLU   C O   
1330 C CB  . GLU   B 28  ? 0.1711 0.1863 0.2753 0.0105  0.0193  0.0178  34  GLU   C CB  
1331 C CG  . GLU   B 28  ? 0.1801 0.1940 0.2930 0.0117  0.0223  0.0175  34  GLU   C CG  
1332 C CD  . GLU   B 28  ? 0.2025 0.2143 0.3200 0.0116  0.0224  0.0154  34  GLU   C CD  
1333 O OE1 . GLU   B 28  ? 0.2362 0.2454 0.3586 0.0127  0.0250  0.0130  34  GLU   C OE1 
1334 O OE2 . GLU   B 28  ? 0.1867 0.1992 0.3035 0.0106  0.0203  0.0161  34  GLU   C OE2 
1335 N N   . ASP   B 29  ? 0.1523 0.1641 0.2459 0.0098  0.0155  0.0096  35  ASP   C N   
1336 C CA  . ASP   B 29  ? 0.1576 0.1681 0.2530 0.0095  0.0144  0.0061  35  ASP   C CA  
1337 C C   . ASP   B 29  ? 0.1553 0.1679 0.2543 0.0085  0.0132  0.0094  35  ASP   C C   
1338 O O   . ASP   B 29  ? 0.1536 0.1677 0.2473 0.0081  0.0115  0.0108  35  ASP   C O   
1339 C CB  . ASP   B 29  ? 0.1695 0.1786 0.2563 0.0100  0.0126  0.0016  35  ASP   C CB  
1340 C CG  . ASP   B 29  ? 0.2212 0.2294 0.3102 0.0096  0.0107  -0.0026 35  ASP   C CG  
1341 O OD1 . ASP   B 29  ? 0.2189 0.2286 0.3145 0.0086  0.0101  -0.0010 35  ASP   C OD1 
1342 O OD2 . ASP   B 29  ? 0.2595 0.2656 0.3431 0.0104  0.0095  -0.0072 35  ASP   C OD2 
1343 N N   . SER   B 30  ? 0.1434 0.1559 0.2514 0.0082  0.0145  0.0108  36  SER   C N   
1344 C CA  A SER   B 30  ? 0.1456 0.1597 0.2571 0.0074  0.0142  0.0144  36  SER   C CA  
1345 C CA  B SER   B 30  ? 0.1505 0.1647 0.2617 0.0074  0.0141  0.0145  36  SER   C CA  
1346 C C   . SER   B 30  ? 0.1540 0.1686 0.2636 0.0068  0.0124  0.0119  36  SER   C C   
1347 O O   . SER   B 30  ? 0.1468 0.1632 0.2542 0.0065  0.0119  0.0148  36  SER   C O   
1348 C CB  A SER   B 30  ? 0.1583 0.1715 0.2803 0.0074  0.0163  0.0162  36  SER   C CB  
1349 C CB  B SER   B 30  ? 0.1809 0.1945 0.3022 0.0074  0.0162  0.0171  36  SER   C CB  
1350 O OG  A SER   B 30  ? 0.1597 0.1739 0.2855 0.0067  0.0166  0.0192  36  SER   C OG  
1351 O OG  B SER   B 30  ? 0.2072 0.2183 0.3341 0.0073  0.0170  0.0125  36  SER   C OG  
1352 N N   . SER   B 31  ? 0.1522 0.1653 0.2624 0.0068  0.0114  0.0065  37  SER   C N   
1353 C CA  . SER   B 31  ? 0.1639 0.1782 0.2738 0.0062  0.0094  0.0041  37  SER   C CA  
1354 C C   . SER   B 31  ? 0.1535 0.1691 0.2537 0.0067  0.0076  0.0047  37  SER   C C   
1355 O O   . SER   B 31  ? 0.1630 0.1803 0.2635 0.0065  0.0064  0.0047  37  SER   C O   
1356 C CB  . SER   B 31  ? 0.2023 0.2148 0.3143 0.0061  0.0077  -0.0021 37  SER   C CB  
1357 O OG  . SER   B 31  ? 0.2593 0.2704 0.3620 0.0072  0.0062  -0.0055 37  SER   C OG  
1358 N N   . ARG   B 32  ? 0.1465 0.1615 0.2390 0.0074  0.0076  0.0054  38  ARG   C N   
1359 C CA  . ARG   B 32  ? 0.1521 0.1677 0.2357 0.0078  0.0061  0.0062  38  ARG   C CA  
1360 C C   . ARG   B 32  ? 0.1430 0.1597 0.2245 0.0075  0.0069  0.0112  38  ARG   C C   
1361 O O   . ARG   B 32  ? 0.1340 0.1508 0.2085 0.0077  0.0059  0.0120  38  ARG   C O   
1362 C CB  . ARG   B 32  ? 0.1803 0.1941 0.2566 0.0087  0.0058  0.0037  38  ARG   C CB  
1363 C CG  . ARG   B 32  ? 0.1855 0.1977 0.2607 0.0094  0.0043  -0.0017 38  ARG   C CG  
1364 C CD  . ARG   B 32  ? 0.1608 0.1706 0.2274 0.0106  0.0046  -0.0037 38  ARG   C CD  
1365 N NE  . ARG   B 32  ? 0.1543 0.1642 0.2125 0.0112  0.0035  -0.0023 38  ARG   C NE  
1366 C CZ  . ARG   B 32  ? 0.1563 0.1643 0.2059 0.0125  0.0027  -0.0043 38  ARG   C CZ  
1367 N NH1 . ARG   B 32  ? 0.1770 0.1825 0.2241 0.0136  0.0029  -0.0081 38  ARG   C NH1 
1368 N NH2 . ARG   B 32  ? 0.1708 0.1787 0.2138 0.0130  0.0018  -0.0028 38  ARG   C NH2 
1369 N N   . ASP   B 33  ? 0.1233 0.1404 0.2103 0.0072  0.0086  0.0145  39  ASP   C N   
1370 C CA  . ASP   B 33  ? 0.1253 0.1434 0.2101 0.0070  0.0087  0.0191  39  ASP   C CA  
1371 C C   . ASP   B 33  ? 0.1276 0.1452 0.2063 0.0070  0.0079  0.0191  39  ASP   C C   
1372 O O   . ASP   B 33  ? 0.1331 0.1512 0.2070 0.0067  0.0068  0.0214  39  ASP   C O   
1373 C CB  . ASP   B 33  ? 0.1292 0.1480 0.2109 0.0069  0.0082  0.0212  39  ASP   C CB  
1374 C CG  . ASP   B 33  ? 0.1409 0.1601 0.2194 0.0068  0.0079  0.0257  39  ASP   C CG  
1375 O OD1 . ASP   B 33  ? 0.1487 0.1684 0.2318 0.0068  0.0085  0.0285  39  ASP   C OD1 
1376 O OD2 . ASP   B 33  ? 0.1391 0.1580 0.2110 0.0069  0.0069  0.0266  39  ASP   C OD2 
1377 N N   . LEU   B 34  ? 0.1202 0.1369 0.1996 0.0074  0.0087  0.0167  40  LEU   C N   
1378 C CA  . LEU   B 34  ? 0.1337 0.1501 0.2085 0.0074  0.0087  0.0172  40  LEU   C CA  
1379 C C   . LEU   B 34  ? 0.1373 0.1541 0.2179 0.0077  0.0107  0.0185  40  LEU   C C   
1380 O O   . LEU   B 34  ? 0.1385 0.1546 0.2247 0.0083  0.0123  0.0170  40  LEU   C O   
1381 C CB  . LEU   B 34  ? 0.1443 0.1588 0.2126 0.0081  0.0085  0.0134  40  LEU   C CB  
1382 C CG  . LEU   B 34  ? 0.1557 0.1698 0.2174 0.0082  0.0065  0.0124  40  LEU   C CG  
1383 C CD1 . LEU   B 34  ? 0.1669 0.1790 0.2221 0.0093  0.0062  0.0091  40  LEU   C CD1 
1384 C CD2 . LEU   B 34  ? 0.1690 0.1836 0.2270 0.0074  0.0055  0.0156  40  LEU   C CD2 
1385 N N   . LEU   B 35  ? 0.1252 0.1430 0.2049 0.0072  0.0105  0.0210  41  LEU   C N   
1386 C CA  . LEU   B 35  ? 0.1282 0.1468 0.2136 0.0076  0.0126  0.0222  41  LEU   C CA  
1387 C C   . LEU   B 35  ? 0.1325 0.1512 0.2140 0.0072  0.0126  0.0229  41  LEU   C C   
1388 O O   . LEU   B 35  ? 0.1435 0.1626 0.2205 0.0061  0.0103  0.0241  41  LEU   C O   
1389 C CB  . LEU   B 35  ? 0.1290 0.1501 0.2220 0.0073  0.0119  0.0266  41  LEU   C CB  
1390 C CG  . LEU   B 35  ? 0.1474 0.1700 0.2483 0.0079  0.0139  0.0285  41  LEU   C CG  
1391 C CD1 . LEU   B 35  ? 0.1662 0.1899 0.2757 0.0086  0.0142  0.0313  41  LEU   C CD1 
1392 C CD2 . LEU   B 35  ? 0.1431 0.1679 0.2438 0.0069  0.0124  0.0312  41  LEU   C CD2 
1393 N N   . VAL   B 36  ? 0.1371 0.1552 0.2203 0.0080  0.0156  0.0219  42  VAL   C N   
1394 C CA  . VAL   B 36  ? 0.1371 0.1552 0.2183 0.0076  0.0168  0.0228  42  VAL   C CA  
1395 C C   . VAL   B 36  ? 0.1423 0.1628 0.2329 0.0079  0.0191  0.0254  42  VAL   C C   
1396 O O   . VAL   B 36  ? 0.1520 0.1721 0.2476 0.0093  0.0219  0.0244  42  VAL   C O   
1397 C CB  . VAL   B 36  ? 0.1493 0.1641 0.2227 0.0089  0.0190  0.0193  42  VAL   C CB  
1398 C CG1 . VAL   B 36  ? 0.1695 0.1839 0.2411 0.0086  0.0210  0.0209  42  VAL   C CG1 
1399 C CG2 . VAL   B 36  ? 0.1599 0.1728 0.2250 0.0089  0.0163  0.0169  42  VAL   C CG2 
1400 N N   . SER   B 37  ? 0.1323 0.1552 0.2260 0.0065  0.0179  0.0286  43  SER   C N   
1401 C CA  . SER   B 37  ? 0.1276 0.1536 0.2316 0.0065  0.0197  0.0315  43  SER   C CA  
1402 C C   . SER   B 37  ? 0.1433 0.1693 0.2466 0.0059  0.0218  0.0322  43  SER   C C   
1403 O O   . SER   B 37  ? 0.1593 0.1830 0.2545 0.0051  0.0209  0.0311  43  SER   C O   
1404 C CB  . SER   B 37  ? 0.1429 0.1726 0.2534 0.0054  0.0157  0.0352  43  SER   C CB  
1405 O OG  . SER   B 37  ? 0.1654 0.1955 0.2710 0.0034  0.0115  0.0362  43  SER   C OG  
1406 N N   . SER   B 38  ? 0.1503 0.1786 0.2629 0.0064  0.0250  0.0342  44  SER   C N   
1407 C CA  . SER   B 38  ? 0.1581 0.1867 0.2723 0.0057  0.0279  0.0355  44  SER   C CA  
1408 C C   . SER   B 38  ? 0.1812 0.2137 0.3023 0.0031  0.0240  0.0390  44  SER   C C   
1409 O O   . SER   B 38  ? 0.1993 0.2353 0.3271 0.0024  0.0202  0.0411  44  SER   C O   
1410 C CB  . SER   B 38  ? 0.1945 0.2235 0.3154 0.0078  0.0343  0.0358  44  SER   C CB  
1411 O OG  . SER   B 38  ? 0.2446 0.2779 0.3782 0.0080  0.0337  0.0385  44  SER   C OG  
1412 N N   . THR   B 39  ? 0.1839 0.2156 0.3032 0.0016  0.0246  0.0396  45  THR   C N   
1413 C CA  . THR   B 39  ? 0.1997 0.2345 0.3252 -0.0013 0.0205  0.0422  45  THR   C CA  
1414 C C   . THR   B 39  ? 0.2265 0.2634 0.3617 -0.0019 0.0248  0.0447  45  THR   C C   
1415 O O   . THR   B 39  ? 0.2190 0.2533 0.3514 -0.0003 0.0310  0.0439  45  THR   C O   
1416 C CB  . THR   B 39  ? 0.2074 0.2387 0.3222 -0.0030 0.0168  0.0407  45  THR   C CB  
1417 O OG1 . THR   B 39  ? 0.2282 0.2555 0.3364 -0.0024 0.0212  0.0395  45  THR   C OG1 
1418 C CG2 . THR   B 39  ? 0.2078 0.2368 0.3127 -0.0023 0.0134  0.0383  45  THR   C CG2 
1419 N N   . THR   B 40  ? 0.2401 0.2816 0.3863 -0.0043 0.0214  0.0475  46  THR   C N   
1420 C CA  . THR   B 40  ? 0.2618 0.3057 0.4189 -0.0054 0.0252  0.0501  46  THR   C CA  
1421 C C   . THR   B 40  ? 0.2714 0.3114 0.4220 -0.0074 0.0256  0.0496  46  THR   C C   
1422 O O   . THR   B 40  ? 0.2959 0.3343 0.4475 -0.0068 0.0319  0.0504  46  THR   C O   
1423 C CB  . THR   B 40  ? 0.3069 0.3577 0.4800 -0.0071 0.0212  0.0534  46  THR   C CB  
1424 O OG1 . THR   B 40  ? 0.3607 0.4118 0.5305 -0.0097 0.0130  0.0530  46  THR   C OG1 
1425 C CG2 . THR   B 40  ? 0.2909 0.3452 0.4710 -0.0047 0.0216  0.0545  46  THR   C CG2 
1426 N N   . ALA   B 41  ? 0.2516 0.2898 0.3953 -0.0095 0.0192  0.0482  47  ALA   C N   
1427 C CA  . ALA   B 41  ? 0.2586 0.2925 0.3961 -0.0114 0.0192  0.0476  47  ALA   C CA  
1428 C C   . ALA   B 41  ? 0.2391 0.2667 0.3604 -0.0092 0.0216  0.0447  47  ALA   C C   
1429 O O   . ALA   B 41  ? 0.2358 0.2625 0.3498 -0.0073 0.0203  0.0426  47  ALA   C O   
1430 C CB  . ALA   B 41  ? 0.2806 0.3151 0.4186 -0.0146 0.0114  0.0473  47  ALA   C CB  
1431 N N   . GLN   B 42  ? 0.2426 0.2659 0.3588 -0.0096 0.0249  0.0448  48  GLN   C N   
1432 C CA  . GLN   B 42  ? 0.2595 0.2769 0.3607 -0.0075 0.0266  0.0425  48  GLN   C CA  
1433 C C   . GLN   B 42  ? 0.2526 0.2676 0.3457 -0.0088 0.0203  0.0404  48  GLN   C C   
1434 O O   . GLN   B 42  ? 0.2695 0.2849 0.3668 -0.0118 0.0162  0.0410  48  GLN   C O   
1435 C CB  . GLN   B 42  ? 0.3257 0.3393 0.4245 -0.0072 0.0325  0.0440  48  GLN   C CB  
1436 C CG  . GLN   B 42  ? 0.4204 0.4349 0.5227 -0.0047 0.0399  0.0454  48  GLN   C CG  
1437 C CD  . GLN   B 42  ? 0.5620 0.5721 0.6601 -0.0040 0.0460  0.0472  48  GLN   C CD  
1438 O OE1 . GLN   B 42  ? 0.6121 0.6229 0.7190 -0.0064 0.0478  0.0502  48  GLN   C OE1 
1439 N NE2 . GLN   B 42  ? 0.6020 0.6074 0.6866 -0.0008 0.0492  0.0456  48  GLN   C NE2 
