data_7HVU
# 
_entry.id   7HVU 
# 
_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   7HVU         pdb_00007hvu 10.2210/pdb7hvu/pdb 
WWPDB D_1001407994 ?            ?                   
# 
_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                        7HVU 
_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-{[4-(3,5-dichlorophenyl)-1-methyl-1H-pyrazol-5-yl]acetyl}piperidine-3-carboxamide' 395.283   1   ? ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                                 65.409    2   ? ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                       78.133    1   ? ? ? ? 
5 water       nat water                                                                                      18.015    316 ? ? ? ? 
# 
_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-{[4-(3,5-dichlorophenyl)-1-methyl-1H-pyrazol-5-yl]acetyl}piperidine-3-carboxamide' A1BPY 
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 
A1BPY non-polymer         . '(3S)-1-{[4-(3,5-dichlorophenyl)-1-methyl-1H-pyrazol-5-yl]acetyl}piperidine-3-carboxamide' ? 
'C18 H20 Cl2 N4 O2' 395.283 
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        A1BPY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BPY 
_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 A1BPY 1   201 201 A1BPY LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 3 ZN    1   201 1   ZN    ZN  C . 
F 4 DMS   1   202 1   DMS   DMS C . 
G 5 HOH   1   301 232 HOH   HOH A . 
G 5 HOH   2   302 118 HOH   HOH A . 
G 5 HOH   3   303 203 HOH   HOH A . 
G 5 HOH   4   304 105 HOH   HOH A . 
G 5 HOH   5   305 233 HOH   HOH A . 
G 5 HOH   6   306 182 HOH   HOH A . 
G 5 HOH   7   307 214 HOH   HOH A . 
G 5 HOH   8   308 140 HOH   HOH A . 
G 5 HOH   9   309 108 HOH   HOH A . 
G 5 HOH   10  310 159 HOH   HOH A . 
G 5 HOH   11  311 130 HOH   HOH A . 
G 5 HOH   12  312 27  HOH   HOH A . 
G 5 HOH   13  313 234 HOH   HOH A . 
G 5 HOH   14  314 253 HOH   HOH A . 
G 5 HOH   15  315 150 HOH   HOH A . 
G 5 HOH   16  316 163 HOH   HOH A . 
G 5 HOH   17  317 93  HOH   HOH A . 
G 5 HOH   18  318 114 HOH   HOH A . 
G 5 HOH   19  319 249 HOH   HOH A . 
G 5 HOH   20  320 191 HOH   HOH A . 
G 5 HOH   21  321 248 HOH   HOH A . 
G 5 HOH   22  322 71  HOH   HOH A . 
G 5 HOH   23  323 152 HOH   HOH A . 
G 5 HOH   24  324 87  HOH   HOH A . 
G 5 HOH   25  325 146 HOH   HOH A . 
G 5 HOH   26  326 57  HOH   HOH A . 
G 5 HOH   27  327 138 HOH   HOH A . 
G 5 HOH   28  328 302 HOH   HOH A . 
G 5 HOH   29  329 92  HOH   HOH A . 
G 5 HOH   30  330 119 HOH   HOH A . 
G 5 HOH   31  331 144 HOH   HOH A . 
G 5 HOH   32  332 98  HOH   HOH A . 
G 5 HOH   33  333 134 HOH   HOH A . 
G 5 HOH   34  334 63  HOH   HOH A . 
G 5 HOH   35  335 126 HOH   HOH A . 
G 5 HOH   36  336 172 HOH   HOH A . 
G 5 HOH   37  337 156 HOH   HOH A . 
G 5 HOH   38  338 2   HOH   HOH A . 
G 5 HOH   39  339 39  HOH   HOH A . 
G 5 HOH   40  340 153 HOH   HOH A . 
G 5 HOH   41  341 245 HOH   HOH A . 
G 5 HOH   42  342 13  HOH   HOH A . 
G 5 HOH   43  343 227 HOH   HOH A . 
G 5 HOH   44  344 276 HOH   HOH A . 
G 5 HOH   45  345 28  HOH   HOH A . 
G 5 HOH   46  346 113 HOH   HOH A . 
G 5 HOH   47  347 165 HOH   HOH A . 
G 5 HOH   48  348 251 HOH   HOH A . 
G 5 HOH   49  349 64  HOH   HOH A . 
G 5 HOH   50  350 53  HOH   HOH A . 
G 5 HOH   51  351 40  HOH   HOH A . 
G 5 HOH   52  352 185 HOH   HOH A . 
G 5 HOH   53  353 169 HOH   HOH A . 
G 5 HOH   54  354 47  HOH   HOH A . 
G 5 HOH   55  355 196 HOH   HOH A . 
G 5 HOH   56  356 299 HOH   HOH A . 
G 5 HOH   57  357 99  HOH   HOH A . 
G 5 HOH   58  358 246 HOH   HOH A . 
G 5 HOH   59  359 258 HOH   HOH A . 
G 5 HOH   60  360 111 HOH   HOH A . 
G 5 HOH   61  361 128 HOH   HOH A . 
G 5 HOH   62  362 30  HOH   HOH A . 
G 5 HOH   63  363 131 HOH   HOH A . 
G 5 HOH   64  364 96  HOH   HOH A . 
G 5 HOH   65  365 65  HOH   HOH A . 
G 5 HOH   66  366 79  HOH   HOH A . 
G 5 HOH   67  367 72  HOH   HOH A . 
G 5 HOH   68  368 25  HOH   HOH A . 
G 5 HOH   69  369 193 HOH   HOH A . 
G 5 HOH   70  370 166 HOH   HOH A . 
G 5 HOH   71  371 31  HOH   HOH A . 
G 5 HOH   72  372 58  HOH   HOH A . 
G 5 HOH   73  373 60  HOH   HOH A . 
G 5 HOH   74  374 257 HOH   HOH A . 
G 5 HOH   75  375 270 HOH   HOH A . 
G 5 HOH   76  376 1   HOH   HOH A . 
G 5 HOH   77  377 123 HOH   HOH A . 
G 5 HOH   78  378 85  HOH   HOH A . 
G 5 HOH   79  379 275 HOH   HOH A . 
G 5 HOH   80  380 82  HOH   HOH A . 
G 5 HOH   81  381 308 HOH   HOH A . 
G 5 HOH   82  382 23  HOH   HOH A . 
G 5 HOH   83  383 289 HOH   HOH A . 
G 5 HOH   84  384 43  HOH   HOH A . 
G 5 HOH   85  385 226 HOH   HOH A . 
G 5 HOH   86  386 314 HOH   HOH A . 
G 5 HOH   87  387 107 HOH   HOH A . 
G 5 HOH   88  388 301 HOH   HOH A . 
G 5 HOH   89  389 213 HOH   HOH A . 
G 5 HOH   90  390 210 HOH   HOH A . 
G 5 HOH   91  391 261 HOH   HOH A . 
G 5 HOH   92  392 11  HOH   HOH A . 
G 5 HOH   93  393 162 HOH   HOH A . 
G 5 HOH   94  394 148 HOH   HOH A . 
G 5 HOH   95  395 19  HOH   HOH A . 
G 5 HOH   96  396 164 HOH   HOH A . 
G 5 HOH   97  397 290 HOH   HOH A . 
G 5 HOH   98  398 177 HOH   HOH A . 
G 5 HOH   99  399 266 HOH   HOH A . 
G 5 HOH   100 400 180 HOH   HOH A . 
G 5 HOH   101 401 49  HOH   HOH A . 
G 5 HOH   102 402 127 HOH   HOH A . 
G 5 HOH   103 403 294 HOH   HOH A . 
G 5 HOH   104 404 240 HOH   HOH A . 
G 5 HOH   105 405 121 HOH   HOH A . 
G 5 HOH   106 406 48  HOH   HOH A . 
G 5 HOH   107 407 229 HOH   HOH A . 
G 5 HOH   108 408 78  HOH   HOH A . 
G 5 HOH   109 409 122 HOH   HOH A . 
G 5 HOH   110 410 95  HOH   HOH A . 
G 5 HOH   111 411 139 HOH   HOH A . 
G 5 HOH   112 412 224 HOH   HOH A . 
G 5 HOH   113 413 5   HOH   HOH A . 
G 5 HOH   114 414 183 HOH   HOH A . 
G 5 HOH   115 415 237 HOH   HOH A . 
G 5 HOH   116 416 66  HOH   HOH A . 
G 5 HOH   117 417 247 HOH   HOH A . 
G 5 HOH   118 418 36  HOH   HOH A . 
G 5 HOH   119 419 167 HOH   HOH A . 
G 5 HOH   120 420 147 HOH   HOH A . 
G 5 HOH   121 421 44  HOH   HOH A . 
G 5 HOH   122 422 103 HOH   HOH A . 
G 5 HOH   123 423 306 HOH   HOH A . 
G 5 HOH   124 424 284 HOH   HOH A . 
G 5 HOH   125 425 69  HOH   HOH A . 
G 5 HOH   126 426 296 HOH   HOH A . 
G 5 HOH   127 427 135 HOH   HOH A . 
G 5 HOH   128 428 239 HOH   HOH A . 
G 5 HOH   129 429 223 HOH   HOH A . 
G 5 HOH   130 430 243 HOH   HOH A . 
G 5 HOH   131 431 250 HOH   HOH A . 
G 5 HOH   132 432 254 HOH   HOH A . 
G 5 HOH   133 433 221 HOH   HOH A . 
G 5 HOH   134 434 217 HOH   HOH A . 
G 5 HOH   135 435 184 HOH   HOH A . 
G 5 HOH   136 436 170 HOH   HOH A . 
G 5 HOH   137 437 317 HOH   HOH A . 
G 5 HOH   138 438 199 HOH   HOH A . 
G 5 HOH   139 439 220 HOH   HOH A . 
G 5 HOH   140 440 133 HOH   HOH A . 
G 5 HOH   141 441 149 HOH   HOH A . 
G 5 HOH   142 442 260 HOH   HOH A . 
G 5 HOH   143 443 215 HOH   HOH A . 
G 5 HOH   144 444 205 HOH   HOH A . 
G 5 HOH   145 445 225 HOH   HOH A . 
G 5 HOH   146 446 235 HOH   HOH A . 
G 5 HOH   147 447 70  HOH   HOH A . 
G 5 HOH   148 448 236 HOH   HOH A . 
G 5 HOH   149 449 115 HOH   HOH A . 
G 5 HOH   150 450 179 HOH   HOH A . 
G 5 HOH   151 451 242 HOH   HOH A . 
G 5 HOH   152 452 256 HOH   HOH A . 
G 5 HOH   153 453 263 HOH   HOH A . 
G 5 HOH   154 454 255 HOH   HOH A . 
G 5 HOH   155 455 230 HOH   HOH A . 
G 5 HOH   156 456 211 HOH   HOH A . 
G 5 HOH   157 457 309 HOH   HOH A . 
G 5 HOH   158 458 155 HOH   HOH A . 
G 5 HOH   159 459 222 HOH   HOH A . 
G 5 HOH   160 460 219 HOH   HOH A . 
H 5 HOH   1   301 161 HOH   HOH C . 
H 5 HOH   2   302 297 HOH   HOH C . 
H 5 HOH   3   303 142 HOH   HOH C . 
H 5 HOH   4   304 160 HOH   HOH C . 
H 5 HOH   5   305 67  HOH   HOH C . 
H 5 HOH   6   306 50  HOH   HOH C . 
H 5 HOH   7   307 32  HOH   HOH C . 
H 5 HOH   8   308 241 HOH   HOH C . 
H 5 HOH   9   309 45  HOH   HOH C . 
H 5 HOH   10  310 81  HOH   HOH C . 
H 5 HOH   11  311 80  HOH   HOH C . 
H 5 HOH   12  312 259 HOH   HOH C . 
H 5 HOH   13  313 287 HOH   HOH C . 
H 5 HOH   14  314 238 HOH   HOH C . 
H 5 HOH   15  315 244 HOH   HOH C . 
H 5 HOH   16  316 188 HOH   HOH C . 
H 5 HOH   17  317 181 HOH   HOH C . 
H 5 HOH   18  318 112 HOH   HOH C . 
H 5 HOH   19  319 46  HOH   HOH C . 
H 5 HOH   20  320 209 HOH   HOH C . 
H 5 HOH   21  321 84  HOH   HOH C . 
H 5 HOH   22  322 271 HOH   HOH C . 
H 5 HOH   23  323 262 HOH   HOH C . 
H 5 HOH   24  324 202 HOH   HOH C . 
H 5 HOH   25  325 10  HOH   HOH C . 
H 5 HOH   26  326 285 HOH   HOH C . 
H 5 HOH   27  327 106 HOH   HOH C . 
H 5 HOH   28  328 208 HOH   HOH C . 
H 5 HOH   29  329 305 HOH   HOH C . 
H 5 HOH   30  330 313 HOH   HOH C . 
H 5 HOH   31  331 91  HOH   HOH C . 
H 5 HOH   32  332 42  HOH   HOH C . 
H 5 HOH   33  333 68  HOH   HOH C . 
H 5 HOH   34  334 278 HOH   HOH C . 
H 5 HOH   35  335 300 HOH   HOH C . 
H 5 HOH   36  336 286 HOH   HOH C . 
H 5 HOH   37  337 158 HOH   HOH C . 
H 5 HOH   38  338 189 HOH   HOH C . 
H 5 HOH   39  339 310 HOH   HOH C . 
H 5 HOH   40  340 129 HOH   HOH C . 
H 5 HOH   41  341 200 HOH   HOH C . 
H 5 HOH   42  342 194 HOH   HOH C . 
H 5 HOH   43  343 212 HOH   HOH C . 
H 5 HOH   44  344 252 HOH   HOH C . 
H 5 HOH   45  345 59  HOH   HOH C . 
H 5 HOH   46  346 76  HOH   HOH C . 
H 5 HOH   47  347 204 HOH   HOH C . 
H 5 HOH   48  348 9   HOH   HOH C . 
H 5 HOH   49  349 12  HOH   HOH C . 
H 5 HOH   50  350 281 HOH   HOH C . 
H 5 HOH   51  351 6   HOH   HOH C . 
H 5 HOH   52  352 77  HOH   HOH C . 
H 5 HOH   53  353 21  HOH   HOH C . 
H 5 HOH   54  354 168 HOH   HOH C . 
H 5 HOH   55  355 186 HOH   HOH C . 
H 5 HOH   56  356 136 HOH   HOH C . 
H 5 HOH   57  357 4   HOH   HOH C . 
H 5 HOH   58  358 268 HOH   HOH C . 
H 5 HOH   59  359 132 HOH   HOH C . 
H 5 HOH   60  360 17  HOH   HOH C . 
H 5 HOH   61  361 38  HOH   HOH C . 
H 5 HOH   62  362 51  HOH   HOH C . 
H 5 HOH   63  363 231 HOH   HOH C . 
H 5 HOH   64  364 33  HOH   HOH C . 
H 5 HOH   65  365 154 HOH   HOH C . 
H 5 HOH   66  366 29  HOH   HOH C . 
H 5 HOH   67  367 293 HOH   HOH C . 
H 5 HOH   68  368 18  HOH   HOH C . 
H 5 HOH   69  369 273 HOH   HOH C . 
H 5 HOH   70  370 187 HOH   HOH C . 
H 5 HOH   71  371 54  HOH   HOH C . 
H 5 HOH   72  372 26  HOH   HOH C . 
H 5 HOH   73  373 116 HOH   HOH C . 
H 5 HOH   74  374 141 HOH   HOH C . 
H 5 HOH   75  375 100 HOH   HOH C . 
H 5 HOH   76  376 16  HOH   HOH C . 
H 5 HOH   77  377 55  HOH   HOH C . 
H 5 HOH   78  378 94  HOH   HOH C . 
H 5 HOH   79  379 73  HOH   HOH C . 
H 5 HOH   80  380 15  HOH   HOH C . 
H 5 HOH   81  381 56  HOH   HOH C . 
H 5 HOH   82  382 157 HOH   HOH C . 
H 5 HOH   83  383 295 HOH   HOH C . 
H 5 HOH   84  384 192 HOH   HOH C . 
H 5 HOH   85  385 282 HOH   HOH C . 
H 5 HOH   86  386 171 HOH   HOH C . 
H 5 HOH   87  387 277 HOH   HOH C . 
H 5 HOH   88  388 62  HOH   HOH C . 
H 5 HOH   89  389 3   HOH   HOH C . 
H 5 HOH   90  390 315 HOH   HOH C . 
H 5 HOH   91  391 124 HOH   HOH C . 
H 5 HOH   92  392 8   HOH   HOH C . 
H 5 HOH   93  393 41  HOH   HOH C . 
H 5 HOH   94  394 176 HOH   HOH C . 
H 5 HOH   95  395 24  HOH   HOH C . 
H 5 HOH   96  396 291 HOH   HOH C . 
H 5 HOH   97  397 37  HOH   HOH C . 
H 5 HOH   98  398 101 HOH   HOH C . 
H 5 HOH   99  399 34  HOH   HOH C . 
H 5 HOH   100 400 61  HOH   HOH C . 
H 5 HOH   101 401 52  HOH   HOH C . 
H 5 HOH   102 402 22  HOH   HOH C . 
H 5 HOH   103 403 292 HOH   HOH C . 
H 5 HOH   104 404 307 HOH   HOH C . 
H 5 HOH   105 405 269 HOH   HOH C . 
H 5 HOH   106 406 83  HOH   HOH C . 
H 5 HOH   107 407 75  HOH   HOH C . 
H 5 HOH   108 408 137 HOH   HOH C . 
H 5 HOH   109 409 288 HOH   HOH C . 
H 5 HOH   110 410 265 HOH   HOH C . 
H 5 HOH   111 411 304 HOH   HOH C . 
H 5 HOH   112 412 20  HOH   HOH C . 
H 5 HOH   113 413 110 HOH   HOH C . 
H 5 HOH   114 414 274 HOH   HOH C . 
H 5 HOH   115 415 104 HOH   HOH C . 
H 5 HOH   116 416 102 HOH   HOH C . 
H 5 HOH   117 417 35  HOH   HOH C . 
H 5 HOH   118 418 264 HOH   HOH C . 
H 5 HOH   119 419 74  HOH   HOH C . 
H 5 HOH   120 420 272 HOH   HOH C . 
H 5 HOH   121 421 316 HOH   HOH C . 
H 5 HOH   122 422 120 HOH   HOH C . 
H 5 HOH   123 423 173 HOH   HOH C . 
H 5 HOH   124 424 90  HOH   HOH C . 
H 5 HOH   125 425 145 HOH   HOH C . 
H 5 HOH   126 426 151 HOH   HOH C . 
H 5 HOH   127 427 7   HOH   HOH C . 
H 5 HOH   128 428 279 HOH   HOH C . 
H 5 HOH   129 429 97  HOH   HOH C . 
H 5 HOH   130 430 303 HOH   HOH C . 
H 5 HOH   131 431 174 HOH   HOH C . 
H 5 HOH   132 432 109 HOH   HOH C . 
H 5 HOH   133 433 298 HOH   HOH C . 
H 5 HOH   134 434 125 HOH   HOH C . 
H 5 HOH   135 435 198 HOH   HOH C . 
H 5 HOH   136 436 267 HOH   HOH C . 
H 5 HOH   137 437 216 HOH   HOH C . 
H 5 HOH   138 438 311 HOH   HOH C . 
H 5 HOH   139 439 89  HOH   HOH C . 
H 5 HOH   140 440 190 HOH   HOH C . 
H 5 HOH   141 441 88  HOH   HOH C . 
H 5 HOH   142 442 312 HOH   HOH C . 
H 5 HOH   143 443 201 HOH   HOH C . 
H 5 HOH   144 444 178 HOH   HOH C . 
H 5 HOH   145 445 283 HOH   HOH C . 
H 5 HOH   146 446 207 HOH   HOH C . 
H 5 HOH   147 447 206 HOH   HOH C . 
H 5 HOH   148 448 318 HOH   HOH C . 
H 5 HOH   149 449 86  HOH   HOH C . 
H 5 HOH   150 450 280 HOH   HOH C . 
H 5 HOH   151 451 197 HOH   HOH C . 
H 5 HOH   152 452 218 HOH   HOH C . 
H 5 HOH   153 453 195 HOH   HOH C . 
H 5 HOH   154 454 175 HOH   HOH C . 
H 5 HOH   155 455 228 HOH   HOH C . 
H 5 HOH   156 456 117 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           7HVU 
_cell.length_a           86.908 
_cell.length_b           57.558 
_cell.length_c           64.920 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.61 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HVU 
_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          7HVU 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.55 
_exptl_crystal.density_percent_sol   51.69 
_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   2024-11-14 
_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   0.92201 
_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        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HVU 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             43.31 
_reflns.d_resolution_high            1.43 
_reflns.number_obs                   58969 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.105 
_reflns.pdbx_netI_over_sigmaI        10.2 
_reflns.pdbx_redundancy              6.4 
_reflns.pdbx_Rrim_I_all              0.115 
_reflns.pdbx_Rpim_I_all              0.046 
_reflns.pdbx_CC_half                 0.960 
_reflns.pdbx_number_measured_all     377329 
_reflns.pdbx_chi_squared             0.51 
_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                  1.43 
_reflns_shell.d_res_low                   1.45 
_reflns_shell.number_measured_all         13060 
_reflns_shell.number_unique_obs           2822 
_reflns_shell.Rmerge_I_obs                1.930 
_reflns_shell.pdbx_chi_squared            0.18 
_reflns_shell.pdbx_redundancy             4.6 
_reflns_shell.percent_possible_obs        96.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.4 
_reflns_shell.pdbx_Rrim_I_all             2.178 
_reflns_shell.pdbx_Rpim_I_all             0.995 
_reflns_shell.pdbx_CC_half                0.365 
_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                                 7HVU 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     58709 
_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                             20.92 
_refine.ls_d_res_high                            1.429 
_refine.ls_percent_reflns_obs                    99.2 
_refine.ls_R_factor_obs                          0.2023 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2015 
_refine.ls_R_factor_R_free                       0.2180 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.950 
_refine.ls_number_reflns_R_free                  2908 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.947 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_refine.B_iso_mean                               25.16 
_refine.aniso_B[1][1]                            -1.22470 
_refine.aniso_B[2][2]                            -4.52000 
_refine.aniso_B[3][3]                            5.74470 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.61600 
_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             0.066 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.065 
_refine.pdbx_overall_SU_R_Blow_DPI               0.069 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.067 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HVU 
_refine_analyze.Luzzati_coordinate_error_obs    0.20 
_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         32 
_refine_hist.number_atoms_solvent             316 
_refine_hist.number_atoms_total               2514 
_refine_hist.d_res_high                       1.429 
_refine_hist.d_res_low                        20.92 
# 
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                  0.011 ? 2.00  2287 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.02  ? 2.00  3123 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  769  '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  420  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2287 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.26  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.28 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  282  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  2054 '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                       1.43 
_refine_ls_shell.d_res_low                        1.44 
_refine_ls_shell.number_reflns_R_work             1117 
_refine_ls_shell.R_factor_R_work                  0.3699 
_refine_ls_shell.percent_reflns_obs               81.76 
_refine_ls_shell.R_factor_R_free                  0.4511 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.94 
_refine_ls_shell.number_reflns_R_free             58 
_refine_ls_shell.number_reflns_all                1175 
_refine_ls_shell.R_factor_all                     0.3739 
# 
_struct.entry_id                  7HVU 
_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-0032503-001 (A71EV2A-x3606)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HVU 
_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 3 ? 
F N N 4 ? 
G N N 5 ? 
H 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 7HVU A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HVU 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,G 
2 1 B,E,F,H 
# 
_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 ? ? ? ? ? ? ? 2.362 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.311 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 E ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.080 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 109.5 ? 
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_555 105.5 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.6 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 104.9 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 103.2 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 117.5 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 110.8 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.1 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 116.8 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 106.3 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.4 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 115.1 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O VAL A 68  ? O VAL A 74  N GLY A 55  ? N GLY A 61  
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                   7HVU 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    408 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    430 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -131.64 
_pdbx_validate_torsion.psi             -31.08 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 14.7976 8.1751   14.3870 -0.0336 -0.0597 0.0518 0.0102 0.0246 0.0076 1.4321 0.6733 0.7071 0.7663 
-0.2766 -0.2066 -0.0049 0.0824 0.1229 0.0339 0.0535 0.0092 -0.0178 -0.0531 -0.0487 
'X-RAY DIFFRACTION' 2 ? refined 25.9148 -20.3202 17.8208 -0.0415 -0.0565 0.0644 0.0039 0.0234 0.0287 0.8296 0.7639 0.5478 0.0301 
-0.0822 -0.1697 0.0281  0.0185 0.1403 0.0065 0.0518 0.0603 0.0529  0.0158  -0.0799 
# 
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 
A1BPY N1   N  Y N 1   
A1BPY N3   N  N N 2   
A1BPY C4   C  Y N 3   
A1BPY C5   C  Y N 4   
A1BPY C6   C  Y N 5   
A1BPY C7   C  Y N 6   
A1BPY C8   C  Y N 7   
A1BPY C10  C  N N 8   
A1BPY C13  C  N N 9   
A1BPY C15  C  N S 10  
A1BPY C17  C  N N 11  
A1BPY O1   O  N N 12  
A1BPY C16  C  N N 13  
A1BPY C14  C  N N 14  
A1BPY C12  C  N N 15  
A1BPY N2   N  N N 16  
A1BPY C11  C  N N 17  
A1BPY O    O  N N 18  
A1BPY C9   C  Y N 19  
A1BPY N    N  Y N 20  
A1BPY C    C  N N 21  
A1BPY C2   C  Y N 22  
A1BPY C1   C  Y N 23  
A1BPY C3   C  Y N 24  
A1BPY CL1  CL N N 25  
A1BPY CL   CL N N 26  
A1BPY H17  H  N N 27  
A1BPY H16  H  N N 28  
A1BPY H5   H  N N 29  
A1BPY H6   H  N N 30  
A1BPY H7   H  N N 31  
A1BPY H8   H  N N 32  
A1BPY H9   H  N N 33  
A1BPY H12  H  N N 34  
A1BPY H13  H  N N 35  
A1BPY H    H  N N 36  
A1BPY H18  H  N N 37  
A1BPY H19  H  N N 38  
A1BPY H14  H  N N 39  
A1BPY H15  H  N N 40  
A1BPY H10  H  N N 41  
A1BPY H11  H  N N 42  
A1BPY H2   H  N N 43  
A1BPY H3   H  N N 44  
A1BPY H1   H  N N 45  
A1BPY H4   H  N N 46  
ALA   N    N  N N 47  
ALA   CA   C  N S 48  
ALA   C    C  N N 49  
ALA   O    O  N N 50  
ALA   CB   C  N N 51  
ALA   OXT  O  N N 52  
ALA   H    H  N N 53  
ALA   H2   H  N N 54  
ALA   HA   H  N N 55  
ALA   HB1  H  N N 56  
ALA   HB2  H  N N 57  
ALA   HB3  H  N N 58  
ALA   HXT  H  N N 59  
ARG   N    N  N N 60  
ARG   CA   C  N S 61  
ARG   C    C  N N 62  
ARG   O    O  N N 63  
ARG   CB   C  N N 64  
ARG   CG   C  N N 65  
ARG   CD   C  N N 66  
ARG   NE   N  N N 67  
ARG   CZ   C  N N 68  
ARG   NH1  N  N N 69  
ARG   NH2  N  N N 70  
ARG   OXT  O  N N 71  
ARG   H    H  N N 72  
ARG   H2   H  N N 73  
ARG   HA   H  N N 74  
ARG   HB2  H  N N 75  
ARG   HB3  H  N N 76  
ARG   HG2  H  N N 77  
ARG   HG3  H  N N 78  
ARG   HD2  H  N N 79  
ARG   HD3  H  N N 80  
ARG   HE   H  N N 81  
ARG   HH11 H  N N 82  
ARG   HH12 H  N N 83  
ARG   HH21 H  N N 84  
ARG   HH22 H  N N 85  
ARG   HXT  H  N N 86  
ASN   N    N  N N 87  
ASN   CA   C  N S 88  
ASN   C    C  N N 89  
ASN   O    O  N N 90  
ASN   CB   C  N N 91  
ASN   CG   C  N N 92  
ASN   OD1  O  N N 93  
ASN   ND2  N  N N 94  
ASN   OXT  O  N N 95  
ASN   H    H  N N 96  
ASN   H2   H  N N 97  
ASN   HA   H  N N 98  
ASN   HB2  H  N N 99  
ASN   HB3  H  N N 100 
ASN   HD21 H  N N 101 
ASN   HD22 H  N N 102 
ASN   HXT  H  N N 103 
ASP   N    N  N N 104 
ASP   CA   C  N S 105 
ASP   C    C  N N 106 
ASP   O    O  N N 107 
ASP   CB   C  N N 108 
ASP   CG   C  N N 109 
ASP   OD1  O  N N 110 
ASP   OD2  O  N N 111 
ASP   OXT  O  N N 112 
ASP   H    H  N N 113 
ASP   H2   H  N N 114 
ASP   HA   H  N N 115 
ASP   HB2  H  N N 116 
ASP   HB3  H  N N 117 
ASP   HD2  H  N N 118 
ASP   HXT  H  N N 119 
CYS   N    N  N N 120 
CYS   CA   C  N R 121 
CYS   C    C  N N 122 
CYS   O    O  N N 123 
CYS   CB   C  N N 124 
CYS   SG   S  N N 125 
CYS   OXT  O  N N 126 
CYS   H    H  N N 127 
CYS   H2   H  N N 128 
CYS   HA   H  N N 129 
CYS   HB2  H  N N 130 
CYS   HB3  H  N N 131 
CYS   HG   H  N N 132 
CYS   HXT  H  N N 133 
DMS   S    S  N N 134 
DMS   O    O  N N 135 
DMS   C1   C  N N 136 
DMS   C2   C  N N 137 
DMS   H11  H  N N 138 
DMS   H12  H  N N 139 
DMS   H13  H  N N 140 
DMS   H21  H  N N 141 
DMS   H22  H  N N 142 
DMS   H23  H  N N 143 
GLN   N    N  N N 144 
GLN   CA   C  N S 145 
GLN   C    C  N N 146 
GLN   O    O  N N 147 
GLN   CB   C  N N 148 
GLN   CG   C  N N 149 
GLN   CD   C  N N 150 
GLN   OE1  O  N N 151 
GLN   NE2  N  N N 152 
GLN   OXT  O  N N 153 
GLN   H    H  N N 154 
GLN   H2   H  N N 155 
GLN   HA   H  N N 156 
GLN   HB2  H  N N 157 
GLN   HB3  H  N N 158 
GLN   HG2  H  N N 159 
GLN   HG3  H  N N 160 
GLN   HE21 H  N N 161 
GLN   HE22 H  N N 162 
GLN   HXT  H  N N 163 
GLU   N    N  N N 164 
GLU   CA   C  N S 165 
GLU   C    C  N N 166 
GLU   O    O  N N 167 
GLU   CB   C  N N 168 
GLU   CG   C  N N 169 
GLU   CD   C  N N 170 
GLU   OE1  O  N N 171 
GLU   OE2  O  N N 172 
GLU   OXT  O  N N 173 
GLU   H    H  N N 174 
GLU   H2   H  N N 175 
GLU   HA   H  N N 176 
GLU   HB2  H  N N 177 
GLU   HB3  H  N N 178 
GLU   HG2  H  N N 179 
GLU   HG3  H  N N 180 
GLU   HE2  H  N N 181 
GLU   HXT  H  N N 182 
GLY   N    N  N N 183 
GLY   CA   C  N N 184 
GLY   C    C  N N 185 
GLY   O    O  N N 186 
GLY   OXT  O  N N 187 
GLY   H    H  N N 188 
GLY   H2   H  N N 189 
GLY   HA2  H  N N 190 
GLY   HA3  H  N N 191 
GLY   HXT  H  N N 192 
HIS   N    N  N N 193 
HIS   CA   C  N S 194 
HIS   C    C  N N 195 
HIS   O    O  N N 196 
HIS   CB   C  N N 197 
HIS   CG   C  Y N 198 
HIS   ND1  N  Y N 199 
HIS   CD2  C  Y N 200 
HIS   CE1  C  Y N 201 
HIS   NE2  N  Y N 202 
HIS   OXT  O  N N 203 
HIS   H    H  N N 204 
HIS   H2   H  N N 205 
HIS   HA   H  N N 206 
HIS   HB2  H  N N 207 
HIS   HB3  H  N N 208 
HIS   HD1  H  N N 209 
HIS   HD2  H  N N 210 
HIS   HE1  H  N N 211 
HIS   HE2  H  N N 212 
HIS   HXT  H  N N 213 
HOH   O    O  N N 214 
HOH   H1   H  N N 215 
HOH   H2   H  N N 216 
ILE   N    N  N N 217 
ILE   CA   C  N S 218 
ILE   C    C  N N 219 
ILE   O    O  N N 220 
ILE   CB   C  N S 221 
ILE   CG1  C  N N 222 
ILE   CG2  C  N N 223 
ILE   CD1  C  N N 224 
ILE   OXT  O  N N 225 
ILE   H    H  N N 226 
ILE   H2   H  N N 227 
ILE   HA   H  N N 228 
ILE   HB   H  N N 229 
ILE   HG12 H  N N 230 
ILE   HG13 H  N N 231 
ILE   HG21 H  N N 232 
ILE   HG22 H  N N 233 
ILE   HG23 H  N N 234 
ILE   HD11 H  N N 235 
ILE   HD12 H  N N 236 
ILE   HD13 H  N N 237 
ILE   HXT  H  N N 238 
LEU   N    N  N N 239 
LEU   CA   C  N S 240 
LEU   C    C  N N 241 
LEU   O    O  N N 242 
LEU   CB   C  N N 243 
LEU   CG   C  N N 244 
LEU   CD1  C  N N 245 
LEU   CD2  C  N N 246 
LEU   OXT  O  N N 247 
LEU   H    H  N N 248 
LEU   H2   H  N N 249 
LEU   HA   H  N N 250 
LEU   HB2  H  N N 251 
LEU   HB3  H  N N 252 
LEU   HG   H  N N 253 
LEU   HD11 H  N N 254 
LEU   HD12 H  N N 255 
LEU   HD13 H  N N 256 
LEU   HD21 H  N N 257 
LEU   HD22 H  N N 258 
LEU   HD23 H  N N 259 
LEU   HXT  H  N N 260 
LYS   N    N  N N 261 
LYS   CA   C  N S 262 
LYS   C    C  N N 263 
LYS   O    O  N N 264 
LYS   CB   C  N N 265 
LYS   CG   C  N N 266 
LYS   CD   C  N N 267 
LYS   CE   C  N N 268 
LYS   NZ   N  N N 269 
LYS   OXT  O  N N 270 
LYS   H    H  N N 271 
LYS   H2   H  N N 272 
LYS   HA   H  N N 273 
LYS   HB2  H  N N 274 
LYS   HB3  H  N N 275 
LYS   HG2  H  N N 276 
LYS   HG3  H  N N 277 
LYS   HD2  H  N N 278 
LYS   HD3  H  N N 279 
LYS   HE2  H  N N 280 
LYS   HE3  H  N N 281 
LYS   HZ1  H  N N 282 
LYS   HZ2  H  N N 283 
LYS   HZ3  H  N N 284 
LYS   HXT  H  N N 285 
MET   N    N  N N 286 
MET   CA   C  N S 287 
MET   C    C  N N 288 
MET   O    O  N N 289 
MET   CB   C  N N 290 
MET   CG   C  N N 291 
MET   SD   S  N N 292 
MET   CE   C  N N 293 
MET   OXT  O  N N 294 
MET   H    H  N N 295 
MET   H2   H  N N 296 
MET   HA   H  N N 297 
MET   HB2  H  N N 298 
MET   HB3  H  N N 299 
MET   HG2  H  N N 300 
MET   HG3  H  N N 301 
MET   HE1  H  N N 302 
MET   HE2  H  N N 303 
MET   HE3  H  N N 304 
MET   HXT  H  N N 305 
PHE   N    N  N N 306 
PHE   CA   C  N S 307 
PHE   C    C  N N 308 
PHE   O    O  N N 309 
PHE   CB   C  N N 310 
PHE   CG   C  Y N 311 
PHE   CD1  C  Y N 312 
PHE   CD2  C  Y N 313 
PHE   CE1  C  Y N 314 
PHE   CE2  C  Y N 315 
PHE   CZ   C  Y N 316 
PHE   OXT  O  N N 317 
PHE   H    H  N N 318 
PHE   H2   H  N N 319 
PHE   HA   H  N N 320 
PHE   HB2  H  N N 321 
PHE   HB3  H  N N 322 
PHE   HD1  H  N N 323 
PHE   HD2  H  N N 324 
PHE   HE1  H  N N 325 
PHE   HE2  H  N N 326 
PHE   HZ   H  N N 327 
PHE   HXT  H  N N 328 
PRO   N    N  N N 329 
PRO   CA   C  N S 330 
PRO   C    C  N N 331 
PRO   O    O  N N 332 
PRO   CB   C  N N 333 
PRO   CG   C  N N 334 
PRO   CD   C  N N 335 
PRO   OXT  O  N N 336 
PRO   H    H  N N 337 
PRO   HA   H  N N 338 
PRO   HB2  H  N N 339 
PRO   HB3  H  N N 340 
PRO   HG2  H  N N 341 
PRO   HG3  H  N N 342 
PRO   HD2  H  N N 343 
PRO   HD3  H  N N 344 
PRO   HXT  H  N N 345 
SER   N    N  N N 346 
SER   CA   C  N S 347 
SER   C    C  N N 348 
SER   O    O  N N 349 
SER   CB   C  N N 350 
SER   OG   O  N N 351 
SER   OXT  O  N N 352 
SER   H    H  N N 353 
SER   H2   H  N N 354 
SER   HA   H  N N 355 
SER   HB2  H  N N 356 
SER   HB3  H  N N 357 
SER   HG   H  N N 358 
SER   HXT  H  N N 359 
THR   N    N  N N 360 
THR   CA   C  N S 361 
THR   C    C  N N 362 
THR   O    O  N N 363 
THR   CB   C  N R 364 
THR   OG1  O  N N 365 
THR   CG2  C  N N 366 
THR   OXT  O  N N 367 
THR   H    H  N N 368 
THR   H2   H  N N 369 
THR   HA   H  N N 370 
THR   HB   H  N N 371 
THR   HG1  H  N N 372 
THR   HG21 H  N N 373 
THR   HG22 H  N N 374 
THR   HG23 H  N N 375 
THR   HXT  H  N N 376 
TRP   N    N  N N 377 
TRP   CA   C  N S 378 
TRP   C    C  N N 379 
TRP   O    O  N N 380 
TRP   CB   C  N N 381 
TRP   CG   C  Y N 382 
TRP   CD1  C  Y N 383 
TRP   CD2  C  Y N 384 
TRP   NE1  N  Y N 385 
TRP   CE2  C  Y N 386 
TRP   CE3  C  Y N 387 
TRP   CZ2  C  Y N 388 
TRP   CZ3  C  Y N 389 
TRP   CH2  C  Y N 390 
TRP   OXT  O  N N 391 
TRP   H    H  N N 392 
TRP   H2   H  N N 393 
TRP   HA   H  N N 394 
TRP   HB2  H  N N 395 
TRP   HB3  H  N N 396 
TRP   HD1  H  N N 397 
TRP   HE1  H  N N 398 
TRP   HE3  H  N N 399 
TRP   HZ2  H  N N 400 
TRP   HZ3  H  N N 401 
TRP   HH2  H  N N 402 
TRP   HXT  H  N N 403 
TYR   N    N  N N 404 
TYR   CA   C  N S 405 
TYR   C    C  N N 406 
TYR   O    O  N N 407 
TYR   CB   C  N N 408 
TYR   CG   C  Y N 409 
TYR   CD1  C  Y N 410 
TYR   CD2  C  Y N 411 
TYR   CE1  C  Y N 412 
TYR   CE2  C  Y N 413 
TYR   CZ   C  Y N 414 
TYR   OH   O  N N 415 
TYR   OXT  O  N N 416 
TYR   H    H  N N 417 
TYR   H2   H  N N 418 
TYR   HA   H  N N 419 
TYR   HB2  H  N N 420 
TYR   HB3  H  N N 421 
TYR   HD1  H  N N 422 
TYR   HD2  H  N N 423 
TYR   HE1  H  N N 424 
TYR   HE2  H  N N 425 
TYR   HH   H  N N 426 
TYR   HXT  H  N N 427 
VAL   N    N  N N 428 
VAL   CA   C  N S 429 
VAL   C    C  N N 430 
VAL   O    O  N N 431 
VAL   CB   C  N N 432 
VAL   CG1  C  N N 433 
VAL   CG2  C  N N 434 
VAL   OXT  O  N N 435 
VAL   H    H  N N 436 
VAL   H2   H  N N 437 
VAL   HA   H  N N 438 
VAL   HB   H  N N 439 
VAL   HG11 H  N N 440 
VAL   HG12 H  N N 441 
VAL   HG13 H  N N 442 
VAL   HG21 H  N N 443 
VAL   HG22 H  N N 444 
VAL   HG23 H  N N 445 
VAL   HXT  H  N N 446 
ZN    ZN   ZN N N 447 
# 
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 
A1BPY C   N    sing N N 1   
A1BPY N   N1   sing Y N 2   
A1BPY N1  C1   doub Y N 3   
A1BPY C1  C2   sing Y N 4   
A1BPY C3  C2   sing N N 5   
A1BPY C3  C4   doub Y N 6   
A1BPY C4  C5   sing Y N 7   
A1BPY CL  C5   sing N N 8   
A1BPY C5  C6   doub Y N 9   
A1BPY C6  C7   sing Y N 10  
A1BPY CL1 C7   sing N N 11  
A1BPY C7  C8   doub Y N 12  
A1BPY C8  C3   sing Y N 13  
A1BPY C2  C9   doub Y N 14  
A1BPY N   C9   sing Y N 15  
A1BPY C9  C10  sing N N 16  
A1BPY C10 C11  sing N N 17  
A1BPY O   C11  doub N N 18  
A1BPY C11 N2   sing N N 19  
A1BPY N2  C12  sing N N 20  
A1BPY C12 C13  sing N N 21  
A1BPY C13 C14  sing N N 22  
A1BPY C14 C15  sing N N 23  
A1BPY C15 C16  sing N N 24  
A1BPY N3  C16  sing N N 25  
A1BPY C16 O1   doub N N 26  
A1BPY C17 C15  sing N N 27  
A1BPY N2  C17  sing N N 28  
A1BPY N3  H17  sing N N 29  
A1BPY N3  H16  sing N N 30  
A1BPY C4  H5   sing N N 31  
A1BPY C6  H6   sing N N 32  
A1BPY C8  H7   sing N N 33  
A1BPY C10 H8   sing N N 34  
A1BPY C10 H9   sing N N 35  
A1BPY C13 H12  sing N N 36  
A1BPY C13 H13  sing N N 37  
A1BPY C15 H    sing N N 38  
A1BPY C17 H18  sing N N 39  
A1BPY C17 H19  sing N N 40  
A1BPY C14 H14  sing N N 41  
A1BPY C14 H15  sing N N 42  
A1BPY C12 H10  sing N N 43  
A1BPY C12 H11  sing N N 44  
A1BPY C   H2   sing N N 45  
A1BPY C   H3   sing N N 46  
A1BPY C   H1   sing N N 47  
A1BPY C1  H4   sing N N 48  
ALA   N   CA   sing N N 49  
ALA   N   H    sing N N 50  
ALA   N   H2   sing N N 51  
ALA   CA  C    sing N N 52  
ALA   CA  CB   sing N N 53  
ALA   CA  HA   sing N N 54  
ALA   C   O    doub N N 55  
ALA   C   OXT  sing N N 56  
ALA   CB  HB1  sing N N 57  
ALA   CB  HB2  sing N N 58  
ALA   CB  HB3  sing N N 59  
ALA   OXT HXT  sing N N 60  
ARG   N   CA   sing N N 61  
ARG   N   H    sing N N 62  
ARG   N   H2   sing N N 63  
ARG   CA  C    sing N N 64  
ARG   CA  CB   sing N N 65  
ARG   CA  HA   sing N N 66  
ARG   C   O    doub N N 67  
ARG   C   OXT  sing N N 68  
ARG   CB  CG   sing N N 69  
ARG   CB  HB2  sing N N 70  
ARG   CB  HB3  sing N N 71  
ARG   CG  CD   sing N N 72  
ARG   CG  HG2  sing N N 73  
ARG   CG  HG3  sing N N 74  
ARG   CD  NE   sing N N 75  
ARG   CD  HD2  sing N N 76  
ARG   CD  HD3  sing N N 77  
ARG   NE  CZ   sing N N 78  
ARG   NE  HE   sing N N 79  
ARG   CZ  NH1  sing N N 80  
ARG   CZ  NH2  doub N N 81  
ARG   NH1 HH11 sing N N 82  
ARG   NH1 HH12 sing N N 83  
ARG   NH2 HH21 sing N N 84  
ARG   NH2 HH22 sing N N 85  
ARG   OXT HXT  sing N N 86  
ASN   N   CA   sing N N 87  
ASN   N   H    sing N N 88  
ASN   N   H2   sing N N 89  
ASN   CA  C    sing N N 90  
ASN   CA  CB   sing N N 91  
ASN   CA  HA   sing N N 92  
ASN   C   O    doub N N 93  
ASN   C   OXT  sing N N 94  
ASN   CB  CG   sing N N 95  
ASN   CB  HB2  sing N N 96  
ASN   CB  HB3  sing N N 97  
ASN   CG  OD1  doub N N 98  
ASN   CG  ND2  sing N N 99  
ASN   ND2 HD21 sing N N 100 
ASN   ND2 HD22 sing N N 101 
ASN   OXT HXT  sing N N 102 
ASP   N   CA   sing N N 103 
ASP   N   H    sing N N 104 
ASP   N   H2   sing N N 105 
ASP   CA  C    sing N N 106 
ASP   CA  CB   sing N N 107 
ASP   CA  HA   sing N N 108 
ASP   C   O    doub N N 109 
ASP   C   OXT  sing N N 110 
ASP   CB  CG   sing N N 111 
ASP   CB  HB2  sing N N 112 
ASP   CB  HB3  sing N N 113 
ASP   CG  OD1  doub N N 114 
ASP   CG  OD2  sing N N 115 
ASP   OD2 HD2  sing N N 116 
ASP   OXT HXT  sing N N 117 
CYS   N   CA   sing N N 118 
CYS   N   H    sing N N 119 
CYS   N   H2   sing N N 120 
CYS   CA  C    sing N N 121 
CYS   CA  CB   sing N N 122 
CYS   CA  HA   sing N N 123 
CYS   C   O    doub N N 124 
CYS   C   OXT  sing N N 125 
CYS   CB  SG   sing N N 126 
CYS   CB  HB2  sing N N 127 
CYS   CB  HB3  sing N N 128 
CYS   SG  HG   sing N N 129 
CYS   OXT HXT  sing N N 130 
DMS   S   O    doub N N 131 
DMS   S   C1   sing N N 132 
DMS   S   C2   sing N N 133 
DMS   C1  H11  sing N N 134 
DMS   C1  H12  sing N N 135 
DMS   C1  H13  sing N N 136 
DMS   C2  H21  sing N N 137 
DMS   C2  H22  sing N N 138 
DMS   C2  H23  sing N N 139 
GLN   N   CA   sing N N 140 
GLN   N   H    sing N N 141 
GLN   N   H2   sing N N 142 
GLN   CA  C    sing N N 143 
GLN   CA  CB   sing N N 144 
GLN   CA  HA   sing N N 145 
GLN   C   O    doub N N 146 
GLN   C   OXT  sing N N 147 
GLN   CB  CG   sing N N 148 
GLN   CB  HB2  sing N N 149 
GLN   CB  HB3  sing N N 150 
GLN   CG  CD   sing N N 151 
GLN   CG  HG2  sing N N 152 
GLN   CG  HG3  sing N N 153 
GLN   CD  OE1  doub N N 154 
GLN   CD  NE2  sing N N 155 
GLN   NE2 HE21 sing N N 156 
GLN   NE2 HE22 sing N N 157 
GLN   OXT HXT  sing N N 158 
GLU   N   CA   sing N N 159 
GLU   N   H    sing N N 160 
GLU   N   H2   sing N N 161 
GLU   CA  C    sing N N 162 
GLU   CA  CB   sing N N 163 
GLU   CA  HA   sing N N 164 
GLU   C   O    doub N N 165 
GLU   C   OXT  sing N N 166 
GLU   CB  CG   sing N N 167 
GLU   CB  HB2  sing N N 168 
GLU   CB  HB3  sing N N 169 
GLU   CG  CD   sing N N 170 
GLU   CG  HG2  sing N N 171 
GLU   CG  HG3  sing N N 172 
GLU   CD  OE1  doub N N 173 
GLU   CD  OE2  sing N N 174 
GLU   OE2 HE2  sing N N 175 
GLU   OXT HXT  sing N N 176 
GLY   N   CA   sing N N 177 
GLY   N   H    sing N N 178 
GLY   N   H2   sing N N 179 
GLY   CA  C    sing N N 180 
GLY   CA  HA2  sing N N 181 
GLY   CA  HA3  sing N N 182 
GLY   C   O    doub N N 183 
GLY   C   OXT  sing N N 184 
GLY   OXT HXT  sing N N 185 
HIS   N   CA   sing N N 186 
HIS   N   H    sing N N 187 
HIS   N   H2   sing N N 188 
HIS   CA  C    sing N N 189 
HIS   CA  CB   sing N N 190 
HIS   CA  HA   sing N N 191 
HIS   C   O    doub N N 192 
HIS   C   OXT  sing N N 193 
HIS   CB  CG   sing N N 194 
HIS   CB  HB2  sing N N 195 
HIS   CB  HB3  sing N N 196 
HIS   CG  ND1  sing Y N 197 
HIS   CG  CD2  doub Y N 198 
HIS   ND1 CE1  doub Y N 199 
HIS   ND1 HD1  sing N N 200 
HIS   CD2 NE2  sing Y N 201 
HIS   CD2 HD2  sing N N 202 
HIS   CE1 NE2  sing Y N 203 
HIS   CE1 HE1  sing N N 204 
HIS   NE2 HE2  sing N N 205 
HIS   OXT HXT  sing N N 206 
HOH   O   H1   sing N N 207 
HOH   O   H2   sing N N 208 
ILE   N   CA   sing N N 209 
ILE   N   H    sing N N 210 
ILE   N   H2   sing N N 211 
ILE   CA  C    sing N N 212 
ILE   CA  CB   sing N N 213 
ILE   CA  HA   sing N N 214 
ILE   C   O    doub N N 215 
ILE   C   OXT  sing N N 216 
ILE   CB  CG1  sing N N 217 
ILE   CB  CG2  sing N N 218 
ILE   CB  HB   sing N N 219 
ILE   CG1 CD1  sing N N 220 
ILE   CG1 HG12 sing N N 221 
ILE   CG1 HG13 sing N N 222 
ILE   CG2 HG21 sing N N 223 
ILE   CG2 HG22 sing N N 224 
ILE   CG2 HG23 sing N N 225 
ILE   CD1 HD11 sing N N 226 
ILE   CD1 HD12 sing N N 227 
ILE   CD1 HD13 sing N N 228 
ILE   OXT HXT  sing N N 229 
LEU   N   CA   sing N N 230 
LEU   N   H    sing N N 231 
LEU   N   H2   sing N N 232 
LEU   CA  C    sing N N 233 
LEU   CA  CB   sing N N 234 
LEU   CA  HA   sing N N 235 
LEU   C   O    doub N N 236 
LEU   C   OXT  sing N N 237 
LEU   CB  CG   sing N N 238 
LEU   CB  HB2  sing N N 239 
LEU   CB  HB3  sing N N 240 
LEU   CG  CD1  sing N N 241 
LEU   CG  CD2  sing N N 242 
LEU   CG  HG   sing N N 243 
LEU   CD1 HD11 sing N N 244 
LEU   CD1 HD12 sing N N 245 
LEU   CD1 HD13 sing N N 246 
LEU   CD2 HD21 sing N N 247 
LEU   CD2 HD22 sing N N 248 
LEU   CD2 HD23 sing N N 249 
LEU   OXT HXT  sing N N 250 
LYS   N   CA   sing N N 251 
LYS   N   H    sing N N 252 
LYS   N   H2   sing N N 253 
LYS   CA  C    sing N N 254 
LYS   CA  CB   sing N N 255 
LYS   CA  HA   sing N N 256 
LYS   C   O    doub N N 257 
LYS   C   OXT  sing N N 258 
LYS   CB  CG   sing N N 259 
LYS   CB  HB2  sing N N 260 
LYS   CB  HB3  sing N N 261 
LYS   CG  CD   sing N N 262 
LYS   CG  HG2  sing N N 263 
LYS   CG  HG3  sing N N 264 
LYS   CD  CE   sing N N 265 
LYS   CD  HD2  sing N N 266 
LYS   CD  HD3  sing N N 267 
LYS   CE  NZ   sing N N 268 
LYS   CE  HE2  sing N N 269 
LYS   CE  HE3  sing N N 270 
LYS   NZ  HZ1  sing N N 271 
LYS   NZ  HZ2  sing N N 272 
LYS   NZ  HZ3  sing N N 273 
LYS   OXT HXT  sing N N 274 
MET   N   CA   sing N N 275 
MET   N   H    sing N N 276 
MET   N   H2   sing N N 277 
MET   CA  C    sing N N 278 
MET   CA  CB   sing N N 279 
MET   CA  HA   sing N N 280 
MET   C   O    doub N N 281 
MET   C   OXT  sing N N 282 
MET   CB  CG   sing N N 283 
MET   CB  HB2  sing N N 284 
MET   CB  HB3  sing N N 285 
MET   CG  SD   sing N N 286 
MET   CG  HG2  sing N N 287 
MET   CG  HG3  sing N N 288 
MET   SD  CE   sing N N 289 
MET   CE  HE1  sing N N 290 
MET   CE  HE2  sing N N 291 
MET   CE  HE3  sing N N 292 
MET   OXT HXT  sing N N 293 
PHE   N   CA   sing N N 294 
PHE   N   H    sing N N 295 
PHE   N   H2   sing N N 296 
PHE   CA  C    sing N N 297 
PHE   CA  CB   sing N N 298 
PHE   CA  HA   sing N N 299 
PHE   C   O    doub N N 300 
PHE   C   OXT  sing N N 301 
PHE   CB  CG   sing N N 302 
PHE   CB  HB2  sing N N 303 
PHE   CB  HB3  sing N N 304 
PHE   CG  CD1  doub Y N 305 
PHE   CG  CD2  sing Y N 306 
PHE   CD1 CE1  sing Y N 307 
PHE   CD1 HD1  sing N N 308 
PHE   CD2 CE2  doub Y N 309 
PHE   CD2 HD2  sing N N 310 
PHE   CE1 CZ   doub Y N 311 
PHE   CE1 HE1  sing N N 312 
PHE   CE2 CZ   sing Y N 313 
PHE   CE2 HE2  sing N N 314 
PHE   CZ  HZ   sing N N 315 
PHE   OXT HXT  sing N N 316 
PRO   N   CA   sing N N 317 
PRO   N   CD   sing N N 318 
PRO   N   H    sing N N 319 
PRO   CA  C    sing N N 320 
PRO   CA  CB   sing N N 321 
PRO   CA  HA   sing N N 322 
PRO   C   O    doub N N 323 
PRO   C   OXT  sing N N 324 
PRO   CB  CG   sing N N 325 
PRO   CB  HB2  sing N N 326 
PRO   CB  HB3  sing N N 327 
PRO   CG  CD   sing N N 328 
PRO   CG  HG2  sing N N 329 
PRO   CG  HG3  sing N N 330 
PRO   CD  HD2  sing N N 331 
PRO   CD  HD3  sing N N 332 
PRO   OXT HXT  sing N N 333 
SER   N   CA   sing N N 334 
SER   N   H    sing N N 335 
SER   N   H2   sing N N 336 
SER   CA  C    sing N N 337 
SER   CA  CB   sing N N 338 
SER   CA  HA   sing N N 339 
SER   C   O    doub N N 340 
SER   C   OXT  sing N N 341 
SER   CB  OG   sing N N 342 
SER   CB  HB2  sing N N 343 
SER   CB  HB3  sing N N 344 
SER   OG  HG   sing N N 345 
SER   OXT HXT  sing N N 346 
THR   N   CA   sing N N 347 
THR   N   H    sing N N 348 
THR   N   H2   sing N N 349 
THR   CA  C    sing N N 350 
THR   CA  CB   sing N N 351 
THR   CA  HA   sing N N 352 
THR   C   O    doub N N 353 
THR   C   OXT  sing N N 354 
THR   CB  OG1  sing N N 355 
THR   CB  CG2  sing N N 356 
THR   CB  HB   sing N N 357 
THR   OG1 HG1  sing N N 358 
THR   CG2 HG21 sing N N 359 
THR   CG2 HG22 sing N N 360 
THR   CG2 HG23 sing N N 361 
THR   OXT HXT  sing N N 362 
TRP   N   CA   sing N N 363 
TRP   N   H    sing N N 364 
TRP   N   H2   sing N N 365 
TRP   CA  C    sing N N 366 
TRP   CA  CB   sing N N 367 
TRP   CA  HA   sing N N 368 
TRP   C   O    doub N N 369 
TRP   C   OXT  sing N N 370 
TRP   CB  CG   sing N N 371 
TRP   CB  HB2  sing N N 372 
TRP   CB  HB3  sing N N 373 
TRP   CG  CD1  doub Y N 374 
TRP   CG  CD2  sing Y N 375 
TRP   CD1 NE1  sing Y N 376 
TRP   CD1 HD1  sing N N 377 
TRP   CD2 CE2  doub Y N 378 
TRP   CD2 CE3  sing Y N 379 
TRP   NE1 CE2  sing Y N 380 
TRP   NE1 HE1  sing N N 381 
TRP   CE2 CZ2  sing Y N 382 
TRP   CE3 CZ3  doub Y N 383 
TRP   CE3 HE3  sing N N 384 
TRP   CZ2 CH2  doub Y N 385 
TRP   CZ2 HZ2  sing N N 386 
TRP   CZ3 CH2  sing Y N 387 
TRP   CZ3 HZ3  sing N N 388 
TRP   CH2 HH2  sing N N 389 
TRP   OXT HXT  sing N N 390 
TYR   N   CA   sing N N 391 
TYR   N   H    sing N N 392 
TYR   N   H2   sing N N 393 
TYR   CA  C    sing N N 394 
TYR   CA  CB   sing N N 395 
TYR   CA  HA   sing N N 396 
TYR   C   O    doub N N 397 
TYR   C   OXT  sing N N 398 
TYR   CB  CG   sing N N 399 
TYR   CB  HB2  sing N N 400 
TYR   CB  HB3  sing N N 401 
TYR   CG  CD1  doub Y N 402 
TYR   CG  CD2  sing Y N 403 
TYR   CD1 CE1  sing Y N 404 
TYR   CD1 HD1  sing N N 405 
TYR   CD2 CE2  doub Y N 406 
TYR   CD2 HD2  sing N N 407 
TYR   CE1 CZ   doub Y N 408 
TYR   CE1 HE1  sing N N 409 
TYR   CE2 CZ   sing Y N 410 
TYR   CE2 HE2  sing N N 411 
TYR   CZ  OH   sing N N 412 
TYR   OH  HH   sing N N 413 
TYR   OXT HXT  sing N N 414 
VAL   N   CA   sing N N 415 
VAL   N   H    sing N N 416 
VAL   N   H2   sing N N 417 
VAL   CA  C    sing N N 418 
VAL   CA  CB   sing N N 419 
VAL   CA  HA   sing N N 420 
VAL   C   O    doub N N 421 
VAL   C   OXT  sing N N 422 
VAL   CB  CG1  sing N N 423 
VAL   CB  CG2  sing N N 424 
VAL   CB  HB   sing N N 425 
VAL   CG1 HG11 sing N N 426 
VAL   CG1 HG12 sing N N 427 
VAL   CG1 HG13 sing N N 428 
VAL   CG2 HG21 sing N N 429 
VAL   CG2 HG22 sing N N 430 
VAL   CG2 HG23 sing N N 431 
VAL   OXT HXT  sing N N 432 
# 
_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                    7HVU 
_atom_sites.fract_transf_matrix[1][1]   0.011506 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000928 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017374 
_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]   0.015454 
_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  
CL 
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   ? 17.537 8.119   24.850 1.00 21.08  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.798 8.220   24.087 1.00 22.01  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 18.949 7.013   23.141 1.00 21.10  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.247 5.995   23.307 1.00 20.90  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 19.987 8.310   25.047 1.00 25.10  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.091 7.082   25.746 1.00 27.57  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.872 7.104   22.180 1.00 19.85  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.111 5.993   21.265 1.00 18.72  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.580 6.475   19.896 1.00 18.40  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.247 7.589   19.479 1.00 18.17  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.282 5.616   19.169 1.00 17.06  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.783 5.978   17.853 1.00 17.79  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.785 4.751   16.944 1.00 17.65  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.676 3.617   17.435 1.00 18.80  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.216 6.510   18.012 1.00 18.29  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.912 4.970   15.618 1.00 16.70  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.112 3.891   14.653 1.00 16.18  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.593 3.990   14.269 1.00 17.03  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.073 5.108   13.974 1.00 16.99  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.276 4.103   13.376 1.00 17.38  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.796 4.259   13.707 1.00 18.52  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.509 2.937   12.388 1.00 18.21  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.946 4.759   12.482 1.00 18.30  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.316 2.861   14.261 1.00 17.81  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.720 2.847   13.873 1.00 19.08  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.823 1.984   12.602 1.00 18.88  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.765 0.764   12.688 1.00 19.48  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.575 2.254   15.007 1.00 19.61  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.600 3.166   16.219 1.00 19.23  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.440 4.274   16.266 1.00 19.75  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.743 2.956   17.295 1.00 20.21  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.445 5.137   17.358 1.00 20.52  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.730 3.829   18.391 1.00 20.71  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.578 4.926   18.411 1.00 21.42  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.573 5.820   19.480 1.00 22.18  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.846 2.633   11.428 1.00 19.05  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.912 2.026   10.103 1.00 19.33  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.158 2.532   9.398  1.00 20.58  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.393 3.736   9.351  1.00 20.69  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.604 2.255   9.269  1.00 19.92  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.249 3.755   9.150  1.00 21.39  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.727 1.599   7.883  1.00 21.23  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.049 1.624   8.973  1.00 21.43  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.301 2.029   8.332  1.00 20.55  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.112 2.939   9.239  1.00 20.88  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.229 2.654   10.441 1.00 20.41  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.572 4.082   8.702  1.00 19.98  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.259 5.063   9.537  1.00 20.40  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.361 6.252   9.864  1.00 19.42  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.825 7.410   9.968  1.00 20.00  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.577 5.511   8.934  1.00 22.59  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.635 4.447   9.052  1.00 27.90  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.410 4.394   10.020 1.00 29.79  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.679 3.581   8.076  1.00 28.91  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.065 5.951   10.094 1.00 18.35  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.106 7.006   10.441 1.00 18.80  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.427 6.683   11.785 1.00 17.98  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.197 5.495   12.122 1.00 18.51  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.992 7.099   9.365  1.00 18.94  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.486 7.499   7.991  1.00 20.28  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.117 8.718   7.783  1.00 21.49  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.333 6.653   6.903  1.00 21.72  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.576 9.090   6.522  1.00 23.25  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.757 7.029   5.634  1.00 23.25  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.373 8.252   5.446  1.00 24.59  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.827 8.630   4.200  1.00 26.12  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.066 7.743   12.509 1.00 17.15  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.292 7.684   13.747 1.00 17.04  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.048 8.538   13.456 1.00 16.99  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.182 9.729   13.154 1.00 17.79  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.103 8.264   14.937 1.00 17.62  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.277 8.578   16.203 1.00 18.67  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.194 8.953   17.390 1.00 18.86  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.648 10.042  18.204 1.00 20.00  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.962 9.858   19.332 1.00 22.06  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.704 8.624   19.769 1.00 22.55  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.515 10.905  20.020 1.00 22.31  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.834 7.928   13.521 1.00 16.06  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.579 8.659   13.267 1.00 16.34  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.915 8.855   14.610 1.00 16.92  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.623 7.870   15.301 1.00 16.04  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.632 7.857   12.344 1.00 17.41  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.421 8.720   11.927 1.00 17.63  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.362 7.329   11.116 1.00 18.28  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.669 10.121  14.978 1.00 16.15  ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.039 10.443  16.259 0.50 15.73  ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.121 10.528  16.288 0.50 18.00  ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.909 11.440  16.057 1.00 17.09  ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.780 12.072  14.984 1.00 17.77  ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.072 11.050  17.250 0.50 14.78  ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.173 11.377  17.127 0.50 21.39  ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 23.031 10.001  17.760 0.50 14.60  ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 22.041 11.152  18.626 0.50 22.21  ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.786 12.286  16.663 0.50 12.43  ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.622 11.201  16.681 0.50 23.33  ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.037 11.616  17.121 1.00 16.76  ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.009 12.655  17.033 1.00 16.40  ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.797 13.990  17.044 1.00 16.88  ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.702 14.166  17.895 1.00 17.69  ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.181 12.648  18.312 1.00 16.55  ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.320 11.411  18.395 1.00 18.04  ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.720 10.392  18.998 1.00 18.98  ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.114 11.481  17.814 1.00 16.93  ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.475 14.939  16.145 1.00 16.39  ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.240 16.216  16.122 1.00 17.23  ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.187 16.917  17.463 1.00 19.73  ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.205 17.444  17.919 1.00 20.76  ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.636 17.129  15.046 1.00 17.86  ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.438 18.434  14.790 1.00 18.62  ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.655 19.308  13.815 1.00 20.73  ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.374 20.505  13.317 1.00 21.91  ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.392 21.679  13.953 1.00 25.24  ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.837 21.799  15.159 1.00 24.90  ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 19.974 22.744  13.389 1.00 25.38  ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.032 16.824  18.155 1.00 19.26  ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 17.910 17.542  19.419 1.00 19.80  ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.788 16.958  20.546 1.00 21.48  ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.005 17.647  21.550 1.00 23.36  ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.440 17.713  19.856 1.00 20.19  ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.800 16.467  20.381 1.00 19.91  ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.177 15.567  19.529 1.00 21.24  ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.623 16.053  21.663 1.00 20.94  ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.704 14.596  20.307 1.00 22.19  ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.913 14.861  21.597 1.00 22.66  ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.297 15.725  20.376 1.00 20.20  ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.183 15.083  21.346 1.00 19.85  ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.654 15.019  20.902 1.00 21.15  ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.471 14.393  21.575 1.00 21.60  ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.661 13.677  21.636 1.00 20.11  ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.248 13.642  22.227 1.00 21.65  ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.853 12.187  22.477 1.00 21.85  ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.170 14.439  23.575 1.00 22.98  ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 21.993 15.635  19.762 1.00 20.60  ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.369 15.613  19.271 1.00 21.02  ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.310 16.291  20.255 1.00 21.48  ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 23.948 17.318  20.862 1.00 22.13  ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.446 16.290  17.905 1.00 21.76  ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.504 15.703  20.421 1.00 20.73  ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.525 16.232  21.320 1.00 21.12  ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.428 17.254  20.590 1.00 21.81  ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.377 17.366  19.363 1.00 21.30  ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.405 15.079  21.839 1.00 22.96  ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.154 14.536  20.730 1.00 24.45  ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.598 13.963  22.515 1.00 23.32  ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.350 17.935  21.324 1.00 22.60  ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.323 18.810  20.685 1.00 23.39  ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.201 17.987  19.740 1.00 22.69  ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.504 18.459  18.649 1.00 22.80  ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.235 19.495  21.732 1.00 26.87  ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.421 20.194  21.107 1.00 35.87  ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.293 21.440  20.512 1.00 40.27  ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.695 19.757  20.927 1.00 39.91  ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.497 21.764  20.066 1.00 41.15  ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.378 20.779  20.273 1.00 42.40  ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.588 16.745  20.136 1.00 21.86  ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.421 15.926  19.241 1.00 22.28  ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.670 15.629  17.935 1.00 21.26  ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.280 15.618  16.870 1.00 21.53  ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.866 14.622  19.885 1.00 24.79  ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.894 13.907  19.040 1.00 32.52  ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.067 14.348  18.922 1.00 35.32  ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.478 12.829  18.375 1.00 34.30  ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.340 15.404  18.016 1.00 20.17  ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.544 