1440 N N   . GLY   B 43  ? 0.2241 0.2363 0.3060 -0.0066 0.0196  0.0377  49  GLY   C N   
1441 C CA  . GLY   B 43  ? 0.2193 0.2287 0.2923 -0.0070 0.0148  0.0356  49  GLY   C CA  
1442 C C   . GLY   B 43  ? 0.2204 0.2241 0.2841 -0.0064 0.0166  0.0350  49  GLY   C C   
1443 O O   . GLY   B 43  ? 0.2569 0.2586 0.3190 -0.0050 0.0217  0.0361  49  GLY   C O   
1444 N N   . CYS   B 44  ? 0.2098 0.2107 0.2671 -0.0070 0.0127  0.0335  50  CYS   C N   
1445 C CA  . CYS   B 44  ? 0.2216 0.2168 0.2712 -0.0066 0.0140  0.0332  50  CYS   C CA  
1446 C C   . CYS   B 44  ? 0.2353 0.2277 0.2739 -0.0041 0.0127  0.0308  50  CYS   C C   
1447 O O   . CYS   B 44  ? 0.2724 0.2600 0.3045 -0.0034 0.0134  0.0308  50  CYS   C O   
1448 C CB  . CYS   B 44  ? 0.2221 0.2154 0.2753 -0.0099 0.0113  0.0339  50  CYS   C CB  
1449 S SG  . CYS   B 44  ? 0.3046 0.3021 0.3732 -0.0131 0.0123  0.0369  50  CYS   C SG  
1450 N N   . ASP   B 45  ? 0.1974 0.1924 0.2343 -0.0027 0.0109  0.0290  51  ASP   C N   
1451 C CA  . ASP   B 45  ? 0.2005 0.1934 0.2286 -0.0005 0.0096  0.0268  51  ASP   C CA  
1452 C C   . ASP   B 45  ? 0.2098 0.2011 0.2327 0.0023  0.0132  0.0265  51  ASP   C C   
1453 O O   . ASP   B 45  ? 0.2301 0.2229 0.2561 0.0029  0.0165  0.0273  51  ASP   C O   
1454 C CB  . ASP   B 45  ? 0.1948 0.1912 0.2242 -0.0001 0.0070  0.0253  51  ASP   C CB  
1455 C CG  . ASP   B 45  ? 0.2447 0.2422 0.2767 -0.0023 0.0031  0.0254  51  ASP   C CG  
1456 O OD1 . ASP   B 45  ? 0.2577 0.2520 0.2869 -0.0035 0.0015  0.0253  51  ASP   C OD1 
1457 O OD2 . ASP   B 45  ? 0.2159 0.2170 0.2520 -0.0025 0.0017  0.0256  51  ASP   C OD2 
1458 N N   . THR   B 46  ? 0.1893 0.1773 0.2040 0.0042  0.0125  0.0253  52  THR   C N   
1459 C CA  . THR   B 46  ? 0.1943 0.1804 0.2022 0.0073  0.0146  0.0246  52  THR   C CA  
1460 C C   . THR   B 46  ? 0.1891 0.1770 0.1942 0.0090  0.0119  0.0217  52  THR   C C   
1461 O O   . THR   B 46  ? 0.1914 0.1795 0.1958 0.0087  0.0090  0.0208  52  THR   C O   
1462 C CB  . THR   B 46  ? 0.2261 0.2071 0.2269 0.0084  0.0153  0.0257  52  THR   C CB  
1463 O OG1 . THR   B 46  ? 0.2577 0.2366 0.2618 0.0066  0.0183  0.0286  52  THR   C OG1 
1464 C CG2 . THR   B 46  ? 0.2536 0.2325 0.2458 0.0120  0.0165  0.0249  52  THR   C CG2 
1465 N N   . ILE   B 47  ? 0.1827 0.1721 0.1869 0.0107  0.0131  0.0202  53  ILE   C N   
1466 C CA  . ILE   B 47  ? 0.1735 0.1646 0.1763 0.0122  0.0105  0.0174  53  ILE   C CA  
1467 C C   . ILE   B 47  ? 0.1787 0.1668 0.1729 0.0148  0.0094  0.0164  53  ILE   C C   
1468 O O   . ILE   B 47  ? 0.1949 0.1801 0.1831 0.0165  0.0115  0.0171  53  ILE   C O   
1469 C CB  . ILE   B 47  ? 0.1838 0.1770 0.1893 0.0129  0.0119  0.0157  53  ILE   C CB  
1470 C CG1 . ILE   B 47  ? 0.1910 0.1870 0.2052 0.0108  0.0135  0.0172  53  ILE   C CG1 
1471 C CG2 . ILE   B 47  ? 0.1978 0.1928 0.2032 0.0140  0.0091  0.0126  53  ILE   C CG2 
1472 C CD1 . ILE   B 47  ? 0.2208 0.2195 0.2405 0.0088  0.0104  0.0177  53  ILE   C CD1 
1473 N N   . ALA   B 48  ? 0.1641 0.1532 0.1578 0.0154  0.0062  0.0149  54  ALA   C N   
1474 C CA  . ALA   B 48  ? 0.1697 0.1568 0.1566 0.0181  0.0045  0.0140  54  ALA   C CA  
1475 C C   . ALA   B 48  ? 0.1742 0.1618 0.1579 0.0201  0.0042  0.0115  54  ALA   C C   
1476 O O   . ALA   B 48  ? 0.1728 0.1633 0.1613 0.0194  0.0039  0.0096  54  ALA   C O   
1477 C CB  . ALA   B 48  ? 0.1731 0.1621 0.1625 0.0182  0.0014  0.0128  54  ALA   C CB  
1478 N N   . ARG   B 49  ? 0.1711 0.1557 0.1464 0.0228  0.0039  0.0116  55  ARG   C N   
1479 C CA  . ARG   B 49  ? 0.1713 0.1557 0.1414 0.0252  0.0027  0.0088  55  ARG   C CA  
1480 C C   . ARG   B 49  ? 0.1923 0.1760 0.1574 0.0277  -0.0011 0.0082  55  ARG   C C   
1481 O O   . ARG   B 49  ? 0.2073 0.1873 0.1648 0.0297  -0.0006 0.0103  55  ARG   C O   
1482 C CB  . ARG   B 49  ? 0.1838 0.1648 0.1474 0.0263  0.0067  0.0099  55  ARG   C CB  
1483 C CG  . ARG   B 49  ? 0.1733 0.1555 0.1437 0.0238  0.0107  0.0111  55  ARG   C CG  
1484 C CD  . ARG   B 49  ? 0.1985 0.1841 0.1755 0.0228  0.0100  0.0080  55  ARG   C CD  
1485 N NE  . ARG   B 49  ? 0.2040 0.1907 0.1877 0.0208  0.0139  0.0098  55  ARG   C NE  
1486 C CZ  . ARG   B 49  ? 0.1975 0.1876 0.1899 0.0191  0.0137  0.0087  55  ARG   C CZ  
1487 N NH1 . ARG   B 49  ? 0.1946 0.1869 0.1899 0.0191  0.0104  0.0057  55  ARG   C NH1 
1488 N NH2 . ARG   B 49  ? 0.1917 0.1831 0.1908 0.0175  0.0169  0.0108  55  ARG   C NH2 
1489 N N   . CYS   B 50  ? 0.1799 0.1673 0.1506 0.0275  -0.0048 0.0057  56  CYS   C N   
1490 C CA  . CYS   B 50  ? 0.1825 0.1704 0.1517 0.0295  -0.0086 0.0054  56  CYS   C CA  
1491 C C   . CYS   B 50  ? 0.1756 0.1683 0.1529 0.0289  -0.0120 0.0023  56  CYS   C C   
1492 O O   . CYS   B 50  ? 0.1826 0.1779 0.1663 0.0269  -0.0112 0.0007  56  CYS   C O   
1493 C CB  . CYS   B 50  ? 0.1855 0.1719 0.1561 0.0288  -0.0073 0.0085  56  CYS   C CB  
1494 S SG  . CYS   B 50  ? 0.1743 0.1641 0.1556 0.0253  -0.0063 0.0086  56  CYS   C SG  
1495 N N   . ASP   B 51  ? 0.1902 0.1845 0.1683 0.0308  -0.0156 0.0019  57  ASP   C N   
1496 C CA  . ASP   B 51  ? 0.1962 0.1954 0.1836 0.0303  -0.0186 -0.0005 57  ASP   C CA  
1497 C C   . ASP   B 51  ? 0.2013 0.2015 0.1932 0.0304  -0.0182 0.0017  57  ASP   C C   
1498 O O   . ASP   B 51  ? 0.2058 0.2096 0.2038 0.0312  -0.0209 0.0005  57  ASP   C O   
1499 C CB  . ASP   B 51  ? 0.2281 0.2289 0.2141 0.0325  -0.0236 -0.0036 57  ASP   C CB  
1500 C CG  . ASP   B 51  ? 0.2718 0.2710 0.2512 0.0358  -0.0264 -0.0023 57  ASP   C CG  
1501 O OD1 . ASP   B 51  ? 0.2670 0.2631 0.2423 0.0365  -0.0240 0.0011  57  ASP   C OD1 
1502 O OD2 . ASP   B 51  ? 0.3447 0.3458 0.3236 0.0378  -0.0314 -0.0048 57  ASP   C OD2 
1503 N N   . CYS   B 52  ? 0.1897 0.1869 0.1794 0.0293  -0.0148 0.0045  58  CYS   C N   
1504 C CA  . CYS   B 52  ? 0.1739 0.1714 0.1673 0.0293  -0.0140 0.0061  58  CYS   C CA  
1505 C C   . CYS   B 52  ? 0.1607 0.1629 0.1639 0.0279  -0.0141 0.0048  58  CYS   C C   
1506 O O   . CYS   B 52  ? 0.1682 0.1725 0.1755 0.0258  -0.0133 0.0037  58  CYS   C O   
1507 C CB  . CYS   B 52  ? 0.1769 0.1704 0.1672 0.0277  -0.0105 0.0086  58  CYS   C CB  
1508 S SG  . CYS   B 52  ? 0.1881 0.1754 0.1685 0.0294  -0.0095 0.0112  58  CYS   C SG  
1509 N N   . GLN   B 53  ? 0.1576 0.1612 0.1645 0.0292  -0.0145 0.0053  59  GLN   C N   
1510 C CA  . GLN   B 53  ? 0.1622 0.1695 0.1780 0.0282  -0.0135 0.0049  59  GLN   C CA  
1511 C C   . GLN   B 53  ? 0.1597 0.1649 0.1746 0.0284  -0.0108 0.0069  59  GLN   C C   
1512 O O   . GLN   B 53  ? 0.1623 0.1700 0.1834 0.0284  -0.0095 0.0070  59  GLN   C O   
1513 C CB  . GLN   B 53  ? 0.1690 0.1812 0.1923 0.0299  -0.0167 0.0032  59  GLN   C CB  
1514 C CG  . GLN   B 53  ? 0.2177 0.2324 0.2437 0.0289  -0.0194 0.0005  59  GLN   C CG  
1515 C CD  . GLN   B 53  ? 0.2316 0.2514 0.2669 0.0299  -0.0227 -0.0015 59  GLN   C CD  
1516 O OE1 . GLN   B 53  ? 0.2549 0.2755 0.2884 0.0316  -0.0271 -0.0033 59  GLN   C OE1 
1517 N NE2 . GLN   B 53  ? 0.2017 0.2251 0.2472 0.0288  -0.0207 -0.0011 59  GLN   C NE2 
1518 N N   . THR   B 54  ? 0.1661 0.1660 0.1733 0.0285  -0.0095 0.0084  60  THR   C N   
1519 C CA  . THR   B 54  ? 0.1785 0.1753 0.1839 0.0282  -0.0069 0.0097  60  THR   C CA  
1520 C C   . THR   B 54  ? 0.1742 0.1671 0.1742 0.0257  -0.0054 0.0107  60  THR   C C   
1521 O O   . THR   B 54  ? 0.1806 0.1717 0.1767 0.0254  -0.0060 0.0110  60  THR   C O   
1522 C CB  . THR   B 54  ? 0.2215 0.2156 0.2245 0.0310  -0.0070 0.0105  60  THR   C CB  
1523 O OG1 . THR   B 54  ? 0.2761 0.2662 0.2725 0.0319  -0.0079 0.0114  60  THR   C OG1 
1524 C CG2 . THR   B 54  ? 0.2127 0.2112 0.2222 0.0337  -0.0088 0.0098  60  THR   C CG2 
1525 N N   . GLY   B 55  ? 0.1608 0.1524 0.1607 0.0241  -0.0035 0.0111  61  GLY   C N   
1526 C CA  . GLY   B 55  ? 0.1685 0.1568 0.1646 0.0216  -0.0026 0.0119  61  GLY   C CA  
1527 C C   . GLY   B 55  ? 0.1597 0.1465 0.1550 0.0205  -0.0012 0.0121  61  GLY   C C   
1528 O O   . GLY   B 55  ? 0.1727 0.1593 0.1686 0.0221  -0.0002 0.0117  61  GLY   C O   
1529 N N   . VAL   B 56  ? 0.1558 0.1413 0.1496 0.0178  -0.0011 0.0126  62  VAL   C N   
1530 C CA  . VAL   B 56  ? 0.1500 0.1334 0.1415 0.0166  -0.0004 0.0127  62  VAL   C CA  
1531 C C   . VAL   B 56  ? 0.1464 0.1330 0.1409 0.0142  -0.0009 0.0134  62  VAL   C C   
1532 O O   . VAL   B 56  ? 0.1619 0.1494 0.1580 0.0128  -0.0016 0.0139  62  VAL   C O   
1533 C CB  . VAL   B 56  ? 0.1657 0.1430 0.1517 0.0157  -0.0008 0.0126  62  VAL   C CB  
1534 C CG1 . VAL   B 56  ? 0.1844 0.1592 0.1671 0.0140  -0.0010 0.0122  62  VAL   C CG1 
1535 C CG2 . VAL   B 56  ? 0.1747 0.1482 0.1579 0.0183  -0.0001 0.0122  62  VAL   C CG2 
1536 N N   . TYR   B 57  ? 0.1506 0.1384 0.1454 0.0141  -0.0001 0.0136  63  TYR   C N   
1537 C CA  . TYR   B 57  ? 0.1363 0.1268 0.1338 0.0120  -0.0007 0.0148  63  TYR   C CA  
1538 C C   . TYR   B 57  ? 0.1492 0.1369 0.1418 0.0109  -0.0013 0.0152  63  TYR   C C   
1539 O O   . TYR   B 57  ? 0.1654 0.1499 0.1530 0.0122  -0.0003 0.0144  63  TYR   C O   
1540 C CB  . TYR   B 57  ? 0.1449 0.1403 0.1488 0.0127  0.0004  0.0153  63  TYR   C CB  
1541 C CG  . TYR   B 57  ? 0.1509 0.1468 0.1543 0.0138  0.0023  0.0160  63  TYR   C CG  
1542 C CD1 . TYR   B 57  ? 0.1663 0.1616 0.1693 0.0161  0.0040  0.0152  63  TYR   C CD1 
1543 C CD2 . TYR   B 57  ? 0.1576 0.1546 0.1613 0.0129  0.0027  0.0177  63  TYR   C CD2 
1544 C CE1 . TYR   B 57  ? 0.1721 0.1679 0.1751 0.0173  0.0065  0.0161  63  TYR   C CE1 
1545 C CE2 . TYR   B 57  ? 0.1705 0.1677 0.1733 0.0141  0.0050  0.0187  63  TYR   C CE2 
1546 C CZ  . TYR   B 57  ? 0.1687 0.1652 0.1711 0.0163  0.0072  0.0179  63  TYR   C CZ  
1547 O OH  . TYR   B 57  ? 0.1927 0.1894 0.1947 0.0179  0.0105  0.0191  63  TYR   C OH  
1548 N N   . TYR   B 58  ? 0.1554 0.1444 0.1495 0.0088  -0.0027 0.0163  64  TYR   C N   
1549 C CA  . TYR   B 58  ? 0.1565 0.1434 0.1458 0.0077  -0.0042 0.0167  64  TYR   C CA  