15.178  16.802 1.00 19.15  ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.615 16.406  15.869 1.00 19.28  ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.842 16.247  14.673 1.00 20.66  ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.070 14.887  17.131 1.00 18.54  ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.839 13.524  17.746 1.00 20.23  ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.469 12.550  17.274 1.00 19.06  ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 25.989 13.423  18.680 1.00 19.80  ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.393 17.617  16.418 1.00 18.88  ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.441 18.837  15.606 1.00 19.33  ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.852 19.102  15.055 1.00 20.25  ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 29.986 19.693  13.984 1.00 21.68  ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 27.953 20.045  16.428 1.00 19.56  ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.456 20.098  16.553 1.00 20.19  ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.690 19.729  17.625 1.00 21.96  ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.544 20.495  15.526 1.00 21.18  ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.351 19.950  17.348 1.00 22.29  ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.238 20.404  16.056 1.00 22.43  ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.709 20.958  14.219 1.00 22.40  ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.115 20.791  15.322 1.00 23.27  ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.603 21.303  13.489 1.00 23.39  ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.330 21.245  14.039 1.00 23.85  ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.903 18.727  15.804 1.00 20.12  ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.274 18.928  15.349 1.00 20.80  ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.712 17.899  14.292 1.00 20.77  ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.770 18.072  13.688 1.00 21.22  ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.231 18.898  16.541 1.00 22.35  ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.904 16.820  14.076 1.00 19.44  ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.192 15.780  13.063 1.00 19.46  ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.944 15.581  12.209 1.00 19.14  ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.582 14.443  11.863 1.00 19.23  ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.583 14.459  13.758 1.00 20.85  ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.936 14.633  14.404 1.00 24.55  ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 34.948 14.590  13.719 1.00 25.31  ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 33.975 14.956  15.722 1.00 26.02  ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.281 16.690  11.881 1.00 18.71  ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 28.998 16.682  11.180 1.00 18.55  ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.079 16.198  9.753  1.00 19.87  ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.954 16.639  8.984  1.00 21.60  ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.381 18.113  11.211 1.00 17.78  ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.020 18.241  10.567 1.00 19.99  ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 25.974 17.431  11.360 1.00 20.30  ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.568 19.695  10.527 1.00 22.18  ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.132 15.301  9.372  1.00 18.49  ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.008 14.848  7.990  1.00 19.03  ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.759 15.519  7.368  1.00 20.05  ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.823 16.068  6.261  1.00 21.66  ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.908 13.296  7.914  1.00 18.99  ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.514 12.837  6.501  1.00 20.06  ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.222 12.649  8.365  1.00 20.46  ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.619 15.504  8.103  1.00 18.88  ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.359 16.037  7.565  1.00 19.75  ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.370 16.220  8.706  1.00 19.58  ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.400 15.441  9.661  1.00 18.79  ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.749 15.010  6.573  1.00 20.54  ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.339 15.264  6.100  1.00 22.46  ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.942 16.063  5.067  1.00 24.84  ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.139 14.646  6.613  1.00 22.25  ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.565 16.007  4.922  1.00 25.58  ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.050 15.144  5.864  1.00 23.57  ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.881 13.734  7.643  1.00 22.53  ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.726 14.704  6.077  1.00 23.90  ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.583 13.319  7.855  1.00 22.74  ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.519 13.803  7.080  1.00 23.15  ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.540 17.262  8.646  1.00 20.02  ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.510 17.455  9.668  1.00 20.12  ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.258 18.047  9.027  1.00 21.08  ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.372 18.809  8.051  1.00 22.41  ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.010 18.330  10.824 1.00 19.91  ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.642 19.669  10.445 1.00 21.17  ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.681 20.823  10.222 1.00 26.45  ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.016 21.739  9.430  1.00 25.43  ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.566 20.800  10.798 1.00 26.28  ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.073 17.759  9.587  1.00 19.37  ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.848 18.332  9.052  1.00 20.34  ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.896 18.528  10.232 1.00 20.92  ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.426 17.551  10.814 1.00 21.10  ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.270 17.417  7.964  1.00 23.20  ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.016 17.941  7.298  1.00 27.82  ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.214 18.589  7.983  1.00 30.60  ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.834 17.679  6.095  1.00 30.65  ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.681 19.793  10.634 1.00 21.95  ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.807 20.116  11.758 0.50 22.16  ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.818 20.078  11.771 0.50 22.82  ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.372 19.654  11.506 1.00 22.53  ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.706 19.174  12.436 1.00 22.88  ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.826 21.626  12.023 0.50 22.99  ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 15.892 21.561  12.134 0.50 25.64  ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 14.867 21.996  13.001 0.50 24.15  ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.502 22.356  11.031 0.50 29.67  ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.878 19.808  10.249 1.00 22.06  ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.496 19.390  9.962  1.00 22.60  ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.280 17.891  10.168 1.00 21.76  ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.150 17.474  10.373 1.00 23.83  ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.051 19.788  8.555  1.00 25.76  ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.655 18.962  7.570  1.00 30.61  ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.346 17.083  10.098 1.00 19.60  ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.220 15.621  10.320 1.00 19.06  ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.674 15.164  11.727 1.00 19.33  ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.611 13.955  12.031 1.00 18.26  ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.105 14.896  9.285  1.00 20.14  ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.587 15.031  7.862  1.00 20.85  ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.487 14.345  6.852  1.00 21.20  ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.398 12.883  6.989  1.00 19.46  ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.526 12.035  5.969  1.00 21.16  ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.748 12.493  4.738  1.00 23.54  ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.425 10.718  6.170  1.00 18.99  ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.262 16.095  12.529 1.00 17.70  ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.862 15.774  13.823 1.00 17.89  ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.007 14.778  13.659 1.00 18.22  ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.235 13.933  14.546 1.00 17.62  ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.851 15.256  14.888 1.00 19.29  ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.444 15.060  16.278 1.00 20.49  ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.282 15.901  16.703 1.00 21.22  ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.089 14.051  16.947 1.00 19.86  ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.793 14.907  12.540 1.00 16.78  ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.901 13.967  12.343 1.00 16.70  ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.261 14.666  12.228 1.00 17.33  ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.345 15.781  11.705 1.00 18.39  ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.722 13.117  11.076 1.00 17.56  ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.616 12.025  11.128 1.00 19.04  ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.520 11.281  9.819  1.00 19.17  ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.866 11.005  12.276 1.00 19.81  ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.306 14.003  12.724 1.00 16.50  ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.681 14.490  12.548 1.00 16.37  ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.551 13.257  12.371 1.00 16.84  ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.350 12.240  13.064 1.00 17.12  ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.158 15.316  13.771 1.00 16.21  ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.598 15.906  13.681 1.00 17.16  ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.677 17.279  14.332 1.00 17.87  ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.646 14.952  14.319 1.00 17.91  ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.517 13.320  11.426 1.00 15.68  ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.448 12.213  11.205 1.00 16.44  ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.872 12.741  11.377 1.00 16.86  ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.195 13.799  10.826 1.00 17.83  ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.258 11.635  9.779  1.00 17.53  ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.284 10.538  9.514  1.00 19.13  ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.828 11.099  9.588  1.00 18.12  ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.688 12.063  12.198 1.00 16.22  ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.104 12.447  12.394 1.00 16.72  ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 29.009 11.277  11.949 1.00 18.68  ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.545 10.133  11.771 1.00 18.21  ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.399 12.816  13.848 1.00 17.35  ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.058 11.748  14.716 1.00 18.08  ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.311 11.561  11.735 1.00 20.04  ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.236 10.504  11.313 1.00 20.86  ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.862 9.793   12.513 1.00 22.04  ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.072 10.414  13.572 1.00 23.00  ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.336 11.104  10.439 1.00 23.16  ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.000 12.112  11.184 1.00 24.04  ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.178 8.483   12.349 1.00 21.89  ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.779 7.692   13.427 1.00 23.87  ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.116 7.110   12.986 1.00 26.38  ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.338 6.901   11.781 1.00 25.98  ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.856 6.518   13.837 1.00 24.69  ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.717 5.632   12.719 1.00 26.12  ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.492 6.995   14.252 1.00 24.96  ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.973 6.783   13.967 1.00 27.49  ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.245 6.157   13.651 1.00 29.44  ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.026 4.639   13.473 1.00 29.49  ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.545 4.056   12.517 1.00 31.08  ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.297 6.537   14.700 1.00 33.80  ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.876 6.051   15.966 1.00 37.42  ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.486 8.031   14.799 1.00 34.89  ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.219 4.021   14.342 1.00 28.81  ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.943 2.575   14.242 1.00 29.61  ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.737 2.281   13.338 1.00 28.63  ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.804 3.085   13.272 1.00 27.82  ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.673 1.999   15.622 1.00 31.15  ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.757 1.116   12.663 1.00 27.82  ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.655 0.685   11.812 1.00 28.40  ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.504 0.113   12.659 1.00 27.36  ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.752 -0.599  13.641 1.00 27.88  ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.134 -0.346  10.786 1.00 31.34  ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.843 0.291   9.584  1.00 36.68  ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.320 -0.727  8.574  1.00 43.81  ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 34.984 -1.715  8.910  1.00 44.57  ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.997 -0.489  7.312  1.00 45.96  ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.265 0.449   12.306 1.00 25.17  ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.107 -0.030  13.048 1.00 23.80  ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.506 -1.284  12.432 1.00 23.19  ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.822 -1.654  11.292 1.00 23.48  ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.618 -1.943  13.189 1.00 21.75  ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 27.024 -3.208  12.758 1.00 21.69  ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.591 -3.146  12.302 1.00 21.07  ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 25.056 -4.192  11.887 1.00 21.98  ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.170 -4.249  13.860 1.00 22.96  ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.890 -4.636  14.268 1.00 27.03  ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.923 -1.990  12.456 1.00 18.71  ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.537 -1.912  12.017 1.00 18.91  ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.472 -1.838  10.474 1.00 20.21  ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.382 -1.315  9.830  1.00 20.72  ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.881 -0.668  12.645 1.00 17.91  ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.762 -0.711  14.176 1.00 19.86  ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.459 -1.813  14.725 1.00 20.22  ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.948 0.360   14.837 1.00 20.48  ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.398 -2.369  9.900  1.00 21.27  ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 22.123 -2.309  8.462  1.00 22.87  ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.787 -1.563  8.299  1.00 22.26  ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.862 -1.809  9.079  1.00 22.34  ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.951 -3.736  7.917  1.00 27.76  ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 23.278 -4.341  7.924  1.00 31.31  ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 21.375 -3.755  6.508  1.00 30.43  ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.675 -0.696  7.273  1.00 21.78  ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.439 0.042   7.029  1.00 20.41  ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.479 -0.758  6.141  1.00 20.29  ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.876 -1.302  5.083  1.00 20.61  ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.705 1.440   6.419  1.00 19.63  ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.804 2.203   7.191  1.00 20.73  ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.417 2.285   6.319  1.00 19.62  ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.430 2.501   8.665  1.00 21.76  ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.207 -0.792  6.534  1.00 18.91  ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.164 -1.419  5.729  1.00 18.76  ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.912 -0.580  4.465  1.00 19.78  ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.918 0.667   4.506  1.00 18.75  ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.869 -1.472  6.540  1.00 18.72  ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.695 -1.258  3.327  1.00 21.28  ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.363 -0.560  2.082  1.00 22.79  ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 14.081 -1.271  1.616  1.00 25.16  ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 14.140 -2.313  0.958  1.00 26.28  ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.519 -0.658  1.050  1.00 22.91  ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.854 -0.092  1.584  1.00 23.20  ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.870 1.423   1.820  1.00 23.50  ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.187 1.863   2.326  1.00 22.89  ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.408 3.018   2.951  1.00 24.73  ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.415 3.875   3.148  1.00 23.44  ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.631 3.331   3.373  1.00 24.85  ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.929 -0.769  2.058  1.00 25.66  ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.634 -1.447  1.875  1.00 27.06  ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.460 -0.485  2.159  1.00 27.55  ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.658 0.677   2.517  1.00 27.94  ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.590 -2.586  2.881  1.00 27.47  ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.501 -1.980  4.589  1.00 26.45  ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 9.201  -1.005  2.053  1.00 28.75  ? 57  ASP   A N   1 
ATOM   397  C  CA  A ASP   A 1 51  ? 8.045  -0.195  2.409  0.50 29.50  ? 57  ASP   A CA  1 
ATOM   398  C  CA  B ASP   A 1 51  ? 8.034  -0.207  2.387  0.50 29.43  ? 57  ASP   A CA  1 
ATOM   399  C  C   . ASP   A 1 51  ? 7.228  -0.900  3.496  1.00 29.54  ? 57  ASP   A C   1 
ATOM   400  O  O   . ASP   A 1 51  ? 6.012  -0.752  3.548  1.00 30.45  ? 57  ASP   A O   1 
ATOM   401  C  CB  A ASP   A 1 51  ? 7.189  0.210   1.190  0.50 32.88  ? 57  ASP   A CB  1 
ATOM   402  C  CB  B ASP   A 1 51  ? 7.148  0.069   1.150  0.50 32.58  ? 57  ASP   A CB  1 
ATOM   403  C  CG  A ASP   A 1 51  ? 6.371  -0.917  0.620  0.50 38.62  ? 57  ASP   A CG  1 
ATOM   404  C  CG  B ASP   A 1 51  ? 6.120  1.170   1.352  0.50 37.87  ? 57  ASP   A CG  1 
ATOM   405  O  OD1 A ASP   A 1 51  ? 6.849  -2.070  0.659  0.50 39.33  ? 57  ASP   A OD1 1 
ATOM   406  O  OD1 B ASP   A 1 51  ? 6.216  1.904   2.377  0.50 39.43  ? 57  ASP   A OD1 1 
ATOM   407  O  OD2 A ASP   A 1 51  ? 5.242  -0.648  0.144  0.50 41.86  ? 57  ASP   A OD2 1 
ATOM   408  O  OD2 B ASP   A 1 51  ? 5.214  1.296   0.499  0.50 39.97  ? 57  ASP   A OD2 1 
ATOM   409  N  N   . CYS   A 1 52  ? 7.909  -1.628  4.414  1.00 27.15  ? 58  CYS   A N   1 
ATOM   410  C  CA  . CYS   A 1 52  ? 7.254  -2.293  5.558  1.00 24.48  ? 58  CYS   A CA  1 
ATOM   411  C  C   . CYS   A 1 52  ? 6.511  -1.285  6.364  1.00 22.99  ? 58  CYS   A C   1 
ATOM   412  O  O   . CYS   A 1 52  ? 6.961  -0.143  6.534  1.00 23.63  ? 58  CYS   A O   1 
ATOM   413  C  CB  . CYS   A 1 52  ? 8.285  -2.992  6.451  1.00 22.75  ? 58  CYS   A CB  1 
ATOM   414  S  SG  . CYS   A 1 52  ? 8.927  -4.564  5.831  1.00 25.35  ? 58  CYS   A SG  1 
ATOM   415  N  N   A GLN   A 1 53  ? 5.320  -1.684  6.864  0.50 21.28  ? 59  GLN   A N   1 
ATOM   416  N  N   B GLN   A 1 53  ? 5.375  -1.708  6.894  0.50 21.45  ? 59  GLN   A N   1 
ATOM   417  C  CA  A GLN   A 1 53  ? 4.515  -0.867  7.776  0.50 20.05  ? 59  GLN   A CA  1 
ATOM   418  C  CA  B GLN   A 1 53  ? 4.646  -0.841  7.788  0.50 20.37  ? 59  GLN   A CA  1 
ATOM   419  C  C   A GLN   A 1 53  ? 4.334  -1.588  9.149  0.50 19.00  ? 59  GLN   A C   1 
ATOM   420  C  C   B GLN   A 1 53  ? 4.310  -1.600  9.113  0.50 19.13  ? 59  GLN   A C   1 
ATOM   421  O  O   A GLN   A 1 53  ? 3.470  -1.179  9.919  0.50 19.07  ? 59  GLN   A O   1 
ATOM   422  O  O   B GLN   A 1 53  ? 3.410  -1.190  9.847  0.50 19.09  ? 59  GLN   A O   1 
ATOM   423  C  CB  A GLN   A 1 53  ? 3.134  -0.457  7.187  0.50 20.72  ? 59  GLN   A CB  1 
ATOM   424  C  CB  B GLN   A 1 53  ? 3.478  -0.149  7.069  0.50 21.83  ? 59  GLN   A CB  1 
ATOM   425  C  CG  A GLN   A 1 53  ? 3.144  0.860   6.383  0.50 22.17  ? 59  GLN   A CG  1 
ATOM   426  C  CG  B GLN   A 1 53  ? 3.989  0.751   5.880  0.50 23.97  ? 59  GLN   A CG  1 
ATOM   427  C  CD  A GLN   A 1 53  ? 1.764  1.394   6.004  0.50 24.18  ? 59  GLN   A CD  1 
ATOM   428  C  CD  B GLN   A 1 53  ? 4.964  1.866   6.289  0.50 26.32  ? 59  GLN   A CD  1 
ATOM   429  O  OE1 A GLN   A 1 53  ? 1.311  1.289   4.857  0.50 25.59  ? 59  GLN   A OE1 1 
ATOM   430  O  OE1 B GLN   A 1 53  ? 5.932  2.261   5.583  0.50 23.44  ? 59  GLN   A OE1 1 
ATOM   431  N  NE2 A GLN   A 1 53  ? 1.092  2.023   6.949  0.50 22.87  ? 59  GLN   A NE2 1 
ATOM   432  N  NE2 B GLN   A 1 53  ? 4.722  2.427   7.431  0.50 27.05  ? 59  GLN   A NE2 1 
ATOM   433  N  N   . THR   A 1 54  ? 5.077  -2.713  9.410  1.00 18.00  ? 60  THR   A N   1 
ATOM   434  C  CA  . THR   A 1 54  ? 5.054  -3.456  10.657 1.00 19.48  ? 60  THR   A CA  1 
ATOM   435  C  C   . THR   A 1 54  ? 6.517  -3.686  11.067 1.00 19.23  ? 60  THR   A C   1 
ATOM   436  O  O   . THR   A 1 54  ? 7.405  -3.905  10.210 1.00 20.35  ? 60  THR   A O   1 
ATOM   437  C  CB  . THR   A 1 54  ? 4.257  -4.774  10.630 1.00 23.97  ? 60  THR   A CB  1 
ATOM   438  O  OG1 . THR   A 1 54  ? 4.891  -5.704  9.760  1.00 27.70  ? 60  THR   A OG1 1 
ATOM   439  C  CG2 . THR   A 1 54  ? 2.845  -4.589  10.178 1.00 23.45  ? 60  THR   A CG2 1 
ATOM   440  N  N   . GLY   A 1 55  ? 6.765  -3.564  12.346 1.00 16.95  ? 61  GLY   A N   1 
ATOM   441  C  CA  . GLY   A 1 55  ? 8.120  -3.770  12.866 1.00 16.75  ? 61  GLY   A CA  1 
ATOM   442  C  C   . GLY   A 1 55  ? 8.146  -3.869  14.376 1.00 16.40  ? 61  GLY   A C   1 
ATOM   443  O  O   . GLY   A 1 55  ? 7.115  -4.097  14.997 1.00 16.98  ? 61  GLY   A O   1 
ATOM   444  N  N   . VAL   A 1 56  ? 9.316  -3.675  14.975 1.00 15.97  ? 62  VAL   A N   1 
ATOM   445  C  CA  . VAL   A 1 56  ? 9.475  -3.763  16.422 1.00 15.69  ? 62  VAL   A CA  1 
ATOM   446  C  C   . VAL   A 1 56  ? 10.350 -2.590  16.862 1.00 15.42  ? 62  VAL   A C   1 
ATOM   447  O  O   . VAL   A 1 56  ? 11.331 -2.274  16.183 1.00 16.42  ? 62  VAL   A O   1 
ATOM   448  C  CB  . VAL   A 1 56  ? 10.188 -5.090  16.785 1.00 17.00  ? 62  VAL   A CB  1 
ATOM   449  C  CG1 . VAL   A 1 56  ? 10.596 -5.120  18.262 1.00 19.98  ? 62  VAL   A CG1 1 
ATOM   450  C  CG2 . VAL   A 1 56  ? 9.298  -6.300  16.438 1.00 16.65  ? 62  VAL   A CG2 1 
ATOM   451  N  N   . TYR   A 1 57  ? 9.961  -1.891  17.957 1.00 14.76  ? 63  TYR   A N   1 
ATOM   452  C  CA  . TYR   A 1 57  ? 10.807 -0.785  18.424 1.00 14.22  ? 63  TYR   A CA  1 
ATOM   453  C  C   . TYR   A 1 57  ? 11.251 -0.994  19.876 1.00 15.27  ? 63  TYR   A C   1 
ATOM   454  O  O   . TYR   A 1 57  ? 10.542 -1.663  20.627 1.00 15.60  ? 63  TYR   A O   1 
ATOM   455  C  CB  . TYR   A 1 57  ? 10.104 0.594   18.265 1.00 13.81  ? 63  TYR   A CB  1 
ATOM   456  C  CG  . TYR   A 1 57  ? 9.092  0.933   19.356 1.00 14.72  ? 63  TYR   A CG  1 
ATOM   457  C  CD1 . TYR   A 1 57  ? 7.819  0.383   19.344 1.00 16.44  ? 63  TYR   A CD1 1 
ATOM   458  C  CD2 . TYR   A 1 57  ? 9.394  1.860   20.348 1.00 15.07  ? 63  TYR   A CD2 1 
ATOM   459  C  CE1 . TYR   A 1 57  ? 6.894  0.683   20.346 1.00 15.83  ? 63  TYR   A CE1 1 
ATOM   460  C  CE2 . TYR   A 1 57  ? 8.470  2.188   21.343 1.00 15.53  ? 63  TYR   A CE2 1 
ATOM   461  C  CZ  . TYR   A 1 57  ? 7.216  1.603   21.325 1.00 16.15  ? 63  TYR   A CZ  1 
ATOM   462  O  OH  . TYR   A 1 57  ? 6.290  1.882   22.299 1.00 18.18  ? 63  TYR   A OH  1 
ATOM   463  N  N   . TYR   A 1 58  ? 12.382 -0.354  20.266 1.00 15.68  ? 64  TYR   A N   1 
ATOM   464  C  CA  . TYR   A 1 58  ? 12.863 -0.420  21.626 1.00 15.68  ? 64  TYR   A CA  1 
ATOM   465  C  C   . TYR   A 1 58  ? 12.371 0.773   22.415 1.00 15.23  ? 64  TYR   A C   1 
ATOM   466  O  O   . TYR   A 1 58  ? 12.580 1.925   21.999 1.00 15.89  ? 64  TYR   A O   1 
ATOM   467  C  CB  . TYR   A 1 58  ? 14.406 -0.476  21.704 1.00 15.96  ? 64  TYR   A CB  1 
ATOM   468  C  CG  . TYR   A 1 58  ? 14.863 -0.588  23.133 1.00 16.58  ? 64  TYR   A CG  1 
ATOM   469  C  CD1 . TYR   A 1 58  ? 14.573 -1.714  23.883 1.00 18.04  ? 64  TYR   A CD1 1 
ATOM   470  C  CD2 . TYR   A 1 58  ? 15.635 0.412   23.720 1.00 16.90  ? 64  TYR   A CD2 1 
ATOM   471  C  CE1 . TYR   A 1 58  ? 14.969 -1.812  25.209 1.00 18.97  ? 64  TYR   A CE1 1 
ATOM   472  C  CE2 . TYR   A 1 58  ? 16.024 0.335   25.047 1.00 18.02  ? 64  TYR   A CE2 1 
ATOM   473  C  CZ  . TYR   A 1 58  ? 15.717 -0.796  25.775 1.00 19.47  ? 64  TYR   A CZ  1 
ATOM   474  O  OH  . TYR   A 1 58  ? 16.115 -0.876  27.077 1.00 21.27  ? 64  TYR   A OH  1 
ATOM   475  N  N   . CYS   A 1 59  ? 11.773 0.478   23.604 1.00 15.23  ? 65  CYS   A N   1 
ATOM   476  C  CA  . CYS   A 1 59  ? 11.216 1.489   24.530 1.00 16.34  ? 65  CYS   A CA  1 
ATOM   477  C  C   . CYS   A 1 59  ? 12.049 1.488   25.801 1.00 17.14  ? 65  CYS   A C   1 
ATOM   478  O  O   . CYS   A 1 59  ? 11.887 0.584   26.624 1.00 18.04  ? 65  CYS   A O   1 
ATOM   479  C  CB  . CYS   A 1 59  ? 9.753  1.149   24.808 1.00 16.59  ? 65  CYS   A CB  1 
ATOM   480  S  SG  . CYS   A 1 59  ? 8.976  2.248   26.023 1.00 18.03  ? 65  CYS   A SG  1 
ATOM   481  N  N   . SER   A 1 60  ? 12.950 2.490   25.963 1.00 17.46  ? 66  SER   A N   1 
ATOM   482  C  CA  . SER   A 1 60  ? 13.838 2.486   27.130 1.00 17.61  ? 66  SER   A CA  1 
ATOM   483  C  C   . SER   A 1 60  ? 13.086 2.644   28.462 1.00 18.46  ? 66  SER   A C   1 
ATOM   484  O  O   . SER   A 1 60  ? 13.509 2.057   29.446 1.00 18.84  ? 66  SER   A O   1 
ATOM   485  C  CB  . SER   A 1 60  ? 14.935 3.541   27.017 1.00 18.78  ? 66  SER   A CB  1 
ATOM   486  O  OG  . SER   A 1 60  ? 14.460 4.873   27.038 1.00 21.56  ? 66  SER   A OG  1 
ATOM   487  N  N   . SER   A 1 61  ? 11.945 3.395   28.460 1.00 16.63  ? 67  SER   A N   1 
ATOM   488  C  CA  . SER   A 1 61  ? 11.147 3.581   29.693 1.00 15.90  ? 67  SER   A CA  1 
ATOM   489  C  C   . SER   A 1 61  ? 10.421 2.317   30.160 1.00 14.99  ? 67  SER   A C   1 
ATOM   490  O  O   . SER   A 1 61  ? 9.818  2.338   31.232 1.00 16.26  ? 67  SER   A O   1 
ATOM   491  C  CB  . SER   A 1 61  ? 10.150 4.733   29.574 1.00 17.45  ? 67  SER   A CB  1 
ATOM   492  O  OG  . SER   A 1 61  ? 9.194  4.500   28.545 1.00 17.67  ? 67  SER   A OG  1 
ATOM   493  N  N   . ARG   A 1 62  ? 10.516 1.216   29.405 1.00 14.98  ? 68  ARG   A N   1 
ATOM   494  C  CA  . ARG   A 1 62  ? 9.947  -0.076  29.794 1.00 15.80  ? 68  ARG   A CA  1 
ATOM   495  C  C   . ARG   A 1 62  ? 10.976 -1.215  29.671 1.00 17.99  ? 68  ARG   A C   1 
ATOM   496  O  O   . ARG   A 1 62  ? 10.615 -2.370  29.942 1.00 19.13  ? 68  ARG   A O   1 
ATOM   497  C  CB  . ARG   A 1 62  ? 8.751  -0.442  28.874 1.00 16.74  ? 68  ARG   A CB  1 
ATOM   498  C  CG  . ARG   A 1 62  ? 7.550  0.506   29.016 1.00 18.35  ? 68  ARG   A CG  1 
ATOM   499  C  CD  . ARG   A 1 62  ? 6.769  0.206   30.274 1.00 17.72  ? 68  ARG   A CD  1 
ATOM   500  N  NE  . ARG   A 1 62  ? 5.612  1.106   30.393 1.00 18.91  ? 68  ARG   A NE  1 
ATOM   501  C  CZ  . ARG   A 1 62  ? 5.645  2.288   31.004 1.00 20.54  ? 68  ARG   A CZ  1 
ATOM   502  N  NH1 . ARG   A 1 62  ? 6.765  2.721   31.570 1.00 20.08  ? 68  ARG   A NH1 1 
ATOM   503  N  NH2 . ARG   A 1 62  ? 4.546  3.027   31.091 1.00 21.49  ? 68  ARG   A NH2 1 
ATOM   504  N  N   . ARG   A 1 63  ? 12.211 -0.928  29.201 1.00 18.97  ? 69  ARG   A N   1 
ATOM   505  C  CA  . ARG   A 1 63  ? 13.233 -1.961  28.929 1.00 20.21  ? 69  ARG   A CA  1 
ATOM   506  C  C   . ARG   A 1 63  ? 12.649 -3.102  28.072 1.00 21.48  ? 69  ARG   A C   1 
ATOM   507  O  O   . ARG   A 1 63  ? 12.823 -4.292  28.387 1.00 24.31  ? 69  ARG   A O   1 
ATOM   508  C  CB  . ARG   A 1 63  ? 13.813 -2.534  30.222 1.00 22.71  ? 69  ARG   A CB  1 
ATOM   509  C  CG  . ARG   A 1 63  ? 14.750 -1.572  30.870 1.00 24.06  ? 69  ARG   A CG  1 
ATOM   510  C  CD  . ARG   A 1 63  ? 15.622 -2.354  31.841 1.00 25.85  ? 69  ARG   A CD  1 
ATOM   511  N  NE  . ARG   A 1 63  ? 16.406 -1.388  32.602 1.00 28.46  ? 69  ARG   A NE  1 
ATOM   512  C  CZ  . ARG   A 1 63  ? 16.105 -0.983  33.830 1.00 27.33  ? 69  ARG   A CZ  1 
ATOM   513  N  NH1 . ARG   A 1 63  ? 15.060 -1.505  34.478 1.00 26.47  ? 69  ARG   A NH1 1 
ATOM   514  N  NH2 . ARG   A 1 63  ? 16.855 -0.075  34.432 1.00 26.28  ? 69  ARG   A NH2 1 
ATOM   515  N  N   . LYS   A 1 64  ? 11.869 -2.727  27.057 1.00 19.75  ? 70  LYS   A N   1 
ATOM   516  C  CA  . LYS   A 1 64  ? 11.150 -3.710  26.270 1.00 18.87  ? 70  LYS   A CA  1 
ATOM   517  C  C   . LYS   A 1 64  ? 11.085 -3.357  24.816 1.00 18.17  ? 70  LYS   A C   1 
ATOM   518  O  O   . LYS   A 1 64  ? 11.003 -2.190  24.485 1.00 17.67  ? 70  LYS   A O   1 
ATOM   519  C  CB  . LYS   A 1 64  ? 9.694  -3.813  26.771 1.00 22.50  ? 70  LYS   A CB  1 
ATOM   520  C  CG  . LYS   A 1 64  ? 9.550  -4.824  27.881 1.00 32.45  ? 70  LYS   A CG  1 
ATOM   521  C  CD  . LYS   A 1 64  ? 8.147  -5.398  27.939 1.00 41.84  ? 70  LYS   A CD  1 
ATOM   522  C  CE  . LYS   A 1 64  ? 7.926  -6.011  29.306 1.00 47.23  ? 70  LYS   A CE  1 
ATOM   523  N  NZ  . LYS   A 1 64  ? 8.381  -5.095  30.391 1.00 50.42  ? 70  LYS   A NZ  1 
ATOM   524  N  N   . HIS   A 1 65  ? 11.047 -4.376  23.957 1.00 17.49  ? 71  HIS   A N   1 
ATOM   525  C  CA  . HIS   A 1 65  ? 10.846 -4.201  22.525 1.00 17.11  ? 71  HIS   A CA  1 
ATOM   526  C  C   . HIS   A 1 65  ? 9.388  -4.554  22.238 1.00 17.75  ? 71  HIS   A C   1 
ATOM   527  O  O   . HIS   A 1 65  ? 8.897  -5.599  22.713 1.00 19.97  ? 71  HIS   A O   1 
ATOM   528  C  CB  . HIS   A 1 65  ? 11.764 -5.181  21.736 1.00 16.19  ? 71  HIS   A CB  1 
ATOM   529  C  CG  . HIS   A 1 65  ? 13.239 -4.885  21.894 1.00 17.14  ? 71  HIS   A CG  1 
ATOM   530  N  ND1 . HIS   A 1 65  ? 13.962 -4.209  20.913 1.00 21.28  ? 71  HIS   A ND1 1 
ATOM   531  C  CD2 . HIS   A 1 65  ? 14.084 -5.218  22.896 1.00 17.93  ? 71  HIS   A CD2 1 
ATOM   532  C  CE1 . HIS   A 1 65  ? 15.221 -4.158  21.352 1.00 19.37  ? 71  HIS   A CE1 1 
ATOM   533  N  NE2 . HIS   A 1 65  ? 15.331 -4.720  22.553 1.00 20.49  ? 71  HIS   A NE2 1 
ATOM   534  N  N   . TYR   A 1 66  ? 8.663  -3.680  21.483 1.00 16.03  ? 72  TYR   A N   1 
ATOM   535  C  CA  . TYR   A 1 66  ? 7.240  -3.908  21.192 1.00 16.75  ? 72  TYR   A CA  1 
ATOM   536  C  C   . TYR   A 1 66  ? 6.985  -4.008  19.707 1.00 17.10  ? 72  TYR   A C   1 
ATOM   537  O  O   . TYR   A 1 66  ? 7.465  -3.162  18.953 1.00 17.07  ? 72  TYR   A O   1 
ATOM   538  C  CB  . TYR   A 1 66  ? 6.424  -2.675  21.702 1.00 16.58  ? 72  TYR   A CB  1 
ATOM   539  C  CG  . TYR   A 1 66  ? 6.376  -2.541  23.214 1.00 17.31  ? 72  TYR   A CG  1 
ATOM   540  C  CD1 . TYR   A 1 66  ? 5.597  -3.398  23.988 1.00 18.80  ? 72  TYR   A CD1 1 
ATOM   541  C  CD2 . TYR   A 1 66  ? 7.106  -1.561  23.864 1.00 17.87  ? 72  TYR   A CD2 1 
ATOM   542  C  CE1 . TYR   A 1 66  ? 5.518  -3.260  25.378 1.00 19.87  ? 72  TYR   A CE1 1 
ATOM   543  C  CE2 . TYR   A 1 66  ? 7.031  -1.400  25.251 1.00 19.28  ? 72  TYR   A CE2 1 
ATOM   544  C  CZ  . TYR   A 1 66  ? 6.240  -2.256  26.008 1.00 20.09  ? 72  TYR   A CZ  1 
ATOM   545  O  OH  . TYR   A 1 66  ? 6.211  -2.091  27.381 1.00 21.48  ? 72  TYR   A OH  1 
ATOM   546  N  N   . PRO   A 1 67  ? 6.159  -4.971  19.273 1.00 17.41  ? 73  PRO   A N   1 
ATOM   547  C  CA  . PRO   A 1 67  ? 5.761  -5.008  17.846 1.00 17.72  ? 73  PRO   A CA  1 
ATOM   548  C  C   . PRO   A 1 67  ? 4.724  -3.901  17.584 1.00 19.90  ? 73  PRO   A C   1 
ATOM   549  O  O   . PRO   A 1 67  ? 3.835  -3.658  18.423 1.00 21.63  ? 73  PRO   A O   1 
ATOM   550  C  CB  . PRO   A 1 67  ? 5.105  -6.396  17.678 1.00 18.57  ? 73  PRO   A CB  1 
ATOM   551  C  CG  . PRO   A 1 67  ? 4.686  -6.796  19.096 1.00 20.06  ? 73  PRO   A CG  1 
ATOM   552  C  CD  . PRO   A 1 67  ? 5.537  -6.053  20.081 1.00 18.32  ? 73  PRO   A CD  1 
ATOM   553  N  N   . VAL   A 1 68  ? 4.853  -3.214  16.447 1.00 18.27  ? 74  VAL   A N   1 
ATOM   554  C  CA  . VAL   A 1 68  ? 3.921  -2.151  16.111 1.00 19.53  ? 74  VAL   A CA  1 
ATOM   555  C  C   . VAL   A 1 68  ? 3.612  -2.140  14.636 1.00 19.02  ? 74  VAL   A C   1 
ATOM   556  O  O   . VAL   A 1 68  ? 4.437  -2.545  13.819 1.00 18.35  ? 74  VAL   A O   1 
ATOM   557  C  CB  . VAL   A 1 68  ? 4.488  -0.752  16.489 1.00 22.42  ? 74  VAL   A CB  1 
ATOM   558  C  CG1 . VAL   A 1 68  ? 4.436  -0.513  17.990 1.00 24.23  ? 74  VAL   A CG1 1 
ATOM   559  C  CG2 . VAL   A 1 68  ? 5.900  -0.560  15.934 1.00 22.56  ? 74  VAL   A CG2 1 
ATOM   560  N  N   . SER   A 1 69  ? 2.431  -1.582  14.290 1.00 18.82  ? 75  SER   A N   1 
ATOM   561  C  CA  . SER   A 1 69  ? 2.055  -1.216  12.942 1.00 19.06  ? 75  SER   A CA  1 
ATOM   562  C  C   . SER   A 1 69  ? 2.231  0.315   12.913 1.00 17.85  ? 75  SER   A C   1 
ATOM   563  O  O   . SER   A 1 69  ? 1.807  1.009   13.883 1.00 17.66  ? 75  SER   A O   1 
ATOM   564  C  CB  . SER   A 1 69  ? 0.572  -1.509  12.708 1.00 23.27  ? 75  SER   A CB  1 
ATOM   565  O  OG  . SER   A 1 69  ? 0.358  -2.908  12.818 1.00 29.29  ? 75  SER   A OG  1 
ATOM   566  N  N   . PHE   A 1 70  ? 2.857  0.839   11.852 1.00 17.65  ? 76  PHE   A N   1 
ATOM   567  C  CA  . PHE   A 1 70  ? 3.136  2.258   11.761 1.00 18.16  ? 76  PHE   A CA  1 
ATOM   568  C  C   . PHE   A 1 70  ? 2.732  2.845   10.436 1.00 19.40  ? 76  PHE   A C   1 
ATOM   569  O  O   . PHE   A 1 70  ? 2.667  2.145   9.418  1.00 20.18  ? 76  PHE   A O   1 
ATOM   570  C  CB  . PHE   A 1 70  ? 4.620  2.560   12.105 1.00 17.52  ? 76  PHE   A CB  1 
ATOM   571  C  CG  . PHE   A 1 70  ? 5.643  1.750   11.313 1.00 17.44  ? 76  PHE   A CG  1 
ATOM   572  C  CD1 . PHE   A 1 70  ? 6.070  0.518   11.759 1.00 17.45  ? 76  PHE   A CD1 1 
ATOM   573  C  CD2 . PHE   A 1 70  ? 6.222  2.258   10.156 1.00 17.86  ? 76  PHE   A CD2 1 
ATOM   574  C  CE1 . PHE   A 1 70  ? 7.019  -0.212  11.042 1.00 18.18  ? 76  PHE   A CE1 1 
ATOM   575  C  CE2 . PHE   A 1 70  ? 7.159  1.505   9.418  1.00 18.34  ? 76  PHE   A CE2 1 
ATOM   576  C  CZ  . PHE   A 1 70  ? 7.556  0.282   9.881  1.00 17.87  ? 76  PHE   A CZ  1 
ATOM   577  N  N   . SER   A 1 71  ? 2.410  4.137   10.443 1.00 19.27  ? 77  SER   A N   1 
ATOM   578  C  CA  . SER   A 1 71  ? 1.980  4.840   9.247  1.00 19.37  ? 77  SER   A CA  1 
ATOM   579  C  C   . SER   A 1 71  ? 3.164  5.104   8.264  1.00 19.45  ? 77  SER   A C   1 
ATOM   580  O  O   . SER   A 1 71  ? 4.320  4.947   8.625  1.00 19.21  ? 77  SER   A O   1 
ATOM   581  C  CB  . SER   A 1 71  ? 1.258  6.140   9.621  1.00 21.60  ? 77  SER   A CB  1 
ATOM   582  O  OG  . SER   A 1 71  ? 2.133  7.049   10.271 1.00 25.21  ? 77  SER   A OG  1 
ATOM   583  N  N   . LYS   A 1 72  ? 2.870  5.476   7.028  1.00 19.68  ? 78  LYS   A N   1 
ATOM   584  C  CA  . LYS   A 1 72  ? 3.890  5.785   6.039  1.00 21.18  ? 78  LYS   A CA  1 
ATOM   585  C  C   . LYS   A 1 72  ? 4.514  7.139   6.379  1.00 21.91  ? 78  LYS   A C   1 
ATOM   586  O  O   . LYS   A 1 72  ? 3.826  8.008   6.934  1.00 21.84  ? 78  LYS   A O   1 
ATOM   587  C  CB  . LYS   A 1 72  ? 3.262  5.792   4.636  1.00 24.13  ? 78  LYS   A CB  1 
ATOM   588  C  CG  . LYS   A 1 72  ? 2.898  4.386   4.162  1.00 29.16  ? 78  LYS   A CG  1 
ATOM   589  C  CD  . LYS   A 1 72  ? 2.459  4.394   2.703  1.00 35.54  ? 78  LYS   A CD  1 
ATOM   590  C  CE  . LYS   A 1 72  ? 2.112  3.004   2.233  1.00 41.16  ? 78  LYS   A CE  1 
ATOM   591  N  NZ  . LYS   A 1 72  ? 2.418  2.824   0.788  1.00 45.30  ? 78  LYS   A NZ  1 
ATOM   592  N  N   . PRO   A 1 73  ? 5.797  7.347   6.047  1.00 22.22  ? 79  PRO   A N   1 
ATOM   593  C  CA  . PRO   A 1 73  ? 6.453  8.624   6.381  1.00 22.73  ? 79  PRO   A CA  1 
ATOM   594  C  C   . PRO   A 1 73  ? 5.679  9.829   5.843  1.00 23.83  ? 79  PRO   A C   1 
ATOM   595  O  O   . PRO   A 1 73  ? 5.293  9.838   4.676  1.00 24.50  ? 79  PRO   A O   1 
ATOM   596  C  CB  . PRO   A 1 73  ? 7.853  8.509   5.728  1.00 24.44  ? 79  PRO   A CB  1 
ATOM   597  C  CG  . PRO   A 1 73  ? 8.049  7.068   5.374  1.00 25.80  ? 79  PRO   A CG  1 
ATOM   598  C  CD  . PRO   A 1 73  ? 6.709  6.382   5.383  1.00 23.36  ? 79  PRO   A CD  1 
ATOM   599  N  N   . SER   A 1 74  ? 5.376  10.786  6.715  1.00 23.68  ? 80  SER   A N   1 
ATOM   600  C  CA  . SER   A 1 74  ? 4.534  11.923  6.326  1.00 24.97  ? 80  SER   A CA  1 
ATOM   601  C  C   . SER   A 1 74  ? 4.899  13.197  7.095  1.00 24.09  ? 80  SER   A C   1 
ATOM   602  O  O   . SER   A 1 74  ? 5.733  13.184  7.996  1.00 23.09  ? 80  SER   A O   1 
ATOM   603  C  CB  . SER   A 1 74  ? 3.051  11.602  6.579  1.00 30.60  ? 80  SER   A CB  1 
ATOM   604  O  OG  . SER   A 1 74  ? 2.711  10.228  6.494  1.00 37.72  ? 80  SER   A OG  1 
ATOM   605  N  N   . LEU   A 1 75  ? 4.249  14.301  6.735  1.00 24.80  ? 81  LEU   A N   1 
ATOM   606  C  CA  . LEU   A 1 75  ? 4.431  15.604  7.353  1.00 26.65  ? 81  LEU   A CA  1 
ATOM   607  C  C   . LEU   A 1 75  ? 3.347  15.713  8.445  1.00 27.84  ? 81  LEU   A C   1 
ATOM   608  O  O   . LEU   A 1 75  ? 2.144  15.680  8.140  1.00 28.86  ? 81  LEU   A O   1 
ATOM   609  C  CB  . LEU   A 1 75  ? 4.215  16.685  6.264  1.00 27.74  ? 81  LEU   A CB  1 
ATOM   610  C  CG  . LEU   A 1 75  ? 4.540  18.102  6.638  1.00 31.13  ? 81  LEU   A CG  1 
ATOM   611  C  CD1 . LEU   A 1 75  ? 6.011  18.269  6.951  1.00 32.28  ? 81  LEU   A CD1 1 
ATOM   612  C  CD2 . LEU   A 1 75  ? 4.171  19.066  5.510  1.00 32.20  ? 81  LEU   A CD2 1 
ATOM   613  N  N   . ILE   A 1 76  ? 3.759  15.791  9.719  1.00 26.80  ? 82  ILE   A N   1 
ATOM   614  C  CA  . ILE   A 1 76  ? 2.834  15.808  10.859 1.00 27.09  ? 82  ILE   A CA  1 
ATOM   615  C  C   . ILE   A 1 76  ? 3.084  16.977  11.822 1.00 27.40  ? 82  ILE   A C   1 
ATOM   616  O  O   . ILE   A 1 76  ? 4.223  17.276  12.145 1.00 25.40  ? 82  ILE   A O   1 
ATOM   617  C  CB  . ILE   A 1 76  ? 2.998  14.469  11.615 1.00 27.29  ? 82  ILE   A CB  1 
ATOM   618  C  CG1 . ILE   A 1 76  ? 2.671  13.278  10.684 1.00 28.88  ? 82  ILE   A CG1 1 
ATOM   619  C  CG2 . ILE   A 1 76  ? 2.157  14.451  12.918 1.00 27.80  ? 82  ILE   A CG2 1 
ATOM   620  C  CD1 . ILE   A 1 76  ? 2.738  11.969  11.258 1.00 30.31  ? 82  ILE   A CD1 1 
ATOM   621  N  N   . PHE   A 1 77  ? 2.011  17.579  12.347 1.00 28.82  ? 83  PHE   A N   1 
ATOM   622  C  CA  . PHE   A 1 77  ? 2.172  18.695  13.277 1.00 30.31  ? 83  PHE   A CA  1 
ATOM   623  C  C   . PHE   A 1 77  ? 2.589  18.155  14.661 1.00 31.43  ? 83  PHE   A C   1 
ATOM   624  O  O   . PHE   A 1 77  ? 1.952  17.240  15.174 1.00 33.03  ? 83  PHE   A O   1 
ATOM   625  C  CB  . PHE   A 1 77  ? 0.882  19.500  13.385 1.00 31.23  ? 83  PHE   A CB  1 
ATOM   626  C  CG  . PHE   A 1 77  ? 1.118  20.805  14.094 1.00 33.17  ? 83  PHE   A CG  1 
ATOM   627  C  CD1 . PHE   A 1 77  ? 1.783  21.842  13.463 1.00 34.50  ? 83  PHE   A CD1 1 
ATOM   628  C  CD2 . PHE   A 1 77  ? 0.682  20.993  15.393 1.00 34.89  ? 83  PHE   A CD2 1 
ATOM   629  C  CE1 . PHE   A 1 77  ? 1.993  23.054  14.114 1.00 36.66  ? 83  PHE   A CE1 1 
ATOM   630  C  CE2 . PHE   A 1 77  ? 0.902  22.199  16.045 1.00 35.12  ? 83  PHE   A CE2 1 
ATOM   631  C  CZ  . PHE   A 1 77  ? 1.543  23.223  15.401 1.00 36.38  ? 83  PHE   A CZ  1 
ATOM   632  N  N   . VAL   A 1 78  ? 3.700  18.669  15.221 1.00 30.89  ? 84  VAL   A N   1 
ATOM   633  C  CA  . VAL   A 1 78  ? 4.209  18.255  16.532 1.00 31.07  ? 84  VAL   A CA  1 
ATOM   634  C  C   . VAL   A 1 78  ? 4.111  19.452  17.490 1.00 31.41  ? 84  VAL   A C   1 
ATOM   635  O  O   . VAL   A 1 78  ? 4.577  20.523  17.121 1.00 32.51  ? 84  VAL   A O   1 
ATOM   636  C  CB  . VAL   A 1 78  ? 5.679  17.798  16.402 1.00 31.17  ? 84  VAL   A CB  1 
ATOM   637  C  CG1 . VAL   A 1 78  ? 6.241  17.396  17.768 1.00 32.14  ? 84  VAL   A CG1 1 
ATOM   638  C  CG2 . VAL   A 1 78  ? 5.793  16.629  15.400 1.00 30.76  ? 84  VAL   A CG2 1 
ATOM   639  N  N   . GLU   A 1 79  ? 3.586  19.262  18.717 1.00 31.56  ? 85  GLU   A N   1 
ATOM   640  C  CA  . GLU   A 1 79  ? 3.473  20.354  19.692 1.00 33.34  ? 85  GLU   A CA  1 
ATOM   641  C  C   . GLU   A 1 79  ? 4.834  20.865  20.157 1.00 33.87  ? 85  GLU   A C   1 
ATOM   642  O  O   . GLU   A 1 79  ? 5.844  20.165  20.042 1.00 34.25  ? 85  GLU   A O   1 
ATOM   643  C  CB  . GLU   A 1 79  ? 2.645  19.908  20.921 1.00 37.06  ? 85  GLU   A CB  1 
ATOM   644  C  CG  . GLU   A 1 79  ? 1.164  19.710  20.647 1.00 45.06  ? 85  GLU   A CG  1 
ATOM   645  C  CD  . GLU   A 1 79  ? 0.471  20.904  20.029 1.00 55.75  ? 85  GLU   A CD  1 
ATOM   646  O  OE1 . GLU   A 1 79  ? 0.685  22.047  20.497 1.00 57.16  ? 85  GLU   A OE1 1 
ATOM   647  O  OE2 . GLU   A 1 79  ? -0.284 20.693  19.055 1.00 60.21  ? 85  GLU   A OE2 1 
ATOM   648  N  N   . ALA   A 1 80  ? 4.836  22.090  20.734 1.00 33.71  ? 86  ALA   A N   1 
ATOM   649  C  CA  . ALA   A 1 80  ? 6.053  22.717  21.239 1.00 33.96  ? 86  ALA   A CA  1 
ATOM   650  C  C   . ALA   A 1 80  ? 6.634  21.892  22.350 1.00 34.58  ? 86  ALA   A C   1 
ATOM   651  O  O   . ALA   A 1 80  ? 5.904  21.286  23.132 1.00 36.46  ? 86  ALA   A O   1 
ATOM   652  C  CB  . ALA   A 1 80  ? 5.748  24.113  21.766 1.00 34.20  ? 86  ALA   A CB  1 
ATOM   653  N  N   . SER   A 1 81  ? 7.953  21.829  22.391 1.00 32.98  ? 87  SER   A N   1 
ATOM   654  C  CA  . SER   A 1 81  ? 8.710  21.157  23.441 1.00 32.55  ? 87  SER   A CA  1 
ATOM   655  C  C   . SER   A 1 81  ? 9.864  22.135  23.819 1.00 32.81  ? 87  SER   A C   1 
ATOM   656  O  O   . SER   A 1 81  ? 9.974  23.228  23.242 1.00 33.30  ? 87  SER   A O   1 
ATOM   657  C  CB  . SER   A 1 81  ? 9.310  19.850  22.909 1.00 32.44  ? 87  SER   A CB  1 
ATOM   658  O  OG  . SER   A 1 81  ? 10.291 20.134  21.922 1.00 32.80  ? 87  SER   A OG  1 
ATOM   659  N  N   . GLU   A 1 82  ? 10.726 21.752  24.771 1.00 33.38  ? 88  GLU   A N   1 
ATOM   660  C  CA  . GLU   A 1 82  ? 11.905 22.581  25.100 1.00 33.66  ? 88  GLU   A CA  1 
ATOM   661  C  C   . GLU   A 1 82  ? 12.936 22.548  23.931 1.00 31.10  ? 88  GLU   A C   1 
ATOM   662  O  O   . GLU   A 1 82  ? 13.904 23.284  23.976 1.00 30.92  ? 88  GLU   A O   1 
ATOM   663  C  CB  . GLU   A 1 82  ? 12.646 22.039  26.339 1.00 38.99  ? 88  GLU   A CB  1 
ATOM   664  C  CG  . GLU   A 1 82  ? 11.811 21.326  27.380 1.00 48.31  ? 88  GLU   A CG  1 
ATOM   665  C  CD  . GLU   A 1 82  ? 12.157 19.853  27.473 1.00 59.87  ? 88  GLU   A CD  1 
ATOM   666  O  OE1 . GLU   A 1 82  ? 13.076 19.503  28.252 1.00 60.15  ? 88  GLU   A OE1 1 
ATOM   667  O  OE2 . GLU   A 1 82  ? 11.511 19.047  26.759 1.00 64.89  ? 88  GLU   A OE2 1 
ATOM   668  N  N   . TYR   A 1 83  ? 12.761 21.669  22.919 1.00 29.04  ? 89  TYR   A N   1 
ATOM   669  C  CA  . TYR   A 1 83  ? 13.730 21.516  21.853 1.00 27.35  ? 89  TYR   A CA  1 
ATOM   670  C  C   . TYR   A 1 83  ? 13.327 22.161  20.561 1.00 27.18  ? 89  TYR   A C   1 
ATOM   671  O  O   . TYR   A 1 83  ? 14.203 22.534  19.804 1.00 27.38  ? 89  TYR   A O   1 
ATOM   672  C  CB  . TYR   A 1 83  ? 14.000 20.014  21.627 1.00 26.33  ? 89  TYR   A CB  1 
ATOM   673  C  CG  . TYR   A 1 83  ? 14.620 19.351  22.831 1.00 27.10  ? 89  TYR   A CG  1 
ATOM   674  C  CD1 . TYR   A 1 83  ? 15.960 19.528  23.132 1.00 28.60  ? 89  TYR   A CD1 1 
ATOM   675  C  CD2 . TYR   A 1 83  ? 13.852 18.600  23.709 1.00 29.34  ? 89  TYR   A CD2 1 
ATOM   676  C  CE1 . TYR   A 1 83  ? 16.547 18.900  24.220 1.00 30.09  ? 89  TYR   A CE1 1 
ATOM   677  C  CE2 . TYR   A 1 83  ? 14.419 17.995  24.828 1.00 30.68  ? 89  TYR   A CE2 1 
ATOM   678  C  CZ  . TYR   A 1 83  ? 15.771 18.136  25.070 1.00 32.36  ? 89  TYR   A CZ  1 
ATOM   679  O  OH  . TYR   A 1 83  ? 16.358 17.522  26.149 1.00 35.95  ? 89  TYR   A OH  1 
ATOM   680  N  N   . TYR   A 1 84  ? 11.997 22.248  20.270 1.00 27.44  ? 90  TYR   A N   1 
ATOM   681  C  CA  . TYR   A 1 84  ? 11.504 22.884  19.043 1.00 27.39  ? 90  TYR   A CA  1 
ATOM   682  C  C   . TYR   A 1 84  ? 10.190 23.613  19.367 1.00 30.32  ? 90  TYR   A C   1 
ATOM   683  O  O   . TYR   A 1 84  ? 9.378  23.101  20.156 1.00 30.93  ? 90  TYR   A O   1 
ATOM   684  C  CB  . TYR   A 1 84  ? 11.178 21.837  17.950 1.00 25.01  ? 90  TYR   A CB  1 
ATOM   685  C  CG  . TYR   A 1 84  ? 12.325 20.950  17.482 1.00 22.17  ? 90  TYR   A CG  1 
ATOM   686  C  CD1 . TYR   A 1 84  ? 13.284 21.424  16.592 1.00 22.60  ? 90  TYR   A CD1 1 
ATOM   687  C  CD2 . TYR   A 1 84  ? 12.395 19.622  17.861 1.00 21.11  ? 90  TYR   A CD2 1 
ATOM   688  C  CE1 . TYR   A 1 84  ? 14.312 20.597  16.126 1.00 21.53  ? 90  TYR   A CE1 1 
ATOM   689  C  CE2 . TYR   A 1 84  ? 13.438 18.801  17.442 1.00 20.57  ? 90  TYR   A CE2 1 
ATOM   690  C  CZ  . TYR   A 1 84  ? 14.391 19.285  16.562 1.00 21.16  ? 90  TYR   A CZ  1 
ATOM   691  O  OH  . TYR   A 1 84  ? 15.415 18.448  16.128 1.00 19.39  ? 90  TYR   A OH  1 
ATOM   692  N  N   . PRO   A 1 85  ? 9.882  24.683  18.626 1.00 32.14  ? 91  PRO   A N   1 
ATOM   693  C  CA  . PRO   A 1 85  ? 8.527  25.260  18.742 1.00 33.88  ? 91  PRO   A CA  1 
ATOM   694  C  C   . PRO   A 1 85  ? 7.512  24.269  18.134 1.00 35.14  ? 91  PRO   A C   1 
ATOM   695  O  O   . PRO   A 1 85  ? 7.907  23.240  17.534 1.00 35.07  ? 91  PRO   A O   1 
ATOM   696  C  CB  . PRO   A 1 85  ? 8.623  26.555  17.913 1.00 34.41  ? 91  PRO   A CB  1 
ATOM   697  C  CG  . PRO   A 1 85  ? 9.673  26.276  16.898 1.00 34.40  ? 91  PRO   A CG  1 
ATOM   698  C  CD  . PRO   A 1 85  ? 10.668 25.317  17.544 1.00 32.03  ? 91  PRO   A CD  1 
ATOM   699  N  N   . ALA   A 1 86  ? 6.203  24.573  18.214 1.00 35.75  ? 92  ALA   A N   1 
ATOM   700  C  CA  . ALA   A 1 86  ? 5.194  23.705  17.574 1.00 35.49  ? 92  ALA   A CA  1 
ATOM   701  C  C   . ALA   A 1 86  ? 5.407  23.891  16.056 1.00 34.28  ? 92  ALA   A C   1 
ATOM   702  O  O   . ALA   A 1 86  ? 5.628  25.016  15.607 1.00 35.85  ? 92  ALA   A O   1 
ATOM   703  C  CB  . ALA   A 1 86  ? 3.788  24.134  17.988 1.00 36.20  ? 92  ALA   A CB  1 
ATOM   704  N  N   . ARG   A 1 87  ? 5.525  22.790  15.310 1.00 32.12  ? 93  ARG   A N   1 
ATOM   705  C  CA  . ARG   A 1 87  ? 5.880  22.875  13.897 1.00 29.64  ? 93  ARG   A CA  1 
ATOM   706  C  C   . ARG   A 1 87  ? 5.523  21.553  13.193 1.00 29.09  ? 93  ARG   A C   1 
ATOM   707  O  O   . ARG   A 1 87  ? 5.190  20.579  13.852 1.00 29.27  ? 93  ARG   A O   1 
ATOM   708  C  CB  . ARG   A 1 87  ? 7.416  23.105  13.775 1.00 29.35  ? 93  ARG   A CB  1 
ATOM   709  C  CG  . ARG   A 1 87  ? 8.230  21.780  14.105 1.00 28.52  ? 93  ARG   A CG  1 
ATOM   710  C  CD  . ARG   A 1 87  ? 9.684  21.904  14.468 1.00 29.12  ? 93  ARG   A CD  1 
ATOM   711  N  NE  . ARG   A 1 87  ? 10.528 20.750  14.106 1.00 28.40  ? 93  ARG   A NE  1 
ATOM   712  C  CZ  . ARG   A 1 87  ? 10.540 19.542  14.676 1.00 27.77  ? 93  ARG   A CZ  1 
ATOM   713  N  NH1 . ARG   A 1 87  ? 9.603  19.207  15.576 1.00 27.86  ? 93  ARG   A NH1 1 
ATOM   714  N  NH2 . ARG   A 1 87  ? 11.436 18.626  14.293 1.00 23.01  ? 93  ARG   A NH2 1 
ATOM   715  N  N   . TYR   A 1 88  ? 5.671  21.527  11.858 1.00 28.21  ? 94  TYR   A N   1 
ATOM   716  C  CA  . TYR   A 1 88  ? 5.472  20.317  11.100 1.00 28.16  ? 94  TYR   A CA  1 
ATOM   717  C  C   . TYR   A 1 88  ? 6.799  19.585  11.028 1.00 26.60  ? 94  TYR   A C   1 
ATOM   718  O  O   . TYR   A 1 88  ? 7.826  20.196  10.734 1.00 27.13  ? 94  TYR   A O   1 
ATOM   719  C  CB  . TYR   A 1 88  ? 5.025  20.667  9.685  1.00 28.81  ? 94  TYR   A CB  1 
ATOM   720  C  CG  . TYR   A 1 88  ? 3.554  21.017  9.636  1.00 31.00  ? 94  TYR   A CG  1 
ATOM   721  C  CD1 . TYR   A 1 88  ? 2.586  20.024  9.581  1.00 32.23  ? 94  TYR   A CD1 1 
ATOM   722  C  CD2 . TYR   A 1 88  ? 3.128  22.327  9.766  1.00 32.95  ? 94  TYR   A CD2 1 
ATOM   723  C  CE1 . TYR   A 1 88  ? 1.233  20.331  9.604  1.00 34.57  ? 94  TYR   A CE1 1 
ATOM   724  C  CE2 . TYR   A 1 88  ? 1.776  22.649  9.761  1.00 34.89  ? 94  TYR   A CE2 1 
ATOM   725  C  CZ  . TYR   A 1 88  ? 0.830  21.644  9.700  1.00 36.46  ? 94  TYR   A CZ  1 
ATOM   726  O  OH  . TYR   A 1 88  ? -0.513 21.943  9.703  1.00 40.84  ? 94  TYR   A OH  1 
ATOM   727  N  N   . GLN   A 1 89  ? 6.797  18.274  11.339 1.00 23.86  ? 95  GLN   A N   1 
ATOM   728  C  CA  . GLN   A 1 89  ? 7.982  17.432  11.216 1.00 22.19  ? 95  GLN   A CA  1 
ATOM   729  C  C   . GLN   A 1 89  ? 7.763  16.515  10.021 1.00 21.64  ? 95  GLN   A C   1 
ATOM   730  O  O   . GLN   A 1 89  ? 6.682  15.929  9.891  1.00 21.97  ? 95  GLN   A O   1 
ATOM   731  C  CB  . GLN   A 1 89  ? 8.265  16.648  12.515 1.00 21.48  ? 95  GLN   A CB  1 
ATOM   732  C  CG  . GLN   A 1 89  ? 9.503  15.766  12.431 1.00 20.63  ? 95  GLN   A CG  1 
ATOM   733  C  CD  . GLN   A 1 89  ? 10.013 15.274  13.789 1.00 21.16  ? 95  GLN   A CD  1 
ATOM   734  O  OE1 . GLN   A 1 89  ? 10.028 15.987  14.793 1.00 23.70  ? 95  GLN   A OE1 1 
ATOM   735  N  NE2 . GLN   A 1 89  ? 10.455 14.017  13.834 1.00 20.53  ? 95  GLN   A NE2 1 
ATOM   736  N  N   . SER   A 1 90  ? 8.757  16.421  9.119  1.00 20.43  ? 96  SER   A N   1 
ATOM   737  C  CA  . SER   A 1 90  ? 8.628  15.596  7.934  1.00 20.46  ? 96  SER   A CA  1 
ATOM   738  C  C   . SER   A 1 90  ? 9.218  14.189  8.142  1.00 20.58  ? 96  SER   A C   1 
ATOM   739  O  O   . SER   A 1 90  ? 9.994  13.968  9.080  1.00 19.97  ? 96  SER   A O   1 
ATOM   740  C  CB  . SER   A 1 90  ? 9.308  16.290  6.761  1.00 23.78  ? 96  SER   A CB  1 
ATOM   741  O  OG  . SER   A 1 90  ? 10.703 16.414  7.028  1.00 27.31  ? 96  SER   A OG  1 
ATOM   742  N  N   . HIS   A 1 91  ? 8.824  13.249  7.251  1.00 19.82  ? 97  HIS   A N   1 
ATOM   743  C  CA  . HIS   A 1 91  ? 9.333  11.877  7.245  1.00 19.98  ? 97  HIS   A CA  1 
ATOM   744  C  C   . HIS   A 1 91  ? 9.070  11.183  8.600  1.00 19.40  ? 97  HIS   A C   1 
ATOM   745  O  O   . HIS   A 1 91  ? 9.882  10.355  9.025  1.00 19.60  ? 97  HIS   A O   1 
ATOM   746  C  CB  . HIS   A 1 91  ? 10.854 11.856  6.865  1.00 21.22  ? 97  HIS   A CB  1 
ATOM   747  C  CG  . HIS   A 1 91  ? 11.139 12.425  5.500  1.00 23.79  ? 97  HIS   A CG  1 
ATOM   748  N  ND1 . HIS   A 1 91  ? 11.227 11.615  4.386  1.00 26.14  ? 97  HIS   A ND1 1 
ATOM   749  C  CD2 . HIS   A 1 91  ? 11.303 13.711  5.113  1.00 25.16  ? 97  HIS   A CD2 1 
ATOM   750  C  CE1 . HIS   A 1 91  ? 11.482 12.424  3.363  1.00 25.63  ? 97  HIS   A CE1 1 
ATOM   751  N  NE2 . HIS   A 1 91  ? 11.549 13.688  3.753  1.00 25.36  ? 97  HIS   A NE2 1 
ATOM   752  N  N   . LEU   A 1 92  ? 7.934  11.493  9.220  1.00 18.05  ? 98  LEU   A N   1 
ATOM   753  C  CA  . LEU   A 1 92  ? 7.555  10.938  10.517 1.00 18.56  ? 98  LEU   A CA  1 
ATOM   754  C  C   . LEU   A 1 92  ? 6.494  9.844   10.359 1.00 18.50  ? 98  LEU   A C   1 
ATOM   755  O  O   . LEU   A 1 92  ? 5.564  10.004  9.573  1.00 19.43  ? 98  LEU   A O   1 
ATOM   756  C  CB  . LEU   A 1 92  ? 6.988  12.096  11.387 1.00 19.64  ? 98  LEU   A CB  1 
ATOM   757  C  CG  . LEU   A 1 92  ? 6.685  11.745  12.854 1.00 22.49  ? 98  LEU   A CG  1 
ATOM   758  C  CD1 . LEU   A 1 92  ? 7.948  11.329  13.578 1.00 22.01  ? 98  LEU   A CD1 1 
ATOM   759  C  CD2 . LEU   A 1 92  ? 6.031  12.964  13.588 1.00 24.90  ? 98  LEU   A CD2 1 
ATOM   760  N  N   . MET   A 1 93  ? 6.630  8.730   11.118 1.00 18.07  ? 99  MET   A N   1 
ATOM   761  C  CA  . MET   A 1 93  ? 5.655  7.632   11.061 1.00 17.33  ? 99  MET   A CA  1 
ATOM   762  C  C   . MET   A 1 93  ? 5.086  7.452   12.464 1.00 18.79  ? 99  MET   A C   1 
ATOM   763  O  O   . MET   A 1 93  ? 5.860  7.413   13.419 1.00 19.83  ? 99  MET   A O   1 
ATOM   764  C  CB  . MET   A 1 93  ? 6.399  6.350   10.662 1.00 18.21  ? 99  MET   A CB  1 
ATOM   765  C  CG  . MET   A 1 93  ? 7.115  6.512   9.323  1.00 19.05  ? 99  MET   A CG  1 
ATOM   766  S  SD  . MET   A 1 93  ? 8.196  5.114   8.816  1.00 22.40  ? 99  MET   A SD  1 
ATOM   767  C  CE  . MET   A 1 93  ? 9.408  5.212   10.016 1.00 20.73  ? 99  MET   A CE  1 
ATOM   768  N  N   . LEU   A 1 94  ? 3.779  7.311   12.583 1.00 17.82  ? 100 LEU   A N   1 
ATOM   769  C  CA  . LEU   A 1 94  ? 3.165  7.151   13.904 1.00 18.28  ? 100 LEU   A CA  1 
ATOM   770  C  C   . LEU   A 1 94  ? 2.701  5.734   14.149 1.00 17.87  ? 100 LEU   A C   1 
ATOM   771  O  O   . LEU   A 1 94  ? 2.261  5.038   13.215 1.00 18.61  ? 100 LEU   A O   1 
ATOM   772  C  CB  . LEU   A 1 94  ? 1.942  8.096   14.086 1.00 20.02  ? 100 LEU   A CB  1 
ATOM   773  C  CG  . LEU   A 1 94  ? 2.180  9.589   14.005 1.00 23.53  ? 100 LEU   A CG  1 
ATOM   774  C  CD1 . LEU   A 1 94  ? 0.898  10.374  14.355 1.00 25.36  ? 100 LEU   A CD1 1 
ATOM   775  C  CD2 . LEU   A 1 94  ? 3.292  10.044  14.951 1.00 24.78  ? 100 LEU   A CD2 1 
ATOM   776  N  N   . ALA   A 1 95  ? 2.702  5.336   15.440 1.00 16.76  ? 101 ALA   A N   1 
ATOM   777  C  CA  . ALA   A 1 95  ? 2.208  4.029   15.846 1.00 16.86  ? 101 ALA   A CA  1 
ATOM   778  C  C   . ALA   A 1 95  ? 1.573  4.171   17.243 1.00 16.97  ? 101 ALA   A C   1 
ATOM   779  O  O   . ALA   A 1 95  ? 1.822  5.154   17.958 1.00 17.55  ? 101 ALA   A O   1 
ATOM   780  C  CB  . ALA   A 1 95  ? 3.383  3.027   15.937 1.00 17.48  ? 101 ALA   A CB  1 
ATOM   781  N  N   . VAL   A 1 96  ? 0.770  3.185   17.630 1.00 15.99  ? 102 VAL   A N   1 
ATOM   782  C  CA  . VAL   A 1 96  ? 0.225  3.109   18.966 1.00 15.93  ? 102 VAL   A CA  1 
ATOM   783  C  C   . VAL   A 1 96  ? 1.263  2.354   19.814 1.00 18.95  ? 102 VAL   A C   1 
ATOM   784  O  O   . VAL   A 1 96  ? 1.611  1.215   19.513 1.00 20.95  ? 102 VAL   A O   1 
ATOM   785  C  CB  . VAL   A 1 96  ? -1.138 2.403   18.981 1.00 16.33  ? 102 VAL   A CB  1 
ATOM   786  C  CG1 . VAL   A 1 96  ? -1.626 2.178   20.428 1.00 17.11  ? 102 VAL   A CG1 1 
ATOM   787  C  CG2 . VAL   A 1 96  ? -2.144 3.235   18.189 1.00 17.57  ? 102 VAL   A CG2 1 
ATOM   788  N  N   . GLY   A 1 97  ? 1.772  3.009   20.817 1.00 19.98  ? 103 GLY   A N   1 
ATOM   789  C  CA  . GLY   A 1 97  ? 2.773  2.421   21.700 1.00 20.49  ? 103 GLY   A CA  1 
ATOM   790  C  C   . GLY   A 1 97  ? 3.197  3.408   22.759 1.00 20.17  ? 103 GLY   A C   1 
ATOM   791  O  O   . GLY   A 1 97  ? 2.954  4.614   22.632 1.00 20.74  ? 103 GLY   A O   1 
ATOM   792  N  N   . HIS   A 1 98  ? 3.822  2.886   23.830 1.00 19.86  ? 104 HIS   A N   1 
ATOM   793  C  CA  . HIS   A 1 98  ? 4.289  3.755   24.891 1.00 19.61  ? 104 HIS   A CA  1 
ATOM   794  C  C   . HIS   A 1 98  ? 5.544  4.515   24.487 1.00 19.29  ? 104 HIS   A C   1 
ATOM   795  O  O   . HIS   A 1 98  ? 6.492  3.923   23.959 1.00 18.96  ? 104 HIS   A O   1 
ATOM   796  C  CB  . HIS   A 1 98  ? 4.602  2.942   26.186 1.00 18.97  ? 104 HIS   A CB  1 
ATOM   797  C  CG  . HIS   A 1 98  ? 5.001  3.833   27.329 1.00 19.36  ? 104 HIS   A CG  1 
ATOM   798  N  ND1 . HIS   A 1 98  ? 4.097  4.721   27.898 1.00 21.52  ? 104 HIS   A ND1 1 
ATOM   799  C  CD2 . HIS   A 1 98  ? 6.199  3.980   27.962 1.00 21.08  ? 104 HIS   A CD2 1 
ATOM   800  C  CE1 . HIS   A 1 98  ? 4.778  5.398   28.828 1.00 21.87  ? 104 HIS   A CE1 1 
ATOM   801  N  NE2 . HIS   A 1 98  ? 6.046  4.987   28.909 1.00 21.39  ? 104 HIS   A NE2 1 
ATOM   802  N  N   . SER   A 1 99  ? 5.595  5.772   24.875 1.00 19.36  ? 105 SER   A N   1 
ATOM   803  C  CA  . SER   A 1 99  ? 6.799  6.563   24.744 1.00 19.95  ? 105 SER   A CA  1 
ATOM   804  C  C   . SER   A 1 99  ? 6.724  7.702   25.758 1.00 22.26  ? 105 SER   A C   1 
ATOM   805  O  O   . SER   A 1 99  ? 5.633  8.219   26.042 1.00 23.40  ? 105 SER   A O   1 
ATOM   806  C  CB  . SER   A 1 99  ? 7.007  7.078   23.311 1.00 22.49  ? 105 SER   A CB  1 
ATOM   807  O  OG  . SER   A 1 99  ? 8.179  7.874   23.198 1.00 24.52  ? 105 SER   A OG  1 
ATOM   808  N  N   . GLU   A 1 100 ? 7.873  8.023   26.345 1.00 22.10  ? 106 GLU   A N   1 
ATOM   809  C  CA  . GLU   A 1 100 ? 8.086  9.157   27.243 1.00 24.79  ? 106 GLU   A CA  1 
ATOM   810  C  C   . GLU   A 1 100 ? 9.301  9.951   26.782 1.00 26.27  ? 106 GLU   A C   1 
ATOM   811  O  O   . GLU   A 1 100 ? 10.152 9.449   26.035 1.00 26.63  ? 106 GLU   A O   1 
ATOM   812  C  CB  . GLU   A 1 100 ? 8.437  8.637   28.664 1.00 28.15  ? 106 GLU   A CB  1 
ATOM   813  C  CG  . GLU   A 1 100 ? 7.283  8.139   29.433 1.00 31.52  ? 106 GLU   A CG  1 
ATOM   814  C  CD  . GLU   A 1 100 ? 7.779  7.342   30.625 1.00 28.78  ? 106 GLU   A CD  1 
ATOM   815  O  OE1 . GLU   A 1 100 ? 8.695  7.810   31.345 1.00 29.67  ? 106 GLU   A OE1 1 
ATOM   816  O  OE2 . GLU   A 1 100 ? 7.231  6.248   30.845 1.00 26.65  ? 106 GLU   A OE2 1 
ATOM   817  N  N   . PRO   A 1 101 ? 9.416  11.217  27.247 1.00 28.57  ? 107 PRO   A N   1 
ATOM   818  C  CA  . PRO   A 1 101 ? 10.639 11.954  27.010 1.00 29.77  ? 107 PRO   A CA  1 
ATOM   819  C  C   . PRO   A 1 101 ? 11.747 11.168  27.746 1.00 29.21  ? 107 PRO   A C   1 
ATOM   820  O  O   . PRO   A 1 101 ? 11.590 10.697  28.922 1.00 29.79  ? 107 PRO   A O   1 
ATOM   821  C  CB  . PRO   A 1 101 ? 10.344 13.362  27.587 1.00 30.80  ? 107 PRO   A CB  1 
ATOM   822  C  CG  . PRO   A 1 101 ? 8.840  13.411  27.751 1.00 30.70  ? 107 PRO   A CG  1 
ATOM   823  C  CD  . PRO   A 1 101 ? 8.479  11.978  28.089 1.00 28.85  ? 107 PRO   A CD  1 
ATOM   824  N  N   . GLY   A 1 102 ? 12.741 10.859  26.934 1.00 24.43  ? 108 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 102 ? 13.890 10.019  27.253 1.00 23.29  ? 108 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 102 ? 13.967 8.817   26.322 1.00 21.39  ? 108 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 102 ? 15.031 8.220   26.181 1.00 22.10  ? 108 GLY   A O   1 
ATOM   828  N  N   . ASP   A 1 103 ? 12.823 8.420   25.691 1.00 18.87  ? 109 ASP   A N   1 
ATOM   829  C  CA  . ASP   A 1 103 ? 12.778 7.274   24.789 1.00 18.38  ? 109 ASP   A CA  1 
ATOM   830  C  C   . ASP   A 1 103 ? 13.285 7.578   23.384 1.00 18.13  ? 109 ASP   A C   1 
ATOM   831  O  O   . ASP   A 1 103 ? 13.502 6.650   22.603 1.00 17.74  ? 109 ASP   A O   1 
ATOM   832  C  CB  . ASP   A 1 103 ? 11.347 6.730   24.687 1.00 17.67  ? 109 ASP   A CB  1 
ATOM   833  C  CG  . ASP   A 1 103 ? 10.991 5.908   25.914 1.00 18.62  ? 109 ASP   A CG  1 
ATOM   834  O  OD1 . ASP   A 1 103 ? 11.903 5.236   26.454 1.00 18.39  ? 109 ASP   A OD1 1 
ATOM   835  O  OD2 . ASP   A 1 103 ? 9.792  5.900   26.306 1.00 20.06  ? 109 ASP   A OD2 1 
ATOM   836  N  N   . CYS   A 1 104 ? 13.530 8.867   23.060 1.00 17.63  ? 110 CYS   A N   1 
ATOM   837  C  CA  . CYS   A 1 104 ? 14.055 9.210   21.726 1.00 17.72  ? 110 CYS   A CA  1 
ATOM   838  C  C   . CYS   A 1 104 ? 15.357 8.470   21.454 1.00 17.07  ? 110 CYS   A C   1 
ATOM   839  O  O   . CYS   A 1 104 ? 16.179 8.331   22.365 1.00 16.86  ? 110 CYS   A O   1 
ATOM   840  C  CB  . CYS   A 1 104 ? 14.262 10.714  21.622 1.00 19.20  ? 110 CYS   A CB  1 
ATOM   841  S  SG  . CYS   A 1 104 ? 12.723 11.650  21.506 1.00 20.71  ? 110 CYS   A SG  1 
ATOM   842  N  N   . GLY   A 1 105 ? 15.532 7.991   20.224 1.00 16.75  ? 111 GLY   A N   1 
ATOM   843  C  CA  . GLY   A 1 105 ? 16.747 7.271   19.869 1.00 15.75  ? 111 GLY   A CA  1 
ATOM   844  C  C   . GLY   A 1 105 ? 16.569 5.764   19.826 1.00 16.26  ? 111 GLY   A C   1 
ATOM   845  O  O   . GLY   A 1 105 ? 17.418 5.050   19.280 1.00 16.47  ? 111 GLY   A O   1 
ATOM   846  N  N   . GLY   A 1 106 ? 15.463 5.261   20.392 1.00 16.02  ? 112 GLY   A N   1 
ATOM   847  C  CA  . GLY   A 1 106 ? 15.212 3.827   20.347 1.00 16.18  ? 112 GLY   A CA  1 
ATOM   848  C  C   . GLY   A 1 106 ? 15.024 3.380   18.901 1.00 16.11  ? 112 GLY   A C   1 
ATOM   849  O  O   . GLY   A 1 106 ? 14.349 4.065   18.122 1.00 15.64  ? 112 GLY   A O   1 
ATOM   850  N  N   . ILE   A 1 107 ? 15.591 2.204   18.518 1.00 14.85  ? 113 ILE   A N   1 
ATOM   851  C  CA  . ILE   A 1 107 ? 15.457 1.773   17.128 1.00 14.63  ? 113 ILE   A CA  1 
ATOM   852  C  C   . ILE   A 1 107 ? 14.138 1.089   16.813 1.00 14.57  ? 113 ILE   A C   1 
ATOM   853  O  O   . ILE   A 1 107 ? 13.694 0.235   17.594 1.00 14.94  ? 113 ILE   A O   1 
ATOM   854  C  CB  . ILE   A 1 107 ? 16.649 0.826   16.777 1.00 15.01  ? 113 ILE   A CB  1 
ATOM   855  C  CG1 . ILE   A 1 107 ? 17.878 1.696   16.513 1.00 16.49  ? 113 ILE   A CG1 1 
ATOM   856  C  CG2 . ILE   A 1 107 ? 16.368 -0.098  15.532 1.00 15.85  ? 113 ILE   A CG2 1 
ATOM   857  C  CD1 . ILE   A 1 107 ? 19.145 0.861   16.330 1.00 18.96  ? 113 ILE   A CD1 1 
ATOM   858  N  N   . LEU   A 1 108 ? 13.570 1.405   15.635 1.00 14.14  ? 114 LEU   A N   1 
ATOM   859  C  CA  . LEU   A 1 108 ? 12.452 0.679   15.035 1.00 14.28  ? 114 LEU   A CA  1 
ATOM   860  C  C   . LEU   A 1 108 ? 13.086 -0.181  13.894 1.00 15.59  ? 114 LEU   A C   1 
ATOM   861  O  O   . LEU   A 1 108 ? 13.842 0.369   13.080 1.00 16.27  ? 114 LEU   A O   1 
ATOM   862  C  CB  . LEU   A 1 108 ? 11.476 1.671   14.365 1.00 14.63  ? 114 LEU   A CB  1 
ATOM   863  C  CG  . LEU   A 1 108 ? 10.370 1.049   13.486 1.00 16.53  ? 114 LEU   A CG  1 
ATOM   864  C  CD1 . LEU   A 1 108 ? 9.403  0.245   14.353 1.00 16.71  ? 114 LEU   A CD1 1 
ATOM   865  C  CD2 . LEU   A 1 108 ? 9.573  2.150   12.751 1.00 17.22  ? 114 LEU   A CD2 1 
ATOM   866  N  N   . ARG   A 1 109 ? 12.785 -1.488  13.854 1.00 15.10  ? 115 ARG   A N   1 
ATOM   867  C  CA  . ARG   A 1 109 ? 13.375 -2.349  12.825 1.00 15.34  ? 115 ARG   A CA  1 
ATOM   868  C  C   . ARG   A 1 109 ? 12.307 -3.270  12.242 1.00 17.64  ? 115 ARG   A C   1 
ATOM   869  O  O   . ARG   A 1 109 ? 11.319 -3.607  12.906 1.00 18.47  ? 115 ARG   A O   1 
ATOM   870  C  CB  . ARG   A 1 109 ? 14.523 -3.167  13.430 1.00 15.78  ? 115 ARG   A CB  1 
ATOM   871  C  CG  . ARG   A 1 109 ? 14.096 -4.139  14.511 1.00 17.93  ? 115 ARG   A CG  1 
ATOM   872  C  CD  . ARG   A 1 109 ? 15.353 -4.837  15.040 1.00 19.56  ? 115 ARG   A CD  1 
ATOM   873  N  NE  . ARG   A 1 109 ? 16.116 -3.944  15.904 1.00 21.07  ? 115 ARG   A NE  1 
ATOM   874  C  CZ  . ARG   A 1 109 ? 17.423 -3.736  15.818 1.00 21.25  ? 115 ARG   A CZ  1 
ATOM   875  N  NH1 . ARG   A 1 109 ? 18.120 -4.236  14.796 1.00 20.16  ? 115 ARG   A NH1 1 
ATOM   876  N  NH2 . ARG   A 1 109 ? 18.043 -2.980  16.722 1.00 20.79  ? 115 ARG   A NH2 1 
ATOM   877  N  N   . CYS   A 1 110 ? 12.565 -3.739  11.035 1.00 18.56  ? 116 CYS   A N   1 
ATOM   878  C  CA  . CYS   A 1 110 ? 11.698 -4.709  10.382 1.00 20.03  ? 116 CYS   A CA  1 
ATOM   879  C  C   . CYS   A 1 110 ? 12.594 -5.908  9.940  1.00 22.35  ? 116 CYS   A C   1 
ATOM   880  O  O   . CYS   A 1 110 ? 13.781 -5.976  10.306 1.00 21.28  ? 116 CYS   A O   1 
ATOM   881  C  CB  . CYS   A 1 110 ? 11.015 -4.045  9.197  1.00 22.10  ? 116 CYS   A CB  1 
ATOM   882  S  SG  . CYS   A 1 110 ? 12.182 -3.617  7.859  1.00 22.04  ? 116 CYS   A SG  1 
ATOM   883  N  N   . GLN   A 1 111 ? 12.030 -6.866  9.135  1.00 24.51  ? 117 GLN   A N   1 
ATOM   884  C  CA  . GLN   A 1 111 ? 12.812 -7.994  8.671  1.00 27.51  ? 117 GLN   A CA  1 
ATOM   885  C  C   . GLN   A 1 111 ? 14.033 -7.568  7.805  1.00 28.66  ? 117 GLN   A C   1 
ATOM   886  O  O   . GLN   A 1 111 ? 14.998 -8.322  7.686  1.00 30.98  ? 117 GLN   A O   1 
ATOM   887  C  CB  . GLN   A 1 111 ? 11.919 -8.971  7.858  1.00 31.82  ? 117 GLN   A CB  1 
ATOM   888  C  CG  . GLN   A 1 111 ? 11.237 -8.303  6.664  1.00 37.40  ? 117 GLN   A CG  1 
ATOM   889  C  CD  . GLN   A 1 111 ? 10.311 -9.196  5.865  1.00 44.89  ? 117 GLN   A CD  1 
ATOM   890  O  OE1 . GLN   A 1 111 ? 9.105  -8.923  5.745  1.00 46.80  ? 117 GLN   A OE1 1 
ATOM   891  N  NE2 . GLN   A 1 111 ? 10.849 -10.252 5.258  1.00 44.74  ? 117 GLN   A NE2 1 
ATOM   892  N  N   . HIS   A 1 112 ? 13.993 -6.368  7.225  1.00 26.19  ? 118 HIS   A N   1 
ATOM   893  C  CA  . HIS   A 1 112 ? 15.068 -5.908  6.323  1.00 25.37  ? 118 HIS   A CA  1 
ATOM   894  C  C   . HIS   A 1 112 ? 16.200 -5.132  7.028  1.00 24.31  ? 118 HIS   A C   1 
ATOM   895  O  O   . HIS   A 1 112 ? 17.247 -4.884  6.418  1.00 25.83  ? 118 HIS   A O   1 
ATOM   896  C  CB  . HIS   A 1 112 ? 14.461 -5.037  5.200  1.00 25.80  ? 118 HIS   A CB  1 
ATOM   897  C  CG  . HIS   A 1 112 ? 13.368 -5.738  4.445  1.00 30.29  ? 118 HIS   A CG  1 
ATOM   898  N  ND1 . HIS   A 1 112 ? 12.029 -5.420  4.626  1.00 32.28  ? 118 HIS   A ND1 1 
ATOM   899  C  CD2 . HIS   A 1 112 ? 13.460 -6.744  3.539  1.00 32.87  ? 118 HIS   A CD2 1 
ATOM   900  C  CE1 . HIS   A 1 112 ? 11.348 -6.228  3.827  1.00 34.25  ? 118 HIS   A CE1 1 
ATOM   901  N  NE2 . HIS   A 1 112 ? 12.168 -7.054  3.156  1.00 34.51  ? 118 HIS   A NE2 1 
ATOM   902  N  N   . GLY   A 1 113 ? 15.966 -4.701  8.274  1.00 22.31  ? 119 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 113 ? 16.982 -3.927  8.981  1.00 20.61  ? 119 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 113 ? 16.352 -2.756  9.727  1.00 17.92  ? 119 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 113 ? 15.149 -2.767  10.030 1.00 18.35  ? 119 GLY   A O   1 
ATOM   906  N  N   . VAL   A 1 114 ? 17.191 -1.720  10.025 1.00 16.06  ? 120 VAL   A N   1 
ATOM   907  C  CA  . VAL   A 1 114 ? 16.748 -0.540  10.757 1.00 16.86  ? 120 VAL   A CA  1 
ATOM   908  C  C   . VAL   A 1 114 ? 15.876 0.361   9.879  1.00 16.59  ? 120 VAL   A C   1 
ATOM   909  O  O   . VAL   A 1 114 ? 16.301 0.763   8.798  1.00 16.29  ? 120 VAL   A O   1 
ATOM   910  C  CB  . VAL   A 1 114 ? 17.949 0.235   11.353 1.00 17.86  ? 120 VAL   A CB  1 
ATOM   911  C  CG1 . VAL   A 1 114 ? 17.512 1.539   12.004 1.00 17.58  ? 120 VAL   A CG1 1 
ATOM   912  C  CG2 . VAL   A 1 114 ? 18.709 -0.647  12.342 1.00 19.00  ? 120 VAL   A CG2 1 
ATOM   913  N  N   . VAL   A 1 115 ? 14.701 0.735   10.395 1.00 16.24  ? 121 VAL   A N   1 
ATOM   914  C  CA  . VAL   A 1 115 ? 13.743 1.576   9.686  1.00 16.21  ? 121 VAL   A CA  1 
ATOM   915  C  C   . VAL   A 1 115 ? 13.888 3.029   10.125 1.00 17.08  ? 121 VAL   A C   1 
ATOM   916  O  O   . VAL   A 1 115 ? 13.757 3.938   9.315  1.00 18.63  ? 121 VAL   A O   1 
ATOM   917  C  CB  . VAL   A 1 115 ? 12.298 1.065   9.982  1.00 17.56  ? 121 VAL   A CB  1 
ATOM   918  C  CG1 . VAL   A 1 115 ? 11.226 1.996   9.415  1.00 17.63  ? 121 VAL   A CG1 1 
ATOM   919  C  CG2 . VAL   A 1 115 ? 12.119 -0.335  9.437  1.00 18.29  ? 121 VAL   A CG2 1 
ATOM   920  N  N   . GLY   A 1 116 ? 14.099 3.260   11.431 1.00 15.76  ? 122 GLY   A N   1 
ATOM   921  C  CA  . GLY   A 1 116 ? 14.167 4.626   11.944 1.00 16.16  ? 122 GLY   A CA  1 
ATOM   922  C  C   . GLY   A 1 116 ? 14.358 4.649   13.448 1.00 16.98  ? 122 GLY   A C   1 
ATOM   923  O  O   . GLY   A 1 116 ? 14.702 3.620   14.034 1.00 17.02  ? 122 GLY   A O   1 
ATOM   924  N  N   . ILE   A 1 117 ? 14.236 5.844   14.073 1.00 15.91  ? 123 ILE   A N   1 
ATOM   925  C  CA  . ILE   A 1 117 ? 14.433 5.983   15.510 1.00 15.39  ? 123 ILE   A CA  1 
ATOM   926  C  C   . ILE   A 1 117 ? 13.274 6.732   16.144 1.00 15.11  ? 123 ILE   A C   1 
ATOM   927  O  O   . ILE   A 1 117 ? 12.699 7.621   15.510 1.00 15.28  ? 123 ILE   A O   1 
ATOM   928  C  CB  . ILE   A 1 117 ? 15.755 6.693   15.865 1.00 16.62  ? 123 ILE   A CB  1 
ATOM   929  C  CG1 . ILE   A 1 117 ? 15.924 8.022   15.105 1.00 16.54  ? 123 ILE   A CG1 1 
ATOM   930  C  CG2 . ILE   A 1 117 ? 16.940 5.746   15.675 1.00 16.64  ? 123 ILE   A CG2 1 
ATOM   931  C  CD1 . ILE   A 1 117 ? 17.229 8.780   15.569 1.00 17.46  ? 123 ILE   A CD1 1 
ATOM   932  N  N   . VAL   A 1 118 ? 12.973 6.454   17.423 1.00 15.05  ? 124 VAL   A N   1 
ATOM   933  C  CA  . VAL   A 1 118 ? 11.930 7.214   18.148 1.00 15.23  ? 124 VAL   A CA  1 
ATOM   934  C  C   . VAL   A 1 118 ? 12.270 8.706   18.130 1.00 15.64  ? 124 VAL   A C   1 
ATOM   935  O  O   . VAL   A 1 118 ? 13.423 9.051   18.405 1.00 15.96  ? 124 VAL   A O   1 
ATOM   936  C  CB  . VAL   A 1 118 ? 11.799 6.709   19.595 1.00 16.36  ? 124 VAL   A CB  1 
ATOM   937  C  CG1 . VAL   A 1 118 ? 10.821 7.584   20.416 1.00 17.79  ? 124 VAL   A CG1 1 
ATOM   938  C  CG2 . VAL   A 1 118 ? 11.345 5.248   19.602 1.00 16.77  ? 124 VAL   A CG2 1 
ATOM   939  N  N   . SER   A 1 119 ? 11.289 9.558   17.786 1.00 15.82  ? 125 SER   A N   1 
ATOM   940  C  CA  . SER   A 1 119 ? 11.505 11.013  17.742 1.00 17.66  ? 125 SER   A CA  1 
ATOM   941  C  C   . SER   A 1 119 ? 10.398 11.777  18.477 1.00 19.28  ? 125 SER   A C   1 
ATOM   942  O  O   . SER   A 1 119 ? 10.655 12.832  19.047 1.00 19.65  ? 125 SER   A O   1 
ATOM   943  C  CB  . SER   A 1 119 ? 11.592 11.493  16.297 1.00 18.73  ? 125 SER   A CB  1 
ATOM   944  O  OG  . SER   A 1 119 ? 11.726 12.910  16.202 1.00 20.25  ? 125 SER   A OG  1 
ATOM   945  N  N   . THR   A 1 120 ? 9.147  11.236  18.488 1.00 18.55  ? 126 THR   A N   1 
ATOM   946  C  CA  . THR   A 1 120 ? 8.030  11.968  19.135 1.00 19.05  ? 126 THR   A CA  1 
ATOM   947  C  C   . THR   A 1 120 ? 7.167  10.986  19.972 1.00 20.25  ? 126 THR   A C   1 
ATOM   948  O  O   . THR   A 1 120 ? 7.313  9.760   19.819 1.00 19.97  ? 126 THR   A O   1 
ATOM   949  C  CB  . THR   A 1 120 ? 7.120  12.665  18.066 1.00 20.43  ? 126 THR   A CB  1 
ATOM   950  O  OG1 . THR   A 1 120 ? 6.328  11.714  17.354 1.00 20.51  ? 126 THR   A OG1 1 
ATOM   951  C  CG2 . THR   A 1 120 ? 7.868  13.575  17.098 1.00 20.34  ? 126 THR   A CG2 1 
ATOM   952  N  N   . GLY   A 1 121 ? 6.278  11.505  20.815 1.00 20.74  ? 127 GLY   A N   1 
ATOM   953  C  CA  . GLY   A 1 121 ? 5.376  10.602  21.547 1.00 22.15  ? 127 GLY   A CA  1 
ATOM   954  C  C   . GLY   A 1 121 ? 4.309  11.324  22.322 1.00 24.18  ? 127 GLY   A C   1 
ATOM   955  O  O   . GLY   A 1 121 ? 4.232  12.546  22.288 1.00 24.75  ? 127 GLY   A O   1 
ATOM   956  N  N   . GLY   A 1 122 ? 3.534  10.561  23.071 1.00 25.25  ? 128 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 122 ? 2.531  11.147  23.952 1.00 26.37  ? 128 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 122 ? 1.224  10.404  23.899 1.00 27.32  ? 128 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 122 ? 0.773  10.035  22.821 1.00 27.68  ? 128 GLY   A O   1 
ATOM   960  N  N   . ASN   A 1 123 ? 0.601  10.218  25.066 1.00 26.84  ? 129 ASN   A N   1 
ATOM   961  C  CA  . ASN   A 1 123 ? -0.703 9.599   25.265 1.00 26.50  ? 129 ASN   A CA  1 
ATOM   962  C  C   . ASN   A 1 123 ? -0.939 8.325   24.488 1.00 24.44  ? 129 ASN   A C   1 
ATOM   963  O  O   . ASN   A 1 123 ? -2.031 8.130   23.926 1.00 25.22  ? 129 ASN   A O   1 
ATOM   964  C  CB  . ASN   A 1 123 ? -1.798 10.625  24.974 1.00 30.11  ? 129 ASN   A CB  1 
ATOM   965  C  CG  . ASN   A 1 123 ? -1.716 11.773  25.910 1.00 36.85  ? 129 ASN   A CG  1 
ATOM   966  O  OD1 . ASN   A 1 123 ? -1.737 11.583  27.130 1.00 39.77  ? 129 ASN   A OD1 1 
ATOM   967  N  ND2 . ASN   A 1 123 ? -1.550 12.969  25.363 1.00 38.22  ? 129 ASN   A ND2 1 
ATOM   968  N  N   . GLY   A 1 124 ? 0.029  7.410   24.545 1.00 21.16  ? 130 GLY   A N   1 
ATOM   969  C  CA  . GLY   A 1 124 ? -0.141 6.128   23.887 1.00 20.02  ? 130 GLY   A CA  1 
ATOM   970  C  C   . GLY   A 1 124 ? 0.218  6.108   22.426 1.00 19.23  ? 130 GLY   A C   1 
ATOM   971  O  O   . GLY   A 1 124 ? 0.014  5.080   21.779 1.00 20.28  ? 130 GLY   A O   1 
ATOM   972  N  N   . LEU   A 1 125 ? 0.808  7.187   21.920 1.00 18.25  ? 131 LEU   A N   1 
ATOM   973  C  CA  . LEU   A 1 125 ? 1.340  7.217   20.552 1.00 19.09  ? 131 LEU   A CA  1 
ATOM   974  C  C   . LEU   A 1 125 ? 2.877  7.296   20.621 1.00 19.19  ? 131 LEU   A C   1 
ATOM   975  O  O   . LEU   A 1 125 ? 3.440  7.826   21.604 1.00 19.95  ? 131 LEU   A O   1 
ATOM   976  C  CB  . LEU   A 1 125 ? 0.860  8.487   19.844 1.00 20.94  ? 131 LEU   A CB  1 
ATOM   977  C  CG  . LEU   A 1 125 ? -0.614 8.495   19.464 1.00 22.58  ? 131 LEU   A CG  1 
ATOM   978  C  CD1 . LEU   A 1 125 ? -1.031 9.877   19.004 1.00 24.91  ? 131 LEU   A CD1 1 
ATOM   979  C  CD2 . LEU   A 1 125 ? -0.945 7.406   18.430 1.00 22.82  ? 131 LEU   A CD2 1 
ATOM   980  N  N   . VAL   A 1 126 ? 3.542  6.818   19.553 1.00 16.59  ? 132 VAL   A N   1 
ATOM   981  C  CA  . VAL   A 1 126 ? 4.995  6.948   19.439 1.00 16.89  ? 132 VAL   A CA  1 
ATOM   982  C  C   . VAL   A 1 126 ? 5.268  7.318   17.933 1.00 16.88  ? 132 VAL   A C   1 
ATOM   983  O  O   . VAL   A 1 126 ? 4.596  6.777   17.064 1.00 17.52  ? 132 VAL   A O   1 
ATOM   984  C  CB  . VAL   A 1 126 ? 5.711  5.650   19.885 1.00 17.27  ? 132 VAL   A CB  1 
ATOM   985  C  CG1 . VAL   A 1 126 ? 5.156  4.439   19.149 1.00 18.03  ? 132 VAL   A CG1 1 
ATOM   986  C  CG2 . VAL   A 1 126 ? 7.227  5.768   19.671 1.00 19.05  ? 132 VAL   A CG2 1 
ATOM   987  N  N   . GLY   A 1 127 ? 6.182  8.249   17.672 1.00 17.24  ? 133 GLY   A N   1 
ATOM   988  C  CA  . GLY   A 1 127 ? 6.521  8.662   16.318 1.00 17.60  ? 133 GLY   A CA  1 
ATOM   989  C  C   . GLY   A 1 127 ? 7.968  8.351   16.010 1.00 17.84  ? 133 GLY   A C   1 
ATOM   990  O  O   . GLY   A 1 127 ? 8.834  8.519   16.868 1.00 18.18  ? 133 GLY   A O   1 
ATOM   991  N  N   . PHE   A 1 128 ? 8.231  7.831   14.790 1.00 17.22  ? 134 PHE   A N   1 
ATOM   992  C  CA  . PHE   A 1 128 ? 9.597  7.459   14.396 1.00 16.72  ? 134 PHE   A CA  1 
ATOM   993  C  C   . PHE   A 1 128 ? 10.070 8.284   13.219 1.00 17.16  ? 134 PHE   A C   1 
ATOM   994  O  O   . PHE   A 1 128 ? 9.335  8.459   12.250 1.00 18.10  ? 134 PHE   A O   1 
ATOM   995  C  CB  . PHE   A 1 128 ? 9.589  5.982   13.977 1.00 16.72  ? 134 PHE   A CB  1 
ATOM   996  C  CG  . PHE   A 1 128 ? 8.970  5.044   15.005 1.00 16.27  ? 134 PHE   A CG  1 
ATOM   997  C  CD1 . PHE   A 1 128 ? 9.720  4.567   16.079 1.00 17.16  ? 134 PHE   A CD1 1 
ATOM   998  C  CD2 . PHE   A 1 128 ? 7.660  4.621   14.875 1.00 17.25  ? 134 PHE   A CD2 1 
ATOM   999  C  CE1 . PHE   A 1 128 ? 9.148  3.705   17.022 1.00 17.66  ? 134 PHE   A CE1 1 
ATOM   1000 C  CE2 . PHE   A 1 128 ? 7.105  3.751   15.799 1.00 18.33  ? 134 PHE   A CE2 1 
ATOM   1001 C  CZ  . PHE   A 1 128 ? 7.848  3.314   16.876 1.00 17.57  ? 134 PHE   A CZ  1 
ATOM   1002 N  N   . ALA   A 1 129 ? 11.305 8.762   13.290 1.00 16.25  ? 135 ALA   A N   1 
ATOM   1003 C  CA  . ALA   A 1 129 ? 11.931 9.458   12.151 1.00 17.13  ? 135 ALA   A CA  1 
ATOM   1004 C  C   . ALA   A 1 129 ? 12.447 8.376   11.206 1.00 17.68  ? 135 ALA   A C   1 
ATOM   1005 O  O   . ALA   A 1 129 ? 13.303 7.576   11.591 1.00 16.54  ? 135 ALA   A O   1 
ATOM   1006 C  CB  . ALA   A 1 129 ? 13.094 10.313  12.647 1.00 16.52  ? 135 ALA   A CB  1 
ATOM   1007 N  N   . ASP   A 1 130 ? 11.904 8.320   9.974  1.00 18.10  ? 136 ASP   A N   1 
ATOM   1008 C  CA  . ASP   A 1 130 ? 12.310 7.332   8.990  1.00 18.74  ? 136 ASP   A CA  1 
ATOM   1009 C  C   . ASP   A 1 130 ? 13.731 7.648   8.483  1.00 18.64  ? 136 ASP   A C   1 
ATOM   1010 O  O   . ASP   A 1 130 ? 14.099 8.823   8.350  1.00 19.05  ? 136 ASP   A O   1 
ATOM   1011 C  CB  . ASP   A 1 130 ? 11.348 7.420   7.782  1.00 20.26  ? 136 ASP   A CB  1 
ATOM   1012 C  CG  . ASP   A 1 130 ? 11.602 6.396   6.694  1.00 28.10  ? 136 ASP   A CG  1 
ATOM   1013 O  OD1 . ASP   A 1 130 ? 11.773 5.200   7.031  1.00 23.75  ? 136 ASP   A OD1 1 
ATOM   1014 O  OD2 . ASP   A 1 130 ? 11.694 6.798   5.506  1.00 35.37  ? 136 ASP   A OD2 1 
ATOM   1015 N  N   . VAL   A 1 131 ? 14.518 6.599   8.192  1.00 17.87  ? 137 VAL   A N   1 
ATOM   1016 C  CA  . VAL   A 1 131 ? 15.852 6.773   7.559  1.00 16.68  ? 137 VAL   A CA  1 
ATOM   1017 C  C   . VAL   A 1 131 ? 15.987 5.936   6.267  1.00 17.93  ? 137 VAL   A C   1 
ATOM   1018 O  O   . VAL   A 1 131 ? 17.049 5.985   5.646  1.00 17.42  ? 137 VAL   A O   1 
ATOM   1019 C  CB  . VAL   A 1 131 ? 17.026 6.427   8.515  1.00 16.38  ? 137 VAL   A CB  1 
ATOM   1020 C  CG1 . VAL   A 1 131 ? 17.022 7.341   9.750  1.00 17.61  ? 137 VAL   A CG1 1 
ATOM   1021 C  CG2 . VAL   A 1 131 ? 17.022 4.926   8.906  1.00 16.52  ? 137 VAL   A CG2 1 
ATOM   1022 N  N   . ARG   A 1 132 ? 14.919 5.210   5.842  1.00 17.73  ? 138 ARG   A N   1 
ATOM   1023 C  CA  . ARG   A 1 132 ? 15.005 4.316   4.685  1.00 17.14  ? 138 ARG   A CA  1 
ATOM   1024 C  C   . ARG   A 1 132 ? 15.291 5.011   3.359  1.00 19.55  ? 138 ARG   A C   1 
ATOM   1025 O  O   . ARG   A 1 132 ? 15.750 4.347   2.405  1.00 20.38  ? 138 ARG   A O   1 
ATOM   1026 C  CB  . ARG   A 1 132 ? 13.750 3.454   4.578  1.00 17.60  ? 138 ARG   A CB  1 
ATOM   1027 C  CG  . ARG   A 1 132 ? 13.603 2.463   5.736  1.00 18.44  ? 138 ARG   A CG  1 
ATOM   1028 C  CD  . ARG   A 1 132 ? 12.274 1.729   5.612  1.00 19.83  ? 138 ARG   A CD  1 
ATOM   1029 N  NE  . ARG   A 1 132 ? 11.141 2.635   5.876  1.00 21.89  ? 138 ARG   A NE  1 
ATOM   1030 C  CZ  . ARG   A 1 132 ? 9.870  2.237   5.952  1.00 23.10  ? 138 ARG   A CZ  1 
ATOM   1031 N  NH1 . ARG   A 1 132 ? 9.551  0.963   5.725  1.00 22.96  ? 138 ARG   A NH1 1 
ATOM   1032 N  NH2 . ARG   A 1 132 ? 8.908  3.115   6.225  1.00 22.79  ? 138 ARG   A NH2 1 
ATOM   1033 N  N   . ASP   A 1 133 ? 14.955 6.306   3.254  1.00 19.26  ? 139 ASP   A N   1 
ATOM   1034 C  CA  . ASP   A 1 133 ? 15.222 7.036   2.019  1.00 20.47  ? 139 ASP   A CA  1 
ATOM   1035 C  C   . ASP   A 1 133 ? 16.669 7.585   1.928  1.00 20.29  ? 139 ASP   A C   1 
ATOM   1036 O  O   . ASP   A 1 133 ? 17.054 8.113   0.868  1.00 20.91  ? 139 ASP   A O   1 
ATOM   1037 C  CB  . ASP   A 1 133 ? 14.226 8.198   1.875  1.00 22.83  ? 139 ASP   A CB  1 
ATOM   1038 C  CG  . ASP   A 1 133 ? 14.439 9.242   2.964  1.00 27.99  ? 139 ASP   A CG  1 
ATOM   1039 O  OD1 . ASP   A 1 133 ? 14.580 8.851   4.149  1.00 26.95  ? 139 ASP   A OD1 1 
ATOM   1040 O  OD2 . ASP   A 1 133 ? 14.501 10.443  2.631  1.00 29.24  ? 139 ASP   A OD2 1 
ATOM   1041 N  N   . LEU   A 1 134 ? 17.457 7.511   3.019  1.00 19.56  ? 140 LEU   A N   1 
ATOM   1042 C  CA  . LEU   A 1 134 ? 18.829 8.071   3.057  1.00 19.94  ? 140 LEU   A CA  1 
ATOM   1043 C  C   . LEU   A 1 134 ? 19.785 7.029   2.504  1.00 20.59  ? 140 LEU   A C   1 
ATOM   1044 O  O   . LEU   A 1 134 ? 20.485 6.346   3.254  1.00 20.48  ? 140 LEU   A O   1 
ATOM   1045 C  CB  . LEU   A 1 134 ? 19.181 8.457   4.512  1.00 19.90  ? 140 LEU   A CB  1 
ATOM   1046 C  CG  . LEU   A 1 134 ? 18.205 9.459   5.136  1.00 20.39  ? 140 LEU   A CG  1 
ATOM   1047 C  CD1 . LEU   A 1 134 ? 18.571 9.703   6.593  1.00 21.22  ? 140 LEU   A CD1 1 
ATOM   1048 C  CD2 . LEU   A 1 134 ? 18.216 10.794  4.374  1.00 21.49  ? 140 LEU   A CD2 1 
ATOM   1049 N  N   . LEU   A 1 135 ? 19.788 6.890   1.173  1.00 19.98  ? 141 LEU   A N   1 
ATOM   1050 C  CA  . LEU   A 1 135 ? 20.544 5.806   0.536  1.00 21.10  ? 141 LEU   A CA  1 
ATOM   1051 C  C   . LEU   A 1 135 ? 22.041 5.921   0.763  1.00 20.77  ? 141 LEU   A C   1 
ATOM   1052 O  O   . LEU   A 1 135 ? 22.747 4.902   0.802  1.00 21.74  ? 141 LEU   A O   1 
ATOM   1053 C  CB  . LEU   A 1 135 ? 20.218 5.677   -0.969 1.00 21.86  ? 141 LEU   A CB  1 
ATOM   1054 C  CG  . LEU   A 1 135 ? 18.720 5.664   -1.313 1.00 23.69  ? 141 LEU   A CG  1 
ATOM   1055 C  CD1 . LEU   A 1 135 ? 18.521 5.406   -2.825 1.00 24.83  ? 141 LEU   A CD1 1 
ATOM   1056 C  CD2 . LEU   A 1 135 ? 17.912 4.634   -0.463 1.00 23.26  ? 141 LEU   A CD2 1 
ATOM   1057 N  N   . TRP   A 1 136 ? 22.536 7.169   0.894  1.00 19.44  ? 142 TRP   A N   1 
ATOM   1058 C  CA  . TRP   A 1 136 ? 23.942 7.426   1.091  1.00 20.30  ? 142 TRP   A CA  1 
ATOM   1059 C  C   . TRP   A 1 136 ? 24.496 6.825   2.385  1.00 21.11  ? 142 TRP   A C   1 
ATOM   1060 O  O   . TRP   A 1 136 ? 25.718 6.706   2.516  1.00 22.07  ? 142 TRP   A O   1 
ATOM   1061 C  CB  . TRP   A 1 136 ? 24.252 8.944   0.977  1.00 21.02  ? 142 TRP   A CB  1 
ATOM   1062 C  CG  . TRP   A 1 136 ? 23.423 9.776   1.907  1.00 20.54  ? 142 TRP   A CG  1 
ATOM   1063 C  CD1 . TRP   A 1 136 ? 22.249 10.419  1.621  1.00 21.14  ? 142 TRP   A CD1 1 
ATOM   1064 C  CD2 . TRP   A 1 136 ? 23.736 10.086  3.274  1.00 20.27  ? 142 TRP   A CD2 1 
ATOM   1065 N  NE1 . TRP   A 1 136 ? 21.791 11.078  2.748  1.00 21.15  ? 142 TRP   A NE1 1 
ATOM   1066 C  CE2 . TRP   A 1 136 ? 22.701 10.900  3.766  1.00 20.32  ? 142 TRP   A CE2 1 
ATOM   1067 C  CE3 . TRP   A 1 136 ? 24.819 9.784   4.111  1.00 20.38  ? 142 TRP   A CE3 1 
ATOM   1068 C  CZ2 . TRP   A 1 136 ? 22.718 11.400  5.074  1.00 20.51  ? 142 TRP   A CZ2 1 
ATOM   1069 C  CZ3 . TRP   A 1 136 ? 24.828 10.274  5.402  1.00 21.03  ? 142 TRP   A CZ3 1 
ATOM   1070 C  CH2 . TRP   A 1 136 ? 23.805 11.091  5.858  1.00 20.36  ? 142 TRP   A CH2 1 
ATOM   1071 N  N   . LEU   A 1 137 ? 23.621 6.438   3.361  1.00 20.31  ? 143 LEU   A N   1 
ATOM   1072 C  CA  . LEU   A 1 137 ? 24.124 5.814   4.592  1.00 22.01  ? 143 LEU   A CA  1 
ATOM   1073 C  C   . LEU   A 1 137 ? 24.820 4.475   4.297  1.00 25.26  ? 143 LEU   A C   1 
ATOM   1074 O  O   . LEU   A 1 137 ? 25.653 4.068   5.107  1.00 24.36  ? 143 LEU   A O   1 
ATOM   1075 C  CB  . LEU   A 1 137 ? 22.975 5.572   5.587  1.00 21.08  ? 143 LEU   A CB  1 
ATOM   1076 C  CG  . LEU   A 1 137 ? 22.397 6.804   6.255  1.00 20.61  ? 143 LEU   A CG  1 
ATOM   1077 C  CD1 . LEU   A 1 137 ? 21.173 6.428   7.070  1.00 21.40  ? 143 LEU   A CD1 1 
ATOM   1078 C  CD2 . LEU   A 1 137 ? 23.446 7.434   7.214  1.00 20.50  ? 143 LEU   A CD2 1 
ATOM   1079 N  N   . ASP   A 1 138 ? 24.503 3.819   3.143  1.00 28.30  ? 144 ASP   A N   1 
ATOM   1080 C  CA  . ASP   A 1 138 ? 25.069 2.516   2.747  1.00 31.81  ? 144 ASP   A CA  1 
ATOM   1081 C  C   . ASP   A 1 138 ? 26.410 2.571   2.051  1.00 35.80  ? 144 ASP   A C   1 
ATOM   1082 O  O   . ASP   A 1 138 ? 26.925 1.512   1.678  1.00 35.77  ? 144 ASP   A O   1 
ATOM   1083 C  CB  . ASP   A 1 138 ? 24.119 1.788   1.777  1.00 34.04  ? 144 ASP   A CB  1 
ATOM   1084 C  CG  . ASP   A 1 138 ? 22.776 1.436   2.337  1.00 40.44  ? 144 ASP   A CG  1 
ATOM   1085 O  OD1 . ASP   A 1 138 ? 22.634 1.449   3.563  1.00 42.42  ? 144 ASP   A OD1 1 
ATOM   1086 O  OD2 . ASP   A 1 138 ? 21.843 1.155   1.535  1.00 44.39  ? 144 ASP   A OD2 1 
ATOM   1087 N  N   . GLU   A 1 139 ? 26.973 3.766   1.836  1.00 38.68  ? 145 GLU   A N   1 
ATOM   1088 C  CA  . GLU   A 1 139 ? 28.249 3.858   1.116  1.00 42.44  ? 145 GLU   A CA  1 
ATOM   1089 C  C   . GLU   A 1 139 ? 29.161 4.983   1.612  1.00 44.77  ? 145 GLU   A C   1 
ATOM   1090 O  O   . GLU   A 1 139 ? 28.761 5.752   2.489  1.00 44.92  ? 145 GLU   A O   1 
ATOM   1091 C  CB  . GLU   A 1 139 ? 27.950 4.024   -0.376 1.00 46.88  ? 145 GLU   A CB  1 
ATOM   1092 C  CG  . GLU   A 1 139 ? 27.196 5.302   -0.661 1.00 54.94  ? 145 GLU   A CG  1 
ATOM   1093 C  CD  . GLU   A 1 139 ? 26.211 5.154   -1.799 1.00 65.42  ? 145 GLU   A CD  1 
ATOM   1094 O  OE1 . GLU   A 1 139 ? 26.012 6.140   -2.547 1.00 68.52  ? 145 GLU   A OE1 1 
ATOM   1095 O  OE2 . GLU   A 1 139 ? 25.634 4.051   -1.943 1.00 68.51  ? 145 GLU   A OE2 1 
ATOM   1096 N  N   . GLU   A 1 140 ? 30.369 5.098   1.016  1.00 46.88  ? 146 GLU   A N   1 
ATOM   1097 C  CA  . GLU   A 1 140 ? 31.399 6.100   1.293  1.00 49.54  ? 146 GLU   A CA  1 
ATOM   1098 C  C   . GLU   A 1 140 ? 31.924 5.969   2.715  1.00 51.41  ? 146 GLU   A C   1 
ATOM   1099 O  O   . GLU   A 1 140 ? 32.999 5.399   2.908  1.00 52.52  ? 146 GLU   A O   1 
ATOM   1100 C  CB  . GLU   A 1 140 ? 30.930 7.531   0.939  1.00 52.79  ? 146 GLU   A CB  1 
ATOM   1101 C  CG  . GLU   A 1 140 ? 31.616 8.672   1.689  1.00 60.63  ? 146 GLU   A CG  1 
ATOM   1102 C  CD  . GLU   A 1 140 ? 32.927 9.190   1.119  1.00 69.67  ? 146 GLU   A CD  1 
ATOM   1103 O  OE1 . GLU   A 1 140 ? 33.120 10.427  1.121  1.00 71.47  ? 146 GLU   A OE1 1 
ATOM   1104 O  OE2 . GLU   A 1 140 ? 33.761 8.368   0.674  1.00 72.77  ? 146 GLU   A OE2 1 
ATOM   1105 N  N   . SER   B 1 1   ? 21.975 -21.324 7.718  1.00 26.43  ? 7   SER   C N   1 
ATOM   1106 C  CA  . SER   B 1 1   ? 20.830 -21.135 8.617  1.00 26.11  ? 7   SER   C CA  1 
ATOM   1107 C  C   . SER   B 1 1   ? 20.788 -22.215 9.729  1.00 25.32  ? 7   SER   C C   1 
ATOM   1108 O  O   . SER   B 1 1   ? 21.445 -23.250 9.597  1.00 26.63  ? 7   SER   C O   1 
ATOM   1109 C  CB  . SER   B 1 1   ? 19.543 -21.161 7.793  1.00 28.58  ? 7   SER   C CB  1 
ATOM   1110 O  OG  . SER   B 1 1   ? 19.346 -22.483 7.305  1.00 33.62  ? 7   SER   C OG  1 
ATOM   1111 N  N   . GLY   B 1 2   ? 20.019 -21.974 10.797 1.00 23.39  ? 8   GLY   C N   1 
ATOM   1112 C  CA  . GLY   B 1 2   ? 19.901 -22.961 11.870 1.00 22.46  ? 8   GLY   C CA  1 
ATOM   1113 C  C   . GLY   B 1 2   ? 19.619 -22.334 13.222 1.00 21.64  ? 8   GLY   C C   1 
ATOM   1114 O  O   . GLY   B 1 2   ? 20.013 -21.191 13.474 1.00 21.59  ? 8   GLY   C O   1 
ATOM   1115 N  N   . ALA   B 1 3   ? 18.964 -23.099 14.109 1.00 21.09  ? 9   ALA   C N   1 
ATOM   1116 C  CA  . ALA   B 1 3   ? 18.638 -22.599 15.441 1.00 20.11  ? 9   ALA   C CA  1 
ATOM   1117 C  C   . ALA   B 1 3   ? 18.733 -23.731 16.459 1.00 19.89  ? 9   ALA   C C   1 
ATOM   1118 O  O   . ALA   B 1 3   ? 18.714 -24.909 16.085 1.00 20.03  ? 9   ALA   C O   1 
ATOM   1119 C  CB  . ALA   B 1 3   ? 17.196 -22.031 15.445 1.00 21.59  ? 9   ALA   C CB  1 
ATOM   1120 N  N   . ILE   B 1 4   ? 18.807 -23.369 17.748 1.00 18.88  ? 10  ILE   C N   1 
ATOM   1121 C  CA  . ILE   B 1 4   ? 18.721 -24.327 18.841 1.00 18.25  ? 10  ILE   C CA  1 
ATOM   1122 C  C   . ILE   B 1 4   ? 17.318 -24.122 19.454 1.00 19.65  ? 10  ILE   C C   1 
ATOM   1123 O  O   . ILE   B 1 4   ? 16.901 -22.965 19.694 1.00 19.61  ? 10  ILE   C O   1 
ATOM   1124 C  CB  . ILE   B 1 4   ? 19.757 -24.016 19.928 1.00 18.21  ? 10  ILE   C CB  1 
ATOM   1125 C  CG1 . ILE   B 1 4   ? 21.190 -23.912 19.364 1.00 19.23  ? 10  ILE   C CG1 1 
ATOM   1126 C  CG2 . ILE   B 1 4   ? 19.663 -25.066 21.038 1.00 19.23  ? 10  ILE   C CG2 1 
ATOM   1127 C  CD1 . ILE   B 1 4   ? 22.199 -23.330 20.392 1.00 20.66  ? 10  ILE   C CD1 1 
ATOM   1128 N  N   . TYR   B 1 5   ? 16.614 -25.211 19.748 1.00 19.42  ? 11  TYR   C N   1 
ATOM   1129 C  CA  . TYR   B 1 5   ? 15.280 -25.140 20.333 1.00 20.32  ? 11  TYR   C CA  1 
ATOM   1130 C  C   . TYR   B 1 5   ? 15.346 -25.830 21.706 1.00 20.32  ? 11  TYR   C C   1 
ATOM   1131 O  O   . TYR   B 1 5   ? 15.448 -27.037 21.770 1.00 21.46  ? 11  TYR   C O   1 
ATOM   1132 C  CB  . TYR   B 1 5   ? 14.242 -25.830 19.421 1.00 20.37  ? 11  TYR   C CB  1 
ATOM   1133 C  CG  . TYR   B 1 5   ? 14.037 -25.075 18.126 1.00 21.40  ? 11  TYR   C CG  1 
ATOM   1134 C  CD1 . TYR   B 1 5   ? 13.224 -23.954 18.077 1.00 22.29  ? 11  TYR   C CD1 1 
ATOM   1135 C  CD2 . TYR   B 1 5   ? 14.746 -25.414 16.979 1.00 22.36  ? 11  TYR   C CD2 1 
ATOM   1136 C  CE1 . TYR   B 1 5   ? 13.062 -23.234 16.906 1.00 23.75  ? 11  TYR   C CE1 1 
ATOM   1137 C  CE2 . TYR   B 1 5   ? 14.605 -24.690 15.801 1.00 24.26  ? 11  TYR   C CE2 1 
ATOM   1138 C  CZ  . TYR   B 1 5   ? 13.778 -23.590 15.772 1.00 25.58  ? 11  TYR   C CZ  1 
ATOM   1139 O  OH  . TYR   B 1 5   ? 13.669 -22.848 14.617 1.00 27.91  ? 11  TYR   C OH  1 
ATOM   1140 N  N   . VAL   B 1 6   ? 15.309 -25.065 22.794 1.00 19.90  ? 12  VAL   C N   1 
ATOM   1141 C  CA  . VAL   B 1 6   ? 15.410 -25.603 24.139 1.00 20.60  ? 12  VAL   C CA  1 
ATOM   1142 C  C   . VAL   B 1 6   ? 14.322 -25.035 24.996 1.00 21.21  ? 12  VAL   C C   1 
ATOM   1143 O  O   . VAL   B 1 6   ? 14.168 -23.822 25.056 1.00 20.82  ? 12  VAL   C O   1 
ATOM   1144 C  CB  . VAL   B 1 6   ? 16.813 -25.372 24.765 1.00 22.61  ? 12  VAL   C CB  1 
ATOM   1145 C  CG1 . VAL   B 1 6   ? 17.241 -23.895 24.725 1.00 22.38  ? 12  VAL   C CG1 1 
ATOM   1146 C  CG2 . VAL   B 1 6   ? 16.855 -25.939 26.176 1.00 24.54  ? 12  VAL   C CG2 1 
ATOM   1147 N  N   . GLY   B 1 7   ? 13.511 -25.893 25.634 1.00 21.66  ? 13  GLY   C N   1 
ATOM   1148 C  CA  . GLY   B 1 7   ? 12.394 -25.382 26.439 1.00 21.96  ? 13  GLY   C CA  1 
ATOM   1149 C  C   . GLY   B 1 7   ? 11.478 -24.509 25.584 1.00 22.40  ? 13  GLY   C C   1 
ATOM   1150 O  O   . GLY   B 1 7   ? 11.194 -24.867 24.440 1.00 24.00  ? 13  GLY   C O   1 
ATOM   1151 N  N   . ASN   B 1 8   ? 11.137 -23.303 26.057 1.00 22.11  ? 14  ASN   C N   1 
ATOM   1152 C  CA  . ASN   B 1 8   ? 10.357 -22.384 25.224 1.00 22.41  ? 14  ASN   C CA  1 
ATOM   1153 C  C   . ASN   B 1 8   ? 11.243 -21.284 24.651 1.00 21.19  ? 14  ASN   C C   1 
ATOM   1154 O  O   . ASN   B 1 8   ? 10.805 -20.127 24.524 1.00 21.60  ? 14  ASN   C O   1 
ATOM   1155 C  CB  . ASN   B 1 8   ? 9.155  -21.823 25.958 1.00 24.78  ? 14  ASN   C CB  1 
ATOM   1156 C  CG  . ASN   B 1 8   ? 8.070  -22.873 26.123 1.00 30.95  ? 14  ASN   C CG  1 
ATOM   1157 O  OD1 . ASN   B 1 8   ? 7.168  -22.995 25.293 1.00 33.03  ? 14  ASN   C OD1 1 
ATOM   1158 N  ND2 . ASN   B 1 8   ? 8.161  -23.661 27.168 1.00 32.32  ? 14  ASN   C ND2 1 
ATOM   1159 N  N   . TYR   B 1 9   ? 12.469 -21.652 24.263 1.00 19.41  ? 15  TYR   C N   1 
ATOM   1160 C  CA  . TYR   B 1 9   ? 13.420 -20.679 23.667 1.00 20.00  ? 15  TYR   C CA  1 
ATOM   1161 C  C   . TYR   B 1 9   ? 13.906 -21.148 22.289 1.00 19.33  ? 15  TYR   C C   1 
ATOM   1162 O  O   . TYR   B 1 9   ? 14.063 -22.359 22.048 1.00 19.75  ? 15  TYR   C O   1 
ATOM   1163 C  CB  . TYR   B 1 9   ? 14.673 -20.521 24.563 1.00 20.53  ? 15  TYR   C CB  1 
ATOM   1164 C  CG  . TYR   B 1 9   ? 14.361 -19.996 25.962 1.00 22.14  ? 15  TYR   C CG  1 
ATOM   1165 C  CD1 . TYR   B 1 9   ? 13.827 -18.727 26.147 1.00 23.71  ? 15  TYR   C CD1 1 
ATOM   1166 C  CD2 . TYR   B 1 9   ? 14.649 -20.754 27.093 1.00 24.09  ? 15  TYR   C CD2 1 
ATOM   1167 C  CE1 . TYR   B 1 9   ? 13.574 -18.229 27.421 1.00 25.99  ? 15  TYR   C CE1 1 
ATOM   1168 C  CE2 . TYR   B 1 9   ? 14.420 -20.256 28.375 1.00 26.08  ? 15  TYR   C CE2 1 
ATOM   1169 C  CZ  . TYR   B 1 9   ? 13.891 -18.990 28.532 1.00 28.32  ? 15  TYR   C CZ  1 
ATOM   1170 O  OH  . TYR   B 1 9   ? 13.636 -18.495 29.793 1.00 33.20  ? 15  TYR   C OH  1 
ATOM   1171 N  N   . ARG   B 1 10  ? 14.166 -20.180 21.399 1.00 18.22  ? 16  ARG   C N   1 
ATOM   1172 C  CA  . ARG   B 1 10  ? 14.762 -20.395 20.080 1.00 18.69  ? 16  ARG   C CA  1 
ATOM   1173 C  C   . ARG   B 1 10  ? 16.040 -19.537 20.063 1.00 18.65  ? 16  ARG   C C   1 
ATOM   1174 O  O   . ARG   B 1 10  ? 15.956 -18.316 20.271 1.00 18.52  ? 16  ARG   C O   1 
ATOM   1175 C  CB  . ARG   B 1 10  ? 13.798 -19.917 18.953 1.00 19.92  ? 16  ARG   C CB  1 
ATOM   1176 C  CG  . ARG   B 1 10  ? 14.431 -19.765 17.538 1.00 20.93  ? 16  ARG   C CG  1 
ATOM   1177 C  CD  . ARG   B 1 10  ? 13.356 -19.496 16.470 1.00 21.84  ? 16  ARG   C CD  1 
ATOM   1178 N  NE  . ARG   B 1 10  ? 13.801 -18.524 15.463 1.00 23.39  ? 16  ARG   C NE  1 
ATOM   1179 C  CZ  . ARG   B 1 10  ? 14.302 -18.835 14.264 1.00 24.38  ? 16  ARG   C CZ  1 
ATOM   1180 N  NH1 . ARG   B 1 10  ? 14.502 -20.103 13.925 1.00 23.55  ? 16  ARG   C NH1 1 
ATOM   1181 N  NH2 . ARG   B 1 10  ? 14.635 -17.877 13.408 1.00 25.68  ? 16  ARG   C NH2 1 
ATOM   1182 N  N   . VAL   B 1 11  ? 17.217 -20.161 19.854 1.00 17.48  ? 17  VAL   C N   1 
ATOM   1183 C  CA  . VAL   B 1 11  ? 18.500 -19.437 19.821 1.00 17.51  ? 17  VAL   C CA  1 
ATOM   1184 C  C   . VAL   B 1 11  ? 18.957 -19.393 18.382 1.00 18.12  ? 17  VAL   C C   1 
ATOM   1185 O  O   . VAL   B 1 11  ? 19.129 -20.450 17.752 1.00 18.53  ? 17  VAL   C O   1 
ATOM   1186 C  CB  . VAL   B 1 11  ? 19.573 -20.166 20.667 1.00 19.02  ? 17  VAL   C CB  1 
ATOM   1187 C  CG1 . VAL   B 1 11  ? 20.836 -19.315 20.788 1.00 20.93  ? 17  VAL   C CG1 1 
ATOM   1188 C  CG2 . VAL   B 1 11  ? 19.036 -20.570 22.044 1.00 20.34  ? 17  VAL   C CG2 1 
ATOM   1189 N  N   . VAL   B 1 12  ? 19.177 -18.172 17.855 1.00 17.82  ? 18  VAL   C N   1 
ATOM   1190 C  CA  A VAL   B 1 12  ? 19.619 -18.009 16.472 0.50 17.31  ? 18  VAL   C CA  1 
ATOM   1191 C  CA  B VAL   B 1 12  ? 19.536 -17.927 16.447 0.50 19.29  ? 18  VAL   C CA  1 
ATOM   1192 C  C   . VAL   B 1 12  ? 20.779 -17.015 16.382 1.00 19.21  ? 18  VAL   C C   1 
ATOM   1193 O  O   . VAL   B 1 12  ? 21.035 -16.246 17.332 1.00 19.54  ? 18  VAL   C O   1 
ATOM   1194 C  CB  A VAL   B 1 12  ? 18.454 -17.494 15.584 0.50 16.82  ? 18  VAL   C CB  1 
ATOM   1195 C  CB  B VAL   B 1 12  ? 18.374 -17.153 15.689 0.50 22.44  ? 18  VAL   C CB  1 
ATOM   1196 C  CG1 A VAL   B 1 12  ? 17.428 -18.571 15.344 0.50 16.71  ? 18  VAL   C CG1 1 
ATOM   1197 C  CG1 B VAL   B 1 12  ? 18.286 -17.541 14.218 0.50 22.96  ? 18  VAL   C CG1 1 
ATOM   1198 C  CG2 A VAL   B 1 12  ? 17.836 -16.196 16.140 0.50 15.31  ? 18  VAL   C CG2 1 
ATOM   1199 C  CG2 B VAL   B 1 12  ? 17.004 -17.255 16.367 0.50 24.52  ? 18  VAL   C CG2 1 
ATOM   1200 N  N   . ASN   B 1 13  ? 21.477 -16.969 15.191 1.00 17.80  ? 19  ASN   C N   1 
ATOM   1201 C  CA  . ASN   B 1 13  ? 22.502 -15.944 15.009 1.00 17.23  ? 19  ASN   C CA  1 
ATOM   1202 C  C   . ASN   B 1 13  ? 21.708 -14.586 14.974 1.00 17.66  ? 19  ASN   C C   1 
ATOM   1203 O  O   . ASN   B 1 13  ? 20.686 -14.495 14.278 1.00 17.64  ? 19  ASN   C O   1 
ATOM   1204 C  CB  . ASN   B 1 13  ? 23.173 -16.092 13.642 1.00 18.02  ? 19  ASN   C CB  1 
ATOM   1205 C  CG  . ASN   B 1 13  ? 24.006 -17.361 13.569 1.00 19.17  ? 19  ASN   C CG  1 
ATOM   1206 O  OD1 . ASN   B 1 13  ? 23.520 -18.425 13.132 1.00 20.61  ? 19  ASN   C OD1 1 
ATOM   1207 N  ND2 . ASN   B 1 13  ? 25.271 -17.271 13.985 1.00 17.87  ? 19  ASN   C ND2 1 
ATOM   1208 N  N   . ARG   B 1 14  ? 22.169 -13.559 15.682 1.00 17.66  ? 20  ARG   C N   1 
ATOM   1209 C  CA  . ARG   B 1 14  ? 21.419 -12.282 15.707 1.00 17.97  ? 20  ARG   C CA  1 
ATOM   1210 C  C   . ARG   B 1 14  ? 21.277 -11.710 14.260 1.00 19.59  ? 20  ARG   C C   1 
ATOM   1211 O  O   . ARG   B 1 14  ? 20.224 -11.149 13.906 1.00 20.24  ? 20  ARG   C O   1 
ATOM   1212 C  CB  . ARG   B 1 14  ? 22.172 -11.276 16.607 1.00 18.24  ? 20  ARG   C CB  1 
ATOM   1213 C  CG  . ARG   B 1 14  ? 21.395 -9.946  16.814 1.00 19.77  ? 20  ARG   C CG  1 
ATOM   1214 C  CD  . ARG   B 1 14  ? 22.287 -8.982  17.567 1.00 20.73  ? 20  ARG   C CD  1 
ATOM   1215 N  NE  . ARG   B 1 14  ? 21.642 -7.730  18.029 1.00 20.89  ? 20  ARG   C NE  1 
ATOM   1216 C  CZ  . ARG   B 1 14  ? 21.503 -6.644  17.279 1.00 21.54  ? 20  ARG   C CZ  1 
ATOM   1217 N  NH1 . ARG   B 1 14  ? 21.892 -6.650  16.009 1.00 22.07  ? 20  ARG   C NH1 1 
ATOM   1218 N  NH2 . ARG   B 1 14  ? 21.016 -5.519  17.805 1.00 21.02  ? 20  ARG   C NH2 1 
ATOM   1219 N  N   . HIS   B 1 15  ? 22.322 -11.884 13.404 1.00 19.71  ? 21  HIS   C N   1 
ATOM   1220 C  CA  . HIS   B 1 15  ? 22.258 -11.349 12.024 1.00 19.59  ? 21  HIS   C CA  1 
ATOM   1221 C  C   . HIS   B 1 15  ? 21.244 -12.095 11.123 1.00 20.98  ? 21  HIS   C C   1 
ATOM   1222 O  O   . HIS   B 1 15  ? 20.960 -11.618 10.024 1.00 22.60  ? 21  HIS   C O   1 
ATOM   1223 C  CB  . HIS   B 1 15  ? 23.661 -11.264 11.347 1.00 20.60  ? 21  HIS   C CB  1 
ATOM   1224 C  CG  . HIS   B 1 15  ? 24.197 -12.595 10.917 1.00 21.39  ? 21  HIS   C CG  1 
ATOM   1225 N  ND1 . HIS   B 1 15  ? 24.949 -13.384 11.777 1.00 23.14  ? 21  HIS   C ND1 1 
ATOM   1226 C  CD2 . HIS   B 1 15  ? 24.130 -13.197 9.709  1.00 22.01  ? 21  HIS   C CD2 1 
ATOM   1227 C  CE1 . HIS   B 1 15  ? 25.291 -14.459 11.073 1.00 23.03  ? 21  HIS   C CE1 1 
ATOM   1228 N  NE2 . HIS   B 1 15  ? 24.824 -14.390 9.820  1.00 22.69  ? 21  HIS   C NE2 1 
ATOM   1229 N  N   . LEU   B 1 16  ? 20.696 -13.237 11.598 1.00 20.31  ? 22  LEU   C N   1 
ATOM   1230 C  CA  . LEU   B 1 16  ? 19.675 -13.972 10.847 1.00 21.05  ? 22  LEU   C CA  1 
ATOM   1231 C  C   . LEU   B 1 16  ? 18.284 -13.934 11.527 1.00 21.75  ? 22  LEU   C C   1 
ATOM   1232 O  O   . LEU   B 1 16  ? 17.386 -14.663 11.104 1.00 22.73  ? 22  LEU   C O   1 
ATOM   1233 C  CB  . LEU   B 1 16  ? 20.136 -15.419 10.662 1.00 20.80  ? 22  LEU   C CB  1 
ATOM   1234 C  CG  . LEU   B 1 16  ? 21.434 -15.572 9.869  1.00 22.03  ? 22  LEU   C CG  1 
ATOM   1235 C  CD1 . LEU   B 1 16  ? 21.839 -17.047 9.768  1.00 22.00  ? 22  LEU   C CD1 1 
ATOM   1236 C  CD2 . LEU   B 1 16  ? 21.298 -14.987 8.446  1.00 21.90  ? 22  LEU   C CD2 1 
ATOM   1237 N  N   . ALA   B 1 17  ? 18.125 -13.161 12.619 1.00 21.45  ? 23  ALA   C N   1 
ATOM   1238 C  CA  . ALA   B 1 17  ? 16.846 -13.118 13.338 1.00 22.46  ? 23  ALA   C CA  1 
ATOM   1239 C  C   . ALA   B 1 17  ? 15.751 -12.557 12.447 1.00 23.64  ? 23  ALA   C C   1 
ATOM   1240 O  O   . ALA   B 1 17  ? 16.008 -11.652 11.640 1.00 23.82  ? 23  ALA   C O   1 
ATOM   1241 C  CB  . ALA   B 1 17  ? 16.973 -12.288 14.608 1.00 23.03  ? 23  ALA   C CB  1 
ATOM   1242 N  N   . THR   B 1 18  ? 14.542 -13.130 12.570 1.00 23.99  ? 24  THR   C N   1 
ATOM   1243 C  CA  . THR   B 1 18  ? 13.393 -12.694 11.765 1.00 23.56  ? 24  THR   C CA  1 
ATOM   1244 C  C   . THR   B 1 18  ? 12.579 -11.628 12.525 1.00 24.68  ? 24  THR   C C   1 
ATOM   1245 O  O   . THR   B 1 18  ? 12.816 -11.384 13.708 1.00 24.79  ? 24  THR   C O   1 
ATOM   1246 C  CB  . THR   B 1 18  ? 12.471 -13.931 11.519 1.00 25.46  ? 24  THR   C CB  1 
ATOM   1247 O  OG1 . THR   B 1 18  ? 11.905 -14.354 12.754 1.00 26.49  ? 24  THR   C OG1 1 
ATOM   1248 C  CG2 . THR   B 1 18  ? 13.187 -15.108 10.842 1.00 25.93  ? 24  THR   C CG2 1 
ATOM   1249 N  N   . HIS   B 1 19  ? 11.526 -11.032 11.872 1.00 24.20  ? 25  HIS   C N   1 
ATOM   1250 C  CA  . HIS   B 1 19  ? 10.629 -10.110 12.563 1.00 25.79  ? 25  HIS   C CA  1 
ATOM   1251 C  C   . HIS   B 1 19  ? 9.945  -10.851 13.703 1.00 24.60  ? 25  HIS   C C   1 
ATOM   1252 O  O   . HIS   B 1 19  ? 9.811  -10.270 14.770 1.00 25.89  ? 25  HIS   C O   1 
ATOM   1253 C  CB  . HIS   B 1 19  ? 9.520  -9.599  11.609 1.00 28.22  ? 25  HIS   C CB  1 
ATOM   1254 C  CG  . HIS   B 1 19  ? 8.386  -8.897  12.312 1.00 33.26  ? 25  HIS   C CG  1 
ATOM   1255 N  ND1 . HIS   B 1 19  ? 8.500  -7.588  12.727 1.00 35.70  ? 25  HIS   C ND1 1 
ATOM   1256 C  CD2 . HIS   B 1 19  ? 7.177  -9.375  12.701 1.00 35.48  ? 25  HIS   C CD2 1 
ATOM   1257 C  CE1 . HIS   B 1 19  ? 7.337  -7.278  13.283 1.00 36.37  ? 25  HIS   C CE1 1 
ATOM   1258 N  NE2 . HIS   B 1 19  ? 6.510  -8.328  13.308 1.00 36.72  ? 25  HIS   C NE2 1 
ATOM   1259 N  N   . ASN   B 1 20  ? 9.527  -12.135 13.508 1.00 24.15  ? 26  ASN   C N   1 
ATOM   1260 C  CA  . ASN   B 1 20  ? 8.880  -12.871 14.601 1.00 24.70  ? 26  ASN   C CA  1 
ATOM   1261 C  C   . ASN   B 1 20  ? 9.823  -13.007 15.803 1.00 24.10  ? 26  ASN   C C   1 
ATOM   1262 O  O   . ASN   B 1 20  ? 9.375  -12.946 16.947 1.00 23.62  ? 26  ASN   C O   1 
ATOM   1263 C  CB  . ASN   B 1 20  ? 8.403  -14.256 14.157 1.00 27.46  ? 26  ASN   C CB  1 
ATOM   1264 C  CG  . ASN   B 1 20  ? 7.539  -14.901 15.230 1.00 34.79  ? 26  ASN   C CG  1 
ATOM   1265 O  OD1 . ASN   B 1 20  ? 6.392  -14.495 15.466 1.00 36.83  ? 26  ASN   C OD1 1 
ATOM   1266 N  ND2 . ASN   B 1 20  ? 8.087  -15.890 15.938 1.00 36.21  ? 26  ASN   C ND2 1 
ATOM   1267 N  N   . ASP   B 1 21  ? 11.135 -13.220 15.545 1.00 22.82  ? 27  ASP   C N   1 
ATOM   1268 C  CA  . ASP   B 1 21  ? 12.100 -13.322 16.646 1.00 22.52  ? 27  ASP   C CA  1 
ATOM   1269 C  C   . ASP   B 1 21  ? 12.145 -11.995 17.437 1.00 23.16  ? 27  ASP   C C   1 
ATOM   1270 O  O   . ASP   B 1 21  ? 12.101 -12.014 18.666 1.00 23.46  ? 27  ASP   C O   1 
ATOM   1271 C  CB  . ASP   B 1 21  ? 13.511 -13.623 16.106 1.00 22.94  ? 27  ASP   C CB  1 
ATOM   1272 C  CG  . ASP   B 1 21  ? 13.690 -15.032 15.618 1.00 23.81  ? 27  ASP   C CG  1 
ATOM   1273 O  OD1 . ASP   B 1 21  ? 13.160 -15.954 16.274 1.00 23.76  ? 27  ASP   C OD1 1 
ATOM   1274 O  OD2 . ASP   B 1 21  ? 14.379 -15.220 14.581 1.00 23.43  ? 27  ASP   C OD2 1 
ATOM   1275 N  N   . TRP   B 1 22  ? 12.250 -10.852 16.732 1.00 23.12  ? 28  TRP   C N   1 
ATOM   1276 C  CA  . TRP   B 1 22  ? 12.285 -9.557  17.414 1.00 23.25  ? 28  TRP   C CA  1 
ATOM   1277 C  C   . TRP   B 1 22  ? 10.953 -9.247  18.141 1.00 23.51  ? 28  TRP   C C   1 
ATOM   1278 O  O   . TRP   B 1 22  ? 10.961 -8.584  19.173 1.00 23.50  ? 28  TRP   C O   1 
ATOM   1279 C  CB  . TRP   B 1 22  ? 12.631 -8.445  16.432 1.00 23.02  ? 28  TRP   C CB  1 
ATOM   1280 C  CG  . TRP   B 1 22  ? 14.097 -8.415  16.110 1.00 22.93  ? 28  TRP   C CG  1 
ATOM   1281 C  CD1 . TRP   B 1 22  ? 14.705 -8.889  14.982 1.00 23.68  ? 28  TRP   C CD1 1 
ATOM   1282 C  CD2 . TRP   B 1 22  ? 15.144 -7.884  16.942 1.00 22.74  ? 28  TRP   C CD2 1 
ATOM   1283 N  NE1 . TRP   B 1 22  ? 16.070 -8.647  15.041 1.00 24.06  ? 28  TRP   C NE1 1 
ATOM   1284 C  CE2 . TRP   B 1 22  ? 16.360 -8.029  16.233 1.00 23.62  ? 28  TRP   C CE2 1 
ATOM   1285 C  CE3 . TRP   B 1 22  ? 15.158 -7.219  18.174 1.00 23.18  ? 28  TRP   C CE3 1 
ATOM   1286 C  CZ2 . TRP   B 1 22  ? 17.581 -7.585  16.740 1.00 23.69  ? 28  TRP   C CZ2 1 
ATOM   1287 C  CZ3 . TRP   B 1 22  ? 16.382 -6.791  18.685 1.00 24.42  ? 28  TRP   C CZ3 1 
ATOM   1288 C  CH2 . TRP   B 1 22  ? 17.572 -6.962  17.954 1.00 24.33  ? 28  TRP   C CH2 1 
ATOM   1289 N  N   . ALA   B 1 23  ? 9.815  -9.694  17.579 1.00 23.50  ? 29  ALA   C N   1 
ATOM   1290 C  CA  . ALA   B 1 23  ? 8.506  -9.469  18.197 1.00 25.00  ? 29  ALA   C CA  1 
ATOM   1291 C  C   . ALA   B 1 23  ? 8.275  -10.364 19.428 1.00 26.33  ? 29  ALA   C C   1 
ATOM   1292 O  O   . ALA   B 1 23  ? 7.285  -10.158 20.148 1.00 27.54  ? 29  ALA   C O   1 
ATOM   1293 C  CB  . ALA   B 1 23  ? 7.389  -9.699  17.182 1.00 25.62  ? 29  ALA   C CB  1 
ATOM   1294 N  N   . ASN   B 1 24  ? 9.131  -11.402 19.638 1.00 25.22  ? 30  ASN   C N   1 
ATOM   1295 C  CA  . ASN   B 1 24  ? 9.006  -12.283 20.801 1.00 24.79  ? 30  ASN   C CA  1 
ATOM   1296 C  C   . ASN   B 1 24  ? 10.387 -12.361 21.491 1.00 24.42  ? 30  ASN   C C   1 
ATOM   1297 O  O   . ASN   B 1 24  ? 10.827 -13.440 21.908 1.00 23.32  ? 30  ASN   C O   1 
ATOM   1298 C  CB  . ASN   B 1 24  ? 8.559  -13.668 20.319 1.00 25.76  ? 30  ASN   C CB  1 
ATOM   1299 C  CG  . ASN   B 1 24  ? 7.133  -13.626 19.852 1.00 27.29  ? 30  ASN   C CG  1 
ATOM   1300 O  OD1 . ASN   B 1 24  ? 6.217  -13.643 20.678 1.00 29.36  ? 30  ASN   C OD1 1 
ATOM   1301 N  ND2 . ASN   B 1 24  ? 6.932  -13.554 18.543 1.00 27.07  ? 30  ASN   C ND2 1 
ATOM   1302 N  N   . LEU   B 1 25  ? 11.086 -11.223 21.572 1.00 24.69  ? 31  LEU   C N   1 
ATOM   1303 C  CA  . LEU   B 1 25  ? 12.461 -11.161 22.070 1.00 23.33  ? 31  LEU   C CA  1 
ATOM   1304 C  C   . LEU   B 1 25  ? 12.607 -11.493 23.539 1.00 24.97  ? 31  LEU   C C   1 
ATOM   1305 O  O   . LEU   B 1 25  ? 11.807 -11.031 24.368 1.00 25.95  ? 31  LEU   C O   1 
ATOM   1306 C  CB  . LEU   B 1 25  ? 13.052 -9.765  21.786 1.00 22.77  ? 31  LEU   C CB  1 
ATOM   1307 C  CG  . LEU   B 1 25  ? 14.511 -9.595  22.188 1.00 23.31  ? 31  LEU   C CG  1 
ATOM   1308 C  CD1 . LEU   B 1 25  ? 15.418 -10.513 21.346 1.00 23.36  ? 31  LEU   C CD1 1 
ATOM   1309 C  CD2 . LEU   B 1 25  ? 14.947 -8.149  22.021 1.00 25.11  ? 31  LEU   C CD2 1 
ATOM   1310 N  N   . VAL   B 1 26  ? 13.613 -12.333 23.868 1.00 23.64  ? 32  VAL   C N   1 
ATOM   1311 C  CA  . VAL   B 1 26  ? 13.945 -12.657 25.257 1.00 23.32  ? 32  VAL   C CA  1 
ATOM   1312 C  C   . VAL   B 1 26  ? 15.270 -11.954 25.610 1.00 23.51  ? 32  VAL   C C   1 
ATOM   1313 O  O   . VAL   B 1 26  ? 15.372 -11.293 26.649 1.00 24.35  ? 32  VAL   C O   1 
ATOM   1314 C  CB  . VAL   B 1 26  ? 14.073 -14.190 25.473 1.00 24.29  ? 32  VAL   C CB  1 
ATOM   1315 C  CG1 . VAL   B 1 26  ? 14.674 -14.510 26.842 1.00 25.03  ? 32  VAL   C CG1 1 
ATOM   1316 C  CG2 . VAL   B 1 26  ? 12.720 -14.874 25.296 1.00 24.43  ? 32  VAL   C CG2 1 
ATOM   1317 N  N   . TRP   B 1 27  ? 16.292 -12.073 24.727 1.00 22.09  ? 33  TRP   C N   1 
ATOM   1318 C  CA  . TRP   B 1 27  ? 17.607 -11.508 25.002 1.00 21.57  ? 33  TRP   C CA  1 
ATOM   1319 C  C   . TRP   B 1 27  ? 18.422 -11.470 23.691 1.00 22.16  ? 33  TRP   C C   1 
ATOM   1320 O  O   . TRP   B 1 27  ? 18.262 -12.363 22.854 1.00 22.30  ? 33  TRP   C O   1 
ATOM   1321 C  CB  . TRP   B 1 27  ? 18.350 -12.424 26.014 1.00 22.11  ? 33  TRP   C CB  1 
ATOM   1322 C  CG  . TRP   B 1 27  ? 19.827 -12.177 26.210 1.00 22.97  ? 33  TRP   C CG  1 
ATOM   1323 C  CD1 . TRP   B 1 27  ? 20.401 -11.275 27.055 1.00 24.95  ? 33  TRP   C CD1 1 
ATOM   1324 C  CD2 . TRP   B 1 27  ? 20.918 -12.891 25.586 1.00 22.71  ? 33  TRP   C CD2 1 
ATOM   1325 N  NE1 . TRP   B 1 27  ? 21.785 -11.354 26.973 1.00 25.59  ? 33  TRP   C NE1 1 
ATOM   1326 C  CE2 . TRP   B 1 27  ? 22.122 -12.337 26.080 1.00 23.71  ? 33  TRP   C CE2 1 
ATOM   1327 C  CE3 . TRP   B 1 27  ? 20.993 -13.898 24.616 1.00 22.86  ? 33  TRP   C CE3 1 
ATOM   1328 C  CZ2 . TRP   B 1 27  ? 23.375 -12.818 25.698 1.00 23.88  ? 33  TRP   C CZ2 1 
ATOM   1329 C  CZ3 . TRP   B 1 27  ? 22.236 -14.358 24.233 1.00 23.75  ? 33  TRP   C CZ3 1 
ATOM   1330 C  CH2 . TRP   B 1 27  ? 23.404 -13.813 24.766 1.00 23.86  ? 33  TRP   C CH2 1 
ATOM   1331 N  N   . GLU   B 1 28  ? 19.243 -10.427 23.509 1.00 21.21  ? 34  GLU   C N   1 
ATOM   1332 C  CA  . GLU   B 1 28  ? 20.108 -10.388 22.323 1.00 21.42  ? 34  GLU   C CA  1 
ATOM   1333 C  C   . GLU   B 1 28  ? 21.445 -9.749  22.695 1.00 21.75  ? 34  GLU   C C   1 
ATOM   1334 O  O   . GLU   B 1 28  ? 21.491 -8.882  23.593 1.00 21.24  ? 34  GLU   C O   1 
ATOM   1335 C  CB  . GLU   B 1 28  ? 19.426 -9.642  21.148 1.00 23.29  ? 34  GLU   C CB  1 
ATOM   1336 C  CG  . GLU   B 1 28  ? 18.853 -8.273  21.475 1.00 25.15  ? 34  GLU   C CG  1 
ATOM   1337 C  CD  . GLU   B 1 28  ? 19.842 -7.126  21.406 1.00 27.78  ? 34  GLU   C CD  1 
ATOM   1338 O  OE1 . GLU   B 1 28  ? 19.626 -6.112  22.105 1.00 28.61  ? 34  GLU   C OE1 1 
ATOM   1339 O  OE2 . GLU   B 1 28  ? 20.843 -7.246  20.666 1.00 24.34  ? 34  GLU   C OE2 1 
ATOM   1340 N  N   . ASP   B 1 29  ? 22.526 -10.114 21.979 1.00 20.29  ? 35  ASP   C N   1 
ATOM   1341 C  CA  . ASP   B 1 29  ? 23.818 -9.510  22.248 1.00 20.86  ? 35  ASP   C CA  1 
ATOM   1342 C  C   . ASP   B 1 29  ? 24.580 -9.454  20.917 1.00 20.70  ? 35  ASP   C C   1 
ATOM   1343 O  O   . ASP   B 1 29  ? 24.956 -10.486 20.393 1.00 20.60  ? 35  ASP   C O   1 
ATOM   1344 C  CB  . ASP   B 1 29  ? 24.548 -10.290 23.337 1.00 22.21  ? 35  ASP   C CB  1 
ATOM   1345 C  CG  . ASP   B 1 29  ? 25.901 -9.715  23.731 1.00 28.66  ? 35  ASP   C CG  1 
ATOM   1346 O  OD1 . ASP   B 1 29  ? 26.606 -9.194  22.850 1.00 29.16  ? 35  ASP   C OD1 1 
ATOM   1347 O  OD2 . ASP   B 1 29  ? 26.272 -9.830  24.913 1.00 30.80  ? 35  ASP   C OD2 1 
ATOM   1348 N  N   . SER   B 1 30  ? 24.724 -8.252  20.347 1.00 20.05  ? 36  SER   C N   1 
ATOM   1349 C  CA  A SER   B 1 30  ? 25.416 -8.062  19.078 0.50 19.43  ? 36  SER   C CA  1 
ATOM   1350 C  CA  B SER   B 1 30  ? 25.402 -8.099  19.071 0.50 20.46  ? 36  SER   C CA  1 
ATOM   1351 C  C   . SER   B 1 30  ? 26.877 -8.524  19.151 1.00 19.89  ? 36  SER   C C   1 
ATOM   1352 O  O   . SER   B 1 30  ? 27.395 -9.121  18.176 1.00 19.78  ? 36  SER   C O   1 
ATOM   1353 C  CB  A SER   B 1 30  ? 25.353 -6.591  18.659 0.50 19.95  ? 36  SER   C CB  1 
ATOM   1354 C  CB  B SER   B 1 30  ? 25.273 -6.662  18.576 0.50 23.96  ? 36  SER   C CB  1 
ATOM   1355 O  OG  A SER   B 1 30  ? 26.201 -6.324  17.551 0.50 18.59  ? 36  SER   C OG  1 
ATOM   1356 O  OG  B SER   B 1 30  ? 25.794 -5.760  19.535 0.50 28.04  ? 36  SER   C OG  1 
ATOM   1357 N  N   . SER   B 1 31  ? 27.568 -8.244  20.283 1.00 20.24  ? 37  SER   C N   1 
ATOM   1358 C  CA  . SER   B 1 31  ? 28.986 -8.650  20.377 1.00 21.11  ? 37  SER   C CA  1 
ATOM   1359 C  C   . SER   B 1 31  ? 29.162 -10.176 20.310 1.00 20.12  ? 37  SER   C C   1 
ATOM   1360 O  O   . SER   B 1 31  ? 30.251 -10.640 19.991 1.00 20.91  ? 37  SER   C O   1 
ATOM   1361 C  CB  . SER   B 1 31  ? 29.631 -8.108  21.640 1.00 25.30  ? 37  SER   C CB  1 
ATOM   1362 O  OG  . SER   B 1 31  ? 29.183 -8.793  22.792 1.00 30.16  ? 37  SER   C OG  1 
ATOM   1363 N  N   . ARG   B 1 32  ? 28.108 -10.949 20.648 1.00 18.46  ? 38  ARG   C N   1 
ATOM   1364 C  CA  . ARG   B 1 32  ? 28.207 -12.422 20.578 1.00 18.57  ? 38  ARG   C CA  1 
ATOM   1365 C  C   . ARG   B 1 32  ? 27.561 -13.010 19.307 1.00 18.88  ? 38  ARG   C C   1 
ATOM   1366 O  O   . ARG   B 1 32  ? 27.559 -14.240 19.120 1.00 18.16  ? 38  ARG   C O   1 
ATOM   1367 C  CB  . ARG   B 1 32  ? 27.452 -13.023 21.801 1.00 21.46  ? 38  ARG   C CB  1 
ATOM   1368 C  CG  . ARG   B 1 32  ? 28.118 -12.709 23.125 1.00 21.90  ? 38  ARG   C CG  1 
ATOM   1369 C  CD  . ARG   B 1 32  ? 27.353 -13.289 24.316 1.00 19.96  ? 38  ARG   C CD  1 
ATOM   1370 N  NE  . ARG   B 1 32  ? 27.409 -14.771 24.343 1.00 19.65  ? 38  ARG   C NE  1 
ATOM   1371 C  CZ  . ARG   B 1 32  ? 27.399 -15.499 25.461 1.00 21.43  ? 38  ARG   C CZ  1 
ATOM   1372 N  NH1 . ARG   B 1 32  ? 27.304 -14.906 26.647 1.00 20.38  ? 38  ARG   C NH1 1 
ATOM   1373 N  NH2 . ARG   B 1 32  ? 27.521 -16.827 25.402 1.00 19.28  ? 38  ARG   C NH2 1 
ATOM   1374 N  N   . ASP   B 1 33  ? 26.877 -12.170 18.516 1.00 18.62  ? 39  ASP   C N   1 
ATOM   1375 C  CA  . ASP   B 1 33  ? 26.091 -12.601 17.361 1.00 17.59  ? 39  ASP   C CA  1 
ATOM   1376 C  C   . ASP   B 1 33  ? 24.971 -13.541 17.801 1.00 17.76  ? 39  ASP   C C   1 
ATOM   1377 O  O   . ASP   B 1 33  ? 24.658 -14.478 17.053 1.00 17.13  ? 39  ASP   C O   1 
ATOM   1378 C  CB  . ASP   B 1 33  ? 26.941 -13.209 16.214 1.00 17.11  ? 39  ASP   C CB  1 
ATOM   1379 C  CG  . ASP   B 1 33  ? 26.138 -13.522 14.967 1.00 20.10  ? 39  ASP   C CG  1 
ATOM   1380 O  OD1 . ASP   B 1 33  ? 25.248 -12.725 14.618 1.00 21.43  ? 39  ASP   C OD1 1 
ATOM   1381 O  OD2 . ASP   B 1 33  ? 26.400 -14.572 14.332 1.00 18.59  ? 39  ASP   C OD2 1 
ATOM   1382 N  N   . LEU   B 1 34  ? 24.365 -13.296 18.998 1.00 17.47  ? 40  LEU   C N   1 
ATOM   1383 C  CA  . LEU   B 1 34  ? 23.268 -14.165 19.478 1.00 17.50  ? 40  LEU   C CA  1 
ATOM   1384 C  C   . LEU   B 1 34  ? 21.950 -13.435 19.712 1.00 17.74  ? 40  LEU   C C   1 
ATOM   1385 O  O   . LEU   B 1 34  ? 21.943 -12.281 20.133 1.00 18.43  ? 40  LEU   C O   1 
ATOM   1386 C  CB  . LEU   B 1 34  ? 23.624 -14.920 20.769 1.00 18.40  ? 40  LEU   C CB  1 
ATOM   1387 C  CG  . LEU   B 1 34  ? 24.713 -16.004 20.657 1.00 19.59  ? 40  LEU   C CG  1 
ATOM   1388 C  CD1 . LEU   B 1 34  ? 24.963 -16.642 22.040 1.00 19.61  ? 40  LEU   C CD1 1 
ATOM   1389 C  CD2 . LEU   B 1 34  ? 24.289 -17.136 19.673 1.00 20.44  ? 40  LEU   C CD2 1 
ATOM   1390 N  N   . LEU   B 1 35  ? 20.834 -14.137 19.470 1.00 16.90  ? 41  LEU   C N   1 
ATOM   1391 C  CA  . LEU   B 1 35  ? 19.506 -13.591 19.801 1.00 18.36  ? 41  LEU   C CA  1 
ATOM   1392 C  C   . LEU   B 1 35  ? 18.667 -14.805 20.252 1.00 18.65  ? 41  LEU   C C   1 
ATOM   1393 O  O   . LEU   B 1 35  ? 18.759 -15.876 19.640 1.00 19.78  ? 41  LEU   C O   1 
ATOM   1394 C  CB  . LEU   B 1 35  ? 18.853 -12.893 18.577 1.00 18.67  ? 41  LEU   C CB  1 
ATOM   1395 C  CG  . LEU   B 1 35  ? 17.441 -12.286 18.834 1.00 20.33  ? 41  LEU   C CG  1 
ATOM   1396 C  CD1 . LEU   B 1 35  ? 17.264 -10.961 18.084 1.00 22.08  ? 41  LEU   C CD1 1 
ATOM   1397 C  CD2 . LEU   B 1 35  ? 16.320 -13.279 18.506 1.00 20.02  ? 41  LEU   C CD2 1 
ATOM   1398 N  N   . VAL   B 1 36  ? 17.869 -14.645 21.313 1.00 18.56  ? 42  VAL   C N   1 
ATOM   1399 C  CA  . VAL   B 1 36  ? 16.984 -15.686 21.817 1.00 18.24  ? 42  VAL   C CA  1 
ATOM   1400 C  C   . VAL   B 1 36  ? 15.565 -15.131 21.806 1.00 19.90  ? 42  VAL   C C   1 
ATOM   1401 O  O   . VAL   B 1 36  ? 15.336 -14.026 22.315 1.00 20.10  ? 42  VAL   C O   1 
ATOM   1402 C  CB  . VAL   B 1 36  ? 17.390 -16.112 23.246 1.00 19.22  ? 42  VAL   C CB  1 
ATOM   1403 C  CG1 . VAL   B 1 36  ? 16.422 -17.164 23.802 1.00 19.34  ? 42  VAL   C CG1 1 
ATOM   1404 C  CG2 . VAL   B 1 36  ? 18.837 -16.654 23.248 1.00 19.74  ? 42  VAL   C CG2 1 
ATOM   1405 N  N   . SER   B 1 37  ? 14.625 -15.878 21.222 1.00 20.14  ? 43  SER   C N   1 
ATOM   1406 C  CA  . SER   B 1 37  ? 13.204 -15.499 21.212 1.00 20.44  ? 43  SER   C CA  1 
ATOM   1407 C  C   . SER   B 1 37  ? 12.378 -16.596 21.896 1.00 22.12  ? 43  SER   C C   1 
ATOM   1408 O  O   . SER   B 1 37  ? 12.862 -17.723 22.107 1.00 21.57  ? 43  SER   C O   1 
ATOM   1409 C  CB  . SER   B 1 37  ? 12.702 -15.295 19.784 1.00 22.83  ? 43  SER   C CB  1 
ATOM   1410 O  OG  . SER   B 1 37  ? 12.915 -16.454 18.992 1.00 23.72  ? 43  SER   C OG  1 
ATOM   1411 N  N   . SER   B 1 38  ? 11.134 -16.257 22.291 1.00 22.49  ? 44  SER   C N   1 
ATOM   1412 C  CA  . SER   B 1 38  ? 10.271 -17.238 22.946 1.00 23.64  ? 44  SER   C CA  1 
ATOM   1413 C  C   . SER   B 1 38  ? 9.456  -18.029 21.920 1.00 25.46  ? 44  SER   C C   1 
ATOM   1414 O  O   . SER   B 1 38  ? 9.126  -17.515 20.855 1.00 25.83  ? 44  SER   C O   1 
ATOM   1415 C  CB  . SER   B 1 38  ? 9.343  -16.539 23.937 1.00 26.47  ? 44  SER   C CB  1 
ATOM   1416 O  OG  . SER   B 1 38  ? 8.555  -15.598 23.226 1.00 30.53  ? 44  SER   C OG  1 
ATOM   1417 N  N   . THR   B 1 39  ? 9.103  -19.273 22.247 1.00 24.94  ? 45  THR   C N   1 
ATOM   1418 C  CA  . THR   B 1 39  ? 8.326  -20.124 21.344 1.00 25.57  ? 45  THR   C CA  1 
ATOM   1419 C  C   . THR   B 1 39  ? 7.044  -20.596 22.050 1.00 28.90  ? 45  THR   C C   1 
ATOM   1420 O  O   . THR   B 1 39  ? 6.996  -20.656 23.277 1.00 28.44  ? 45  THR   C O   1 
ATOM   1421 C  CB  . THR   B 1 39  ? 9.153  -21.376 20.942 1.00 25.85  ? 45  THR   C CB  1 
ATOM   1422 O  OG1 . THR   B 1 39  ? 9.439  -22.122 22.116 1.00 26.62  ? 45  THR   C OG1 1 
ATOM   1423 C  CG2 . THR   B 1 39  ? 10.487 -21.013 20.282 1.00 25.82  ? 45  THR   C CG2 1 
ATOM   1424 N  N   . THR   B 1 40  ? 6.041  -20.987 21.262 1.00 31.00  ? 46  THR   C N   1 
ATOM   1425 C  CA  . THR   B 1 40  ? 4.816  -21.539 21.838 1.00 33.78  ? 46  THR   C CA  1 
ATOM   1426 C  C   . THR   B 1 40  ? 5.032  -23.030 22.125 1.00 33.60  ? 46  THR   C C   1 
ATOM   1427 O  O   . THR   B 1 40  ? 4.665  -23.513 23.199 1.00 35.04  ? 46  THR   C O   1 