1550 C C   . TYR   B 58  ? 0.1538 0.1434 0.1440 0.0084  -0.0031 0.0183  64  TYR   C C   
1551 O O   . TYR   B 58  ? 0.1616 0.1554 0.1582 0.0080  -0.0028 0.0198  64  TYR   C O   
1552 C CB  . TYR   B 58  ? 0.1668 0.1536 0.1576 0.0050  -0.0069 0.0173  64  TYR   C CB  
1553 C CG  . TYR   B 58  ? 0.1841 0.1685 0.1694 0.0039  -0.0094 0.0174  64  TYR   C CG  
1554 C CD1 . TYR   B 58  ? 0.1996 0.1785 0.1770 0.0043  -0.0099 0.0154  64  TYR   C CD1 
1555 C CD2 . TYR   B 58  ? 0.1863 0.1737 0.1741 0.0027  -0.0113 0.0193  64  TYR   C CD2 
1556 C CE1 . TYR   B 58  ? 0.2064 0.1826 0.1773 0.0035  -0.0124 0.0150  64  TYR   C CE1 
1557 C CE2 . TYR   B 58  ? 0.1937 0.1789 0.1755 0.0019  -0.0141 0.0193  64  TYR   C CE2 
1558 C CZ  . TYR   B 58  ? 0.2085 0.1880 0.1816 0.0022  -0.0149 0.0169  64  TYR   C CZ  
1559 O OH  . TYR   B 58  ? 0.2571 0.2337 0.2228 0.0016  -0.0180 0.0165  64  TYR   C OH  
1560 N N   . CYS   B 59  ? 0.1580 0.1446 0.1415 0.0096  -0.0023 0.0181  65  CYS   C N   
1561 C CA  . CYS   B 59  ? 0.1650 0.1532 0.1475 0.0106  -0.0007 0.0200  65  CYS   C CA  
1562 C C   . CYS   B 59  ? 0.1822 0.1677 0.1574 0.0095  -0.0035 0.0205  65  CYS   C C   
1563 O O   . CYS   B 59  ? 0.1915 0.1720 0.1577 0.0101  -0.0038 0.0189  65  CYS   C O   
1564 C CB  . CYS   B 59  ? 0.1663 0.1531 0.1462 0.0133  0.0030  0.0194  65  CYS   C CB  
1565 S SG  . CYS   B 59  ? 0.1959 0.1837 0.1739 0.0149  0.0061  0.0223  65  CYS   C SG  
1566 N N   . SER   B 60  ? 0.1865 0.1750 0.1654 0.0081  -0.0056 0.0227  66  SER   C N   
1567 C CA  . SER   B 60  ? 0.1979 0.1845 0.1708 0.0070  -0.0092 0.0233  66  SER   C CA  
1568 C C   . SER   B 60  ? 0.2128 0.1965 0.1760 0.0090  -0.0079 0.0241  66  SER   C C   
1569 O O   . SER   B 60  ? 0.2347 0.2141 0.1888 0.0086  -0.0106 0.0228  66  SER   C O   
1570 C CB  . SER   B 60  ? 0.2292 0.2203 0.2093 0.0055  -0.0116 0.0259  66  SER   C CB  
1571 O OG  . SER   B 60  ? 0.2947 0.2842 0.2689 0.0045  -0.0157 0.0265  66  SER   C OG  
1572 N N   . SER   B 61  ? 0.1935 0.1791 0.1588 0.0111  -0.0035 0.0261  67  SER   C N   
1573 C CA  . SER   B 61  ? 0.2000 0.1827 0.1561 0.0133  -0.0011 0.0274  67  SER   C CA  
1574 C C   . SER   B 61  ? 0.2277 0.2049 0.1747 0.0150  0.0009  0.0245  67  SER   C C   
1575 O O   . SER   B 61  ? 0.2543 0.2282 0.1920 0.0170  0.0032  0.0252  67  SER   C O   
1576 C CB  . SER   B 61  ? 0.2095 0.1959 0.1720 0.0149  0.0035  0.0306  67  SER   C CB  
1577 O OG  . SER   B 61  ? 0.2157 0.2038 0.1851 0.0158  0.0072  0.0294  67  SER   C OG  
1578 N N   . ARG   B 62  ? 0.2172 0.1930 0.1662 0.0143  0.0005  0.0213  68  ARG   C N   
1579 C CA  . ARG   B 62  ? 0.2221 0.1919 0.1626 0.0158  0.0019  0.0183  68  ARG   C CA  
1580 C C   . ARG   B 62  ? 0.2258 0.1914 0.1625 0.0136  -0.0028 0.0151  68  ARG   C C   
1581 O O   . ARG   B 62  ? 0.2491 0.2093 0.1796 0.0145  -0.0019 0.0122  68  ARG   C O   
1582 C CB  . ARG   B 62  ? 0.2234 0.1945 0.1698 0.0177  0.0064  0.0176  68  ARG   C CB  
1583 C CG  . ARG   B 62  ? 0.2695 0.2447 0.2212 0.0197  0.0113  0.0205  68  ARG   C CG  
1584 C CD  . ARG   B 62  ? 0.2814 0.2522 0.2227 0.0224  0.0149  0.0208  68  ARG   C CD  
1585 N NE  . ARG   B 62  ? 0.3005 0.2749 0.2472 0.0244  0.0204  0.0240  68  ARG   C NE  
1586 C CZ  . ARG   B 62  ? 0.3349 0.3115 0.2820 0.0244  0.0213  0.0276  68  ARG   C CZ  
1587 N NH1 . ARG   B 62  ? 0.3485 0.3241 0.2900 0.0229  0.0169  0.0285  68  ARG   C NH1 
1588 N NH2 . ARG   B 62  ? 0.3550 0.3344 0.3075 0.0263  0.0268  0.0305  68  ARG   C NH2 
1589 N N   . ARG   B 63  ? 0.2372 0.2057 0.1796 0.0107  -0.0071 0.0157  69  ARG   C N   
1590 C CA  . ARG   B 63  ? 0.2584 0.2241 0.2008 0.0081  -0.0112 0.0131  69  ARG   C CA  
1591 C C   . ARG   B 63  ? 0.2644 0.2273 0.2082 0.0088  -0.0089 0.0109  69  ARG   C C   
1592 O O   . ARG   B 63  ? 0.2939 0.2508 0.2319 0.0084  -0.0101 0.0080  69  ARG   C O   
1593 C CB  . ARG   B 63  ? 0.2705 0.2304 0.2018 0.0072  -0.0152 0.0111  69  ARG   C CB  
1594 C CG  . ARG   B 63  ? 0.3155 0.2778 0.2446 0.0064  -0.0187 0.0133  69  ARG   C CG  
1595 C CD  . ARG   B 63  ? 0.3736 0.3408 0.3128 0.0034  -0.0227 0.0148  69  ARG   C CD  
1596 N NE  . ARG   B 63  ? 0.4047 0.3727 0.3404 0.0024  -0.0276 0.0161  69  ARG   C NE  
1597 C CZ  . ARG   B 63  ? 0.4270 0.3997 0.3657 0.0032  -0.0276 0.0199  69  ARG   C CZ  
1598 N NH1 . ARG   B 63  ? 0.4063 0.3831 0.3516 0.0048  -0.0227 0.0225  69  ARG   C NH1 
1599 N NH2 . ARG   B 63  ? 0.4238 0.3971 0.3591 0.0024  -0.0328 0.0212  69  ARG   C NH2 
1600 N N   . LYS   B 64  ? 0.2287 0.1957 0.1800 0.0102  -0.0054 0.0121  70  LYS   C N   
1601 C CA  . LYS   B 64  ? 0.2371 0.2018 0.1897 0.0116  -0.0032 0.0105  70  LYS   C CA  
1602 C C   . LYS   B 64  ? 0.2126 0.1824 0.1751 0.0113  -0.0025 0.0117  70  LYS   C C   
1603 O O   . LYS   B 64  ? 0.2106 0.1859 0.1792 0.0113  -0.0019 0.0138  70  LYS   C O   
1604 C CB  . LYS   B 64  ? 0.2912 0.2544 0.2399 0.0150  0.0013  0.0102  70  LYS   C CB  
1605 C CG  . LYS   B 64  ? 0.4391 0.3949 0.3762 0.0161  0.0016  0.0077  70  LYS   C CG  
1606 C CD  . LYS   B 64  ? 0.5400 0.4940 0.4748 0.0198  0.0068  0.0073  70  LYS   C CD  
1607 C CE  . LYS   B 64  ? 0.6124 0.5584 0.5347 0.0211  0.0076  0.0046  70  LYS   C CE  
1608 N NZ  . LYS   B 64  ? 0.6643 0.6093 0.5785 0.0202  0.0055  0.0052  70  LYS   C NZ  
1609 N N   . HIS   B 65  ? 0.2086 0.1760 0.1722 0.0114  -0.0025 0.0104  71  HIS   C N   
1610 C CA  . HIS   B 65  ? 0.2022 0.1734 0.1733 0.0119  -0.0017 0.0113  71  HIS   C CA  
1611 C C   . HIS   B 65  ? 0.2172 0.1881 0.1885 0.0151  0.0013  0.0108  71  HIS   C C   
1612 O O   . HIS   B 65  ? 0.2595 0.2253 0.2258 0.0165  0.0023  0.0093  71  HIS   C O   
1613 C CB  . HIS   B 65  ? 0.2046 0.1731 0.1765 0.0103  -0.0033 0.0108  71  HIS   C CB  
1614 C CG  . HIS   B 65  ? 0.1868 0.1564 0.1608 0.0070  -0.0061 0.0115  71  HIS   C CG  
1615 N ND1 . HIS   B 65  ? 0.2244 0.1986 0.2051 0.0058  -0.0065 0.0131  71  HIS   C ND1 
1616 C CD2 . HIS   B 65  ? 0.2006 0.1672 0.1709 0.0049  -0.0087 0.0107  71  HIS   C CD2 
1617 C CE1 . HIS   B 65  ? 0.2029 0.1770 0.1848 0.0031  -0.0090 0.0135  71  HIS   C CE1 
1618 N NE2 . HIS   B 65  ? 0.2305 0.2002 0.2064 0.0023  -0.0108 0.0121  71  HIS   C NE2 
1619 N N   . TYR   B 66  ? 0.1888 0.1652 0.1667 0.0163  0.0028  0.0119  72  TYR   C N   
1620 C CA  . TYR   B 66  ? 0.1826 0.1598 0.1625 0.0194  0.0053  0.0116  72  TYR   C CA  
1621 C C   . TYR   B 66  ? 0.1769 0.1567 0.1624 0.0202  0.0045  0.0116  72  TYR   C C   
1622 O O   . TYR   B 66  ? 0.1759 0.1598 0.1662 0.0189  0.0032  0.0123  72  TYR   C O   
1623 C CB  . TYR   B 66  ? 0.1916 0.1735 0.1759 0.0203  0.0076  0.0129  72  TYR   C CB  
1624 C CG  . TYR   B 66  ? 0.1986 0.1781 0.1767 0.0205  0.0093  0.0133  72  TYR   C CG  
1625 C CD1 . TYR   B 66  ? 0.2241 0.1997 0.1971 0.0230  0.0122  0.0124  72  TYR   C CD1 
1626 C CD2 . TYR   B 66  ? 0.2081 0.1891 0.1853 0.0187  0.0083  0.0147  72  TYR   C CD2 
1627 C CE1 . TYR   B 66  ? 0.2452 0.2182 0.2112 0.0236  0.0142  0.0128  72  TYR   C CE1 
1628 C CE2 . TYR   B 66  ? 0.2280 0.2066 0.1985 0.0193  0.0098  0.0154  72  TYR   C CE2 
1629 C CZ  . TYR   B 66  ? 0.2412 0.2156 0.2056 0.0218  0.0128  0.0144  72  TYR   C CZ  
1630 O OH  . TYR   B 66  ? 0.2670 0.2387 0.2233 0.0226  0.0145  0.0150  72  TYR   C OH  
1631 N N   . PRO   B 67  ? 0.1746 0.1521 0.1593 0.0225  0.0053  0.0109  73  PRO   C N   
1632 C CA  . PRO   B 67  ? 0.1692 0.1495 0.1588 0.0239  0.0043  0.0111  73  PRO   C CA  
1633 C C   . PRO   B 67  ? 0.1818 0.1683 0.1791 0.0253  0.0051  0.0114  73  PRO   C C   
1634 O O   . PRO   B 67  ? 0.2057 0.1928 0.2043 0.0268  0.0077  0.0115  73  PRO   C O   
1635 C CB  . PRO   B 67  ? 0.2025 0.1780 0.1888 0.0263  0.0049  0.0106  73  PRO   C CB  
1636 C CG  . PRO   B 67  ? 0.2397 0.2109 0.2211 0.0269  0.0072  0.0097  73  PRO   C CG  
1637 C CD  . PRO   B 67  ? 0.1942 0.1659 0.1731 0.0243  0.0071  0.0098  73  PRO   C CD  
1638 N N   . VAL   B 68  ? 0.1646 0.1555 0.1670 0.0248  0.0033  0.0115  74  VAL   C N   
1639 C CA  . VAL   B 68  ? 0.1612 0.1580 0.1720 0.0255  0.0036  0.0115  74  VAL   C CA  
1640 C C   . VAL   B 68  ? 0.1514 0.1511 0.1661 0.0265  0.0009  0.0107  74  VAL   C C   
1641 O O   . VAL   B 68  ? 0.1624 0.1603 0.1733 0.0259  -0.0011 0.0105  74  VAL   C O   
1642 C CB  . VAL   B 68  ? 0.1862 0.1860 0.2002 0.0231  0.0040  0.0121  74  VAL   C CB  
1643 C CG1 . VAL   B 68  ? 0.2212 0.2194 0.2325 0.0227  0.0069  0.0132  74  VAL   C CG1 
1644 C CG2 . VAL   B 68  ? 0.1952 0.1943 0.2069 0.0208  0.0020  0.0121  74  VAL   C CG2 
1645 N N   . SER   B 69  ? 0.1473 0.1517 0.1700 0.0279  0.0007  0.0103  75  SER   C N   
1646 C CA  . SER   B 69  ? 0.1561 0.1647 0.1843 0.0284  -0.0024 0.0092  75  SER   C CA  
1647 C C   . SER   B 69  ? 0.1446 0.1568 0.1784 0.0260  -0.0024 0.0088  75  SER   C C   
1648 O O   . SER   B 69  ? 0.1506 0.1641 0.1881 0.0252  0.0004  0.0097  75  SER   C O   
1649 C CB  . SER   B 69  ? 0.1888 0.2010 0.2244 0.0311  -0.0031 0.0089  75  SER   C CB  
1650 O OG  . SER   B 69  ? 0.2519 0.2604 0.2825 0.0336  -0.0029 0.0095  75  SER   C OG  
1651 N N   . PHE   B 70  ? 0.1390 0.1523 0.1730 0.0251  -0.0051 0.0075  76  PHE   C N   
1652 C CA  . PHE   B 70  ? 0.1363 0.1523 0.1758 0.0229  -0.0050 0.0068  76  PHE   C CA  
1653 C C   . PHE   B 70  ? 0.1392 0.1584 0.1836 0.0232  -0.0085 0.0044  76  PHE   C C   
1654 O O   . PHE   B 70  ? 0.1443 0.1626 0.1848 0.0248  -0.0114 0.0033  76  PHE   C O   
1655 C CB  . PHE   B 70  ? 0.1425 0.1557 0.1765 0.0207  -0.0039 0.0077  76  PHE   C CB  
1656 C CG  . PHE   B 70  ? 0.1380 0.1477 0.1641 0.0209  -0.0054 0.0073  76  PHE   C CG  
1657 C CD1 . PHE   B 70  ? 0.1508 0.1562 0.1695 0.0215  -0.0047 0.0086  76  PHE   C CD1 
1658 C CD2 . PHE   B 70  ? 0.1489 0.1592 0.1748 0.0205  -0.0072 0.0058  76  PHE   C CD2 
1659 C CE1 . PHE   B 70  ? 0.1489 0.1512 0.1613 0.0216  -0.0056 0.0087  76  PHE   C CE1 
1660 C CE2 . PHE   B 70  ? 0.1512 0.1582 0.1696 0.0208  -0.0078 0.0059  76  PHE   C CE2 
1661 C CZ  . PHE   B 70  ? 0.1601 0.1632 0.1721 0.0214  -0.0069 0.0075  76  PHE   C CZ  
1662 N N   . SER   B 71  ? 0.1244 0.1469 0.1772 0.0217  -0.0084 0.0035  77  SER   C N   
1663 C CA  . SER   B 71  ? 0.1366 0.1622 0.1955 0.0218  -0.0119 0.0006  77  SER   C CA  
1664 C C   . SER   B 71  ? 0.1540 0.1773 0.2069 0.0211  -0.0140 -0.0013 77  SER   C C   
1665 O O   . SER   B 71  ? 0.1696 0.1893 0.2149 0.0204  -0.0122 -0.0001 77  SER   C O   
1666 C CB  . SER   B 71  ? 0.1502 0.1799 0.2215 0.0204  -0.0107 0.0004  77  SER   C CB  
1667 O OG  . SER   B 71  ? 0.1720 0.2005 0.2438 0.0182  -0.0080 0.0015  77  SER   C OG  
1668 N N   . LYS   B 72  ? 0.1628 0.1880 0.2192 0.0213  -0.0176 -0.0045 78  LYS   C N   
1669 C CA  . LYS   B 72  ? 0.1602 0.1828 0.2103 0.0211  -0.0193 -0.0068 78  LYS   C CA  
1670 C C   . LYS   B 72  ? 0.1730 0.1956 0.2277 0.0186  -0.0168 -0.0071 78  LYS   C C   
1671 O O   . LYS   B 72  ? 0.1847 0.2101 0.2495 0.0173  -0.0157 -0.0068 78  LYS   C O   
1672 C CB  . LYS   B 72  ? 0.2165 0.2411 0.2688 0.0222  -0.0246 -0.0106 78  LYS   C CB  
1673 C CG  . LYS   B 72  ? 0.2461 0.2712 0.2945 0.0250  -0.0276 -0.0102 78  LYS   C CG  
1674 C CD  . LYS   B 72  ? 0.3841 0.4100 0.4310 0.0265  -0.0336 -0.0140 78  LYS   C CD  
1675 C CE  . LYS   B 72  ? 0.4933 0.5189 0.5343 0.0297  -0.0366 -0.0129 78  LYS   C CE  
1676 N NZ  . LYS   B 72  ? 0.5629 0.5833 0.5888 0.0316  -0.0373 -0.0127 78  LYS   C NZ  
1677 N N   . PRO   B 73  ? 0.1580 0.1773 0.2063 0.0181  -0.0157 -0.0074 79  PRO   C N   
1678 C CA  . PRO   B 73  ? 0.1658 0.1849 0.2191 0.0160  -0.0133 -0.0075 79  PRO   C CA  
1679 C C   . PRO   B 73  ? 0.1657 0.1870 0.2283 0.0151  -0.0154 -0.0109 79  PRO   C C   
1680 O O   . PRO   B 73  ? 0.1998 0.2209 0.2606 0.0161  -0.0191 -0.0147 79  PRO   C O   
1681 C CB  . PRO   B 73  ? 0.1970 0.2124 0.2417 0.0163  -0.0124 -0.0080 79  PRO   C CB  
1682 C CG  . PRO   B 73  ? 0.2206 0.2341 0.2556 0.0180  -0.0130 -0.0067 79  PRO   C CG  
1683 C CD  . PRO   B 73  ? 0.1781 0.1937 0.2146 0.0195  -0.0161 -0.0073 79  PRO   C CD  
1684 N N   . SER   B 74  ? 0.1475 0.1709 0.2202 0.0134  -0.0132 -0.0096 80  SER   C N   
1685 C CA  . SER   B 74  ? 0.1531 0.1788 0.2369 0.0123  -0.0150 -0.0125 80  SER   C CA  
1686 C C   . SER   B 74  ? 0.1457 0.1714 0.2378 0.0103  -0.0114 -0.0108 80  SER   C C   
1687 O O   . SER   B 74  ? 0.1485 0.1730 0.2377 0.0100  -0.0079 -0.0071 80  SER   C O   
1688 C CB  . SER   B 74  ? 0.1925 0.2222 0.2837 0.0128  -0.0165 -0.0121 80  SER   C CB  
1689 O OG  . SER   B 74  ? 0.2460 0.2759 0.3300 0.0149  -0.0197 -0.0128 80  SER   C OG  
1690 N N   . LEU   B 75  ? 0.1583 0.1854 0.2613 0.0090  -0.0126 -0.0134 81  LEU   C N   
1691 C CA  . LEU   B 75  ? 0.1692 0.1963 0.2821 0.0072  -0.0093 -0.0119 81  LEU   C CA  
1692 C C   . LEU   B 75  ? 0.1709 0.2016 0.2929 0.0067  -0.0072 -0.0084 81  LEU   C C   
1693 O O   . LEU   B 75  ? 0.1905 0.2243 0.3206 0.0065  -0.0096 -0.0104 81  LEU   C O   
1694 C CB  . LEU   B 75  ? 0.1938 0.2199 0.3137 0.0060  -0.0118 -0.0170 81  LEU   C CB  
1695 C CG  . LEU   B 75  ? 0.2288 0.2539 0.3591 0.0041  -0.0085 -0.0158 81  LEU   C CG  
1696 C CD1 . LEU   B 75  ? 0.2187 0.2404 0.3425 0.0045  -0.0051 -0.0134 81  LEU   C CD1 
1697 C CD2 . LEU   B 75  ? 0.2588 0.2828 0.3972 0.0028  -0.0116 -0.0217 81  LEU   C CD2 
1698 N N   . ILE   B 76  ? 0.1842 0.2146 0.3047 0.0067  -0.0029 -0.0034 82  ILE   C N   
1699 C CA  . ILE   B 76  ? 0.1986 0.2316 0.3246 0.0068  0.0000  0.0004  82  ILE   C CA  
1700 C C   . ILE   B 76  ? 0.1896 0.2221 0.3226 0.0056  0.0044  0.0041  82  ILE   C C   
1701 O O   . ILE   B 76  ? 0.1757 0.2054 0.3037 0.0055  0.0059  0.0059  82  ILE   C O   
1702 C CB  . ILE   B 76  ? 0.2295 0.2617 0.3438 0.0085  0.0011  0.0034  82  ILE   C CB  
1703 C CG1 . ILE   B 76  ? 0.2693 0.3014 0.3757 0.0101  -0.0029 0.0003  82  ILE   C CG1 
1704 C CG2 . ILE   B 76  ? 0.2521 0.2860 0.3696 0.0091  0.0050  0.0076  82  ILE   C CG2 
1705 C CD1 . ILE   B 76  ? 0.3091 0.3443 0.4188 0.0113  -0.0043 -0.0001 82  ILE   C CD1 
1706 N N   . PHE   B 77  ? 0.1887 0.2238 0.3332 0.0050  0.0067  0.0060  83  PHE   C N   
1707 C CA  . PHE   B 77  ? 0.1993 0.2336 0.3499 0.0041  0.0116  0.0105  83  PHE   C CA  
1708 C C   . PHE   B 77  ? 0.2092 0.2427 0.3501 0.0057  0.0149  0.0155  83  PHE   C C   
1709 O O   . PHE   B 77  ? 0.2413 0.2764 0.3791 0.0070  0.0154  0.0163  83  PHE   C O   
1710 C CB  . PHE   B 77  ? 0.2009 0.2381 0.3674 0.0029  0.0135  0.0110  83  PHE   C CB  
1711 C CG  . PHE   B 77  ? 0.2037 0.2393 0.3775 0.0019  0.0182  0.0152  83  PHE   C CG  
1712 C CD1 . PHE   B 77  ? 0.2183 0.2512 0.3954 0.0006  0.0175  0.0136  83  PHE   C CD1 
1713 C CD2 . PHE   B 77  ? 0.2280 0.2641 0.4034 0.0026  0.0237  0.0211  83  PHE   C CD2 
1714 C CE1 . PHE   B 77  ? 0.2386 0.2696 0.4221 0.0000  0.0219  0.0180  83  PHE   C CE1 
1715 C CE2 . PHE   B 77  ? 0.2257 0.2600 0.4066 0.0020  0.0281  0.0256  83  PHE   C CE2 
1716 C CZ  . PHE   B 77  ? 0.2336 0.2653 0.4190 0.0006  0.0271  0.0241  83  PHE   C CZ  
1717 N N   . VAL   B 78  ? 0.1716 0.2024 0.3076 0.0057  0.0170  0.0188  84  VAL   C N   
1718 C CA  . VAL   B 78  ? 0.1819 0.2114 0.3078 0.0070  0.0194  0.0233  84  VAL   C CA  
1719 C C   . VAL   B 78  ? 0.1745 0.2035 0.3057 0.0069  0.0243  0.0286  84  VAL   C C   
1720 O O   . VAL   B 78  ? 0.1682 0.1961 0.3055 0.0059  0.0250  0.0294  84  VAL   C O   
1721 C CB  . VAL   B 78  ? 0.1964 0.2233 0.3113 0.0072  0.0171  0.0228  84  VAL   C CB  
1722 C CG1 . VAL   B 78  ? 0.2103 0.2358 0.3147 0.0084  0.0187  0.0269  84  VAL   C CG1 
1723 C CG2 . VAL   B 78  ? 0.2105 0.2375 0.3204 0.0074  0.0129  0.0179  84  VAL   C CG2 
1724 N N   . GLU   B 79  ? 0.1651 0.1943 0.2929 0.0082  0.0278  0.0324  85  GLU   C N   
1725 C CA  . GLU   B 79  ? 0.1673 0.1953 0.2979 0.0086  0.0328  0.0381  85  GLU   C CA  
1726 C C   . GLU   B 79  ? 0.1660 0.1912 0.2883 0.0089  0.0324  0.0411  85  GLU   C C   
1727 O O   . GLU   B 79  ? 0.1649 0.1891 0.2779 0.0091  0.0287  0.0393  85  GLU   C O   
1728 C CB  . GLU   B 79  ? 0.2065 0.2349 0.3332 0.0103  0.0369  0.0413  85  GLU   C CB  
1729 C CG  . GLU   B 79  ? 0.2513 0.2832 0.3895 0.0101  0.0383  0.0395  85  GLU   C CG  
1730 C CD  . GLU   B 79  ? 0.3697 0.4034 0.5251 0.0082  0.0402  0.0398  85  GLU   C CD  
1731 O OE1 . GLU   B 79  ? 0.4190 0.4511 0.5779 0.0081  0.0442  0.0445  85  GLU   C OE1 
1732 O OE2 . GLU   B 79  ? 0.4058 0.4424 0.5713 0.0069  0.0372  0.0353  85  GLU   C OE2 
1733 N N   . ALA   B 80  ? 0.1728 0.1968 0.2994 0.0090  0.0360  0.0461  86  ALA   C N   
1734 C CA  . ALA   B 80  ? 0.1902 0.2117 0.3104 0.0096  0.0356  0.0496  86  ALA   C CA  
1735 C C   . ALA   B 80  ? 0.2019 0.2222 0.3064 0.0111  0.0342  0.0510  86  ALA   C C   
1736 O O   . ALA   B 80  ? 0.2190 0.2391 0.3178 0.0123  0.0362  0.0517  86  ALA   C O   
1737 C CB  . ALA   B 80  ? 0.2077 0.2281 0.3344 0.0101  0.0406  0.0556  86  ALA   C CB  
1738 N N   . SER   B 81  ? 0.1913 0.2105 0.2896 0.0110  0.0306  0.0506  87  SER   C N   
1739 C CA  . SER   B 81  ? 0.2031 0.2209 0.2875 0.0121  0.0286  0.0518  87  SER   C CA  
1740 C C   . SER   B 81  ? 0.2219 0.2383 0.3035 0.0127  0.0281  0.0566  87  SER   C C   
1741 O O   . SER   B 81  ? 0.2250 0.2415 0.3158 0.0125  0.0299  0.0591  87  SER   C O   
1742 C CB  . SER   B 81  ? 0.1903 0.2086 0.2700 0.0113  0.0240  0.0468  87  SER   C CB  
1743 O OG  . SER   B 81  ? 0.1977 0.2164 0.2821 0.0103  0.0216  0.0458  87  SER   C OG  
1744 N N   . GLU   B 82  ? 0.2413 0.2564 0.3108 0.0135  0.0254  0.0577  88  GLU   C N   
1745 C CA  . GLU   B 82  ? 0.2510 0.2653 0.3181 0.0142  0.0241  0.0622  88  GLU   C CA  
1746 C C   . GLU   B 82  ? 0.2437 0.2594 0.3189 0.0130  0.0214  0.0609  88  GLU   C C   
1747 O O   . GLU   B 82  ? 0.2697 0.2851 0.3477 0.0137  0.0212  0.0650  88  GLU   C O   
1748 C CB  . GLU   B 82  ? 0.3182 0.3307 0.3706 0.0153  0.0214  0.0636  88  GLU   C CB  
1749 C CG  . GLU   B 82  ? 0.4271 0.4400 0.4740 0.0141  0.0163  0.0593  88  GLU   C CG  
1750 C CD  . GLU   B 82  ? 0.5108 0.5217 0.5444 0.0150  0.0132  0.0612  88  GLU   C CD  
1751 O OE1 . GLU   B 82  ? 0.5282 0.5367 0.5533 0.0167  0.0156  0.0636  88  GLU   C OE1 
1752 O OE2 . GLU   B 82  ? 0.5271 0.5388 0.5589 0.0141  0.0084  0.0602  88  GLU   C OE2 
1753 N N   . TYR   B 83  ? 0.2088 0.2258 0.2883 0.0116  0.0198  0.0555  89  TYR   C N   
1754 C CA  . TYR   B 83  ? 0.1977 0.2158 0.2835 0.0108  0.0176  0.0539  89  TYR   C CA  
1755 C C   . TYR   B 83  ? 0.2107 0.2292 0.3081 0.0098  0.0193  0.0505  89  TYR   C C   
1756 O O   . TYR   B 83  ? 0.2246 0.2434 0.3278 0.0094  0.0184  0.0496  89  TYR   C O   
1757 C CB  . TYR   B 83  ? 0.1970 0.2156 0.2755 0.0101  0.0135  0.0508  89  TYR   C CB  
1758 C CG  . TYR   B 83  ? 0.1979 0.2163 0.2709 0.0096  0.0131  0.0465  89  TYR   C CG  
1759 C CD1 . TYR   B 83  ? 0.2020 0.2191 0.2649 0.0103  0.0129  0.0473  89  TYR   C CD1 
1760 C CD2 . TYR   B 83  ? 0.1847 0.2037 0.2621 0.0088  0.0130  0.0417  89  TYR   C CD2 
1761 C CE1 . TYR   B 83  ? 0.1952 0.2117 0.2535 0.0102  0.0127  0.0436  89  TYR   C CE1 
1762 C CE2 . TYR   B 83  ? 0.1797 0.1985 0.2524 0.0087  0.0124  0.0382  89  TYR   C CE2 
1763 C CZ  . TYR   B 83  ? 0.1832 0.2009 0.2468 0.0094  0.0124  0.0393  89  TYR   C CZ  
1764 O OH  . TYR   B 83  ? 0.1968 0.2141 0.2565 0.0096  0.0122  0.0361  89  TYR   C OH  
1765 N N   . TYR   B 84  ? 0.1794 0.1980 0.2811 0.0094  0.0217  0.0486  90  TYR   C N   
1766 C CA  . TYR   B 84  ? 0.1751 0.1939 0.2884 0.0083  0.0230  0.0455  90  TYR   C CA  
1767 C C   . TYR   B 84  ? 0.1685 0.1873 0.2886 0.0083  0.0269  0.0474  90  TYR   C C   
1768 O O   . TYR   B 84  ? 0.1681 0.1872 0.2829 0.0090  0.0283  0.0490  90  TYR   C O   
1769 C CB  . TYR   B 84  ? 0.1694 0.1891 0.2819 0.0074  0.0206  0.0389  90  TYR   C CB  