ATOM   1428 C  CB  . THR   B 1 40  ? 3.623  -21.210 20.935 1.00 38.73  ? 46  THR   C CB  1 
ATOM   1429 O  OG1 . THR   B 1 40  ? 3.826  -21.851 19.675 1.00 42.35  ? 46  THR   C OG1 1 
ATOM   1430 C  CG2 . THR   B 1 40  ? 3.498  -19.714 20.686 1.00 39.13  ? 46  THR   C CG2 1 
ATOM   1431 N  N   . ALA   B 1 41  ? 5.670  -23.758 21.195 1.00 31.85  ? 47  ALA   C N   1 
ATOM   1432 C  CA  . ALA   B 1 41  ? 5.928  -25.189 21.396 1.00 31.43  ? 47  ALA   C CA  1 
ATOM   1433 C  C   . ALA   B 1 41  ? 7.246  -25.436 22.133 1.00 30.14  ? 47  ALA   C C   1 
ATOM   1434 O  O   . ALA   B 1 41  ? 8.191  -24.649 22.006 1.00 29.76  ? 47  ALA   C O   1 
ATOM   1435 C  CB  . ALA   B 1 41  ? 5.952  -25.910 20.055 1.00 32.07  ? 47  ALA   C CB  1 
ATOM   1436 N  N   . GLN   B 1 42  ? 7.326  -26.539 22.874 1.00 29.64  ? 48  GLN   C N   1 
ATOM   1437 C  CA  . GLN   B 1 42  ? 8.548  -26.896 23.587 1.00 30.64  ? 48  GLN   C CA  1 
ATOM   1438 C  C   . GLN   B 1 42  ? 9.572  -27.511 22.626 1.00 30.14  ? 48  GLN   C C   1 
ATOM   1439 O  O   . GLN   B 1 42  ? 9.200  -28.248 21.700 1.00 30.70  ? 48  GLN   C O   1 
ATOM   1440 C  CB  . GLN   B 1 42  ? 8.246  -27.848 24.760 1.00 34.87  ? 48  GLN   C CB  1 
ATOM   1441 C  CG  . GLN   B 1 42  ? 7.760  -27.101 26.005 1.00 43.12  ? 48  GLN   C CG  1 
ATOM   1442 C  CD  . GLN   B 1 42  ? 7.539  -28.053 27.157 1.00 52.94  ? 48  GLN   C CD  1 
ATOM   1443 O  OE1 . GLN   B 1 42  ? 6.955  -29.135 27.013 1.00 55.74  ? 48  GLN   C OE1 1 
ATOM   1444 N  NE2 . GLN   B 1 42  ? 7.991  -27.677 28.342 1.00 55.92  ? 48  GLN   C NE2 1 
ATOM   1445 N  N   . GLY   B 1 43  ? 10.830 -27.133 22.835 1.00 28.08  ? 49  GLY   C N   1 
ATOM   1446 C  CA  . GLY   B 1 43  ? 11.982 -27.600 22.069 1.00 27.01  ? 49  GLY   C CA  1 
ATOM   1447 C  C   . GLY   B 1 43  ? 12.614 -28.809 22.722 1.00 26.60  ? 49  GLY   C C   1 
ATOM   1448 O  O   . GLY   B 1 43  ? 12.387 -29.059 23.910 1.00 28.20  ? 49  GLY   C O   1 
ATOM   1449 N  N   . CYS   B 1 44  ? 13.370 -29.588 21.953 1.00 25.01  ? 50  CYS   C N   1 
ATOM   1450 C  CA  . CYS   B 1 44  ? 13.940 -30.829 22.453 1.00 25.50  ? 50  CYS   C CA  1 
ATOM   1451 C  C   . CYS   B 1 44  ? 15.437 -30.854 22.574 1.00 25.00  ? 50  CYS   C C   1 
ATOM   1452 O  O   . CYS   B 1 44  ? 15.965 -31.901 22.975 1.00 26.64  ? 50  CYS   C O   1 
ATOM   1453 C  CB  . CYS   B 1 44  ? 13.459 -31.981 21.590 1.00 27.08  ? 50  CYS   C CB  1 
ATOM   1454 S  SG  . CYS   B 1 44  ? 11.663 -32.012 21.409 1.00 35.86  ? 50  CYS   C SG  1 
ATOM   1455 N  N   . ASP   B 1 45  ? 16.134 -29.784 22.194 1.00 22.84  ? 51  ASP   C N   1 
ATOM   1456 C  CA  . ASP   B 1 45  ? 17.595 -29.799 22.282 1.00 21.78  ? 51  ASP   C CA  1 
ATOM   1457 C  C   . ASP   B 1 45  ? 17.975 -29.609 23.762 1.00 22.80  ? 51  ASP   C C   1 
ATOM   1458 O  O   . ASP   B 1 45  ? 17.235 -28.982 24.544 1.00 23.80  ? 51  ASP   C O   1 
ATOM   1459 C  CB  . ASP   B 1 45  ? 18.194 -28.642 21.426 1.00 21.18  ? 51  ASP   C CB  1 
ATOM   1460 C  CG  . ASP   B 1 45  ? 18.034 -28.810 19.919 1.00 25.22  ? 51  ASP   C CG  1 
ATOM   1461 O  OD1 . ASP   B 1 45  ? 18.073 -29.963 19.433 1.00 24.99  ? 51  ASP   C OD1 1 
ATOM   1462 O  OD2 . ASP   B 1 45  ? 17.847 -27.785 19.221 1.00 23.05  ? 51  ASP   C OD2 1 
ATOM   1463 N  N   . THR   B 1 46  ? 19.118 -30.174 24.147 1.00 20.98  ? 52  THR   C N   1 
ATOM   1464 C  CA  . THR   B 1 46  ? 19.666 -30.014 25.477 1.00 21.21  ? 52  THR   C CA  1 
ATOM   1465 C  C   . THR   B 1 46  ? 20.972 -29.208 25.316 1.00 21.50  ? 52  THR   C C   1 
ATOM   1466 O  O   . THR   B 1 46  ? 21.779 -29.542 24.433 1.00 21.27  ? 52  THR   C O   1 
ATOM   1467 C  CB  . THR   B 1 46  ? 20.008 -31.374 26.079 1.00 24.13  ? 52  THR   C CB  1 
ATOM   1468 O  OG1 . THR   B 1 46  ? 18.814 -32.172 26.224 1.00 26.27  ? 52  THR   C OG1 1 
ATOM   1469 C  CG2 . THR   B 1 46  ? 20.711 -31.230 27.434 1.00 24.98  ? 52  THR   C CG2 1 
ATOM   1470 N  N   . ILE   B 1 47  ? 21.188 -28.206 26.178 1.00 20.44  ? 53  ILE   C N   1 
ATOM   1471 C  CA  . ILE   B 1 47  ? 22.423 -27.420 26.131 1.00 19.53  ? 53  ILE   C CA  1 
ATOM   1472 C  C   . ILE   B 1 47  ? 23.504 -28.128 26.966 1.00 17.70  ? 53  ILE   C C   1 
ATOM   1473 O  O   . ILE   B 1 47  ? 23.263 -28.564 28.096 1.00 18.89  ? 53  ILE   C O   1 
ATOM   1474 C  CB  . ILE   B 1 47  ? 22.224 -25.998 26.692 1.00 20.70  ? 53  ILE   C CB  1 
ATOM   1475 C  CG1 . ILE   B 1 47  ? 21.032 -25.287 26.043 1.00 21.00  ? 53  ILE   C CG1 1 
ATOM   1476 C  CG2 . ILE   B 1 47  ? 23.499 -25.172 26.563 1.00 21.65  ? 53  ILE   C CG2 1 
ATOM   1477 C  CD1 . ILE   B 1 47  ? 21.203 -25.148 24.479 1.00 23.38  ? 53  ILE   C CD1 1 
ATOM   1478 N  N   . ALA   B 1 48  ? 24.718 -28.206 26.402 1.00 16.44  ? 54  ALA   C N   1 
ATOM   1479 C  CA  . ALA   B 1 48  ? 25.826 -28.798 27.132 1.00 15.66  ? 54  ALA   C CA  1 
ATOM   1480 C  C   . ALA   B 1 48  ? 26.207 -27.895 28.296 1.00 17.14  ? 54  ALA   C C   1 
ATOM   1481 O  O   . ALA   B 1 48  ? 26.195 -26.663 28.142 1.00 18.00  ? 54  ALA   C O   1 
ATOM   1482 C  CB  . ALA   B 1 48  ? 27.025 -28.955 26.192 1.00 16.01  ? 54  ALA   C CB  1 
ATOM   1483 N  N   . ARG   B 1 49  ? 26.564 -28.480 29.453 1.00 16.99  ? 55  ARG   C N   1 
ATOM   1484 C  CA  . ARG   B 1 49  ? 27.030 -27.702 30.583 1.00 17.39  ? 55  ARG   C CA  1 
ATOM   1485 C  C   . ARG   B 1 49  ? 28.349 -28.379 30.928 1.00 17.26  ? 55  ARG   C C   1 
ATOM   1486 O  O   . ARG   B 1 49  ? 28.370 -29.399 31.643 1.00 18.49  ? 55  ARG   C O   1 
ATOM   1487 C  CB  . ARG   B 1 49  ? 26.028 -27.726 31.758 1.00 17.24  ? 55  ARG   C CB  1 
ATOM   1488 C  CG  . ARG   B 1 49  ? 24.666 -27.169 31.358 1.00 17.72  ? 55  ARG   C CG  1 
ATOM   1489 C  CD  . ARG   B 1 49  ? 24.675 -25.689 31.014 1.00 19.68  ? 55  ARG   C CD  1 
ATOM   1490 N  NE  . ARG   B 1 49  ? 23.319 -25.263 30.649 1.00 20.21  ? 55  ARG   C NE  1 
ATOM   1491 C  CZ  . ARG   B 1 49  ? 23.032 -24.158 29.969 1.00 22.79  ? 55  ARG   C CZ  1 
ATOM   1492 N  NH1 . ARG   B 1 49  ? 24.006 -23.337 29.577 1.00 20.11  ? 55  ARG   C NH1 1 
ATOM   1493 N  NH2 . ARG   B 1 49  ? 21.767 -23.862 29.672 1.00 23.21  ? 55  ARG   C NH2 1 
ATOM   1494 N  N   . CYS   B 1 50  ? 29.450 -27.844 30.360 1.00 17.32  ? 56  CYS   C N   1 
ATOM   1495 C  CA  . CYS   B 1 50  ? 30.771 -28.514 30.430 1.00 17.22  ? 56  CYS   C CA  1 
ATOM   1496 C  C   . CYS   B 1 50  ? 31.865 -27.574 29.933 1.00 17.38  ? 56  CYS   C C   1 
ATOM   1497 O  O   . CYS   B 1 50  ? 31.573 -26.461 29.501 1.00 17.53  ? 56  CYS   C O   1 
ATOM   1498 C  CB  . CYS   B 1 50  ? 30.706 -29.723 29.502 1.00 18.82  ? 56  CYS   C CB  1 
ATOM   1499 S  SG  . CYS   B 1 50  ? 30.546 -29.246 27.748 1.00 18.23  ? 56  CYS   C SG  1 
ATOM   1500 N  N   . ASP   B 1 51  ? 33.138 -28.057 29.933 1.00 18.29  ? 57  ASP   C N   1 
ATOM   1501 C  CA  . ASP   B 1 51  ? 34.223 -27.293 29.341 1.00 18.95  ? 57  ASP   C CA  1 
ATOM   1502 C  C   . ASP   B 1 51  ? 34.910 -28.142 28.246 1.00 19.67  ? 57  ASP   C C   1 
ATOM   1503 O  O   . ASP   B 1 51  ? 36.118 -28.031 28.040 1.00 20.81  ? 57  ASP   C O   1 
ATOM   1504 C  CB  . ASP   B 1 51  ? 35.235 -26.867 30.399 1.00 21.64  ? 57  ASP   C CB  1 
ATOM   1505 C  CG  . ASP   B 1 51  ? 35.895 -27.991 31.154 1.00 26.05  ? 57  ASP   C CG  1 
ATOM   1506 O  OD1 . ASP   B 1 51  ? 35.585 -29.166 30.876 1.00 24.57  ? 57  ASP   C OD1 1 
ATOM   1507 O  OD2 . ASP   B 1 51  ? 36.756 -27.698 32.009 1.00 33.32  ? 57  ASP   C OD2 1 
ATOM   1508 N  N   . CYS   B 1 52  ? 34.121 -28.972 27.509 1.00 18.43  ? 58  CYS   C N   1 
ATOM   1509 C  CA  . CYS   B 1 52  ? 34.654 -29.791 26.389 1.00 16.39  ? 58  CYS   C CA  1 
ATOM   1510 C  C   . CYS   B 1 52  ? 35.338 -28.895 25.381 1.00 17.08  ? 58  CYS   C C   1 
ATOM   1511 O  O   . CYS   B 1 52  ? 34.888 -27.756 25.140 1.00 17.84  ? 58  CYS   C O   1 
ATOM   1512 C  CB  . CYS   B 1 52  ? 33.521 -30.556 25.700 1.00 16.35  ? 58  CYS   C CB  1 
ATOM   1513 S  SG  . CYS   B 1 52  ? 32.967 -32.028 26.595 1.00 18.93  ? 58  CYS   C SG  1 
ATOM   1514 N  N   . GLN   B 1 53  ? 36.362 -29.434 24.742 1.00 16.60  ? 59  GLN   C N   1 
ATOM   1515 C  CA  . GLN   B 1 53  ? 37.038 -28.796 23.607 1.00 17.50  ? 59  GLN   C CA  1 
ATOM   1516 C  C   . GLN   B 1 53  ? 37.090 -29.746 22.392 1.00 17.28  ? 59  GLN   C C   1 
ATOM   1517 O  O   . GLN   B 1 53  ? 37.868 -29.527 21.453 1.00 17.36  ? 59  GLN   C O   1 
ATOM   1518 C  CB  . GLN   B 1 53  ? 38.463 -28.369 23.950 1.00 16.83  ? 59  GLN   C CB  1 
ATOM   1519 C  CG  . GLN   B 1 53  ? 38.481 -27.105 24.815 1.00 19.16  ? 59  GLN   C CG  1 
ATOM   1520 C  CD  . GLN   B 1 53  ? 39.905 -26.634 25.025 1.00 23.84  ? 59  GLN   C CD  1 
ATOM   1521 O  OE1 . GLN   B 1 53  ? 40.462 -26.762 26.148 1.00 25.92  ? 59  GLN   C OE1 1 
ATOM   1522 N  NE2 . GLN   B 1 53  ? 40.541 -26.063 23.998 1.00 20.67  ? 59  GLN   C NE2 1 
ATOM   1523 N  N   . THR   B 1 54  ? 36.259 -30.815 22.396 1.00 16.81  ? 60  THR   C N   1 
ATOM   1524 C  CA  . THR   B 1 54  ? 36.129 -31.705 21.236 1.00 18.84  ? 60  THR   C CA  1 
ATOM   1525 C  C   . THR   B 1 54  ? 34.652 -31.938 21.017 1.00 19.01  ? 60  THR   C C   1 
ATOM   1526 O  O   . THR   B 1 54  ? 33.872 -32.041 21.982 1.00 19.57  ? 60  THR   C O   1 
ATOM   1527 C  CB  . THR   B 1 54  ? 36.920 -32.997 21.359 1.00 22.44  ? 60  THR   C CB  1 
ATOM   1528 O  OG1 . THR   B 1 54  ? 36.388 -33.741 22.420 1.00 24.45  ? 60  THR   C OG1 1 
ATOM   1529 C  CG2 . THR   B 1 54  ? 38.399 -32.746 21.675 1.00 22.47  ? 60  THR   C CG2 1 
ATOM   1530 N  N   . GLY   B 1 55  ? 34.263 -31.993 19.748 1.00 17.30  ? 61  GLY   C N   1 
ATOM   1531 C  CA  . GLY   B 1 55  ? 32.855 -32.175 19.414 1.00 16.85  ? 61  GLY   C CA  1 
ATOM   1532 C  C   . GLY   B 1 55  ? 32.672 -32.440 17.940 1.00 17.35  ? 61  GLY   C C   1 
ATOM   1533 O  O   . GLY   B 1 55  ? 33.639 -32.781 17.234 1.00 17.73  ? 61  GLY   C O   1 
ATOM   1534 N  N   . VAL   B 1 56  ? 31.434 -32.293 17.472 1.00 17.55  ? 62  VAL   C N   1 
ATOM   1535 C  CA  . VAL   B 1 56  ? 31.115 -32.501 16.048 1.00 17.14  ? 62  VAL   C CA  1 
ATOM   1536 C  C   . VAL   B 1 56  ? 30.205 -31.347 15.620 1.00 16.74  ? 62  VAL   C C   1 
ATOM   1537 O  O   . VAL   B 1 56  ? 29.277 -31.000 16.375 1.00 16.81  ? 62  VAL   C O   1 
ATOM   1538 C  CB  . VAL   B 1 56  ? 30.364 -33.843 15.874 1.00 17.69  ? 62  VAL   C CB  1 
ATOM   1539 C  CG1 . VAL   B 1 56  ? 29.824 -33.994 14.441 1.00 18.79  ? 62  VAL   C CG1 1 
ATOM   1540 C  CG2 . VAL   B 1 56  ? 31.284 -35.023 16.253 1.00 18.19  ? 62  VAL   C CG2 1 
ATOM   1541 N  N   . TYR   B 1 57  ? 30.455 -30.753 14.430 1.00 16.03  ? 63  TYR   C N   1 
ATOM   1542 C  CA  . TYR   B 1 57  ? 29.583 -29.654 13.977 1.00 15.10  ? 63  TYR   C CA  1 
ATOM   1543 C  C   . TYR   B 1 57  ? 29.001 -29.974 12.597 1.00 16.46  ? 63  TYR   C C   1 
ATOM   1544 O  O   . TYR   B 1 57  ? 29.649 -30.684 11.830 1.00 16.54  ? 63  TYR   C O   1 
ATOM   1545 C  CB  . TYR   B 1 57  ? 30.300 -28.256 13.952 1.00 15.50  ? 63  TYR   C CB  1 
ATOM   1546 C  CG  . TYR   B 1 57  ? 31.175 -27.974 12.739 1.00 16.36  ? 63  TYR   C CG  1 
ATOM   1547 C  CD1 . TYR   B 1 57  ? 32.452 -28.494 12.647 1.00 17.20  ? 63  TYR   C CD1 1 
ATOM   1548 C  CD2 . TYR   B 1 57  ? 30.749 -27.100 11.734 1.00 16.72  ? 63  TYR   C CD2 1 
ATOM   1549 C  CE1 . TYR   B 1 57  ? 33.277 -28.217 11.544 1.00 18.45  ? 63  TYR   C CE1 1 
ATOM   1550 C  CE2 . TYR   B 1 57  ? 31.564 -26.808 10.635 1.00 17.58  ? 63  TYR   C CE2 1 
ATOM   1551 C  CZ  . TYR   B 1 57  ? 32.833 -27.369 10.544 1.00 18.84  ? 63  TYR   C CZ  1 
ATOM   1552 O  OH  . TYR   B 1 57  ? 33.671 -27.050 9.476  1.00 20.81  ? 63  TYR   C OH  1 
ATOM   1553 N  N   . TYR   B 1 58  ? 27.829 -29.402 12.297 1.00 17.07  ? 64  TYR   C N   1 
ATOM   1554 C  CA  . TYR   B 1 58  ? 27.202 -29.597 10.999 1.00 18.21  ? 64  TYR   C CA  1 
ATOM   1555 C  C   . TYR   B 1 58  ? 27.600 -28.441 10.065 1.00 17.26  ? 64  TYR   C C   1 
ATOM   1556 O  O   . TYR   B 1 58  ? 27.401 -27.248 10.408 1.00 16.87  ? 64  TYR   C O   1 
ATOM   1557 C  CB  . TYR   B 1 58  ? 25.680 -29.682 11.066 1.00 18.92  ? 64  TYR   C CB  1 
ATOM   1558 C  CG  . TYR   B 1 58  ? 25.096 -29.954 9.680  1.00 19.78  ? 64  TYR   C CG  1 
ATOM   1559 C  CD1 . TYR   B 1 58  ? 25.414 -31.120 8.978  1.00 20.16  ? 64  TYR   C CD1 1 
ATOM   1560 C  CD2 . TYR   B 1 58  ? 24.247 -29.047 9.070  1.00 19.59  ? 64  TYR   C CD2 1 
ATOM   1561 C  CE1 . TYR   B 1 58  ? 24.924 -31.353 7.691  1.00 21.02  ? 64  TYR   C CE1 1 
ATOM   1562 C  CE2 . TYR   B 1 58  ? 23.743 -29.283 7.790  1.00 21.00  ? 64  TYR   C CE2 1 
ATOM   1563 C  CZ  . TYR   B 1 58  ? 24.065 -30.449 7.123  1.00 22.21  ? 64  TYR   C CZ  1 
ATOM   1564 O  OH  . TYR   B 1 58  ? 23.601 -30.679 5.849  1.00 25.45  ? 64  TYR   C OH  1 
ATOM   1565 N  N   . CYS   B 1 59  ? 28.122 -28.822 8.856  1.00 16.97  ? 65  CYS   C N   1 
ATOM   1566 C  CA  . CYS   B 1 59  ? 28.560 -27.857 7.829  1.00 17.68  ? 65  CYS   C CA  1 
ATOM   1567 C  C   . CYS   B 1 59  ? 27.620 -28.023 6.629  1.00 19.11  ? 65  CYS   C C   1 
ATOM   1568 O  O   . CYS   B 1 59  ? 27.773 -28.981 5.880  1.00 20.30  ? 65  CYS   C O   1 
ATOM   1569 C  CB  . CYS   B 1 59  ? 30.004 -28.151 7.443  1.00 18.29  ? 65  CYS   C CB  1 
ATOM   1570 S  SG  . CYS   B 1 59  ? 30.610 -27.120 6.072  1.00 19.94  ? 65  CYS   C SG  1 
ATOM   1571 N  N   . SER   B 1 60  ? 26.653 -27.096 6.466  1.00 19.30  ? 66  SER   C N   1 
ATOM   1572 C  CA  A SER   B 1 60  ? 25.677 -27.247 5.392  0.50 20.48  ? 66  SER   C CA  1 
ATOM   1573 C  CA  B SER   B 1 60  ? 25.682 -27.238 5.393  0.50 19.91  ? 66  SER   C CA  1 
ATOM   1574 C  C   . SER   B 1 60  ? 26.296 -27.169 3.994  1.00 20.99  ? 66  SER   C C   1 
ATOM   1575 O  O   . SER   B 1 60  ? 25.841 -27.870 3.098  1.00 22.62  ? 66  SER   C O   1 
ATOM   1576 C  CB  A SER   B 1 60  ? 24.545 -26.244 5.541  0.50 23.21  ? 66  SER   C CB  1 
ATOM   1577 C  CB  B SER   B 1 60  ? 24.597 -26.189 5.518  0.50 21.01  ? 66  SER   C CB  1 
ATOM   1578 O  OG  A SER   B 1 60  ? 25.035 -24.920 5.654  0.50 26.22  ? 66  SER   C OG  1 
ATOM   1579 O  OG  B SER   B 1 60  ? 23.625 -26.480 4.531  0.50 21.24  ? 66  SER   C OG  1 
ATOM   1580 N  N   . SER   B 1 61  ? 27.334 -26.347 3.820  1.00 20.12  ? 67  SER   C N   1 
ATOM   1581 C  CA  . SER   B 1 61  ? 27.985 -26.216 2.503  1.00 20.46  ? 67  SER   C CA  1 
ATOM   1582 C  C   . SER   B 1 61  ? 28.765 -27.468 2.064  1.00 21.71  ? 67  SER   C C   1 
ATOM   1583 O  O   . SER   B 1 61  ? 29.232 -27.532 0.915  1.00 22.77  ? 67  SER   C O   1 
ATOM   1584 C  CB  . SER   B 1 61  ? 28.883 -24.985 2.471  1.00 21.60  ? 67  SER   C CB  1 
ATOM   1585 O  OG  . SER   B 1 61  ? 29.946 -25.077 3.404  1.00 23.37  ? 67  SER   C OG  1 
ATOM   1586 N  N   . ARG   B 1 62  ? 28.912 -28.467 2.953  1.00 21.06  ? 68  ARG   C N   1 
ATOM   1587 C  CA  . ARG   B 1 62  ? 29.531 -29.739 2.588  1.00 21.03  ? 68  ARG   C CA  1 
ATOM   1588 C  C   . ARG   B 1 62  ? 28.596 -30.936 2.852  1.00 22.50  ? 68  ARG   C C   1 
ATOM   1589 O  O   . ARG   B 1 62  ? 29.031 -32.077 2.647  1.00 23.29  ? 68  ARG   C O   1 
ATOM   1590 C  CB  . ARG   B 1 62  ? 30.806 -29.966 3.378  1.00 22.95  ? 68  ARG   C CB  1 
ATOM   1591 C  CG  . ARG   B 1 62  ? 31.897 -28.918 3.104  1.00 27.22  ? 68  ARG   C CG  1 
ATOM   1592 C  CD  . ARG   B 1 62  ? 32.598 -29.176 1.803  1.00 28.00  ? 68  ARG   C CD  1 
ATOM   1593 N  NE  . ARG   B 1 62  ? 33.625 -28.150 1.548  1.00 30.89  ? 68  ARG   C NE  1 
ATOM   1594 C  CZ  . ARG   B 1 62  ? 33.419 -27.027 0.866  1.00 35.69  ? 68  ARG   C CZ  1 
ATOM   1595 N  NH1 . ARG   B 1 62  ? 32.222 -26.764 0.351  1.00 38.05  ? 68  ARG   C NH1 1 
ATOM   1596 N  NH2 . ARG   B 1 62  ? 34.422 -26.179 0.648  1.00 35.70  ? 68  ARG   C NH2 1 
ATOM   1597 N  N   . ARG   B 1 63  ? 27.382 -30.696 3.410  1.00 23.15  ? 69  ARG   C N   1 
ATOM   1598 C  CA  . ARG   B 1 63  ? 26.404 -31.732 3.826  1.00 24.92  ? 69  ARG   C CA  1 
ATOM   1599 C  C   . ARG   B 1 63  ? 27.102 -32.769 4.694  1.00 25.56  ? 69  ARG   C C   1 
ATOM   1600 O  O   . ARG   B 1 63  ? 26.974 -33.978 4.470  1.00 26.89  ? 69  ARG   C O   1 
ATOM   1601 C  CB  . ARG   B 1 63  ? 25.787 -32.415 2.589  1.00 27.13  ? 69  ARG   C CB  1 
ATOM   1602 C  CG  . ARG   B 1 63  ? 24.940 -31.561 1.732  1.00 31.47  ? 69  ARG   C CG  1 
ATOM   1603 C  CD  . ARG   B 1 63  ? 23.615 -31.270 2.368  1.00 37.04  ? 69  ARG   C CD  1 
ATOM   1604 N  NE  . ARG   B 1 63  ? 22.634 -30.886 1.362  1.00 39.00  ? 69  ARG   C NE  1 
ATOM   1605 C  CZ  . ARG   B 1 63  ? 22.453 -29.644 0.927  1.00 39.83  ? 69  ARG   C CZ  1 
ATOM   1606 N  NH1 . ARG   B 1 63  ? 23.193 -28.644 1.411  1.00 37.39  ? 69  ARG   C NH1 1 
ATOM   1607 N  NH2 . ARG   B 1 63  ? 21.521 -29.384 0.024  1.00 37.04  ? 69  ARG   C NH2 1 
ATOM   1608 N  N   . LYS   B 1 64  ? 27.917 -32.287 5.627  1.00 23.73  ? 70  LYS   C N   1 
ATOM   1609 C  CA  . LYS   B 1 64  ? 28.734 -33.176 6.420  1.00 23.28  ? 70  LYS   C CA  1 
ATOM   1610 C  C   . LYS   B 1 64  ? 28.834 -32.734 7.849  1.00 21.72  ? 70  LYS   C C   1 
ATOM   1611 O  O   . LYS   B 1 64  ? 28.865 -31.538 8.112  1.00 20.94  ? 70  LYS   C O   1 
ATOM   1612 C  CB  . LYS   B 1 64  ? 30.155 -33.224 5.840  1.00 26.88  ? 70  LYS   C CB  1 
ATOM   1613 C  CG  . LYS   B 1 64  ? 30.310 -34.311 4.793  1.00 37.00  ? 70  LYS   C CG  1 
ATOM   1614 C  CD  . LYS   B 1 64  ? 31.741 -34.803 4.691  1.00 44.58  ? 70  LYS   C CD  1 
ATOM   1615 C  CE  . LYS   B 1 64  ? 31.935 -35.502 3.366  1.00 50.70  ? 70  LYS   C CE  1 
ATOM   1616 N  NZ  . LYS   B 1 64  ? 31.371 -34.689 2.253  1.00 55.48  ? 70  LYS   C NZ  1 
ATOM   1617 N  N   . HIS   B 1 65  ? 28.945 -33.714 8.764  1.00 20.40  ? 71  HIS   C N   1 
ATOM   1618 C  CA  . HIS   B 1 65  ? 29.218 -33.419 10.163 1.00 20.63  ? 71  HIS   C CA  1 
ATOM   1619 C  C   . HIS   B 1 65  ? 30.711 -33.690 10.324 1.00 20.84  ? 71  HIS   C C   1 
ATOM   1620 O  O   . HIS   B 1 65  ? 31.191 -34.766 9.906  1.00 23.53  ? 71  HIS   C O   1 
ATOM   1621 C  CB  . HIS   B 1 65  ? 28.405 -34.365 11.085 1.00 19.49  ? 71  HIS   C CB  1 
ATOM   1622 C  CG  . HIS   B 1 65  ? 26.930 -34.109 11.038 1.00 19.28  ? 71  HIS   C CG  1 
ATOM   1623 N  ND1 . HIS   B 1 65  ? 26.277 -33.376 12.030 1.00 21.30  ? 71  HIS   C ND1 1 
ATOM   1624 C  CD2 . HIS   B 1 65  ? 26.014 -34.530 10.140 1.00 20.84  ? 71  HIS   C CD2 1 
ATOM   1625 C  CE1 . HIS   B 1 65  ? 24.995 -33.383 11.703 1.00 20.87  ? 71  HIS   C CE1 1 
ATOM   1626 N  NE2 . HIS   B 1 65  ? 24.785 -34.039 10.568 1.00 21.92  ? 71  HIS   C NE2 1 
ATOM   1627 N  N   . TYR   B 1 66  ? 31.463 -32.755 10.943 1.00 18.47  ? 72  TYR   C N   1 
ATOM   1628 C  CA  . TYR   B 1 66  ? 32.897 -32.958 11.094 1.00 18.53  ? 72  TYR   C CA  1 
ATOM   1629 C  C   . TYR   B 1 66  ? 33.275 -33.003 12.554 1.00 18.00  ? 72  TYR   C C   1 
ATOM   1630 O  O   . TYR   B 1 66  ? 32.873 -32.087 13.293 1.00 18.14  ? 72  TYR   C O   1 
ATOM   1631 C  CB  . TYR   B 1 66  ? 33.636 -31.732 10.490 1.00 19.48  ? 72  TYR   C CB  1 
ATOM   1632 C  CG  . TYR   B 1 66  ? 33.599 -31.648 8.978  1.00 21.59  ? 72  TYR   C CG  1 
ATOM   1633 C  CD1 . TYR   B 1 66  ? 34.402 -32.461 8.201  1.00 23.93  ? 72  TYR   C CD1 1 
ATOM   1634 C  CD2 . TYR   B 1 66  ? 32.788 -30.724 8.334  1.00 23.22  ? 72  TYR   C CD2 1 
ATOM   1635 C  CE1 . TYR   B 1 66  ? 34.419 -32.338 6.811  1.00 24.75  ? 72  TYR   C CE1 1 
ATOM   1636 C  CE2 . TYR   B 1 66  ? 32.771 -30.612 6.950  1.00 24.65  ? 72  TYR   C CE2 1 
ATOM   1637 C  CZ  . TYR   B 1 66  ? 33.587 -31.422 6.190  1.00 26.00  ? 72  TYR   C CZ  1 
ATOM   1638 O  OH  . TYR   B 1 66  ? 33.573 -31.252 4.817  1.00 27.50  ? 72  TYR   C OH  1 
ATOM   1639 N  N   . PRO   B 1 67  ? 34.093 -33.994 12.956 1.00 17.84  ? 73  PRO   C N   1 
ATOM   1640 C  CA  . PRO   B 1 67  ? 34.638 -33.961 14.325 1.00 18.29  ? 73  PRO   C CA  1 
ATOM   1641 C  C   . PRO   B 1 67  ? 35.740 -32.879 14.385 1.00 19.78  ? 73  PRO   C C   1 
ATOM   1642 O  O   . PRO   B 1 67  ? 36.536 -32.743 13.416 1.00 20.62  ? 73  PRO   C O   1 
ATOM   1643 C  CB  . PRO   B 1 67  ? 35.240 -35.374 14.518 1.00 20.10  ? 73  PRO   C CB  1 
ATOM   1644 C  CG  . PRO   B 1 67  ? 35.474 -35.887 13.124 1.00 21.44  ? 73  PRO   C CG  1 
ATOM   1645 C  CD  . PRO   B 1 67  ? 34.605 -35.139 12.153 1.00 18.66  ? 73  PRO   C CD  1 
ATOM   1646 N  N   . VAL   B 1 68  ? 35.730 -32.063 15.428 1.00 18.23  ? 74  VAL   C N   1 
ATOM   1647 C  CA  . VAL   B 1 68  ? 36.699 -30.981 15.555 1.00 18.83  ? 74  VAL   C CA  1 
ATOM   1648 C  C   . VAL   B 1 68  ? 37.132 -30.815 17.002 1.00 18.13  ? 74  VAL   C C   1 
ATOM   1649 O  O   . VAL   B 1 68  ? 36.391 -31.133 17.933 1.00 18.33  ? 74  VAL   C O   1 
ATOM   1650 C  CB  . VAL   B 1 68  ? 36.083 -29.598 15.111 1.00 19.92  ? 74  VAL   C CB  1 
ATOM   1651 C  CG1 . VAL   B 1 68  ? 36.012 -29.443 13.580 1.00 22.52  ? 74  VAL   C CG1 1 
ATOM   1652 C  CG2 . VAL   B 1 68  ? 34.741 -29.314 15.784 1.00 19.46  ? 74  VAL   C CG2 1 
ATOM   1653 N  N   . SER   B 1 69  ? 38.344 -30.266 17.176 1.00 17.49  ? 75  SER   C N   1 
ATOM   1654 C  CA  . SER   B 1 69  ? 38.830 -29.709 18.424 1.00 17.06  ? 75  SER   C CA  1 
ATOM   1655 C  C   . SER   B 1 69  ? 38.577 -28.177 18.300 1.00 15.87  ? 75  SER   C C   1 
ATOM   1656 O  O   . SER   B 1 69  ? 38.754 -27.582 17.229 1.00 16.50  ? 75  SER   C O   1 
ATOM   1657 C  CB  . SER   B 1 69  ? 40.339 -29.915 18.528 1.00 20.08  ? 75  SER   C CB  1 
ATOM   1658 O  OG  . SER   B 1 69  ? 40.586 -31.299 18.688 1.00 25.45  ? 75  SER   C OG  1 
ATOM   1659 N  N   . PHE   B 1 70  ? 38.128 -27.548 19.388 1.00 16.01  ? 76  PHE   C N   1 
ATOM   1660 C  CA  . PHE   B 1 70  ? 37.841 -26.108 19.363 1.00 15.92  ? 76  PHE   C CA  1 
ATOM   1661 C  C   . PHE   B 1 70  ? 38.387 -25.388 20.597 1.00 16.80  ? 76  PHE   C C   1 
ATOM   1662 O  O   . PHE   B 1 70  ? 38.565 -26.005 21.665 1.00 17.14  ? 76  PHE   C O   1 
ATOM   1663 C  CB  . PHE   B 1 70  ? 36.334 -25.814 19.139 1.00 16.30  ? 76  PHE   C CB  1 
ATOM   1664 C  CG  . PHE   B 1 70  ? 35.431 -26.540 20.132 1.00 15.87  ? 76  PHE   C CG  1 
ATOM   1665 C  CD1 . PHE   B 1 70  ? 34.987 -27.834 19.880 1.00 15.52  ? 76  PHE   C CD1 1 
ATOM   1666 C  CD2 . PHE   B 1 70  ? 34.976 -25.899 21.267 1.00 15.80  ? 76  PHE   C CD2 1 
ATOM   1667 C  CE1 . PHE   B 1 70  ? 34.171 -28.482 20.786 1.00 16.58  ? 76  PHE   C CE1 1 
ATOM   1668 C  CE2 . PHE   B 1 70  ? 34.162 -26.553 22.170 1.00 16.24  ? 76  PHE   C CE2 1 
ATOM   1669 C  CZ  . PHE   B 1 70  ? 33.762 -27.831 21.930 1.00 16.18  ? 76  PHE   C CZ  1 
ATOM   1670 N  N   . SER   B 1 71  ? 38.626 -24.084 20.461 1.00 16.12  ? 77  SER   C N   1 
ATOM   1671 C  CA  . SER   B 1 71  ? 39.240 -23.306 21.546 1.00 17.10  ? 77  SER   C CA  1 
ATOM   1672 C  C   . SER   B 1 71  ? 38.246 -22.932 22.659 1.00 18.77  ? 77  SER   C C   1 
ATOM   1673 O  O   . SER   B 1 71  ? 37.057 -23.239 22.563 1.00 18.52  ? 77  SER   C O   1 
ATOM   1674 C  CB  . SER   B 1 71  ? 39.949 -22.080 20.984 1.00 18.16  ? 77  SER   C CB  1 
ATOM   1675 O  OG  . SER   B 1 71  ? 39.025 -21.203 20.360 1.00 19.90  ? 77  SER   C OG  1 
ATOM   1676 N  N   . LYS   B 1 72  ? 38.751 -22.295 23.739 1.00 18.23  ? 78  LYS   C N   1 
ATOM   1677 C  CA  . LYS   B 1 72  ? 37.885 -21.887 24.861 1.00 18.12  ? 78  LYS   C CA  1 
ATOM   1678 C  C   . LYS   B 1 72  ? 37.203 -20.559 24.454 1.00 18.16  ? 78  LYS   C C   1 
ATOM   1679 O  O   . LYS   B 1 72  ? 37.793 -19.735 23.732 1.00 18.76  ? 78  LYS   C O   1 
ATOM   1680 C  CB  . LYS   B 1 72  ? 38.742 -21.679 26.127 1.00 22.58  ? 78  LYS   C CB  1 
ATOM   1681 C  CG  . LYS   B 1 72  ? 39.424 -22.956 26.605 1.00 28.21  ? 78  LYS   C CG  1 
ATOM   1682 C  CD  . LYS   B 1 72  ? 39.756 -22.919 28.098 1.00 37.89  ? 78  LYS   C CD  1 
ATOM   1683 C  CE  . LYS   B 1 72  ? 40.357 -24.237 28.534 1.00 46.47  ? 78  LYS   C CE  1 
ATOM   1684 N  NZ  . LYS   B 1 72  ? 39.735 -24.757 29.804 1.00 51.31  ? 78  LYS   C NZ  1 
ATOM   1685 N  N   . PRO   B 1 73  ? 35.978 -20.308 24.934 1.00 17.96  ? 79  PRO   C N   1 
ATOM   1686 C  CA  . PRO   B 1 73  ? 35.264 -19.069 24.532 1.00 18.58  ? 79  PRO   C CA  1 
ATOM   1687 C  C   . PRO   B 1 73  ? 36.058 -17.818 24.882 1.00 20.10  ? 79  PRO   C C   1 
ATOM   1688 O  O   . PRO   B 1 73  ? 36.572 -17.711 26.004 1.00 21.30  ? 79  PRO   C O   1 
ATOM   1689 C  CB  . PRO   B 1 73  ? 33.969 -19.086 25.356 1.00 20.26  ? 79  PRO   C CB  1 
ATOM   1690 C  CG  . PRO   B 1 73  ? 33.830 -20.504 25.843 1.00 20.61  ? 79  PRO   C CG  1 
ATOM   1691 C  CD  . PRO   B 1 73  ? 35.174 -21.189 25.817 1.00 18.00  ? 79  PRO   C CD  1 
ATOM   1692 N  N   . SER   B 1 74  ? 36.269 -16.929 23.901 1.00 18.96  ? 80  SER   C N   1 
ATOM   1693 C  CA  . SER   B 1 74  ? 37.145 -15.763 24.121 1.00 20.52  ? 80  SER   C CA  1 
ATOM   1694 C  C   . SER   B 1 74  ? 36.726 -14.550 23.247 1.00 20.44  ? 80  SER   C C   1 
ATOM   1695 O  O   . SER   B 1 74  ? 35.834 -14.669 22.408 1.00 19.13  ? 80  SER   C O   1 
ATOM   1696 C  CB  . SER   B 1 74  ? 38.592 -16.118 23.740 1.00 25.33  ? 80  SER   C CB  1 
ATOM   1697 O  OG  . SER   B 1 74  ? 38.942 -17.479 23.925 1.00 33.77  ? 80  SER   C OG  1 
ATOM   1698 N  N   . LEU   B 1 75  ? 37.396 -13.389 23.449 1.00 21.06  ? 81  LEU   C N   1 
ATOM   1699 C  CA  . LEU   B 1 75  ? 37.184 -12.173 22.653 1.00 22.57  ? 81  LEU   C CA  1 
ATOM   1700 C  C   . LEU   B 1 75  ? 38.203 -12.213 21.523 1.00 23.96  ? 81  LEU   C C   1 
ATOM   1701 O  O   . LEU   B 1 75  ? 39.416 -12.175 21.800 1.00 25.08  ? 81  LEU   C O   1 
ATOM   1702 C  CB  . LEU   B 1 75  ? 37.472 -10.930 23.526 1.00 24.06  ? 81  LEU   C CB  1 
ATOM   1703 C  CG  . LEU   B 1 75  ? 37.179 -9.558  22.883 1.00 26.21  ? 81  LEU   C CG  1 
ATOM   1704 C  CD1 . LEU   B 1 75  ? 35.698 -9.388  22.622 1.00 26.06  ? 81  LEU   C CD1 1 
ATOM   1705 C  CD2 . LEU   B 1 75  ? 37.660 -8.410  23.813 1.00 27.90  ? 81  LEU   C CD2 1 
ATOM   1706 N  N   . ILE   B 1 76  ? 37.745 -12.414 20.296 1.00 23.63  ? 82  ILE   C N   1 
ATOM   1707 C  CA  . ILE   B 1 76  ? 38.620 -12.624 19.139 1.00 25.39  ? 82  ILE   C CA  1 
ATOM   1708 C  C   . ILE   B 1 76  ? 38.331 -11.552 18.096 1.00 25.13  ? 82  ILE   C C   1 
ATOM   1709 O  O   . ILE   B 1 76  ? 37.160 -11.262 17.841 1.00 23.55  ? 82  ILE   C O   1 
ATOM   1710 C  CB  . ILE   B 1 76  ? 38.336 -14.049 18.550 1.00 27.99  ? 82  ILE   C CB  1 
ATOM   1711 C  CG1 . ILE   B 1 76  ? 38.674 -15.208 19.533 1.00 30.86  ? 82  ILE   C CG1 1 
ATOM   1712 C  CG2 . ILE   B 1 76  ? 39.026 -14.278 17.195 1.00 30.18  ? 82  ILE   C CG2 1 
ATOM   1713 C  CD1 . ILE   B 1 76  ? 40.149 -15.360 19.834 1.00 33.34  ? 82  ILE   C CD1 1 
ATOM   1714 N  N   . PHE   B 1 77  ? 39.384 -11.011 17.436 1.00 24.97  ? 83  PHE   C N   1 
ATOM   1715 C  CA  . PHE   B 1 77  ? 39.164 -10.093 16.332 1.00 26.17  ? 83  PHE   C CA  1 
ATOM   1716 C  C   . PHE   B 1 77  ? 38.747 -10.958 15.098 1.00 25.93  ? 83  PHE   C C   1 
ATOM   1717 O  O   . PHE   B 1 77  ? 39.427 -11.930 14.730 1.00 27.89  ? 83  PHE   C O   1 
ATOM   1718 C  CB  . PHE   B 1 77  ? 40.439 -9.303  16.015 1.00 27.07  ? 83  PHE   C CB  1 
ATOM   1719 C  CG  . PHE   B 1 77  ? 40.160 -8.198  15.018 1.00 27.82  ? 83  PHE   C CG  1 
ATOM   1720 C  CD1 . PHE   B 1 77  ? 39.472 -7.062  15.397 1.00 28.69  ? 83  PHE   C CD1 1 
ATOM   1721 C  CD2 . PHE   B 1 77  ? 40.560 -8.316  13.691 1.00 29.41  ? 83  PHE   C CD2 1 
ATOM   1722 C  CE1 . PHE   B 1 77  ? 39.200 -6.053  14.474 1.00 29.74  ? 83  PHE   C CE1 1 
ATOM   1723 C  CE2 . PHE   B 1 77  ? 40.282 -7.307  12.771 1.00 29.60  ? 83  PHE   C CE2 1 
ATOM   1724 C  CZ  . PHE   B 1 77  ? 39.615 -6.184  13.172 1.00 29.88  ? 83  PHE   C CZ  1 
ATOM   1725 N  N   . VAL   B 1 78  ? 37.614 -10.609 14.469 1.00 22.65  ? 84  VAL   C N   1 
ATOM   1726 C  CA  . VAL   B 1 78  ? 37.106 -11.345 13.315 1.00 22.18  ? 84  VAL   C CA  1 
ATOM   1727 C  C   . VAL   B 1 78  ? 37.193 -10.430 12.085 1.00 21.74  ? 84  VAL   C C   1 
ATOM   1728 O  O   . VAL   B 1 78  ? 36.713 -9.293  12.178 1.00 22.38  ? 84  VAL   C O   1 
ATOM   1729 C  CB  . VAL   B 1 78  ? 35.617 -11.731 13.581 1.00 23.21  ? 84  VAL   C CB  1 
ATOM   1730 C  CG1 . VAL   B 1 78  ? 35.036 -12.473 12.381 1.00 23.90  ? 84  VAL   C CG1 1 
ATOM   1731 C  CG2 . VAL   B 1 78  ? 35.477 -12.574 14.856 1.00 23.50  ? 84  VAL   C CG2 1 
ATOM   1732 N  N   . GLU   B 1 79  ? 37.715 -10.914 10.930 1.00 20.50  ? 85  GLU   C N   1 
ATOM   1733 C  CA  . GLU   B 1 79  ? 37.742 -10.100 9.706  1.00 21.39  ? 85  GLU   C CA  1 
ATOM   1734 C  C   . GLU   B 1 79  ? 36.330 -9.831  9.175  1.00 20.63  ? 85  GLU   C C   1 
ATOM   1735 O  O   . GLU   B 1 79  ? 35.350 -10.508 9.557  1.00 20.10  ? 85  GLU   C O   1 
ATOM   1736 C  CB  . GLU   B 1 79  ? 38.578 -10.778 8.592  1.00 24.79  ? 85  GLU   C CB  1 
ATOM   1737 C  CG  . GLU   B 1 79  ? 40.072 -10.799 8.881  1.00 30.12  ? 85  GLU   C CG  1 
ATOM   1738 C  CD  . GLU   B 1 79  ? 40.698 -9.445  9.167  1.00 40.34  ? 85  GLU   C CD  1 
ATOM   1739 O  OE1 . GLU   B 1 79  ? 40.385 -8.456  8.458  1.00 43.45  ? 85  GLU   C OE1 1 
ATOM   1740 O  OE2 . GLU   B 1 79  ? 41.500 -9.369  10.127 1.00 43.41  ? 85  GLU   C OE2 1 
ATOM   1741 N  N   . ALA   B 1 80  ? 36.199 -8.823  8.292  1.00 21.19  ? 86  ALA   C N   1 
ATOM   1742 C  CA  . ALA   B 1 80  ? 34.908 -8.482  7.716  1.00 21.90  ? 86  ALA   C CA  1 
ATOM   1743 C  C   . ALA   B 1 80  ? 34.281 -9.680  7.003  1.00 22.67  ? 86  ALA   C C   1 
ATOM   1744 O  O   . ALA   B 1 80  ? 35.003 -10.500 6.408  1.00 22.75  ? 86  ALA   C O   1 
ATOM   1745 C  CB  . ALA   B 1 80  ? 35.077 -7.331  6.727  1.00 22.60  ? 86  ALA   C CB  1 
ATOM   1746 N  N   . SER   B 1 81  ? 32.963 -9.829  7.166  1.00 22.00  ? 87  SER   C N   1 
ATOM   1747 C  CA  . SER   B 1 81  ? 32.209 -10.865 6.495  1.00 23.31  ? 87  SER   C CA  1 
ATOM   1748 C  C   . SER   B 1 81  ? 31.073 -10.183 5.700  1.00 24.67  ? 87  SER   C C   1 
ATOM   1749 O  O   . SER   B 1 81  ? 30.965 -8.934  5.717  1.00 24.93  ? 87  SER   C O   1 
ATOM   1750 C  CB  . SER   B 1 81  ? 31.637 -11.839 7.529  1.00 22.97  ? 87  SER   C CB  1 
ATOM   1751 O  OG  . SER   B 1 81  ? 30.613 -11.159 8.247  1.00 22.54  ? 87  SER   C OG  1 
ATOM   1752 N  N   . GLU   B 1 82  ? 30.222 -10.979 5.012  1.00 25.85  ? 88  GLU   C N   1 
ATOM   1753 C  CA  . GLU   B 1 82  ? 29.125 -10.332 4.270  1.00 27.67  ? 88  GLU   C CA  1 
ATOM   1754 C  C   . GLU   B 1 82  ? 28.069 -9.711  5.199  1.00 27.27  ? 88  GLU   C C   1 
ATOM   1755 O  O   . GLU   B 1 82  ? 27.291 -8.855  4.751  1.00 28.78  ? 88  GLU   C O   1 
ATOM   1756 C  CB  . GLU   B 1 82  ? 28.490 -11.249 3.205  1.00 32.83  ? 88  GLU   C CB  1 
ATOM   1757 C  CG  . GLU   B 1 82  ? 27.840 -12.520 3.702  1.00 40.71  ? 88  GLU   C CG  1 
ATOM   1758 C  CD  . GLU   B 1 82  ? 27.232 -13.330 2.568  1.00 48.36  ? 88  GLU   C CD  1 
ATOM   1759 O  OE1 . GLU   B 1 82  ? 27.894 -13.442 1.510  1.00 49.25  ? 88  GLU   C OE1 1 
ATOM   1760 O  OE2 . GLU   B 1 82  ? 26.101 -13.849 2.733  1.00 51.50  ? 88  GLU   C OE2 1 
ATOM   1761 N  N   . TYR   B 1 83  ? 28.065 -10.079 6.494  1.00 24.79  ? 89  TYR   C N   1 
ATOM   1762 C  CA  . TYR   B 1 83  ? 27.043 -9.588  7.430  1.00 23.99  ? 89  TYR   C CA  1 
ATOM   1763 C  C   . TYR   B 1 83  ? 27.555 -8.678  8.580  1.00 23.79  ? 89  TYR   C C   1 
ATOM   1764 O  O   . TYR   B 1 83  ? 26.713 -8.081  9.293  1.00 24.53  ? 89  TYR   C O   1 
ATOM   1765 C  CB  . TYR   B 1 83  ? 26.238 -10.784 8.012  1.00 23.27  ? 89  TYR   C CB  1 
ATOM   1766 C  CG  . TYR   B 1 83  ? 27.090 -11.987 8.411  1.00 23.33  ? 89  TYR   C CG  1 
ATOM   1767 C  CD1 . TYR   B 1 83  ? 27.426 -12.975 7.484  1.00 23.31  ? 89  TYR   C CD1 1 
ATOM   1768 C  CD2 . TYR   B 1 83  ? 27.560 -12.129 9.704  1.00 23.40  ? 89  TYR   C CD2 1 
ATOM   1769 C  CE1 . TYR   B 1 83  ? 28.220 -14.066 7.847  1.00 23.24  ? 89  TYR   C CE1 1 
ATOM   1770 C  CE2 . TYR   B 1 83  ? 28.343 -13.213 10.079 1.00 24.03  ? 89  TYR   C CE2 1 
ATOM   1771 C  CZ  . TYR   B 1 83  ? 28.658 -14.189 9.155  1.00 24.44  ? 89  TYR   C CZ  1 
ATOM   1772 O  OH  . TYR   B 1 83  ? 29.456 -15.242 9.565  1.00 24.26  ? 89  TYR   C OH  1 
ATOM   1773 N  N   . TYR   B 1 84  ? 28.898 -8.606  8.822  1.00 21.96  ? 90  TYR   C N   1 
ATOM   1774 C  CA  . TYR   B 1 84  ? 29.449 -7.710  9.858  1.00 21.74  ? 90  TYR   C CA  1 
ATOM   1775 C  C   . TYR   B 1 84  ? 30.757 -7.102  9.341  1.00 22.60  ? 90  TYR   C C   1 
ATOM   1776 O  O   . TYR   B 1 84  ? 31.505 -7.774  8.616  1.00 21.51  ? 90  TYR   C O   1 
ATOM   1777 C  CB  . TYR   B 1 84  ? 29.840 -8.501  11.150 1.00 20.38  ? 90  TYR   C CB  1 
ATOM   1778 C  CG  . TYR   B 1 84  ? 28.676 -8.916  12.031 1.00 19.12  ? 90  TYR   C CG  1 
ATOM   1779 C  CD1 . TYR   B 1 84  ? 27.771 -7.977  12.516 1.00 19.43  ? 90  TYR   C CD1 1 
ATOM   1780 C  CD2 . TYR   B 1 84  ? 28.494 -10.240 12.392 1.00 19.24  ? 90  TYR   C CD2 1 
ATOM   1781 C  CE1 . TYR   B 1 84  ? 26.711 -8.358  13.347 1.00 20.29  ? 90  TYR   C CE1 1 
ATOM   1782 C  CE2 . TYR   B 1 84  ? 27.422 -10.639 13.187 1.00 19.76  ? 90  TYR   C CE2 1 
ATOM   1783 C  CZ  . TYR   B 1 84  ? 26.542 -9.696  13.684 1.00 20.60  ? 90  TYR   C CZ  1 
ATOM   1784 O  OH  . TYR   B 1 84  ? 25.486 -10.113 14.492 1.00 21.04  ? 90  TYR   C OH  1 
ATOM   1785 N  N   . PRO   B 1 85  ? 31.125 -5.895  9.803  1.00 23.16  ? 91  PRO   C N   1 
ATOM   1786 C  CA  . PRO   B 1 85  ? 32.475 -5.392  9.492  1.00 23.39  ? 91  PRO   C CA  1 
ATOM   1787 C  C   . PRO   B 1 85  ? 33.532 -6.147  10.334 1.00 22.77  ? 91  PRO   C C   1 
ATOM   1788 O  O   . PRO   B 1 85  ? 33.188 -6.981  11.207 1.00 22.21  ? 91  PRO   C O   1 
ATOM   1789 C  CB  . PRO   B 1 85  ? 32.391 -3.911  9.912  1.00 24.80  ? 91  PRO   C CB  1 
ATOM   1790 C  CG  . PRO   B 1 85  ? 31.393 -3.923  11.055 1.00 25.73  ? 91  PRO   C CG  1 
ATOM   1791 C  CD  . PRO   B 1 85  ? 30.387 -5.001  10.734 1.00 23.51  ? 91  PRO   C CD  1 
ATOM   1792 N  N   . ALA   B 1 86  ? 34.829 -5.845  10.123 1.00 22.50  ? 92  ALA   C N   1 
ATOM   1793 C  CA  . ALA   B 1 86  ? 35.892 -6.444  10.950 1.00 23.04  ? 92  ALA   C CA  1 
ATOM   1794 C  C   . ALA   B 1 86  ? 35.704 -5.862  12.374 1.00 23.84  ? 92  ALA   C C   1 
ATOM   1795 O  O   . ALA   B 1 86  ? 35.480 -4.640  12.498 1.00 24.48  ? 92  ALA   C O   1 
ATOM   1796 C  CB  . ALA   B 1 86  ? 37.258 -6.060  10.406 1.00 22.83  ? 92  ALA   C CB  1 
ATOM   1797 N  N   . ARG   B 1 87  ? 35.667 -6.719  13.398 1.00 22.59  ? 93  ARG   C N   1 
ATOM   1798 C  CA  . ARG   B 1 87  ? 35.369 -6.288  14.767 1.00 23.15  ? 93  ARG   C CA  1 
ATOM   1799 C  C   . ARG   B 1 87  ? 35.753 -7.359  15.779 1.00 24.34  ? 93  ARG   C C   1 
ATOM   1800 O  O   . ARG   B 1 87  ? 36.043 -8.495  15.386 1.00 24.58  ? 93  ARG   C O   1 
ATOM   1801 C  CB  . ARG   B 1 87  ? 33.845 -5.987  14.884 1.00 23.70  ? 93  ARG   C CB  1 
ATOM   1802 C  CG  . ARG   B 1 87  ? 32.996 -7.294  14.896 1.00 23.06  ? 93  ARG   C CG  1 
ATOM   1803 C  CD  . ARG   B 1 87  ? 31.496 -7.091  14.756 1.00 23.08  ? 93  ARG   C CD  1 
ATOM   1804 N  NE  . ARG   B 1 87  ? 30.839 -8.371  15.054 1.00 23.80  ? 93  ARG   C NE  1 
ATOM   1805 C  CZ  . ARG   B 1 87  ? 29.797 -8.559  15.840 1.00 24.70  ? 93  ARG   C CZ  1 
ATOM   1806 N  NH1 . ARG   B 1 87  ? 29.173 -7.521  16.392 1.00 24.47  ? 93  ARG   C NH1 1 
ATOM   1807 N  NH2 . ARG   B 1 87  ? 29.366 -9.793  16.094 1.00 23.42  ? 93  ARG   C NH2 1 
ATOM   1808 N  N   . TYR   B 1 88  ? 35.670 -7.050  17.084 1.00 25.56  ? 94  TYR   C N   1 
ATOM   1809 C  CA  . TYR   B 1 88  ? 35.872 -8.075  18.117 1.00 27.45  ? 94  TYR   C CA  1 
ATOM   1810 C  C   . TYR   B 1 88  ? 34.547 -8.749  18.398 1.00 24.48  ? 94  TYR   C C   1 
ATOM   1811 O  O   . TYR   B 1 88  ? 33.528 -8.074  18.546 1.00 25.21  ? 94  TYR   C O   1 
ATOM   1812 C  CB  . TYR   B 1 88  ? 36.344 -7.448  19.437 1.00 30.50  ? 94  TYR   C CB  1 
ATOM   1813 C  CG  . TYR   B 1 88  ? 37.789 -7.054  19.366 1.00 34.06  ? 94  TYR   C CG  1 
ATOM   1814 C  CD1 . TYR   B 1 88  ? 38.792 -7.978  19.613 1.00 36.22  ? 94  TYR   C CD1 1 
ATOM   1815 C  CD2 . TYR   B 1 88  ? 38.158 -5.781  18.957 1.00 36.31  ? 94  TYR   C CD2 1 
ATOM   1816 C  CE1 . TYR   B 1 88  ? 40.130 -7.629  19.497 1.00 37.94  ? 94  TYR   C CE1 1 
ATOM   1817 C  CE2 . TYR   B 1 88  ? 39.485 -5.414  18.858 1.00 37.64  ? 94  TYR   C CE2 1 
ATOM   1818 C  CZ  . TYR   B 1 88  ? 40.469 -6.341  19.123 1.00 39.42  ? 94  TYR   C CZ  1 
ATOM   1819 O  OH  . TYR   B 1 88  ? 41.770 -5.928  19.010 1.00 42.48  ? 94  TYR   C OH  1 
ATOM   1820 N  N   . GLN   B 1 89  ? 34.543 -10.085 18.450 1.00 22.39  ? 95  GLN   C N   1 
ATOM   1821 C  CA  . GLN   B 1 89  ? 33.328 -10.817 18.809 1.00 21.56  ? 95  GLN   C CA  1 
ATOM   1822 C  C   . GLN   B 1 89  ? 33.662 -11.583 20.103 1.00 21.00  ? 95  GLN   C C   1 
ATOM   1823 O  O   . GLN   B 1 89  ? 34.757 -12.165 20.222 1.00 21.55  ? 95  GLN   C O   1 
ATOM   1824 C  CB  . GLN   B 1 89  ? 32.921 -11.789 17.677 1.00 22.23  ? 95  GLN   C CB  1 
ATOM   1825 C  CG  . GLN   B 1 89  ? 31.626 -12.536 17.973 1.00 22.71  ? 95  GLN   C CG  1 
ATOM   1826 C  CD  . GLN   B 1 89  ? 30.970 -13.140 16.747 1.00 21.65  ? 95  GLN   C CD  1 
ATOM   1827 O  OE1 . GLN   B 1 89  ? 30.907 -12.534 15.647 1.00 22.18  ? 95  GLN   C OE1 1 
ATOM   1828 N  NE2 . GLN   B 1 89  ? 30.465 -14.344 16.935 1.00 21.46  ? 95  GLN   C NE2 1 
ATOM   1829 N  N   . SER   B 1 90  ? 32.766 -11.546 21.078 1.00 19.12  ? 96  SER   C N   1 
ATOM   1830 C  CA  . SER   B 1 90  ? 33.015 -12.193 22.371 1.00 19.58  ? 96  SER   C CA  1 
ATOM   1831 C  C   . SER   B 1 90  ? 32.395 -13.612 22.429 1.00 18.55  ? 96  SER   C C   1 
ATOM   1832 O  O   . SER   B 1 90  ? 31.519 -13.931 21.618 1.00 17.87  ? 96  SER   C O   1 
ATOM   1833 C  CB  . SER   B 1 90  ? 32.483 -11.326 23.517 1.00 21.19  ? 96  SER   C CB  1 
ATOM   1834 O  OG  . SER   B 1 90  ? 31.077 -11.233 23.415 1.00 21.24  ? 96  SER   C OG  1 
ATOM   1835 N  N   . HIS   B 1 91  ? 32.834 -14.431 23.403 1.00 17.86  ? 97  HIS   C N   1 
ATOM   1836 C  CA  . HIS   B 1 91  ? 32.345 -15.792 23.645 1.00 18.53  ? 97  HIS   C CA  1 
ATOM   1837 C  C   . HIS   B 1 91  ? 32.432 -16.653 22.370 1.00 18.25  ? 97  HIS   C C   1 
ATOM   1838 O  O   . HIS   B 1 91  ? 31.547 -17.468 22.114 1.00 19.31  ? 97  HIS   C O   1 
ATOM   1839 C  CB  . HIS   B 1 91  ? 30.900 -15.754 24.198 1.00 19.13  ? 97  HIS   C CB  1 
ATOM   1840 C  CG  . HIS   B 1 91  ? 30.778 -14.998 25.495 1.00 20.19  ? 97  HIS   C CG  1 
ATOM   1841 N  ND1 . HIS   B 1 91  ? 30.808 -15.663 26.716 1.00 22.75  ? 97  HIS   C ND1 1 
ATOM   1842 C  CD2 . HIS   B 1 91  ? 30.667 -13.652 25.729 1.00 21.39  ? 97  HIS   C CD2 1 
ATOM   1843 C  CE1 . HIS   B 1 91  ? 30.653 -14.717 27.650 1.00 23.07  ? 97  HIS   C CE1 1 
ATOM   1844 N  NE2 . HIS   B 1 91  ? 30.560 -13.491 27.103 1.00 22.35  ? 97  HIS   C NE2 1 
ATOM   1845 N  N   . LEU   B 1 92  ? 33.512 -16.460 21.586 1.00 17.63  ? 98  LEU   C N   1 
ATOM   1846 C  CA  . LEU   B 1 92  ? 33.718 -17.153 20.339 1.00 17.55  ? 98  LEU   C CA  1 
ATOM   1847 C  C   . LEU   B 1 92  ? 34.768 -18.239 20.509 1.00 17.12  ? 98  LEU   C C   1 
ATOM   1848 O  O   . LEU   B 1 92  ? 35.778 -18.036 21.206 1.00 17.92  ? 98  LEU   C O   1 
ATOM   1849 C  CB  . LEU   B 1 92  ? 34.206 -16.127 19.273 1.00 18.42  ? 98  LEU   C CB  1 
ATOM   1850 C  CG  . LEU   B 1 92  ? 34.314 -16.640 17.845 1.00 20.08  ? 98  LEU   C CG  1 
ATOM   1851 C  CD1 . LEU   B 1 92  ? 32.952 -17.077 17.303 1.00 21.25  ? 98  LEU   C CD1 1 
ATOM   1852 C  CD2 . LEU   B 1 92  ? 34.925 -15.565 16.888 1.00 21.41  ? 98  LEU   C CD2 1 
ATOM   1853 N  N   . MET   B 1 93  ? 34.548 -19.409 19.874 1.00 16.07  ? 99  MET   C N   1 
ATOM   1854 C  CA  . MET   B 1 93  ? 35.515 -20.525 19.917 1.00 16.12  ? 99  MET   C CA  1 
ATOM   1855 C  C   . MET   B 1 93  ? 35.918 -20.839 18.459 1.00 16.40  ? 99  MET   C C   1 
ATOM   1856 O  O   . MET   B 1 93  ? 35.033 -20.915 17.612 1.00 16.79  ? 99  MET   C O   1 
ATOM   1857 C  CB  . MET   B 1 93  ? 34.830 -21.768 20.520 1.00 17.54  ? 99  MET   C CB  1 
ATOM   1858 C  CG  . MET   B 1 93  ? 34.296 -21.450 21.892 1.00 18.72  ? 99  MET   C CG  1 
ATOM   1859 S  SD  . MET   B 1 93  ? 33.298 -22.787 22.565 1.00 19.96  ? 99  MET   C SD  1 
ATOM   1860 C  CE  . MET   B 1 93  ? 31.942 -22.762 21.536 1.00 18.49  ? 99  MET   C CE  1 
ATOM   1861 N  N   . LEU   B 1 94  ? 37.179 -21.086 18.199 1.00 16.32  ? 100 LEU   C N   1 
ATOM   1862 C  CA  . LEU   B 1 94  ? 37.626 -21.379 16.846 1.00 17.64  ? 100 LEU   C CA  1 
ATOM   1863 C  C   . LEU   B 1 94  ? 38.049 -22.836 16.693 1.00 17.88  ? 100 LEU   C C   1 
ATOM   1864 O  O   . LEU   B 1 94  ? 38.529 -23.458 17.622 1.00 17.83  ? 100 LEU   C O   1 
ATOM   1865 C  CB  . LEU   B 1 94  ? 38.849 -20.506 16.465 1.00 19.03  ? 100 LEU   C CB  1 
ATOM   1866 C  CG  . LEU   B 1 94  ? 38.697 -19.004 16.430 1.00 20.96  ? 100 LEU   C CG  1 
ATOM   1867 C  CD1 . LEU   B 1 94  ? 40.019 -18.349 15.898 1.00 23.43  ? 100 LEU   C CD1 1 
ATOM   1868 C  CD2 . LEU   B 1 94  ? 37.496 -18.584 15.558 1.00 22.39  ? 100 LEU   C CD2 1 
ATOM   1869 N  N   . ALA   B 1 95  ? 37.883 -23.355 15.470 1.00 18.00  ? 101 ALA   C N   1 
ATOM   1870 C  CA  . ALA   B 1 95  ? 38.367 -24.685 15.082 1.00 18.08  ? 101 ALA   C CA  1 
ATOM   1871 C  C   . ALA   B 1 95  ? 38.922 -24.582 13.640 1.00 17.87  ? 101 ALA   C C   1 
ATOM   1872 O  O   . ALA   B 1 95  ? 38.595 -23.651 12.904 1.00 18.14  ? 101 ALA   C O   1 
ATOM   1873 C  CB  . ALA   B 1 95  ? 37.240 -25.744 15.128 1.00 18.26  ? 101 ALA   C CB  1 
ATOM   1874 N  N   . VAL   B 1 96  ? 39.734 -25.550 13.242 1.00 17.34  ? 102 VAL   C N   1 
ATOM   1875 C  CA  . VAL   B 1 96  ? 40.206 -25.638 11.860 1.00 18.73  ? 102 VAL   C CA  1 
ATOM   1876 C  C   . VAL   B 1 96  ? 39.121 -26.392 11.084 1.00 19.41  ? 102 VAL   C C   1 
ATOM   1877 O  O   . VAL   B 1 96  ? 38.837 -27.561 11.386 1.00 20.46  ? 102 VAL   C O   1 
ATOM   1878 C  CB  . VAL   B 1 96  ? 41.556 -26.384 11.789 1.00 19.65  ? 102 VAL   C CB  1 
ATOM   1879 C  CG1 . VAL   B 1 96  ? 42.004 -26.515 10.327 1.00 20.91  ? 102 VAL   C CG1 1 
ATOM   1880 C  CG2 . VAL   B 1 96  ? 42.600 -25.660 12.630 1.00 20.08  ? 102 VAL   C CG2 1 
ATOM   1881 N  N   . GLY   B 1 97  ? 38.522 -25.733 10.110 1.00 22.16  ? 103 GLY   C N   1 
ATOM   1882 C  CA  . GLY   B 1 97  ? 37.456 -26.369 9.343  1.00 22.75  ? 103 GLY   C CA  1 
ATOM   1883 C  C   . GLY   B 1 97  ? 36.781 -25.416 8.414  1.00 23.84  ? 103 GLY   C C   1 
ATOM   1884 O  O   . GLY   B 1 97  ? 37.054 -24.206 8.449  1.00 24.37  ? 103 GLY   C O   1 
ATOM   1885 N  N   . HIS   B 1 98  ? 35.885 -25.946 7.577  1.00 23.78  ? 104 HIS   C N   1 
ATOM   1886 C  CA  . HIS   B 1 98  ? 35.221 -25.120 6.592  1.00 23.93  ? 104 HIS   C CA  1 
ATOM   1887 C  C   . HIS   B 1 98  ? 33.974 -24.393 7.139  1.00 23.05  ? 104 HIS   C C   1 
ATOM   1888 O  O   . HIS   B 1 98  ? 33.168 -25.003 7.828  1.00 22.18  ? 104 HIS   C O   1 
ATOM   1889 C  CB  . HIS   B 1 98  ? 34.813 -25.997 5.410  1.00 26.00  ? 104 HIS   C CB  1 
ATOM   1890 C  CG  . HIS   B 1 98  ? 34.241 -25.193 4.297  1.00 31.26  ? 104 HIS   C CG  1 
ATOM   1891 N  ND1 . HIS   B 1 98  ? 35.010 -24.244 3.607  1.00 33.96  ? 104 HIS   C ND1 1 
ATOM   1892 C  CD2 . HIS   B 1 98  ? 32.986 -25.201 3.791  1.00 33.86  ? 104 HIS   C CD2 1 
ATOM   1893 C  CE1 . HIS   B 1 98  ? 34.184 -23.694 2.723  1.00 35.65  ? 104 HIS   C CE1 1 
ATOM   1894 N  NE2 . HIS   B 1 98  ? 32.957 -24.254 2.782  1.00 35.87  ? 104 HIS   C NE2 1 
ATOM   1895 N  N   . SER   B 1 99  ? 33.772 -23.110 6.736  1.00 22.85  ? 105 SER   C N   1 
ATOM   1896 C  CA  . SER   B 1 99  ? 32.596 -22.321 7.127  1.00 23.07  ? 105 SER   C CA  1 
ATOM   1897 C  C   . SER   B 1 99  ? 32.354 -21.174 6.113  1.00 24.29  ? 105 SER   C C   1 
ATOM   1898 O  O   . SER   B 1 99  ? 33.173 -20.254 6.017  1.00 26.64  ? 105 SER   C O   1 
ATOM   1899 C  CB  . SER   B 1 99  ? 32.817 -21.715 8.507  1.00 24.17  ? 105 SER   C CB  1 
ATOM   1900 O  OG  . SER   B 1 99  ? 31.758 -20.842 8.868  1.00 27.07  ? 105 SER   C OG  1 
ATOM   1901 N  N   . GLU   B 1 100 ? 31.239 -21.238 5.373  1.00 23.50  ? 106 GLU   C N   1 
ATOM   1902 C  CA  . GLU   B 1 100 ? 30.815 -20.170 4.466  1.00 23.64  ? 106 GLU   C CA  1 
ATOM   1903 C  C   . GLU   B 1 100 ? 29.706 -19.401 5.184  1.00 22.41  ? 106 GLU   C C   1 
ATOM   1904 O  O   . GLU   B 1 100 ? 29.124 -19.916 6.155  1.00 21.41  ? 106 GLU   C O   1 
ATOM   1905 C  CB  . GLU   B 1 100 ? 30.252 -20.821 3.201  1.00 29.03  ? 106 GLU   C CB  1 
ATOM   1906 C  CG  . GLU   B 1 100 ? 31.366 -21.249 2.277  1.00 42.71  ? 106 GLU   C CG  1 
ATOM   1907 C  CD  . GLU   B 1 100 ? 30.846 -22.165 1.207  1.00 53.41  ? 106 GLU   C CD  1 
ATOM   1908 O  OE1 . GLU   B 1 100 ? 29.769 -21.854 0.653  1.00 58.11  ? 106 GLU   C OE1 1 
ATOM   1909 O  OE2 . GLU   B 1 100 ? 31.494 -23.201 0.940  1.00 56.67  ? 106 GLU   C OE2 1 
ATOM   1910 N  N   . PRO   B 1 101 ? 29.291 -18.211 4.698  1.00 22.95  ? 107 PRO   C N   1 
ATOM   1911 C  CA  . PRO   B 1 101 ? 28.218 -17.483 5.409  1.00 22.80  ? 107 PRO   C CA  1 
ATOM   1912 C  C   . PRO   B 1 101 ? 26.925 -18.298 5.635  1.00 22.89  ? 107 PRO   C C   1 
ATOM   1913 O  O   . PRO   B 1 101 ? 26.299 -18.182 6.690  1.00 22.36  ? 107 PRO   C O   1 
ATOM   1914 C  CB  . PRO   B 1 101 ? 28.002 -16.210 4.550  1.00 25.18  ? 107 PRO   C CB  1 
ATOM   1915 C  CG  . PRO   B 1 101 ? 29.096 -16.177 3.559  1.00 26.33  ? 107 PRO   C CG  1 
ATOM   1916 C  CD  . PRO   B 1 101 ? 29.881 -17.437 3.573  1.00 23.86  ? 107 PRO   C CD  1 
ATOM   1917 N  N   . GLY   B 1 102 ? 26.527 -19.113 4.643  1.00 21.89  ? 108 GLY   C N   1 
ATOM   1918 C  CA  . GLY   B 1 102 ? 25.324 -19.942 4.722  1.00 21.32  ? 108 GLY   C CA  1 
ATOM   1919 C  C   . GLY   B 1 102 ? 25.401 -21.056 5.754  1.00 20.37  ? 108 GLY   C C   1 
ATOM   1920 O  O   . GLY   B 1 102 ? 24.379 -21.666 6.106  1.00 20.64  ? 108 GLY   C O   1 
ATOM   1921 N  N   . ASP   B 1 103 ? 26.629 -21.346 6.260  1.00 18.97  ? 109 ASP   C N   1 
ATOM   1922 C  CA  . ASP   B 1 103 ? 26.792 -22.359 7.303  1.00 19.07  ? 109 ASP   C CA  1 
ATOM   1923 C  C   . ASP   B 1 103 ? 26.385 -21.862 8.700  1.00 18.77  ? 109 ASP   C C   1 
ATOM   1924 O  O   . ASP   B 1 103 ? 26.288 -22.676 9.632  1.00 18.73  ? 109 ASP   C O   1 
ATOM   1925 C  CB  . ASP   B 1 103 ? 28.257 -22.884 7.365  1.00 20.09  ? 109 ASP   C CB  1 
ATOM   1926 C  CG  . ASP   B 1 103 ? 28.580 -23.670 6.129  1.00 22.01  ? 109 ASP   C CG  1 
ATOM   1927 O  OD1 . ASP   B 1 103 ? 27.696 -24.380 5.645  1.00 22.77  ? 109 ASP   C OD1 1 
ATOM   1928 O  OD2 . ASP   B 1 103 ? 29.716 -23.560 5.629  1.00 22.35  ? 109 ASP   C OD2 1 
ATOM   1929 N  N   . CYS   B 1 104 ? 26.208 -20.512 8.885  1.00 17.16  ? 110 CYS   C N   1 
ATOM   1930 C  CA  . CYS   B 1 104 ? 25.835 -19.953 10.194 1.00 16.62  ? 110 CYS   C CA  1 
ATOM   1931 C  C   . CYS   B 1 104 ? 24.584 -20.637 10.731 1.00 17.96  ? 110 CYS   C C   1 
ATOM   1932 O  O   . CYS   B 1 104 ? 23.654 -20.858 9.955  1.00 19.83  ? 110 CYS   C O   1 
ATOM   1933 C  CB  . CYS   B 1 104 ? 25.626 -18.446 10.108 1.00 17.87  ? 110 CYS   C CB  1 
ATOM   1934 S  SG  . CYS   B 1 104 ? 27.165 -17.513 10.002 1.00 21.68  ? 110 CYS   C SG  1 
ATOM   1935 N  N   . GLY   B 1 105 ? 24.588 -20.970 12.009 1.00 16.95  ? 111 GLY   C N   1 
ATOM   1936 C  CA  . GLY   B 1 105 ? 23.441 -21.648 12.604 1.00 17.78  ? 111 GLY   C CA  1 
ATOM   1937 C  C   . GLY   B 1 105 ? 23.633 -23.159 12.733 1.00 18.03  ? 111 GLY   C C   1 
ATOM   1938 O  O   . GLY   B 1 105 ? 22.867 -23.815 13.443 1.00 19.11  ? 111 GLY   C O   1 
ATOM   1939 N  N   . GLY   B 1 106 ? 24.671 -23.714 12.075 1.00 16.64  ? 112 GLY   C N   1 
ATOM   1940 C  CA  . GLY   B 1 106 ? 24.987 -25.143 12.183 1.00 16.56  ? 112 GLY   C CA  1 
ATOM   1941 C  C   . GLY   B 1 106 ? 25.362 -25.468 13.621 1.00 17.34  ? 112 GLY   C C   1 
ATOM   1942 O  O   . GLY   B 1 106 ? 26.078 -24.691 14.269 1.00 18.12  ? 112 GLY   C O   1 
ATOM   1943 N  N   . ILE   B 1 107 ? 24.858 -26.594 14.154 1.00 17.63  ? 113 ILE   C N   1 
ATOM   1944 C  CA  . ILE   B 1 107 ? 25.123 -26.907 15.556 1.00 17.93  ? 113 ILE   C CA  1 
ATOM   1945 C  C   . ILE   B 1 107 ? 26.468 -27.584 15.786 1.00 16.99  ? 113 ILE   C C   1 
ATOM   1946 O  O   . ILE   B 1 107 ? 26.838 -28.500 15.038 1.00 16.16  ? 113 ILE   C O   1 
ATOM   1947 C  CB  . ILE   B 1 107 ? 23.942 -27.761 16.150 1.00 21.38  ? 113 ILE   C CB  1 
ATOM   1948 C  CG1 . ILE   B 1 107 ? 22.747 -26.824 16.512 1.00 23.96  ? 113 ILE   C CG1 1 
ATOM   1949 C  CG2 . ILE   B 1 107 ? 24.387 -28.587 17.420 1.00 21.94  ? 113 ILE   C CG2 1 
ATOM   1950 C  CD1 . ILE   B 1 107 ? 21.470 -27.586 16.946 1.00 26.65  ? 113 ILE   C CD1 1 
ATOM   1951 N  N   . LEU   B 1 108 ? 27.169 -27.171 16.874 1.00 15.44  ? 114 LEU   C N   1 
ATOM   1952 C  CA  . LEU   B 1 108 ? 28.355 -27.855 17.393 1.00 14.79  ? 114 LEU   C CA  1 
ATOM   1953 C  C   . LEU   B 1 108 ? 27.867 -28.606 18.666 1.00 16.06  ? 114 LEU   C C   1 
ATOM   1954 O  O   . LEU   B 1 108 ? 27.234 -27.990 19.519 1.00 14.81  ? 114 LEU   C O   1 
ATOM   1955 C  CB  . LEU   B 1 108 ? 29.409 -26.813 17.809 1.00 15.13  ? 114 LEU   C CB  1 
ATOM   1956 C  CG  . LEU   B 1 108 ? 30.613 -27.366 18.590 1.00 16.43  ? 114 LEU   C CG  1 
ATOM   1957 C  CD1 . LEU   B 1 108 ? 31.460 -28.305 17.707 1.00 18.37  ? 114 LEU   C CD1 1 
ATOM   1958 C  CD2 . LEU   B 1 108 ? 31.466 -26.216 19.089 1.00 16.68  ? 114 LEU   C CD2 1 
ATOM   1959 N  N   . ARG   B 1 109 ? 28.139 -29.909 18.758 1.00 16.02  ? 115 ARG   C N   1 
ATOM   1960 C  CA  . ARG   B 1 109 ? 27.680 -30.665 19.931 1.00 17.38  ? 115 ARG   C CA  1 
ATOM   1961 C  C   . ARG   B 1 109 ? 28.780 -31.552 20.461 1.00 17.90  ? 115 ARG   C C   1 
ATOM   1962 O  O   . ARG   B 1 109 ? 29.659 -32.026 19.713 1.00 18.51  ? 115 ARG   C O   1 
ATOM   1963 C  CB  . ARG   B 1 109 ? 26.452 -31.518 19.549 1.00 21.67  ? 115 ARG   C CB  1 
ATOM   1964 C  CG  . ARG   B 1 109 ? 26.738 -32.581 18.514 1.00 30.25  ? 115 ARG   C CG  1 
ATOM   1965 C  CD  . ARG   B 1 109 ? 25.442 -33.318 18.166 1.00 39.07  ? 115 ARG   C CD  1 
ATOM   1966 N  NE  . ARG   B 1 109 ? 24.547 -32.526 17.307 1.00 46.50  ? 115 ARG   C NE  1 
ATOM   1967 C  CZ  . ARG   B 1 109 ? 23.292 -32.195 17.631 1.00 52.35  ? 115 ARG   C CZ  1 
ATOM   1968 N  NH1 . ARG   B 1 109 ? 22.779 -32.566 18.803 1.00 52.32  ? 115 ARG   C NH1 1 
ATOM   1969 N  NH2 . ARG   B 1 109 ? 22.547 -31.483 16.792 1.00 53.33  ? 115 ARG   C NH2 1 
ATOM   1970 N  N   . CYS   B 1 110 ? 28.697 -31.823 21.753 1.00 17.42  ? 116 CYS   C N   1 
ATOM   1971 C  CA  . CYS   B 1 110 ? 29.638 -32.728 22.409 1.00 17.68  ? 116 CYS   C CA  1 
ATOM   1972 C  C   . CYS   B 1 110 ? 28.792 -33.828 23.103 1.00 18.93  ? 116 CYS   C C   1 
ATOM   1973 O  O   . CYS   B 1 110 ? 27.563 -33.896 22.886 1.00 18.60  ? 116 CYS   C O   1 
ATOM   1974 C  CB  . CYS   B 1 110 ? 30.469 -31.949 23.413 1.00 18.25  ? 116 CYS   C CB  1 
ATOM   1975 S  SG  . CYS   B 1 110 ? 29.473 -31.296 24.783 1.00 17.79  ? 116 CYS   C SG  1 
ATOM   1976 N  N   . GLN   B 1 111 ? 29.430 -34.689 23.938 1.00 19.44  ? 117 GLN   C N   1 
ATOM   1977 C  CA  . GLN   B 1 111 ? 28.675 -35.745 24.649 1.00 21.72  ? 117 GLN   C CA  1 
ATOM   1978 C  C   . GLN   B 1 111 ? 27.599 -35.175 25.594 1.00 21.41  ? 117 GLN   C C   1 
ATOM   1979 O  O   . GLN   B 1 111 ? 26.648 -35.886 25.972 1.00 22.53  ? 117 GLN   C O   1 
ATOM   1980 C  CB  . GLN   B 1 111 ? 29.628 -36.652 25.477 1.00 24.40  ? 117 GLN   C CB  1 
ATOM   1981 C  CG  . GLN   B 1 111 ? 30.486 -35.861 26.467 1.00 30.61  ? 117 GLN   C CG  1 
ATOM   1982 C  CD  . GLN   B 1 111 ? 31.520 -36.647 27.235 1.00 40.08  ? 117 GLN   C CD  1 
ATOM   1983 O  OE1 . GLN   B 1 111 ? 32.725 -36.361 27.152 1.00 42.63  ? 117 GLN   C OE1 1 
ATOM   1984 N  NE2 . GLN   B 1 111 ? 31.069 -37.600 28.049 1.00 40.41  ? 117 GLN   C NE2 1 
ATOM   1985 N  N   . HIS   B 1 112 ? 27.733 -33.909 25.990 1.00 19.32  ? 118 HIS   C N   1 
ATOM   1986 C  CA  . HIS   B 1 112 ? 26.795 -33.312 26.956 1.00 18.97  ? 118 HIS   C CA  1 
ATOM   1987 C  C   . HIS   B 1 112 ? 25.614 -32.587 26.291 1.00 20.67  ? 118 HIS   C C   1 
ATOM   1988 O  O   . HIS   B 1 112 ? 24.671 -32.213 26.991 1.00 21.94  ? 118 HIS   C O   1 
ATOM   1989 C  CB  . HIS   B 1 112 ? 27.545 -32.337 27.868 1.00 19.12  ? 118 HIS   C CB  1 
ATOM   1990 C  CG  . HIS   B 1 112 ? 28.722 -32.964 28.585 1.00 19.61  ? 118 HIS   C CG  1 
ATOM   1991 N  ND1 . HIS   B 1 112 ? 30.028 -32.717 28.191 1.00 19.80  ? 118 HIS   C ND1 1 
ATOM   1992 C  CD2 . HIS   B 1 112 ? 28.741 -33.825 29.630 1.00 19.49  ? 118 HIS   C CD2 1 
ATOM   1993 C  CE1 . HIS   B 1 112 ? 30.799 -33.422 28.993 1.00 20.51  ? 118 HIS   C CE1 1 
ATOM   1994 N  NE2 . HIS   B 1 112 ? 30.063 -34.121 29.879 1.00 20.55  ? 118 HIS   C NE2 1 
ATOM   1995 N  N   . GLY   B 1 113 ? 25.683 -32.328 24.988 1.00 19.72  ? 119 GLY   C N   1 
ATOM   1996 C  CA  . GLY   B 1 113 ? 24.602 -31.624 24.305 1.00 19.35  ? 119 GLY   C CA  1 
ATOM   1997 C  C   . GLY   B 1 113 ? 25.127 -30.557 23.362 1.00 17.51  ? 119 GLY   C C   1 
ATOM   1998 O  O   . GLY   B 1 113 ? 26.271 -30.642 22.905 1.00 17.09  ? 119 GLY   C O   1 
ATOM   1999 N  N   . VAL   B 1 114 ? 24.291 -29.538 23.094 1.00 16.22  ? 120 VAL   C N   1 
ATOM   2000 C  CA  . VAL   B 1 114 ? 24.627 -28.444 22.188 1.00 17.64  ? 120 VAL   C CA  1 
ATOM   2001 C  C   . VAL   B 1 114 ? 25.599 -27.473 22.851 1.00 16.67  ? 120 VAL   C C   1 
ATOM   2002 O  O   . VAL   B 1 114 ? 25.306 -26.930 23.912 1.00 17.59  ? 120 VAL   C O   1 
ATOM   2003 C  CB  . VAL   B 1 114 ? 23.348 -27.720 21.713 1.00 18.65  ? 120 VAL   C CB  1 
ATOM   2004 C  CG1 . VAL   B 1 114 ? 23.724 -26.488 20.863 1.00 20.01  ? 120 VAL   C CG1 1 
ATOM   2005 C  CG2 . VAL   B 1 114 ? 22.424 -28.691 20.940 1.00 19.36  ? 120 VAL   C CG2 1 
ATOM   2006 N  N   . VAL   B 1 115 ? 26.748 -27.243 22.202 1.00 16.29  ? 121 VAL   C N   1 
ATOM   2007 C  CA  . VAL   B 1 115 ? 27.776 -26.322 22.707 1.00 16.14  ? 121 VAL   C CA  1 
ATOM   2008 C  C   . VAL   B 1 115 ? 27.594 -24.917 22.163 1.00 17.03  ? 121 VAL   C C   1 
ATOM   2009 O  O   . VAL   B 1 115 ? 27.821 -23.916 22.871 1.00 18.18  ? 121 VAL   C O   1 
ATOM   2010 C  CB  . VAL   B 1 115 ? 29.158 -26.881 22.278 1.00 16.67  ? 121 VAL   C CB  1 
ATOM   2011 C  CG1 . VAL   B 1 115 ? 30.276 -25.891 22.609 1.00 15.62  ? 121 VAL   C CG1 1 
ATOM   2012 C  CG2 . VAL   B 1 115 ? 29.393 -28.255 22.882 1.00 17.79  ? 121 VAL   C CG2 1 
ATOM   2013 N  N   . GLY   B 1 116 ? 27.219 -24.830 20.881 1.00 15.26  ? 122 GLY   C N   1 
ATOM   2014 C  CA  . GLY   B 1 116 ? 27.042 -23.522 20.255 1.00 16.89  ? 122 GLY   C CA  1 
ATOM   2015 C  C   . GLY   B 1 116 ? 26.686 -23.659 18.789 1.00 17.11  ? 122 GLY   C C   1 
ATOM   2016 O  O   . GLY   B 1 116 ? 26.317 -24.750 18.344 1.00 16.61  ? 122 GLY   C O   1 
ATOM   2017 N  N   . ILE   B 1 117 ? 26.680 -22.513 18.068 1.00 15.87  ? 123 ILE   C N   1 
ATOM   2018 C  CA  . ILE   B 1 117 ? 26.304 -22.523 16.671 1.00 16.39  ? 123 ILE   C CA  1 
ATOM   2019 C  C   . ILE   B 1 117 ? 27.351 -21.800 15.837 1.00 16.07  ? 123 ILE   C C   1 
ATOM   2020 O  O   . ILE   B 1 117 ? 27.984 -20.840 16.297 1.00 15.90  ? 123 ILE   C O   1 
ATOM   2021 C  CB  . ILE   B 1 117 ? 24.927 -21.845 16.438 1.00 18.52  ? 123 ILE   C CB  1 
ATOM   2022 C  CG1 . ILE   B 1 117 ? 24.829 -20.470 17.104 1.00 19.51  ? 123 ILE   C CG1 1 
ATOM   2023 C  CG2 . ILE   B 1 117 ? 23.780 -22.771 16.864 1.00 19.11  ? 123 ILE   C CG2 1 
ATOM   2024 C  CD1 . ILE   B 1 117 ? 23.464 -19.695 16.723 1.00 20.56  ? 123 ILE   C CD1 1 
ATOM   2025 N  N   . VAL   B 1 118 ? 27.512 -22.221 14.571 1.00 16.05  ? 124 VAL   C N   1 
ATOM   2026 C  CA  . VAL   B 1 118 ? 28.439 -21.530 13.662 1.00 15.55  ? 124 VAL   C CA  1 
ATOM   2027 C  C   . VAL   B 1 118 ? 28.091 -20.042 13.557 1.00 16.37  ? 124 VAL   C C   1 
ATOM   2028 O  O   . VAL   B 1 118 ? 26.915 -19.705 13.397 1.00 16.75  ? 124 VAL   C O   1 
ATOM   2029 C  CB  . VAL   B 1 118 ? 28.420 -22.203 12.272 1.00 16.90  ? 124 VAL   C CB  1 
ATOM   2030 C  CG1 . VAL   B 1 118 ? 29.270 -21.420 11.255 1.00 16.64  ? 124 VAL   C CG1 1 
ATOM   2031 C  CG2 . VAL   B 1 118 ? 28.903 -23.652 12.384 1.00 17.36  ? 124 VAL   C CG2 1 
ATOM   2032 N  N   . SER   B 1 119 ? 29.125 -19.166 13.678 1.00 15.84  ? 125 SER   C N   1 
ATOM   2033 C  CA  . SER   B 1 119 ? 28.909 -17.715 13.578 1.00 17.11  ? 125 SER   C CA  1 
ATOM   2034 C  C   . SER   B 1 119 ? 29.922 -17.035 12.649 1.00 17.79  ? 125 SER   C C   1 
ATOM   2035 O  O   . SER   B 1 119 ? 29.623 -15.982 12.063 1.00 18.23  ? 125 SER   C O   1 
ATOM   2036 C  CB  . SER   B 1 119 ? 29.005 -17.096 14.964 1.00 18.59  ? 125 SER   C CB  1 
ATOM   2037 O  OG  . SER   B 1 119 ? 28.851 -15.680 14.901 1.00 19.35  ? 125 SER   C OG  1 
ATOM   2038 N  N   . THR   B 1 120 ? 31.157 -17.588 12.548 1.00 16.74  ? 126 THR   C N   1 
ATOM   2039 C  CA  . THR   B 1 120 ? 32.192 -16.945 11.724 1.00 16.69  ? 126 THR   C CA  1 
ATOM   2040 C  C   . THR   B 1 120 ? 32.899 -17.987 10.833 1.00 17.14  ? 126 THR   C C   1 
ATOM   2041 O  O   . THR   B 1 120 ? 32.795 -19.210 11.049 1.00 17.26  ? 126 THR   C O   1 
ATOM   2042 C  CB  . THR   B 1 120 ? 33.259 -16.202 12.608 1.00 17.64  ? 126 THR   C CB  1 
ATOM   2043 O  OG1 . THR   B 1 120 ? 34.152 -17.147 13.235 1.00 18.02  ? 126 THR   C OG1 1 
ATOM   2044 C  CG2 . THR   B 1 120 ? 32.670 -15.256 13.609 1.00 19.05  ? 126 THR   C CG2 1 
ATOM   2045 N  N   . GLY   B 1 121 ? 33.611 -17.492 9.832  1.00 19.68  ? 127 GLY   C N   1 
ATOM   2046 C  CA  . GLY   B 1 121 ? 34.341 -18.391 8.927  1.00 21.93  ? 127 GLY   C CA  1 
ATOM   2047 C  C   . GLY   B 1 121 ? 35.348 -17.612 8.100  1.00 25.37  ? 127 GLY   C C   1 
ATOM   2048 O  O   . GLY   B 1 121 ? 35.237 -16.392 7.962  1.00 26.53  ? 127 GLY   C O   1 
ATOM   2049 N  N   . GLY   B 1 122 ? 36.293 -18.320 7.523  1.00 27.01  ? 128 GLY   C N   1 
ATOM   2050 C  CA  . GLY   B 1 122 ? 37.322 -17.680 6.704  1.00 28.45  ? 128 GLY   C CA  1 