1770 C CG  . TYR   B 84  ? 0.1496 0.1692 0.2580 0.0073  0.0176  0.0363  90  TYR   C CG  
1771 C CD1 . TYR   B 84  ? 0.1567 0.1756 0.2711 0.0072  0.0177  0.0361  90  TYR   C CD1 
1772 C CD2 . TYR   B 84  ? 0.1458 0.1657 0.2451 0.0073  0.0152  0.0341  90  TYR   C CD2 
1773 C CE1 . TYR   B 84  ? 0.1656 0.1845 0.2768 0.0072  0.0158  0.0339  90  TYR   C CE1 
1774 C CE2 . TYR   B 84  ? 0.1519 0.1718 0.2481 0.0072  0.0131  0.0320  90  TYR   C CE2 
1775 C CZ  . TYR   B 84  ? 0.1615 0.1810 0.2637 0.0071  0.0135  0.0319  90  TYR   C CZ  
1776 O OH  . TYR   B 84  ? 0.1530 0.1725 0.2527 0.0071  0.0121  0.0301  90  TYR   C OH  
1777 N N   . PRO   B 85  ? 0.1755 0.1938 0.3079 0.0074  0.0287  0.0467  91  PRO   C N   
1778 C CA  . PRO   B 85  ? 0.1676 0.1863 0.3086 0.0069  0.0322  0.0476  91  PRO   C CA  
1779 C C   . PRO   B 85  ? 0.1624 0.1831 0.3041 0.0060  0.0306  0.0421  91  PRO   C C   
1780 O O   . PRO   B 85  ? 0.1661 0.1874 0.3018 0.0059  0.0268  0.0375  91  PRO   C O   
1781 C CB  . PRO   B 85  ? 0.1780 0.1952 0.3321 0.0059  0.0337  0.0475  91  PRO   C CB  
1782 C CG  . PRO   B 85  ? 0.1854 0.2021 0.3380 0.0055  0.0299  0.0425  91  PRO   C CG  
1783 C CD  . PRO   B 85  ? 0.1795 0.1968 0.3189 0.0067  0.0275  0.0439  91  PRO   C CD  
1784 N N   . ALA   B 86  ? 0.1575 0.1795 0.3076 0.0055  0.0334  0.0425  92  ALA   C N   
1785 C CA  . ALA   B 86  ? 0.1767 0.2011 0.3303 0.0047  0.0315  0.0374  92  ALA   C CA  
1786 C C   . ALA   B 86  ? 0.1854 0.2094 0.3455 0.0032  0.0280  0.0314  92  ALA   C C   
1787 O O   . ALA   B 86  ? 0.2034 0.2256 0.3721 0.0023  0.0292  0.0318  92  ALA   C O   
1788 C CB  . ALA   B 86  ? 0.1744 0.2003 0.3386 0.0042  0.0356  0.0396  92  ALA   C CB  
1789 N N   . ARG   B 87  ? 0.1741 0.1991 0.3283 0.0032  0.0239  0.0262  93  ARG   C N   
1790 C CA  . ARG   B 87  ? 0.1777 0.2017 0.3349 0.0022  0.0205  0.0205  93  ARG   C CA  
1791 C C   . ARG   B 87  ? 0.1805 0.2060 0.3315 0.0025  0.0163  0.0154  93  ARG   C C   
1792 O O   . ARG   B 87  ? 0.1706 0.1975 0.3138 0.0036  0.0160  0.0166  93  ARG   C O   
1793 C CB  . ARG   B 87  ? 0.1867 0.2080 0.3381 0.0027  0.0201  0.0213  93  ARG   C CB  
1794 C CG  . ARG   B 87  ? 0.1723 0.1939 0.3097 0.0040  0.0183  0.0220  93  ARG   C CG  
1795 C CD  . ARG   B 87  ? 0.1820 0.2017 0.3156 0.0045  0.0181  0.0231  93  ARG   C CD  
1796 N NE  . ARG   B 87  ? 0.1736 0.1936 0.2954 0.0053  0.0158  0.0224  93  ARG   C NE  
1797 C CZ  . ARG   B 87  ? 0.1950 0.2140 0.3126 0.0056  0.0143  0.0204  93  ARG   C CZ  
1798 N NH1 . ARG   B 87  ? 0.1940 0.2113 0.3175 0.0054  0.0151  0.0192  93  ARG   C NH1 
1799 N NH2 . ARG   B 87  ? 0.1902 0.2095 0.2981 0.0061  0.0125  0.0198  93  ARG   C NH2 
1800 N N   . TYR   B 88  ? 0.1888 0.2136 0.3422 0.0018  0.0130  0.0097  94  TYR   C N   
1801 C CA  . TYR   B 88  ? 0.2073 0.2327 0.3529 0.0024  0.0088  0.0050  94  TYR   C CA  
1802 C C   . TYR   B 88  ? 0.1908 0.2141 0.3237 0.0036  0.0082  0.0054  94  TYR   C C   
1803 O O   . TYR   B 88  ? 0.2100 0.2310 0.3431 0.0035  0.0094  0.0061  94  TYR   C O   
1804 C CB  . TYR   B 88  ? 0.2380 0.2626 0.3899 0.0014  0.0055  -0.0013 94  TYR   C CB  
1805 C CG  . TYR   B 88  ? 0.2688 0.2962 0.4330 0.0001  0.0046  -0.0029 94  TYR   C CG  
1806 C CD1 . TYR   B 88  ? 0.2756 0.3063 0.4385 0.0007  0.0019  -0.0045 94  TYR   C CD1 
1807 C CD2 . TYR   B 88  ? 0.2797 0.3067 0.4578 -0.0016 0.0069  -0.0022 94  TYR   C CD2 
1808 C CE1 . TYR   B 88  ? 0.2821 0.3161 0.4578 -0.0004 0.0010  -0.0057 94  TYR   C CE1 
1809 C CE2 . TYR   B 88  ? 0.2881 0.3181 0.4791 -0.0030 0.0063  -0.0034 94  TYR   C CE2 
1810 C CZ  . TYR   B 88  ? 0.2985 0.3324 0.4886 -0.0024 0.0033  -0.0050 94  TYR   C CZ  
1811 O OH  . TYR   B 88  ? 0.3242 0.3616 0.5288 -0.0038 0.0027  -0.0061 94  TYR   C OH  
1812 N N   . GLN   B 89  ? 0.1655 0.1896 0.2883 0.0048  0.0065  0.0054  95  GLN   C N   
1813 C CA  . GLN   B 89  ? 0.1572 0.1795 0.2687 0.0057  0.0058  0.0055  95  GLN   C CA  
1814 C C   . GLN   B 89  ? 0.1471 0.1692 0.2528 0.0064  0.0021  0.0007  95  GLN   C C   
1815 O O   . GLN   B 89  ? 0.1556 0.1797 0.2620 0.0068  0.0003  -0.0007 95  GLN   C O   
1816 C CB  . GLN   B 89  ? 0.1660 0.1887 0.2706 0.0064  0.0073  0.0102  95  GLN   C CB  
1817 C CG  . GLN   B 89  ? 0.1855 0.2065 0.2801 0.0070  0.0065  0.0105  95  GLN   C CG  
1818 C CD  . GLN   B 89  ? 0.1703 0.1912 0.2596 0.0072  0.0079  0.0152  95  GLN   C CD  
1819 O OE1 . GLN   B 89  ? 0.1756 0.1968 0.2685 0.0070  0.0100  0.0189  95  GLN   C OE1 
1820 N NE2 . GLN   B 89  ? 0.1583 0.1784 0.2387 0.0077  0.0065  0.0150  95  GLN   C NE2 
1821 N N   . SER   B 90  ? 0.1417 0.1615 0.2419 0.0068  0.0012  -0.0018 96  SER   C N   
1822 C CA  . SER   B 90  ? 0.1496 0.1684 0.2428 0.0078  -0.0020 -0.0060 96  SER   C CA  
1823 C C   . SER   B 90  ? 0.1432 0.1613 0.2251 0.0090  -0.0021 -0.0042 96  SER   C C   
1824 O O   . SER   B 90  ? 0.1450 0.1629 0.2242 0.0089  0.0000  -0.0004 96  SER   C O   
1825 C CB  . SER   B 90  ? 0.1804 0.1965 0.2736 0.0078  -0.0025 -0.0102 96  SER   C CB  
1826 O OG  . SER   B 90  ? 0.1878 0.2019 0.2774 0.0081  0.0003  -0.0079 96  SER   C OG  
1827 N N   . HIS   B 91  ? 0.1462 0.1639 0.2217 0.0102  -0.0050 -0.0071 97  HIS   C N   
1828 C CA  . HIS   B 91  ? 0.1414 0.1579 0.2062 0.0115  -0.0053 -0.0058 97  HIS   C CA  
1829 C C   . HIS   B 91  ? 0.1483 0.1660 0.2121 0.0113  -0.0039 -0.0016 97  HIS   C C   
1830 O O   . HIS   B 91  ? 0.1589 0.1752 0.2162 0.0115  -0.0027 0.0008  97  HIS   C O   
1831 C CB  . HIS   B 91  ? 0.1636 0.1772 0.2225 0.0117  -0.0035 -0.0056 97  HIS   C CB  
1832 C CG  . HIS   B 91  ? 0.1825 0.1940 0.2402 0.0123  -0.0044 -0.0101 97  HIS   C CG  
1833 N ND1 . HIS   B 91  ? 0.2168 0.2261 0.2650 0.0140  -0.0061 -0.0126 97  HIS   C ND1 
1834 C CD2 . HIS   B 91  ? 0.1895 0.2003 0.2539 0.0116  -0.0038 -0.0125 97  HIS   C CD2 
1835 C CE1 . HIS   B 91  ? 0.2123 0.2195 0.2607 0.0143  -0.0065 -0.0166 97  HIS   C CE1 
1836 N NE2 . HIS   B 91  ? 0.2111 0.2190 0.2694 0.0128  -0.0052 -0.0169 97  HIS   C NE2 
1837 N N   . LEU   B 92  ? 0.1367 0.1569 0.2070 0.0110  -0.0040 -0.0008 98  LEU   C N   
1838 C CA  . LEU   B 92  ? 0.1342 0.1552 0.2037 0.0111  -0.0022 0.0029  98  LEU   C CA  
1839 C C   . LEU   B 92  ? 0.1342 0.1562 0.2012 0.0125  -0.0040 0.0021  98  LEU   C C   
1840 O O   . LEU   B 92  ? 0.1357 0.1595 0.2069 0.0130  -0.0064 -0.0007 98  LEU   C O   
1841 C CB  . LEU   B 92  ? 0.1503 0.1733 0.2295 0.0100  0.0001  0.0049  98  LEU   C CB  
1842 C CG  . LEU   B 92  ? 0.1596 0.1829 0.2370 0.0102  0.0026  0.0090  98  LEU   C CG  
1843 C CD1 . LEU   B 92  ? 0.1822 0.2033 0.2527 0.0099  0.0036  0.0116  98  LEU   C CD1 
1844 C CD2 . LEU   B 92  ? 0.1673 0.1924 0.2543 0.0095  0.0052  0.0111  98  LEU   C CD2 
1845 N N   . MET   B 93  ? 0.1329 0.1537 0.1935 0.0132  -0.0031 0.0044  99  MET   C N   
1846 C CA  . MET   B 93  ? 0.1232 0.1444 0.1811 0.0148  -0.0042 0.0043  99  MET   C CA  
1847 C C   . MET   B 93  ? 0.1303 0.1520 0.1896 0.0150  -0.0013 0.0072  99  MET   C C   
1848 O O   . MET   B 93  ? 0.1386 0.1585 0.1942 0.0141  0.0006  0.0096  99  MET   C O   
1849 C CB  . MET   B 93  ? 0.1509 0.1688 0.1983 0.0158  -0.0051 0.0043  99  MET   C CB  
1850 C CG  . MET   B 93  ? 0.1585 0.1753 0.2028 0.0160  -0.0073 0.0017  99  MET   C CG  
1851 S SD  . MET   B 93  ? 0.1855 0.1981 0.2182 0.0169  -0.0073 0.0026  99  MET   C SD  
1852 C CE  . MET   B 93  ? 0.1858 0.1971 0.2179 0.0149  -0.0043 0.0055  99  MET   C CE  
1853 N N   . LEU   B 94  ? 0.1313 0.1552 0.1952 0.0161  -0.0011 0.0072  100 LEU   C N   
1854 C CA  . LEU   B 94  ? 0.1389 0.1628 0.2034 0.0166  0.0023  0.0100  100 LEU   C CA  
1855 C C   . LEU   B 94  ? 0.1330 0.1553 0.1914 0.0186  0.0023  0.0102  100 LEU   C C   
1856 O O   . LEU   B 94  ? 0.1536 0.1764 0.2115 0.0199  -0.0004 0.0083  100 LEU   C O   
1857 C CB  . LEU   B 94  ? 0.1447 0.1728 0.2213 0.0166  0.0039  0.0103  100 LEU   C CB  
1858 C CG  . LEU   B 94  ? 0.1606 0.1903 0.2455 0.0147  0.0045  0.0103  100 LEU   C CG  
1859 C CD1 . LEU   B 94  ? 0.1980 0.2315 0.2954 0.0147  0.0065  0.0110  100 LEU   C CD1 
1860 C CD2 . LEU   B 94  ? 0.1838 0.2110 0.2644 0.0135  0.0070  0.0131  100 LEU   C CD2 
1861 N N   . ALA   B 95  ? 0.1443 0.1644 0.1979 0.0190  0.0052  0.0125  101 ALA   C N   
1862 C CA  . ALA   B 95  ? 0.1436 0.1617 0.1923 0.0210  0.0062  0.0128  101 ALA   C CA  
1863 C C   . ALA   B 95  ? 0.1475 0.1657 0.1977 0.0217  0.0106  0.0151  101 ALA   C C   
1864 O O   . ALA   B 95  ? 0.1456 0.1643 0.1975 0.0204  0.0126  0.0168  101 ALA   C O   
1865 C CB  . ALA   B 95  ? 0.1564 0.1694 0.1937 0.0209  0.0053  0.0128  101 ALA   C CB  
1866 N N   . VAL   B 96  ? 0.1447 0.1619 0.1935 0.0240  0.0125  0.0153  102 VAL   C N   
1867 C CA  . VAL   B 96  ? 0.1552 0.1714 0.2027 0.0251  0.0172  0.0174  102 VAL   C CA  
1868 C C   . VAL   B 96  ? 0.1615 0.1718 0.1960 0.0248  0.0177  0.0179  102 VAL   C C   
1869 O O   . VAL   B 96  ? 0.1877 0.1943 0.2149 0.0255  0.0160  0.0165  102 VAL   C O   
1870 C CB  . VAL   B 96  ? 0.1731 0.1906 0.2251 0.0279  0.0192  0.0171  102 VAL   C CB  
1871 C CG1 . VAL   B 96  ? 0.1912 0.2069 0.2406 0.0295  0.0250  0.0193  102 VAL   C CG1 
1872 C CG2 . VAL   B 96  ? 0.1867 0.2107 0.2529 0.0279  0.0179  0.0165  102 VAL   C CG2 
1873 N N   . GLY   B 97  ? 0.1819 0.1912 0.2136 0.0236  0.0195  0.0198  103 GLY   C N   
1874 C CA  . GLY   B 97  ? 0.1998 0.2040 0.2196 0.0231  0.0190  0.0201  103 GLY   C CA  
1875 C C   . GLY   B 97  ? 0.1954 0.1995 0.2134 0.0218  0.0202  0.0226  103 GLY   C C   
1876 O O   . GLY   B 97  ? 0.2176 0.2255 0.2440 0.0213  0.0216  0.0243  103 GLY   C O   
1877 N N   . HIS   B 98  ? 0.2028 0.2023 0.2099 0.0215  0.0195  0.0229  104 HIS   C N   
1878 C CA  . HIS   B 98  ? 0.1960 0.1949 0.1996 0.0207  0.0201  0.0255  104 HIS   C CA  
1879 C C   . HIS   B 98  ? 0.1875 0.1880 0.1933 0.0181  0.0162  0.0259  104 HIS   C C   