ATOM   2051 C  C   . GLY   B 1 122 ? 38.716 -18.097 7.112  1.00 28.65  ? 128 GLY   C C   1 
ATOM   2052 O  O   . GLY   B 1 122 ? 38.932 -18.546 8.235  1.00 28.25  ? 128 GLY   C O   1 
ATOM   2053 N  N   . ASN   B 1 123 ? 39.689 -17.954 6.200  1.00 29.19  ? 129 ASN   C N   1 
ATOM   2054 C  CA  . ASN   B 1 123 ? 41.079 -18.348 6.438  1.00 30.22  ? 129 ASN   C CA  1 
ATOM   2055 C  C   . ASN   B 1 123 ? 41.212 -19.772 6.962  1.00 28.58  ? 129 ASN   C C   1 
ATOM   2056 O  O   . ASN   B 1 123 ? 42.125 -20.067 7.726  1.00 29.92  ? 129 ASN   C O   1 
ATOM   2057 C  CB  . ASN   B 1 123 ? 41.830 -17.346 7.322  1.00 34.76  ? 129 ASN   C CB  1 
ATOM   2058 C  CG  . ASN   B 1 123 ? 42.546 -16.265 6.524  1.00 42.61  ? 129 ASN   C CG  1 
ATOM   2059 O  OD1 . ASN   B 1 123 ? 42.311 -16.053 5.322  1.00 45.88  ? 129 ASN   C OD1 1 
ATOM   2060 N  ND2 . ASN   B 1 123 ? 43.453 -15.556 7.165  1.00 43.86  ? 129 ASN   C ND2 1 
ATOM   2061 N  N   . GLY   B 1 124 ? 40.322 -20.652 6.514  1.00 26.37  ? 130 GLY   C N   1 
ATOM   2062 C  CA  . GLY   B 1 124 ? 40.374 -22.048 6.925  1.00 25.65  ? 130 GLY   C CA  1 
ATOM   2063 C  C   . GLY   B 1 124 ? 39.947 -22.304 8.356  1.00 24.29  ? 130 GLY   C C   1 
ATOM   2064 O  O   . GLY   B 1 124 ? 40.196 -23.393 8.873  1.00 23.99  ? 130 GLY   C O   1 
ATOM   2065 N  N   . LEU   B 1 125 ? 39.306 -21.318 9.005  1.00 22.37  ? 131 LEU   C N   1 
ATOM   2066 C  CA  . LEU   B 1 125 ? 38.838 -21.508 10.376 1.00 21.54  ? 131 LEU   C CA  1 
ATOM   2067 C  C   . LEU   B 1 125 ? 37.325 -21.395 10.429 1.00 20.31  ? 131 LEU   C C   1 
ATOM   2068 O  O   . LEU   B 1 125 ? 36.727 -20.711 9.602  1.00 21.26  ? 131 LEU   C O   1 
ATOM   2069 C  CB  . LEU   B 1 125 ? 39.435 -20.453 11.296 1.00 22.98  ? 131 LEU   C CB  1 
ATOM   2070 C  CG  . LEU   B 1 125 ? 40.970 -20.482 11.407 1.00 26.00  ? 131 LEU   C CG  1 
ATOM   2071 C  CD1 . LEU   B 1 125 ? 41.494 -19.227 12.046 1.00 28.87  ? 131 LEU   C CD1 1 
ATOM   2072 C  CD2 . LEU   B 1 125 ? 41.444 -21.737 12.075 1.00 26.75  ? 131 LEU   C CD2 1 
ATOM   2073 N  N   . VAL   B 1 126 ? 36.706 -22.015 11.434 1.00 17.08  ? 132 VAL   C N   1 
ATOM   2074 C  CA  . VAL   B 1 126 ? 35.266 -21.880 11.648 1.00 16.54  ? 132 VAL   C CA  1 
ATOM   2075 C  C   . VAL   B 1 126 ? 35.112 -21.437 13.114 1.00 16.97  ? 132 VAL   C C   1 
ATOM   2076 O  O   . VAL   B 1 126 ? 35.848 -21.914 13.989 1.00 17.25  ? 132 VAL   C O   1 
ATOM   2077 C  CB  . VAL   B 1 126 ? 34.506 -23.228 11.427 1.00 18.28  ? 132 VAL   C CB  1 
ATOM   2078 C  CG1 . VAL   B 1 126 ? 35.175 -24.393 12.162 1.00 20.43  ? 132 VAL   C CG1 1 
ATOM   2079 C  CG2 . VAL   B 1 126 ? 33.011 -23.109 11.826 1.00 18.61  ? 132 VAL   C CG2 1 
ATOM   2080 N  N   . GLY   B 1 127 ? 34.237 -20.463 13.348 1.00 16.15  ? 133 GLY   C N   1 
ATOM   2081 C  CA  . GLY   B 1 127 ? 34.044 -19.943 14.699 1.00 15.71  ? 133 GLY   C CA  1 
ATOM   2082 C  C   . GLY   B 1 127 ? 32.631 -20.224 15.175 1.00 16.61  ? 133 GLY   C C   1 
ATOM   2083 O  O   . GLY   B 1 127 ? 31.675 -20.107 14.390 1.00 16.59  ? 133 GLY   C O   1 
ATOM   2084 N  N   . PHE   B 1 128 ? 32.509 -20.614 16.457 1.00 15.89  ? 134 PHE   C N   1 
ATOM   2085 C  CA  . PHE   B 1 128 ? 31.213 -20.954 17.028 1.00 15.77  ? 134 PHE   C CA  1 
ATOM   2086 C  C   . PHE   B 1 128 ? 30.890 -19.995 18.176 1.00 15.73  ? 134 PHE   C C   1 
ATOM   2087 O  O   . PHE   B 1 128 ? 31.742 -19.755 19.032 1.00 16.60  ? 134 PHE   C O   1 
ATOM   2088 C  CB  . PHE   B 1 128 ? 31.281 -22.392 17.603 1.00 14.98  ? 134 PHE   C CB  1 
ATOM   2089 C  CG  . PHE   B 1 128 ? 31.778 -23.431 16.622 1.00 15.46  ? 134 PHE   C CG  1 
ATOM   2090 C  CD1 . PHE   B 1 128 ? 30.917 -24.011 15.704 1.00 15.78  ? 134 PHE   C CD1 1 
ATOM   2091 C  CD2 . PHE   B 1 128 ? 33.106 -23.836 16.627 1.00 16.80  ? 134 PHE   C CD2 1 
ATOM   2092 C  CE1 . PHE   B 1 128 ? 31.371 -24.980 14.825 1.00 17.19  ? 134 PHE   C CE1 1 
ATOM   2093 C  CE2 . PHE   B 1 128 ? 33.565 -24.826 15.743 1.00 17.79  ? 134 PHE   C CE2 1 
ATOM   2094 C  CZ  . PHE   B 1 128 ? 32.701 -25.358 14.823 1.00 17.85  ? 134 PHE   C CZ  1 
ATOM   2095 N  N   . ALA   B 1 129 ? 29.657 -19.525 18.228 1.00 14.96  ? 135 ALA   C N   1 
ATOM   2096 C  CA  . ALA   B 1 129 ? 29.182 -18.711 19.353 1.00 15.88  ? 135 ALA   C CA  1 
ATOM   2097 C  C   . ALA   B 1 129 ? 28.788 -19.696 20.458 1.00 16.55  ? 135 ALA   C C   1 
ATOM   2098 O  O   . ALA   B 1 129 ? 27.887 -20.537 20.268 1.00 16.19  ? 135 ALA   C O   1 
ATOM   2099 C  CB  . ALA   B 1 129 ? 27.953 -17.896 18.918 1.00 16.35  ? 135 ALA   C CB  1 
ATOM   2100 N  N   . ASP   B 1 130 ? 29.464 -19.608 21.596 1.00 16.15  ? 136 ASP   C N   1 
ATOM   2101 C  CA  . ASP   B 1 130 ? 29.196 -20.500 22.713 1.00 16.51  ? 136 ASP   C CA  1 
ATOM   2102 C  C   . ASP   B 1 130 ? 27.851 -20.146 23.355 1.00 17.19  ? 136 ASP   C C   1 
ATOM   2103 O  O   . ASP   B 1 130 ? 27.496 -18.963 23.437 1.00 18.11  ? 136 ASP   C O   1 
ATOM   2104 C  CB  . ASP   B 1 130 ? 30.289 -20.286 23.778 1.00 17.78  ? 136 ASP   C CB  1 
ATOM   2105 C  CG  . ASP   B 1 130 ? 30.207 -21.218 24.974 1.00 21.03  ? 136 ASP   C CG  1 
ATOM   2106 O  OD1 . ASP   B 1 130 ? 30.026 -22.427 24.772 1.00 21.23  ? 136 ASP   C OD1 1 
ATOM   2107 O  OD2 . ASP   B 1 130 ? 30.246 -20.716 26.114 1.00 25.14  ? 136 ASP   C OD2 1 
ATOM   2108 N  N   . VAL   B 1 131 ? 27.134 -21.154 23.871 1.00 16.03  ? 137 VAL   C N   1 
ATOM   2109 C  CA  . VAL   B 1 131 ? 25.899 -20.921 24.641 1.00 16.06  ? 137 VAL   C CA  1 
ATOM   2110 C  C   . VAL   B 1 131 ? 25.955 -21.629 26.017 1.00 16.91  ? 137 VAL   C C   1 
ATOM   2111 O  O   . VAL   B 1 131 ? 24.988 -21.557 26.787 1.00 17.35  ? 137 VAL   C O   1 
ATOM   2112 C  CB  . VAL   B 1 131 ? 24.615 -21.355 23.879 1.00 16.83  ? 137 VAL   C CB  1 
ATOM   2113 C  CG1 . VAL   B 1 131 ? 24.467 -20.570 22.573 1.00 16.66  ? 137 VAL   C CG1 1 
ATOM   2114 C  CG2 . VAL   B 1 131 ? 24.638 -22.866 23.602 1.00 16.74  ? 137 VAL   C CG2 1 
ATOM   2115 N  N   . ARG   B 1 132 ? 27.082 -22.308 26.348 1.00 16.54  ? 138 ARG   C N   1 
ATOM   2116 C  CA  . ARG   B 1 132 ? 27.149 -23.088 27.587 1.00 16.57  ? 138 ARG   C CA  1 
ATOM   2117 C  C   . ARG   B 1 132 ? 27.085 -22.276 28.884 1.00 17.59  ? 138 ARG   C C   1 
ATOM   2118 O  O   . ARG   B 1 132 ? 26.802 -22.846 29.939 1.00 19.29  ? 138 ARG   C O   1 
ATOM   2119 C  CB  . ARG   B 1 132 ? 28.393 -23.972 27.589 1.00 16.39  ? 138 ARG   C CB  1 
ATOM   2120 C  CG  . ARG   B 1 132 ? 28.369 -25.023 26.487 1.00 16.64  ? 138 ARG   C CG  1 
ATOM   2121 C  CD  . ARG   B 1 132 ? 29.709 -25.780 26.476 1.00 16.43  ? 138 ARG   C CD  1 
ATOM   2122 N  NE  . ARG   B 1 132 ? 30.786 -24.896 26.040 1.00 16.06  ? 138 ARG   C NE  1 
ATOM   2123 C  CZ  . ARG   B 1 132 ? 32.038 -25.294 25.843 1.00 19.12  ? 138 ARG   C CZ  1 
ATOM   2124 N  NH1 . ARG   B 1 132 ? 32.404 -26.545 26.134 1.00 16.88  ? 138 ARG   C NH1 1 
ATOM   2125 N  NH2 . ARG   B 1 132 ? 32.947 -24.440 25.381 1.00 18.50  ? 138 ARG   C NH2 1 
ATOM   2126 N  N   . ASP   B 1 133 ? 27.404 -20.982 28.821 1.00 17.04  ? 139 ASP   C N   1 
ATOM   2127 C  CA  . ASP   B 1 133 ? 27.338 -20.123 29.990 1.00 18.28  ? 139 ASP   C CA  1 
ATOM   2128 C  C   . ASP   B 1 133 ? 25.924 -19.553 30.236 1.00 19.04  ? 139 ASP   C C   1 
ATOM   2129 O  O   . ASP   B 1 133 ? 25.697 -18.926 31.282 1.00 20.31  ? 139 ASP   C O   1 
ATOM   2130 C  CB  . ASP   B 1 133 ? 28.331 -18.946 29.847 1.00 19.33  ? 139 ASP   C CB  1 
ATOM   2131 C  CG  . ASP   B 1 133 ? 27.958 -18.009 28.707 1.00 23.68  ? 139 ASP   C CG  1 
ATOM   2132 O  OD1 . ASP   B 1 133 ? 27.589 -18.511 27.626 1.00 21.36  ? 139 ASP   C OD1 1 
ATOM   2133 O  OD2 . ASP   B 1 133 ? 27.971 -16.766 28.923 1.00 25.77  ? 139 ASP   C OD2 1 
ATOM   2134 N  N   . LEU   B 1 134 ? 24.990 -19.733 29.282 1.00 18.01  ? 140 LEU   C N   1 
ATOM   2135 C  CA  . LEU   B 1 134 ? 23.631 -19.167 29.392 1.00 18.02  ? 140 LEU   C CA  1 
ATOM   2136 C  C   . LEU   B 1 134 ? 22.770 -20.148 30.180 1.00 19.28  ? 140 LEU   C C   1 
ATOM   2137 O  O   . LEU   B 1 134 ? 21.925 -20.847 29.604 1.00 20.01  ? 140 LEU   C O   1 
ATOM   2138 C  CB  . LEU   B 1 134 ? 23.069 -18.928 27.982 1.00 17.69  ? 140 LEU   C CB  1 
ATOM   2139 C  CG  . LEU   B 1 134 ? 23.938 -17.990 27.099 1.00 19.72  ? 140 LEU   C CG  1 
ATOM   2140 C  CD1 . LEU   B 1 134 ? 23.351 -17.869 25.682 1.00 20.50  ? 140 LEU   C CD1 1 
ATOM   2141 C  CD2 . LEU   B 1 134 ? 24.046 -16.568 27.728 1.00 20.98  ? 140 LEU   C CD2 1 
ATOM   2142 N  N   . LEU   B 1 135 ? 23.000 -20.213 31.510 1.00 19.38  ? 141 LEU   C N   1 
ATOM   2143 C  CA  . LEU   B 1 135 ? 22.339 -21.228 32.331 1.00 20.59  ? 141 LEU   C CA  1 
ATOM   2144 C  C   . LEU   B 1 135 ? 20.825 -21.086 32.357 1.00 20.64  ? 141 LEU   C C   1 
ATOM   2145 O  O   . LEU   B 1 135 ? 20.110 -22.090 32.529 1.00 21.02  ? 141 LEU   C O   1 
ATOM   2146 C  CB  . LEU   B 1 135 ? 22.905 -21.281 33.769 1.00 21.87  ? 141 LEU   C CB  1 
ATOM   2147 C  CG  . LEU   B 1 135 ? 24.457 -21.308 33.882 1.00 24.57  ? 141 LEU   C CG  1 
ATOM   2148 C  CD1 . LEU   B 1 135 ? 24.911 -21.496 35.291 1.00 26.06  ? 141 LEU   C CD1 1 
ATOM   2149 C  CD2 . LEU   B 1 135 ? 25.100 -22.377 32.982 1.00 23.82  ? 141 LEU   C CD2 1 
ATOM   2150 N  N   . TRP   B 1 136 ? 20.338 -19.838 32.195 1.00 20.20  ? 142 TRP   C N   1 
ATOM   2151 C  CA  . TRP   B 1 136 ? 18.907 -19.565 32.225 1.00 21.75  ? 142 TRP   C CA  1 
ATOM   2152 C  C   . TRP   B 1 136 ? 18.146 -20.261 31.081 1.00 22.47  ? 142 TRP   C C   1 
ATOM   2153 O  O   . TRP   B 1 136 ? 16.923 -20.351 31.159 1.00 24.18  ? 142 TRP   C O   1 
ATOM   2154 C  CB  . TRP   B 1 136 ? 18.657 -18.033 32.230 1.00 21.67  ? 142 TRP   C CB  1 
ATOM   2155 C  CG  . TRP   B 1 136 ? 19.343 -17.307 31.103 1.00 21.69  ? 142 TRP   C CG  1 
ATOM   2156 C  CD1 . TRP   B 1 136 ? 20.547 -16.668 31.145 1.00 23.03  ? 142 TRP   C CD1 1 
ATOM   2157 C  CD2 . TRP   B 1 136 ? 18.816 -17.086 29.779 1.00 22.08  ? 142 TRP   C CD2 1 
ATOM   2158 N  NE1 . TRP   B 1 136 ? 20.824 -16.087 29.911 1.00 23.28  ? 142 TRP   C NE1 1 
ATOM   2159 C  CE2 . TRP   B 1 136 ? 19.771 -16.332 29.059 1.00 22.89  ? 142 TRP   C CE2 1 
ATOM   2160 C  CE3 . TRP   B 1 136 ? 17.625 -17.449 29.141 1.00 22.24  ? 142 TRP   C CE3 1 
ATOM   2161 C  CZ2 . TRP   B 1 136 ? 19.564 -15.924 27.736 1.00 22.74  ? 142 TRP   C CZ2 1 
ATOM   2162 C  CZ3 . TRP   B 1 136 ? 17.417 -17.037 27.837 1.00 22.98  ? 142 TRP   C CZ3 1 
ATOM   2163 C  CH2 . TRP   B 1 136 ? 18.385 -16.299 27.143 1.00 22.59  ? 142 TRP   C CH2 1 
ATOM   2164 N  N   . LEU   B 1 137 ? 18.847 -20.751 30.023 1.00 21.75  ? 143 LEU   C N   1 
ATOM   2165 C  CA  . LEU   B 1 137 ? 18.139 -21.462 28.944 1.00 22.08  ? 143 LEU   C CA  1 
ATOM   2166 C  C   . LEU   B 1 137 ? 17.489 -22.765 29.475 1.00 24.37  ? 143 LEU   C C   1 
ATOM   2167 O  O   . LEU   B 1 137 ? 16.525 -23.249 28.855 1.00 25.29  ? 143 LEU   C O   1 
ATOM   2168 C  CB  . LEU   B 1 137 ? 19.089 -21.819 27.788 1.00 21.33  ? 143 LEU   C CB  1 
ATOM   2169 C  CG  . LEU   B 1 137 ? 19.572 -20.636 26.927 1.00 21.65  ? 143 LEU   C CG  1 
ATOM   2170 C  CD1 . LEU   B 1 137 ? 20.676 -21.090 25.962 1.00 21.80  ? 143 LEU   C CD1 1 
ATOM   2171 C  CD2 . LEU   B 1 137 ? 18.432 -20.072 26.089 1.00 22.00  ? 143 LEU   C CD2 1 
ATOM   2172 N  N   . ASP   B 1 138 ? 17.997 -23.318 30.607 1.00 24.40  ? 144 ASP   C N   1 
ATOM   2173 C  CA  . ASP   B 1 138 ? 17.512 -24.580 31.202 1.00 26.13  ? 144 ASP   C CA  1 
ATOM   2174 C  C   . ASP   B 1 138 ? 16.294 -24.436 32.091 1.00 30.21  ? 144 ASP   C C   1 
ATOM   2175 O  O   . ASP   B 1 138 ? 15.846 -25.456 32.639 1.00 30.75  ? 144 ASP   C O   1 
ATOM   2176 C  CB  . ASP   B 1 138 ? 18.602 -25.238 32.063 1.00 26.10  ? 144 ASP   C CB  1 
ATOM   2177 C  CG  . ASP   B 1 138 ? 19.836 -25.665 31.281 1.00 28.18  ? 144 ASP   C CG  1 
ATOM   2178 O  OD1 . ASP   B 1 138 ? 19.759 -25.739 30.025 1.00 28.05  ? 144 ASP   C OD1 1 
ATOM   2179 O  OD2 . ASP   B 1 138 ? 20.882 -25.922 31.924 1.00 30.24  ? 144 ASP   C OD2 1 
ATOM   2180 N  N   . GLU   B 1 139 ? 15.773 -23.221 32.273 1.00 32.64  ? 145 GLU   C N   1 
ATOM   2181 C  CA  . GLU   B 1 139 ? 14.617 -23.038 33.164 1.00 37.45  ? 145 GLU   C CA  1 
ATOM   2182 C  C   . GLU   B 1 139 ? 13.647 -21.932 32.716 1.00 41.36  ? 145 GLU   C C   1 
ATOM   2183 O  O   . GLU   B 1 139 ? 13.907 -21.255 31.723 1.00 41.96  ? 145 GLU   C O   1 
ATOM   2184 C  CB  . GLU   B 1 139 ? 15.151 -22.749 34.569 1.00 42.16  ? 145 GLU   C CB  1 
ATOM   2185 C  CG  . GLU   B 1 139 ? 15.942 -21.464 34.621 1.00 50.39  ? 145 GLU   C CG  1 
ATOM   2186 C  CD  . GLU   B 1 139 ? 17.082 -21.523 35.610 1.00 60.64  ? 145 GLU   C CD  1 
ATOM   2187 O  OE1 . GLU   B 1 139 ? 17.397 -20.477 36.220 1.00 62.76  ? 145 GLU   C OE1 1 
ATOM   2188 O  OE2 . GLU   B 1 139 ? 17.669 -22.618 35.770 1.00 64.98  ? 145 GLU   C OE2 1 
ATOM   2189 N  N   . GLU   B 1 140 ? 12.547 -21.726 33.487 1.00 43.67  ? 146 GLU   C N   1 
ATOM   2190 C  CA  . GLU   B 1 140 ? 11.524 -20.687 33.296 1.00 46.19  ? 146 GLU   C CA  1 
ATOM   2191 C  C   . GLU   B 1 140 ? 10.779 -20.876 31.999 1.00 48.63  ? 146 GLU   C C   1 
ATOM   2192 O  O   . GLU   B 1 140 ? 9.663  -21.399 32.030 1.00 50.51  ? 146 GLU   C O   1 
ATOM   2193 C  CB  . GLU   B 1 140 ? 12.098 -19.266 33.462 1.00 48.75  ? 146 GLU   C CB  1 
ATOM   2194 C  CG  . GLU   B 1 140 ? 11.369 -18.139 32.738 1.00 56.36  ? 146 GLU   C CG  1 
ATOM   2195 C  CD  . GLU   B 1 140 ? 10.207 -17.493 33.466 1.00 63.30  ? 146 GLU   C CD  1 
ATOM   2196 O  OE1 . GLU   B 1 140 ? 10.111 -16.246 33.428 1.00 65.42  ? 146 GLU   C OE1 1 
ATOM   2197 O  OE2 . GLU   B 1 140 ? 9.382  -18.227 34.055 1.00 65.74  ? 146 GLU   C OE2 1 
HETATM 2198 N  N1  . A1BPY C 2 .   ? 7.390  10.572  24.128 1.00 30.04  ? 201 A1BPY A N1  1 
HETATM 2199 N  N3  . A1BPY C 2 .   ? 10.753 15.450  17.521 1.00 22.10  ? 201 A1BPY A N3  1 
HETATM 2200 C  C4  . A1BPY C 2 .   ? 6.330  15.066  25.255 1.00 45.14  ? 201 A1BPY A C4  1 
HETATM 2201 C  C5  . A1BPY C 2 .   ? 5.755  16.032  26.057 1.00 48.96  ? 201 A1BPY A C5  1 
HETATM 2202 C  C6  . A1BPY C 2 .   ? 4.796  15.720  27.001 1.00 48.54  ? 201 A1BPY A C6  1 
HETATM 2203 C  C7  . A1BPY C 2 .   ? 4.427  14.394  27.129 1.00 47.71  ? 201 A1BPY A C7  1 
HETATM 2204 C  C8  . A1BPY C 2 .   ? 4.979  13.400  26.345 1.00 44.17  ? 201 A1BPY A C8  1 
HETATM 2205 C  C10 . A1BPY C 2 .   ? 8.677  13.982  23.675 1.00 27.46  ? 201 A1BPY A C10 1 
HETATM 2206 C  C13 . A1BPY C 2 .   ? 11.567 16.110  22.126 1.00 25.76  ? 201 A1BPY A C13 1 
HETATM 2207 C  C15 . A1BPY C 2 .   ? 10.453 15.862  19.873 1.00 24.67  ? 201 A1BPY A C15 1 
HETATM 2208 C  C17 . A1BPY C 2 .   ? 9.093  16.081  20.546 1.00 25.72  ? 201 A1BPY A C17 1 
HETATM 2209 O  O1  . A1BPY C 2 .   ? 9.924  17.445  18.145 1.00 24.76  ? 201 A1BPY A O1  1 
HETATM 2210 C  C16 . A1BPY C 2 .   ? 10.373 16.330  18.432 1.00 23.76  ? 201 A1BPY A C16 1 
HETATM 2211 C  C14 . A1BPY C 2 .   ? 11.541 16.600  20.675 1.00 24.90  ? 201 A1BPY A C14 1 
HETATM 2212 C  C12 . A1BPY C 2 .   ? 10.182 16.215  22.758 1.00 25.95  ? 201 A1BPY A C12 1 
HETATM 2213 N  N2  . A1BPY C 2 .   ? 9.161  15.570  21.915 1.00 26.17  ? 201 A1BPY A N2  1 
HETATM 2214 C  C11 . A1BPY C 2 .   ? 8.386  14.534  22.298 1.00 26.39  ? 201 A1BPY A C11 1 
HETATM 2215 O  O   . A1BPY C 2 .   ? 7.475  14.110  21.604 1.00 25.88  ? 201 A1BPY A O   1 
HETATM 2216 C  C9  . A1BPY C 2 .   ? 7.878  12.772  23.997 1.00 29.59  ? 201 A1BPY A C9  1 
HETATM 2217 N  N   . A1BPY C 2 .   ? 8.263  11.502  23.659 1.00 28.95  ? 201 A1BPY A N   1 
HETATM 2218 C  C   . A1BPY C 2 .   ? 9.462  11.082  22.941 1.00 28.31  ? 201 A1BPY A C   1 
HETATM 2219 C  C2  . A1BPY C 2 .   ? 6.719  12.652  24.726 1.00 33.74  ? 201 A1BPY A C2  1 
HETATM 2220 C  C1  . A1BPY C 2 .   ? 6.466  11.273  24.766 1.00 31.57  ? 201 A1BPY A C1  1 
HETATM 2221 C  C3  . A1BPY C 2 .   ? 5.959  13.731  25.415 1.00 41.05  ? 201 A1BPY A C3  1 
HETATM 2222 CL CL1 . A1BPY C 2 .   ? 3.291  13.951  28.375 1.00 50.12  ? 201 A1BPY A CL1 1 
HETATM 2223 CL CL  . A1BPY C 2 .   ? 6.235  17.702  25.857 1.00 52.83  ? 201 A1BPY A CL  1 
HETATM 2224 ZN ZN  . ZN    D 3 .   ? 11.212 -3.990  5.795  1.00 25.06  2 202 ZN    A ZN  1 
HETATM 2225 ZN ZN  . ZN    E 3 .   ? 30.711 -31.360 26.770 1.00 19.01  2 201 ZN    C ZN  1 
HETATM 2226 S  S   . DMS   F 4 .   ? 20.898 -32.377 10.527 1.00 101.13 ? 202 DMS   C S   1 
HETATM 2227 O  O   . DMS   F 4 .   ? 21.551 -32.013 9.232  1.00 101.06 ? 202 DMS   C O   1 
HETATM 2228 C  C1  . DMS   F 4 .   ? 22.165 -32.500 11.814 1.00 101.13 ? 202 DMS   C C1  1 
HETATM 2229 C  C2  . DMS   F 4 .   ? 20.162 -30.854 11.187 1.00 101.17 ? 202 DMS   C C2  1 
HETATM 2230 O  O   . HOH   G 5 .   ? 11.282 8.873   4.384  1.00 27.90  ? 301 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 5 .   ? 35.466 -3.920  8.047  1.00 27.14  ? 302 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 5 .   ? 15.932 -6.745  11.101 1.00 42.38  ? 303 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 5 .   ? 27.830 7.985   1.795  1.00 42.75  ? 304 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 5 .   ? 7.229  26.417  14.246 1.00 43.71  ? 305 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 5 .   ? 2.756  -3.361  20.725 1.00 30.73  ? 306 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 5 .   ? 21.932 2.355   -0.760 1.00 39.39  ? 307 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 5 .   ? 7.555  20.667  17.493 1.00 27.63  ? 308 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 5 .   ? 17.465 1.073   28.164 1.00 27.92  ? 309 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 5 .   ? 23.561 21.639  7.320  1.00 34.23  ? 310 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 5 .   ? 4.927  -3.711  28.988 1.00 34.72  ? 311 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 5 .   ? 19.253 10.095  19.684 1.00 17.38  ? 312 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 5 .   ? 19.296 20.270  21.683 1.00 47.25  ? 313 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 5 .   ? 6.302  17.936  21.395 1.00 49.54  ? 314 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 5 .   ? 8.541  25.432  23.575 1.00 39.53  ? 315 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 5 .   ? 2.951  9.397   9.020  1.00 34.36  ? 316 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 5 .   ? 5.526  5.398   32.696 1.00 28.84  ? 317 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 5 .   ? 8.993  19.497  19.685 1.00 24.93  ? 318 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 5 .   ? 33.819 14.231  9.784  1.00 40.58  ? 319 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 5 .   ? 7.329  -3.777  -1.338 1.00 69.62  ? 320 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 5 .   ? 36.363 18.223  14.317 1.00 36.82  ? 321 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 5 .   ? 16.527 3.954   23.558 1.00 23.07  ? 322 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 5 .   ? 12.286 22.244  12.285 1.00 45.87  ? 323 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 5 .   ? 18.434 21.863  9.534  1.00 26.41  ? 324 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 5 .   ? 4.474  9.821   27.877 1.00 33.38  ? 325 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 5 .   ? -0.160 1.220   15.722 1.00 17.10  ? 326 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 5 .   ? 24.704 5.329   21.369 1.00 36.06  ? 327 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 5 .   ? 31.620 -2.681  15.359 1.00 47.94  ? 328 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 5 .   ? 28.193 3.140   5.054  1.00 35.19  ? 329 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 5 .   ? 0.422  -1.208  19.307 1.00 33.98  ? 330 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 5 .   ? 30.413 10.455  15.721 1.00 36.34  ? 331 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 5 .   ? 29.224 12.087  21.214 1.00 37.25  ? 332 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 5 .   ? 22.996 13.384  24.042 1.00 44.14  ? 333 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 5 .   ? 35.304 11.176  12.284 1.00 56.08  ? 334 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 5 .   ? 31.519 20.175  11.783 1.00 28.89  ? 335 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 5 .   ? 1.048  8.075   6.326  1.00 42.65  ? 336 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 5 .   ? 28.897 16.072  4.467  1.00 34.59  ? 337 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 5 .   ? 28.987 3.450   12.755 1.00 23.88  ? 338 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 5 .   ? 11.333 12.668  11.200 1.00 22.49  ? 339 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 5 .   ? 26.996 -1.265  8.984  1.00 30.75  ? 340 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 5 .   ? 3.438  0.102   29.042 1.00 38.28  ? 341 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 5 .   ? 13.669 4.039   23.480 1.00 18.56  ? 342 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 5 .   ? 1.454  5.148   27.228 1.00 35.80  ? 343 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 5 .   ? 9.422  -8.075  21.594 1.00 42.95  ? 344 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 5 .   ? 22.657 0.922   17.537 1.00 24.00  ? 345 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 5 .   ? 29.923 11.745  18.437 1.00 38.56  ? 346 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 5 .   ? 3.866  -8.279  9.963  1.00 50.97  ? 347 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 5 .   ? 17.606 -5.096  12.202 1.00 40.54  ? 348 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 5 .   ? 22.926 -0.632  5.395  1.00 27.79  ? 349 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 5 .   ? 21.039 -4.170  14.204 1.00 23.48  ? 350 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 5 .   ? 13.282 11.357  9.223  1.00 19.10  ? 351 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 5 .   ? 20.744 -0.998  3.016  1.00 38.06  ? 352 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 5 .   ? 16.915 6.222   26.936 1.00 30.12  ? 353 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 5 .   ? 14.172 13.771  24.072 1.00 25.21  ? 354 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 5 .   ? 32.749 16.637  9.234  1.00 42.64  ? 355 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 5 .   ? 23.475 -6.472  12.321 1.00 47.04  ? 356 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 5 .   ? 10.694 5.339   3.317  1.00 31.51  ? 357 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 5 .   ? 16.226 2.174   30.181 1.00 31.34  ? 358 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 5 .   ? 34.698 22.255  18.269 1.00 35.08  ? 359 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 5 .   ? 11.657 17.818  4.761  1.00 40.59  ? 360 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 5 .   ? 10.091 10.344  31.307 1.00 30.17  ? 361 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 5 .   ? 17.711 20.015  17.060 1.00 22.90  ? 362 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 5 .   ? 32.067 8.805   7.826  1.00 27.93  ? 363 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 5 .   ? 20.917 -2.643  16.971 1.00 21.68  ? 364 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 5 .   ? 30.308 4.579   5.910  1.00 29.58  ? 365 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 5 .   ? 17.283 10.706  26.016 1.00 30.50  ? 366 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 5 .   ? 19.387 2.990   19.433 1.00 26.62  ? 367 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 5 .   ? 14.465 -2.496  17.897 1.00 22.31  ? 368 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 5 .   ? 33.700 11.136  15.809 1.00 45.92  ? 369 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 5 .   ? 11.573 -7.054  24.814 1.00 36.11  ? 370 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 5 .   ? 9.678  4.030   33.537 1.00 18.53  ? 371 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 5 .   ? 30.481 2.990   14.957 1.00 26.49  ? 372 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 5 .   ? 6.661  -7.043  23.795 1.00 28.25  ? 373 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 5 .   ? 6.154  -3.644  31.521 1.00 30.57  ? 374 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 5 .   ? 0.145  5.606   6.071  1.00 35.64  ? 375 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 5 .   ? 4.171  -4.228  6.065  1.00 33.29  ? 376 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 5 .   ? 15.159 14.880  26.334 1.00 39.03  ? 377 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 5 .   ? 36.253 -0.382  12.589 1.00 39.95  ? 378 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 5 .   ? 22.377 19.476  19.691 1.00 46.02  ? 379 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 5 .   ? 27.803 17.749  24.181 1.00 30.03  ? 380 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 5 .   ? 4.862  8.237   2.278  1.00 39.03  ? 381 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 5 .   ? 3.077  7.391   24.464 1.00 27.32  ? 382 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 5 .   ? 18.002 17.706  4.140  1.00 45.31  ? 383 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 5 .   ? 8.303  6.495   33.925 1.00 24.59  ? 384 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 5 .   ? 14.702 11.325  24.812 1.00 36.47  ? 385 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 5 .   ? 35.352 8.117   9.318  1.00 64.70  ? 386 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 5 .   ? 33.989 18.839  10.870 1.00 33.54  ? 387 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 5 .   ? 8.616  -6.519  9.678  1.00 37.93  ? 388 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 5 .   ? 30.152 -1.426  8.690  1.00 36.31  ? 389 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 5 .   ? 5.502  26.946  19.788 1.00 37.49  ? 390 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 5 .   ? 17.143 -3.503  27.901 1.00 36.80  ? 391 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 5 .   ? 4.098  -0.039  24.041 1.00 21.66  ? 392 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 5 .   ? 25.198 17.852  4.555  1.00 43.91  ? 393 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 5 .   ? 16.823 21.290  19.204 1.00 29.99  ? 394 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 5 .   ? 17.530 0.853   20.310 1.00 24.78  ? 395 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 5 .   ? 0.486  -1.391  9.391  1.00 45.83  ? 396 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 5 .   ? 14.099 25.552  25.878 1.00 37.47  ? 397 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 5 .   ? 19.543 -0.391  33.211 1.00 45.95  ? 398 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 5 .   ? 19.756 20.285  5.549  1.00 53.80  ? 399 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 5 .   ? 30.788 15.804  22.952 1.00 34.87  ? 400 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 5 .   ? 2.765  16.491  19.427 1.00 40.72  ? 401 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 5 .   ? 19.832 13.260  2.231  1.00 42.10  ? 402 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 5 .   ? 17.704 24.298  10.533 1.00 44.39  ? 403 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 5 .   ? 24.274 -3.467  16.410 1.00 40.82  ? 404 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 5 .   ? 15.436 15.210  3.703  1.00 41.93  ? 405 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 5 .   ? 15.230 21.764  8.114  1.00 39.65  ? 406 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 5 .   ? 34.120 7.748   16.672 1.00 38.03  ? 407 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 5 .   ? 27.451 -1.308  16.121 1.00 35.67  ? 408 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 5 .   ? 16.276 9.489   -1.689 1.00 30.39  ? 409 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 5 .   ? 23.419 8.408   21.722 1.00 29.18  ? 410 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 5 .   ? 16.920 -3.983  2.910  1.00 31.61  ? 411 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 5 .   ? 3.651  10.986  18.563 1.00 35.92  ? 412 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 5 .   ? 7.260  13.632  4.687  1.00 26.04  ? 413 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 5 .   ? 5.002  15.580  20.628 1.00 55.47  ? 414 HOH   A O   1 
HETATM 2344 O  O   . HOH   G 5 .   ? 33.826 5.285   16.731 1.00 37.34  ? 415 HOH   A O   1 
HETATM 2345 O  O   . HOH   G 5 .   ? 0.562  -1.321  16.676 1.00 27.22  ? 416 HOH   A O   1 
HETATM 2346 O  O   . HOH   G 5 .   ? 36.463 16.099  17.053 1.00 43.97  ? 417 HOH   A O   1 
HETATM 2347 O  O   . HOH   G 5 .   ? 23.237 19.147  6.359  1.00 24.86  ? 418 HOH   A O   1 
HETATM 2348 O  O   . HOH   G 5 .   ? 32.148 2.085   5.906  1.00 39.32  ? 419 HOH   A O   1 
HETATM 2349 O  O   . HOH   G 5 .   ? 37.155 2.418   9.997  1.00 52.03  ? 420 HOH   A O   1 
HETATM 2350 O  O   . HOH   G 5 .   ? 20.974 9.989   21.990 1.00 22.26  ? 421 HOH   A O   1 
HETATM 2351 O  O   . HOH   G 5 .   ? 17.215 -2.368  19.656 1.00 28.76  ? 422 HOH   A O   1 
HETATM 2352 O  O   . HOH   G 5 .   ? 1.221  -5.006  17.387 1.00 45.63  ? 423 HOH   A O   1 
HETATM 2353 O  O   . HOH   G 5 .   ? 9.340  3.486   2.857  1.00 47.91  ? 424 HOH   A O   1 
HETATM 2354 O  O   . HOH   G 5 .   ? 22.722 3.487   21.051 1.00 27.56  ? 425 HOH   A O   1 
HETATM 2355 O  O   . HOH   G 5 .   ? 15.311 -5.279  0.589  1.00 48.61  ? 426 HOH   A O   1 
HETATM 2356 O  O   . HOH   G 5 .   ? 20.210 -4.397  11.142 1.00 32.04  ? 427 HOH   A O   1 
HETATM 2357 O  O   . HOH   G 5 .   ? 38.227 1.311   12.067 1.00 53.84  ? 428 HOH   A O   1 
HETATM 2358 O  O   . HOH   G 5 .   ? 9.129  16.819  26.174 1.00 60.11  ? 429 HOH   A O   1 
HETATM 2359 O  O   . HOH   G 5 .   ? 25.353 -1.106  16.713 1.00 43.85  ? 430 HOH   A O   1 
HETATM 2360 O  O   . HOH   G 5 .   ? 31.903 7.222   5.594  1.00 37.29  ? 431 HOH   A O   1 
HETATM 2361 O  O   . HOH   G 5 .   ? 0.517  7.628   28.092 1.00 38.61  ? 432 HOH   A O   1 
HETATM 2362 O  O   . HOH   G 5 .   ? 19.163 -3.368  33.793 1.00 45.54  ? 433 HOH   A O   1 
HETATM 2363 O  O   . HOH   G 5 .   ? 14.037 -6.665  25.834 1.00 48.94  ? 434 HOH   A O   1 
HETATM 2364 O  O   . HOH   G 5 .   ? 30.761 13.199  23.116 1.00 42.44  ? 435 HOH   A O   1 
HETATM 2365 O  O   . HOH   G 5 .   ? 29.729 0.741   16.539 1.00 41.60  ? 436 HOH   A O   1 
HETATM 2366 O  O   . HOH   G 5 .   ? 2.398  -5.729  14.446 1.00 52.78  ? 437 HOH   A O   1 
HETATM 2367 O  O   . HOH   G 5 .   ? 21.815 14.758  1.482  1.00 53.09  ? 438 HOH   A O   1 
HETATM 2368 O  O   . HOH   G 5 .   ? 16.885 -4.935  34.437 1.00 39.34  ? 439 HOH   A O   1 
HETATM 2369 O  O   . HOH   G 5 .   ? 2.791  -0.480  26.466 1.00 31.01  ? 440 HOH   A O   1 
HETATM 2370 O  O   . HOH   G 5 .   ? 18.604 2.097   22.843 1.00 39.71  ? 441 HOH   A O   1 
HETATM 2371 O  O   . HOH   G 5 .   ? 18.522 -2.497  23.700 1.00 47.54  ? 442 HOH   A O   1 
HETATM 2372 O  O   . HOH   G 5 .   ? 0.104  -0.013  23.172 1.00 27.47  ? 443 HOH   A O   1 
HETATM 2373 O  O   . HOH   G 5 .   ? 23.753 0.961   19.940 1.00 40.05  ? 444 HOH   A O   1 
HETATM 2374 O  O   . HOH   G 5 .   ? 2.123  12.500  18.086 1.00 52.54  ? 445 HOH   A O   1 
HETATM 2375 O  O   . HOH   G 5 .   ? 21.194 11.392  24.471 1.00 34.92  ? 446 HOH   A O   1 
HETATM 2376 O  O   . HOH   G 5 .   ? 2.521  -1.644  22.681 1.00 30.79  ? 447 HOH   A O   1 
HETATM 2377 O  O   . HOH   G 5 .   ? 30.396 7.209   17.836 1.00 43.59  ? 448 HOH   A O   1 
HETATM 2378 O  O   . HOH   G 5 .   ? 31.163 4.736   17.009 1.00 33.40  ? 449 HOH   A O   1 
HETATM 2379 O  O   . HOH   G 5 .   ? 37.817 -4.540  7.008  1.00 33.55  ? 450 HOH   A O   1 
HETATM 2380 O  O   . HOH   G 5 .   ? 21.398 -1.044  18.971 1.00 40.98  ? 451 HOH   A O   1 
HETATM 2381 O  O   . HOH   G 5 .   ? 3.573  16.743  23.728 1.00 35.85  ? 452 HOH   A O   1 
HETATM 2382 O  O   . HOH   G 5 .   ? 12.485 -4.968  33.095 1.00 32.99  ? 453 HOH   A O   1 
HETATM 2383 O  O   . HOH   G 5 .   ? 0.253  13.546  19.839 1.00 47.89  ? 454 HOH   A O   1 
HETATM 2384 O  O   . HOH   G 5 .   ? 26.578 1.389   20.874 1.00 49.06  ? 455 HOH   A O   1 
HETATM 2385 O  O   . HOH   G 5 .   ? 1.614  -2.872  26.784 1.00 42.68  ? 456 HOH   A O   1 
HETATM 2386 O  O   . HOH   G 5 .   ? 1.264  -7.875  18.170 1.00 46.30  ? 457 HOH   A O   1 
HETATM 2387 O  O   . HOH   G 5 .   ? 4.135  -6.829  23.522 1.00 41.49  ? 458 HOH   A O   1 
HETATM 2388 O  O   . HOH   G 5 .   ? 6.062  13.759  30.120 1.00 55.59  ? 459 HOH   A O   1 
HETATM 2389 O  O   . HOH   G 5 .   ? 29.077 1.352   19.336 1.00 54.88  ? 460 HOH   A O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 31.068 -23.988 -1.322 1.00 27.57  ? 301 HOH   C O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 17.474 -33.383 24.281 1.00 51.83  ? 302 HOH   C O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 38.475 -7.364  7.220  1.00 27.28  ? 303 HOH   C O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? 29.374 -25.981 -1.113 1.00 31.63  ? 304 HOH   C O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 17.974 -27.567 16.675 1.00 24.05  ? 305 HOH   C O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 30.918 -18.359 26.923 1.00 25.11  ? 306 HOH   C O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 20.922 -18.816 13.015 1.00 19.71  ? 307 HOH   C O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 24.712 -5.814  15.490 1.00 33.17  ? 308 HOH   C O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 19.925 -4.193  20.379 1.00 25.14  ? 309 HOH   C O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 37.200 -32.339 10.929 1.00 31.80  ? 310 HOH   C O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 24.104 -8.123  9.575  1.00 28.84  ? 311 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? 18.077 -6.168  24.233 1.00 34.17  ? 312 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 26.743 -15.362 30.795 1.00 43.51  ? 313 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 36.301 -2.510  11.157 1.00 37.45  ? 314 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 39.274 -18.925 21.691 1.00 34.27  ? 315 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? 26.660 -5.539  10.036 1.00 30.66  ? 316 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? 10.321 -17.498 18.475 1.00 39.00  ? 317 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? 42.725 -11.472 11.211 1.00 35.16  ? 318 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? 23.146 -6.032  21.252 1.00 25.87  ? 319 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? 24.678 -9.722  27.057 1.00 42.18  ? 320 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? 40.438 -25.539 7.289  1.00 43.26  ? 321 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? 40.048 -29.897 11.907 1.00 35.71  ? 322 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? 14.976 -18.731 32.105 1.00 43.19  ? 323 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? 18.951 -8.788  13.861 1.00 36.81  ? 324 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? 31.196 -21.740 28.405 1.00 19.24  ? 325 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 5 .   ? 38.504 -26.874 28.464 1.00 37.07  ? 326 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 5 .   ? 15.029 -23.719 12.469 1.00 40.11  ? 327 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 5 .   ? 7.479  -30.313 21.704 1.00 48.84  ? 328 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 5 .   ? 20.098 -21.502 36.117 1.00 44.73  ? 329 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 5 .   ? 38.467 -29.452 33.172 1.00 58.88  ? 330 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 5 .   ? 10.904 -16.886 12.680 1.00 37.55  ? 331 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 5 .   ? 10.228 -8.883  23.796 1.00 37.85  ? 332 HOH   C O   1 
HETATM 2422 O  O   . HOH   H 5 .   ? 19.306 -27.808 28.307 1.00 25.68  ? 333 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 5 .   ? 24.176 -3.564  19.556 1.00 41.97  ? 334 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 5 .   ? 16.539 -17.256 11.143 1.00 47.63  ? 335 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 5 .   ? 14.070 -24.340 29.342 1.00 37.52  ? 336 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 5 .   ? 21.880 -28.557 4.862  1.00 35.27  ? 337 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 5 .   ? 23.698 -33.619 29.124 1.00 34.99  ? 338 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 5 .   ? 37.305 -10.485 4.927  1.00 42.22  ? 339 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 5 .   ? 37.391 -19.006 28.276 1.00 29.05  ? 340 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 5 .   ? 22.414 -23.576 6.021  1.00 50.39  ? 341 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 5 .   ? 28.414 -5.112  18.634 1.00 46.54  ? 342 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 5 .   ? 20.920 -25.709 13.877 1.00 32.25  ? 343 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 5 .   ? 10.987 -6.536  13.251 1.00 33.46  ? 344 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 5 .   ? 24.896 -15.907 7.356  1.00 26.51  ? 345 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 5 .   ? 32.175 -10.494 13.913 1.00 23.44  ? 346 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 5 .   ? 36.328 -26.462 34.435 1.00 38.67  ? 347 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 5 .   ? 12.089 -24.285 21.875 1.00 22.20  ? 348 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 5 .   ? 40.575 -27.561 15.147 1.00 16.99  ? 349 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 5 .   ? 10.608 -16.920 15.382 1.00 39.44  ? 350 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 5 .   ? 26.054 -25.375 8.855  1.00 19.12  ? 351 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 5 .   ? 36.396 -21.502 6.955  1.00 31.74  ? 352 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 5 .   ? 32.736 -23.937 29.282 1.00 20.43  ? 353 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 5 .   ? 29.764 -31.580 32.710 1.00 31.41  ? 354 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 5 .   ? 36.778 -16.433 12.569 1.00 39.50  ? 355 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 5 .   ? 6.896  -9.392  22.820 1.00 41.53  ? 356 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 5 .   ? 30.074 -15.362 19.667 1.00 21.38  ? 357 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 5 .   ? 25.786 -37.977 24.308 1.00 44.94  ? 358 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 5 .   ? 31.720 -35.413 31.765 1.00 42.96  ? 359 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 5 .   ? 28.345 -16.542 22.258 1.00 21.55  ? 360 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 5 .   ? 22.859 -28.030 12.762 1.00 28.35  ? 361 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 5 .   ? 29.914 -13.237 13.092 1.00 23.15  ? 362 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 5 .   ? 31.088 -6.123  6.075  1.00 42.16  ? 363 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 5 .   ? 23.144 -8.537  14.143 1.00 22.95  ? 364 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 5 .   ? 14.608 -28.774 25.671 1.00 40.44  ? 365 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 5 .   ? 35.293 -13.278 8.872  1.00 24.24  ? 366 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 5 .   ? 39.128 -33.882 13.840 1.00 50.07  ? 367 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 5 .   ? 35.730 -24.893 24.885 1.00 21.48  ? 368 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 5 .   ? 24.627 -16.301 2.863  1.00 46.09  ? 369 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 5 .   ? 38.974 -14.546 13.635 1.00 38.87  ? 370 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 5 .   ? 38.677 -13.622 10.915 1.00 36.65  ? 371 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 5 .   ? 37.462 -31.981 25.498 1.00 33.33  ? 372 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 5 .   ? 3.985  -8.559  14.670 1.00 32.94  ? 373 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 5 .   ? 30.452 -10.655 27.586 1.00 44.33  ? 374 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 5 .   ? 4.423  -10.435 19.986 1.00 44.26  ? 375 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 5 .   ? 33.119 -9.892  11.274 1.00 22.50  ? 376 HOH   C O   1 
HETATM 2466 O  O   . HOH   H 5 .   ? 26.999 -35.867 20.855 1.00 32.42  ? 377 HOH   C O   1 
HETATM 2467 O  O   . HOH   H 5 .   ? 31.113 -37.557 9.165  1.00 51.06  ? 378 HOH   C O   1 
HETATM 2468 O  O   . HOH   H 5 .   ? 30.442 -18.285 8.541  1.00 31.93  ? 379 HOH   C O   1 
HETATM 2469 O  O   . HOH   H 5 .   ? 43.410 -25.983 23.582 1.00 24.77  ? 380 HOH   C O   1 
HETATM 2470 O  O   . HOH   H 5 .   ? 31.455 -12.251 10.800 1.00 21.70  ? 381 HOH   C O   1 
HETATM 2471 O  O   . HOH   H 5 .   ? 21.803 -18.972 6.023  1.00 35.35  ? 382 HOH   C O   1 
HETATM 2472 O  O   . HOH   H 5 .   ? 10.991 -11.915 9.143  1.00 38.81  ? 383 HOH   C O   1 
HETATM 2473 O  O   . HOH   H 5 .   ? 35.252 -4.232  17.725 1.00 35.53  ? 384 HOH   C O   1 
HETATM 2474 O  O   . HOH   H 5 .   ? 4.973  -28.258 23.085 1.00 49.27  ? 385 HOH   C O   1 
HETATM 2475 O  O   . HOH   H 5 .   ? 39.013 -13.266 25.888 1.00 33.98  ? 386 HOH   C O   1 
HETATM 2476 O  O   . HOH   H 5 .   ? 30.519 -16.222 30.263 1.00 39.84  ? 387 HOH   C O   1 
HETATM 2477 O  O   . HOH   H 5 .   ? 26.900 -12.227 27.783 1.00 30.20  ? 388 HOH   C O   1 
HETATM 2478 O  O   . HOH   H 5 .   ? 34.509 -13.605 25.672 1.00 25.37  ? 389 HOH   C O   1 
HETATM 2479 O  O   . HOH   H 5 .   ? 33.703 -34.049 24.126 1.00 42.09  ? 390 HOH   C O   1 
HETATM 2480 O  O   . HOH   H 5 .   ? 11.657 -22.558 28.860 1.00 31.23  ? 391 HOH   C O   1 
HETATM 2481 O  O   . HOH   H 5 .   ? 26.692 -6.265  22.520 1.00 33.91  ? 392 HOH   C O   1 
HETATM 2482 O  O   . HOH   H 5 .   ? 35.746 -28.876 7.881  1.00 26.39  ? 393 HOH   C O   1 
HETATM 2483 O  O   . HOH   H 5 .   ? 22.909 -13.985 29.957 1.00 41.01  ? 394 HOH   C O   1 
HETATM 2484 O  O   . HOH   H 5 .   ? 10.237 -24.884 19.868 1.00 26.77  ? 395 HOH   C O   1 
HETATM 2485 O  O   . HOH   H 5 .   ? 10.148 -18.450 26.886 1.00 38.40  ? 396 HOH   C O   1 
HETATM 2486 O  O   . HOH   H 5 .   ? 28.891 -36.561 7.913  1.00 31.02  ? 397 HOH   C O   1 
HETATM 2487 O  O   . HOH   H 5 .   ? 26.433 -31.451 14.922 1.00 28.88  ? 398 HOH   C O   1 
HETATM 2488 O  O   . HOH   H 5 .   ? 18.841 -8.339  25.600 1.00 24.69  ? 399 HOH   C O   1 
HETATM 2489 O  O   . HOH   H 5 .   ? 23.316 -25.519 9.080  1.00 26.88  ? 400 HOH   C O   1 
HETATM 2490 O  O   . HOH   H 5 .   ? 33.132 -30.640 31.730 1.00 24.52  ? 401 HOH   C O   1 
HETATM 2491 O  O   . HOH   H 5 .   ? 26.124 -31.245 30.916 1.00 21.17  ? 402 HOH   C O   1 
HETATM 2492 O  O   . HOH   H 5 .   ? 39.345 -33.681 17.354 1.00 57.05  ? 403 HOH   C O   1 
HETATM 2493 O  O   . HOH   H 5 .   ? 37.161 -14.834 9.670  1.00 38.57  ? 404 HOH   C O   1 
HETATM 2494 O  O   . HOH   H 5 .   ? 15.468 -30.099 17.931 1.00 50.80  ? 405 HOH   C O   1 
HETATM 2495 O  O   . HOH   H 5 .   ? 38.511 -29.876 28.195 1.00 58.90  ? 406 HOH   C O   1 
HETATM 2496 O  O   . HOH   H 5 .   ? 17.220 -25.294 12.960 1.00 30.95  ? 407 HOH   C O   1 
HETATM 2497 O  O   . HOH   H 5 .   ? 31.890 -40.287 26.913 1.00 63.99  ? 408 HOH   C O   1 
HETATM 2498 O  O   . HOH   H 5 .   ? 20.561 -23.909 34.935 1.00 37.48  ? 409 HOH   C O   1 
HETATM 2499 O  O   . HOH   H 5 .   ? 8.952  -13.349 10.751 1.00 29.57  ? 410 HOH   C O   1 
HETATM 2500 O  O   . HOH   H 5 .   ? 36.680 -34.188 17.965 1.00 55.94  ? 411 HOH   C O   1 
HETATM 2501 O  O   . HOH   H 5 .   ? 39.973 -30.211 14.556 1.00 24.53  ? 412 HOH   C O   1 
HETATM 2502 O  O   . HOH   H 5 .   ? 31.486 -13.781 4.699  1.00 41.57  ? 413 HOH   C O   1 
HETATM 2503 O  O   . HOH   H 5 .   ? 36.501 -25.019 27.428 1.00 42.47  ? 414 HOH   C O   1 
HETATM 2504 O  O   . HOH   H 5 .   ? 6.685  -22.823 18.418 1.00 39.20  ? 415 HOH   C O   1 
HETATM 2505 O  O   . HOH   H 5 .   ? 31.486 -15.935 7.323  1.00 41.07  ? 416 HOH   C O   1 
HETATM 2506 O  O   . HOH   H 5 .   ? 32.914 -14.479 9.533  1.00 24.34  ? 417 HOH   C O   1 
HETATM 2507 O  O   . HOH   H 5 .   ? 23.795 -17.793 33.466 1.00 37.77  ? 418 HOH   C O   1 
HETATM 2508 O  O   . HOH   H 5 .   ? 16.591 -20.693 11.693 1.00 29.16  ? 419 HOH   C O   1 
HETATM 2509 O  O   . HOH   H 5 .   ? 35.049 -30.411 33.683 1.00 44.65  ? 420 HOH   C O   1 
HETATM 2510 O  O   . HOH   H 5 .   ? 34.256 -2.394  14.289 1.00 52.34  ? 421 HOH   C O   1 
HETATM 2511 O  O   . HOH   H 5 .   ? 20.566 -32.205 22.251 1.00 34.09  ? 422 HOH   C O   1 
HETATM 2512 O  O   . HOH   H 5 .   ? 22.928 -33.718 5.394  1.00 49.34  ? 423 HOH   C O   1 
HETATM 2513 O  O   . HOH   H 5 .   ? 36.931 -29.679 10.047 1.00 35.62  ? 424 HOH   C O   1 
HETATM 2514 O  O   . HOH   H 5 .   ? 34.287 -15.945 27.267 1.00 38.18  ? 425 HOH   C O   1 
HETATM 2515 O  O   . HOH   H 5 .   ? 6.542  -20.274 18.230 1.00 38.53  ? 426 HOH   C O   1 
HETATM 2516 O  O   . HOH   H 5 .   ? 18.869 -19.042 10.981 1.00 24.52  ? 427 HOH   C O   1 
HETATM 2517 O  O   . HOH   H 5 .   ? 13.017 -15.043 33.110 1.00 50.14  ? 428 HOH   C O   1 
HETATM 2518 O  O   . HOH   H 5 .   ? 35.276 -13.716 6.276  1.00 38.92  ? 429 HOH   C O   1 
HETATM 2519 O  O   . HOH   H 5 .   ? 9.926  -24.709 29.589 1.00 42.78  ? 430 HOH   C O   1 
HETATM 2520 O  O   . HOH   H 5 .   ? 6.786  -18.747 25.805 1.00 51.44  ? 431 HOH   C O   1 
HETATM 2521 O  O   . HOH   H 5 .   ? 5.826  -16.970 22.355 1.00 55.08  ? 432 HOH   C O   1 
HETATM 2522 O  O   . HOH   H 5 .   ? 34.750 -23.427 -0.952 1.00 41.41  ? 433 HOH   C O   1 
HETATM 2523 O  O   . HOH   H 5 .   ? 27.011 -37.872 28.526 1.00 48.33  ? 434 HOH   C O   1 
HETATM 2524 O  O   . HOH   H 5 .   ? 10.413 -20.018 29.010 1.00 40.31  ? 435 HOH   C O   1 
HETATM 2525 O  O   . HOH   H 5 .   ? 23.932 -16.000 31.441 1.00 41.52  ? 436 HOH   C O   1 
HETATM 2526 O  O   . HOH   H 5 .   ? 34.272 -32.083 29.499 1.00 28.82  ? 437 HOH   C O   1 
HETATM 2527 O  O   . HOH   H 5 .   ? 2.621  -26.381 22.894 1.00 55.40  ? 438 HOH   C O   1 
HETATM 2528 O  O   . HOH   H 5 .   ? 26.210 -35.699 7.472  1.00 35.71  ? 439 HOH   C O   1 
HETATM 2529 O  O   . HOH   H 5 .   ? 20.798 -19.286 35.956 1.00 44.68  ? 440 HOH   C O   1 
HETATM 2530 O  O   . HOH   H 5 .   ? 43.989 -25.541 26.158 1.00 37.60  ? 441 HOH   C O   1 
HETATM 2531 O  O   . HOH   H 5 .   ? 22.010 -2.772  20.355 1.00 45.54  ? 442 HOH   C O   1 
HETATM 2532 O  O   . HOH   H 5 .   ? 5.637  -10.264 9.749  1.00 57.29  ? 443 HOH   C O   1 
HETATM 2533 O  O   . HOH   H 5 .   ? 18.722 -26.241 10.537 1.00 42.65  ? 444 HOH   C O   1 
HETATM 2534 O  O   . HOH   H 5 .   ? 15.410 -16.345 32.879 1.00 52.51  ? 445 HOH   C O   1 
HETATM 2535 O  O   . HOH   H 5 .   ? 40.431 -28.561 7.619  1.00 46.92  ? 446 HOH   C O   1 
HETATM 2536 O  O   . HOH   H 5 .   ? 18.170 -17.897 8.508  1.00 47.70  ? 447 HOH   C O   1 
HETATM 2537 O  O   . HOH   H 5 .   ? 17.037 -29.081 28.784 1.00 42.77  ? 448 HOH   C O   1 
HETATM 2538 O  O   . HOH   H 5 .   ? 32.863 -19.784 29.361 1.00 31.15  ? 449 HOH   C O   1 
HETATM 2539 O  O   . HOH   H 5 .   ? 6.294  -12.655 10.689 1.00 47.08  ? 450 HOH   C O   1 
HETATM 2540 O  O   . HOH   H 5 .   ? 10.221 -21.157 16.601 1.00 42.20  ? 451 HOH   C O   1 
HETATM 2541 O  O   . HOH   H 5 .   ? 29.824 -16.219 32.872 1.00 39.31  ? 452 HOH   C O   1 
HETATM 2542 O  O   . HOH   H 5 .   ? 9.270  -23.302 17.748 1.00 36.61  ? 453 HOH   C O   1 
HETATM 2543 O  O   . HOH   H 5 .   ? 18.653 -16.675 38.375 1.00 34.95  ? 454 HOH   C O   1 
HETATM 2544 O  O   . HOH   H 5 .   ? 39.150 -2.446  10.887 1.00 39.73  ? 455 HOH   C O   1 
HETATM 2545 O  O   . HOH   H 5 .   ? 35.407 -23.293 29.085 1.00 31.85  ? 456 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   ? 0.2639 0.2221 0.3150 -0.0074 0.0186  -0.0123 7   SER   A N   
2    C  CA  . SER   A 1   ? 0.2736 0.2324 0.3303 -0.0056 0.0159  -0.0104 7   SER   A CA  
3    C  C   . SER   A 1   ? 0.2602 0.2201 0.3212 -0.0016 0.0132  -0.0058 7   SER   A C   
4    O  O   . SER   A 1   ? 0.2584 0.2186 0.3172 -0.0011 0.0123  -0.0037 7   SER   A O   
5    C  CB  . SER   A 1   ? 0.3127 0.2748 0.3660 -0.0107 0.0123  -0.0104 7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.3438 0.3098 0.3939 -0.0125 0.0077  -0.0060 7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.2421 0.2027 0.3094 0.0007  0.0124  -0.0047 8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.2259 0.1875 0.2979 0.0039  0.0110  -0.0019 8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.2197 0.1818 0.2975 0.0062  0.0129  -0.0025 8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.2172 0.1780 0.2953 0.0062  0.0156  -0.0039 8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.2005 0.1643 0.2835 0.0080  0.0119  -0.0012 9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.2075 0.1730 0.2952 0.0091  0.0140  -0.0021 9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.2045 0.1708 0.2955 0.0107  0.0150  -0.0022 9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.2193 0.1841 0.3110 0.0113  0.0137  -0.0011 9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.2116 0.1798 0.3036 0.0082  0.0124  -0.0021 9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.1908 0.1595 0.2841 0.0106  0.0177  -0.0034 10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.1827 0.1527 0.2795 0.0109  0.0199  -0.0052 10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.1899 0.1632 0.2941 0.0114  0.0203  -0.0063 10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.1884 0.1645 0.2928 0.0102  0.0203  -0.0061 10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.1981 0.1708 0.2915 0.0088  0.0228  -0.0061 10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.2151 0.1862 0.3025 0.0084  0.0224  -0.0042 10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.2073 0.1814 0.3033 0.0078  0.0260  -0.0095 10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.2114 0.1874 0.2964 0.0059  0.0242  -0.0030 10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.1974 0.1707 0.3087 0.0131  0.0208  -0.0073 11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.2091 0.1865 0.3295 0.0139  0.0218  -0.0085 11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.2048 0.1834 0.3293 0.0134  0.0272  -0.0131 11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.2119 0.1870 0.3412 0.0151  0.0286  -0.0144 11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.2132 0.1905 0.3414 0.0164  0.0182  -0.0053 11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.2098 0.1877 0.3330 0.0151  0.0133  -0.0017 11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.2147 0.1969 0.3389 0.0134  0.0122  -0.0016 11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.2257 0.1999 0.3424 0.0145  0.0104  0.0008  11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.2262 0.2085 0.3450 0.0110  0.0086  0.0004  11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.2336 0.2087 0.3446 0.0120  0.0070  0.0026  11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.2411 0.2198 0.3530 0.0102  0.0063  0.0021  11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.2526 0.2318 0.3583 0.0067  0.0037  0.0026  11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.2064 0.1895 0.3280 0.0104  0.0303  -0.0156 12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.2086 0.1945 0.3314 0.0078  0.0360  -0.0209 12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.2202 0.2128 0.3491 0.0067  0.0384  -0.0230 12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.2214 0.2175 0.3474 0.0052  0.0363  -0.0203 12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.2192 0.2064 0.3312 0.0034  0.0374  -0.0214 12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.2387 0.2292 0.3446 0.0015  0.0346  -0.0169 12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.2344 0.2258 0.3463 -0.0010 0.0436  -0.0276 12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.2270 0.2212 0.3660 0.0078  0.0429  -0.0277 13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.2110 0.2127 0.3573 0.0068  0.0458  -0.0301 13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.2131 0.2169 0.3633 0.0091  0.0405  -0.0248 13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.2071 0.2072 0.3613 0.0129  0.0361  -0.0209 13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.2006 0.2104 0.3480 0.0057  0.0405  -0.0242 14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.2048 0.2162 0.3541 0.0065  0.0356  -0.0196 14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.1975 0.2052 0.3353 0.0043  0.0318  -0.0156 14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.2044 0.2144 0.3412 0.0022  0.0299  -0.0134 14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.2271 0.2471 0.3840 0.0047  0.0380  -0.0213 14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.2881 0.3117 0.4604 0.0085  0.0405  -0.0238 14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.3085 0.3338 0.4895 0.0116  0.0366  -0.0201 14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.2990 0.3241 0.4754 0.0080  0.0473  -0.0298 14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.1883 0.1902 0.3188 0.0049  0.0309  -0.0148 15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.1982 0.1963 0.3198 0.0035  0.0281  -0.0111 15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.1909 0.1823 0.3100 0.0064  0.0246  -0.0092 15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.1977 0.1868 0.3188 0.0087  0.0247  -0.0102 15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.2020 0.2010 0.3165 0.0006  0.0305  -0.0111 15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.2164 0.2231 0.3310 -0.0039 0.0337  -0.0122 15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.2305 0.2401 0.3460 -0.0061 0.0328  -0.0096 15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.2337 0.2447 0.3470 -0.0068 0.0381  -0.0162 15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.2503 0.2677 0.3654 -0.0110 0.0357  -0.0100 15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.2506 0.2700 0.3627 -0.0122 0.0413  -0.0174 15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.2662 0.2891 0.3791 -0.0143 0.0398  -0.0138 15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.2830 0.3149 0.3944 -0.0204 0.0428  -0.0144 15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.1830 0.1713 0.2976 0.0057  0.0219  -0.0066 16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.1847 0.1675 0.2950 0.0070  0.0193  -0.0053 16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.1872 0.1670 0.2915 0.0060  0.0203  -0.0039 16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.1973 0.1771 0.3015 0.0042  0.0208  -0.0027 16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.1918 0.1744 0.3033 0.0062  0.0160  -0.0044 16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.2088 0.1864 0.3140 0.0057  0.0140  -0.0037 16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.2106 0.1899 0.3163 0.0034  0.0107  -0.0033 16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.2286 0.2035 0.3279 0.0005  0.0109  -0.0046 16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.2575 0.2297 0.3509 -0.0006 0.0097  -0.0049 16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.2634 0.2368 0.3565 0.0010  0.0076  -0.0030 16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.2637 0.2319 0.3521 -0.0037 0.0112  -0.0075 16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.1775 0.1548 0.2778 0.0070  0.0207  -0.0036 17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.1830 0.1586 0.2795 0.0065  0.0216  -0.0014 17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.1930 0.1635 0.2865 0.0076  0.0204  -0.0015 17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.1830 0.1521 0.2744 0.0086  0.0192  -0.0022 17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.1963 0.1746 0.2904 0.0060  0.0231  -0.0010 17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.1994 0.1786 0.2920 0.0053  0.0236  0.0028  17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.2049 0.1887 0.3009 0.0039  0.0251  -0.0029 17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.1842 0.1517 0.2778 0.0071  0.0210  -0.0008 18  VAL   A N   
86   C  CA  A VAL   A 12  ? 0.1813 0.1442 0.2720 0.0073  0.0211  -0.0021 18  VAL   A CA  
87   C  CA  B VAL   A 12  ? 0.2101 0.1728 0.3010 0.0071  0.0211  -0.0022 18  VAL   A CA  
88   C  C   . VAL   A 12  ? 0.1989 0.1593 0.2913 0.0080  0.0237  -0.0005 18  VAL   A C   
89   O  O   . VAL   A 12  ? 0.2055 0.1677 0.3019 0.0082  0.0247  0.0027  18  VAL   A O   
90   C  CB  A VAL   A 12  ? 0.1700 0.1310 0.2604 0.0051  0.0200  -0.0045 18  VAL   A CB  
91   C  CB  B VAL   A 12  ? 0.2536 0.2143 0.3449 0.0048  0.0204  -0.0045 18  VAL   A CB  
92   C  CG1 A VAL   A 12  ? 0.1669 0.1311 0.2568 0.0046  0.0167  -0.0049 18  VAL   A CG1 
93   C  CG1 B VAL   A 12  ? 0.2663 0.2249 0.3526 0.0031  0.0193  -0.0069 18  VAL   A CG1 
94   C  CG2 A VAL   A 12  ? 0.1391 0.0996 0.2335 0.0036  0.0212  -0.0042 18  VAL   A CG2 
95   C  CG2 B VAL   A 12  ? 0.2757 0.2406 0.3702 0.0037  0.0186  -0.0043 18  VAL   A CG2 
96   N  N   . ASN   A 13  ? 0.1967 0.1534 0.2869 0.0084  0.0250  -0.0023 19  ASN   A N   
97   C  CA  . ASN   A 13  ? 0.1916 0.1455 0.2861 0.0097  0.0283  -0.0011 19  ASN   A CA  
98   C  C   . ASN   A 13  ? 0.1976 0.1474 0.2964 0.0084  0.0299  -0.0020 19  ASN   A C   
99   O  O   . ASN   A 13  ? 0.2097 0.1571 0.3053 0.0057  0.0294  -0.0061 19  ASN   A O   
100  C  CB  . ASN   A 13  ? 0.1955 0.1461 0.2871 0.0096  0.0304  -0.0046 19  ASN   A CB  
101  C  CG  . ASN   A 13  ? 0.2146 0.1688 0.3022 0.0105  0.0292  -0.0035 19  ASN   A CG  
102  O  OD1 . ASN   A 13  ? 0.2281 0.1832 0.3097 0.0090  0.0266  -0.0050 19  ASN   A OD1 
103  N  ND2 . ASN   A 13  ? 0.1984 0.1549 0.2899 0.0126  0.0308  -0.0003 19  ASN   A ND2 
104  N  N   . ARG   A 14  ? 0.1892 0.1384 0.2953 0.0096  0.0316  0.0021  20  ARG   A N   