1880 O O   . HIS   B 98  ? 0.1835 0.1828 0.1870 0.0169  0.0126  0.0239  104 HIS   C O   
1881 C CB  . HIS   B 98  ? 0.2402 0.2334 0.2305 0.0218  0.0207  0.0254  104 HIS   C CB  
1882 C CG  . HIS   B 98  ? 0.2841 0.2766 0.2699 0.0215  0.0214  0.0285  104 HIS   C CG  
1883 N ND1 . HIS   B 98  ? 0.3012 0.2956 0.2905 0.0229  0.0261  0.0317  104 HIS   C ND1 
1884 C CD2 . HIS   B 98  ? 0.3169 0.3074 0.2960 0.0200  0.0177  0.0290  104 HIS   C CD2 
1885 C CE1 . HIS   B 98  ? 0.3358 0.3288 0.3193 0.0224  0.0251  0.0342  104 HIS   C CE1 
1886 N NE2 . HIS   B 98  ? 0.3453 0.3362 0.3225 0.0207  0.0199  0.0326  104 HIS   C NE2 
1887 N N   . SER   B 99  ? 0.1868 0.1898 0.1976 0.0175  0.0173  0.0286  105 SER   C N   
1888 C CA  . SER   B 99  ? 0.1932 0.1977 0.2067 0.0155  0.0142  0.0295  105 SER   C CA  
1889 C C   . SER   B 99  ? 0.2059 0.2111 0.2203 0.0156  0.0161  0.0334  105 SER   C C   
1890 O O   . SER   B 99  ? 0.2419 0.2493 0.2635 0.0163  0.0196  0.0351  105 SER   C O   
1891 C CB  . SER   B 99  ? 0.2013 0.2094 0.2253 0.0146  0.0133  0.0278  105 SER   C CB  
1892 O OG  . SER   B 99  ? 0.2076 0.2172 0.2352 0.0129  0.0113  0.0288  105 SER   C OG  
1893 N N   . GLU   B 100 ? 0.2136 0.2167 0.2209 0.0150  0.0136  0.0348  106 GLU   C N   
1894 C CA  . GLU   B 100 ? 0.2254 0.2290 0.2326 0.0153  0.0144  0.0389  106 GLU   C CA  
1895 C C   . GLU   B 100 ? 0.1990 0.2050 0.2125 0.0134  0.0111  0.0394  106 GLU   C C   
1896 O O   . GLU   B 100 ? 0.1874 0.1940 0.2028 0.0120  0.0082  0.0366  106 GLU   C O   
1897 C CB  . GLU   B 100 ? 0.2931 0.2926 0.2870 0.0162  0.0133  0.0401  106 GLU   C CB  
1898 C CG  . GLU   B 100 ? 0.4549 0.4526 0.4442 0.0186  0.0186  0.0425  106 GLU   C CG  
1899 C CD  . GLU   B 100 ? 0.5095 0.5021 0.4846 0.0201  0.0187  0.0411  106 GLU   C CD  
1900 O OE1 . GLU   B 100 ? 0.5256 0.5163 0.4965 0.0224  0.0236  0.0425  106 GLU   C OE1 
1901 O OE2 . GLU   B 100 ? 0.5430 0.5332 0.5115 0.0190  0.0141  0.0384  106 GLU   C OE2 
1902 N N   . PRO   B 101 ? 0.2075 0.2149 0.2249 0.0135  0.0118  0.0432  107 PRO   C N   
1903 C CA  . PRO   B 101 ? 0.1986 0.2082 0.2228 0.0120  0.0090  0.0437  107 PRO   C CA  
1904 C C   . PRO   B 101 ? 0.2004 0.2094 0.2200 0.0107  0.0042  0.0420  107 PRO   C C   
1905 O O   . PRO   B 101 ? 0.1971 0.2079 0.2229 0.0093  0.0026  0.0402  107 PRO   C O   
1906 C CB  . PRO   B 101 ? 0.2277 0.2377 0.2536 0.0129  0.0103  0.0488  107 PRO   C CB  
1907 C CG  . PRO   B 101 ? 0.2664 0.2749 0.2895 0.0146  0.0149  0.0506  107 PRO   C CG  
1908 C CD  . PRO   B 101 ? 0.2306 0.2372 0.2466 0.0152  0.0156  0.0474  107 PRO   C CD  
1909 N N   . GLY   B 102 ? 0.1968 0.2029 0.2055 0.0110  0.0020  0.0424  108 GLY   C N   
1910 C CA  . GLY   B 102 ? 0.1971 0.2026 0.2023 0.0095  -0.0029 0.0409  108 GLY   C CA  
1911 C C   . GLY   B 102 ? 0.1890 0.1938 0.1946 0.0083  -0.0036 0.0366  108 GLY   C C   
1912 O O   . GLY   B 102 ? 0.2049 0.2095 0.2101 0.0067  -0.0071 0.0353  108 GLY   C O   
1913 N N   . ASP   B 103 ? 0.1697 0.1740 0.1762 0.0092  -0.0003 0.0346  109 ASP   C N   
1914 C CA  . ASP   B 103 ? 0.1642 0.1676 0.1708 0.0086  -0.0008 0.0310  109 ASP   C CA  
1915 C C   . ASP   B 103 ? 0.1533 0.1596 0.1690 0.0076  -0.0010 0.0300  109 ASP   C C   
1916 O O   . ASP   B 103 ? 0.1579 0.1635 0.1735 0.0070  -0.0018 0.0275  109 ASP   C O   
1917 C CB  . ASP   B 103 ? 0.1793 0.1812 0.1836 0.0103  0.0024  0.0293  109 ASP   C CB  
1918 C CG  . ASP   B 103 ? 0.1996 0.1974 0.1932 0.0114  0.0028  0.0294  109 ASP   C CG  
1919 O OD1 . ASP   B 103 ? 0.2156 0.2108 0.2026 0.0105  -0.0005 0.0287  109 ASP   C OD1 
1920 O OD2 . ASP   B 103 ? 0.2115 0.2087 0.2036 0.0133  0.0064  0.0301  109 ASP   C OD2 
1921 N N   . CYS   B 104 ? 0.1471 0.1564 0.1706 0.0075  0.0000  0.0319  110 CYS   C N   
1922 C CA  . CYS   B 104 ? 0.1495 0.1611 0.1811 0.0068  0.0001  0.0308  110 CYS   C CA  
1923 C C   . CYS   B 104 ? 0.1488 0.1601 0.1795 0.0053  -0.0026 0.0300  110 CYS   C C   
1924 O O   . CYS   B 104 ? 0.1646 0.1756 0.1930 0.0045  -0.0050 0.0317  110 CYS   C O   
1925 C CB  . CYS   B 104 ? 0.1534 0.1675 0.1930 0.0069  0.0013  0.0333  110 CYS   C CB  
1926 S SG  . CYS   B 104 ? 0.1696 0.1845 0.2143 0.0081  0.0051  0.0336  110 CYS   C SG  
1927 N N   . GLY   B 105 ? 0.1275 0.1389 0.1605 0.0050  -0.0022 0.0276  111 GLY   C N   
1928 C CA  . GLY   B 105 ? 0.1431 0.1541 0.1761 0.0037  -0.0038 0.0270  111 GLY   C CA  
1929 C C   . GLY   B 105 ? 0.1426 0.1504 0.1688 0.0035  -0.0046 0.0251  111 GLY   C C   
1930 O O   . GLY   B 105 ? 0.1588 0.1660 0.1855 0.0025  -0.0053 0.0244  111 GLY   C O   
1931 N N   . GLY   B 106 ? 0.1507 0.1563 0.1709 0.0045  -0.0043 0.0243  112 GLY   C N   
1932 C CA  . GLY   B 106 ? 0.1616 0.1636 0.1755 0.0045  -0.0049 0.0224  112 GLY   C CA  
1933 C C   . GLY   B 106 ? 0.1471 0.1490 0.1627 0.0052  -0.0036 0.0206  112 GLY   C C   
1934 O O   . GLY   B 106 ? 0.1474 0.1514 0.1667 0.0063  -0.0021 0.0200  112 GLY   C O   
1935 N N   . ILE   B 107 ? 0.1449 0.1442 0.1576 0.0045  -0.0043 0.0198  113 ILE   C N   
1936 C CA  . ILE   B 107 ? 0.1463 0.1450 0.1593 0.0054  -0.0031 0.0185  113 ILE   C CA  
1937 C C   . ILE   B 107 ? 0.1487 0.1455 0.1578 0.0074  -0.0025 0.0170  113 ILE   C C   
1938 O O   . ILE   B 107 ? 0.1518 0.1457 0.1560 0.0077  -0.0028 0.0167  113 ILE   C O   
1939 C CB  . ILE   B 107 ? 0.1830 0.1795 0.1952 0.0039  -0.0036 0.0189  113 ILE   C CB  
1940 C CG1 . ILE   B 107 ? 0.2248 0.2246 0.2438 0.0026  -0.0032 0.0203  113 ILE   C CG1 
1941 C CG2 . ILE   B 107 ? 0.1867 0.1806 0.1957 0.0052  -0.0024 0.0179  113 ILE   C CG2 
1942 C CD1 . ILE   B 107 ? 0.2683 0.2669 0.2890 0.0008  -0.0034 0.0213  113 ILE   C CD1 
1943 N N   . LEU   B 108 ? 0.1366 0.1350 0.1478 0.0088  -0.0017 0.0160  114 LEU   C N   
1944 C CA  . LEU   B 108 ? 0.1299 0.1270 0.1383 0.0109  -0.0015 0.0147  114 LEU   C CA  
1945 C C   . LEU   B 108 ? 0.1369 0.1317 0.1426 0.0111  -0.0016 0.0145  114 LEU   C C   
1946 O O   . LEU   B 108 ? 0.1392 0.1353 0.1469 0.0108  -0.0011 0.0145  114 LEU   C O   
1947 C CB  . LEU   B 108 ? 0.1323 0.1330 0.1455 0.0122  -0.0013 0.0136  114 LEU   C CB  
1948 C CG  . LEU   B 108 ? 0.1406 0.1410 0.1525 0.0145  -0.0018 0.0122  114 LEU   C CG  
1949 C CD1 . LEU   B 108 ? 0.1618 0.1604 0.1712 0.0157  -0.0014 0.0123  114 LEU   C CD1 
1950 C CD2 . LEU   B 108 ? 0.1513 0.1556 0.1693 0.0152  -0.0023 0.0108  114 LEU   C CD2 
1951 N N   . ARG   B 109 ? 0.1405 0.1315 0.1413 0.0120  -0.0017 0.0144  115 ARG   C N   
1952 C CA  . ARG   B 109 ? 0.1504 0.1385 0.1480 0.0124  -0.0013 0.0148  115 ARG   C CA  
1953 C C   . ARG   B 109 ? 0.1560 0.1419 0.1499 0.0150  -0.0016 0.0143  115 ARG   C C   
1954 O O   . ARG   B 109 ? 0.1675 0.1528 0.1607 0.0161  -0.0019 0.0137  115 ARG   C O   
1955 C CB  . ARG   B 109 ? 0.2017 0.1863 0.1977 0.0103  -0.0011 0.0161  115 ARG   C CB  
1956 C CG  . ARG   B 109 ? 0.2595 0.2405 0.2522 0.0102  -0.0017 0.0156  115 ARG   C CG  
1957 C CD  . ARG   B 109 ? 0.3468 0.3243 0.3388 0.0076  -0.0021 0.0164  115 ARG   C CD  
1958 N NE  . ARG   B 109 ? 0.4189 0.3991 0.4145 0.0051  -0.0032 0.0167  115 ARG   C NE  
1959 C CZ  . ARG   B 109 ? 0.5228 0.5046 0.5227 0.0030  -0.0033 0.0180  115 ARG   C CZ  
1960 N NH1 . ARG   B 109 ? 0.5439 0.5250 0.5450 0.0031  -0.0016 0.0191  115 ARG   C NH1 
1961 N NH2 . ARG   B 109 ? 0.5301 0.5145 0.5333 0.0012  -0.0048 0.0185  115 ARG   C NH2 
1962 N N   . CYS   B 110 ? 0.1593 0.1441 0.1507 0.0163  -0.0014 0.0146  116 CYS   C N   
1963 C CA  . CYS   B 110 ? 0.1723 0.1547 0.1596 0.0192  -0.0020 0.0146  116 CYS   C CA  
1964 C C   . CYS   B 110 ? 0.1975 0.1750 0.1803 0.0190  -0.0006 0.0165  116 CYS   C C   
1965 O O   . CYS   B 110 ? 0.1980 0.1742 0.1818 0.0165  0.0007  0.0175  116 CYS   C O   
1966 C CB  . CYS   B 110 ? 0.1655 0.1512 0.1534 0.0213  -0.0034 0.0133  116 CYS   C CB  
1967 S SG  . CYS   B 110 ? 0.1725 0.1582 0.1581 0.0210  -0.0025 0.0135  116 CYS   C SG  
1968 N N   . GLN   B 111 ? 0.2109 0.1855 0.1891 0.0217  -0.0009 0.0172  117 GLN   C N   
1969 C CA  . GLN   B 111 ? 0.2395 0.2090 0.2134 0.0218  0.0009  0.0195  117 GLN   C CA  
1970 C C   . GLN   B 111 ? 0.2367 0.2067 0.2099 0.0208  0.0026  0.0205  117 GLN   C C   
1971 O O   . GLN   B 111 ? 0.2544 0.2207 0.2261 0.0198  0.0050  0.0227  117 GLN   C O   
1972 C CB  . GLN   B 111 ? 0.2592 0.2254 0.2279 0.0253  0.0002  0.0206  117 GLN   C CB  
1973 C CG  . GLN   B 111 ? 0.3025 0.2714 0.2684 0.0281  -0.0014 0.0200  117 GLN   C CG  
1974 C CD  . GLN   B 111 ? 0.4444 0.4108 0.4056 0.0320  -0.0029 0.0211  117 GLN   C CD  
1975 O OE1 . GLN   B 111 ? 0.4851 0.4541 0.4486 0.0339  -0.0054 0.0198  117 GLN   C OE1 
1976 N NE2 . GLN   B 111 ? 0.4523 0.4140 0.4073 0.0333  -0.0013 0.0238  117 GLN   C NE2 
1977 N N   . HIS   B 112 ? 0.2075 0.1819 0.1822 0.0212  0.0019  0.0189  118 HIS   C N   
1978 C CA  . HIS   B 112 ? 0.2036 0.1784 0.1773 0.0208  0.0040  0.0195  118 HIS   C CA  
1979 C C   . HIS   B 112 ? 0.2084 0.1855 0.1884 0.0175  0.0056  0.0196  118 HIS   C C   
1980 O O   . HIS   B 112 ? 0.2180 0.1951 0.1980 0.0171  0.0080  0.0205  118 HIS   C O   
1981 C CB  . HIS   B 112 ? 0.2098 0.1871 0.1809 0.0231  0.0025  0.0174  118 HIS   C CB  
1982 C CG  . HIS   B 112 ? 0.2078 0.1834 0.1732 0.0265  0.0002  0.0174  118 HIS   C CG  
1983 N ND1 . HIS   B 112 ? 0.1936 0.1724 0.1616 0.0278  -0.0033 0.0152  118 HIS   C ND1 
1984 C CD2 . HIS   B 112 ? 0.2349 0.2064 0.1926 0.0291  0.0009  0.0193  118 HIS   C CD2 
1985 C CE1 . HIS   B 112 ? 0.2185 0.1951 0.1809 0.0310  -0.0049 0.0160  118 HIS   C CE1 
1986 N NE2 . HIS   B 112 ? 0.2356 0.2076 0.1910 0.0320  -0.0026 0.0184  118 HIS   C NE2 
1987 N N   . GLY   B 113 ? 0.1917 0.1709 0.1767 0.0155  0.0042  0.0188  119 GLY   C N   
1988 C CA  . GLY   B 113 ? 0.1797 0.1616 0.1710 0.0127  0.0049  0.0191  119 GLY   C CA  
1989 C C   . GLY   B 113 ? 0.1608 0.1469 0.1565 0.0121  0.0029  0.0173  119 GLY   C C   
1990 O O   . GLY   B 113 ? 0.1711 0.1576 0.1659 0.0132  0.0012  0.0161  119 GLY   C O   
1991 N N   . VAL   B 114 ? 0.1568 0.1460 0.1580 0.0104  0.0036  0.0175  120 VAL   C N   
1992 C CA  . VAL   B 114 ? 0.1539 0.1469 0.1598 0.0097  0.0023  0.0165  120 VAL   C CA  
1993 C C   . VAL   B 114 ? 0.1580 0.1532 0.1642 0.0116  0.0018  0.0144  120 VAL   C C   
1994 O O   . VAL   B 114 ? 0.1560 0.1514 0.1617 0.0125  0.0030  0.0137  120 VAL   C O   
1995 C CB  . VAL   B 114 ? 0.1660 0.1612 0.1779 0.0075  0.0030  0.0178  120 VAL   C CB  
1996 C CG1 . VAL   B 114 ? 0.1783 0.1772 0.1948 0.0072  0.0019  0.0172  120 VAL   C CG1 
1997 C CG2 . VAL   B 114 ? 0.1827 0.1761 0.1952 0.0053  0.0026  0.0195  120 VAL   C CG2 
1998 N N   . VAL   B 115 ? 0.1402 0.1369 0.1474 0.0124  0.0002  0.0133  121 VAL   C N   
1999 C CA  . VAL   B 115 ? 0.1416 0.1406 0.1506 0.0138  -0.0008 0.0111  121 VAL   C CA  
2000 C C   . VAL   B 115 ? 0.1508 0.1531 0.1666 0.0126  -0.0005 0.0107  121 VAL   C C   
2001 O O   . VAL   B 115 ? 0.1551 0.1589 0.1734 0.0132  -0.0006 0.0089  121 VAL   C O   
2002 C CB  . VAL   B 115 ? 0.1410 0.1402 0.1491 0.0153  -0.0024 0.0104  121 VAL   C CB  
2003 C CG1 . VAL   B 115 ? 0.1585 0.1609 0.1708 0.0164  -0.0038 0.0081  121 VAL   C CG1 
2004 C CG2 . VAL   B 115 ? 0.1683 0.1640 0.1699 0.0169  -0.0028 0.0109  121 VAL   C CG2 
2005 N N   . GLY   B 116 ? 0.1404 0.1436 0.1591 0.0111  -0.0002 0.0124  122 GLY   C N   
2006 C CA  . GLY   B 116 ? 0.1517 0.1579 0.1770 0.0101  0.0002  0.0127  122 GLY   C CA  
2007 C C   . GLY   B 116 ? 0.1368 0.1432 0.1629 0.0088  0.0001  0.0149  122 GLY   C C   
2008 O O   . GLY   B 116 ? 0.1452 0.1493 0.1670 0.0083  -0.0004 0.0158  122 GLY   C O   
2009 N N   . ILE   B 117 ? 0.1279 0.1368 0.1596 0.0082  0.0005  0.0158  123 ILE   C N   
2010 C CA  . ILE   B 117 ? 0.1286 0.1376 0.1602 0.0072  0.0001  0.0181  123 ILE   C CA  
2011 C C   . ILE   B 117 ? 0.1321 0.1427 0.1665 0.0079  0.0008  0.0186  123 ILE   C C   
2012 O O   . ILE   B 117 ? 0.1340 0.1464 0.1737 0.0084  0.0016  0.0175  123 ILE   C O   
2013 C CB  . ILE   B 117 ? 0.1421 0.1524 0.1777 0.0059  0.0001  0.0201  123 ILE   C CB  
2014 C CG1 . ILE   B 117 ? 0.1540 0.1665 0.1965 0.0062  0.0014  0.0197  123 ILE   C CG1 
2015 C CG2 . ILE   B 117 ? 0.1586 0.1674 0.1918 0.0049  -0.0005 0.0205  123 ILE   C CG2 
2016 C CD1 . ILE   B 117 ? 0.1599 0.1741 0.2079 0.0052  0.0016  0.0222  123 ILE   C CD1 
2017 N N   . VAL   B 118 ? 0.1242 0.1338 0.1550 0.0078  0.0006  0.0201  124 VAL   C N   
2018 C CA  . VAL   B 118 ? 0.1273 0.1381 0.1605 0.0085  0.0021  0.0212  124 VAL   C CA  
2019 C C   . VAL   B 118 ? 0.1278 0.1410 0.1683 0.0080  0.0029  0.0228  124 VAL   C C   
2020 O O   . VAL   B 118 ? 0.1254 0.1389 0.1669 0.0071  0.0021  0.0244  124 VAL   C O   
2021 C CB  . VAL   B 118 ? 0.1278 0.1365 0.1545 0.0087  0.0020  0.0229  124 VAL   C CB  
2022 C CG1 . VAL   B 118 ? 0.1416 0.1514 0.1703 0.0096  0.0042  0.0248  124 VAL   C CG1 
2023 C CG2 . VAL   B 118 ? 0.1466 0.1523 0.1663 0.0094  0.0015  0.0212  124 VAL   C CG2 
2024 N N   . SER   B 119 ? 0.1251 0.1401 0.1716 0.0087  0.0045  0.0224  125 SER   C N   
2025 C CA  . SER   B 119 ? 0.1246 0.1412 0.1788 0.0083  0.0057  0.0238  125 SER   C CA  
2026 C C   . SER   B 119 ? 0.1392 0.1568 0.1973 0.0088  0.0081  0.0258  125 SER   C C   
2027 O O   . SER   B 119 ? 0.1407 0.1590 0.2036 0.0086  0.0093  0.0284  125 SER   C O   
2028 C CB  . SER   B 119 ? 0.1403 0.1579 0.2000 0.0081  0.0054  0.0209  125 SER   C CB  
2029 O OG  . SER   B 119 ? 0.1524 0.1710 0.2202 0.0077  0.0067  0.0218  125 SER   C OG  
2030 N N   . THR   B 120 ? 0.1399 0.1576 0.1970 0.0097  0.0090  0.0248  126 THR   C N   
2031 C CA  . THR   B 120 ? 0.1390 0.1578 0.2010 0.0103  0.0120  0.0269  126 THR   C CA  
2032 C C   . THR   B 120 ? 0.1338 0.1512 0.1889 0.0117  0.0134  0.0278  126 THR   C C   
2033 O O   . THR   B 120 ? 0.1408 0.1567 0.1889 0.0121  0.0118  0.0259  126 THR   C O   
2034 C CB  . THR   B 120 ? 0.1339 0.1551 0.2062 0.0102  0.0126  0.0245  126 THR   C CB  
2035 O OG1 . THR   B 120 ? 0.1440 0.1657 0.2145 0.0109  0.0113  0.0215  126 THR   C OG1 
2036 C CG2 . THR   B 120 ? 0.1537 0.1754 0.2318 0.0091  0.0111  0.0226  126 THR   C CG2 
2037 N N   . GLY   B 121 ? 0.1534 0.1712 0.2107 0.0124  0.0168  0.0305  127 GLY   C N   
2038 C CA  . GLY   B 121 ? 0.1739 0.1902 0.2250 0.0141  0.0191  0.0315  127 GLY   C CA  
2039 C C   . GLY   B 121 ? 0.2172 0.2347 0.2743 0.0150  0.0237  0.0343  127 GLY   C C   
2040 O O   . GLY   B 121 ? 0.2466 0.2654 0.3111 0.0142  0.0251  0.0365  127 GLY   C O   
2041 N N   . GLY   B 122 ? 0.2467 0.2632 0.2996 0.0167  0.0266  0.0350  128 GLY   C N   
2042 C CA  . GLY   B 122 ? 0.2750 0.2927 0.3340 0.0178  0.0320  0.0380  128 GLY   C CA  
2043 C C   . GLY   B 122 ? 0.2778 0.2983 0.3449 0.0186  0.0335  0.0359  128 GLY   C C   
2044 O O   . GLY   B 122 ? 0.2775 0.2998 0.3482 0.0181  0.0301  0.0322  128 GLY   C O   
2045 N N   . ASN   B 123 ? 0.2646 0.2856 0.3347 0.0202  0.0390  0.0386  129 ASN   C N   
2046 C CA  . ASN   B 123 ? 0.2779 0.3020 0.3568 0.0214  0.0414  0.0374  129 ASN   C CA  
2047 C C   . ASN   B 123 ? 0.2525 0.2753 0.3243 0.0227  0.0388  0.0339  129 ASN   C C   
2048 O O   . ASN   B 123 ? 0.2810 0.3070 0.3612 0.0233  0.0384  0.0320  129 ASN   C O   
2049 C CB  . ASN   B 123 ? 0.3371 0.3662 0.4327 0.0195  0.0397  0.0357  129 ASN   C CB  
2050 C CG  . ASN   B 123 ? 0.4308 0.4628 0.5401 0.0194  0.0450  0.0389  129 ASN   C CG  
2051 O OD1 . ASN   B 123 ? 0.4589 0.4896 0.5660 0.0210  0.0510  0.0428  129 ASN   C OD1 
2052 N ND2 . ASN   B 123 ? 0.4614 0.4970 0.5851 0.0173  0.0431  0.0374  129 ASN   C ND2 
2053 N N   . GLY   B 124 ? 0.2271 0.2452 0.2842 0.0232  0.0371  0.0334  130 GLY   C N   
2054 C CA  . GLY   B 124 ? 0.2185 0.2345 0.2685 0.0244  0.0348  0.0303  130 GLY   C CA  
2055 C C   . GLY   B 124 ? 0.2008 0.2184 0.2538 0.0230  0.0290  0.0268  130 GLY   C C   
2056 O O   . GLY   B 124 ? 0.1979 0.2146 0.2481 0.0241  0.0273  0.0245  130 GLY   C O   
2057 N N   . LEU   B 125 ? 0.1791 0.1987 0.2373 0.0207  0.0263  0.0266  131 LEU   C N   
2058 C CA  . LEU   B 125 ? 0.1702 0.1907 0.2299 0.0195  0.0212  0.0234  131 LEU   C CA  
2059 C C   . LEU   B 125 ? 0.1781 0.1959 0.2302 0.0178  0.0186  0.0236  131 LEU   C C   
2060 O O   . LEU   B 125 ? 0.2095 0.2262 0.2593 0.0172  0.0201  0.0263  131 LEU   C O   
2061 C CB  . LEU   B 125 ? 0.1913 0.2165 0.2648 0.0184  0.0202  0.0223  131 LEU   C CB  
2062 C CG  . LEU   B 125 ? 0.2218 0.2509 0.3058 0.0197  0.0222  0.0220  131 LEU   C CG  
2063 C CD1 . LEU   B 125 ? 0.2686 0.3019 0.3673 0.0181  0.0222  0.0219  131 LEU   C CD1 
2064 C CD2 . LEU   B 125 ? 0.2314 0.2608 0.3139 0.0211  0.0192  0.0193  131 LEU   C CD2 
2065 N N   . VAL   B 126 ? 0.1448 0.1616 0.1931 0.0173  0.0148  0.0211  132 VAL   C N   
2066 C CA  . VAL   B 126 ? 0.1387 0.1537 0.1820 0.0157  0.0122  0.0210  132 VAL   C CA  
2067 C C   . VAL   B 126 ? 0.1284 0.1455 0.1774 0.0147  0.0094  0.0186  132 VAL   C C   
2068 O O   . VAL   B 126 ? 0.1342 0.1521 0.1847 0.0156  0.0079  0.0163  132 VAL   C O   
2069 C CB  . VAL   B 126 ? 0.1515 0.1622 0.1835 0.0159  0.0107  0.0205  132 VAL   C CB  
2070 C CG1 . VAL   B 126 ? 0.1803 0.1898 0.2099 0.0173  0.0098  0.0182  132 VAL   C CG1 
2071 C CG2 . VAL   B 126 ? 0.1584 0.1679 0.1873 0.0140  0.0080  0.0204  132 VAL   C CG2 
2072 N N   . GLY   B 127 ? 0.1245 0.1421 0.1762 0.0132  0.0087  0.0191  133 GLY   C N   
2073 C CA  . GLY   B 127 ? 0.1245 0.1435 0.1805 0.0125  0.0064  0.0165  133 GLY   C CA  
2074 C C   . GLY   B 127 ? 0.1272 0.1440 0.1773 0.0116  0.0047  0.0163  133 GLY   C C   
2075 O O   . GLY   B 127 ? 0.1335 0.1492 0.1809 0.0108  0.0052  0.0186  133 GLY   C O   
2076 N N   . PHE   B 128 ? 0.1274 0.1438 0.1760 0.0118  0.0027  0.0137  134 PHE   C N   
2077 C CA  . PHE   B 128 ? 0.1217 0.1362 0.1654 0.0111  0.0015  0.0134  134 PHE   C CA  
2078 C C   . PHE   B 128 ? 0.1223 0.1377 0.1701 0.0108  0.0009  0.0114  134 PHE   C C   
2079 O O   . PHE   B 128 ? 0.1312 0.1476 0.1817 0.0115  -0.0002 0.0088  134 PHE   C O   
2080 C CB  . PHE   B 128 ? 0.1292 0.1413 0.1654 0.0121  0.0002  0.0123  134 PHE   C CB  
2081 C CG  . PHE   B 128 ? 0.1279 0.1384 0.1598 0.0129  0.0009  0.0135  134 PHE   C CG  
2082 C CD1 . PHE   B 128 ? 0.1382 0.1464 0.1650 0.0120  0.0012  0.0152  134 PHE   C CD1 
2083 C CD2 . PHE   B 128 ? 0.1380 0.1494 0.1713 0.0145  0.0011  0.0126  134 PHE   C CD2 
2084 C CE1 . PHE   B 128 ? 0.1508 0.1568 0.1726 0.0129  0.0019  0.0158  134 PHE   C CE1 
2085 C CE2 . PHE   B 128 ? 0.1456 0.1551 0.1747 0.0155  0.0022  0.0135  134 PHE   C CE2 
2086 C CZ  . PHE   B 128 ? 0.1535 0.1600 0.1764 0.0147  0.0027  0.0149  134 PHE   C CZ  
2087 N N   . ALA   B 129 ? 0.1237 0.1386 0.1720 0.0097  0.0015  0.0125  135 ALA   C N   
2088 C CA  . ALA   B 129 ? 0.1164 0.1313 0.1673 0.0096  0.0014  0.0105  135 ALA   C CA  
2089 C C   . ALA   B 129 ? 0.1351 0.1479 0.1789 0.0104  0.0005  0.0089  135 ALA   C C   
2090 O O   . ALA   B 129 ? 0.1351 0.1464 0.1744 0.0100  0.0009  0.0106  135 ALA   C O   
2091 C CB  . ALA   B 129 ? 0.1282 0.1433 0.1826 0.0086  0.0028  0.0127  135 ALA   C CB  
2092 N N   . ASP   B 130 ? 0.1336 0.1461 0.1764 0.0115  -0.0008 0.0058  136 ASP   C N   
2093 C CA  . ASP   B 130 ? 0.1420 0.1522 0.1772 0.0127  -0.0015 0.0046  136 ASP   C CA  
2094 C C   . ASP   B 130 ? 0.1510 0.1598 0.1850 0.0123  0.0004  0.0048  136 ASP   C C   
2095 O O   . ASP   B 130 ? 0.1526 0.1621 0.1919 0.0118  0.0015  0.0041  136 ASP   C O   
2096 C CB  . ASP   B 130 ? 0.1534 0.1638 0.1879 0.0141  -0.0038 0.0010  136 ASP   C CB  
2097 C CG  . ASP   B 130 ? 0.1855 0.1933 0.2111 0.0158  -0.0047 0.0000  136 ASP   C CG  
2098 O OD1 . ASP   B 130 ? 0.1876 0.1939 0.2081 0.0163  -0.0045 0.0020  136 ASP   C OD1 
2099 O OD2 . ASP   B 130 ? 0.2247 0.2313 0.2480 0.0167  -0.0053 -0.0027 136 ASP   C OD2 
2100 N N   . VAL   B 131 ? 0.1435 0.1499 0.1710 0.0127  0.0011  0.0059  137 VAL   C N   