105  C  CA  . ARG   A 14  ? 0.1999 0.1441 0.3106 0.0079  0.0333  0.0015  20  ARG   A CA  
106  C  C   . ARG   A 14  ? 0.2343 0.1710 0.3443 0.0064  0.0367  -0.0048 20  ARG   A C   
107  O  O   . ARG   A 14  ? 0.2489 0.1825 0.3573 0.0030  0.0368  -0.0084 20  ARG   A O   
108  C  CB  . ARG   A 14  ? 0.2048 0.1490 0.3249 0.0098  0.0347  0.0083  20  ARG   A CB  
109  C  CG  . ARG   A 14  ? 0.2141 0.1532 0.3401 0.0079  0.0362  0.0092  20  ARG   A CG  
110  C  CD  . ARG   A 14  ? 0.2372 0.1764 0.3740 0.0100  0.0374  0.0176  20  ARG   A CD  
111  N  NE  . ARG   A 14  ? 0.2514 0.1864 0.3947 0.0081  0.0383  0.0207  20  ARG   A NE  
112  C  CZ  . ARG   A 14  ? 0.2947 0.2192 0.4450 0.0080  0.0426  0.0180  20  ARG   A CZ  
113  N  NH1 . ARG   A 14  ? 0.2926 0.2103 0.4430 0.0092  0.0467  0.0109  20  ARG   A NH1 
114  N  NH2 . ARG   A 14  ? 0.2956 0.2161 0.4527 0.0061  0.0433  0.0220  20  ARG   A NH2 
115  N  N   . HIS   A 15  ? 0.2289 0.1636 0.3392 0.0082  0.0395  -0.0068 21  HIS   A N   
116  C  CA  . HIS   A 15  ? 0.2384 0.1661 0.3479 0.0059  0.0441  -0.0140 21  HIS   A CA  
117  C  C   . HIS   A 15  ? 0.2629 0.1919 0.3613 0.0008  0.0418  -0.0199 21  HIS   A C   
118  O  O   . HIS   A 15  ? 0.2892 0.2132 0.3853 -0.0032 0.0452  -0.0264 21  HIS   A O   
119  C  CB  . HIS   A 15  ? 0.2425 0.1681 0.3565 0.0087  0.0488  -0.0151 21  HIS   A CB  
120  C  CG  . HIS   A 15  ? 0.2397 0.1708 0.3460 0.0089  0.0469  -0.0160 21  HIS   A CG  
121  N  ND1 . HIS   A 15  ? 0.2541 0.1918 0.3610 0.0120  0.0437  -0.0098 21  HIS   A ND1 
122  C  CD2 . HIS   A 15  ? 0.2556 0.1864 0.3538 0.0057  0.0483  -0.0222 21  HIS   A CD2 
123  C  CE1 . HIS   A 15  ? 0.2678 0.2082 0.3672 0.0110  0.0430  -0.0123 21  HIS   A CE1 
124  N  NE2 . HIS   A 15  ? 0.2767 0.2135 0.3709 0.0072  0.0456  -0.0193 21  HIS   A NE2 
125  N  N   . LEU   A 16  ? 0.2464 0.1822 0.3388 0.0007  0.0364  -0.0174 22  LEU   A N   
126  C  CA  . LEU   A 16  ? 0.2439 0.1827 0.3278 -0.0037 0.0330  -0.0205 22  LEU   A CA  
127  C  C   . LEU   A 16  ? 0.2590 0.2012 0.3433 -0.0056 0.0291  -0.0187 22  LEU   A C   
128  O  O   . LEU   A 16  ? 0.2649 0.2115 0.3443 -0.0087 0.0253  -0.0195 22  LEU   A O   
129  C  CB  . LEU   A 16  ? 0.2472 0.1909 0.3259 -0.0025 0.0300  -0.0186 22  LEU   A CB  
130  C  CG  . LEU   A 16  ? 0.2678 0.2096 0.3451 -0.0016 0.0338  -0.0207 22  LEU   A CG  
131  C  CD1 . LEU   A 16  ? 0.2706 0.2172 0.3423 -0.0011 0.0302  -0.0182 22  LEU   A CD1 
132  C  CD2 . LEU   A 16  ? 0.2874 0.2253 0.3604 -0.0068 0.0379  -0.0280 22  LEU   A CD2 
133  N  N   . ALA   A 17  ? 0.2501 0.1915 0.3410 -0.0038 0.0296  -0.0157 23  ALA   A N   
134  C  CA  . ALA   A 17  ? 0.2537 0.1992 0.3459 -0.0056 0.0265  -0.0142 23  ALA   A CA  
135  C  C   . ALA   A 17  ? 0.2610 0.2051 0.3502 -0.0115 0.0265  -0.0188 23  ALA   A C   
136  O  O   . ALA   A 17  ? 0.2716 0.2088 0.3604 -0.0141 0.0306  -0.0232 23  ALA   A O   
137  C  CB  . ALA   A 17  ? 0.2610 0.2058 0.3601 -0.0038 0.0278  -0.0102 23  ALA   A CB  
138  N  N   . THR   A 18  ? 0.2497 0.2007 0.3373 -0.0138 0.0220  -0.0179 24  THR   A N   
139  C  CA  . THR   A 18  ? 0.2551 0.2076 0.3396 -0.0204 0.0208  -0.0213 24  THR   A CA  
140  C  C   . THR   A 18  ? 0.2626 0.2139 0.3523 -0.0224 0.0219  -0.0210 24  THR   A C   
141  O  O   . THR   A 18  ? 0.2542 0.2053 0.3497 -0.0186 0.0226  -0.0174 24  THR   A O   
142  C  CB  . THR   A 18  ? 0.2759 0.2380 0.3583 -0.0217 0.0149  -0.0187 24  THR   A CB  
143  O  OG1 . THR   A 18  ? 0.2906 0.2583 0.3800 -0.0181 0.0127  -0.0144 24  THR   A OG1 
144  C  CG2 . THR   A 18  ? 0.2815 0.2452 0.3593 -0.0200 0.0132  -0.0176 24  THR   A CG2 
145  N  N   . HIS   A 19  ? 0.2731 0.2252 0.3603 -0.0293 0.0214  -0.0245 25  HIS   A N   
146  C  CA  . HIS   A 19  ? 0.2816 0.2337 0.3735 -0.0320 0.0218  -0.0241 25  HIS   A CA  
147  C  C   . HIS   A 19  ? 0.2678 0.2296 0.3648 -0.0289 0.0178  -0.0187 25  HIS   A C   
148  O  O   . HIS   A 19  ? 0.2676 0.2290 0.3699 -0.0278 0.0191  -0.0163 25  HIS   A O   
149  C  CB  . HIS   A 19  ? 0.3268 0.2801 0.4141 -0.0410 0.0212  -0.0289 25  HIS   A CB  
150  C  CG  . HIS   A 19  ? 0.4383 0.3942 0.5304 -0.0444 0.0206  -0.0277 25  HIS   A CG  
151  N  ND1 . HIS   A 19  ? 0.4959 0.4423 0.5920 -0.0455 0.0252  -0.0290 25  HIS   A ND1 
152  C  CD2 . HIS   A 19  ? 0.4848 0.4520 0.5794 -0.0464 0.0158  -0.0247 25  HIS   A CD2 
153  C  CE1 . HIS   A 19  ? 0.5041 0.4560 0.6033 -0.0491 0.0232  -0.0273 25  HIS   A CE1 
154  N  NE2 . HIS   A 19  ? 0.5158 0.4808 0.6146 -0.0496 0.0177  -0.0249 25  HIS   A NE2 
155  N  N   . ASN   A 20  ? 0.2546 0.2252 0.3507 -0.0277 0.0133  -0.0165 26  ASN   A N   
156  C  CA  . ASN   A 20  ? 0.2548 0.2342 0.3577 -0.0244 0.0106  -0.0123 26  ASN   A CA  
157  C  C   . ASN   A 20  ? 0.2416 0.2184 0.3478 -0.0184 0.0133  -0.0101 26  ASN   A C   
158  O  O   . ASN   A 20  ? 0.2417 0.2229 0.3532 -0.0175 0.0138  -0.0081 26  ASN   A O   
159  C  CB  . ASN   A 20  ? 0.2833 0.2714 0.3872 -0.0232 0.0059  -0.0098 26  ASN   A CB  
160  C  CG  . ASN   A 20  ? 0.3751 0.3723 0.4884 -0.0203 0.0042  -0.0065 26  ASN   A CG  
161  O  OD1 . ASN   A 20  ? 0.4068 0.4105 0.5246 -0.0237 0.0030  -0.0060 26  ASN   A OD1 
162  N  ND2 . ASN   A 20  ? 0.3961 0.3940 0.5130 -0.0144 0.0048  -0.0046 26  ASN   A ND2 
163  N  N   . ASP   A 21  ? 0.2310 0.2016 0.3337 -0.0152 0.0152  -0.0104 27  ASP   A N   
164  C  CA  . ASP   A 21  ? 0.2177 0.1870 0.3228 -0.0108 0.0174  -0.0078 27  ASP   A CA  
165  C  C   . ASP   A 21  ? 0.2193 0.1854 0.3277 -0.0123 0.0201  -0.0065 27  ASP   A C   
166  O  O   . ASP   A 21  ? 0.2343 0.2048 0.3460 -0.0113 0.0206  -0.0036 27  ASP   A O   
167  C  CB  . ASP   A 21  ? 0.2131 0.1768 0.3144 -0.0078 0.0189  -0.0081 27  ASP   A CB  
168  C  CG  . ASP   A 21  ? 0.2344 0.2012 0.3329 -0.0058 0.0163  -0.0080 27  ASP   A CG  
169  O  OD1 . ASP   A 21  ? 0.2165 0.1894 0.3184 -0.0040 0.0145  -0.0064 27  ASP   A OD1 
170  O  OD2 . ASP   A 21  ? 0.2318 0.1949 0.3255 -0.0060 0.0167  -0.0097 27  ASP   A OD2 
171  N  N   . TRP   A 22  ? 0.2171 0.1755 0.3247 -0.0152 0.0223  -0.0085 28  TRP   A N   
172  C  CA  . TRP   A 22  ? 0.2227 0.1769 0.3348 -0.0168 0.0249  -0.0063 28  TRP   A CA  
173  C  C   . TRP   A 22  ? 0.2313 0.1918 0.3462 -0.0205 0.0235  -0.0054 28  TRP   A C   
174  O  O   . TRP   A 22  ? 0.2480 0.2090 0.3667 -0.0212 0.0247  -0.0016 28  TRP   A O   
175  C  CB  . TRP   A 22  ? 0.2293 0.1725 0.3414 -0.0192 0.0284  -0.0097 28  TRP   A CB  
176  C  CG  . TRP   A 22  ? 0.2391 0.1760 0.3521 -0.0150 0.0312  -0.0092 28  TRP   A CG  
177  C  CD1 . TRP   A 22  ? 0.2640 0.1979 0.3726 -0.0142 0.0323  -0.0133 28  TRP   A CD1 
178  C  CD2 . TRP   A 22  ? 0.2503 0.1848 0.3695 -0.0114 0.0330  -0.0034 28  TRP   A CD2 
179  N  NE1 . TRP   A 22  ? 0.2684 0.1974 0.3810 -0.0099 0.0353  -0.0112 28  TRP   A NE1 
180  C  CE2 . TRP   A 22  ? 0.2676 0.1974 0.3871 -0.0080 0.0355  -0.0045 28  TRP   A CE2 
181  C  CE3 . TRP   A 22  ? 0.2632 0.2001 0.3878 -0.0113 0.0327  0.0032  28  TRP   A CE3 
182  C  CZ2 . TRP   A 22  ? 0.2767 0.2042 0.4033 -0.0041 0.0374  0.0011  28  TRP   A CZ2 
183  C  CZ3 . TRP   A 22  ? 0.2744 0.2094 0.4049 -0.0080 0.0341  0.0093  28  TRP   A CZ3 
184  C  CH2 . TRP   A 22  ? 0.2812 0.2116 0.4134 -0.0042 0.0364  0.0084  28  TRP   A CH2 
185  N  N   . ALA   A 23  ? 0.2283 0.1944 0.3417 -0.0234 0.0208  -0.0081 29  ALA   A N   
186  C  CA  . ALA   A 23  ? 0.2333 0.2069 0.3503 -0.0270 0.0195  -0.0073 29  ALA   A CA  
187  C  C   . ALA   A 23  ? 0.2282 0.2119 0.3491 -0.0238 0.0185  -0.0046 29  ALA   A C   
188  O  O   . ALA   A 23  ? 0.2302 0.2209 0.3552 -0.0264 0.0183  -0.0037 29  ALA   A O   
189  C  CB  . ALA   A 23  ? 0.2521 0.2297 0.3672 -0.0315 0.0167  -0.0105 29  ALA   A CB  
190  N  N   . ASN   A 24  ? 0.2115 0.1960 0.3312 -0.0188 0.0185  -0.0039 30  ASN   A N   
191  C  CA  . ASN   A 24  ? 0.2077 0.2006 0.3310 -0.0162 0.0188  -0.0027 30  ASN   A CA  
192  C  C   . ASN   A 24  ? 0.2056 0.1954 0.3263 -0.0135 0.0209  -0.0007 30  ASN   A C   
193  O  O   . ASN   A 24  ? 0.2057 0.1987 0.3262 -0.0105 0.0212  -0.0011 30  ASN   A O   
194  C  CB  . ASN   A 24  ? 0.2230 0.2210 0.3483 -0.0133 0.0164  -0.0041 30  ASN   A CB  
195  C  CG  . ASN   A 24  ? 0.2663 0.2706 0.3958 -0.0164 0.0139  -0.0046 30  ASN   A CG  
196  O  OD1 . ASN   A 24  ? 0.2712 0.2835 0.4069 -0.0176 0.0145  -0.0043 30  ASN   A OD1 
197  N  ND2 . ASN   A 24  ? 0.2870 0.2887 0.4129 -0.0190 0.0112  -0.0055 30  ASN   A ND2 
198  N  N   . LEU   A 25  ? 0.2025 0.1862 0.3221 -0.0149 0.0223  0.0019  31  LEU   A N   
199  C  CA  . LEU   A 25  ? 0.2018 0.1831 0.3199 -0.0129 0.0236  0.0052  31  LEU   A CA  
200  C  C   . LEU   A 25  ? 0.2155 0.2054 0.3341 -0.0140 0.0246  0.0076  31  LEU   A C   
201  O  O   . LEU   A 25  ? 0.2349 0.2302 0.3557 -0.0177 0.0253  0.0089  31  LEU   A O   
202  C  CB  . LEU   A 25  ? 0.1942 0.1672 0.3140 -0.0141 0.0249  0.0085  31  LEU   A CB  
203  C  CG  . LEU   A 25  ? 0.2227 0.1939 0.3430 -0.0119 0.0258  0.0134  31  LEU   A CG  
204  C  CD1 . LEU   A 25  ? 0.2287 0.1968 0.3459 -0.0078 0.0257  0.0110  31  LEU   A CD1 
205  C  CD2 . LEU   A 25  ? 0.2514 0.2146 0.3767 -0.0128 0.0274  0.0176  31  LEU   A CD2 
206  N  N   . VAL   A 26  ? 0.1984 0.1900 0.3143 -0.0116 0.0250  0.0080  32  VAL   A N   
207  C  CA  . VAL   A 26  ? 0.2029 0.2028 0.3175 -0.0139 0.0264  0.0099  32  VAL   A CA  
208  C  C   . VAL   A 26  ? 0.2166 0.2153 0.3301 -0.0147 0.0262  0.0164  32  VAL   A C   
209  O  O   . VAL   A 26  ? 0.2349 0.2393 0.3487 -0.0189 0.0265  0.0212  32  VAL   A O   
210  C  CB  . VAL   A 26  ? 0.2017 0.2053 0.3146 -0.0119 0.0273  0.0053  32  VAL   A CB  
211  C  CG1 . VAL   A 26  ? 0.2136 0.2253 0.3235 -0.0154 0.0294  0.0064  32  VAL   A CG1 
212  C  CG2 . VAL   A 26  ? 0.2179 0.2244 0.3351 -0.0109 0.0276  0.0004  32  VAL   A CG2 
213  N  N   . TRP   A 27  ? 0.2042 0.1962 0.3170 -0.0110 0.0255  0.0173  33  TRP   A N   
214  C  CA  . TRP   A 27  ? 0.2149 0.2068 0.3286 -0.0109 0.0252  0.0241  33  TRP   A CA  
215  C  C   . TRP   A 27  ? 0.2153 0.1983 0.3305 -0.0063 0.0252  0.0235  33  TRP   A C   
216  O  O   . TRP   A 27  ? 0.2072 0.1871 0.3195 -0.0038 0.0251  0.0178  33  TRP   A O   
217  C  CB  . TRP   A 27  ? 0.2233 0.2244 0.3326 -0.0128 0.0252  0.0251  33  TRP   A CB  
218  C  CG  . TRP   A 27  ? 0.2467 0.2501 0.3566 -0.0127 0.0242  0.0323  33  TRP   A CG  
219  C  CD1 . TRP   A 27  ? 0.2740 0.2833 0.3865 -0.0163 0.0231  0.0413  33  TRP   A CD1 
220  C  CD2 . TRP   A 27  ? 0.2451 0.2465 0.3537 -0.0094 0.0238  0.0318  33  TRP   A CD2 
221  N  NE1 . TRP   A 27  ? 0.2822 0.2938 0.3960 -0.0150 0.0218  0.0468  33  TRP   A NE1 
222  C  CE2 . TRP   A 27  ? 0.2592 0.2659 0.3704 -0.0107 0.0225  0.0407  33  TRP   A CE2 
223  C  CE3 . TRP   A 27  ? 0.2513 0.2476 0.3572 -0.0056 0.0243  0.0255  33  TRP   A CE3 
224  C  CZ2 . TRP   A 27  ? 0.2630 0.2708 0.3742 -0.0085 0.0219  0.0427  33  TRP   A CZ2 
225  C  CZ3 . TRP   A 27  ? 0.2542 0.2506 0.3591 -0.0037 0.0239  0.0272  33  TRP   A CZ3 
226  C  CH2 . TRP   A 27  ? 0.2565 0.2588 0.3643 -0.0050 0.0228  0.0355  33  TRP   A CH2 
227  N  N   . GLU   A 28  ? 0.2204 0.1994 0.3409 -0.0053 0.0255  0.0294  34  GLU   A N   
228  C  CA  . GLU   A 28  ? 0.2234 0.1948 0.3464 -0.0011 0.0266  0.0284  34  GLU   A CA  
229  C  C   . GLU   A 28  ? 0.2327 0.2059 0.3621 0.0001  0.0265  0.0372  34  GLU   A C   
230  O  O   . GLU   A 28  ? 0.2469 0.2237 0.3809 -0.0024 0.0257  0.0447  34  GLU   A O   
231  C  CB  . GLU   A 28  ? 0.2233 0.1842 0.3491 -0.0004 0.0284  0.0239  34  GLU   A CB  
232  C  CG  . GLU   A 28  ? 0.2384 0.1956 0.3703 -0.0029 0.0293  0.0275  34  GLU   A CG  
233  C  CD  . GLU   A 28  ? 0.3037 0.2555 0.4457 -0.0011 0.0311  0.0344  34  GLU   A CD  
234  O  OE1 . GLU   A 28  ? 0.2888 0.2407 0.4365 -0.0035 0.0309  0.0409  34  GLU   A OE1 
235  O  OE2 . GLU   A 28  ? 0.3018 0.2498 0.4470 0.0028  0.0328  0.0341  34  GLU   A OE2 
236  N  N   . ASP   A 29  ? 0.2112 0.1826 0.3421 0.0038  0.0272  0.0371  35  ASP   A N   
237  C  CA  . ASP   A 29  ? 0.2199 0.1940 0.3591 0.0055  0.0271  0.0461  35  ASP   A CA  
238  C  C   . ASP   A 29  ? 0.2283 0.1945 0.3722 0.0103  0.0300  0.0429  35  ASP   A C   
239  O  O   . ASP   A 29  ? 0.2321 0.1995 0.3700 0.0116  0.0300  0.0380  35  ASP   A O   
240  C  CB  . ASP   A 29  ? 0.2534 0.2403 0.3879 0.0029  0.0243  0.0509  35  ASP   A CB  
241  C  CG  . ASP   A 29  ? 0.3069 0.2999 0.4503 0.0037  0.0231  0.0620  35  ASP   A CG  
242  O  OD1 . ASP   A 29  ? 0.3409 0.3277 0.4939 0.0084  0.0251  0.0637  35  ASP   A OD1 
243  O  OD2 . ASP   A 29  ? 0.3395 0.3444 0.4807 -0.0008 0.0203  0.0689  35  ASP   A OD2 
244  N  N   . SER   A 30  ? 0.2404 0.1982 0.3952 0.0126  0.0330  0.0448  36  SER   A N   
245  C  CA  A SER   A 30  ? 0.2438 0.1938 0.4044 0.0168  0.0372  0.0408  36  SER   A CA  
246  C  CA  B SER   A 30  ? 0.2523 0.2023 0.4125 0.0168  0.0371  0.0406  36  SER   A CA  
247  C  C   . SER   A 30  ? 0.2446 0.2019 0.4096 0.0198  0.0366  0.0462  36  SER   A C   
248  O  O   . SER   A 30  ? 0.2504 0.2055 0.4133 0.0221  0.0388  0.0405  36  SER   A O   
249  C  CB  A SER   A 30  ? 0.2535 0.1929 0.4273 0.0184  0.0413  0.0424  36  SER   A CB  
250  C  CB  B SER   A 30  ? 0.2876 0.2265 0.4601 0.0183  0.0415  0.0412  36  SER   A CB  
251  O  OG  A SER   A 30  ? 0.2679 0.2004 0.4494 0.0225  0.0465  0.0386  36  SER   A OG  
252  O  OG  B SER   A 30  ? 0.3334 0.2758 0.5180 0.0190  0.0401  0.0534  36  SER   A OG  
253  N  N   . SER   A 31  ? 0.2334 0.2003 0.4043 0.0191  0.0334  0.0577  37  SER   A N   
254  C  CA  . SER   A 31  ? 0.2358 0.2115 0.4115 0.0213  0.0324  0.0639  37  SER   A CA  
255  C  C   . SER   A 31  ? 0.2277 0.2095 0.3897 0.0195  0.0306  0.0580  37  SER   A C   
256  O  O   . SER   A 31  ? 0.2516 0.2379 0.4161 0.0216  0.0309  0.0595  37  SER   A O   
257  C  CB  . SER   A 31  ? 0.2693 0.2565 0.4529 0.0195  0.0284  0.0782  37  SER   A CB  
258  O  OG  . SER   A 31  ? 0.3316 0.3289 0.5025 0.0133  0.0241  0.0793  37  SER   A OG  
259  N  N   . ARG   A 32  ? 0.2046 0.1866 0.3533 0.0158  0.0289  0.0516  38  ARG   A N   
260  C  CA  . ARG   A 32  ? 0.2005 0.1865 0.3372 0.0142  0.0276  0.0458  38  ARG   A CA  
261  C  C   . ARG   A 32  ? 0.2092 0.1859 0.3394 0.0157  0.0298  0.0350  38  ARG   A C   
262  O  O   . ARG   A 32  ? 0.1979 0.1766 0.3191 0.0146  0.0288  0.0304  38  ARG   A O   
263  C  CB  . ARG   A 32  ? 0.2149 0.2080 0.3425 0.0090  0.0247  0.0457  38  ARG   A CB  
264  C  CG  . ARG   A 32  ? 0.2189 0.2243 0.3491 0.0054  0.0219  0.0558  38  ARG   A CG  
265  C  CD  . ARG   A 32  ? 0.2242 0.2367 0.3448 -0.0008 0.0203  0.0542  38  ARG   A CD  
266  N  NE  . ARG   A 32  ? 0.2048 0.2194 0.3153 -0.0025 0.0205  0.0471  38  ARG   A NE  
267  C  CZ  . ARG   A 32  ? 0.2257 0.2496 0.3287 -0.0085 0.0196  0.0465  38  ARG   A CZ  
268  N  NH1 . ARG   A 32  ? 0.2527 0.2860 0.3557 -0.0139 0.0181  0.0529  38  ARG   A NH1 
269  N  NH2 . ARG   A 32  ? 0.2008 0.2246 0.2960 -0.0097 0.0205  0.0395  38  ARG   A NH2 
270  N  N   . ASP   A 33  ? 0.1905 0.1574 0.3244 0.0170  0.0326  0.0310  39  ASP   A N   
271  C  CA  . ASP   A 33  ? 0.1978 0.1573 0.3247 0.0168  0.0341  0.0215  39  ASP   A CA  
272  C  C   . ASP   A 33  ? 0.2044 0.1665 0.3212 0.0138  0.0310  0.0179  39  ASP   A C   
273  O  O   . ASP   A 33  ? 0.1999 0.1601 0.3095 0.0133  0.0306  0.0121  39  ASP   A O   
274  C  CB  . ASP   A 33  ? 0.2166 0.1748 0.3416 0.0186  0.0362  0.0174  39  ASP   A CB  
275  C  CG  . ASP   A 33  ? 0.2364 0.1879 0.3542 0.0172  0.0377  0.0085  39  ASP   A CG  
276  O  OD1 . ASP   A 33  ? 0.2474 0.1926 0.3664 0.0159  0.0393  0.0051  39  ASP   A OD1 
277  O  OD2 . ASP   A 33  ? 0.2303 0.1835 0.3409 0.0166  0.0370  0.0053  39  ASP   A OD2 
278  N  N   . LEU   A 34  ? 0.1847 0.1510 0.3017 0.0115  0.0291  0.0214  40  LEU   A N   
279  C  CA  . LEU   A 34  ? 0.1853 0.1544 0.2950 0.0090  0.0271  0.0176  40  LEU   A CA  
280  C  C   . LEU   A 34  ? 0.1936 0.1604 0.3046 0.0070  0.0270  0.0163  40  LEU   A C   
281  O  O   . LEU   A 34  ? 0.2053 0.1711 0.3222 0.0064  0.0277  0.0207  40  LEU   A O   
282  C  CB  . LEU   A 34  ? 0.1941 0.1725 0.3008 0.0068  0.0254  0.0208  40  LEU   A CB  
283  C  CG  . LEU   A 34  ? 0.2129 0.1949 0.3158 0.0073  0.0250  0.0206  40  LEU   A CG  
284  C  CD1 . LEU   A 34  ? 0.2126 0.2038 0.3120 0.0035  0.0240  0.0229  40  LEU   A CD1 
285  C  CD2 . LEU   A 34  ? 0.2261 0.2032 0.3234 0.0085  0.0250  0.0139  40  LEU   A CD2 
286  N  N   . LEU   A 35  ? 0.1847 0.1511 0.2910 0.0060  0.0260  0.0111  41  LEU   A N   
287  C  CA  . LEU   A 35  ? 0.1826 0.1491 0.2902 0.0036  0.0255  0.0098  41  LEU   A CA  
288  C  C   . LEU   A 35  ? 0.1881 0.1597 0.2921 0.0028  0.0241  0.0067  41  LEU   A C   
289  O  O   . LEU   A 35  ? 0.1929 0.1639 0.2937 0.0043  0.0233  0.0039  41  LEU   A O   
290  C  CB  . LEU   A 35  ? 0.1830 0.1419 0.2912 0.0031  0.0265  0.0059  41  LEU   A CB  
291  C  CG  . LEU   A 35  ? 0.1944 0.1537 0.3041 -0.0001 0.0259  0.0047  41  LEU   A CG  
292  C  CD1 . LEU   A 35  ? 0.2050 0.1561 0.3178 -0.0016 0.0282  0.0033  41  LEU   A CD1 
293  C  CD2 . LEU   A 35  ? 0.2039 0.1665 0.3099 -0.0010 0.0236  0.0005  41  LEU   A CD2 
294  N  N   . VAL   A 36  ? 0.1712 0.1480 0.2767 0.0004  0.0240  0.0075  42  VAL   A N   
295  C  CA  . VAL   A 36  ? 0.1794 0.1612 0.2843 -0.0001 0.0237  0.0041  42  VAL   A CA  
296  C  C   . VAL   A 36  ? 0.1832 0.1661 0.2914 -0.0019 0.0232  0.0026  42  VAL   A C   
297  O  O   . VAL   A 36  ? 0.1945 0.1781 0.3047 -0.0043 0.0238  0.0051  42  VAL   A O   
298  C  CB  . VAL   A 36  ? 0.1910 0.1802 0.2948 -0.0022 0.0250  0.0053  42  VAL   A CB  
299  C  CG1 . VAL   A 36  ? 0.2094 0.2030 0.3146 -0.0026 0.0261  0.0007  42  VAL   A CG1 
300  C  CG2 . VAL   A 36  ? 0.1996 0.1890 0.3000 -0.0013 0.0252  0.0070  42  VAL   A CG2 
301  N  N   . SER   A 37  ? 0.1746 0.1580 0.2839 -0.0009 0.0219  -0.0006 43  SER   A N   
302  C  CA  . SER   A 37  ? 0.1786 0.1650 0.2917 -0.0028 0.0211  -0.0018 43  SER   A CA  
303  C  C   . SER   A 37  ? 0.1995 0.1930 0.3173 -0.0019 0.0215  -0.0038 43  SER   A C   
304  O  O   . SER   A 37  ? 0.1935 0.1874 0.3110 0.0003  0.0223  -0.0050 43  SER   A O   
305  C  CB  . SER   A 37  ? 0.1882 0.1706 0.3004 -0.0033 0.0188  -0.0031 43  SER   A CB  
306  O  OG  . SER   A 37  ? 0.1984 0.1799 0.3088 -0.0009 0.0170  -0.0040 43  SER   A OG  
307  N  N   . SER   A 38  ? 0.2132 0.2122 0.3362 -0.0038 0.0216  -0.0044 44  SER   A N   
308  C  CA  . SER   A 38  ? 0.2188 0.2249 0.3488 -0.0026 0.0229  -0.0066 44  SER   A CA  
309  C  C   . SER   A 38  ? 0.2318 0.2387 0.3669 -0.0001 0.0197  -0.0066 44  SER   A C   
310  O  O   . SER   A 38  ? 0.2451 0.2502 0.3785 -0.0014 0.0164  -0.0052 44  SER   A O   
311  C  CB  . SER   A 38  ? 0.2440 0.2574 0.3784 -0.0060 0.0248  -0.0071 44  SER   A CB  
312  O  OG  . SER   A 38  ? 0.2551 0.2680 0.3902 -0.0082 0.0221  -0.0056 44  SER   A OG  
313  N  N   . THR   A 39  ? 0.2266 0.2365 0.3686 0.0031  0.0210  -0.0080 45  THR   A N   
314  C  CA  . THR   A 39  ? 0.2487 0.2604 0.3979 0.0058  0.0176  -0.0062 45  THR   A CA  
315  C  C   . THR   A 39  ? 0.2731 0.2934 0.4358 0.0073  0.0194  -0.0071 45  THR   A C   
316  O  O   . THR   A 39  ? 0.2659 0.2894 0.4318 0.0070  0.0245  -0.0107 45  THR   A O   
317  C  CB  . THR   A 39  ? 0.2615 0.2675 0.4092 0.0093  0.0173  -0.0059 45  THR   A CB  
318  O  OG1 . THR   A 39  ? 0.2780 0.2846 0.4297 0.0109  0.0224  -0.0094 45  THR   A OG1 
319  C  CG2 . THR   A 39  ? 0.2714 0.2699 0.4070 0.0081  0.0161  -0.0053 45  THR   A CG2 
320  N  N   . THR   A 40  ? 0.2828 0.3077 0.4540 0.0087  0.0153  -0.0037 46  THR   A N   
321  C  CA  . THR   A 40  ? 0.2991 0.3330 0.4862 0.0109  0.0169  -0.0037 46  THR   A CA  
322  C  C   . THR   A 40  ? 0.2975 0.3289 0.4939 0.0163  0.0197  -0.0046 46  THR   A C   
323  O  O   . THR   A 40  ? 0.3132 0.3482 0.5196 0.0181  0.0255  -0.0086 46  THR   A O   
324  C  CB  . THR   A 40  ? 0.3497 0.3914 0.5431 0.0095  0.0111  0.0013  46  THR   A CB  
325  O  OG1 . THR   A 40  ? 0.3971 0.4360 0.5885 0.0105  0.0055  0.0060  46  THR   A OG1 
326  C  CG2 . THR   A 40  ? 0.3662 0.4090 0.5503 0.0035  0.0094  0.0009  46  THR   A CG2 
327  N  N   . ALA   A 41  ? 0.2925 0.3172 0.4850 0.0182  0.0163  -0.0016 47  ALA   A N   
328  C  CA  . ALA   A 41  ? 0.3010 0.3218 0.5023 0.0230  0.0189  -0.0020 47  ALA   A CA  
329  C  C   . ALA   A 41  ? 0.2946 0.3072 0.4858 0.0223  0.0242  -0.0077 47  ALA   A C   
330  O  O   . ALA   A 41  ? 0.2907 0.2994 0.4670 0.0189  0.0232  -0.0084 47  ALA   A O   
331  C  CB  . ALA   A 41  ? 0.3210 0.3392 0.5233 0.0247  0.0124  0.0049  47  ALA   A CB  
332  N  N   . GLN   A 42  ? 0.2820 0.2926 0.4825 0.0251  0.0298  -0.0117 48  GLN   A N   
333  C  CA  . GLN   A 42  ? 0.2945 0.2984 0.4861 0.0236  0.0349  -0.0173 48  GLN   A CA  
334  C  C   . GLN   A 42  ? 0.2867 0.2818 0.4712 0.0247  0.0314  -0.0139 48  GLN   A C   
335  O  O   . GLN   A 42  ? 0.2909 0.2844 0.4840 0.0281  0.0277  -0.0088 48  GLN   A O   
336  C  CB  . GLN   A 42  ? 0.3274 0.3320 0.5312 0.0251  0.0433  -0.0241 48  GLN   A CB  
337  C  CG  . GLN   A 42  ? 0.3920 0.4049 0.5967 0.0216  0.0488  -0.0297 48  GLN   A CG  
338  C  CD  . GLN   A 42  ? 0.4780 0.4920 0.6945 0.0222  0.0582  -0.0380 48  GLN   A CD  
339  O  OE1 . GLN   A 42  ? 0.4820 0.4951 0.7163 0.0274  0.0604  -0.0379 48  GLN   A OE1 
340  N  NE2 . GLN   A 42  ? 0.5075 0.5241 0.7148 0.0164  0.0643  -0.0451 48  GLN   A NE2 
341  N  N   . GLY   A 43  ? 0.2653 0.2560 0.4349 0.0215  0.0321  -0.0160 49  GLY   A N   
342  C  CA  . GLY   A 43  ? 0.2529 0.2363 0.4151 0.0219  0.0292  -0.0133 49  GLY   A CA  
343  C  C   . GLY   A 43  ? 0.2465 0.2241 0.4108 0.0223  0.0344  -0.0178 49  GLY   A C   
344  O  O   . GLY   A 43  ? 0.2480 0.2273 0.4167 0.0212  0.0411  -0.0243 49  GLY   A O   
345  N  N   . CYS   A 44  ? 0.2316 0.2025 0.3923 0.0231  0.0318  -0.0148 50  CYS   A N   
346  C  CA  . CYS   A 44  ? 0.2323 0.1965 0.3953 0.0232  0.0364  -0.0186 50  CYS   A CA  
347  C  C   . CYS   A 44  ? 0.2304 0.1916 0.3787 0.0189  0.0378  -0.0213 50  CYS   A C   
348  O  O   . CYS   A 44  ? 0.2435 0.1992 0.3926 0.0178  0.0420  -0.0252 50  CYS   A O   
349  C  CB  . CYS   A 44  ? 0.2470 0.2057 0.4198 0.0272  0.0332  -0.0130 50  CYS   A CB  
350  S  SG  . CYS   A 44  ? 0.2896 0.2528 0.4847 0.0326  0.0323  -0.0090 50  CYS   A SG  
351  N  N   . ASP   A 45  ? 0.2037 0.1679 0.3394 0.0165  0.0343  -0.0189 51  ASP   A N   
352  C  CA  . ASP   A 45  ? 0.2107 0.1736 0.3342 0.0126  0.0353  -0.0204 51  ASP   A CA  
353  C  C   . ASP   A 45  ? 0.2267 0.1941 0.3472 0.0082  0.0412  -0.0268 51  ASP   A C   
354  O  O   . ASP   A 45  ? 0.2300 0.2029 0.3545 0.0076  0.0433  -0.0290 51  ASP   A O   
355  C  CB  . ASP   A 45  ? 0.2005 0.1656 0.3144 0.0120  0.0303  -0.0156 51  ASP   A CB  
356  C  CG  . ASP   A 45  ? 0.2265 0.1881 0.3402 0.0144  0.0249  -0.0101 51  ASP   A CG  
357  O  OD1 . ASP   A 45  ? 0.2318 0.1884 0.3479 0.0154  0.0244  -0.0089 51  ASP   A OD1 
358  O  OD2 . ASP   A 45  ? 0.2344 0.1985 0.3452 0.0146  0.0214  -0.0072 51  ASP   A OD2 
359  N  N   . THR   A 46  ? 0.2429 0.2090 0.3562 0.0042  0.0437  -0.0297 52  THR   A N   
360  C  CA  . THR   A 46  ? 0.2631 0.2349 0.3708 -0.0020 0.0488  -0.0352 52  THR   A CA  
361  C  C   . THR   A 46  ? 0.2582 0.2341 0.3536 -0.0057 0.0456  -0.0312 52  THR   A C   
362  O  O   . THR   A 46  ? 0.2618 0.2334 0.3536 -0.0045 0.0426  -0.0279 52  THR   A O   
363  C  CB  . THR   A 46  ? 0.3257 0.2928 0.4361 -0.0047 0.0550  -0.0424 52  THR   A CB  
364  O  OG1 . THR   A 46  ? 0.3669 0.3312 0.4915 -0.0009 0.0589  -0.0462 52  THR   A OG1 
365  C  CG2 . THR   A 46  ? 0.3604 0.3340 0.4616 -0.0132 0.0598  -0.0481 52  THR   A CG2 
366  N  N   . ILE   A 47  ? 0.2510 0.2356 0.3408 -0.0104 0.0464  -0.0311 53  ILE   A N   
367  C  CA  . ILE   A 47  ? 0.2350 0.2248 0.3158 -0.0137 0.0433  -0.0261 53  ILE   A CA  
368  C  C   . ILE   A 47  ? 0.2346 0.2279 0.3084 -0.0208 0.0465  -0.0297 53  ILE   A C   
369  O  O   . ILE   A 47  ? 0.2378 0.2346 0.3106 -0.0263 0.0518  -0.0363 53  ILE   A O   
370  C  CB  . ILE   A 47  ? 0.2228 0.2210 0.3020 -0.0155 0.0417  -0.0219 53  ILE   A CB  
371  C  CG1 . ILE   A 47  ? 0.2355 0.2306 0.3215 -0.0099 0.0394  -0.0197 53  ILE   A CG1 
372  C  CG2 . ILE   A 47  ? 0.2230 0.2261 0.2962 -0.0174 0.0380  -0.0149 53  ILE   A CG2 
373  C  CD1 . ILE   A 47  ? 0.2505 0.2387 0.3377 -0.0042 0.0349  -0.0153 53  ILE   A CD1 
374  N  N   . ALA   A 48  ? 0.2189 0.2120 0.2875 -0.0214 0.0435  -0.0256 54  ALA   A N   
375  C  CA  . ALA   A 48  ? 0.2179 0.2159 0.2789 -0.0289 0.0454  -0.0278 54  ALA   A CA  
376  C  C   . ALA   A 48  ? 0.2283 0.2396 0.2836 -0.0359 0.0452  -0.0252 54  ALA   A C   
377  O  O   . ALA   A 48  ? 0.2133 0.2294 0.2698 -0.0338 0.0414  -0.0181 54  ALA   A O   
378  C  CB  . ALA   A 48  ? 0.2191 0.2153 0.2771 -0.0274 0.0416  -0.0226 54  ALA   A CB  
379  N  N   . ARG   A 49  ? 0.2473 0.2649 0.2965 -0.0450 0.0495  -0.0309 55  ARG   A N   
380  C  CA  . ARG   A 49  ? 0.2638 0.2960 0.3062 -0.0536 0.0488  -0.0276 55  ARG   A CA  
381  C  C   . ARG   A 49  ? 0.2946 0.3325 0.3287 -0.0617 0.0491  -0.0283 55  ARG   A C   
382  O  O   . ARG   A 49  ? 0.3104 0.3484 0.3399 -0.0691 0.0547  -0.0374 55  ARG   A O   
383  C  CB  . ARG   A 49  ? 0.2640 0.3006 0.3059 -0.0589 0.0544  -0.0348 55  ARG   A CB  
384  C  CG  . ARG   A 49  ? 0.2666 0.2972 0.3177 -0.0508 0.0545  -0.0348 55  ARG   A CG  
385  C  CD  . ARG   A 49  ? 0.2682 0.3032 0.3214 -0.0470 0.0484  -0.0243 55  ARG   A CD  
386  N  NE  . ARG   A 49  ? 0.2596 0.2890 0.3210 -0.0404 0.0489  -0.0254 55  ARG   A NE  
387  C  CZ  . ARG   A 49  ? 0.2820 0.3098 0.3476 -0.0348 0.0444  -0.0182 55  ARG   A CZ  
388  N  NH1 . ARG   A 49  ? 0.2654 0.2960 0.3292 -0.0341 0.0395  -0.0093 55  ARG   A NH1 
389  N  NH2 . ARG   A 49  ? 0.2827 0.3063 0.3552 -0.0301 0.0450  -0.0199 55  ARG   A NH2 
390  N  N   . CYS   A 50  ? 0.3000 0.3417 0.3333 -0.0599 0.0436  -0.0194 56  CYS   A N   
391  C  CA  . CYS   A 50  ? 0.3183 0.3648 0.3453 -0.0663 0.0430  -0.0189 56  CYS   A CA  
392  C  C   . CYS   A 50  ? 0.3211 0.3762 0.3495 -0.0643 0.0364  -0.0066 56  CYS   A C   
393  O  O   . CYS   A 50  ? 0.3237 0.3794 0.3583 -0.0578 0.0329  0.0008  56  CYS   A O   
394  C  CB  . CYS   A 50  ? 0.3275 0.3593 0.3569 -0.0616 0.0453  -0.0251 56  CYS   A CB  
395  S  SG  . CYS   A 50  ? 0.3153 0.3366 0.3532 -0.0483 0.0404  -0.0181 56  CYS   A SG  
396  N  N   . ASP   A 51  ? 0.3358 0.3971 0.3596 -0.0697 0.0350  -0.0047 57  ASP   A N   
397  C  CA  A ASP   A 51  ? 0.3414 0.4105 0.3688 -0.0669 0.0294  0.0066  57  ASP   A CA  
398  C  CA  B ASP   A 51  ? 0.3405 0.4100 0.3678 -0.0672 0.0294  0.0066  57  ASP   A CA  
399  C  C   . ASP   A 51  ? 0.3442 0.4055 0.3727 -0.0630 0.0291  0.0054  57  ASP   A C   
400  O  O   . ASP   A 51  ? 0.3526 0.4229 0.3815 -0.0649 0.0260  0.0120  57  ASP   A O   
401  C  CB  A ASP   A 51  ? 0.3790 0.4683 0.4019 -0.0772 0.0263  0.0142  57  ASP   A CB  
402  C  CB  B ASP   A 51  ? 0.3755 0.4649 0.3974 -0.0782 0.0267  0.0133  57  ASP   A CB  
403  C  CG  A ASP   A 51  ? 0.4526 0.5488 0.4661 -0.0882 0.0279  0.0097  57  ASP   A CG  
404  C  CG  B ASP   A 51  ? 0.4365 0.5363 0.4660 -0.0745 0.0207  0.0272  57  ASP   A CG  
405  O  OD1 A ASP   A 51  ? 0.4666 0.5528 0.4749 -0.0912 0.0334  -0.0022 57  ASP   A OD1 
406  O  OD1 B ASP   A 51  ? 0.4560 0.5471 0.4950 -0.0633 0.0193  0.0310  57  ASP   A OD1 
407  O  OD2 A ASP   A 51  ? 0.4889 0.6006 0.5012 -0.0940 0.0238  0.0182  57  ASP   A OD2 
408  O  OD2 B ASP   A 51  ? 0.4583 0.5753 0.4850 -0.0831 0.0176  0.0342  57  ASP   A OD2 
409  N  N   . CYS   A 52  ? 0.3188 0.3639 0.3490 -0.0573 0.0321  -0.0021 58  CYS   A N   
410  C  CA  . CYS   A 52  ? 0.2874 0.3239 0.3187 -0.0534 0.0318  -0.0029 58  CYS   A CA  
411  C  C   . CYS   A 52  ? 0.2655 0.3053 0.3029 -0.0467 0.0277  0.0062  58  CYS   A C   
412  O  O   . CYS   A 52  ? 0.2714 0.3117 0.3147 -0.0409 0.0260  0.0108  58  CYS   A O   
413  C  CB  . CYS   A 52  ? 0.2702 0.2898 0.3044 -0.0473 0.0346  -0.0098 58  CYS   A CB  
414  S  SG  . CYS   A 52  ? 0.3073 0.3188 0.3372 -0.0541 0.0410  -0.0218 58  CYS   A SG  
415  N  N   A GLN   A 53  ? 0.2432 0.2856 0.2797 -0.0478 0.0264  0.0086  59  GLN   A N   
416  N  N   B GLN   A 53  ? 0.2456 0.2872 0.2821 -0.0476 0.0266  0.0082  59  GLN   A N   
417  C  CA  A GLN   A 53  ? 0.2247 0.2694 0.2679 -0.0413 0.0237  0.0158  59  GLN   A CA  
418  C  CA  B GLN   A 53  ? 0.2290 0.2727 0.2723 -0.0409 0.0239  0.0154  59  GLN   A CA  
419  C  C   A GLN   A 53  ? 0.2154 0.2482 0.2583 -0.0372 0.0248  0.0123  59  GLN   A C   
420  C  C   B GLN   A 53  ? 0.2170 0.2502 0.2597 -0.0374 0.0248  0.0123  59  GLN   A C   
421  O  O   A GLN   A 53  ? 0.2140 0.2496 0.2608 -0.0338 0.0235  0.0167  59  GLN   A O   
422  O  O   B GLN   A 53  ? 0.2141 0.2505 0.2608 -0.0342 0.0234  0.0169  59  GLN   A O   
423  C  CB  A GLN   A 53  ? 0.2269 0.2886 0.2718 -0.0459 0.0210  0.0241  59  GLN   A CB  
424  C  CB  B GLN   A 53  ? 0.2407 0.3018 0.2868 -0.0446 0.0209  0.0245  59  GLN   A CB  
425  C  CG  A GLN   A 53  ? 0.2392 0.3127 0.2904 -0.0453 0.0183  0.0327  59  GLN   A CG  
426  C  CG  B GLN   A 53  ? 0.2641 0.3348 0.3117 -0.0473 0.0194  0.0290  59  GLN   A CG  
427  C  CD  A GLN   A 53  ? 0.2571 0.3477 0.3139 -0.0478 0.0149  0.0431  59  GLN   A CD  
428  C  CD  B GLN   A 53  ? 0.2940 0.3573 0.3488 -0.0389 0.0193  0.0307  59  GLN   A CD  
429  O  OE1 A GLN   A 53  ? 0.2713 0.3766 0.3246 -0.0566 0.0129  0.0473  59  GLN   A OE1 
430  O  OE1 B GLN   A 53  ? 0.2576 0.3213 0.3115 -0.0402 0.0197  0.0299  59  GLN   A OE1 
431  N  NE2 A GLN   A 53  ? 0.2375 0.3274 0.3039 -0.0402 0.0145  0.0478  59  GLN   A NE2 
432  N  NE2 B GLN   A 53  ? 0.3030 0.3601 0.3649 -0.0307 0.0191  0.0327  59  GLN   A NE2 
433  N  N   . THR   A 54  ? 0.2081 0.2289 0.2469 -0.0382 0.0273  0.0047  60  THR   A N   
434  C  CA  . THR   A 54  ? 0.2308 0.2403 0.2692 -0.0350 0.0278  0.0023  60  THR   A CA  
435  C  C   . THR   A 54  ? 0.2311 0.2279 0.2716 -0.0304 0.0291  -0.0022 60  THR   A C   
436  O  O   . THR   A 54  ? 0.2459 0.2413 0.2862 -0.0325 0.0312  -0.0065 60  THR   A O   
437  C  CB  . THR   A 54  ? 0.2898 0.2982 0.3226 -0.0417 0.0291  -0.0006 60  THR   A CB  
438  O  OG1 . THR   A 54  ? 0.3398 0.3437 0.3689 -0.0473 0.0323  -0.0074 60  THR   A OG1 
439  C  CG2 . THR   A 54  ? 0.2791 0.3016 0.3101 -0.0469 0.0276  0.0041  60  THR   A CG2 
440  N  N   . GLY   A 55  ? 0.2038 0.1931 0.2469 -0.0246 0.0279  -0.0010 61  GLY   A N   
441  C  CA  . GLY   A 55  ? 0.2038 0.1825 0.2500 -0.0203 0.0283  -0.0038 61  GLY   A CA  
442  C  C   . GLY   A 55  ? 0.2013 0.1734 0.2484 -0.0162 0.0265  -0.0018 61  GLY   A C   
443  O  O   . GLY   A 55  ? 0.2090 0.1828 0.2533 -0.0177 0.0258  0.0003  61  GLY   A O   
444  N  N   . VAL   A 56  ? 0.1969 0.1626 0.2475 -0.0118 0.0256  -0.0022 62  VAL   A N   
445  C  CA  . VAL   A 56  ? 0.1950 0.1555 0.2457 -0.0091 0.0235  0.0001  62  VAL   A CA  
446  C  C   . VAL   A 56  ? 0.1904 0.1514 0.2442 -0.0047 0.0222  0.0011  62  VAL   A C   
447  O  O   . VAL   A 56  ? 0.2019 0.1626 0.2593 -0.0032 0.0227  -0.0006 62  VAL   A O   
448  C  CB  . VAL   A 56  ? 0.2140 0.1651 0.2669 -0.0094 0.0234  -0.0009 62  VAL   A CB  
449  C  CG1 . VAL   A 56  ? 0.2529 0.2001 0.3063 -0.0071 0.0202  0.0028  62  VAL   A CG1 
450  C  CG2 . VAL   A 56  ? 0.2113 0.1602 0.2611 -0.0144 0.0251  -0.0023 62  VAL   A CG2 
451  N  N   . TYR   A 57  ? 0.1821 0.1445 0.2342 -0.0034 0.0210  0.0032  63  TYR   A N   
452  C  CA  . TYR   A 57  ? 0.1745 0.1367 0.2290 -0.0002 0.0201  0.0032  63  TYR   A CA  
453  C  C   . TYR   A 57  ? 0.1897 0.1482 0.2422 -0.0002 0.0178  0.0045  63  TYR   A C   
454  O  O   . TYR   A 57  ? 0.1954 0.1533 0.2440 -0.0025 0.0172  0.0059  63  TYR   A O   
455  C  CB  . TYR   A 57  ? 0.1670 0.1351 0.2227 0.0010  0.0217  0.0038  63  TYR   A CB  
456  C  CG  . TYR   A 57  ? 0.1786 0.1486 0.2318 0.0004  0.0225  0.0044  63  TYR   A CG  
457  C  CD1 . TYR   A 57  ? 0.1999 0.1736 0.2509 -0.0019 0.0233  0.0055  63  TYR   A CD1 
458  C  CD2 . TYR   A 57  ? 0.1835 0.1523 0.2367 0.0016  0.0230  0.0033  63  TYR   A CD2 
459  C  CE1 . TYR   A 57  ? 0.1920 0.1683 0.2413 -0.0026 0.0247  0.0056  63  TYR   A CE1 
460  C  CE2 . TYR   A 57  ? 0.1894 0.1604 0.2403 0.0005  0.0248  0.0026  63  TYR   A CE2 
461  C  CZ  . TYR   A 57  ? 0.1964 0.1713 0.2458 -0.0013 0.0258  0.0039  63  TYR   A CZ  
462  O  OH  . TYR   A 57  ? 0.2217 0.1996 0.2694 -0.0027 0.0282  0.0029  63  TYR   A OH  
463  N  N   . TYR   A 58  ? 0.1946 0.1519 0.2493 0.0016  0.0165  0.0043  64  TYR   A N   
464  C  CA  . TYR   A 58  ? 0.1959 0.1518 0.2482 0.0005  0.0139  0.0059  64  TYR   A CA  
465  C  C   . TYR   A 58  ? 0.1903 0.1493 0.2390 -0.0004 0.0153  0.0043  64  TYR   A C   
466  O  O   . TYR   A 58  ? 0.1974 0.1576 0.2488 0.0014  0.0171  0.0022  64  TYR   A O   
467  C  CB  . TYR   A 58  ? 0.1984 0.1525 0.2555 0.0020  0.0113  0.0069  64  TYR   A CB  
468  C  CG  . TYR   A 58  ? 0.2070 0.1616 0.2611 -0.0004 0.0077  0.0098  64  TYR   A CG  
469  C  CD1 . TYR   A 58  ? 0.2268 0.1800 0.2786 -0.0027 0.0053  0.0137  64  TYR   A CD1 
470  C  CD2 . TYR   A 58  ? 0.2105 0.1676 0.2639 -0.0011 0.0066  0.0090  64  TYR   A CD2 
471  C  CE1 . TYR   A 58  ? 0.2390 0.1944 0.2873 -0.0061 0.0015  0.0175  64  TYR   A CE1 
472  C  CE2 . TYR   A 58  ? 0.2255 0.1848 0.2746 -0.0049 0.0032  0.0117  64  TYR   A CE2 
473  C  CZ  . TYR   A 58  ? 0.2447 0.2036 0.2914 -0.0074 0.0003  0.0164  64  TYR   A CZ  
474  O  OH  . TYR   A 58  ? 0.2678 0.2305 0.3099 -0.0121 -0.0037 0.0202  64  TYR   A OH  
475  N  N   . CYS   A 59  ? 0.1920 0.1519 0.2348 -0.0038 0.0147  0.0053  65  CYS   A N   
476  C  CA  . CYS   A 59  ? 0.2064 0.1692 0.2451 -0.0058 0.0171  0.0026  65  CYS   A CA  
477  C  C   . CYS   A 59  ? 0.2180 0.1812 0.2520 -0.0095 0.0142  0.0033  65  CYS   A C   
478  O  O   . CYS   A 59  ? 0.2307 0.1948 0.2598 -0.0131 0.0116  0.0065  65  CYS   A O   
479  C  CB  . CYS   A 59  ? 0.2098 0.1754 0.2452 -0.0077 0.0195  0.0025  65  CYS   A CB  
480  S  SG  . CYS   A 59  ? 0.2281 0.1975 0.2593 -0.0106 0.0240  -0.0020 65  CYS   A SG  
481  N  N   . SER   A 60  ? 0.2216 0.1849 0.2567 -0.0094 0.0143  0.0010  66  SER   A N   
482  C  CA  . SER   A 60  ? 0.2245 0.1898 0.2549 -0.0140 0.0108  0.0022  66  SER   A CA  
483  C  C   . SER   A 60  ? 0.2371 0.2061 0.2582 -0.0203 0.0124  0.0003  66  SER   A C   
484  O  O   . SER   A 60  ? 0.2428 0.2148 0.2583 -0.0254 0.0082  0.0039  66  SER   A O   
485  C  CB  . SER   A 60  ? 0.2385 0.2036 0.2715 -0.0136 0.0108  -0.0004 66  SER   A CB  
486  O  OG  . SER   A 60  ? 0.2740 0.2385 0.3068 -0.0137 0.0163  -0.0065 66  SER   A OG  
487  N  N   . SER   A 61  ? 0.2140 0.1834 0.2343 -0.0200 0.0185  -0.0050 67  SER   A N   
488  C  CA  . SER   A 61  ? 0.2063 0.1796 0.2183 -0.0262 0.0215  -0.0082 67  SER   A CA  
489  C  C   . SER   A 61  ? 0.1957 0.1715 0.2024 -0.0293 0.0191  -0.0036 67  SER   A C   
490  O  O   . SER   A 61  ? 0.2129 0.1931 0.2118 -0.0355 0.0211  -0.0056 67  SER   A O   
491  C  CB  . SER   A 61  ? 0.2250 0.1980 0.2401 -0.0246 0.0294  -0.0153 67  SER   A CB  
492  O  OG  . SER   A 61  ? 0.2256 0.1980 0.2478 -0.0189 0.0314  -0.0136 67  SER   A OG  
493  N  N   . ARG   A 62  ? 0.1951 0.1683 0.2060 -0.0259 0.0152  0.0023  68  ARG   A N   
494  C  CA  . ARG   A 62  ? 0.2064 0.1805 0.2133 -0.0289 0.0125  0.0075  68  ARG   A CA  
495  C  C   . ARG   A 62  ? 0.2342 0.2053 0.2441 -0.0283 0.0058  0.0150  68  ARG   A C   
496  O  O   . ARG   A 62  ? 0.2494 0.2198 0.2576 -0.0305 0.0032  0.0203  68  ARG   A O   
497  C  CB  . ARG   A 62  ? 0.2174 0.1904 0.2282 -0.0254 0.0157  0.0069  68  ARG   A CB  
498  C  CG  . ARG   A 62  ? 0.2366 0.2137 0.2469 -0.0256 0.0224  0.0010  68  ARG   A CG  
499  C  CD  . ARG   A 62  ? 0.2299 0.2121 0.2314 -0.0326 0.0237  0.0006  68  ARG   A CD  
500  N  NE  . ARG   A 62  ? 0.2430 0.2294 0.2462 -0.0322 0.0311  -0.0056 68  ARG   A NE  
501  C  CZ  . ARG   A 62  ? 0.2633 0.2515 0.2657 -0.0338 0.0361  -0.0122 68  ARG   A CZ  
502  N  NH1 . ARG   A 62  ? 0.2593 0.2460 0.2575 -0.0367 0.0341  -0.0137 68  ARG   A NH1 
503  N  NH2 . ARG   A 62  ? 0.2729 0.2645 0.2793 -0.0329 0.0434  -0.0176 68  ARG   A NH2 
504  N  N   . ARG   A 63  ? 0.2452 0.2143 0.2612 -0.0249 0.0034  0.0157  69  ARG   A N   
505  C  CA  . ARG   A 63  ? 0.2598 0.2258 0.2822 -0.0229 -0.0020 0.0225  69  ARG   A CA  
506  C  C   . ARG   A 63  ? 0.2760 0.2367 0.3032 -0.0198 -0.0014 0.0246  69  ARG   A C   
507  O  O   . ARG   A 63  ? 0.3121 0.2705 0.3412 -0.0211 -0.0051 0.0311  69  ARG   A O   
508  C  CB  . ARG   A 63  ? 0.2915 0.2617 0.3096 -0.0289 -0.0079 0.0295  69  ARG   A CB  
509  C  CG  . ARG   A 63  ? 0.3077 0.2833 0.3231 -0.0320 -0.0096 0.0282  69  ARG   A CG  
510  C  CD  . ARG   A 63  ? 0.3290 0.3093 0.3441 -0.0367 -0.0171 0.0379  69  ARG   A CD  
511  N  NE  . ARG   A 63  ? 0.3613 0.3486 0.3713 -0.0419 -0.0187 0.0362  69  ARG   A NE  
512  C  CZ  . ARG   A 63  ? 0.3487 0.3432 0.3463 -0.0512 -0.0190 0.0352  69  ARG   A CZ  
513  N  NH1 . ARG   A 63  ? 0.3400 0.3363 0.3295 -0.0560 -0.0182 0.0364  69  ARG   A NH1 
514  N  NH2 . ARG   A 63  ? 0.3349 0.3356 0.3279 -0.0565 -0.0200 0.0326  69  ARG   A NH2 
515  N  N   . LYS   A 64  ? 0.2541 0.2133 0.2830 -0.0165 0.0034  0.0195  70  LYS   A N   
516  C  CA  . LYS   A 64  ? 0.2434 0.1988 0.2748 -0.0153 0.0047  0.0202  70  LYS   A CA  
517  C  C   . LYS   A 64  ? 0.2332 0.1869 0.2702 -0.0108 0.0080  0.0160  70  LYS   A C   
518  O  O   . LYS   A 64  ? 0.2258 0.1825 0.2630 -0.0090 0.0105  0.0122  70  LYS   A O   
519  C  CB  . LYS   A 64  ? 0.2907 0.2493 0.3148 -0.0192 0.0070  0.0194  70  LYS   A CB  
520  C  CG  . LYS   A 64  ? 0.4184 0.3771 0.4376 -0.0245 0.0034  0.0253  70  LYS   A CG  
521  C  CD  . LYS   A 64  ? 0.5383 0.4982 0.5531 -0.0277 0.0057  0.0253  70  LYS   A CD  
522  C  CE  . LYS   A 64  ? 0.6082 0.5706 0.6157 -0.0343 0.0026  0.0307  70  LYS   A CE  
523  N  NZ  . LYS   A 64  ? 0.6486 0.6171 0.6502 -0.0376 0.0017  0.0298  70  LYS   A NZ  
524  N  N   . HIS   A 65  ? 0.2247 0.1738 0.2659 -0.0097 0.0084  0.0167  71  HIS   A N   
525  C  CA  . HIS   A 65  ? 0.2188 0.1676 0.2637 -0.0073 0.0117  0.0127  71  HIS   A CA  
526  C  C   . HIS   A 65  ? 0.2275 0.1786 0.2682 -0.0101 0.0140  0.0119  71  HIS   A C   
527  O  O   . HIS   A 65  ? 0.2574 0.2058 0.2956 -0.0132 0.0131  0.0144  71  HIS   A O   
528  C  CB  . HIS   A 65  ? 0.2068 0.1494 0.2591 -0.0054 0.0115  0.0129  71  HIS   A CB  
529  C  CG  . HIS   A 65  ? 0.2170 0.1586 0.2755 -0.0024 0.0093  0.0140  71  HIS   A CG  
530  N  ND1 . HIS   A 65  ? 0.2675 0.2104 0.3306 0.0006  0.0112  0.0105  71  HIS   A ND1 
531  C  CD2 . HIS   A 65  ? 0.2266 0.1671 0.2877 -0.0023 0.0053  0.0189  71  HIS   A CD2 
532  C  CE1 . HIS   A 65  ? 0.2417 0.1840 0.3104 0.0025  0.0085  0.0128  71  HIS   A CE1 
533  N  NE2 . HIS   A 65  ? 0.2564 0.1978 0.3242 0.0009  0.0047  0.0182  71  HIS   A NE2 
534  N  N   . TYR   A 66  ? 0.2040 0.1605 0.2445 -0.0093 0.0169  0.0091  72  TYR   A N   
535  C  CA  . TYR   A 66  ? 0.2126 0.1736 0.2502 -0.0121 0.0188  0.0089  72  TYR   A CA  
536  C  C   . TYR   A 66  ? 0.2154 0.1786 0.2555 -0.0123 0.0207  0.0070  72  TYR   A C   
537  O  O   . TYR   A 66  ? 0.2131 0.1787 0.2567 -0.0097 0.0214  0.0058  72  TYR   A O   
538  C  CB  . TYR   A 66  ? 0.2084 0.1767 0.2450 -0.0114 0.0207  0.0084  72  TYR   A CB  
539  C  CG  . TYR   A 66  ? 0.2191 0.1874 0.2512 -0.0131 0.0200  0.0091  72  TYR   A CG  
540  C  CD1 . TYR   A 66  ? 0.2395 0.2085 0.2664 -0.0175 0.0195  0.0110  72  TYR   A CD1 
541  C  CD2 . TYR   A 66  ? 0.2263 0.1944 0.2585 -0.0116 0.0199  0.0077  72  TYR   A CD2 
542  C  CE1 . TYR   A 66  ? 0.2543 0.2249 0.2758 -0.0204 0.0190  0.0117  72  TYR   A CE1 
543  C  CE2 . TYR   A 66  ? 0.2455 0.2150 0.2721 -0.0147 0.0197  0.0076  72  TYR   A CE2 
544  C  CZ  . TYR   A 66  ? 0.2571 0.2282 0.2781 -0.0193 0.0192  0.0097  72  TYR   A CZ  
545  O  OH  . TYR   A 66  ? 0.2761 0.2497 0.2905 -0.0236 0.0190  0.0097  72  TYR   A OH  
546  N  N   . PRO   A 67  ? 0.2201 0.1837 0.2579 -0.0163 0.0215  0.0070  73  PRO   A N   
547  C  CA  . PRO   A 67  ? 0.2222 0.1903 0.2608 -0.0184 0.0233  0.0051  73  PRO   A CA  
548  C  C   . PRO   A 67  ? 0.2458 0.2251 0.2853 -0.0180 0.0241  0.0069  73  PRO   A C   
549  O  O   . PRO   A 67  ? 0.2668 0.2500 0.3052 -0.0182 0.0242  0.0087  73  PRO   A O   
550  C  CB  . PRO   A 67  ? 0.2350 0.2002 0.2702 -0.0239 0.0241  0.0044  73  PRO   A CB  
551  C  CG  . PRO   A 67  ? 0.2558 0.2184 0.2881 -0.0246 0.0225  0.0074  73  PRO   A CG  
552  C  CD  . PRO   A 67  ? 0.2339 0.1944 0.2677 -0.0202 0.0208  0.0088  73  PRO   A CD  
553  N  N   . VAL   A 68  ? 0.2223 0.2072 0.2648 -0.0173 0.0246  0.0067  74  VAL   A N   
554  C  CA  . VAL   A 68  ? 0.2335 0.2292 0.2794 -0.0165 0.0250  0.0099  74  VAL   A CA  
555  C  C   . VAL   A 68  ? 0.2241 0.2281 0.2706 -0.0202 0.0250  0.0109  74  VAL   A C   
556  O  O   . VAL   A 68  ? 0.2173 0.2180 0.2621 -0.0220 0.0253  0.0080  74  VAL   A O   
557  C  CB  . VAL   A 68  ? 0.2683 0.2639 0.3197 -0.0107 0.0252  0.0108  74  VAL   A CB  
558  C  CG1 . VAL   A 68  ? 0.2928 0.2843 0.3434 -0.0084 0.0257  0.0100  74  VAL   A CG1 
559  C  CG2 . VAL   A 68  ? 0.2715 0.2616 0.3239 -0.0089 0.0246  0.0088  74  VAL   A CG2 
560  N  N   . SER   A 69  ? 0.2165 0.2323 0.2661 -0.0213 0.0248  0.0152  75  SER   A N   
561  C  CA  . SER   A 69  ? 0.2152 0.2423 0.2668 -0.0246 0.0240  0.0185  75  SER   A CA  
562  C  C   . SER   A 69  ? 0.1957 0.2266 0.2560 -0.0187 0.0237  0.0228  75  SER   A C   
563  O  O   . SER   A 69  ? 0.1915 0.2220 0.2574 -0.0138 0.0247  0.0243  75  SER   A O   
564  C  CB  . SER   A 69  ? 0.2644 0.3035 0.3161 -0.0293 0.0235  0.0223  75  SER   A CB  
565  O  OG  . SER   A 69  ? 0.3449 0.3795 0.3886 -0.0352 0.0241  0.0182  75  SER   A OG  
566  N  N   . PHE   A 70  ? 0.1915 0.2258 0.2534 -0.0194 0.0228  0.0244  76  PHE   A N   
567  C  CA  . PHE   A 70  ? 0.1943 0.2307 0.2649 -0.0141 0.0225  0.0287  76  PHE   A CA  
568  C  C   . PHE   A 70  ? 0.2042 0.2541 0.2789 -0.0173 0.0205  0.0357  76  PHE   A C   
569  O  O   . PHE   A 70  ? 0.2141 0.2704 0.2824 -0.0246 0.0194  0.0354  76  PHE   A O   
570  C  CB  . PHE   A 70  ? 0.1905 0.2151 0.2601 -0.0103 0.0232  0.0242  76  PHE   A CB  
571  C  CG  . PHE   A 70  ? 0.1929 0.2139 0.2558 -0.0144 0.0232  0.0196  76  PHE   A CG  
572  C  CD1 . PHE   A 70  ? 0.1980 0.2102 0.2546 -0.0161 0.0242  0.0136  76  PHE   A CD1 
573  C  CD2 . PHE   A 70  ? 0.1962 0.2223 0.2600 -0.0165 0.0226  0.0214  76  PHE   A CD2 
574  C  CE1 . PHE   A 70  ? 0.2099 0.2183 0.2626 -0.0193 0.0253  0.0088  76  PHE   A CE1 
575  C  CE2 . PHE   A 70  ? 0.2052 0.2285 0.2632 -0.0206 0.0237  0.0161  76  PHE   A CE2 
576  C  CZ  . PHE   A 70  ? 0.2038 0.2179 0.2571 -0.0216 0.0254  0.0095  76  PHE   A CZ  
577  N  N   . SER   A 71  ? 0.1972 0.2520 0.2830 -0.0126 0.0201  0.0423  77  SER   A N   
578  C  CA  . SER   A 71  ? 0.1918 0.2605 0.2838 -0.0152 0.0175  0.0514  77  SER   A CA  
579  C  C   . SER   A 71  ? 0.1944 0.2620 0.2826 -0.0178 0.0165  0.0511  77  SER   A C   
580  O  O   . SER   A 71  ? 0.1968 0.2525 0.2805 -0.0159 0.0181  0.0441  77  SER   A O   
581  C  CB  . SER   A 71  ? 0.2133 0.2865 0.3210 -0.0085 0.0179  0.0592  77  SER   A CB  
582  O  OG  . SER   A 71  ? 0.2613 0.3225 0.3740 -0.0018 0.0202  0.0565  77  SER   A OG  
583  N  N   . LYS   A 72  ? 0.1920 0.2735 0.2822 -0.0229 0.0136  0.0589  78  LYS   A N   
584  C  CA  . LYS   A 72  ? 0.2117 0.2946 0.2985 -0.0265 0.0127  0.0594  78  LYS   A CA  
585  C  C   . LYS   A 72  ? 0.2197 0.2960 0.3168 -0.0189 0.0131  0.0631  78  LYS   A C   
586  O  O   . LYS   A 72  ? 0.2144 0.2915 0.3239 -0.0128 0.0132  0.0689  78  LYS   A O   
587  C  CB  . LYS   A 72  ? 0.2433 0.3451 0.3285 -0.0355 0.0091  0.0679  78  LYS   A CB  
588  C  CG  . LYS   A 72  ? 0.3095 0.4167 0.3819 -0.0451 0.0095  0.0620  78  LYS   A CG  
589  C  CD  . LYS   A 72  ? 0.3850 0.5117 0.4535 -0.0561 0.0061  0.0694  78  LYS   A CD  
590  C  CE  . LYS   A 72  ? 0.4590 0.5906 0.5143 -0.0667 0.0072  0.0625  78  LYS   A CE  
591  N  NZ  . LYS   A 72  ? 0.5104 0.6546 0.5561 -0.0789 0.0063  0.0629  78  LYS   A NZ  
592  N  N   . PRO   A 73  ? 0.2270 0.2971 0.3203 -0.0195 0.0137  0.0594  79  PRO   A N   
593  C  CA  . PRO   A 73  ? 0.2327 0.2958 0.3353 -0.0131 0.0143  0.0622  79  PRO   A CA  
594  C  C   . PRO   A 73  ? 0.2386 0.3122 0.3547 -0.0117 0.0118  0.0755  79  PRO   A C   
595  O  O   . PRO   A 73  ? 0.2425 0.3307 0.3578 -0.0183 0.0084  0.0834  79  PRO   A O   
596  C  CB  . PRO   A 73  ? 0.2578 0.3178 0.3529 -0.0168 0.0147  0.0576  79  PRO   A CB  
597  C  CG  . PRO   A 73  ? 0.2790 0.3400 0.3614 -0.0232 0.0158  0.0495  79  PRO   A CG  
598  C  CD  . PRO   A 73  ? 0.2459 0.3149 0.3267 -0.0262 0.0147  0.0517  79  PRO   A CD  
599  N  N   . SER   A 74  ? 0.2348 0.3016 0.3635 -0.0036 0.0135  0.0780  80  SER   A N   
600  C  CA  . SER   A 74  ? 0.2426 0.3184 0.3877 -0.0010 0.0118  0.0910  80  SER   A CA  
601  C  C   . SER   A 74  ? 0.2312 0.2946 0.3894 0.0073  0.0150  0.0914  80  SER   A C   
602  O  O   . SER   A 74  ? 0.2249 0.2740 0.3785 0.0104  0.0184  0.0812  80  SER   A O   
603  C  CB  . SER   A 74  ? 0.3086 0.3940 0.4602 -0.0001 0.0114  0.0955  80  SER   A CB  
604  O  OG  . SER   A 74  ? 0.4018 0.4919 0.5397 -0.0060 0.0106  0.0897  80  SER   A OG  
605  N  N   . LEU   A 75  ? 0.2323 0.3020 0.4078 0.0104  0.0140  0.1034  81  LEU   A N   
606  C  CA  . LEU   A 75  ? 0.2543 0.3130 0.4452 0.0179  0.0176  0.1050  81  LEU   A CA  
607  C  C   . LEU   A 75  ? 0.2666 0.3225 0.4685 0.0245  0.0220  0.1026  81  LEU   A C   
608  O  O   . LEU   A 75  ? 0.2720 0.3407 0.4839 0.0250  0.0204  0.1114  81  LEU   A O   
609  C  CB  . LEU   A 75  ? 0.2600 0.3282 0.4658 0.0174  0.0140  0.1211  81  LEU   A CB  
610  C  CG  . LEU   A 75  ? 0.3013 0.3579 0.5238 0.0240  0.0175  0.1242  81  LEU   A CG  
611  C  CD1 . LEU   A 75  ? 0.3242 0.3663 0.5361 0.0230  0.0195  0.1141  81  LEU   A CD1 
612  C  CD2 . LEU   A 75  ? 0.3056 0.3736 0.5443 0.0232  0.0131  0.1424  81  LEU   A CD2 
613  N  N   . ILE   A 76  ? 0.2594 0.3000 0.4589 0.0286  0.0275  0.0906  82  ILE   A N   
614  C  CA  . ILE   A 76  ? 0.2616 0.2989 0.4687 0.0337  0.0326  0.0858  82  ILE   A CA  
615  C  C   . ILE   A 76  ? 0.2663 0.2892 0.4857 0.0400  0.0394  0.0809  82  ILE   A C   
616  O  O   . ILE   A 76  ? 0.2472 0.2582 0.4598 0.0394  0.0409  0.0740  82  ILE   A O   
617  C  CB  . ILE   A 76  ? 0.2715 0.3056 0.4597 0.0304  0.0332  0.0740  82  ILE   A CB  
618  C  CG1 . ILE   A 76  ? 0.2910 0.3384 0.4678 0.0238  0.0275  0.0778  82  ILE   A CG1 
619  C  CG2 . ILE   A 76  ? 0.2775 0.3076 0.4709 0.0346  0.0390  0.0675  82  ILE   A CG2 
620  C  CD1 . ILE   A 76  ? 0.3153 0.3603 0.4761 0.0204  0.0277  0.0684  82  ILE   A CD1 
621  N  N   . PHE   A 77  ? 0.2779 0.3019 0.5151 0.0457  0.0442  0.0832  83  PHE   A N   
622  C  CA  . PHE   A 77  ? 0.2973 0.3072 0.5470 0.0511  0.0520  0.0773  83  PHE   A CA  
623  C  C   . PHE   A 77  ? 0.3201 0.3191 0.5548 0.0497  0.0569  0.0609  83  PHE   A C   
624  O  O   . PHE   A 77  ? 0.3412 0.3455 0.5683 0.0483  0.0572  0.0566  83  PHE   A O   
625  C  CB  . PHE   A 77  ? 0.2987 0.3135 0.5742 0.0577  0.0566  0.0846  83  PHE   A CB  
626  C  CG  . PHE   A 77  ? 0.3231 0.3228 0.6144 0.0631  0.0649  0.0797  83  PHE   A CG  
627  C  CD1 . PHE   A 77  ? 0.3388 0.3321 0.6400 0.0643  0.0641  0.0865  83  PHE   A CD1 
628  C  CD2 . PHE   A 77  ? 0.3460 0.3378 0.6417 0.0660  0.0741  0.0680  83  PHE   A CD2 
629  C  CE1 . PHE   A 77  ? 0.3661 0.3443 0.6825 0.0688  0.0725  0.0814  83  PHE   A CE1 
630  C  CE2 . PHE   A 77  ? 0.3491 0.3264 0.6590 0.0700  0.0828  0.0622  83  PHE   A CE2 
631  C  CZ  . PHE   A 77  ? 0.3638 0.3339 0.6846 0.0715  0.0821  0.0689  83  PHE   A CZ  
632  N  N   . VAL   A 78  ? 0.3198 0.3047 0.5490 0.0489  0.0599  0.0523  84  VAL   A N   
633  C  CA  . VAL   A 78  ? 0.3301 0.3055 0.5450 0.0465  0.0639  0.0378  84  VAL   A CA  
634  C  C   . VAL   A 78  ? 0.3340 0.2975 0.5619 0.0499  0.0733  0.0306  84  VAL   A C   
635  O  O   . VAL   A 78  ? 0.3466 0.3031 0.5856 0.0519  0.0749  0.0337  84  VAL   A O   
636  C  CB  . VAL   A 78  ? 0.3393 0.3093 0.5358 0.0414  0.0593  0.0333  84  VAL   A CB  
637  C  CG1 . VAL   A 78  ? 0.3591 0.3207 0.5414 0.0383  0.0626  0.0198  84  VAL   A CG1 
638  C  CG2 . VAL   A 78  ? 0.3343 0.3152 0.5191 0.0378  0.0512  0.0394  84  VAL   A CG2 
639  N  N   . GLU   A 79  ? 0.3376 0.2985 0.5632 0.0497  0.0798  0.0204  85  GLU   A N   
640  C  CA  . GLU   A 79  ? 0.3601 0.3098 0.5971 0.0518  0.0900  0.0115  85  GLU   A CA  
641  C  C   . GLU   A 79  ? 0.3744 0.3110 0.6016 0.0478  0.0915  0.0029  85  GLU   A C   
642  O  O   . GLU   A 79  ? 0.3853 0.3220 0.5940 0.0429  0.0850  0.0014  85  GLU   A O   
643  C  CB  . GLU   A 79  ? 0.4076 0.3592 0.6411 0.0507  0.0966  0.0015  85  GLU   A CB  
644  C  CG  . GLU   A 79  ? 0.5000 0.4635 0.7485 0.0555  0.0979  0.0087  85  GLU   A CG  
645  C  CD  . GLU   A 79  ? 0.6257 0.5893 0.9031 0.0630  0.1022  0.0175  85  GLU   A CD  
646  O  OE1 . GLU   A 79  ? 0.6434 0.5949 0.9334 0.0653  0.1106  0.0116  85  GLU   A OE1 
647  O  OE2 . GLU   A 79  ? 0.6745 0.6506 0.9627 0.0663  0.0970  0.0308  85  GLU   A OE2 
648  N  N   . ALA   A 80  ? 0.3717 0.2968 0.6122 0.0496  0.1007  -0.0035 86  ALA   A N   
649  C  CA  . ALA   A 80  ? 0.3816 0.2940 0.6146 0.0451  0.1033  -0.0125 86  ALA   A CA  
650  C  C   . ALA   A 80  ? 0.3975 0.3094 0.6071 0.0377  0.1029  -0.0243 86  ALA   A C   
651  O  O   . ALA   A 80  ? 0.4213 0.3381 0.6257 0.0365  0.1058  -0.0298 86  ALA   A O   
652  C  CB  . ALA   A 80  ? 0.3823 0.2826 0.6346 0.0479  0.1149  -0.0187 86  ALA   A CB  
653  N  N   . SER   A 81  ? 0.3834 0.2908 0.5791 0.0325  0.0987  -0.0273 87  SER   A N   
654  C  CA  . SER   A 81  ? 0.3851 0.2920 0.5594 0.0247  0.0975  -0.0374 87  SER   A CA  
655  C  C   . SER   A 81  ? 0.3930 0.2885 0.5653 0.0201  0.1007  -0.0447 87  SER   A C   
656  O  O   . SER   A 81  ? 0.3966 0.2845 0.5840 0.0234  0.1038  -0.0416 87  SER   A O   
657  C  CB  . SER   A 81  ? 0.3861 0.3019 0.5446 0.0227  0.0865  -0.0312 87  SER   A CB  
658  O  OG  . SER   A 81  ? 0.3910 0.3049 0.5502 0.0231  0.0810  -0.0249 87  SER   A OG  
659  N  N   . GLU   A 82  ? 0.4064 0.3012 0.5606 0.0121  0.0996  -0.0535 88  GLU   A N   
660  C  CA  . GLU   A 82  ? 0.4142 0.3000 0.5646 0.0064  0.1015  -0.0600 88  GLU   A CA  
661  C  C   . GLU   A 82  ? 0.3815 0.2683 0.5318 0.0078  0.0930  -0.0504 88  GLU   A C   
662  O  O   . GLU   A 82  ? 0.3818 0.2616 0.5313 0.0040  0.0939  -0.0536 88  GLU   A O   
663  C  CB  . GLU   A 82  ? 0.4878 0.3760 0.6177 -0.0034 0.1004  -0.0697 88  GLU   A CB  
664  C  CG  . GLU   A 82  ? 0.6067 0.5009 0.7280 -0.0064 0.1034  -0.0757 88  GLU   A CG  
665  C  CD  . GLU   A 82  ? 0.7548 0.6599 0.8599 -0.0089 0.0933  -0.0706 88  GLU   A CD  
666  O  OE1 . GLU   A 82  ? 0.7627 0.6702 0.8526 -0.0171 0.0901  -0.0750 88  GLU   A OE1 
667  O  OE2 . GLU   A 82  ? 0.8152 0.7267 0.9235 -0.0030 0.0887  -0.0618 88  GLU   A OE2 
668  N  N   . TYR   A 83  ? 0.3526 0.2483 0.5025 0.0123  0.0850  -0.0393 89  TYR   A N   
669  C  CA  . TYR   A 83  ? 0.3309 0.2291 0.4790 0.0126  0.0774  -0.0313 89  TYR   A CA  
670  C  C   . TYR   A 83  ? 0.3235 0.2212 0.4879 0.0187  0.0770  -0.0208 89  TYR   A C   
671  O  O   . TYR   A 83  ? 0.3262 0.2224 0.4918 0.0178  0.0735  -0.0162 89  TYR   A O   
672  C  CB  . TYR   A 83  ? 0.3190 0.2280 0.4535 0.0117  0.0689  -0.0273 89  TYR   A CB  
673  C  CG  . TYR   A 83  ? 0.3336 0.2441 0.4521 0.0051  0.0676  -0.0354 89  TYR   A CG  
674  C  CD1 . TYR   A 83  ? 0.3557 0.2644 0.4664 -0.0005 0.0651  -0.0388 89  TYR   A CD1 
675  C  CD2 . TYR   A 83  ? 0.3629 0.2773 0.4745 0.0038  0.0689  -0.0393 89  TYR   A CD2 
676  C  CE1 . TYR   A 83  ? 0.3782 0.2902 0.4749 -0.0070 0.0629  -0.0445 89  TYR   A CE1 
677  C  CE2 . TYR   A 83  ? 0.3839 0.3009 0.4808 -0.0030 0.0671  -0.0453 89  TYR   A CE2 
678  C  CZ  . TYR   A 83  ? 0.4079 0.3240 0.4976 -0.0084 0.0638  -0.0474 89  TYR   A CZ  
679  O  OH  . TYR   A 83  ? 0.4565 0.3769 0.5325 -0.0156 0.0610  -0.0517 89  TYR   A OH  
680  N  N   . TYR   A 84  ? 0.3217 0.2220 0.4989 0.0245  0.0798  -0.0159 90  TYR   A N   
681  C  CA  . TYR   A 84  ? 0.3149 0.2164 0.5094 0.0301  0.0789  -0.0040 90  TYR   A CA  
682  C  C   . TYR   A 84  ? 0.3470 0.2451 0.5601 0.0355  0.0871  -0.0041 90  TYR   A C   
683  O  O   . TYR   A 84  ? 0.3545 0.2558 0.5650 0.0360  0.0905  -0.0097 90  TYR   A O   
684  C  CB  . TYR   A 84  ? 0.2816 0.1965 0.4723 0.0320  0.0706  0.0069  90  TYR   A CB  
685  C  CG  . TYR   A 84  ? 0.2492 0.1693 0.4237 0.0276  0.0629  0.0078  90  TYR   A CG  
686  C  CD1 . TYR   A 84  ? 0.2545 0.1737 0.4303 0.0261  0.0595  0.0130  90  TYR   A CD1 
687  C  CD2 . TYR   A 84  ? 0.2387 0.1653 0.3982 0.0253  0.0591  0.0043  90  TYR   A CD2 
688  C  CE1 . TYR   A 84  ? 0.2436 0.1683 0.4063 0.0224  0.0532  0.0136  90  TYR   A CE1 
689  C  CE2 . TYR   A 84  ? 0.2345 0.1654 0.3817 0.0220  0.0529  0.0050  90  TYR   A CE2 
690  C  CZ  . TYR   A 84  ? 0.2415 0.1718 0.3906 0.0207  0.0502  0.0093  90  TYR   A CZ  
691  O  OH  . TYR   A 84  ? 0.2210 0.1563 0.3593 0.0176  0.0448  0.0095  90  TYR   A OH  
692  N  N   . PRO   A 85  ? 0.3647 0.2586 0.5978 0.0400  0.0895  0.0041  91  PRO   A N   
693  C  CA  . PRO   A 85  ? 0.3798 0.2731 0.6341 0.0465  0.0964  0.0068  91  PRO   A CA  
694  C  C   . PRO   A 85  ? 0.3905 0.2994 0.6452 0.0498  0.0907  0.0163  91  PRO   A C   
695  O  O   . PRO   A 85  ? 0.3915 0.3101 0.6310 0.0469  0.0818  0.0209  91  PRO   A O   
696  C  CB  . PRO   A 85  ? 0.3820 0.2682 0.6574 0.0502  0.0980  0.0162  91  PRO   A CB  
697  C  CG  . PRO   A 85  ? 0.3839 0.2746 0.6484 0.0466  0.0885  0.0241  91  PRO   A CG  
698  C  CD  . PRO   A 85  ? 0.3624 0.2539 0.6009 0.0397  0.0853  0.0132  91  PRO   A CD  
699  N  N   . ALA   A 86  ? 0.3910 0.3031 0.6643 0.0556  0.0957  0.0199  92  ALA   A N   
700  C  CA  . ALA   A 86  ? 0.3817 0.3097 0.6569 0.0583  0.0902  0.0299  92  ALA   A CA  
701  C  C   . ALA   A 86  ? 0.3618 0.2972 0.6436 0.0592  0.0818  0.0463  92  ALA   A C   
702  O  O   . ALA   A 86  ? 0.3786 0.3070 0.6764 0.0617  0.0838  0.0524  92  ALA   A O   
703  C  CB  . ALA   A 86  ? 0.3829 0.3131 0.6794 0.0645  0.0979  0.0306  92  ALA   A CB  
704  N  N   . ARG   A 87  ? 0.3352 0.2830 0.6023 0.0559  0.0728  0.0522  93  ARG   A N   
705  C  CA  . ARG   A 87  ? 0.3005 0.2561 0.5694 0.0545  0.0649  0.0660  93  ARG   A CA  
706  C  C   . ARG   A 87  ? 0.2926 0.2644 0.5482 0.0512  0.0570  0.0714  93  ARG   A C   
707  O  O   . ARG   A 87  ? 0.2978 0.2725 0.5417 0.0499  0.0575  0.0637  93  ARG   A O   
708  C  CB  . ARG   A 87  ? 0.3042 0.2507 0.5604 0.0498  0.0629  0.0614  93  ARG   A CB  
709  C  CG  . ARG   A 87  ? 0.3016 0.2506 0.5313 0.0439  0.0588  0.0519  93  ARG   A CG  
710  C  CD  . ARG   A 87  ? 0.3168 0.2561 0.5337 0.0396  0.0588  0.0433  93  ARG   A CD  
711  N  NE  . ARG   A 87  ? 0.3120 0.2578 0.5094 0.0346  0.0523  0.0415  93  ARG   A NE  
712  C  CZ  . ARG   A 87  ? 0.3078 0.2569 0.4904 0.0325  0.0508  0.0345  93  ARG   A CZ  
713  N  NH1 . ARG   A 87  ? 0.3087 0.2578 0.4920 0.0345  0.0545  0.0296  93  ARG   A NH1 
714  N  NH2 . ARG   A 87  ? 0.2510 0.2042 0.4189 0.0284  0.0457  0.0331  93  ARG   A NH2 
715  N  N   . TYR   A 88  ? 0.2778 0.2598 0.5344 0.0489  0.0499  0.0842  94  TYR   A N   
716  C  CA  . TYR   A 88  ? 0.2768 0.2735 0.5197 0.0442  0.0428  0.0884  94  TYR   A CA  
717  C  C   . TYR   A 88  ? 0.2656 0.2586 0.4864 0.0383  0.0398  0.0803  94  TYR   A C   
718  O  O   . TYR   A 88  ? 0.2748 0.2613 0.4947 0.0368  0.0393  0.0804  94  TYR   A O   
719  C  CB  . TYR   A 88  ? 0.2768 0.2874 0.5306 0.0432  0.0369  0.1058  94  TYR   A CB  
720  C  CG  . TYR   A 88  ? 0.2945 0.3142 0.5691 0.0483  0.0381  0.1156  94  TYR   A CG  
721  C  CD1 . TYR   A 88  ? 0.3072 0.3402 0.5773 0.0469  0.0357  0.1169  94  TYR   A CD1 
722  C  CD2 . TYR   A 88  ? 0.3128 0.3268 0.6125 0.0549  0.0425  0.1223  94  TYR   A CD2 
723  C  CE1 . TYR   A 88  ? 0.3270 0.3693 0.6171 0.0517  0.0371  0.1256  94  TYR   A CE1 
724  C  CE2 . TYR   A 88  ? 0.3272 0.3500 0.6485 0.0603  0.0442  0.1314  94  TYR   A CE2 
725  C  CZ  . TYR   A 88  ? 0.3439 0.3813 0.6601 0.0588  0.0414  0.1329  94  TYR   A CZ  
726  O  OH  . TYR   A 88  ? 0.3886 0.4362 0.7269 0.0641  0.0429  0.1422  94  TYR   A OH  
727  N  N   . GLN   A 89  ? 0.2352 0.2320 0.4392 0.0352  0.0380  0.0729  95  GLN   A N   
728  C  CA  . GLN   A 89  ? 0.2212 0.2161 0.4060 0.0300  0.0351  0.0660  95  GLN   A CA  
729  C  C   . GLN   A 89  ? 0.2120 0.2213 0.3890 0.0249  0.0292  0.0727  95  GLN   A C   
730  O  O   . GLN   A 89  ? 0.2126 0.2314 0.3908 0.0247  0.0280  0.0761  95  GLN   A O   
731  C  CB  . GLN   A 89  ? 0.2188 0.2058 0.3914 0.0298  0.0380  0.0526  95  GLN   A CB  
732  C  CG  . GLN   A 89  ? 0.2144 0.1995 0.3700 0.0252  0.0350  0.0463  95  GLN   A CG  
733  C  CD  . GLN   A 89  ? 0.2274 0.2033 0.3732 0.0250  0.0376  0.0345  95  GLN   A CD  
734  O  OE1 . GLN   A 89  ? 0.2610 0.2283 0.4112 0.0271  0.0421  0.0293  95  GLN   A OE1 
735  N  NE2 . GLN   A 89  ? 0.2232 0.2014 0.3556 0.0219  0.0348  0.0303  95  GLN   A NE2 
736  N  N   . SER   A 90  ? 0.1983 0.2102 0.3677 0.0202  0.0258  0.0745  96  SER   A N   
737  C  CA  . SER   A 90  ? 0.1969 0.2225 0.3580 0.0140  0.0211  0.0796  96  SER   A CA  
738  C  C   . SER   A 90  ? 0.2048 0.2292 0.3482 0.0102  0.0207  0.0690  96  SER   A C   
739  O  O   . SER   A 90  ? 0.2026 0.2158 0.3403 0.0120  0.0232  0.0591  96  SER   A O   
740  C  CB  . SER   A 90  ? 0.2366 0.2672 0.3999 0.0102  0.0181  0.0879  96  SER   A CB  
741  O  OG  . SER   A 90  ? 0.2869 0.3074 0.4432 0.0094  0.0196  0.0800  96  SER   A OG  