2101 C CA  . VAL   B 131 ? 0.1465 0.1515 0.1725 0.0128  0.0034  0.0062  137 VAL   C CA  
2102 C C   . VAL   B 131 ? 0.1555 0.1576 0.1731 0.0146  0.0036  0.0048  137 VAL   C C   
2103 O O   . VAL   B 131 ? 0.1619 0.1623 0.1773 0.0150  0.0062  0.0050  137 VAL   C O   
2104 C CB  . VAL   B 131 ? 0.1528 0.1580 0.1808 0.0112  0.0052  0.0097  137 VAL   C CB  
2105 C CG1 . VAL   B 131 ? 0.1513 0.1592 0.1868 0.0097  0.0049  0.0112  137 VAL   C CG1 
2106 C CG2 . VAL   B 131 ? 0.1629 0.1663 0.1855 0.0110  0.0044  0.0113  137 VAL   C CG2 
2107 N N   . ARG   B 132 ? 0.1568 0.1582 0.1697 0.0160  0.0011  0.0034  138 ARG   C N   
2108 C CA  . ARG   B 132 ? 0.1596 0.1578 0.1633 0.0181  0.0010  0.0028  138 ARG   C CA  
2109 C C   . ARG   B 132 ? 0.1606 0.1575 0.1609 0.0196  0.0012  -0.0003 138 ARG   C C   
2110 O O   . ARG   B 132 ? 0.1838 0.1774 0.1755 0.0214  0.0023  -0.0003 138 ARG   C O   
2111 C CB  . ARG   B 132 ? 0.1535 0.1516 0.1538 0.0194  -0.0021 0.0025  138 ARG   C CB  
2112 C CG  . ARG   B 132 ? 0.1611 0.1591 0.1625 0.0184  -0.0019 0.0054  138 ARG   C CG  
2113 C CD  . ARG   B 132 ? 0.1606 0.1586 0.1596 0.0201  -0.0047 0.0049  138 ARG   C CD  
2114 N NE  . ARG   B 132 ? 0.1505 0.1522 0.1562 0.0200  -0.0069 0.0027  138 ARG   C NE  
2115 C CZ  . ARG   B 132 ? 0.1634 0.1665 0.1704 0.0212  -0.0093 0.0022  138 ARG   C CZ  
2116 N NH1 . ARG   B 132 ? 0.1756 0.1765 0.1767 0.0231  -0.0102 0.0033  138 ARG   C NH1 
2117 N NH2 . ARG   B 132 ? 0.1615 0.1683 0.1762 0.0208  -0.0106 0.0006  138 ARG   C NH2 
2118 N N   . ASP   B 133 ? 0.1552 0.1538 0.1615 0.0191  0.0004  -0.0031 139 ASP   C N   
2119 C CA  . ASP   B 133 ? 0.1732 0.1699 0.1760 0.0205  0.0006  -0.0067 139 ASP   C CA  
2120 C C   . ASP   B 133 ? 0.1790 0.1744 0.1832 0.0201  0.0053  -0.0057 139 ASP   C C   
2121 O O   . ASP   B 133 ? 0.2040 0.1968 0.2039 0.0215  0.0065  -0.0086 139 ASP   C O   
2122 C CB  . ASP   B 133 ? 0.1906 0.1894 0.2003 0.0199  -0.0024 -0.0104 139 ASP   C CB  
2123 C CG  . ASP   B 133 ? 0.2061 0.2075 0.2270 0.0176  -0.0007 -0.0091 139 ASP   C CG  
2124 O OD1 . ASP   B 133 ? 0.1934 0.1965 0.2177 0.0163  0.0006  -0.0053 139 ASP   C OD1 
2125 O OD2 . ASP   B 133 ? 0.2401 0.2414 0.2661 0.0172  -0.0005 -0.0120 139 ASP   C OD2 
2126 N N   . LEU   B 134 ? 0.1701 0.1670 0.1799 0.0183  0.0079  -0.0019 140 LEU   C N   
2127 C CA  . LEU   B 134 ? 0.1740 0.1706 0.1875 0.0179  0.0122  -0.0006 140 LEU   C CA  
2128 C C   . LEU   B 134 ? 0.1779 0.1717 0.1841 0.0190  0.0154  0.0015  140 LEU   C C   
2129 O O   . LEU   B 134 ? 0.1807 0.1753 0.1897 0.0177  0.0173  0.0053  140 LEU   C O   
2130 C CB  . LEU   B 134 ? 0.1660 0.1659 0.1894 0.0155  0.0126  0.0026  140 LEU   C CB  
2131 C CG  . LEU   B 134 ? 0.1693 0.1718 0.2002 0.0145  0.0100  0.0012  140 LEU   C CG  
2132 C CD1 . LEU   B 134 ? 0.1828 0.1883 0.2218 0.0124  0.0103  0.0050  140 LEU   C CD1 
2133 C CD2 . LEU   B 134 ? 0.1874 0.1890 0.2212 0.0152  0.0107  -0.0024 140 LEU   C CD2 
2134 N N   . LEU   B 135 ? 0.1948 0.1850 0.1913 0.0215  0.0161  -0.0009 141 LEU   C N   
2135 C CA  . LEU   B 135 ? 0.2114 0.1984 0.1995 0.0230  0.0193  0.0014  141 LEU   C CA  
2136 C C   . LEU   B 135 ? 0.2015 0.1884 0.1939 0.0225  0.0250  0.0041  141 LEU   C C   
2137 O O   . LEU   B 135 ? 0.2150 0.2007 0.2053 0.0224  0.0279  0.0077  141 LEU   C O   
2138 C CB  . LEU   B 135 ? 0.2222 0.2051 0.1977 0.0261  0.0187  -0.0017 141 LEU   C CB  
2139 C CG  . LEU   B 135 ? 0.2878 0.2697 0.2553 0.0275  0.0139  -0.0024 141 LEU   C CG  
2140 C CD1 . LEU   B 135 ? 0.2631 0.2487 0.2375 0.0258  0.0091  -0.0027 141 LEU   C CD1 
2141 C CD2 . LEU   B 135 ? 0.3153 0.2941 0.2726 0.0304  0.0116  -0.0070 141 LEU   C CD2 
2142 N N   . TRP   B 136 ? 0.1972 0.1855 0.1969 0.0220  0.0267  0.0026  142 TRP   C N   
2143 C CA  . TRP   B 136 ? 0.2018 0.1907 0.2075 0.0218  0.0322  0.0051  142 TRP   C CA  
2144 C C   . TRP   B 136 ? 0.2073 0.1996 0.2218 0.0191  0.0323  0.0099  142 TRP   C C   
2145 O O   . TRP   B 136 ? 0.2259 0.2190 0.2454 0.0188  0.0368  0.0128  142 TRP   C O   
2146 C CB  . TRP   B 136 ? 0.2019 0.1914 0.2139 0.0221  0.0334  0.0024  142 TRP   C CB  
2147 C CG  . TRP   B 136 ? 0.1974 0.1903 0.2179 0.0202  0.0291  0.0014  142 TRP   C CG  
2148 C CD1 . TRP   B 136 ? 0.2140 0.2064 0.2330 0.0205  0.0252  -0.0027 142 TRP   C CD1 
2149 C CD2 . TRP   B 136 ? 0.1955 0.1927 0.2277 0.0178  0.0284  0.0047  142 TRP   C CD2 
2150 N NE1 . TRP   B 136 ? 0.2147 0.2107 0.2439 0.0184  0.0227  -0.0018 142 TRP   C NE1 
2151 C CE2 . TRP   B 136 ? 0.2083 0.2071 0.2450 0.0170  0.0247  0.0027  142 TRP   C CE2 
2152 C CE3 . TRP   B 136 ? 0.2052 0.2051 0.2449 0.0165  0.0307  0.0091  142 TRP   C CE3 
2153 C CZ2 . TRP   B 136 ? 0.2135 0.2159 0.2600 0.0150  0.0232  0.0054  142 TRP   C CZ2 
2154 C CZ3 . TRP   B 136 ? 0.2130 0.2168 0.2627 0.0145  0.0285  0.0113  142 TRP   C CZ3 
2155 C CH2 . TRP   B 136 ? 0.2152 0.2200 0.2675 0.0139  0.0250  0.0096  142 TRP   C CH2 
2156 N N   . LEU   B 137 ? 0.1934 0.1880 0.2105 0.0172  0.0276  0.0107  143 LEU   C N   
2157 C CA  . LEU   B 137 ? 0.2001 0.1973 0.2241 0.0146  0.0272  0.0147  143 LEU   C CA  
2158 C C   . LEU   B 137 ? 0.2400 0.2348 0.2596 0.0148  0.0301  0.0175  143 LEU   C C   
2159 O O   . LEU   B 137 ? 0.2584 0.2550 0.2850 0.0127  0.0311  0.0208  143 LEU   C O   
2160 C CB  . LEU   B 137 ? 0.1854 0.1844 0.2104 0.0131  0.0220  0.0146  143 LEU   C CB  
2161 C CG  . LEU   B 137 ? 0.1853 0.1871 0.2169 0.0123  0.0196  0.0132  143 LEU   C CG  
2162 C CD1 . LEU   B 137 ? 0.1995 0.2022 0.2298 0.0114  0.0152  0.0129  143 LEU   C CD1 
2163 C CD2 . LEU   B 137 ? 0.2024 0.2076 0.2448 0.0107  0.0207  0.0159  143 LEU   C CD2 
2164 N N   . ASP   B 138 ? 0.2343 0.2249 0.2426 0.0171  0.0312  0.0164  144 ASP   C N   
2165 C CA  . ASP   B 138 ? 0.2608 0.2484 0.2641 0.0175  0.0342  0.0194  144 ASP   C CA  
2166 C C   . ASP   B 138 ? 0.2989 0.2852 0.3030 0.0186  0.0409  0.0213  144 ASP   C C   
2167 O O   . ASP   B 138 ? 0.3153 0.2989 0.3158 0.0190  0.0443  0.0242  144 ASP   C O   
2168 C CB  . ASP   B 138 ? 0.2647 0.2482 0.2549 0.0200  0.0325  0.0180  144 ASP   C CB  
2169 C CG  . ASP   B 138 ? 0.2720 0.2564 0.2609 0.0193  0.0265  0.0167  144 ASP   C CG  
2170 O OD1 . ASP   B 138 ? 0.2795 0.2670 0.2765 0.0167  0.0241  0.0175  144 ASP   C OD1 
2171 O OD2 . ASP   B 138 ? 0.2990 0.2809 0.2786 0.0216  0.0242  0.0148  144 ASP   C OD2 
2172 N N   . GLU   B 139 ? 0.3074 0.2953 0.3164 0.0193  0.0434  0.0198  145 GLU   C N   
2173 C CA  . GLU   B 139 ? 0.3655 0.3519 0.3750 0.0209  0.0505  0.0213  145 GLU   C CA  
2174 C C   . GLU   B 139 ? 0.4137 0.4043 0.4368 0.0198  0.0529  0.0220  145 GLU   C C   
2175 O O   . GLU   B 139 ? 0.4152 0.4097 0.4468 0.0178  0.0487  0.0215  145 GLU   C O   
2176 C CB  . GLU   B 139 ? 0.4406 0.4222 0.4366 0.0247  0.0522  0.0176  145 GLU   C CB  
2177 C CG  . GLU   B 139 ? 0.5478 0.5304 0.5450 0.0252  0.0489  0.0127  145 GLU   C CG  
2178 C CD  . GLU   B 139 ? 0.6590 0.6373 0.6428 0.0282  0.0474  0.0079  145 GLU   C CD  
2179 O OE1 . GLU   B 139 ? 0.6767 0.6550 0.6621 0.0289  0.0464  0.0039  145 GLU   C OE1 
2180 O OE2 . GLU   B 139 ? 0.6808 0.6555 0.6527 0.0299  0.0469  0.0082  145 GLU   C OE2 
2181 N N   . GLU   B 140 ? 0.4499 0.4393 0.4743 0.0216  0.0599  0.0231  146 GLU   C N   
2182 C CA  . GLU   B 140 ? 0.4762 0.4685 0.5117 0.0219  0.0636  0.0233  146 GLU   C CA  
2183 C C   . GLU   B 140 ? 0.4827 0.4812 0.5341 0.0187  0.0611  0.0263  146 GLU   C C   
2184 O O   . GLU   B 140 ? 0.4873 0.4887 0.5468 0.0184  0.0595  0.0252  146 GLU   C O   
2185 C CB  . GLU   B 140 ? 0.5224 0.5129 0.5533 0.0240  0.0624  0.0180  146 GLU   C CB  
2186 C CG  . GLU   B 140 ? 0.6262 0.6186 0.6673 0.0249  0.0659  0.0173  146 GLU   C CG  
2187 C CD  . GLU   B 140 ? 0.7369 0.7300 0.7850 0.0260  0.0739  0.0206  146 GLU   C CD  
2188 O OE1 . GLU   B 140 ? 0.7551 0.7533 0.8184 0.0244  0.0745  0.0236  146 GLU   C OE1 
2189 O OE2 . GLU   B 140 ? 0.7838 0.7723 0.8222 0.0287  0.0797  0.0204  146 GLU   C OE2 
2190 N N1  . A1BO8 C .   ? 0.2648 0.2544 0.3262 0.0335  0.0223  0.0057  201 A1BO8 A N1  
2191 C C4  . A1BO8 C .   ? 0.3134 0.2862 0.3596 0.0243  0.0407  -0.0235 201 A1BO8 A C4  
2192 C C5  . A1BO8 C .   ? 0.3103 0.2829 0.3517 0.0228  0.0343  -0.0209 201 A1BO8 A C5  
2193 C C6  . A1BO8 C .   ? 0.2936 0.2667 0.3456 0.0277  0.0331  -0.0136 201 A1BO8 A C6  
2194 C C7  . A1BO8 C .   ? 0.2941 0.2760 0.3516 0.0316  0.0308  -0.0065 201 A1BO8 A C7  
2195 C C8  . A1BO8 C .   ? 0.2825 0.2672 0.3494 0.0351  0.0287  0.0019  201 A1BO8 A C8  
2196 C C10 . A1BO8 C .   ? 0.3916 0.3705 0.4263 0.0187  0.0452  -0.0318 201 A1BO8 A C10 
2197 C C13 . A1BO8 C .   ? 0.4216 0.4137 0.4621 0.0228  0.0459  -0.0267 201 A1BO8 A C13 
2198 O O2  . A1BO8 C .   ? 0.2939 0.2760 0.3730 0.0388  0.0332  0.0051  201 A1BO8 A O2  
2199 C C9  . A1BO8 C .   ? 0.3056 0.2883 0.3690 0.0335  0.0368  -0.0085 201 A1BO8 A C9  
2200 N N   . A1BO8 C .   ? 0.3205 0.3014 0.3730 0.0287  0.0383  -0.0164 201 A1BO8 A N   
2201 C C3  . A1BO8 C .   ? 0.3330 0.3201 0.3812 0.0278  0.0370  -0.0164 201 A1BO8 A C3  
2202 O O1  . A1BO8 C .   ? 0.2967 0.2908 0.3510 0.0310  0.0355  -0.0106 201 A1BO8 A O1  
2203 C C2  . A1BO8 C .   ? 0.3849 0.3715 0.4207 0.0220  0.0375  -0.0233 201 A1BO8 A C2  
2204 C C1  . A1BO8 C .   ? 0.3999 0.3882 0.4241 0.0181  0.0301  -0.0227 201 A1BO8 A C1  
2205 O O   . A1BO8 C .   ? 0.3933 0.3876 0.4184 0.0205  0.0246  -0.0162 201 A1BO8 A O   
2206 C C   . A1BO8 C .   ? 0.3565 0.3534 0.3721 0.0170  0.0197  -0.0160 201 A1BO8 A C   
2207 O O3  . A1BO8 C .   ? 0.4194 0.4124 0.4555 0.0227  0.0380  -0.0221 201 A1BO8 A O3  
2208 C C12 . A1BO8 C .   ? 0.4158 0.4006 0.4680 0.0256  0.0543  -0.0294 201 A1BO8 A C12 
2209 C C11 . A1BO8 C .   ? 0.3999 0.3765 0.4481 0.0230  0.0542  -0.0329 201 A1BO8 A C11 
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