742  N  N   . HIS   A 91  ? 0.1936 0.2301 0.3293 0.0044  0.0177  0.0715  97  HIS   A N   
743  C  CA  . HIS   A 91  ? 0.2008 0.2367 0.3215 0.0002  0.0178  0.0623  97  HIS   A CA  
744  C  C   . HIS   A 91  ? 0.1977 0.2245 0.3149 0.0041  0.0203  0.0535  97  HIS   A C   
745  O  O   . HIS   A 91  ? 0.2055 0.2257 0.3134 0.0032  0.0212  0.0447  97  HIS   A O   
746  C  CB  . HIS   A 91  ? 0.2203 0.2517 0.3342 -0.0025 0.0180  0.0573  97  HIS   A CB  
747  C  CG  . HIS   A 91  ? 0.2490 0.2906 0.3642 -0.0078 0.0156  0.0656  97  HIS   A CG  
748  N  ND1 . HIS   A 91  ? 0.2782 0.3309 0.3840 -0.0158 0.0141  0.0656  97  HIS   A ND1 
749  C  CD2 . HIS   A 91  ? 0.2628 0.3053 0.3878 -0.0067 0.0146  0.0741  97  HIS   A CD2 
750  C  CE1 . HIS   A 91  ? 0.2680 0.3289 0.3769 -0.0198 0.0120  0.0742  97  HIS   A CE1 
751  N  NE2 . HIS   A 91  ? 0.2627 0.3174 0.3834 -0.0143 0.0119  0.0800  97  HIS   A NE2 
752  N  N   . LEU   A 92  ? 0.1776 0.2052 0.3029 0.0080  0.0214  0.0564  98  LEU   A N   
753  C  CA  . LEU   A 92  ? 0.1874 0.2079 0.3099 0.0110  0.0240  0.0490  98  LEU   A CA  
754  C  C   . LEU   A 92  ? 0.1854 0.2145 0.3031 0.0078  0.0228  0.0498  98  LEU   A C   
755  O  O   . LEU   A 92  ? 0.1913 0.2324 0.3146 0.0060  0.0209  0.0581  98  LEU   A O   
756  C  CB  . LEU   A 92  ? 0.1984 0.2139 0.3341 0.0172  0.0274  0.0507  98  LEU   A CB  
757  C  CG  . LEU   A 92  ? 0.2379 0.2456 0.3709 0.0198  0.0309  0.0424  98  LEU   A CG  
758  C  CD1 . LEU   A 92  ? 0.2389 0.2363 0.3612 0.0187  0.0314  0.0333  98  LEU   A CD1 
759  C  CD2 . LEU   A 92  ? 0.2649 0.2688 0.4125 0.0253  0.0356  0.0436  98  LEU   A CD2 
760  N  N   . MET   A 93  ? 0.1851 0.2086 0.2930 0.0068  0.0237  0.0416  99  MET   A N   
761  C  CA  . MET   A 93  ? 0.1752 0.2053 0.2778 0.0034  0.0229  0.0415  99  MET   A CA  
762  C  C   . MET   A 93  ? 0.1954 0.2196 0.2988 0.0069  0.0256  0.0372  99  MET   A C   
763  O  O   . MET   A 93  ? 0.2135 0.2270 0.3131 0.0089  0.0272  0.0307  99  MET   A O   
764  C  CB  . MET   A 93  ? 0.1913 0.2191 0.2815 -0.0018 0.0220  0.0355  99  MET   A CB  
765  C  CG  . MET   A 93  ? 0.2008 0.2341 0.2890 -0.0061 0.0205  0.0379  99  MET   A CG  
766  S  SD  . MET   A 93  ? 0.2486 0.2779 0.3246 -0.0117 0.0212  0.0292  99  MET   A SD  
767  C  CE  . MET   A 93  ? 0.2322 0.2468 0.3085 -0.0059 0.0227  0.0227  99  MET   A CE  
768  N  N   . LEU   A 94  ? 0.1791 0.2112 0.2868 0.0067  0.0259  0.0407  100 LEU   A N   
769  C  CA  . LEU   A 94  ? 0.1861 0.2140 0.2944 0.0093  0.0289  0.0366  100 LEU   A CA  
770  C  C   . LEU   A 94  ? 0.1838 0.2133 0.2819 0.0048  0.0280  0.0334  100 LEU   A C   
771  O  O   . LEU   A 94  ? 0.1915 0.2294 0.2861 -0.0001 0.0256  0.0364  100 LEU   A O   
772  C  CB  . LEU   A 94  ? 0.2008 0.2361 0.3238 0.0133  0.0312  0.0423  100 LEU   A CB  
773  C  CG  . LEU   A 94  ? 0.2416 0.2743 0.3781 0.0185  0.0333  0.0459  100 LEU   A CG  
774  C  CD1 . LEU   A 94  ? 0.2572 0.2963 0.4102 0.0230  0.0367  0.0505  100 LEU   A CD1 
775  C  CD2 . LEU   A 94  ? 0.2633 0.2817 0.3964 0.0209  0.0361  0.0378  100 LEU   A CD2 
776  N  N   . ALA   A 95  ? 0.1737 0.1958 0.2672 0.0057  0.0302  0.0275  101 ALA   A N   
777  C  CA  . ALA   A 95  ? 0.1778 0.2003 0.2626 0.0016  0.0296  0.0249  101 ALA   A CA  
778  C  C   . ALA   A 95  ? 0.1794 0.1999 0.2655 0.0035  0.0329  0.0221  101 ALA   A C   
779  O  O   . ALA   A 95  ? 0.1865 0.2026 0.2777 0.0074  0.0358  0.0200  101 ALA   A O   
780  C  CB  . ALA   A 95  ? 0.1925 0.2054 0.2665 -0.0009 0.0280  0.0199  101 ALA   A CB  
781  N  N   . VAL   A 96  ? 0.1677 0.1913 0.2485 -0.0001 0.0328  0.0215  102 VAL   A N   
782  C  CA  . VAL   A 96  ? 0.1679 0.1901 0.2473 0.0000  0.0359  0.0182  102 VAL   A CA  
783  C  C   . VAL   A 96  ? 0.2136 0.2247 0.2818 -0.0021 0.0346  0.0133  102 VAL   A C   
784  O  O   . VAL   A 96  ? 0.2425 0.2505 0.3031 -0.0056 0.0317  0.0132  102 VAL   A O   
785  C  CB  . VAL   A 96  ? 0.1698 0.2016 0.2493 -0.0035 0.0362  0.0206  102 VAL   A CB  
786  C  CG1 . VAL   A 96  ? 0.1814 0.2116 0.2573 -0.0046 0.0394  0.0167  102 VAL   A CG1 
787  C  CG2 . VAL   A 96  ? 0.1768 0.2211 0.2696 -0.0010 0.0371  0.0268  102 VAL   A CG2 
788  N  N   . GLY   A 97  ? 0.2285 0.2341 0.2965 -0.0001 0.0368  0.0096  103 GLY   A N   
789  C  CA  . GLY   A 97  ? 0.2410 0.2380 0.2995 -0.0023 0.0351  0.0062  103 GLY   A CA  
790  C  C   . GLY   A 97  ? 0.2379 0.2313 0.2971 -0.0009 0.0382  0.0021  103 GLY   A C   
791  O  O   . GLY   A 97  ? 0.2416 0.2367 0.3097 0.0026  0.0418  0.0013  103 GLY   A O   
792  N  N   . HIS   A 98  ? 0.2387 0.2272 0.2888 -0.0043 0.0369  -0.0003 104 HIS   A N   
793  C  CA  . HIS   A 98  ? 0.2368 0.2226 0.2855 -0.0049 0.0397  -0.0050 104 HIS   A CA  
794  C  C   . HIS   A 98  ? 0.2337 0.2140 0.2851 -0.0022 0.0384  -0.0059 104 HIS   A C   
795  O  O   . HIS   A 98  ? 0.2315 0.2084 0.2806 -0.0020 0.0339  -0.0036 104 HIS   A O   
796  C  CB  . HIS   A 98  ? 0.2331 0.2174 0.2703 -0.0107 0.0377  -0.0061 104 HIS   A CB  
797  C  CG  . HIS   A 98  ? 0.2395 0.2227 0.2735 -0.0132 0.0410  -0.0115 104 HIS   A CG  
798  N  ND1 . HIS   A 98  ? 0.2644 0.2512 0.3019 -0.0135 0.0479  -0.0165 104 HIS   A ND1 
799  C  CD2 . HIS   A 98  ? 0.2644 0.2439 0.2927 -0.0159 0.0385  -0.0130 104 HIS   A CD2 
800  C  CE1 . HIS   A 98  ? 0.2712 0.2556 0.3041 -0.0168 0.0499  -0.0218 104 HIS   A CE1 
801  N  NE2 . HIS   A 98  ? 0.2685 0.2490 0.2953 -0.0186 0.0440  -0.0195 104 HIS   A NE2 
802  N  N   . SER   A 99  ? 0.2335 0.2127 0.2896 -0.0008 0.0429  -0.0100 105 SER   A N   
803  C  CA  . SER   A 99  ? 0.2422 0.2160 0.2997 0.0005  0.0423  -0.0117 105 SER   A CA  
804  C  C   . SER   A 99  ? 0.2718 0.2438 0.3303 -0.0010 0.0482  -0.0183 105 SER   A C   
805  O  O   . SER   A 99  ? 0.2833 0.2582 0.3475 0.0000  0.0540  -0.0208 105 SER   A O   
806  C  CB  . SER   A 99  ? 0.2713 0.2449 0.3383 0.0054  0.0413  -0.0080 105 SER   A CB  
807  O  OG  . SER   A 99  ? 0.2983 0.2668 0.3668 0.0062  0.0409  -0.0097 105 SER   A OG  
808  N  N   . GLU   A 100 ? 0.2729 0.2408 0.3260 -0.0039 0.0470  -0.0215 106 GLU   A N   
809  C  CA  . GLU   A 100 ? 0.3079 0.2730 0.3609 -0.0065 0.0525  -0.0288 106 GLU   A CA  
810  C  C   . GLU   A 100 ? 0.3274 0.2871 0.3835 -0.0052 0.0512  -0.0294 106 GLU   A C   
811  O  O   . GLU   A 100 ? 0.3324 0.2915 0.3880 -0.0036 0.0453  -0.0245 106 GLU   A O   
812  C  CB  . GLU   A 100 ? 0.3545 0.3215 0.3938 -0.0147 0.0514  -0.0322 106 GLU   A CB  
813  C  CG  . GLU   A 100 ? 0.3968 0.3690 0.4317 -0.0180 0.0545  -0.0339 106 GLU   A CG  
814  C  CD  . GLU   A 100 ? 0.3659 0.3413 0.3864 -0.0264 0.0506  -0.0340 106 GLU   A CD  
815  O  OE1 . GLU   A 100 ? 0.3795 0.3539 0.3939 -0.0316 0.0503  -0.0376 106 GLU   A OE1 
816  O  OE2 . GLU   A 100 ? 0.3392 0.3186 0.3547 -0.0284 0.0478  -0.0298 106 GLU   A OE2 
817  N  N   . PRO   A 101 ? 0.3567 0.3123 0.4165 -0.0063 0.0573  -0.0360 107 PRO   A N   
818  C  CA  . PRO   A 101 ? 0.3732 0.3238 0.4342 -0.0067 0.0561  -0.0372 107 PRO   A CA  
819  C  C   . PRO   A 101 ? 0.3697 0.3225 0.4177 -0.0130 0.0499  -0.0369 107 PRO   A C   
820  O  O   . PRO   A 101 ? 0.3793 0.3357 0.4171 -0.0194 0.0499  -0.0397 107 PRO   A O   
821  C  CB  . PRO   A 101 ? 0.3860 0.3315 0.4526 -0.0080 0.0651  -0.0457 107 PRO   A CB  
822  C  CG  . PRO   A 101 ? 0.3817 0.3299 0.4549 -0.0054 0.0712  -0.0471 107 PRO   A CG  
823  C  CD  . PRO   A 101 ? 0.3594 0.3148 0.4221 -0.0080 0.0661  -0.0434 107 PRO   A CD  
824  N  N   . GLY   A 102 ? 0.3088 0.2610 0.3583 -0.0107 0.0440  -0.0317 108 GLY   A N   
825  C  CA  . GLY   A 102 ? 0.2960 0.2509 0.3380 -0.0142 0.0369  -0.0285 108 GLY   A CA  
826  C  C   . GLY   A 102 ? 0.2705 0.2275 0.3147 -0.0100 0.0314  -0.0211 108 GLY   A C   
827  O  O   . GLY   A 102 ? 0.2795 0.2376 0.3224 -0.0105 0.0259  -0.0176 108 GLY   A O   
828  N  N   . ASP   A 103 ? 0.2371 0.1949 0.2851 -0.0060 0.0330  -0.0189 109 ASP   A N   
829  C  CA  . ASP   A 103 ? 0.2299 0.1892 0.2794 -0.0030 0.0288  -0.0131 109 ASP   A CA  
830  C  C   . ASP   A 103 ? 0.2246 0.1826 0.2818 0.0015  0.0280  -0.0106 109 ASP   A C   
831  O  O   . ASP   A 103 ? 0.2189 0.1781 0.2771 0.0031  0.0248  -0.0069 109 ASP   A O   
832  C  CB  . ASP   A 103 ? 0.2199 0.1818 0.2696 -0.0020 0.0309  -0.0118 109 ASP   A CB  
833  C  CG  . ASP   A 103 ? 0.2342 0.1984 0.2750 -0.0069 0.0298  -0.0122 109 ASP   A CG  
834  O  OD1 . ASP   A 103 ? 0.2330 0.1972 0.2685 -0.0100 0.0251  -0.0102 109 ASP   A OD1 
835  O  OD2 . ASP   A 103 ? 0.2520 0.2186 0.2917 -0.0078 0.0334  -0.0137 109 ASP   A OD2 
836  N  N   . CYS   A 104 ? 0.2172 0.1728 0.2799 0.0028  0.0310  -0.0127 110 CYS   A N   
837  C  CA  . CYS   A 104 ? 0.2162 0.1715 0.2857 0.0061  0.0300  -0.0098 110 CYS   A CA  
838  C  C   . CYS   A 104 ? 0.2084 0.1644 0.2759 0.0053  0.0253  -0.0081 110 CYS   A C   
839  O  O   . CYS   A 104 ? 0.2073 0.1629 0.2704 0.0023  0.0232  -0.0096 110 CYS   A O   
840  C  CB  . CYS   A 104 ? 0.2341 0.1859 0.3095 0.0068  0.0337  -0.0121 110 CYS   A CB  
841  S  SG  . CYS   A 104 ? 0.2506 0.2018 0.3344 0.0098  0.0399  -0.0123 110 CYS   A SG  
842  N  N   . GLY   A 105 ? 0.2026 0.1604 0.2735 0.0076  0.0238  -0.0049 111 GLY   A N   
843  C  CA  . GLY   A 105 ? 0.1895 0.1481 0.2607 0.0074  0.0205  -0.0038 111 GLY   A CA  
844  C  C   . GLY   A 105 ? 0.1964 0.1560 0.2655 0.0074  0.0183  -0.0021 111 GLY   A C   
845  O  O   . GLY   A 105 ? 0.1980 0.1581 0.2697 0.0081  0.0166  -0.0012 111 GLY   A O   
846  N  N   . GLY   A 106 ? 0.1947 0.1543 0.2598 0.0066  0.0189  -0.0019 112 GLY   A N   
847  C  CA  . GLY   A 106 ? 0.1973 0.1568 0.2606 0.0062  0.0171  -0.0001 112 GLY   A CA  
848  C  C   . GLY   A 106 ? 0.1950 0.1558 0.2615 0.0075  0.0183  0.0004  112 GLY   A C   
849  O  O   . GLY   A 106 ? 0.1875 0.1510 0.2556 0.0080  0.0204  0.0007  112 GLY   A O   
850  N  N   . ILE   A 107 ? 0.1788 0.1383 0.2470 0.0075  0.0171  0.0007  113 ILE   A N   
851  C  CA  . ILE   A 107 ? 0.1749 0.1360 0.2451 0.0073  0.0190  -0.0002 113 ILE   A CA  
852  C  C   . ILE   A 107 ? 0.1749 0.1371 0.2416 0.0054  0.0202  0.0002  113 ILE   A C   
853  O  O   . ILE   A 107 ? 0.1814 0.1409 0.2454 0.0045  0.0192  0.0009  113 ILE   A O   
854  C  CB  . ILE   A 107 ? 0.1788 0.1375 0.2538 0.0080  0.0187  -0.0013 113 ILE   A CB  
855  C  CG1 . ILE   A 107 ? 0.1955 0.1560 0.2750 0.0094  0.0184  -0.0019 113 ILE   A CG1 
856  C  CG2 . ILE   A 107 ? 0.1891 0.1482 0.2649 0.0063  0.0215  -0.0037 113 ILE   A CG2 
857  C  CD1 . ILE   A 107 ? 0.2249 0.1841 0.3113 0.0106  0.0182  -0.0028 113 ILE   A CD1 
858  N  N   . LEU   A 108 ? 0.1678 0.1348 0.2346 0.0042  0.0220  0.0001  114 LEU   A N   
859  C  CA  . LEU   A 108 ? 0.1696 0.1395 0.2334 0.0012  0.0232  0.0003  114 LEU   A CA  
860  C  C   . LEU   A 108 ? 0.1861 0.1557 0.2508 -0.0011 0.0249  -0.0029 114 LEU   A C   
861  O  O   . LEU   A 108 ? 0.1929 0.1652 0.2601 -0.0011 0.0258  -0.0038 114 LEU   A O   
862  C  CB  . LEU   A 108 ? 0.1714 0.1488 0.2355 0.0005  0.0238  0.0031  114 LEU   A CB  
863  C  CG  . LEU   A 108 ? 0.1945 0.1780 0.2557 -0.0038 0.0246  0.0039  114 LEU   A CG  
864  C  CD1 . LEU   A 108 ? 0.1984 0.1801 0.2564 -0.0048 0.0243  0.0041  114 LEU   A CD1 
865  C  CD2 . LEU   A 108 ? 0.1992 0.1920 0.2632 -0.0042 0.0244  0.0086  114 LEU   A CD2 
866  N  N   . ARG   A 109 ? 0.1816 0.1478 0.2445 -0.0035 0.0259  -0.0049 115 ARG   A N   
867  C  CA  . ARG   A 109 ? 0.1845 0.1494 0.2489 -0.0061 0.0289  -0.0094 115 ARG   A CA  
868  C  C   . ARG   A 109 ? 0.2148 0.1812 0.2744 -0.0115 0.0308  -0.0112 115 ARG   A C   
869  O  O   . ARG   A 109 ? 0.2266 0.1922 0.2830 -0.0123 0.0295  -0.0090 115 ARG   A O   
870  C  CB  . ARG   A 109 ? 0.1909 0.1474 0.2613 -0.0031 0.0290  -0.0111 115 ARG   A CB  
871  C  CG  . ARG   A 109 ? 0.2205 0.1705 0.2905 -0.0026 0.0275  -0.0091 115 ARG   A CG  
872  C  CD  . ARG   A 109 ? 0.2405 0.1837 0.3191 0.0007  0.0271  -0.0090 115 ARG   A CD  
873  N  NE  . ARG   A 109 ? 0.2583 0.2031 0.3391 0.0044  0.0235  -0.0055 115 ARG   A NE  
874  C  CZ  . ARG   A 109 ? 0.2581 0.2029 0.3463 0.0072  0.0233  -0.0059 115 ARG   A CZ  
875  N  NH1 . ARG   A 109 ? 0.2425 0.1864 0.3369 0.0072  0.0273  -0.0103 115 ARG   A NH1 
876  N  NH2 . ARG   A 109 ? 0.2513 0.1979 0.3406 0.0094  0.0196  -0.0024 115 ARG   A NH2 
877  N  N   . CYS   A 110 ? 0.2260 0.1944 0.2850 -0.0158 0.0343  -0.0159 116 CYS   A N   
878  C  CA  . CYS   A 110 ? 0.2459 0.2154 0.2999 -0.0224 0.0369  -0.0191 116 CYS   A CA  
879  C  C   . CYS   A 110 ? 0.2766 0.2380 0.3347 -0.0239 0.0418  -0.0265 116 CYS   A C   
880  O  O   . CYS   A 110 ? 0.2625 0.2180 0.3282 -0.0189 0.0423  -0.0275 116 CYS   A O   
881  C  CB  . CYS   A 110 ? 0.2696 0.2517 0.3184 -0.0281 0.0371  -0.0181 116 CYS   A CB  
882  S  SG  . CYS   A 110 ? 0.2668 0.2539 0.3168 -0.0308 0.0403  -0.0224 116 CYS   A SG  
883  N  N   . GLN   A 111 ? 0.3053 0.2668 0.3591 -0.0312 0.0458  -0.0319 117 GLN   A N   
884  C  CA  . GLN   A 111 ? 0.3444 0.2976 0.4031 -0.0331 0.0517  -0.0399 117 GLN   A CA  
885  C  C   . GLN   A 111 ? 0.3565 0.3129 0.4195 -0.0326 0.0552  -0.0445 117 GLN   A C   
886  O  O   . GLN   A 111 ? 0.3857 0.3343 0.4570 -0.0310 0.0600  -0.0503 117 GLN   A O   
887  C  CB  . GLN   A 111 ? 0.4010 0.3548 0.4530 -0.0427 0.0561  -0.0460 117 GLN   A CB  
888  C  CG  . GLN   A 111 ? 0.4701 0.4388 0.5123 -0.0509 0.0561  -0.0464 117 GLN   A CG  
889  C  CD  . GLN   A 111 ? 0.5666 0.5382 0.6007 -0.0618 0.0598  -0.0520 117 GLN   A CD  
890  O  OE1 . GLN   A 111 ? 0.5901 0.5714 0.6167 -0.0667 0.0564  -0.0474 117 GLN   A OE1 
891  N  NE2 . GLN   A 111 ? 0.5667 0.5307 0.6025 -0.0665 0.0672  -0.0623 117 GLN   A NE2 
892  N  N   . HIS   A 112 ? 0.3229 0.2908 0.3815 -0.0340 0.0530  -0.0415 118 HIS   A N   
893  C  CA  . HIS   A 112 ? 0.3101 0.2826 0.3712 -0.0350 0.0563  -0.0455 118 HIS   A CA  
894  C  C   . HIS   A 112 ? 0.2946 0.2648 0.3643 -0.0263 0.0535  -0.0416 118 HIS   A C   
895  O  O   . HIS   A 112 ? 0.3116 0.2844 0.3855 -0.0263 0.0565  -0.0453 118 HIS   A O   
896  C  CB  . HIS   A 112 ? 0.3138 0.3010 0.3656 -0.0424 0.0553  -0.0436 118 HIS   A CB  
897  C  CG  . HIS   A 112 ? 0.3719 0.3641 0.4147 -0.0523 0.0576  -0.0471 118 HIS   A CG  
898  N  ND1 . HIS   A 112 ? 0.3970 0.3959 0.4336 -0.0547 0.0529  -0.0403 118 HIS   A ND1 
899  C  CD2 . HIS   A 112 ? 0.4059 0.3973 0.4455 -0.0606 0.0645  -0.0569 118 HIS   A CD2 
900  C  CE1 . HIS   A 112 ? 0.4231 0.4259 0.4523 -0.0647 0.0563  -0.0455 118 HIS   A CE1 
901  N  NE2 . HIS   A 112 ? 0.4277 0.4257 0.4579 -0.0689 0.0636  -0.0561 118 HIS   A NE2 
902  N  N   . GLY   A 113 ? 0.2699 0.2366 0.3413 -0.0200 0.0478  -0.0345 119 GLY   A N   
903  C  CA  . GLY   A 113 ? 0.2465 0.2119 0.3247 -0.0131 0.0449  -0.0308 119 GLY   A CA  
904  C  C   . GLY   A 113 ? 0.2126 0.1815 0.2869 -0.0104 0.0391  -0.0232 119 GLY   A C   
905  O  O   . GLY   A 113 ? 0.2195 0.1896 0.2881 -0.0121 0.0371  -0.0202 119 GLY   A O   
906  N  N   . VAL   A 114 ? 0.1872 0.1579 0.2652 -0.0065 0.0369  -0.0204 120 VAL   A N   
907  C  CA  . VAL   A 114 ? 0.1973 0.1701 0.2732 -0.0039 0.0325  -0.0144 120 VAL   A CA  
908  C  C   . VAL   A 114 ? 0.1927 0.1743 0.2635 -0.0076 0.0321  -0.0116 120 VAL   A C   
909  O  O   . VAL   A 114 ? 0.1869 0.1746 0.2574 -0.0107 0.0338  -0.0127 120 VAL   A O   
910  C  CB  . VAL   A 114 ? 0.2085 0.1799 0.2901 0.0005  0.0306  -0.0129 120 VAL   A CB  
911  C  CG1 . VAL   A 114 ? 0.2052 0.1782 0.2847 0.0024  0.0274  -0.0081 120 VAL   A CG1 
912  C  CG2 . VAL   A 114 ? 0.2233 0.1876 0.3108 0.0041  0.0298  -0.0135 120 VAL   A CG2 
913  N  N   . VAL   A 115 ? 0.1887 0.1718 0.2565 -0.0072 0.0298  -0.0072 121 VAL   A N   
914  C  CA  . VAL   A 115 ? 0.1863 0.1782 0.2515 -0.0100 0.0289  -0.0028 121 VAL   A CA  
915  C  C   . VAL   A 115 ? 0.1957 0.1884 0.2649 -0.0060 0.0268  0.0020  121 VAL   A C   
916  O  O   . VAL   A 115 ? 0.2127 0.2123 0.2830 -0.0077 0.0263  0.0058  121 VAL   A O   
917  C  CB  . VAL   A 115 ? 0.2040 0.1977 0.2656 -0.0118 0.0281  -0.0009 121 VAL   A CB  
918  C  CG1 . VAL   A 115 ? 0.2015 0.2054 0.2631 -0.0138 0.0265  0.0055  121 VAL   A CG1 
919  C  CG2 . VAL   A 115 ? 0.2149 0.2077 0.2722 -0.0170 0.0306  -0.0060 121 VAL   A CG2 
920  N  N   . GLY   A 116 ? 0.1805 0.1662 0.2518 -0.0013 0.0255  0.0020  122 GLY   A N   
921  C  CA  . GLY   A 116 ? 0.1847 0.1698 0.2596 0.0019  0.0245  0.0053  122 GLY   A CA  
922  C  C   . GLY   A 116 ? 0.1973 0.1753 0.2725 0.0052  0.0236  0.0039  122 GLY   A C   
923  O  O   . GLY   A 116 ? 0.1999 0.1736 0.2732 0.0053  0.0232  0.0013  122 GLY   A O   
924  N  N   . ILE   A 117 ? 0.1834 0.1599 0.2613 0.0075  0.0236  0.0056  123 ILE   A N   
925  C  CA  . ILE   A 117 ? 0.1789 0.1499 0.2559 0.0091  0.0232  0.0037  123 ILE   A CA  
926  C  C   . ILE   A 117 ? 0.1749 0.1460 0.2530 0.0103  0.0247  0.0050  123 ILE   A C   
927  O  O   . ILE   A 117 ? 0.1745 0.1489 0.2574 0.0111  0.0259  0.0081  123 ILE   A O   
928  C  CB  . ILE   A 117 ? 0.1949 0.1627 0.2739 0.0099  0.0226  0.0021  123 ILE   A CB  
929  C  CG1 . ILE   A 117 ? 0.1917 0.1613 0.2756 0.0103  0.0237  0.0042  123 ILE   A CG1 
930  C  CG2 . ILE   A 117 ? 0.1953 0.1625 0.2743 0.0094  0.0212  0.0003  123 ILE   A CG2 
931  C  CD1 . ILE   A 117 ? 0.2038 0.1700 0.2895 0.0103  0.0233  0.0023  123 ILE   A CD1 
932  N  N   . VAL   A 118 ? 0.1763 0.1443 0.2510 0.0102  0.0248  0.0028  124 VAL   A N   
933  C  CA  . VAL   A 118 ? 0.1781 0.1461 0.2546 0.0111  0.0274  0.0027  124 VAL   A CA  
934  C  C   . VAL   A 118 ? 0.1820 0.1478 0.2646 0.0127  0.0296  0.0023  124 VAL   A C   
935  O  O   . VAL   A 118 ? 0.1876 0.1498 0.2692 0.0120  0.0288  0.0001  124 VAL   A O   
936  C  CB  . VAL   A 118 ? 0.1952 0.1606 0.2657 0.0094  0.0274  -0.0004 124 VAL   A CB  
937  C  CG1 . VAL   A 118 ? 0.2126 0.1779 0.2852 0.0098  0.0314  -0.0023 124 VAL   A CG1 
938  C  CG2 . VAL   A 118 ? 0.2016 0.1684 0.2671 0.0077  0.0255  0.0008  124 VAL   A CG2 
939  N  N   . SER   A 119 ? 0.1810 0.1491 0.2709 0.0147  0.0323  0.0050  125 SER   A N   
940  C  CA  . SER   A 119 ? 0.2028 0.1676 0.3006 0.0165  0.0350  0.0051  125 SER   A CA  
941  C  C   . SER   A 119 ? 0.2217 0.1852 0.3258 0.0184  0.0398  0.0038  125 SER   A C   
942  O  O   . SER   A 119 ? 0.2267 0.1846 0.3352 0.0190  0.0434  0.0005  125 SER   A O   
943  C  CB  . SER   A 119 ? 0.2128 0.1817 0.3171 0.0175  0.0337  0.0114  125 SER   A CB  
944  O  OG  . SER   A 119 ? 0.2302 0.1954 0.3437 0.0193  0.0363  0.0128  125 SER   A OG  
945  N  N   . THR   A 120 ? 0.2101 0.1792 0.3154 0.0191  0.0405  0.0059  126 THR   A N   
946  C  CA  . THR   A 120 ? 0.2137 0.1828 0.3273 0.0214  0.0459  0.0047  126 THR   A CA  
947  C  C   . THR   A 120 ? 0.2301 0.2026 0.3369 0.0195  0.0466  0.0020  126 THR   A C   
948  O  O   . THR   A 120 ? 0.2286 0.2038 0.3262 0.0170  0.0424  0.0029  126 THR   A O   
949  C  CB  . THR   A 120 ? 0.2245 0.1996 0.3523 0.0251  0.0467  0.0127  126 THR   A CB  
950  O  OG1 . THR   A 120 ? 0.2230 0.2076 0.3489 0.0242  0.0433  0.0181  126 THR   A OG1 
951  C  CG2 . THR   A 120 ? 0.2216 0.1948 0.3563 0.0264  0.0453  0.0174  126 THR   A CG2 
952  N  N   . GLY   A 121 ? 0.2345 0.2069 0.3466 0.0205  0.0521  -0.0013 127 GLY   A N   
953  C  CA  . GLY   A 121 ? 0.2527 0.2297 0.3590 0.0184  0.0530  -0.0031 127 GLY   A CA  
954  C  C   . GLY   A 121 ? 0.2752 0.2534 0.3902 0.0200  0.0603  -0.0067 127 GLY   A C   
955  O  O   . GLY   A 121 ? 0.2796 0.2543 0.4065 0.0232  0.0651  -0.0078 127 GLY   A O   
956  N  N   . GLY   A 122 ? 0.2892 0.2717 0.3984 0.0173  0.0615  -0.0090 128 GLY   A N   
957  C  CA  . GLY   A 122 ? 0.3004 0.2847 0.4168 0.0179  0.0694  -0.0139 128 GLY   A CA  
958  C  C   . GLY   A 122 ? 0.3085 0.3026 0.4269 0.0179  0.0696  -0.0106 128 GLY   A C   
959  O  O   . GLY   A 122 ? 0.3091 0.3098 0.4326 0.0200  0.0655  -0.0026 128 GLY   A O   
960  N  N   . ASN   A 123 ? 0.3030 0.2992 0.4175 0.0147  0.0746  -0.0168 129 ASN   A N   
961  C  CA  . ASN   A 123 ? 0.2948 0.3007 0.4114 0.0138  0.0764  -0.0151 129 ASN   A CA  
962  C  C   . ASN   A 123 ? 0.2690 0.2809 0.3788 0.0120  0.0688  -0.0077 129 ASN   A C   
963  O  O   . ASN   A 123 ? 0.2728 0.2942 0.3913 0.0138  0.0688  -0.0024 129 ASN   A O   
964  C  CB  . ASN   A 123 ? 0.3317 0.3429 0.4694 0.0198  0.0832  -0.0135 129 ASN   A CB  
965  C  CG  . ASN   A 123 ? 0.4170 0.4218 0.5613 0.0206  0.0925  -0.0228 129 ASN   A CG  
966  O  OD1 . ASN   A 123 ? 0.4578 0.4614 0.5921 0.0153  0.0969  -0.0315 129 ASN   A OD1 
967  N  ND2 . ASN   A 123 ? 0.4305 0.4307 0.5909 0.0265  0.0957  -0.0212 129 ASN   A ND2 
968  N  N   . GLY   A 124 ? 0.2341 0.2410 0.3288 0.0080  0.0627  -0.0077 130 GLY   A N   
969  C  CA  . GLY   A 124 ? 0.2207 0.2316 0.3085 0.0055  0.0564  -0.0022 130 GLY   A CA  
970  C  C   . GLY   A 124 ? 0.2089 0.2206 0.3012 0.0082  0.0516  0.0042  130 GLY   A C   
971  O  O   . GLY   A 124 ? 0.2226 0.2379 0.3099 0.0056  0.0472  0.0081  130 GLY   A O   
972  N  N   . LEU   A 125 ? 0.1949 0.2030 0.2955 0.0123  0.0524  0.0048  131 LEU   A N   
973  C  CA  . LEU   A 125 ? 0.2045 0.2132 0.3077 0.0138  0.0477  0.0106  131 LEU   A CA  
974  C  C   . LEU   A 125 ? 0.2115 0.2103 0.3073 0.0132  0.0453  0.0074  131 LEU   A C   
975  O  O   . LEU   A 125 ? 0.2241 0.2163 0.3176 0.0131  0.0482  0.0017  131 LEU   A O   
976  C  CB  . LEU   A 125 ? 0.2208 0.2339 0.3410 0.0190  0.0502  0.0154  131 LEU   A CB  
977  C  CG  . LEU   A 125 ? 0.2338 0.2592 0.3649 0.0202  0.0515  0.0211  131 LEU   A CG  
978  C  CD1 . LEU   A 125 ? 0.2559 0.2843 0.4063 0.0261  0.0547  0.0260  131 LEU   A CD1 
979  C  CD2 . LEU   A 125 ? 0.2361 0.2699 0.3612 0.0163  0.0456  0.0270  131 LEU   A CD2 
980  N  N   . VAL   A 126 ? 0.1797 0.1785 0.2723 0.0124  0.0405  0.0109  132 VAL   A N   
981  C  CA  . VAL   A 126 ? 0.1876 0.1786 0.2756 0.0123  0.0384  0.0087  132 VAL   A CA  
982  C  C   . VAL   A 126 ? 0.1843 0.1790 0.2782 0.0136  0.0359  0.0143  132 VAL   A C   
983  O  O   . VAL   A 126 ? 0.1896 0.1919 0.2841 0.0120  0.0340  0.0187  132 VAL   A O   
984  C  CB  . VAL   A 126 ? 0.1979 0.1847 0.2737 0.0086  0.0350  0.0061  132 VAL   A CB  
985  C  CG1 . VAL   A 126 ? 0.2071 0.1986 0.2792 0.0059  0.0324  0.0091  132 VAL   A CG1 
986  C  CG2 . VAL   A 126 ? 0.2234 0.2038 0.2966 0.0088  0.0327  0.0046  132 VAL   A CG2 
987  N  N   . GLY   A 127 ? 0.1890 0.1791 0.2868 0.0156  0.0362  0.0141  133 GLY   A N   
988  C  CA  . GLY   A 127 ? 0.1907 0.1846 0.2934 0.0161  0.0339  0.0195  133 GLY   A CA  
989  C  C   . GLY   A 127 ? 0.1978 0.1864 0.2937 0.0144  0.0314  0.0169  133 GLY   A C   
990  O  O   . GLY   A 127 ? 0.2057 0.1869 0.2983 0.0147  0.0322  0.0120  133 GLY   A O   
991  N  N   . PHE   A 128 ? 0.1890 0.1825 0.2826 0.0119  0.0287  0.0200  134 PHE   A N   
992  C  CA  . PHE   A 128 ? 0.1858 0.1755 0.2742 0.0103  0.0269  0.0173  134 PHE   A CA  
993  C  C   . PHE   A 128 ? 0.1884 0.1818 0.2817 0.0100  0.0262  0.0215  134 PHE   A C   
994  O  O   . PHE   A 128 ? 0.1963 0.1984 0.2931 0.0085  0.0253  0.0274  134 PHE   A O   
995  C  CB  . PHE   A 128 ? 0.1876 0.1793 0.2683 0.0066  0.0254  0.0155  134 PHE   A CB  
996  C  CG  . PHE   A 128 ? 0.1844 0.1735 0.2603 0.0061  0.0257  0.0128  134 PHE   A CG  
997  C  CD1 . PHE   A 128 ? 0.1996 0.1811 0.2712 0.0066  0.0254  0.0086  134 PHE   A CD1 
998  C  CD2 . PHE   A 128 ? 0.1948 0.1901 0.2704 0.0044  0.0259  0.0152  134 PHE   A CD2 
999  C  CE1 . PHE   A 128 ? 0.2082 0.1878 0.2751 0.0053  0.0253  0.0072  134 PHE   A CE1 
1000 C  CE2 . PHE   A 128 ? 0.2108 0.2039 0.2817 0.0033  0.0263  0.0130  134 PHE   A CE2 
1001 C  CZ  . PHE   A 128 ? 0.2054 0.1905 0.2719 0.0037  0.0260  0.0092  134 PHE   A CZ  
1002 N  N   . ALA   A 129 ? 0.1787 0.1668 0.2721 0.0106  0.0261  0.0192  135 ALA   A N   
1003 C  CA  . ALA   A 129 ? 0.1876 0.1791 0.2844 0.0094  0.0253  0.0230  135 ALA   A CA  
1004 C  C   . ALA   A 129 ? 0.1953 0.1913 0.2853 0.0051  0.0240  0.0214  135 ALA   A C   
1005 O  O   . ALA   A 129 ? 0.1840 0.1751 0.2693 0.0048  0.0241  0.0158  135 ALA   A O   
1006 C  CB  . ALA   A 129 ? 0.1815 0.1657 0.2805 0.0111  0.0261  0.0203  135 ALA   A CB  
1007 N  N   . ASP   A 130 ? 0.1974 0.2030 0.2875 0.0015  0.0230  0.0263  136 ASP   A N   
1008 C  CA  . ASP   A 130 ? 0.2060 0.2166 0.2894 -0.0038 0.0228  0.0238  136 ASP   A CA  
1009 C  C   . ASP   A 130 ? 0.2053 0.2144 0.2886 -0.0049 0.0233  0.0216  136 ASP   A C   
1010 O  O   . ASP   A 130 ? 0.2087 0.2177 0.2973 -0.0035 0.0228  0.0255  136 ASP   A O   
1011 C  CB  . ASP   A 130 ? 0.2210 0.2444 0.3044 -0.0088 0.0214  0.0306  136 ASP   A CB  
1012 C  CG  . ASP   A 130 ? 0.3208 0.3506 0.3961 -0.0161 0.0219  0.0272  136 ASP   A CG  
1013 O  OD1 . ASP   A 130 ? 0.2692 0.2940 0.3391 -0.0170 0.0236  0.0200  136 ASP   A OD1 
1014 O  OD2 . ASP   A 130 ? 0.4099 0.4495 0.4845 -0.0213 0.0210  0.0316  136 ASP   A OD2 
1015 N  N   . VAL   A 131 ? 0.1976 0.2056 0.2759 -0.0075 0.0246  0.0153  137 VAL   A N   
1016 C  CA  . VAL   A 131 ? 0.1821 0.1909 0.2607 -0.0094 0.0258  0.0127  137 VAL   A CA  
1017 C  C   . VAL   A 131 ? 0.1971 0.2138 0.2704 -0.0163 0.0277  0.0098  137 VAL   A C   
1018 O  O   . VAL   A 131 ? 0.1900 0.2086 0.2634 -0.0186 0.0294  0.0070  137 VAL   A O   
1019 C  CB  . VAL   A 131 ? 0.1807 0.1804 0.2611 -0.0054 0.0266  0.0069  137 VAL   A CB  
1020 C  CG1 . VAL   A 131 ? 0.1973 0.1902 0.2816 -0.0003 0.0251  0.0088  137 VAL   A CG1 
1021 C  CG2 . VAL   A 131 ? 0.1848 0.1804 0.2624 -0.0053 0.0279  0.0011  137 VAL   A CG2 
1022 N  N   . ARG   A 132 ? 0.1944 0.2163 0.2630 -0.0204 0.0278  0.0102  138 ARG   A N   
1023 C  CA  . ARG   A 132 ? 0.1867 0.2155 0.2490 -0.0282 0.0304  0.0058  138 ARG   A CA  
1024 C  C   . ARG   A 132 ? 0.2139 0.2544 0.2743 -0.0348 0.0303  0.0095  138 ARG   A C   
1025 O  O   . ARG   A 132 ? 0.2245 0.2702 0.2796 -0.0418 0.0337  0.0038  138 ARG   A O   
1026 C  CB  . ARG   A 132 ? 0.1930 0.2252 0.2503 -0.0320 0.0303  0.0056  138 ARG   A CB  
1027 C  CG  . ARG   A 132 ? 0.2073 0.2282 0.2651 -0.0273 0.0313  0.0005  138 ARG   A CG  
1028 C  CD  . ARG   A 132 ? 0.2251 0.2502 0.2780 -0.0316 0.0309  0.0012  138 ARG   A CD  
1029 N  NE  . ARG   A 132 ? 0.2484 0.2794 0.3040 -0.0297 0.0271  0.0103  138 ARG   A NE  
1030 C  CZ  . ARG   A 132 ? 0.2628 0.2986 0.3162 -0.0322 0.0259  0.0129  138 ARG   A CZ  
1031 N  NH1 . ARG   A 132 ? 0.2633 0.2985 0.3104 -0.0375 0.0280  0.0071  138 ARG   A NH1 
1032 N  NH2 . ARG   A 132 ? 0.2553 0.2967 0.3137 -0.0295 0.0229  0.0213  138 ARG   A NH2 
1033 N  N   . ASP   A 133 ? 0.2074 0.2524 0.2720 -0.0335 0.0268  0.0191  139 ASP   A N   
1034 C  CA  . ASP   A 133 ? 0.2193 0.2758 0.2824 -0.0401 0.0260  0.0245  139 ASP   A CA  
1035 C  C   . ASP   A 133 ? 0.2173 0.2704 0.2833 -0.0388 0.0276  0.0218  139 ASP   A C   
1036 O  O   . ASP   A 133 ? 0.2225 0.2853 0.2865 -0.0452 0.0275  0.0254  139 ASP   A O   
1037 C  CB  . ASP   A 133 ? 0.2452 0.3085 0.3137 -0.0394 0.0214  0.0373  139 ASP   A CB  
1038 C  CG  . ASP   A 133 ? 0.3109 0.3634 0.3891 -0.0300 0.0202  0.0406  139 ASP   A CG  
1039 O  OD1 . ASP   A 133 ? 0.3012 0.3421 0.3808 -0.0236 0.0216  0.0345  139 ASP   A OD1 
1040 O  OD2 . ASP   A 133 ? 0.3238 0.3793 0.4080 -0.0297 0.0181  0.0492  139 ASP   A OD2 
1041 N  N   . LEU   A 134 ? 0.2106 0.2515 0.2811 -0.0314 0.0288  0.0166  140 LEU   A N   
1042 C  CA  . LEU   A 134 ? 0.2151 0.2530 0.2893 -0.0298 0.0300  0.0145  140 LEU   A CA  
1043 C  C   . LEU   A 134 ? 0.2238 0.2635 0.2949 -0.0337 0.0346  0.0049  140 LEU   A C   
1044 O  O   . LEU   A 134 ? 0.2241 0.2555 0.2984 -0.0291 0.0367  -0.0020 140 LEU   A O   
1045 C  CB  . LEU   A 134 ? 0.2168 0.2422 0.2972 -0.0211 0.0288  0.0136  140 LEU   A CB  
1046 C  CG  . LEU   A 134 ? 0.2225 0.2450 0.3071 -0.0171 0.0256  0.0214  140 LEU   A CG  
1047 C  CD1 . LEU   A 134 ? 0.2356 0.2464 0.3244 -0.0101 0.0253  0.0186  140 LEU   A CD1 
1048 C  CD2 . LEU   A 134 ? 0.2333 0.2617 0.3216 -0.0196 0.0239  0.0302  140 LEU   A CD2 
1049 N  N   . LEU   A 135 ? 0.2142 0.2655 0.2795 -0.0427 0.0365  0.0045  141 LEU   A N   
1050 C  CA  . LEU   A 135 ? 0.2287 0.2824 0.2908 -0.0476 0.0424  -0.0060 141 LEU   A CA  
1051 C  C   . LEU   A 135 ? 0.2236 0.2734 0.2921 -0.0443 0.0452  -0.0111 141 LEU   A C   
1052 O  O   . LEU   A 135 ? 0.2362 0.2828 0.3071 -0.0436 0.0503  -0.0205 141 LEU   A O   
1053 C  CB  . LEU   A 135 ? 0.2363 0.3047 0.2895 -0.0596 0.0444  -0.0059 141 LEU   A CB  
1054 C  CG  . LEU   A 135 ? 0.2592 0.3347 0.3063 -0.0643 0.0408  0.0009  141 LEU   A CG  
1055 C  CD1 . LEU   A 135 ? 0.2716 0.3632 0.3086 -0.0780 0.0430  -0.0001 141 LEU   A CD1 
1056 C  CD2 . LEU   A 135 ? 0.2567 0.3233 0.3038 -0.0599 0.0412  -0.0034 141 LEU   A CD2 
1057 N  N   . TRP   A 136 ? 0.2052 0.2557 0.2775 -0.0423 0.0422  -0.0045 142 TRP   A N   
1058 C  CA  . TRP   A 136 ? 0.2148 0.2632 0.2932 -0.0399 0.0442  -0.0081 142 TRP   A CA  
1059 C  C   . TRP   A 136 ? 0.2264 0.2634 0.3122 -0.0312 0.0445  -0.0131 142 TRP   A C   
1060 O  O   . TRP   A 136 ? 0.2367 0.2733 0.3286 -0.0294 0.0469  -0.0175 142 TRP   A O   
1061 C  CB  . TRP   A 136 ? 0.2224 0.2734 0.3030 -0.0404 0.0406  0.0005  142 TRP   A CB  
1062 C  CG  . TRP   A 136 ? 0.2179 0.2613 0.3011 -0.0346 0.0354  0.0084  142 TRP   A CG  
1063 C  CD1 . TRP   A 136 ? 0.2252 0.2718 0.3064 -0.0363 0.0320  0.0173  142 TRP   A CD1 
1064 C  CD2 . TRP   A 136 ? 0.2162 0.2484 0.3054 -0.0266 0.0336  0.0080  142 TRP   A CD2 
1065 N  NE1 . TRP   A 136 ? 0.2267 0.2637 0.3132 -0.0292 0.0290  0.0214  142 TRP   A NE1 
1066 C  CE2 . TRP   A 136 ? 0.2178 0.2460 0.3082 -0.0239 0.0300  0.0154  142 TRP   A CE2 
1067 C  CE3 . TRP   A 136 ? 0.2180 0.2443 0.3123 -0.0222 0.0347  0.0023  142 TRP   A CE3 
1068 C  CZ2 . TRP   A 136 ? 0.2222 0.2400 0.3171 -0.0174 0.0282  0.0158  142 TRP   A CZ2 
1069 C  CZ3 . TRP   A 136 ? 0.2280 0.2451 0.3261 -0.0163 0.0319  0.0038  142 TRP   A CZ3 
1070 C  CH2 . TRP   A 136 ? 0.2210 0.2337 0.3187 -0.0143 0.0291  0.0099  142 TRP   A CH2 
1071 N  N   . LEU   A 137 ? 0.2190 0.2478 0.3047 -0.0260 0.0419  -0.0118 143 LEU   A N   
1072 C  CA  . LEU   A 137 ? 0.2417 0.2610 0.3338 -0.0188 0.0417  -0.0155 143 LEU   A CA  
1073 C  C   . LEU   A 137 ? 0.2816 0.3007 0.3775 -0.0192 0.0471  -0.0244 143 LEU   A C   
1074 O  O   . LEU   A 137 ? 0.2692 0.2832 0.3733 -0.0138 0.0473  -0.0267 143 LEU   A O   
1075 C  CB  . LEU   A 137 ? 0.2330 0.2450 0.3231 -0.0147 0.0383  -0.0126 143 LEU   A CB  
1076 C  CG  . LEU   A 137 ? 0.2280 0.2372 0.3177 -0.0120 0.0338  -0.0052 143 LEU   A CG  
1077 C  CD1 . LEU   A 137 ? 0.2407 0.2446 0.3279 -0.0091 0.0318  -0.0035 143 LEU   A CD1 
1078 C  CD2 . LEU   A 137 ? 0.2264 0.2307 0.3220 -0.0077 0.0321  -0.0050 143 LEU   A CD2 
1079 N  N   . ASP   A 138 ? 0.3198 0.3449 0.4105 -0.0260 0.0518  -0.0292 144 ASP   A N   
1080 C  CA  . ASP   A 138 ? 0.3632 0.3876 0.4581 -0.0273 0.0585  -0.0390 144 ASP   A CA  
1081 C  C   . ASP   A 138 ? 0.4096 0.4402 0.5104 -0.0295 0.0637  -0.0443 144 ASP   A C   
1082 O  O   . ASP   A 138 ? 0.4077 0.4377 0.5137 -0.0305 0.0705  -0.0532 144 ASP   A O   
1083 C  CB  . ASP   A 138 ? 0.3930 0.4215 0.4787 -0.0352 0.0622  -0.0432 144 ASP   A CB  
1084 C  CG  . ASP   A 138 ? 0.4775 0.5009 0.5581 -0.0339 0.0586  -0.0398 144 ASP   A CG  
1085 O  OD1 . ASP   A 138 ? 0.5041 0.5187 0.5891 -0.0263 0.0546  -0.0360 144 ASP   A OD1 
1086 O  OD2 . ASP   A 138 ? 0.5287 0.5577 0.6002 -0.0414 0.0599  -0.0407 144 ASP   A OD2 
1087 N  N   . GLU   A 139 ? 0.4442 0.4807 0.5448 -0.0308 0.0613  -0.0395 145 GLU   A N   
1088 C  CA  . GLU   A 139 ? 0.4875 0.5315 0.5935 -0.0337 0.0664  -0.0445 145 GLU   A CA  
1089 C  C   . GLU   A 139 ? 0.5148 0.5599 0.6263 -0.0304 0.0625  -0.0390 145 GLU   A C   
1090 O  O   . GLU   A 139 ? 0.5188 0.5586 0.6293 -0.0263 0.0560  -0.0315 145 GLU   A O   
1091 C  CB  . GLU   A 139 ? 0.5433 0.5988 0.6391 -0.0449 0.0703  -0.0468 145 GLU   A CB  
1092 C  CG  . GLU   A 139 ? 0.6467 0.7073 0.7335 -0.0488 0.0640  -0.0361 145 GLU   A CG  
1093 C  CD  . GLU   A 139 ? 0.7804 0.8501 0.8552 -0.0589 0.0652  -0.0357 145 GLU   A CD  
1094 O  OE1 . GLU   A 139 ? 0.8185 0.8978 0.8871 -0.0655 0.0625  -0.0286 145 GLU   A OE1 
1095 O  OE2 . GLU   A 139 ? 0.8212 0.8889 0.8929 -0.0608 0.0686  -0.0421 145 GLU   A OE2 
1096 N  N   . GLU   A 140 ? 0.5371 0.5896 0.6544 -0.0329 0.0670  -0.0432 146 GLU   A N   
1097 C  CA  . GLU   A 140 ? 0.5679 0.6236 0.6909 -0.0315 0.0645  -0.0392 146 GLU   A CA  
1098 C  C   . GLU   A 140 ? 0.5908 0.6384 0.7240 -0.0224 0.0606  -0.0372 146 GLU   A C   
1099 O  O   . GLU   A 140 ? 0.6003 0.6497 0.7454 -0.0191 0.0639  -0.0417 146 GLU   A O   
1100 C  CB  . GLU   A 140 ? 0.6109 0.6702 0.7248 -0.0363 0.0596  -0.0304 146 GLU   A CB  
1101 C  CG  . GLU   A 140 ? 0.7093 0.7663 0.8279 -0.0331 0.0548  -0.0244 146 GLU   A CG  
1102 C  CD  . GLU   A 140 ? 0.8191 0.8852 0.9428 -0.0369 0.0576  -0.0259 146 GLU   A CD  
1103 O  OE1 . GLU   A 140 ? 0.8422 0.9093 0.9641 -0.0391 0.0540  -0.0194 146 GLU   A OE1 
1104 O  OE2 . GLU   A 140 ? 0.8544 0.9262 0.9844 -0.0376 0.0638  -0.0337 146 GLU   A OE2 
1105 N  N   . SER   B 1   ? 0.3067 0.3019 0.3954 -0.0076 0.0020  0.0607  7   SER   C N   
1106 C  CA  . SER   B 1   ? 0.2990 0.2952 0.3978 -0.0085 0.0017  0.0624  7   SER   C CA  
1107 C  C   . SER   B 1   ? 0.2919 0.2832 0.3871 -0.0084 0.0020  0.0573  7   SER   C C   
1108 O  O   . SER   B 1   ? 0.3135 0.3004 0.3979 -0.0081 0.0009  0.0531  7   SER   C O   
1109 C  CB  . SER   B 1   ? 0.3284 0.3281 0.4295 -0.0112 -0.0031 0.0681  7   SER   C CB  
1110 O  OG  . SER   B 1   ? 0.3972 0.3935 0.4869 -0.0134 -0.0075 0.0656  7   SER   C OG  
1111 N  N   . GLY   B 2   ? 0.2642 0.2562 0.3684 -0.0085 0.0036  0.0579  8   GLY   C N   
1112 C  CA  . GLY   B 2   ? 0.2549 0.2427 0.3559 -0.0086 0.0040  0.0541  8   GLY   C CA  
1113 C  C   . GLY   B 2   ? 0.2411 0.2298 0.3513 -0.0073 0.0083  0.0534  8   GLY   C C   
1114 O  O   . GLY   B 2   ? 0.2376 0.2285 0.3544 -0.0056 0.0117  0.0536  8   GLY   C O   
1115 N  N   . ALA   B 3   ? 0.2349 0.2214 0.3449 -0.0082 0.0083  0.0525  9   ALA   C N   
1116 C  CA  . ALA   B 3   ? 0.2199 0.2071 0.3369 -0.0070 0.0127  0.0516  9   ALA   C CA  
1117 C  C   . ALA   B 3   ? 0.2211 0.2037 0.3311 -0.0071 0.0131  0.0484  9   ALA   C C   
1118 O  O   . ALA   B 3   ? 0.2265 0.2056 0.3288 -0.0086 0.0097  0.0480  9   ALA   C O   
1119 C  CB  . ALA   B 3   ? 0.2330 0.2250 0.3622 -0.0084 0.0132  0.0567  9   ALA   C CB  
1120 N  N   . ILE   B 4   ? 0.2074 0.1898 0.3199 -0.0055 0.0174  0.0463  10  ILE   C N   
1121 C  CA  . ILE   B 4   ? 0.2026 0.1814 0.3095 -0.0056 0.0183  0.0444  10  ILE   C CA  
1122 C  C   . ILE   B 4   ? 0.2163 0.1980 0.3322 -0.0069 0.0208  0.0477  10  ILE   C C   
1123 O  O   . ILE   B 4   ? 0.2113 0.1970 0.3368 -0.0059 0.0242  0.0487  10  ILE   C O   
1124 C  CB  . ILE   B 4   ? 0.2039 0.1811 0.3068 -0.0029 0.0215  0.0397  10  ILE   C CB  
1125 C  CG1 . ILE   B 4   ? 0.2190 0.1952 0.3163 -0.0012 0.0199  0.0367  10  ILE   C CG1 
1126 C  CG2 . ILE   B 4   ? 0.2204 0.1939 0.3164 -0.0029 0.0221  0.0386  10  ILE   C CG2 
1127 C  CD1 . ILE   B 4   ? 0.2376 0.2139 0.3335 0.0011  0.0227  0.0323  10  ILE   C CD1 
1128 N  N   . TYR   B 5   ? 0.2148 0.1946 0.3284 -0.0090 0.0196  0.0493  11  TYR   C N   
1129 C  CA  . TYR   B 5   ? 0.2222 0.2053 0.3447 -0.0105 0.0222  0.0528  11  TYR   C CA  
1130 C  C   . TYR   B 5   ? 0.2253 0.2050 0.3417 -0.0099 0.0254  0.0511  11  TYR   C C   
1131 O  O   . TYR   B 5   ? 0.2438 0.2189 0.3527 -0.0114 0.0230  0.0512  11  TYR   C O   
1132 C  CB  . TYR   B 5   ? 0.2209 0.2056 0.3474 -0.0143 0.0177  0.0573  11  TYR   C CB  
1133 C  CG  . TYR   B 5   ? 0.2304 0.2195 0.3631 -0.0148 0.0146  0.0599  11  TYR   C CG  
1134 C  CD1 . TYR   B 5   ? 0.2352 0.2308 0.3811 -0.0142 0.0170  0.0635  11  TYR   C CD1 
1135 C  CD2 . TYR   B 5   ? 0.2460 0.2327 0.3709 -0.0155 0.0097  0.0588  11  TYR   C CD2 
1136 C  CE1 . TYR   B 5   ? 0.2504 0.2502 0.4020 -0.0145 0.0140  0.0666  11  TYR   C CE1 
1137 C  CE2 . TYR   B 5   ? 0.2672 0.2581 0.3966 -0.0159 0.0070  0.0616  11  TYR   C CE2 
1138 C  CZ  . TYR   B 5   ? 0.2772 0.2747 0.4199 -0.0154 0.0090  0.0657  11  TYR   C CZ  
1139 O  OH  . TYR   B 5   ? 0.3039 0.3056 0.4510 -0.0155 0.0062  0.0692  11  TYR   C OH  
1140 N  N   . VAL   B 6   ? 0.2186 0.2000 0.3376 -0.0078 0.0309  0.0494  12  VAL   C N   
1141 C  CA  . VAL   B 6   ? 0.2306 0.2092 0.3428 -0.0071 0.0343  0.0478  12  VAL   C CA  
1142 C  C   . VAL   B 6   ? 0.2342 0.2169 0.3548 -0.0070 0.0402  0.0496  12  VAL   C C   
1143 O  O   . VAL   B 6   ? 0.2256 0.2117 0.3539 -0.0053 0.0435  0.0486  12  VAL   C O   
1144 C  CB  . VAL   B 6   ? 0.2603 0.2359 0.3628 -0.0042 0.0349  0.0424  12  VAL   C CB  
1145 C  CG1 . VAL   B 6   ? 0.2546 0.2331 0.3627 -0.0022 0.0373  0.0394  12  VAL   C CG1 
1146 C  CG2 . VAL   B 6   ? 0.2882 0.2614 0.3829 -0.0035 0.0380  0.0414  12  VAL   C CG2 
1147 N  N   . GLY   B 7   ? 0.2401 0.2225 0.3603 -0.0088 0.0419  0.0526  13  GLY   C N   
1148 C  CA  . GLY   B 7   ? 0.2394 0.2265 0.3684 -0.0086 0.0483  0.0547  13  GLY   C CA  
1149 C  C   . GLY   B 7   ? 0.2377 0.2310 0.3822 -0.0091 0.0484  0.0580  13  GLY   C C   
1150 O  O   . GLY   B 7   ? 0.2562 0.2507 0.4048 -0.0115 0.0429  0.0611  13  GLY   C O   
1151 N  N   . ASN   B 8   ? 0.2302 0.2271 0.3828 -0.0066 0.0542  0.0568  14  ASN   C N   
1152 C  CA  . ASN   B 8   ? 0.2269 0.2296 0.3949 -0.0064 0.0542  0.0602  14  ASN   C CA  
1153 C  C   . ASN   B 8   ? 0.2117 0.2132 0.3802 -0.0040 0.0530  0.0569  14  ASN   C C   
1154 O  O   . ASN   B 8   ? 0.2119 0.2168 0.3920 -0.0021 0.0563  0.0577  14  ASN   C O   
1155 C  CB  . ASN   B 8   ? 0.2510 0.2592 0.4312 -0.0053 0.0614  0.0626  14  ASN   C CB  
1156 C  CG  . ASN   B 8   ? 0.3268 0.3382 0.5112 -0.0085 0.0614  0.0679  14  ASN   C CG  
1157 O  OD1 . ASN   B 8   ? 0.3473 0.3641 0.5435 -0.0107 0.0584  0.0733  14  ASN   C OD1 
1158 N  ND2 . ASN   B 8   ? 0.3483 0.3566 0.5231 -0.0091 0.0645  0.0667  14  ASN   C ND2 
1159 N  N   . TYR   B 9   ? 0.1946 0.1914 0.3515 -0.0042 0.0484  0.0537  15  TYR   C N   
1160 C  CA  . TYR   B 9   ? 0.2024 0.1980 0.3594 -0.0024 0.0470  0.0508  15  TYR   C CA  
1161 C  C   . TYR   B 9   ? 0.1952 0.1902 0.3490 -0.0041 0.0399  0.0528  15  TYR   C C   
1162 O  O   . TYR   B 9   ? 0.2042 0.1967 0.3497 -0.0061 0.0358  0.0533  15  TYR   C O   
1163 C  CB  . TYR   B 9   ? 0.2144 0.2053 0.3601 -0.0005 0.0489  0.0441  15  TYR   C CB  
1164 C  CG  . TYR   B 9   ? 0.2348 0.2255 0.3808 0.0013  0.0560  0.0409  15  TYR   C CG  
1165 C  CD1 . TYR   B 9   ? 0.2502 0.2431 0.4075 0.0032  0.0611  0.0404  15  TYR   C CD1 
1166 C  CD2 . TYR   B 9   ? 0.2643 0.2522 0.3988 0.0013  0.0576  0.0383  15  TYR   C CD2 
1167 C  CE1 . TYR   B 9   ? 0.2795 0.2717 0.4361 0.0050  0.0680  0.0366  15  TYR   C CE1 
1168 C  CE2 . TYR   B 9   ? 0.2901 0.2778 0.4231 0.0030  0.0642  0.0349  15  TYR   C CE2 
1169 C  CZ  . TYR   B 9   ? 0.3143 0.3039 0.4580 0.0048  0.0695  0.0336  15  TYR   C CZ  
1170 O  OH  . TYR   B 9   ? 0.3769 0.3659 0.5185 0.0065  0.0765  0.0297  15  TYR   C OH  
1171 N  N   . ARG   B 10  ? 0.1785 0.1753 0.3385 -0.0032 0.0386  0.0537  16  ARG   C N   
1172 C  CA  . ARG   B 10  ? 0.1859 0.1823 0.3421 -0.0043 0.0327  0.0550  16  ARG   C CA  
1173 C  C   . ARG   B 10  ? 0.1872 0.1812 0.3403 -0.0022 0.0339  0.0508  16  ARG   C C   
1174 O  O   . ARG   B 10  ? 0.1822 0.1775 0.3440 -0.0004 0.0377  0.0504  16  ARG   C O   
1175 C  CB  . ARG   B 10  ? 0.1957 0.1975 0.3636 -0.0054 0.0302  0.0614  16  ARG   C CB  
1176 C  CG  . ARG   B 10  ? 0.2095 0.2116 0.3743 -0.0061 0.0250  0.0630  16  ARG   C CG  
1177 C  CD  . ARG   B 10  ? 0.2156 0.2236 0.3906 -0.0076 0.0216  0.0700  16  ARG   C CD  
1178 N  NE  . ARG   B 10  ? 0.2336 0.2432 0.4117 -0.0066 0.0202  0.0724  16  ARG   C NE  
1179 C  CZ  . ARG   B 10  ? 0.2487 0.2581 0.4194 -0.0080 0.0151  0.0737  16  ARG   C CZ  
1180 N  NH1 . ARG   B 10  ? 0.2429 0.2497 0.4021 -0.0103 0.0108  0.0720  16  ARG   C NH1 
1181 N  NH2 . ARG   B 10  ? 0.2634 0.2747 0.4378 -0.0069 0.0145  0.0767  16  ARG   C NH2 
1182 N  N   . VAL   B 11  ? 0.1774 0.1679 0.3189 -0.0022 0.0310  0.0475  17  VAL   C N   
1183 C  CA  . VAL   B 11  ? 0.1792 0.1681 0.3181 -0.0006 0.0318  0.0436  17  VAL   C CA  
1184 C  C   . VAL   B 11  ? 0.1868 0.1768 0.3248 -0.0013 0.0278  0.0461  17  VAL   C C   
1185 O  O   . VAL   B 11  ? 0.1951 0.1839 0.3252 -0.0025 0.0237  0.0468  17  VAL   C O   
1186 C  CB  . VAL   B 11  ? 0.2034 0.1886 0.3306 0.0002  0.0317  0.0382  17  VAL   C CB  
1187 C  CG1 . VAL   B 11  ? 0.2280 0.2127 0.3546 0.0016  0.0328  0.0340  17  VAL   C CG1 
1188 C  CG2 . VAL   B 11  ? 0.2214 0.2053 0.3461 0.0004  0.0348  0.0365  17  VAL   C CG2 
1189 N  N   . VAL   B 12  ? 0.1797 0.1717 0.3255 -0.0005 0.0292  0.0475  18  VAL   C N   
1190 C  CA  A VAL   B 12  ? 0.1731 0.1665 0.3180 -0.0011 0.0259  0.0505  18  VAL   C CA  
1191 C  CA  B VAL   B 12  ? 0.1978 0.1915 0.3438 -0.0011 0.0260  0.0509  18  VAL   C CA  
1192 C  C   . VAL   B 12  ? 0.1967 0.1897 0.3435 0.0002  0.0281  0.0482  18  VAL   C C   
1193 O  O   . VAL   B 12  ? 0.1998 0.1915 0.3511 0.0013  0.0320  0.0447  18  VAL   C O   
1194 C  CB  A VAL   B 12  ? 0.1622 0.1598 0.3170 -0.0019 0.0246  0.0574  18  VAL   C CB  
1195 C  CB  B VAL   B 12  ? 0.2323 0.2302 0.3901 -0.0015 0.0257  0.0577  18  VAL   C CB  
1196 C  CG1 A VAL   B 12  ? 0.1612 0.1600 0.3137 -0.0040 0.0210  0.0602  18  VAL   C CG1 
1197 C  CG1 B VAL   B 12  ? 0.2394 0.2395 0.3935 -0.0032 0.0205  0.0623  18  VAL   C CG1 
1198 C  CG2 A VAL   B 12  ? 0.1380 0.1371 0.3065 -0.0004 0.0292  0.0588  18  VAL   C CG2 
1199 C  CG2 B VAL   B 12  ? 0.2555 0.2554 0.4210 -0.0018 0.0272  0.0598  18  VAL   C CG2 
1200 N  N   . ASN   B 13  ? 0.1795 0.1736 0.3232 -0.0002 0.0257  0.0501  19  ASN   C N   
1201 C  CA  . ASN   B 13  ? 0.1710 0.1653 0.3184 0.0006  0.0280  0.0490  19  ASN   C CA  
1202 C  C   . ASN   B 13  ? 0.1713 0.1670 0.3326 0.0010  0.0308  0.0530  19  ASN   C C   
1203 O  O   . ASN   B 13  ? 0.1687 0.1669 0.3348 0.0005  0.0292  0.0588  19  ASN   C O   
1204 C  CB  . ASN   B 13  ? 0.1821 0.1780 0.3245 0.0001  0.0255  0.0519  19  ASN   C CB  
1205 C  CG  . ASN   B 13  ? 0.2014 0.1957 0.3311 0.0002  0.0232  0.0480  19  ASN   C CG  
1206 O  OD1 . ASN   B 13  ? 0.2224 0.2159 0.3448 -0.0006 0.0199  0.0491  19  ASN   C OD1 
1207 N  ND2 . ASN   B 13  ? 0.1859 0.1796 0.3134 0.0012  0.0248  0.0436  19  ASN   C ND2 
1208 N  N   . ARG   B 14  ? 0.1697 0.1637 0.3377 0.0018  0.0348  0.0498  20  ARG   C N   
1209 C  CA  . ARG   B 14  ? 0.1690 0.1631 0.3507 0.0026  0.0380  0.0531  20  ARG   C CA  
1210 C  C   . ARG   B 14  ? 0.1868 0.1837 0.3737 0.0022  0.0362  0.0609  20  ARG   C C   
1211 O  O   . ARG   B 14  ? 0.1913 0.1900 0.3878 0.0028  0.0365  0.0666  20  ARG   C O   
1212 C  CB  . ARG   B 14  ? 0.1718 0.1626 0.3586 0.0031  0.0422  0.0476  20  ARG   C CB  
1213 C  CG  . ARG   B 14  ? 0.1869 0.1762 0.3882 0.0043  0.0464  0.0498  20  ARG   C CG  
1214 C  CD  . ARG   B 14  ? 0.1990 0.1843 0.4043 0.0042  0.0500  0.0438  20  ARG   C CD  
1215 N  NE  . ARG   B 14  ? 0.1977 0.1797 0.4161 0.0055  0.0548  0.0437  20  ARG   C NE  
1216 C  CZ  . ARG   B 14  ? 0.2024 0.1837 0.4325 0.0060  0.0563  0.0490  20  ARG   C CZ  
1217 N  NH1 . ARG   B 14  ? 0.2082 0.1923 0.4379 0.0051  0.0533  0.0553  20  ARG   C NH1 
1218 N  NH2 . ARG   B 14  ? 0.1933 0.1704 0.4351 0.0074  0.0611  0.0479  20  ARG   C NH2 
1219 N  N   . HIS   B 15  ? 0.1903 0.1880 0.3707 0.0014  0.0344  0.0615  21  HIS   C N   
1220 C  CA  . HIS   B 15  ? 0.1868 0.1873 0.3704 0.0010  0.0329  0.0691  21  HIS   C CA  
1221 C  C   . HIS   B 15  ? 0.2045 0.2084 0.3841 0.0003  0.0283  0.0748  21  HIS   C C   
1222 O  O   . HIS   B 15  ? 0.2230 0.2298 0.4058 0.0000  0.0267  0.0818  21  HIS   C O   
1223 C  CB  . HIS   B 15  ? 0.2012 0.2021 0.3793 0.0004  0.0331  0.0684  21  HIS   C CB  
1224 C  CG  . HIS   B 15  ? 0.2157 0.2176 0.3794 -0.0002 0.0298  0.0661  21  HIS   C CG  
1225 N  ND1 . HIS   B 15  ? 0.2410 0.2410 0.3974 0.0001  0.0300  0.0588  21  HIS   C ND1 
1226 C  CD2 . HIS   B 15  ? 0.2255 0.2298 0.3811 -0.0008 0.0265  0.0702  21  HIS   C CD2 
1227 C  CE1 . HIS   B 15  ? 0.2431 0.2440 0.3880 -0.0001 0.0271  0.0587  21  HIS   C CE1 
1228 N  NE2 . HIS   B 15  ? 0.2385 0.2418 0.3820 -0.0008 0.0250  0.0650  21  HIS   C NE2 
1229 N  N   . LEU   B 16  ? 0.1983 0.2021 0.3713 -0.0002 0.0260  0.0720  22  LEU   C N   
1230 C  CA  . LEU   B 16  ? 0.2076 0.2145 0.3776 -0.0015 0.0213  0.0768  22  LEU   C CA  
1231 C  C   . LEU   B 16  ? 0.2129 0.2212 0.3923 -0.0012 0.0217  0.0786  22  LEU   C C   
1232 O  O   . LEU   B 16  ? 0.2249 0.2360 0.4025 -0.0027 0.0176  0.0817  22  LEU   C O   
1233 C  CB  . LEU   B 16  ? 0.2100 0.2154 0.3649 -0.0028 0.0179  0.0728  22  LEU   C CB  
1234 C  CG  . LEU   B 16  ? 0.2290 0.2338 0.3744 -0.0028 0.0175  0.0715  22  LEU   C CG  
1235 C  CD1 . LEU   B 16  ? 0.2341 0.2366 0.3652 -0.0035 0.0146  0.0670  22  LEU   C CD1 
1236 C  CD2 . LEU   B 16  ? 0.2258 0.2342 0.3722 -0.0034 0.0156  0.0788  22  LEU   C CD2 
1237 N  N   . ALA   B 17  ? 0.2065 0.2129 0.3954 0.0005  0.0267  0.0760  23  ALA   C N   
1238 C  CA  . ALA   B 17  ? 0.2157 0.2238 0.4138 0.0011  0.0282  0.0773  23  ALA   C CA  
1239 C  C   . ALA   B 17  ? 0.2253 0.2386 0.4345 0.0013  0.0260  0.0861  23  ALA   C C   
1240 O  O   . ALA   B 17  ? 0.2255 0.2397 0.4397 0.0020  0.0259  0.0907  23  ALA   C O   
1241 C  CB  . ALA   B 17  ? 0.2216 0.2262 0.4270 0.0032  0.0346  0.0724  23  ALA   C CB  
1242 N  N   . THR   B 18  ? 0.2271 0.2441 0.4403 0.0005  0.0240  0.0889  24  THR   C N   
1243 C  CA  . THR   B 18  ? 0.2157 0.2389 0.4403 0.0006  0.0212  0.0977  24  THR   C CA  
1244 C  C   . THR   B 18  ? 0.2238 0.2481 0.4659 0.0036  0.0268  0.0995  24  THR   C C   
1245 O  O   . THR   B 18  ? 0.2261 0.2461 0.4696 0.0052  0.0326  0.0934  24  THR   C O   
1246 C  CB  . THR   B 18  ? 0.2397 0.2671 0.4605 -0.0023 0.0157  0.0996  24  THR   C CB  
1247 O  OG1 . THR   B 18  ? 0.2518 0.2785 0.4761 -0.0020 0.0193  0.0958  24  THR   C OG1 
1248 C  CG2 . THR   B 18  ? 0.2522 0.2776 0.4554 -0.0052 0.0104  0.0968  24  THR   C CG2 
1249 N  N   . HIS   B 19  ? 0.2111 0.2414 0.4669 0.0045  0.0249  0.1082  25  HIS   C N   
1250 C  CA  . HIS   B 19  ? 0.2249 0.2567 0.4984 0.0078  0.0303  0.1103  25  HIS   C CA  
1251 C  C   . HIS   B 19  ? 0.2092 0.2418 0.4835 0.0075  0.0331  0.1060  25  HIS   C C   
1252 O  O   . HIS   B 19  ? 0.2242 0.2538 0.5056 0.0101  0.0401  0.1021  25  HIS   C O   
1253 C  CB  . HIS   B 19  ? 0.2483 0.2879 0.5361 0.0086  0.0266  0.1211  25  HIS   C CB  
1254 C  CG  . HIS   B 19  ? 0.3047 0.3474 0.6117 0.0120  0.0317  0.1239  25  HIS   C CG  
1255 N  ND1 . HIS   B 19  ? 0.3330 0.3716 0.6519 0.0160  0.0383  0.1237  25  HIS   C ND1 
1256 C  CD2 . HIS   B 19  ? 0.3277 0.3768 0.6437 0.0119  0.0316  0.1262  25  HIS   C CD2 
1257 C  CE1 . HIS   B 19  ? 0.3348 0.3775 0.6696 0.0187  0.0420  0.1264  25  HIS   C CE1 
1258 N  NE2 . HIS   B 19  ? 0.3372 0.3868 0.6712 0.0163  0.0383  0.1280  25  HIS   C NE2 
1259 N  N   . ASN   B 20  ? 0.2050 0.2411 0.4717 0.0042  0.0280  0.1064  26  ASN   C N   
1260 C  CA  . ASN   B 20  ? 0.2114 0.2482 0.4789 0.0036  0.0310  0.1029  26  ASN   C CA  
1261 C  C   . ASN   B 20  ? 0.2098 0.2387 0.4671 0.0045  0.0366  0.0934  26  ASN   C C   
1262 O  O   . ASN   B 20  ? 0.2025 0.2307 0.4643 0.0060  0.0425  0.0902  26  ASN   C O   
1263 C  CB  . ASN   B 20  ? 0.2476 0.2881 0.5078 -0.0006 0.0242  0.1046  26  ASN   C CB  
1264 C  CG  . ASN   B 20  ? 0.3383 0.3808 0.6028 -0.0012 0.0277  0.1030  26  ASN   C CG  
1265 O  OD1 . ASN   B 20  ? 0.3567 0.4055 0.6374 0.0002  0.0301  0.1077  26  ASN   C OD1 
1266 N  ND2 . ASN   B 20  ? 0.3626 0.3999 0.6135 -0.0030 0.0285  0.0966  26  ASN   C ND2 
1267 N  N   . ASP   B 21  ? 0.2002 0.2237 0.4433 0.0035  0.0348  0.0889  27  ASP   C N   
1268 C  CA  . ASP   B 21  ? 0.2018 0.2185 0.4353 0.0042  0.0393  0.0801  27  ASP   C CA  
1269 C  C   . ASP   B 21  ? 0.2075 0.2213 0.4512 0.0077  0.0467  0.0775  27  ASP   C C   
1270 O  O   . ASP   B 21  ? 0.2126 0.2236 0.4550 0.0088  0.0520  0.0719  27  ASP   C O   
1271 C  CB  . ASP   B 21  ? 0.2132 0.2258 0.4326 0.0029  0.0360  0.0767  27  ASP   C CB  
1272 C  CG  . ASP   B 21  ? 0.2285 0.2414 0.4348 -0.0001 0.0301  0.0764  27  ASP   C CG  
1273 O  OD1 . ASP   B 21  ? 0.2289 0.2419 0.4321 -0.0013 0.0302  0.0749  27  ASP   C OD1 
1274 O  OD2 . ASP   B 21  ? 0.2263 0.2388 0.4252 -0.0013 0.0258  0.0777  27  ASP   C OD2 
1275 N  N   . TRP   B 22  ? 0.2038 0.2177 0.4570 0.0093  0.0470  0.0815  28  TRP   C N   
1276 C  CA  . TRP   B 22  ? 0.2032 0.2133 0.4669 0.0125  0.0540  0.0790  28  TRP   C CA  
1277 C  C   . TRP   B 22  ? 0.2009 0.2142 0.4783 0.0150  0.0591  0.0807  28  TRP   C C   
1278 O  O   . TRP   B 22  ? 0.2009 0.2098 0.4822 0.0173  0.0660  0.0753  28  TRP   C O   
1279 C  CB  . TRP   B 22  ? 0.1979 0.2073 0.4695 0.0136  0.0531  0.0839  28  TRP   C CB  
1280 C  CG  . TRP   B 22  ? 0.2021 0.2069 0.4623 0.0119  0.0513  0.0800  28  TRP   C CG  
1281 C  CD1 . TRP   B 22  ? 0.2138 0.2205 0.4654 0.0097  0.0454  0.0833  28  TRP   C CD1 
1282 C  CD2 . TRP   B 22  ? 0.2033 0.2012 0.4596 0.0123  0.0556  0.0718  28  TRP   C CD2 
1283 N  NE1 . TRP   B 22  ? 0.2228 0.2247 0.4668 0.0090  0.0463  0.0783  28  TRP   C NE1 
1284 C  CE2 . TRP   B 22  ? 0.2179 0.2145 0.4650 0.0103  0.0521  0.0713  28  TRP   C CE2 
1285 C  CE3 . TRP   B 22  ? 0.2090 0.2020 0.4697 0.0141  0.0622  0.0651  28  TRP   C CE3 
1286 C  CZ2 . TRP   B 22  ? 0.2220 0.2133 0.4649 0.0098  0.0545  0.0644  28  TRP   C CZ2 
1287 C  CZ3 . TRP   B 22  ? 0.2287 0.2157 0.4836 0.0134  0.0642  0.0578  28  TRP   C CZ3 
1288 C  CH2 . TRP   B 22  ? 0.2303 0.2169 0.4773 0.0112  0.0602  0.0578  28  TRP   C CH2 
1289 N  N   . ALA   B 23  ? 0.1957 0.2166 0.4807 0.0144  0.0558  0.0881  29  ALA   C N   
1290 C  CA  . ALA   B 23  ? 0.2084 0.2336 0.5077 0.0168  0.0605  0.0906  29  ALA   C CA  
1291 C  C   . ALA   B 23  ? 0.2281 0.2527 0.5198 0.0159  0.0642  0.0847  29  ALA   C C   
1292 O  O   . ALA   B 23  ? 0.2387 0.2664 0.5413 0.0181  0.0698  0.0854  29  ALA   C O   
1293 C  CB  . ALA   B 23  ? 0.2094 0.2441 0.5200 0.0160  0.0551  0.1008  29  ALA   C CB  
1294 N  N   . ASN   B 24  ? 0.2211 0.2423 0.4948 0.0128  0.0610  0.0797  30  ASN   C N   
1295 C  CA  . ASN   B 24  ? 0.2189 0.2389 0.4840 0.0119  0.0642  0.0745  30  ASN   C CA  
1296 C  C   . ASN   B 24  ? 0.2222 0.2342 0.4714 0.0116  0.0655  0.0656  30  ASN   C C   
1297 O  O   . ASN   B 24  ? 0.2135 0.2237 0.4488 0.0094  0.0635  0.0623  30  ASN   C O   
1298 C  CB  . ASN   B 24  ? 0.2315 0.2561 0.4911 0.0081  0.0578  0.0785  30  ASN   C CB  
1299 C  CG  . ASN   B 24  ? 0.2425 0.2759 0.5185 0.0081  0.0569  0.0867  30  ASN   C CG  
1300 O  OD1 . ASN   B 24  ? 0.2649 0.3015 0.5493 0.0093  0.0624  0.0872  30  ASN   C OD1 
1301 N  ND2 . ASN   B 24  ? 0.2366 0.2743 0.5175 0.0068  0.0501  0.0932  30  ASN   C ND2 
1302 N  N   . LEU   B 25  ? 0.2265 0.2337 0.4781 0.0137  0.0685  0.0622  31  LEU   C N   
1303 C  CA  . LEU   B 25  ? 0.2159 0.2164 0.4544 0.0131  0.0688  0.0543  31  LEU   C CA  
1304 C  C   . LEU   B 25  ? 0.2407 0.2378 0.4701 0.0135  0.0738  0.0468  31  LEU   C C   
1305 O  O   . LEU   B 25  ? 0.2507 0.2481 0.4873 0.0158  0.0804  0.0454  31  LEU   C O   
1306 C  CB  . LEU   B 25  ? 0.2076 0.2040 0.4535 0.0149  0.0710  0.0529  31  LEU   C CB  
1307 C  CG  . LEU   B 25  ? 0.2204 0.2106 0.4548 0.0139  0.0707  0.0452  31  LEU   C CG  
1308 C  CD1 . LEU   B 25  ? 0.2245 0.2159 0.4473 0.0111  0.0634  0.0466  31  LEU   C CD1 
1309 C  CD2 . LEU   B 25  ? 0.2414 0.2273 0.4854 0.0154  0.0738  0.0438  31  LEU   C CD2 
1310 N  N   . VAL   B 26  ? 0.2302 0.2245 0.4436 0.0115  0.0707  0.0421  32  VAL   C N   
1311 C  CA  . VAL   B 26  ? 0.2309 0.2218 0.4333 0.0118  0.0745  0.0350  32  VAL   C CA  
1312 C  C   . VAL   B 26  ? 0.2373 0.2226 0.4334 0.0119  0.0748  0.0277  32  VAL   C C   
1313 O  O   . VAL   B 26  ? 0.2494 0.2311 0.4447 0.0133  0.0803  0.0214  32  VAL   C O   
1314 C  CB  . VAL   B 26  ? 0.2472 0.2393 0.4365 0.0095  0.0706  0.0356  32  VAL   C CB  
1315 C  CG1 . VAL   B 26  ? 0.2623 0.2505 0.4382 0.0097  0.0734  0.0283  32  VAL   C CG1 
1316 C  CG2 . VAL   B 26  ? 0.2450 0.2424 0.4410 0.0089  0.0708  0.0421  32  VAL   C CG2 
1317 N  N   . TRP   B 27  ? 0.2209 0.2056 0.4130 0.0104  0.0691  0.0283  33  TRP   C N   
1318 C  CA  . TRP   B 27  ? 0.2175 0.1979 0.4043 0.0100  0.0687  0.0219  33  TRP   C CA  
1319 C  C   . TRP   B 27  ? 0.2242 0.2057 0.4119 0.0087  0.0632  0.0254  33  TRP   C C   
1320 O  O   . TRP   B 27  ? 0.2260 0.2107 0.4107 0.0076  0.0586  0.0306  33  TRP   C O   
1321 C  CB  . TRP   B 27  ? 0.2301 0.2090 0.4008 0.0091  0.0674  0.0161  33  TRP   C CB  
1322 C  CG  . TRP   B 27  ? 0.2443 0.2206 0.4079 0.0081  0.0650  0.0102  33  TRP   C CG  
1323 C  CD1 . TRP   B 27  ? 0.2708 0.2433 0.4337 0.0082  0.0680  0.0029  33  TRP   C CD1 
1324 C  CD2 . TRP   B 27  ? 0.2431 0.2205 0.3992 0.0067  0.0590  0.0109  33  TRP   C CD2 
1325 N  NE1 . TRP   B 27  ? 0.2813 0.2533 0.4379 0.0067  0.0639  -0.0006 33  TRP   C NE1 
1326 C  CE2 . TRP   B 27  ? 0.2577 0.2329 0.4103 0.0060  0.0586  0.0043  33  TRP   C CE2 
1327 C  CE3 . TRP   B 27  ? 0.2453 0.2254 0.3979 0.0059  0.0541  0.0162  33  TRP   C CE3 
1328 C  CZ2 . TRP   B 27  ? 0.2616 0.2380 0.4078 0.0049  0.0537  0.0034  33  TRP   C CZ2 
1329 C  CZ3 . TRP   B 27  ? 0.2588 0.2392 0.4043 0.0051  0.0497  0.0147  33  TRP   C CZ3 
1330 C  CH2 . TRP   B 27  ? 0.2616 0.2405 0.4046 0.0047  0.0496  0.0087  33  TRP   C CH2 
1331 N  N   . GLU   B 28  ? 0.2117 0.1904 0.4038 0.0086  0.0640  0.0227  34  GLU   C N   
1332 C  CA  . GLU   B 28  ? 0.2140 0.1938 0.4062 0.0073  0.0595  0.0259  34  GLU   C CA  
1333 C  C   . GLU   B 28  ? 0.2200 0.1965 0.4098 0.0064  0.0597  0.0194  34  GLU   C C   
1334 O  O   . GLU   B 28  ? 0.2137 0.1864 0.4070 0.0069  0.0640  0.0138  34  GLU   C O   
1335 C  CB  . GLU   B 28  ? 0.2325 0.2142 0.4380 0.0080  0.0596  0.0336  34  GLU   C CB  
1336 C  CG  . GLU   B 28  ? 0.2525 0.2312 0.4717 0.0099  0.0652  0.0332  34  GLU   C CG  
1337 C  CD  . GLU   B 28  ? 0.2857 0.2600 0.5098 0.0093  0.0667  0.0299  34  GLU   C CD  
1338 O  OE1 . GLU   B 28  ? 0.2953 0.2650 0.5270 0.0106  0.0719  0.0259  34  GLU   C OE1 
1339 O  OE2 . GLU   B 28  ? 0.2431 0.2183 0.4634 0.0076  0.0630  0.0311  34  GLU   C OE2 
1340 N  N   . ASP   B 29  ? 0.2027 0.1808 0.3875 0.0050  0.0555  0.0202  35  ASP   C N   
1341 C  CA  . ASP   B 29  ? 0.2107 0.1868 0.3949 0.0037  0.0554  0.0148  35  ASP   C CA  
1342 C  C   . ASP   B 29  ? 0.2071 0.1858 0.3936 0.0027  0.0523  0.0196  35  ASP   C C   
1343 O  O   . ASP   B 29  ? 0.2076 0.1893 0.3858 0.0024  0.0485  0.0216  35  ASP   C O   
1344 C  CB  . ASP   B 29  ? 0.2320 0.2080 0.4038 0.0032  0.0537  0.0080  35  ASP   C CB  
1345 C  CG  . ASP   B 29  ? 0.3143 0.2891 0.4855 0.0016  0.0530  0.0018  35  ASP   C CG  
1346 O  OD1 . ASP   B 29  ? 0.3183 0.2941 0.4956 0.0005  0.0520  0.0041  35  ASP   C OD1 
1347 O  OD2 . ASP   B 29  ? 0.3441 0.3175 0.5084 0.0012  0.0532  -0.0050 35  ASP   C OD2 
1348 N  N   . SER   B 30  ? 0.1957 0.1728 0.3934 0.0023  0.0543  0.0218  36  SER   C N   
1349 C  CA  A SER   B 30  ? 0.1860 0.1656 0.3865 0.0012  0.0523  0.0270  36  SER   C CA  
1350 C  CA  B SER   B 30  ? 0.1991 0.1788 0.3994 0.0013  0.0522  0.0270  36  SER   C CA  
1351 C  C   . SER   B 30  ? 0.1936 0.1752 0.3868 -0.0003 0.0497  0.0228  36  SER   C C   
1352 O  O   . SER   B 30  ? 0.1924 0.1776 0.3813 -0.0006 0.0469  0.0267  36  SER   C O   
1353 C  CB  A SER   B 30  ? 0.1889 0.1656 0.4035 0.0010  0.0556  0.0296  36  SER   C CB  
1354 C  CB  B SER   B 30  ? 0.2397 0.2167 0.4540 0.0011  0.0554  0.0303  36  SER   C CB  
1355 O  OG  A SER   B 30  ? 0.1702 0.1491 0.3872 -0.0004 0.0542  0.0340  36  SER   C OG  
1356 O  OG  B SER   B 30  ? 0.2913 0.2637 0.5103 0.0002  0.0584  0.0232  36  SER   C OG  
1357 N  N   . SER   B 31  ? 0.1993 0.1787 0.3910 -0.0012 0.0505  0.0149  37  SER   C N   
1358 C  CA  . SER   B 31  ? 0.2112 0.1935 0.3975 -0.0026 0.0477  0.0113  37  SER   C CA  
1359 C  C   . SER   B 31  ? 0.2016 0.1875 0.3753 -0.0015 0.0440  0.0118  37  SER   C C   
1360 O  O   . SER   B 31  ? 0.2117 0.2010 0.3818 -0.0019 0.0416  0.0112  37  SER   C O   
1361 C  CB  . SER   B 31  ? 0.2650 0.2448 0.4516 -0.0041 0.0485  0.0027  37  SER   C CB  
1362 O  OG  . SER   B 31  ? 0.3300 0.3087 0.5073 -0.0030 0.0481  -0.0020 37  SER   C OG  
1363 N  N   . ARG   B 32  ? 0.1830 0.1679 0.3506 0.0000  0.0437  0.0129  38  ARG   C N   
1364 C  CA  . ARG   B 32  ? 0.1874 0.1745 0.3434 0.0010  0.0403  0.0136  38  ARG   C CA  
1365 C  C   . ARG   B 32  ? 0.1912 0.1799 0.3461 0.0016  0.0388  0.0207  38  ARG   C C   
1366 O  O   . ARG   B 32  ? 0.1850 0.1746 0.3306 0.0023  0.0360  0.0216  38  ARG   C O   
1367 C  CB  . ARG   B 32  ? 0.2271 0.2120 0.3764 0.0019  0.0408  0.0103  38  ARG   C CB  
1368 C  CG  . ARG   B 32  ? 0.2339 0.2177 0.3805 0.0014  0.0413  0.0028  38  ARG   C CG  
1369 C  CD  . ARG   B 32  ? 0.2126 0.1943 0.3514 0.0023  0.0423  0.0002  38  ARG   C CD  
1370 N  NE  . ARG   B 32  ? 0.2118 0.1950 0.3399 0.0033  0.0389  0.0019  38  ARG   C NE  
1371 C  CZ  . ARG   B 32  ? 0.2377 0.2201 0.3563 0.0039  0.0383  -0.0011 38  ARG   C CZ  
1372 N  NH1 . ARG   B 32  ? 0.2254 0.2061 0.3428 0.0035  0.0407  -0.0064 38  ARG   C NH1 
1373 N  NH2 . ARG   B 32  ? 0.2132 0.1963 0.3231 0.0048  0.0352  0.0010  38  ARG   C NH2 
1374 N  N   . ASP   B 33  ? 0.1850 0.1735 0.3489 0.0013  0.0405  0.0258  39  ASP   C N   
1375 C  CA  . ASP   B 33  ? 0.1717 0.1618 0.3349 0.0016  0.0389  0.0328  39  ASP   C CA  
1376 C  C   . ASP   B 33  ? 0.1758 0.1653 0.3338 0.0022  0.0377  0.0333  39  ASP   C C   
1377 O  O   . ASP   B 33  ? 0.1694 0.1602 0.3213 0.0021  0.0347  0.0368  39  ASP   C O   
1378 C  CB  . ASP   B 33  ? 0.1666 0.1596 0.3238 0.0014  0.0362  0.0353  39  ASP   C CB  
1379 C  CG  . ASP   B 33  ? 0.2043 0.1989 0.3604 0.0012  0.0342  0.0422  39  ASP   C CG  
1380 O  OD1 . ASP   B 33  ? 0.2183 0.2130 0.3829 0.0011  0.0354  0.0468  39  ASP   C OD1 
1381 O  OD2 . ASP   B 33  ? 0.1880 0.1837 0.3346 0.0013  0.0314  0.0430  39  ASP   C OD2 
1382 N  N   . LEU   B 34  ? 0.1721 0.1594 0.3322 0.0027  0.0403  0.0299  40  LEU   C N   
1383 C  CA  . LEU   B 34  ? 0.1739 0.1610 0.3301 0.0031  0.0399  0.0309  40  LEU   C CA  
1384 C  C   . LEU   B 34  ? 0.1736 0.1605 0.3399 0.0037  0.0433  0.0335  40  LEU   C C   
1385 O  O   . LEU   B 34  ? 0.1801 0.1653 0.3547 0.0043  0.0470  0.0316  40  LEU   C O   
1386 C  CB  . LEU   B 34  ? 0.1890 0.1743 0.3358 0.0035  0.0400  0.0250  40  LEU   C CB  
1387 C  CG  . LEU   B 34  ? 0.2077 0.1933 0.3435 0.0034  0.0363  0.0230  40  LEU   C CG  
1388 C  CD1 . LEU   B 34  ? 0.2112 0.1952 0.3387 0.0040  0.0365  0.0179  40  LEU   C CD1 
1389 C  CD2 . LEU   B 34  ? 0.2199 0.2063 0.3505 0.0031  0.0328  0.0277  40  LEU   C CD2 
1390 N  N   . LEU   B 35  ? 0.1624 0.1511 0.3286 0.0036  0.0420  0.0378  41  LEU   C N   
1391 C  CA  . LEU   B 35  ? 0.1772 0.1667 0.3535 0.0044  0.0453  0.0405  41  LEU   C CA  
1392 C  C   . LEU   B 35  ? 0.1824 0.1730 0.3531 0.0039  0.0442  0.0414  41  LEU   C C   
1393 O  O   . LEU   B 35  ? 0.1990 0.1905 0.3622 0.0026  0.0397  0.0434  41  LEU   C O   
1394 C  CB  . LEU   B 35  ? 0.1765 0.1689 0.3639 0.0045  0.0444  0.0479  41  LEU   C CB  
1395 C  CG  . LEU   B 35  ? 0.1926 0.1869 0.3928 0.0059  0.0478  0.0516  41  LEU   C CG  
1396 C  CD1 . LEU   B 35  ? 0.2103 0.2051 0.4237 0.0070  0.0492  0.0562  41  LEU   C CD1 
1397 C  CD2 . LEU   B 35  ? 0.1875 0.1859 0.3873 0.0049  0.0448  0.0565  41  LEU   C CD2 
1398 N  N   . VAL   B 36  ? 0.1803 0.1705 0.3544 0.0048  0.0486  0.0397  42  VAL   C N   
1399 C  CA  . VAL   B 36  ? 0.1769 0.1684 0.3476 0.0042  0.0485  0.0411  42  VAL   C CA  
1400 C  C   . VAL   B 36  ? 0.1924 0.1873 0.3766 0.0050  0.0518  0.0457  42  VAL   C C   
1401 O  O   . VAL   B 36  ? 0.1923 0.1863 0.3850 0.0069  0.0570  0.0439  42  VAL   C O   
1402 C  CB  . VAL   B 36  ? 0.1936 0.1820 0.3545 0.0046  0.0513  0.0348  42  VAL   C CB  
1403 C  CG1 . VAL   B 36  ? 0.1958 0.1854 0.3537 0.0039  0.0519  0.0370  42  VAL   C CG1 
1404 C  CG2 . VAL   B 36  ? 0.2051 0.1909 0.3538 0.0041  0.0476  0.0307  42  VAL   C CG2 
1405 N  N   . SER   B 37  ? 0.1932 0.1919 0.3802 0.0035  0.0488  0.0514  43  SER   C N   
1406 C  CA  . SER   B 37  ? 0.1908 0.1942 0.3917 0.0042  0.0514  0.0565  43  SER   C CA  
1407 C  C   . SER   B 37  ? 0.2125 0.2176 0.4104 0.0028  0.0522  0.0574  43  SER   C C   
1408 O  O   . SER   B 37  ? 0.2105 0.2131 0.3959 0.0010  0.0493  0.0554  43  SER   C O   
1409 C  CB  . SER   B 37  ? 0.2167 0.2247 0.4260 0.0033  0.0466  0.0638  43  SER   C CB  
1410 O  OG  . SER   B 37  ? 0.2310 0.2394 0.4309 0.0004  0.0400  0.0657  43  SER   C OG  
1411 N  N   . SER   B 38  ? 0.2117 0.2210 0.4220 0.0038  0.0565  0.0607  44  SER   C N   
1412 C  CA  . SER   B 38  ? 0.2257 0.2374 0.4351 0.0023  0.0579  0.0622  44  SER   C CA  
1413 C  C   . SER   B 38  ? 0.2453 0.2622 0.4597 -0.0008 0.0518  0.0692  44  SER   C C   
1414 O  O   . SER   B 38  ? 0.2457 0.2664 0.4693 -0.0009 0.0484  0.0739  44  SER   C O   
1415 C  CB  . SER   B 38  ? 0.2572 0.2714 0.4773 0.0049  0.0663  0.0620  44  SER   C CB  
1416 O  OG  . SER   B 38  ? 0.3012 0.3205 0.5385 0.0064  0.0668  0.0672  44  SER   C OG  
1417 N  N   . THR   B 39  ? 0.2407 0.2577 0.4493 -0.0036 0.0502  0.0700  45  THR   C N   
1418 C  CA  . THR   B 39  ? 0.2458 0.2671 0.4585 -0.0073 0.0441  0.0759  45  THR   C CA  
1419 C  C   . THR   B 39  ? 0.2834 0.3096 0.5049 -0.0086 0.0478  0.0795  45  THR   C C   
1420 O  O   . THR   B 39  ? 0.2791 0.3036 0.4978 -0.0072 0.0544  0.0766  45  THR   C O   
1421 C  CB  . THR   B 39  ? 0.2566 0.2723 0.4533 -0.0103 0.0379  0.0737  45  THR   C CB  
1422 O  OG1 . THR   B 39  ? 0.2711 0.2823 0.4580 -0.0103 0.0413  0.0701  45  THR   C OG1 
1423 C  CG2 . THR   B 39  ? 0.2609 0.2720 0.4482 -0.0090 0.0347  0.0701  45  THR   C CG2 
1424 N  N   . THR   B 40  ? 0.3045 0.3372 0.5362 -0.0116 0.0433  0.0858  46  THR   C N   
1425 C  CA  . THR   B 40  ? 0.3347 0.3729 0.5759 -0.0135 0.0462  0.0898  46  THR   C CA  
1426 C  C   . THR   B 40  ? 0.3382 0.3716 0.5669 -0.0175 0.0433  0.0885  46  THR   C C   
1427 O  O   . THR   B 40  ? 0.3569 0.3898 0.5845 -0.0179 0.0487  0.0883  46  THR   C O   
1428 C  CB  . THR   B 40  ? 0.3879 0.4361 0.6475 -0.0149 0.0427  0.0973  46  THR   C CB  
1429 O  OG1 . THR   B 40  ? 0.4357 0.4834 0.6901 -0.0188 0.0329  0.0992  46  THR   C OG1 
1430 C  CG2 . THR   B 40  ? 0.3877 0.4396 0.6595 -0.0103 0.0459  0.0987  46  THR   C CG2 
1431 N  N   . ALA   B 41  ? 0.3209 0.3499 0.5392 -0.0203 0.0353  0.0876  47  ALA   C N   
1432 C  CA  . ALA   B 41  ? 0.3216 0.3446 0.5280 -0.0240 0.0323  0.0863  47  ALA   C CA  
1433 C  C   . ALA   B 41  ? 0.3140 0.3279 0.5033 -0.0215 0.0347  0.0799  47  ALA   C C   
1434 O  O   . ALA   B 41  ? 0.3118 0.3231 0.4960 -0.0182 0.0353  0.0760  47  ALA   C O   
1435 C  CB  . ALA   B 41  ? 0.3310 0.3532 0.5343 -0.0281 0.0228  0.0879  47  ALA   C CB  
1436 N  N   . GLN   B 42  ? 0.3120 0.3211 0.4929 -0.0233 0.0357  0.0791  48  GLN   C N   
1437 C  CA  . GLN   B 42  ? 0.3328 0.3337 0.4976 -0.0212 0.0372  0.0738  48  GLN   C CA  
1438 C  C   . GLN   B 42  ? 0.3324 0.3269 0.4857 -0.0221 0.0300  0.0711  48  GLN   C C   
1439 O  O   . GLN   B 42  ? 0.3393 0.3335 0.4938 -0.0259 0.0240  0.0734  48  GLN   C O   
1440 C  CB  . GLN   B 42  ? 0.3889 0.3870 0.5489 -0.0225 0.0411  0.0748  48  GLN   C CB  
1441 C  CG  . GLN   B 42  ? 0.4904 0.4927 0.6555 -0.0197 0.0501  0.0748  48  GLN   C CG  
1442 C  CD  . GLN   B 42  ? 0.6179 0.6173 0.7765 -0.0209 0.0542  0.0761  48  GLN   C CD  
1443 O  OE1 . GLN   B 42  ? 0.6530 0.6516 0.8133 -0.0250 0.0518  0.0802  48  GLN   C OE1 
1444 N  NE2 . GLN   B 42  ? 0.6588 0.6564 0.8095 -0.0176 0.0603  0.0728  48  GLN   C NE2 
1445 N  N   . GLY   B 43  ? 0.3112 0.3013 0.4545 -0.0187 0.0307  0.0660  49  GLY   C N   
1446 C  CA  . GLY   B 43  ? 0.3033 0.2875 0.4353 -0.0185 0.0253  0.0627  49  GLY   C CA  
1447 C  C   . GLY   B 43  ? 0.3048 0.2816 0.4244 -0.0187 0.0248  0.0608  49  GLY   C C   
1448 O  O   . GLY   B 43  ? 0.3258 0.3018 0.4438 -0.0182 0.0294  0.0613  49  GLY   C O   
1449 N  N   . CYS   B 44  ? 0.2895 0.2605 0.4003 -0.0193 0.0196  0.0589  50  CYS   C N   
1450 C  CA  . CYS   B 44  ? 0.3020 0.2651 0.4018 -0.0195 0.0186  0.0576  50  CYS   C CA  
1451 C  C   . CYS   B 44  ? 0.3008 0.2594 0.3897 -0.0157 0.0180  0.0529  50  CYS   C C   
1452 O  O   . CYS   B 44  ? 0.3267 0.2786 0.4068 -0.0153 0.0169  0.0521  50  CYS   C O   
1453 C  CB  . CYS   B 44  ? 0.3237 0.2826 0.4227 -0.0237 0.0132  0.0594  50  CYS   C CB  
1454 S  SG  . CYS   B 44  ? 0.4278 0.3933 0.5413 -0.0288 0.0131  0.0654  50  CYS   C SG  
1455 N  N   . ASP   B 45  ? 0.2720 0.2339 0.3618 -0.0131 0.0183  0.0501  51  ASP   C N   
1456 C  CA  . ASP   B 45  ? 0.2628 0.2213 0.3434 -0.0097 0.0176  0.0458  51  ASP   C CA  
1457 C  C   . ASP   B 45  ? 0.2770 0.2354 0.3539 -0.0072 0.0219  0.0443  51  ASP   C C   
1458 O  O   . ASP   B 45  ? 0.2865 0.2489 0.3689 -0.0074 0.0262  0.0456  51  ASP   C O   
1459 C  CB  . ASP   B 45  ? 0.2528 0.2153 0.3368 -0.0081 0.0170  0.0437  51  ASP   C CB  
1460 C  CG  . ASP   B 45  ? 0.3036 0.2661 0.3886 -0.0101 0.0125  0.0448  51  ASP   C CG  
1461 O  OD1 . ASP   B 45  ? 0.3045 0.2617 0.3835 -0.0116 0.0090  0.0448  51  ASP   C OD1 
1462 O  OD2 . ASP   B 45  ? 0.2722 0.2398 0.3639 -0.0102 0.0125  0.0458  51  ASP   C OD2 
1463 N  N   . THR   B 46  ? 0.2586 0.2127 0.3259 -0.0048 0.0206  0.0417  52  THR   C N   
1464 C  CA  . THR   B 46  ? 0.2633 0.2175 0.3253 -0.0023 0.0236  0.0400  52  THR   C CA  
1465 C  C   . THR   B 46  ? 0.2668 0.2232 0.3270 0.0006  0.0228  0.0355  52  THR   C C   
1466 O  O   . THR   B 46  ? 0.2654 0.2197 0.3230 0.0015  0.0194  0.0341  52  THR   C O   
1467 C  CB  . THR   B 46  ? 0.3054 0.2532 0.3583 -0.0018 0.0221  0.0413  52  THR   C CB  
1468 O  OG1 . THR   B 46  ? 0.3324 0.2780 0.3876 -0.0050 0.0228  0.0457  52  THR   C OG1 
1469 C  CG2 . THR   B 46  ? 0.3183 0.2667 0.3642 0.0010  0.0243  0.0396  52  THR   C CG2 
1470 N  N   . ILE   B 47  ? 0.2518 0.2118 0.3130 0.0020  0.0261  0.0331  53  ILE   C N   
1471 C  CA  . ILE   B 47  ? 0.2398 0.2021 0.3000 0.0043  0.0253  0.0287  53  ILE   C CA  
1472 C  C   . ILE   B 47  ? 0.2207 0.1806 0.2711 0.0066  0.0236  0.0270  53  ILE   C C   
1473 O  O   . ILE   B 47  ? 0.2381 0.1968 0.2830 0.0069  0.0251  0.0279  53  ILE   C O   
1474 C  CB  . ILE   B 47  ? 0.2513 0.2180 0.3172 0.0045  0.0293  0.0262  53  ILE   C CB  
1475 C  CG1 . ILE   B 47  ? 0.2507 0.2200 0.3273 0.0026  0.0316  0.0288  53  ILE   C CG1 
1476 C  CG2 . ILE   B 47  ? 0.2625 0.2315 0.3286 0.0061  0.0282  0.0218  53  ILE   C CG2 
1477 C  CD1 . ILE   B 47  ? 0.2789 0.2489 0.3604 0.0018  0.0282  0.0301  53  ILE   C CD1 
1478 N  N   . ALA   B 48  ? 0.2052 0.1653 0.2539 0.0085  0.0205  0.0247  54  ALA   C N   
1479 C  CA  . ALA   B 48  ? 0.1983 0.1573 0.2393 0.0111  0.0184  0.0233  54  ALA   C CA  
1480 C  C   . ALA   B 48  ? 0.2163 0.1792 0.2558 0.0118  0.0202  0.0201  54  ALA   C C   
1481 O  O   . ALA   B 48  ? 0.2239 0.1906 0.2696 0.0110  0.0221  0.0174  54  ALA   C O   
1482 C  CB  . ALA   B 48  ? 0.2025 0.1619 0.2440 0.0131  0.0153  0.0215  54  ALA   C CB  
1483 N  N   . ARG   B 49  ? 0.2175 0.1795 0.2487 0.0132  0.0195  0.0203  55  ARG   C N   
1484 C  CA  . ARG   B 49  ? 0.2224 0.1880 0.2503 0.0137  0.0204  0.0167  55  ARG   C CA  
1485 C  C   . ARG   B 49  ? 0.2226 0.1887 0.2443 0.0165  0.0160  0.0162  55  ARG   C C   
1486 O  O   . ARG   B 49  ? 0.2419 0.2051 0.2557 0.0177  0.0147  0.0192  55  ARG   C O   
1487 C  CB  . ARG   B 49  ? 0.2226 0.1872 0.2453 0.0127  0.0242  0.0180  55  ARG   C CB  
1488 C  CG  . ARG   B 49  ? 0.2261 0.1907 0.2565 0.0103  0.0287  0.0194  55  ARG   C CG  
1489 C  CD  . ARG   B 49  ? 0.2469 0.2152 0.2858 0.0096  0.0308  0.0152  55  ARG   C CD  
1490 N  NE  . ARG   B 49  ? 0.2509 0.2193 0.2977 0.0078  0.0350  0.0174  55  ARG   C NE  
1491 C  CZ  . ARG   B 49  ? 0.2795 0.2501 0.3363 0.0071  0.0368  0.0160  55  ARG   C CZ  
1492 N  NH1 . ARG   B 49  ? 0.2439 0.2164 0.3039 0.0077  0.0351  0.0121  55  ARG   C NH1 
1493 N  NH2 . ARG   B 49  ? 0.2820 0.2532 0.3465 0.0058  0.0403  0.0187  55  ARG   C NH2 
1494 N  N   . CYS   B 50  ? 0.2206 0.1904 0.2469 0.0175  0.0136  0.0130  56  CYS   C N   
1495 C  CA  . CYS   B 50  ? 0.2200 0.1911 0.2432 0.0205  0.0092  0.0129  56  CYS   C CA  
1496 C  C   . CYS   B 50  ? 0.2177 0.1947 0.2479 0.0207  0.0078  0.0088  56  CYS   C C   
1497 O  O   . CYS   B 50  ? 0.2166 0.1957 0.2536 0.0186  0.0102  0.0064  56  CYS   C O   
1498 C  CB  . CYS   B 50  ? 0.2420 0.2080 0.2651 0.0219  0.0079  0.0166  56  CYS   C CB  
1499 S  SG  . CYS   B 50  ? 0.2313 0.1974 0.2638 0.0206  0.0091  0.0158  56  CYS   C SG  
1500 N  N   . ASP   B 51  ? 0.2286 0.2083 0.2582 0.0235  0.0039  0.0085  57  ASP   C N   
1501 C  CA  . ASP   B 51  ? 0.2322 0.2179 0.2697 0.0238  0.0026  0.0053  57  ASP   C CA  
1502 C  C   . ASP   B 51  ? 0.2407 0.2256 0.2811 0.0266  0.0012  0.0074  57  ASP   C C   
1503 O  O   . ASP   B 51  ? 0.2519 0.2422 0.2966 0.0284  -0.0010 0.0059  57  ASP   C O   
1504 C  CB  . ASP   B 51  ? 0.2648 0.2567 0.3008 0.0242  -0.0006 0.0022  57  ASP   C CB  
1505 C  CG  . ASP   B 51  ? 0.3228 0.3150 0.3518 0.0276  -0.0047 0.0047  57  ASP   C CG  
1506 O  OD1 . ASP   B 51  ? 0.3072 0.2939 0.3325 0.0297  -0.0047 0.0089  57  ASP   C OD1 
1507 O  OD2 . ASP   B 51  ? 0.4135 0.4115 0.4411 0.0280  -0.0081 0.0026  57  ASP   C OD2 
1508 N  N   . CYS   B 52  ? 0.2278 0.2061 0.2661 0.0268  0.0026  0.0105  58  CYS   C N   
1509 C  CA  . CYS   B 52  ? 0.2022 0.1783 0.2422 0.0294  0.0019  0.0118  58  CYS   C CA  
1510 C  C   . CYS   B 52  ? 0.2062 0.1879 0.2547 0.0290  0.0029  0.0094  58  CYS   C C   
1511 O  O   . CYS   B 52  ? 0.2136 0.1976 0.2667 0.0259  0.0051  0.0079  58  CYS   C O   
1512 C  CB  . CYS   B 52  ? 0.2055 0.1736 0.2423 0.0283  0.0035  0.0145  58  CYS   C CB  
1513 S  SG  . CYS   B 52  ? 0.2438 0.2040 0.2715 0.0297  0.0021  0.0184  58  CYS   C SG  
1514 N  N   . GLN   B 53  ? 0.1990 0.1823 0.2495 0.0322  0.0019  0.0094  59  GLN   C N   
1515 C  CA  . GLN   B 53  ? 0.2063 0.1943 0.2643 0.0322  0.0035  0.0080  59  GLN   C CA  
1516 C  C   . GLN   B 53  ? 0.2058 0.1889 0.2618 0.0345  0.0045  0.0092  59  GLN   C C   
1517 O  O   . GLN   B 53  ? 0.2040 0.1909 0.2648 0.0358  0.0059  0.0083  59  GLN   C O   
1518 C  CB  . GLN   B 53  ? 0.1928 0.1896 0.2570 0.0340  0.0017  0.0061  59  GLN   C CB  
1519 C  CG  . GLN   B 53  ? 0.2193 0.2215 0.2872 0.0307  0.0012  0.0036  59  GLN   C CG  
1520 C  CD  . GLN   B 53  ? 0.2729 0.2844 0.3484 0.0317  -0.0008 0.0016  59  GLN   C CD  
1521 O  OE1 . GLN   B 53  ? 0.2987 0.3138 0.3726 0.0326  -0.0045 0.0007  59  GLN   C OE1 
1522 N  NE2 . GLN   B 53  ? 0.2284 0.2445 0.3123 0.0314  0.0012  0.0010  59  GLN   C NE2 
1523 N  N   . THR   B 54  ? 0.2051 0.1796 0.2539 0.0349  0.0041  0.0111  60  THR   C N   
1524 C  CA  . THR   B 54  ? 0.2340 0.2023 0.2797 0.0363  0.0051  0.0116  60  THR   C CA  
1525 C  C   . THR   B 54  ? 0.2400 0.2012 0.2811 0.0328  0.0056  0.0132  60  THR   C C   
1526 O  O   . THR   B 54  ? 0.2489 0.2076 0.2873 0.0311  0.0049  0.0147  60  THR   C O   
1527 C  CB  . THR   B 54  ? 0.2817 0.2465 0.3245 0.0413  0.0037  0.0121  60  THR   C CB  
1528 O  OG1 . THR   B 54  ? 0.3107 0.2701 0.3481 0.0415  0.0017  0.0142  60  THR   C OG1 
1529 C  CG2 . THR   B 54  ? 0.2771 0.2505 0.3260 0.0449  0.0028  0.0110  60  THR   C CG2 
1530 N  N   . GLY   B 55  ? 0.2195 0.1779 0.2598 0.0316  0.0069  0.0129  61  GLY   C N   
1531 C  CA  . GLY   B 55  ? 0.2168 0.1694 0.2539 0.0278  0.0069  0.0144  61  GLY   C CA  
1532 C  C   . GLY   B 55  ? 0.2250 0.1745 0.2598 0.0272  0.0076  0.0137  61  GLY   C C   
1533 O  O   . GLY   B 55  ? 0.2300 0.1798 0.2639 0.0303  0.0084  0.0120  61  GLY   C O   
1534 N  N   . VAL   B 56  ? 0.2288 0.1756 0.2626 0.0232  0.0073  0.0152  62  VAL   C N   
1535 C  CA  . VAL   B 56  ? 0.2256 0.1696 0.2561 0.0218  0.0073  0.0146  62  VAL   C CA  
1536 C  C   . VAL   B 56  ? 0.2174 0.1662 0.2524 0.0177  0.0077  0.0166  62  VAL   C C   
1537 O  O   . VAL   B 56  ? 0.2170 0.1665 0.2552 0.0152  0.0073  0.0186  62  VAL   C O   
1538 C  CB  . VAL   B 56  ? 0.2382 0.1720 0.2618 0.0207  0.0053  0.0147  62  VAL   C CB  
1539 C  CG1 . VAL   B 56  ? 0.2546 0.1855 0.2740 0.0182  0.0045  0.0139  62  VAL   C CG1 
1540 C  CG2 . VAL   B 56  ? 0.2478 0.1759 0.2674 0.0253  0.0051  0.0130  62  VAL   C CG2 
1541 N  N   . TYR   B 57  ? 0.2071 0.1594 0.2426 0.0173  0.0087  0.0164  63  TYR   C N   
1542 C  CA  . TYR   B 57  ? 0.1923 0.1490 0.2326 0.0137  0.0089  0.0190  63  TYR   C CA  
1543 C  C   . TYR   B 57  ? 0.2122 0.1662 0.2469 0.0115  0.0074  0.0196  63  TYR   C C   
1544 O  O   . TYR   B 57  ? 0.2166 0.1674 0.2446 0.0134  0.0076  0.0172  63  TYR   C O   
1545 C  CB  . TYR   B 57  ? 0.1920 0.1571 0.2400 0.0143  0.0115  0.0195  63  TYR   C CB  
1546 C  CG  . TYR   B 57  ? 0.2022 0.1704 0.2488 0.0157  0.0131  0.0189  63  TYR   C CG  
1547 C  CD1 . TYR   B 57  ? 0.2136 0.1821 0.2579 0.0194  0.0145  0.0163  63  TYR   C CD1 
1548 C  CD2 . TYR   B 57  ? 0.2051 0.1767 0.2536 0.0133  0.0137  0.0216  63  TYR   C CD2 
1549 C  CE1 . TYR   B 57  ? 0.2286 0.2005 0.2720 0.0208  0.0168  0.0159  63  TYR   C CE1 
1550 C  CE2 . TYR   B 57  ? 0.2154 0.1903 0.2622 0.0145  0.0158  0.0216  63  TYR   C CE2 
1551 C  CZ  . TYR   B 57  ? 0.2321 0.2072 0.2763 0.0182  0.0176  0.0186  63  TYR   C CZ  
1552 O  OH  . TYR   B 57  ? 0.2562 0.2351 0.2992 0.0195  0.0204  0.0188  63  TYR   C OH  
1553 N  N   . TYR   B 58  ? 0.2183 0.1741 0.2562 0.0078  0.0061  0.0227  64  TYR   C N   
1554 C  CA  . TYR   B 58  ? 0.2349 0.1892 0.2677 0.0053  0.0040  0.0238  64  TYR   C CA  
1555 C  C   . TYR   B 58  ? 0.2198 0.1809 0.2552 0.0053  0.0057  0.0257  64  TYR   C C   
1556 O  O   . TYR   B 58  ? 0.2099 0.1769 0.2544 0.0046  0.0071  0.0285  64  TYR   C O   
1557 C  CB  . TYR   B 58  ? 0.2435 0.1967 0.2787 0.0010  0.0009  0.0267  64  TYR   C CB  
1558 C  CG  . TYR   B 58  ? 0.2569 0.2089 0.2859 -0.0018 -0.0022 0.0275  64  TYR   C CG  
1559 C  CD1 . TYR   B 58  ? 0.2676 0.2126 0.2857 -0.0015 -0.0037 0.0238  64  TYR   C CD1 
1560 C  CD2 . TYR   B 58  ? 0.2509 0.2086 0.2847 -0.0047 -0.0036 0.0318  64  TYR   C CD2 
1561 C  CE1 . TYR   B 58  ? 0.2813 0.2250 0.2922 -0.0043 -0.0068 0.0239  64  TYR   C CE1 
1562 C  CE2 . TYR   B 58  ? 0.2712 0.2284 0.2985 -0.0073 -0.0071 0.0326  64  TYR   C CE2 
1563 C  CZ  . TYR   B 58  ? 0.2928 0.2429 0.3081 -0.0074 -0.0088 0.0284  64  TYR   C CZ  
1564 O  OH  . TYR   B 58  ? 0.3367 0.2861 0.3442 -0.0102 -0.0123 0.0286  64  TYR   C OH  
1565 N  N   . CYS   B 59  ? 0.2193 0.1791 0.2464 0.0061  0.0058  0.0241  65  CYS   C N   
1566 C  CA  . CYS   B 59  ? 0.2260 0.1918 0.2537 0.0062  0.0077  0.0262  65  CYS   C CA  
1567 C  C   . CYS   B 59  ? 0.2468 0.2115 0.2678 0.0028  0.0043  0.0282  65  CYS   C C   
1568 O  O   . CYS   B 59  ? 0.2673 0.2268 0.2773 0.0030  0.0031  0.0251  65  CYS   C O   
1569 C  CB  . CYS   B 59  ? 0.2352 0.2012 0.2584 0.0100  0.0110  0.0229  65  CYS   C CB  
1570 S  SG  . CYS   B 59  ? 0.2542 0.2271 0.2764 0.0102  0.0140  0.0257  65  CYS   C SG  
1571 N  N   . SER   B 60  ? 0.2455 0.2149 0.2730 -0.0001 0.0026  0.0333  66  SER   C N   
1572 C  CA  A SER   B 60  ? 0.2623 0.2316 0.2842 -0.0036 -0.0015 0.0357  66  SER   C CA  
1573 C  CA  B SER   B 60  ? 0.2550 0.2243 0.2770 -0.0035 -0.0015 0.0357  66  SER   C CA  
1574 C  C   . SER   B 60  ? 0.2717 0.2423 0.2837 -0.0030 -0.0007 0.0356  66  SER   C C   
1575 O  O   . SER   B 60  ? 0.2968 0.2641 0.2984 -0.0051 -0.0042 0.0344  66  SER   C O   
1576 C  CB  A SER   B 60  ? 0.2915 0.2663 0.3239 -0.0062 -0.0033 0.0417  66  SER   C CB  
1577 C  CB  B SER   B 60  ? 0.2635 0.2386 0.2960 -0.0061 -0.0031 0.0418  66  SER   C CB  
1578 O  OG  A SER   B 60  ? 0.3247 0.3056 0.3660 -0.0047 0.0004  0.0449  66  SER   C OG  
1579 O  OG  B SER   B 60  ? 0.2683 0.2434 0.2952 -0.0096 -0.0081 0.0440  66  SER   C OG  
1580 N  N   . SER   B 61  ? 0.2581 0.2334 0.2730 -0.0004 0.0039  0.0366  67  SER   C N   
1581 C  CA  . SER   B 61  ? 0.2649 0.2421 0.2705 0.0004  0.0056  0.0370  67  SER   C CA  
1582 C  C   . SER   B 61  ? 0.2871 0.2581 0.2797 0.0026  0.0068  0.0305  67  SER   C C   
1583 O  O   . SER   B 61  ? 0.3036 0.2753 0.2862 0.0032  0.0083  0.0300  67  SER   C O   
1584 C  CB  . SER   B 61  ? 0.2743 0.2585 0.2880 0.0023  0.0106  0.0403  67  SER   C CB  
1585 O  OG  . SER   B 61  ? 0.2948 0.2789 0.3141 0.0055  0.0145  0.0367  67  SER   C OG  
1586 N  N   . ARG   B 62  ? 0.2810 0.2457 0.2734 0.0041  0.0064  0.0257  68  ARG   C N   
1587 C  CA  . ARG   B 62  ? 0.2870 0.2443 0.2677 0.0063  0.0073  0.0194  68  ARG   C CA  
1588 C  C   . ARG   B 62  ? 0.3104 0.2587 0.2858 0.0039  0.0024  0.0163  68  ARG   C C   
1589 O  O   . ARG   B 62  ? 0.3261 0.2666 0.2924 0.0057  0.0029  0.0108  68  ARG   C O   
1590 C  CB  . ARG   B 62  ? 0.3098 0.2670 0.2952 0.0112  0.0119  0.0163  68  ARG   C CB  
1591 C  CG  . ARG   B 62  ? 0.3592 0.3249 0.3501 0.0137  0.0172  0.0186  68  ARG   C CG  
1592 C  CD  . ARG   B 62  ? 0.3729 0.3386 0.3525 0.0154  0.0203  0.0167  68  ARG   C CD  
1593 N  NE  . ARG   B 62  ? 0.4044 0.3789 0.3904 0.0174  0.0256  0.0195  68  ARG   C NE  
1594 C  CZ  . ARG   B 62  ? 0.4623 0.4433 0.4503 0.0151  0.0264  0.0251  68  ARG   C CZ  
1595 N  NH1 . ARG   B 62  ? 0.4937 0.4742 0.4779 0.0111  0.0219  0.0285  68  ARG   C NH1 
1596 N  NH2 . ARG   B 62  ? 0.4580 0.4464 0.4522 0.0169  0.0317  0.0275  68  ARG   C NH2 
1597 N  N   . ARG   B 63  ? 0.3160 0.2652 0.2984 0.0001  -0.0017 0.0198  69  ARG   C N   
1598 C  CA  . ARG   B 63  ? 0.3416 0.2834 0.3220 -0.0028 -0.0063 0.0179  69  ARG   C CA  
1599 C  C   . ARG   B 63  ? 0.3525 0.2868 0.3319 0.0006  -0.0043 0.0131  69  ARG   C C   
1600 O  O   . ARG   B 63  ? 0.3752 0.3003 0.3461 0.0001  -0.0061 0.0088  69  ARG   C O   
1601 C  CB  . ARG   B 63  ? 0.3753 0.3125 0.3430 -0.0063 -0.0106 0.0158  69  ARG   C CB  
1602 C  CG  . ARG   B 63  ? 0.4280 0.3721 0.3958 -0.0101 -0.0140 0.0209  69  ARG   C CG  
1603 C  CD  . ARG   B 63  ? 0.4939 0.4409 0.4724 -0.0141 -0.0183 0.0255  69  ARG   C CD  
1604 N  NE  . ARG   B 63  ? 0.5182 0.4696 0.4940 -0.0185 -0.0234 0.0294  69  ARG   C NE  
1605 C  CZ  . ARG   B 63  ? 0.5239 0.4844 0.5051 -0.0187 -0.0232 0.0356  69  ARG   C CZ  
1606 N  NH1 . ARG   B 63  ? 0.4884 0.4540 0.4781 -0.0151 -0.0178 0.0382  69  ARG   C NH1 
1607 N  NH2 . ARG   B 63  ? 0.4881 0.4526 0.4666 -0.0227 -0.0286 0.0394  69  ARG   C NH2 
1608 N  N   . LYS   B 64  ? 0.3253 0.2634 0.3131 0.0042  -0.0004 0.0138  70  LYS   C N   
1609 C  CA  . LYS   B 64  ? 0.3217 0.2540 0.3089 0.0082  0.0017  0.0100  70  LYS   C CA  
1610 C  C   . LYS   B 64  ? 0.2971 0.2329 0.2954 0.0094  0.0028  0.0122  70  LYS   C C   
1611 O  O   . LYS   B 64  ? 0.2817 0.2257 0.2882 0.0091  0.0042  0.0156  70  LYS   C O   
1612 C  CB  . LYS   B 64  ? 0.3684 0.3019 0.3512 0.0130  0.0062  0.0069  70  LYS   C CB  
1613 C  CG  . LYS   B 64  ? 0.5037 0.4289 0.4731 0.0135  0.0059  0.0020  70  LYS   C CG  
1614 C  CD  . LYS   B 64  ? 0.6012 0.5247 0.5679 0.0195  0.0107  -0.0021 70  LYS   C CD  
1615 C  CE  . LYS   B 64  ? 0.6853 0.6029 0.6381 0.0200  0.0116  -0.0067 70  LYS   C CE  
1616 N  NZ  . LYS   B 64  ? 0.7458 0.6688 0.6935 0.0161  0.0103  -0.0042 70  LYS   C NZ  
1617 N  N   . HIS   B 65  ? 0.2827 0.2118 0.2806 0.0110  0.0023  0.0102  71  HIS   C N   
1618 C  CA  . HIS   B 65  ? 0.2817 0.2138 0.2882 0.0129  0.0036  0.0117  71  HIS   C CA  
1619 C  C   . HIS   B 65  ? 0.2845 0.2170 0.2904 0.0184  0.0068  0.0089  71  HIS   C C   
1620 O  O   . HIS   B 65  ? 0.3234 0.2487 0.3220 0.0209  0.0071  0.0054  71  HIS   C O   
1621 C  CB  . HIS   B 65  ? 0.2698 0.1945 0.2760 0.0112  0.0010  0.0121  71  HIS   C CB  
1622 C  CG  . HIS   B 65  ? 0.2661 0.1914 0.2749 0.0057  -0.0019 0.0152  71  HIS   C CG  
1623 N  ND1 . HIS   B 65  ? 0.2871 0.2176 0.3047 0.0041  -0.0017 0.0188  71  HIS   C ND1 
1624 C  CD2 . HIS   B 65  ? 0.2888 0.2104 0.2928 0.0017  -0.0052 0.0151  71  HIS   C CD2 
1625 C  CE1 . HIS   B 65  ? 0.2814 0.2115 0.3002 -0.0005 -0.0045 0.0212  71  HIS   C CE1 
1626 N  NE2 . HIS   B 65  ? 0.2988 0.2241 0.3099 -0.0024 -0.0071 0.0192  71  HIS   C NE2 
1627 N  N   . TYR   B 66  ? 0.2491 0.1897 0.2629 0.0205  0.0092  0.0101  72  TYR   C N   
1628 C  CA  . TYR   B 66  ? 0.2489 0.1915 0.2638 0.0256  0.0120  0.0079  72  TYR   C CA  
1629 C  C   . TYR   B 66  ? 0.2396 0.1837 0.2605 0.0277  0.0116  0.0085  72  TYR   C C   
1630 O  O   . TYR   B 66  ? 0.2375 0.1868 0.2649 0.0255  0.0112  0.0108  72  TYR   C O   
1631 C  CB  . TYR   B 66  ? 0.2560 0.2084 0.2759 0.0262  0.0150  0.0088  72  TYR   C CB  
1632 C  CG  . TYR   B 66  ? 0.2850 0.2372 0.2981 0.0253  0.0163  0.0083  72  TYR   C CG  
1633 C  CD1 . TYR   B 66  ? 0.3181 0.2668 0.3242 0.0287  0.0185  0.0049  72  TYR   C CD1 
1634 C  CD2 . TYR   B 66  ? 0.3041 0.2601 0.3180 0.0212  0.0155  0.0115  72  TYR   C CD2 
1635 C  CE1 . TYR   B 66  ? 0.3309 0.2800 0.3296 0.0280  0.0201  0.0042  72  TYR   C CE1 
1636 C  CE2 . TYR   B 66  ? 0.3244 0.2809 0.3313 0.0203  0.0164  0.0115  72  TYR   C CE2 
1637 C  CZ  . TYR   B 66  ? 0.3454 0.2984 0.3440 0.0236  0.0188  0.0077  72  TYR   C CZ  
1638 O  OH  . TYR   B 66  ? 0.3669 0.3208 0.3573 0.0226  0.0200  0.0077  72  TYR   C OH  
1639 N  N   . PRO   B 67  ? 0.2397 0.1797 0.2586 0.0320  0.0119  0.0065  73  PRO   C N   
1640 C  CA  . PRO   B 67  ? 0.2425 0.1855 0.2669 0.0344  0.0113  0.0074  73  PRO   C CA  
1641 C  C   . PRO   B 67  ? 0.2550 0.2090 0.2874 0.0362  0.0135  0.0073  73  PRO   C C   
1642 O  O   . PRO   B 67  ? 0.2645 0.2217 0.2971 0.0382  0.0162  0.0059  73  PRO   C O   
1643 C  CB  . PRO   B 67  ? 0.2694 0.2048 0.2895 0.0390  0.0110  0.0057  73  PRO   C CB  
1644 C  CG  . PRO   B 67  ? 0.2899 0.2209 0.3039 0.0402  0.0129  0.0028  73  PRO   C CG  
1645 C  CD  . PRO   B 67  ? 0.2548 0.1876 0.2665 0.0353  0.0129  0.0033  73  PRO   C CD  
1646 N  N   . VAL   B 68  ? 0.2313 0.1912 0.2701 0.0349  0.0127  0.0088  74  VAL   C N   
1647 C  CA  . VAL   B 68  ? 0.2327 0.2027 0.2798 0.0357  0.0144  0.0086  74  VAL   C CA  
1648 C  C   . VAL   B 68  ? 0.2211 0.1949 0.2727 0.0367  0.0125  0.0087  74  VAL   C C   
1649 O  O   . VAL   B 68  ? 0.2260 0.1957 0.2748 0.0355  0.0104  0.0097  74  VAL   C O   
1650 C  CB  . VAL   B 68  ? 0.2435 0.2183 0.2949 0.0312  0.0156  0.0101  74  VAL   C CB  
1651 C  CG1 . VAL   B 68  ? 0.2774 0.2521 0.3259 0.0304  0.0177  0.0103  74  VAL   C CG1 
1652 C  CG2 . VAL   B 68  ? 0.2389 0.2107 0.2897 0.0274  0.0138  0.0117  74  VAL   C CG2 
1653 N  N   . SER   B 69  ? 0.2079 0.1901 0.2667 0.0387  0.0133  0.0079  75  SER   C N   
1654 C  CA  . SER   B 69  ? 0.1985 0.1868 0.2629 0.0386  0.0114  0.0077  75  SER   C CA  
1655 C  C   . SER   B 69  ? 0.1793 0.1734 0.2503 0.0343  0.0129  0.0077  75  SER   C C   
1656 O  O   . SER   B 69  ? 0.1852 0.1822 0.2594 0.0334  0.0156  0.0080  75  SER   C O   
1657 C  CB  . SER   B 69  ? 0.2326 0.2277 0.3028 0.0429  0.0114  0.0067  75  SER   C CB  
1658 O  OG  . SER   B 69  ? 0.3041 0.2936 0.3692 0.0473  0.0102  0.0070  75  SER   C OG  
1659 N  N   . PHE   B 70  ? 0.1801 0.1754 0.2527 0.0318  0.0113  0.0074  76  PHE   C N   
1660 C  CA  . PHE   B 70  ? 0.1755 0.1750 0.2546 0.0279  0.0128  0.0071  76  PHE   C CA  
1661 C  C   . PHE   B 70  ? 0.1831 0.1881 0.2672 0.0270  0.0111  0.0051  76  PHE   C C   
1662 O  O   . PHE   B 70  ? 0.1889 0.1932 0.2691 0.0286  0.0083  0.0044  76  PHE   C O   
1663 C  CB  . PHE   B 70  ? 0.1831 0.1771 0.2591 0.0246  0.0137  0.0087  76  PHE   C CB  
1664 C  CG  . PHE   B 70  ? 0.1819 0.1700 0.2511 0.0244  0.0118  0.0091  76  PHE   C CG  
1665 C  CD1 . PHE   B 70  ? 0.1824 0.1636 0.2439 0.0260  0.0108  0.0104  76  PHE   C CD1 
1666 C  CD2 . PHE   B 70  ? 0.1804 0.1693 0.2508 0.0224  0.0114  0.0083  76  PHE   C CD2 
1667 C  CE1 . PHE   B 70  ? 0.1993 0.1753 0.2554 0.0255  0.0094  0.0114  76  PHE   C CE1 
1668 C  CE2 . PHE   B 70  ? 0.1896 0.1737 0.2537 0.0223  0.0103  0.0091  76  PHE   C CE2 
1669 C  CZ  . PHE   B 70  ? 0.1932 0.1710 0.2506 0.0237  0.0093  0.0109  76  PHE   C CZ  
1670 N  N   . SER   B 71  ? 0.1700 0.1802 0.2623 0.0242  0.0125  0.0042  77  SER   C N   
1671 C  CA  . SER   B 71  ? 0.1788 0.1944 0.2764 0.0228  0.0108  0.0014  77  SER   C CA  
1672 C  C   . SER   B 71  ? 0.2025 0.2142 0.2962 0.0204  0.0100  0.0001  77  SER   C C   
1673 O  O   . SER   B 71  ? 0.2034 0.2088 0.2916 0.0198  0.0111  0.0017  77  SER   C O   
1674 C  CB  . SER   B 71  ? 0.1864 0.2084 0.2951 0.0205  0.0128  0.0007  77  SER   C CB  
1675 O  OG  . SER   B 71  ? 0.2088 0.2277 0.3196 0.0175  0.0157  0.0021  77  SER   C OG  
1676 N  N   . LYS   B 72  ? 0.1935 0.2093 0.2900 0.0190  0.0081  -0.0031 78  LYS   C N   
1677 C  CA  . LYS   B 72  ? 0.1947 0.2070 0.2867 0.0169  0.0078  -0.0051 78  LYS   C CA  
1678 C  C   . LYS   B 72  ? 0.1935 0.2045 0.2922 0.0134  0.0113  -0.0058 78  LYS   C C   
1679 O  O   . LYS   B 72  ? 0.1968 0.2116 0.3046 0.0120  0.0127  -0.0060 78  LYS   C O   
1680 C  CB  . LYS   B 72  ? 0.2496 0.2669 0.3414 0.0166  0.0042  -0.0088 78  LYS   C CB  
1681 C  CG  . LYS   B 72  ? 0.3223 0.3413 0.4082 0.0204  0.0003  -0.0075 78  LYS   C CG  
1682 C  CD  . LYS   B 72  ? 0.4458 0.4674 0.5267 0.0200  -0.0036 -0.0103 78  LYS   C CD  
1683 C  CE  . LYS   B 72  ? 0.5559 0.5788 0.6311 0.0241  -0.0075 -0.0078 78  LYS   C CE  
1684 N  NZ  . LYS   B 72  ? 0.6224 0.6413 0.6858 0.0245  -0.0092 -0.0074 78  LYS   C NZ  
1685 N  N   . PRO   B 73  ? 0.1939 0.1997 0.2889 0.0120  0.0131  -0.0060 79  PRO   C N   
1686 C  CA  . PRO   B 73  ? 0.2000 0.2040 0.3021 0.0092  0.0167  -0.0062 79  PRO   C CA  
1687 C  C   . PRO   B 73  ? 0.2152 0.2230 0.3256 0.0067  0.0167  -0.0102 79  PRO   C C   
1688 O  O   . PRO   B 73  ? 0.2305 0.2403 0.3384 0.0061  0.0143  -0.0144 79  PRO   C O   
1689 C  CB  . PRO   B 73  ? 0.2248 0.2237 0.3213 0.0086  0.0182  -0.0066 79  PRO   C CB  
1690 C  CG  . PRO   B 73  ? 0.2334 0.2304 0.3194 0.0110  0.0159  -0.0050 79  PRO   C CG  
1691 C  CD  . PRO   B 73  ? 0.1993 0.2007 0.2841 0.0131  0.0122  -0.0054 79  PRO   C CD  
1692 N  N   . SER   B 74  ? 0.1969 0.2063 0.3172 0.0051  0.0190  -0.0089 80  SER   C N   
1693 C  CA  . SER   B 74  ? 0.2124 0.2254 0.3420 0.0023  0.0190  -0.0125 80  SER   C CA  
1694 C  C   . SER   B 74  ? 0.2086 0.2197 0.3484 0.0001  0.0230  -0.0105 80  SER   C C   
1695 O  O   . SER   B 74  ? 0.1933 0.2012 0.3325 0.0009  0.0253  -0.0060 80  SER   C O   
1696 C  CB  . SER   B 74  ? 0.2695 0.2898 0.4030 0.0032  0.0165  -0.0122 80  SER   C CB  
1697 O  OG  . SER   B 74  ? 0.3787 0.4006 0.5040 0.0066  0.0136  -0.0111 80  SER   C OG  
1698 N  N   . LEU   B 75  ? 0.2126 0.2256 0.3618 -0.0030 0.0235  -0.0137 81  LEU   C N   
1699 C  CA  . LEU   B 75  ? 0.2287 0.2400 0.3889 -0.0053 0.0272  -0.0116 81  LEU   C CA  
1700 C  C   . LEU   B 75  ? 0.2422 0.2594 0.4088 -0.0053 0.0273  -0.0079 81  LEU   C C   
1701 O  O   . LEU   B 75  ? 0.2531 0.2761 0.4237 -0.0063 0.0252  -0.0105 81  LEU   C O   
1702 C  CB  . LEU   B 75  ? 0.2458 0.2554 0.4130 -0.0088 0.0275  -0.0176 81  LEU   C CB  
1703 C  CG  . LEU   B 75  ? 0.2702 0.2764 0.4495 -0.0113 0.0316  -0.0158 81  LEU   C CG  
1704 C  CD1 . LEU   B 75  ? 0.2709 0.2707 0.4487 -0.0099 0.0350  -0.0126 81  LEU   C CD1 
1705 C  CD2 . LEU   B 75  ? 0.2898 0.2942 0.4760 -0.0151 0.0314  -0.0229 81  LEU   C CD2 
1706 N  N   . ILE   B 76  ? 0.2383 0.2547 0.4049 -0.0040 0.0296  -0.0018 82  ILE   C N   
1707 C  CA  . ILE   B 76  ? 0.2575 0.2794 0.4277 -0.0034 0.0305  0.0022  82  ILE   C CA  
1708 C  C   . ILE   B 76  ? 0.2517 0.2723 0.4308 -0.0053 0.0343  0.0070  82  ILE   C C   
1709 O  O   . ILE   B 76  ? 0.2339 0.2492 0.4119 -0.0052 0.0359  0.0096  82  ILE   C O   
1710 C  CB  . ILE   B 76  ? 0.2941 0.3161 0.4533 0.0004  0.0295  0.0053  82  ILE   C CB  
1711 C  CG1 . ILE   B 76  ? 0.3330 0.3560 0.4835 0.0027  0.0256  0.0016  82  ILE   C CG1 
1712 C  CG2 . ILE   B 76  ? 0.3197 0.3461 0.4809 0.0014  0.0313  0.0098  82  ILE   C CG2 
1713 C  CD1 . ILE   B 76  ? 0.3605 0.3909 0.5155 0.0030  0.0236  -0.0009 82  ILE   C CD1 
1714 N  N   . PHE   B 77  ? 0.2450 0.2708 0.4331 -0.0069 0.0359  0.0088  83  PHE   C N   
1715 C  CA  . PHE   B 77  ? 0.2579 0.2828 0.4537 -0.0085 0.0397  0.0145  83  PHE   C CA  
1716 C  C   . PHE   B 77  ? 0.2575 0.2831 0.4448 -0.0056 0.0406  0.0205  83  PHE   C C   
1717 O  O   . PHE   B 77  ? 0.2827 0.3128 0.4644 -0.0034 0.0398  0.0207  83  PHE   C O   
1718 C  CB  . PHE   B 77  ? 0.2634 0.2940 0.4713 -0.0113 0.0413  0.0150  83  PHE   C CB  
1719 C  CG  . PHE   B 77  ? 0.2706 0.2993 0.4874 -0.0134 0.0454  0.0211  83  PHE   C CG  
1720 C  CD1 . PHE   B 77  ? 0.2814 0.3035 0.5053 -0.0158 0.0468  0.0206  83  PHE   C CD1 
1721 C  CD2 . PHE   B 77  ? 0.2890 0.3220 0.5063 -0.0127 0.0481  0.0277  83  PHE   C CD2 
1722 C  CE1 . PHE   B 77  ? 0.2925 0.3125 0.5249 -0.0174 0.0505  0.0270  83  PHE   C CE1 
1723 C  CE2 . PHE   B 77  ? 0.2896 0.3208 0.5143 -0.0145 0.0518  0.0341  83  PHE   C CE2 
1724 C  CZ  . PHE   B 77  ? 0.2926 0.3173 0.5253 -0.0168 0.0528  0.0340  83  PHE   C CZ  
1725 N  N   . VAL   B 78  ? 0.2177 0.2388 0.4040 -0.0056 0.0421  0.0252  84  VAL   C N   
1726 C  CA  . VAL   B 78  ? 0.2146 0.2358 0.3923 -0.0034 0.0425  0.0306  84  VAL   C CA  
1727 C  C   . VAL   B 78  ? 0.2064 0.2290 0.3908 -0.0049 0.0459  0.0375  84  VAL   C C   
1728 O  O   . VAL   B 78  ? 0.2126 0.2320 0.4059 -0.0069 0.0475  0.0395  84  VAL   C O   
1729 C  CB  . VAL   B 78  ? 0.2319 0.2472 0.4026 -0.0023 0.0408  0.0311  84  VAL   C CB  
1730 C  CG1 . VAL   B 78  ? 0.2436 0.2590 0.4055 -0.0007 0.0404  0.0364  84  VAL   C CG1 
1731 C  CG2 . VAL   B 78  ? 0.2384 0.2519 0.4026 -0.0010 0.0378  0.0249  84  VAL   C CG2 
1732 N  N   . GLU   B 79  ? 0.1907 0.2176 0.3705 -0.0038 0.0473  0.0415  85  GLU   C N   
1733 C  CA  . GLU   B 79  ? 0.1999 0.2284 0.3844 -0.0051 0.0507  0.0490  85  GLU   C CA  
1734 C  C   . GLU   B 79  ? 0.1929 0.2166 0.3743 -0.0049 0.0501  0.0543  85  GLU   C C   
1735 O  O   . GLU   B 79  ? 0.1899 0.2100 0.3638 -0.0035 0.0471  0.0525  85  GLU   C O   
1736 C  CB  . GLU   B 79  ? 0.2432 0.2774 0.4212 -0.0036 0.0526  0.0517  85  GLU   C CB  
1737 C  CG  . GLU   B 79  ? 0.3064 0.3469 0.4910 -0.0039 0.0543  0.0484  85  GLU   C CG  
1738 C  CD  . GLU   B 79  ? 0.4300 0.4723 0.6306 -0.0076 0.0567  0.0493  85  GLU   C CD  
1739 O  OE1 . GLU   B 79  ? 0.4678 0.5088 0.6742 -0.0095 0.0594  0.0555  85  GLU   C OE1 
1740 O  OE2 . GLU   B 79  ? 0.4656 0.5105 0.6731 -0.0086 0.0555  0.0437  85  GLU   C OE2 
1741 N  N   . ALA   B 80  ? 0.1977 0.2217 0.3858 -0.0065 0.0529  0.0614  86  ALA   C N   
1742 C  CA  . ALA   B 80  ? 0.2083 0.2289 0.3950 -0.0062 0.0521  0.0675  86  ALA   C CA  
1743 C  C   . ALA   B 80  ? 0.2229 0.2441 0.3946 -0.0041 0.0494  0.0690  86  ALA   C C   
1744 O  O   . ALA   B 80  ? 0.2256 0.2504 0.3885 -0.0031 0.0498  0.0683  86  ALA   C O   
1745 C  CB  . ALA   B 80  ? 0.2140 0.2358 0.4089 -0.0079 0.0556  0.0758  86  ALA   C CB  
1746 N  N   . SER   B 81  ? 0.2165 0.2340 0.3856 -0.0036 0.0465  0.0703  87  SER   C N   
1747 C  CA  . SER   B 81  ? 0.2374 0.2549 0.3935 -0.0023 0.0433  0.0720  87  SER   C CA  
1748 C  C   . SER   B 81  ? 0.2539 0.2708 0.4127 -0.0029 0.0424  0.0803  87  SER   C C   
1749 O  O   . SER   B 81  ? 0.2533 0.2694 0.4244 -0.0039 0.0448  0.0846  87  SER   C O   
1750 C  CB  . SER   B 81  ? 0.2358 0.2503 0.3866 -0.0013 0.0401  0.0655  87  SER   C CB  
1751 O  OG  . SER   B 81  ? 0.2285 0.2397 0.3880 -0.0018 0.0396  0.0661  87  SER   C OG  
1752 N  N   . GLU   B 82  ? 0.2722 0.2894 0.4203 -0.0024 0.0389  0.0829  88  GLU   C N   
1753 C  CA  . GLU   B 82  ? 0.2941 0.3117 0.4454 -0.0029 0.0373  0.0913  88  GLU   C CA  
1754 C  C   . GLU   B 82  ? 0.2863 0.3007 0.4493 -0.0028 0.0366  0.0914  88  GLU   C C   
1755 O  O   . GLU   B 82  ? 0.3028 0.3175 0.4734 -0.0029 0.0364  0.0987  88  GLU   C O   
1756 C  CB  . GLU   B 82  ? 0.3636 0.3830 0.5009 -0.0029 0.0332  0.0944  88  GLU   C CB  
1757 C  CG  . GLU   B 82  ? 0.4670 0.4843 0.5956 -0.0025 0.0291  0.0888  88  GLU   C CG  
1758 C  CD  . GLU   B 82  ? 0.5679 0.5866 0.6830 -0.0031 0.0248  0.0919  88  GLU   C CD  
1759 O  OE1 . GLU   B 82  ? 0.5813 0.6024 0.6876 -0.0031 0.0259  0.0942  88  GLU   C OE1 
1760 O  OE2 . GLU   B 82  ? 0.6085 0.6263 0.7219 -0.0037 0.0204  0.0920  88  GLU   C OE2 
1761 N  N   . TYR   B 83  ? 0.2551 0.2667 0.4200 -0.0023 0.0366  0.0836  89  TYR   C N   
1762 C  CA  . TYR   B 83  ? 0.2428 0.2514 0.4175 -0.0019 0.0365  0.0829  89  TYR   C CA  
1763 C  C   . TYR   B 83  ? 0.2374 0.2428 0.4237 -0.0021 0.0404  0.0780  89  TYR   C C   
1764 O  O   . TYR   B 83  ? 0.2447 0.2472 0.4402 -0.0016 0.0413  0.0778  89  TYR   C O   
1765 C  CB  . TYR   B 83  ? 0.2365 0.2442 0.4034 -0.0014 0.0330  0.0786  89  TYR   C CB  
1766 C  CG  . TYR   B 83  ? 0.2412 0.2484 0.3967 -0.0011 0.0322  0.0713  89  TYR   C CG  
1767 C  CD1 . TYR   B 83  ? 0.2447 0.2537 0.3873 -0.0011 0.0299  0.0718  89  TYR   C CD1 
1768 C  CD2 . TYR   B 83  ? 0.2423 0.2472 0.3996 -0.0007 0.0336  0.0639  89  TYR   C CD2 
1769 C  CE1 . TYR   B 83  ? 0.2472 0.2554 0.3804 -0.0004 0.0294  0.0653  89  TYR   C CE1 
1770 C  CE2 . TYR   B 83  ? 0.2535 0.2582 0.4012 -0.0001 0.0326  0.0580  89  TYR   C CE2 
1771 C  CZ  . TYR   B 83  ? 0.2621 0.2683 0.3983 0.0002  0.0306  0.0588  89  TYR   C CZ  
1772 O  OH  . TYR   B 83  ? 0.2628 0.2683 0.3907 0.0013  0.0300  0.0529  89  TYR   C OH  
1773 N  N   . TYR   B 84  ? 0.2142 0.2201 0.4002 -0.0028 0.0426  0.0736  90  TYR   C N   
1774 C  CA  . TYR   B 84  ? 0.2087 0.2117 0.4055 -0.0036 0.0457  0.0688  90  TYR   C CA  
1775 C  C   . TYR   B 84  ? 0.2176 0.2228 0.4185 -0.0052 0.0484  0.0702  90  TYR   C C   
1776 O  O   . TYR   B 84  ? 0.2052 0.2145 0.3978 -0.0051 0.0480  0.0710  90  TYR   C O   
1777 C  CB  . TYR   B 84  ? 0.1937 0.1955 0.3852 -0.0033 0.0447  0.0592  90  TYR   C CB  
1778 C  CG  . TYR   B 84  ? 0.1793 0.1782 0.3691 -0.0022 0.0432  0.0564  90  TYR   C CG  
1779 C  CD1 . TYR   B 84  ? 0.1808 0.1762 0.3810 -0.0019 0.0452  0.0575  90  TYR   C CD1 
1780 C  CD2 . TYR   B 84  ? 0.1844 0.1839 0.3628 -0.0013 0.0403  0.0527  90  TYR   C CD2 
1781 C  CE1 . TYR   B 84  ? 0.1929 0.1863 0.3920 -0.0008 0.0446  0.0550  90  TYR   C CE1 
1782 C  CE2 . TYR   B 84  ? 0.1922 0.1894 0.3693 -0.0004 0.0394  0.0507  90  TYR   C CE2 
1783 C  CZ  . TYR   B 84  ? 0.2003 0.1948 0.3878 -0.0002 0.0417  0.0518  90  TYR   C CZ  
1784 O  OH  . TYR   B 84  ? 0.2067 0.1996 0.3931 0.0007  0.0414  0.0499  90  TYR   C OH  
1785 N  N   . PRO   B 85  ? 0.2212 0.2237 0.4351 -0.0066 0.0515  0.0694  91  PRO   C N   
1786 C  CA  . PRO   B 85  ? 0.2216 0.2265 0.4404 -0.0086 0.0541  0.0695  91  PRO   C CA  
1787 C  C   . PRO   B 85  ? 0.2146 0.2219 0.4286 -0.0090 0.0531  0.0607  91  PRO   C C   
1788 O  O   . PRO   B 85  ? 0.2102 0.2164 0.4171 -0.0077 0.0506  0.0546  91  PRO   C O   
1789 C  CB  . PRO   B 85  ? 0.2360 0.2359 0.4706 -0.0103 0.0572  0.0702  91  PRO   C CB  
1790 C  CG  . PRO   B 85  ? 0.2491 0.2439 0.4848 -0.0090 0.0562  0.0649  91  PRO   C CG  
1791 C  CD  . PRO   B 85  ? 0.2241 0.2208 0.4485 -0.0066 0.0530  0.0671  91  PRO   C CD  
1792 N  N   . ALA   B 86  ? 0.2085 0.2195 0.4270 -0.0108 0.0551  0.0601  92  ALA   C N   
1793 C  CA  . ALA   B 86  ? 0.2151 0.2291 0.4313 -0.0111 0.0539  0.0522  92  ALA   C CA  
1794 C  C   . ALA   B 86  ? 0.2246 0.2336 0.4476 -0.0125 0.0534  0.0450  92  ALA   C C   
1795 O  O   . ALA   B 86  ? 0.2303 0.2351 0.4648 -0.0143 0.0557  0.0464  92  ALA   C O   
1796 C  CB  . ALA   B 86  ? 0.2085 0.2279 0.4310 -0.0131 0.0565  0.0539  92  ALA   C CB  
1797 N  N   . ARG   B 87  ? 0.2114 0.2202 0.4269 -0.0112 0.0505  0.0379  93  ARG   C N   
1798 C  CA  . ARG   B 87  ? 0.2189 0.2229 0.4379 -0.0121 0.0499  0.0308  93  ARG   C CA  
1799 C  C   . ARG   B 87  ? 0.2364 0.2424 0.4459 -0.0110 0.0466  0.0236  93  ARG   C C   
1800 O  O   . ARG   B 87  ? 0.2411 0.2513 0.4414 -0.0090 0.0448  0.0245  93  ARG   C O   
1801 C  CB  . ARG   B 87  ? 0.2278 0.2257 0.4470 -0.0107 0.0507  0.0331  93  ARG   C CB  
1802 C  CG  . ARG   B 87  ? 0.2238 0.2224 0.4299 -0.0078 0.0480  0.0335  93  ARG   C CG  
1803 C  CD  . ARG   B 87  ? 0.2250 0.2197 0.4321 -0.0064 0.0487  0.0375  93  ARG   C CD  
1804 N  NE  . ARG   B 87  ? 0.2379 0.2332 0.4332 -0.0043 0.0459  0.0361  93  ARG   C NE  
1805 C  CZ  . ARG   B 87  ? 0.2510 0.2431 0.4446 -0.0032 0.0457  0.0339  93  ARG   C CZ  
1806 N  NH1 . ARG   B 87  ? 0.2463 0.2341 0.4493 -0.0035 0.0485  0.0329  93  ARG   C NH1 
1807 N  NH2 . ARG   B 87  ? 0.2380 0.2310 0.4210 -0.0018 0.0431  0.0327  93  ARG   C NH2 
1808 N  N   . TYR   B 88  ? 0.2525 0.2551 0.4634 -0.0120 0.0458  0.0164  94  TYR   C N   
1809 C  CA  . TYR   B 88  ? 0.2793 0.2834 0.4801 -0.0107 0.0425  0.0102  94  TYR   C CA  
1810 C  C   . TYR   B 88  ? 0.2460 0.2463 0.4380 -0.0082 0.0419  0.0109  94  TYR   C C   
1811 O  O   . TYR   B 88  ? 0.2556 0.2508 0.4516 -0.0082 0.0441  0.0118  94  TYR   C O   
1812 C  CB  . TYR   B 88  ? 0.3172 0.3195 0.5220 -0.0132 0.0416  0.0021  94  TYR   C CB  
1813 C  CG  . TYR   B 88  ? 0.3580 0.3656 0.5704 -0.0159 0.0409  0.0002  94  TYR   C CG  
1814 C  CD1 . TYR   B 88  ? 0.3848 0.3993 0.5922 -0.0152 0.0375  -0.0021 94  TYR   C CD1 
1815 C  CD2 . TYR   B 88  ? 0.3826 0.3889 0.6083 -0.0192 0.0436  0.0017  94  TYR   C CD2 
1816 C  CE1 . TYR   B 88  ? 0.4017 0.4223 0.6177 -0.0177 0.0368  -0.0032 94  TYR   C CE1 
1817 C  CE2 . TYR   B 88  ? 0.3948 0.4066 0.6288 -0.0221 0.0430  0.0005  94  TYR   C CE2 
1818 C  CZ  . TYR   B 88  ? 0.4162 0.4357 0.6457 -0.0214 0.0396  -0.0020 94  TYR   C CZ  
1819 O  OH  . TYR   B 88  ? 0.4496 0.4754 0.6890 -0.0244 0.0391  -0.0029 94  TYR   C OH  
1820 N  N   . GLN   B 89  ? 0.2225 0.2251 0.4031 -0.0059 0.0392  0.0107  95  GLN   C N   
1821 C  CA  . GLN   B 89  ? 0.2159 0.2151 0.3882 -0.0038 0.0385  0.0111  95  GLN   C CA  
1822 C  C   . GLN   B 89  ? 0.2114 0.2110 0.3755 -0.0032 0.0359  0.0046  95  GLN   C C   
1823 O  O   . GLN   B 89  ? 0.2179 0.2218 0.3790 -0.0029 0.0335  0.0026  95  GLN   C O   
1824 C  CB  . GLN   B 89  ? 0.2262 0.2270 0.3916 -0.0019 0.0375  0.0170  95  GLN   C CB  
1825 C  CG  . GLN   B 89  ? 0.2357 0.2333 0.3939 -0.0004 0.0366  0.0180  95  GLN   C CG  
1826 C  CD  . GLN   B 89  ? 0.2234 0.2215 0.3776 0.0006  0.0358  0.0243  95  GLN   C CD  
1827 O  OE1 . GLN   B 89  ? 0.2280 0.2273 0.3874 -0.0001 0.0371  0.0295  95  GLN   C OE1 
1828 N  NE2 . GLN   B 89  ? 0.2245 0.2217 0.3692 0.0019  0.0336  0.0240  95  GLN   C NE2 
1829 N  N   . SER   B 90  ? 0.1901 0.1855 0.3510 -0.0028 0.0365  0.0017  96  SER   C N   
1830 C  CA  . SER   B 90  ? 0.1987 0.1942 0.3512 -0.0023 0.0342  -0.0040 96  SER   C CA  
1831 C  C   . SER   B 90  ? 0.1895 0.1846 0.3307 0.0002  0.0324  -0.0018 96  SER   C C   
1832 O  O   . SER   B 90  ? 0.1815 0.1753 0.3222 0.0011  0.0332  0.0034  96  SER   C O   
1833 C  CB  . SER   B 90  ? 0.2198 0.2110 0.3744 -0.0035 0.0363  -0.0093 96  SER   C CB  
1834 O  OG  . SER   B 90  ? 0.2216 0.2088 0.3766 -0.0024 0.0392  -0.0063 96  SER   C OG  
1835 N  N   . HIS   B 91  ? 0.1833 0.1795 0.3159 0.0011  0.0297  -0.0055 97  HIS   C N   
1836 C  CA  . HIS   B 91  ? 0.1957 0.1908 0.3175 0.0032  0.0279  -0.0038 97  HIS   C CA  
1837 C  C   . HIS   B 91  ? 0.1924 0.1887 0.3124 0.0047  0.0267  0.0014  97  HIS   C C   
1838 O  O   . HIS   B 91  ? 0.2084 0.2022 0.3230 0.0057  0.0265  0.0045  97  HIS   C O   
1839 C  CB  . HIS   B 91  ? 0.2056 0.1962 0.3251 0.0033  0.0304  -0.0033 97  HIS   C CB  
1840 C  CG  . HIS   B 91  ? 0.2196 0.2085 0.3391 0.0023  0.0320  -0.0090 97  HIS   C CG  
1841 N  ND1 . HIS   B 91  ? 0.2555 0.2439 0.3649 0.0030  0.0306  -0.0122 97  HIS   C ND1 
1842 C  CD2 . HIS   B 91  ? 0.2327 0.2197 0.3603 0.0006  0.0350  -0.0121 97  HIS   C CD2 
1843 C  CE1 . HIS   B 91  ? 0.2598 0.2463 0.3706 0.0017  0.0328  -0.0175 97  HIS   C CE1 
1844 N  NE2 . HIS   B 91  ? 0.2474 0.2326 0.3694 0.0003  0.0356  -0.0178 97  HIS   C NE2 
1845 N  N   . LEU   B 92  ? 0.1817 0.1820 0.3062 0.0045  0.0261  0.0021  98  LEU   C N   
1846 C  CA  . LEU   B 92  ? 0.1809 0.1826 0.3035 0.0059  0.0256  0.0063  98  LEU   C CA  
1847 C  C   . LEU   B 92  ? 0.1764 0.1808 0.2931 0.0081  0.0228  0.0048  98  LEU   C C   
1848 O  O   . LEU   B 92  ? 0.1845 0.1927 0.3036 0.0080  0.0214  0.0013  98  LEU   C O   
1849 C  CB  . LEU   B 92  ? 0.1877 0.1923 0.3199 0.0044  0.0278  0.0087  98  LEU   C CB  
1850 C  CG  . LEU   B 92  ? 0.2090 0.2149 0.3392 0.0055  0.0281  0.0134  98  LEU   C CG  
1851 C  CD1 . LEU   B 92  ? 0.2268 0.2286 0.3521 0.0057  0.0281  0.0172  98  LEU   C CD1 
1852 C  CD2 . LEU   B 92  ? 0.2215 0.2308 0.3611 0.0039  0.0306  0.0160  98  LEU   C CD2 
1853 N  N   . MET   B 93  ? 0.1661 0.1688 0.2756 0.0102  0.0218  0.0075  99  MET   C N   
1854 C  CA  . MET   B 93  ? 0.1678 0.1724 0.2722 0.0130  0.0195  0.0065  99  MET   C CA  
1855 C  C   . MET   B 93  ? 0.1708 0.1768 0.2754 0.0141  0.0207  0.0094  99  MET   C C   
1856 O  O   . MET   B 93  ? 0.1776 0.1804 0.2799 0.0134  0.0217  0.0124  99  MET   C O   
1857 C  CB  . MET   B 93  ? 0.1908 0.1903 0.2852 0.0146  0.0176  0.0068  99  MET   C CB  
1858 C  CG  . MET   B 93  ? 0.2068 0.2048 0.2998 0.0134  0.0171  0.0044  99  MET   C CG  
1859 S  SD  . MET   B 93  ? 0.2281 0.2199 0.3103 0.0147  0.0157  0.0059  99  MET   C SD  
1860 C  CE  . MET   B 93  ? 0.2106 0.1985 0.2935 0.0131  0.0176  0.0097  99  MET   C CE  
1861 N  N   . LEU   B 94  ? 0.1675 0.1783 0.2743 0.0159  0.0205  0.0085  100 LEU   C N   
1862 C  CA  . LEU   B 94  ? 0.1839 0.1962 0.2902 0.0172  0.0224  0.0108  100 LEU   C CA  
1863 C  C   . LEU   B 94  ? 0.1901 0.2007 0.2886 0.0211  0.0210  0.0103  100 LEU   C C   
1864 O  O   . LEU   B 94  ? 0.1899 0.2009 0.2867 0.0230  0.0187  0.0082  100 LEU   C O   
1865 C  CB  . LEU   B 94  ? 0.1955 0.2155 0.3119 0.0166  0.0243  0.0107  100 LEU   C CB  
1866 C  CG  . LEU   B 94  ? 0.2162 0.2381 0.3420 0.0129  0.0262  0.0115  100 LEU   C CG  
1867 C  CD1 . LEU   B 94  ? 0.2417 0.2714 0.3773 0.0124  0.0284  0.0119  100 LEU   C CD1 
1868 C  CD2 . LEU   B 94  ? 0.2363 0.2539 0.3605 0.0112  0.0281  0.0154  100 LEU   C CD2 
1869 N  N   . ALA   B 95  ? 0.1940 0.2024 0.2876 0.0221  0.0225  0.0122  101 ALA   C N   
1870 C  CA  . ALA   B 95  ? 0.1980 0.2041 0.2847 0.0259  0.0222  0.0114  101 ALA   C CA  
1871 C  C   . ALA   B 95  ? 0.1945 0.2034 0.2813 0.0268  0.0256  0.0128  101 ALA   C C   
1872 O  O   . ALA   B 95  ? 0.1963 0.2070 0.2861 0.0241  0.0276  0.0152  101 ALA   C O   
1873 C  CB  . ALA   B 95  ? 0.2067 0.2038 0.2832 0.0261  0.0202  0.0117  101 ALA   C CB  
1874 N  N   . VAL   B 96  ? 0.1889 0.1979 0.2723 0.0307  0.0265  0.0115  102 VAL   C N   
1875 C  CA  . VAL   B 96  ? 0.2066 0.2174 0.2878 0.0321  0.0302  0.0124  102 VAL   C CA  
1876 C  C   . VAL   B 96  ? 0.2221 0.2242 0.2913 0.0315  0.0295  0.0127  102 VAL   C C   
1877 O  O   . VAL   B 96  ? 0.2400 0.2353 0.3020 0.0335  0.0274  0.0108  102 VAL   C O   
1878 C  CB  . VAL   B 96  ? 0.2163 0.2308 0.2994 0.0370  0.0319  0.0105  102 VAL   C CB  
1879 C  CG1 . VAL   B 96  ? 0.2330 0.2490 0.3125 0.0386  0.0366  0.0111  102 VAL   C CG1 
1880 C  CG2 . VAL   B 96  ? 0.2145 0.2384 0.3103 0.0370  0.0317  0.0101  102 VAL   C CG2 
1881 N  N   . GLY   B 97  ? 0.2574 0.2597 0.3247 0.0287  0.0309  0.0153  103 GLY   C N   
1882 C  CA  . GLY   B 97  ? 0.2711 0.2660 0.3273 0.0275  0.0295  0.0157  103 GLY   C CA  
1883 C  C   . GLY   B 97  ? 0.2843 0.2811 0.3403 0.0240  0.0304  0.0195  103 GLY   C C   
1884 O  O   . GLY   B 97  ? 0.2859 0.2889 0.3511 0.0223  0.0322  0.0221  103 GLY   C O   
1885 N  N   . HIS   B 98  ? 0.2888 0.2801 0.3347 0.0227  0.0288  0.0201  104 HIS   C N   
1886 C  CA  . HIS   B 98  ? 0.2904 0.2838 0.3350 0.0195  0.0292  0.0243  104 HIS   C CA  
1887 C  C   . HIS   B 98  ? 0.2777 0.2705 0.3278 0.0158  0.0261  0.0274  104 HIS   C C   
1888 O  O   . HIS   B 98  ? 0.2689 0.2566 0.3170 0.0151  0.0228  0.0261  104 HIS   C O   
1889 C  CB  . HIS   B 98  ? 0.3230 0.3113 0.3537 0.0195  0.0284  0.0233  104 HIS   C CB  
1890 C  CG  . HIS   B 98  ? 0.3894 0.3806 0.4176 0.0166  0.0285  0.0280  104 HIS   C CG  
1891 N  ND1 . HIS   B 98  ? 0.4200 0.4182 0.4521 0.0169  0.0328  0.0312  104 HIS   C ND1 
1892 C  CD2 . HIS   B 98  ? 0.4251 0.4135 0.4479 0.0133  0.0247  0.0305  104 HIS   C CD2 
1893 C  CE1 . HIS   B 98  ? 0.4424 0.4414 0.4707 0.0140  0.0314  0.0358  104 HIS   C CE1 
1894 N  NE2 . HIS   B 98  ? 0.4489 0.4424 0.4716 0.0118  0.0263  0.0354  104 HIS   C NE2 
1895 N  N   . SER   B 99  ? 0.2712 0.2690 0.3280 0.0136  0.0274  0.0320  105 SER   C N   
1896 C  CA  . SER   B 99  ? 0.2720 0.2696 0.3351 0.0105  0.0252  0.0355  105 SER   C CA  
1897 C  C   . SER   B 99  ? 0.2849 0.2868 0.3511 0.0085  0.0267  0.0414  105 SER   C C   
1898 O  O   . SER   B 99  ? 0.3105 0.3173 0.3843 0.0088  0.0302  0.0431  105 SER   C O   
1899 C  CB  . SER   B 99  ? 0.2816 0.2808 0.3557 0.0106  0.0258  0.0340  105 SER   C CB  
1900 O  OG  . SER   B 99  ? 0.3161 0.3153 0.3972 0.0081  0.0247  0.0372  105 SER   C OG  
1901 N  N   . GLU   B 100 ? 0.2772 0.2775 0.3382 0.0065  0.0238  0.0447  106 GLU   C N   
1902 C  CA  . GLU   B 100 ? 0.2767 0.2808 0.3407 0.0045  0.0242  0.0513  106 GLU   C CA  
1903 C  C   . GLU   B 100 ? 0.2576 0.2617 0.3321 0.0026  0.0223  0.0544  106 GLU   C C   
1904 O  O   . GLU   B 100 ? 0.2456 0.2463 0.3214 0.0025  0.0201  0.0514  106 GLU   C O   
1905 C  CB  . GLU   B 100 ? 0.3498 0.3525 0.4006 0.0035  0.0215  0.0530  106 GLU   C CB  
1906 C  CG  . GLU   B 100 ? 0.5259 0.5297 0.5671 0.0054  0.0248  0.0512  106 GLU   C CG  
1907 C  CD  . GLU   B 100 ? 0.6677 0.6683 0.6934 0.0045  0.0218  0.0504  106 GLU   C CD  
1908 O  OE1 . GLU   B 100 ? 0.7276 0.7288 0.7515 0.0018  0.0180  0.0550  106 GLU   C OE1 
1909 O  OE2 . GLU   B 100 ? 0.7135 0.7107 0.7291 0.0066  0.0230  0.0451  106 GLU   C OE2 
1910 N  N   . PRO   B 101 ? 0.2609 0.2684 0.3427 0.0012  0.0230  0.0608  107 PRO   C N   
1911 C  CA  . PRO   B 101 ? 0.2554 0.2626 0.3481 0.0000  0.0216  0.0635  107 PRO   C CA  
1912 C  C   . PRO   B 101 ? 0.2589 0.2632 0.3477 -0.0012 0.0169  0.0630  107 PRO   C C   
1913 O  O   . PRO   B 101 ? 0.2502 0.2531 0.3464 -0.0014 0.0165  0.0617  107 PRO   C O   
1914 C  CB  . PRO   B 101 ? 0.2822 0.2932 0.3815 -0.0010 0.0228  0.0713  107 PRO   C CB  
1915 C  CG  . PRO   B 101 ? 0.2979 0.3115 0.3909 -0.0004 0.0256  0.0723  107 PRO   C CG  
1916 C  CD  . PRO   B 101 ? 0.2711 0.2828 0.3526 0.0010  0.0258  0.0658  107 PRO   C CD  
1917 N  N   . GLY   B 102 ? 0.2503 0.2539 0.3276 -0.0022 0.0135  0.0639  108 GLY   C N   
1918 C  CA  . GLY   B 102 ? 0.2452 0.2463 0.3185 -0.0040 0.0085  0.0636  108 GLY   C CA  
1919 C  C   . GLY   B 102 ? 0.2358 0.2320 0.3060 -0.0033 0.0080  0.0570  108 GLY   C C   
1920 O  O   . GLY   B 102 ? 0.2401 0.2341 0.3100 -0.0049 0.0046  0.0567  108 GLY   C O   
1921 N  N   . ASP   B 103 ? 0.2194 0.2139 0.2875 -0.0009 0.0113  0.0520  109 ASP   C N   
1922 C  CA  . ASP   B 103 ? 0.2231 0.2130 0.2885 0.0001  0.0109  0.0464  109 ASP   C CA  
1923 C  C   . ASP   B 103 ? 0.2157 0.2057 0.2919 0.0002  0.0121  0.0459  109 ASP   C C   
1924 O  O   . ASP   B 103 ? 0.2171 0.2034 0.2912 0.0007  0.0114  0.0423  109 ASP   C O   
1925 C  CB  . ASP   B 103 ? 0.2382 0.2269 0.2981 0.0030  0.0137  0.0415  109 ASP   C CB  
1926 C  CG  . ASP   B 103 ? 0.2673 0.2542 0.3146 0.0033  0.0128  0.0405  109 ASP   C CG  
1927 O  OD1 . ASP   B 103 ? 0.2805 0.2641 0.3208 0.0014  0.0090  0.0408  109 ASP   C OD1 
1928 O  OD2 . ASP   B 103 ? 0.2718 0.2608 0.3165 0.0054  0.0161  0.0394  109 ASP   C OD2 
1929 N  N   . CYS   B 104 ? 0.1902 0.1841 0.2776 -0.0001 0.0142  0.0494  110 CYS   C N   
1930 C  CA  . CYS   B 104 ? 0.1802 0.1739 0.2773 0.0001  0.0159  0.0484  110 CYS   C CA  
1931 C  C   . CYS   B 104 ? 0.1981 0.1895 0.2948 -0.0013 0.0133  0.0486  110 CYS   C C   
1932 O  O   . CYS   B 104 ? 0.2220 0.2141 0.3172 -0.0031 0.0102  0.0523  110 CYS   C O   
1933 C  CB  . CYS   B 104 ? 0.1909 0.1881 0.2999 -0.0003 0.0183  0.0526  110 CYS   C CB  
1934 S  SG  . CYS   B 104 ? 0.2370 0.2366 0.3501 0.0010  0.0224  0.0513  110 CYS   C SG  
1935 N  N   . GLY   B 105 ? 0.1858 0.1748 0.2836 -0.0005 0.0144  0.0450  111 GLY   C N   
1936 C  CA  . GLY   B 105 ? 0.1969 0.1838 0.2948 -0.0018 0.0126  0.0453  111 GLY   C CA  
1937 C  C   . GLY   B 105 ? 0.2053 0.1873 0.2923 -0.0018 0.0102  0.0421  111 GLY   C C   
1938 O  O   . GLY   B 105 ? 0.2199 0.1996 0.3067 -0.0028 0.0093  0.0418  111 GLY   C O   
1939 N  N   . GLY   B 106 ? 0.1911 0.1714 0.2696 -0.0006 0.0097  0.0397  112 GLY   C N   
1940 C  CA  . GLY   B 106 ? 0.1952 0.1701 0.2638 0.0000  0.0079  0.0362  112 GLY   C CA  
1941 C  C   . GLY   B 106 ? 0.2056 0.1783 0.2750 0.0018  0.0095  0.0331  112 GLY   C C   
1942 O  O   . GLY   B 106 ? 0.2129 0.1885 0.2870 0.0034  0.0122  0.0317  112 GLY   C O   
1943 N  N   . ILE   B 107 ? 0.2124 0.1801 0.2771 0.0011  0.0078  0.0322  113 ILE   C N   
1944 C  CA  . ILE   B 107 ? 0.2169 0.1828 0.2817 0.0027  0.0092  0.0301  113 ILE   C CA  
1945 C  C   . ILE   B 107 ? 0.2078 0.1712 0.2663 0.0059  0.0094  0.0264  113 ILE   C C   
1946 O  O   . ILE   B 107 ? 0.2011 0.1605 0.2525 0.0066  0.0078  0.0252  113 ILE   C O   
1947 C  CB  . ILE   B 107 ? 0.2622 0.2242 0.3260 0.0005  0.0078  0.0316  113 ILE   C CB  
1948 C  CG1 . ILE   B 107 ? 0.2902 0.2565 0.3636 -0.0017 0.0092  0.0350  113 ILE   C CG1 
1949 C  CG2 . ILE   B 107 ? 0.2721 0.2300 0.3314 0.0024  0.0085  0.0295  113 ILE   C CG2 
1950 C  CD1 . ILE   B 107 ? 0.3249 0.2888 0.3991 -0.0043 0.0081  0.0374  113 ILE   C CD1 
1951 N  N   . LEU   B 108 ? 0.1867 0.1522 0.2477 0.0079  0.0113  0.0246  114 LEU   C N   
1952 C  CA  . LEU   B 108 ? 0.1806 0.1445 0.2369 0.0111  0.0111  0.0216  114 LEU   C CA  
1953 C  C   . LEU   B 108 ? 0.1989 0.1589 0.2523 0.0111  0.0105  0.0219  114 LEU   C C   
1954 O  O   . LEU   B 108 ? 0.1811 0.1431 0.2385 0.0098  0.0119  0.0227  114 LEU   C O   
1955 C  CB  . LEU   B 108 ? 0.1811 0.1510 0.2427 0.0127  0.0130  0.0198  114 LEU   C CB  
1956 C  CG  . LEU   B 108 ? 0.1985 0.1685 0.2573 0.0160  0.0124  0.0171  114 LEU   C CG  
1957 C  CD1 . LEU   B 108 ? 0.2255 0.1932 0.2792 0.0186  0.0116  0.0161  114 LEU   C CD1 
1958 C  CD2 . LEU   B 108 ? 0.1973 0.1738 0.2627 0.0164  0.0138  0.0153  114 LEU   C CD2 
1959 N  N   . ARG   B 109 ? 0.2027 0.1569 0.2492 0.0126  0.0089  0.0213  115 ARG   C N   
1960 C  CA  . ARG   B 109 ? 0.2223 0.1725 0.2657 0.0126  0.0085  0.0223  115 ARG   C CA  
1961 C  C   . ARG   B 109 ? 0.2315 0.1789 0.2698 0.0164  0.0075  0.0208  115 ARG   C C   
1962 O  O   . ARG   B 109 ? 0.2404 0.1863 0.2764 0.0188  0.0067  0.0192  115 ARG   C O   
1963 C  CB  . ARG   B 109 ? 0.2793 0.2236 0.3205 0.0096  0.0071  0.0247  115 ARG   C CB  
1964 C  CG  . ARG   B 109 ? 0.3920 0.3301 0.4274 0.0102  0.0050  0.0236  115 ARG   C CG  
1965 C  CD  . ARG   B 109 ? 0.5059 0.4386 0.5399 0.0063  0.0032  0.0257  115 ARG   C CD  
1966 N  NE  . ARG   B 109 ? 0.5970 0.5340 0.6358 0.0028  0.0028  0.0273  115 ARG   C NE  
1967 C  CZ  . ARG   B 109 ? 0.6686 0.6077 0.7129 -0.0006 0.0029  0.0304  115 ARG   C CZ  
1968 N  NH1 . ARG   B 109 ? 0.6684 0.6059 0.7136 -0.0012 0.0041  0.0321  115 ARG   C NH1 
1969 N  NH2 . ARG   B 109 ? 0.6779 0.6214 0.7270 -0.0033 0.0021  0.0321  115 ARG   C NH2 
1970 N  N   . CYS   B 110 ? 0.2263 0.1728 0.2627 0.0170  0.0075  0.0217  116 CYS   C N   
1971 C  CA  . CYS   B 110 ? 0.2321 0.1760 0.2638 0.0207  0.0061  0.0213  116 CYS   C CA  
1972 C  C   . CYS   B 110 ? 0.2519 0.1886 0.2787 0.0197  0.0055  0.0244  116 CYS   C C   
1973 O  O   . CYS   B 110 ? 0.2483 0.1824 0.2760 0.0161  0.0061  0.0263  116 CYS   C O   
1974 C  CB  . CYS   B 110 ? 0.2364 0.1870 0.2699 0.0225  0.0064  0.0198  116 CYS   C CB  
1975 S  SG  . CYS   B 110 ? 0.2300 0.1826 0.2634 0.0198  0.0082  0.0211  116 CYS   C SG  
1976 N  N   . GLN   B 111 ? 0.2610 0.1945 0.2831 0.0228  0.0043  0.0253  117 GLN   C N   
1977 C  CA  . GLN   B 111 ? 0.2938 0.2202 0.3114 0.0219  0.0040  0.0289  117 GLN   C CA  
1978 C  C   . GLN   B 111 ? 0.2887 0.2178 0.3070 0.0186  0.0061  0.0311  117 GLN   C C   
1979 O  O   . GLN   B 111 ? 0.3053 0.2292 0.3216 0.0164  0.0066  0.0345  117 GLN   C O   
1980 C  CB  . GLN   B 111 ? 0.3303 0.2538 0.3431 0.0262  0.0023  0.0302  117 GLN   C CB  
1981 C  CG  . GLN   B 111 ? 0.4061 0.3379 0.4190 0.0285  0.0019  0.0292  117 GLN   C CG  
1982 C  CD  . GLN   B 111 ? 0.5277 0.4584 0.5367 0.0331  -0.0004 0.0307  117 GLN   C CD  
1983 O  OE1 . GLN   B 111 ? 0.5573 0.4935 0.5687 0.0364  -0.0019 0.0285  117 GLN   C OE1 
1984 N  NE2 . GLN   B 111 ? 0.5358 0.4603 0.5394 0.0333  -0.0008 0.0350  117 GLN   C NE2 
1985 N  N   . HIS   B 112 ? 0.2585 0.1955 0.2801 0.0182  0.0076  0.0291  118 HIS   C N   
1986 C  CA  . HIS   B 112 ? 0.2529 0.1927 0.2750 0.0158  0.0103  0.0305  118 HIS   C CA  
1987 C  C   . HIS   B 112 ? 0.2717 0.2133 0.3005 0.0120  0.0124  0.0308  118 HIS   C C   
1988 O  O   . HIS   B 112 ? 0.2867 0.2300 0.3169 0.0099  0.0152  0.0324  118 HIS   C O   
1989 C  CB  . HIS   B 112 ? 0.2527 0.1993 0.2743 0.0174  0.0108  0.0278  118 HIS   C CB  
1990 C  CG  . HIS   B 112 ? 0.2611 0.2073 0.2767 0.0211  0.0081  0.0278  118 HIS   C CG  
1991 N  ND1 . HIS   B 112 ? 0.2616 0.2116 0.2792 0.0239  0.0058  0.0249  118 HIS   C ND1 
1992 C  CD2 . HIS   B 112 ? 0.2631 0.2061 0.2715 0.0225  0.0073  0.0309  118 HIS   C CD2 
1993 C  CE1 . HIS   B 112 ? 0.2725 0.2219 0.2848 0.0270  0.0034  0.0262  118 HIS   C CE1 
1994 N  NE2 . HIS   B 112 ? 0.2766 0.2215 0.2828 0.0263  0.0041  0.0300  118 HIS   C NE2 
1995 N  N   . GLY   B 113 ? 0.2580 0.2002 0.2911 0.0113  0.0114  0.0295  119 GLY   C N   
1996 C  CA  . GLY   B 113 ? 0.2502 0.1948 0.2900 0.0079  0.0128  0.0304  119 GLY   C CA  
1997 C  C   . GLY   B 113 ? 0.2236 0.1732 0.2686 0.0083  0.0127  0.0278  119 GLY   C C   
1998 O  O   . GLY   B 113 ? 0.2188 0.1688 0.2619 0.0108  0.0112  0.0255  119 GLY   C O   
1999 N  N   . VAL   B 114 ? 0.2034 0.1572 0.2555 0.0060  0.0146  0.0285  120 VAL   C N   
2000 C  CA  . VAL   B 114 ? 0.2180 0.1764 0.2759 0.0060  0.0149  0.0271  120 VAL   C CA  
2001 C  C   . VAL   B 114 ? 0.2037 0.1665 0.2631 0.0080  0.0164  0.0238  120 VAL   C C   
2002 O  O   . VAL   B 114 ? 0.2144 0.1790 0.2749 0.0079  0.0188  0.0231  120 VAL   C O   
2003 C  CB  . VAL   B 114 ? 0.2271 0.1884 0.2930 0.0031  0.0163  0.0297  120 VAL   C CB  
2004 C  CG1 . VAL   B 114 ? 0.2407 0.2067 0.3129 0.0033  0.0168  0.0289  120 VAL   C CG1 
2005 C  CG2 . VAL   B 114 ? 0.2378 0.1953 0.3027 0.0005  0.0138  0.0328  120 VAL   C CG2 
2006 N  N   . VAL   B 115 ? 0.1982 0.1629 0.2578 0.0097  0.0152  0.0217  121 VAL   C N   
2007 C  CA  . VAL   B 115 ? 0.1941 0.1632 0.2561 0.0112  0.0161  0.0185  121 VAL   C CA  
2008 C  C   . VAL   B 115 ? 0.2010 0.1744 0.2717 0.0098  0.0181  0.0182  121 VAL   C C   
2009 O  O   . VAL   B 115 ? 0.2133 0.1895 0.2878 0.0096  0.0200  0.0158  121 VAL   C O   
2010 C  CB  . VAL   B 115 ? 0.2017 0.1711 0.2605 0.0139  0.0139  0.0168  121 VAL   C CB  
2011 C  CG1 . VAL   B 115 ? 0.1851 0.1602 0.2481 0.0149  0.0144  0.0137  121 VAL   C CG1 
2012 C  CG2 . VAL   B 115 ? 0.2200 0.1849 0.2709 0.0159  0.0119  0.0174  121 VAL   C CG2 
2013 N  N   . GLY   B 116 ? 0.1776 0.1510 0.2512 0.0086  0.0177  0.0205  122 GLY   C N   
2014 C  CA  . GLY   B 116 ? 0.1942 0.1713 0.2763 0.0074  0.0195  0.0213  122 GLY   C CA  
2015 C  C   . GLY   B 116 ? 0.1968 0.1738 0.2797 0.0064  0.0182  0.0244  122 GLY   C C   
2016 O  O   . GLY   B 116 ? 0.1935 0.1671 0.2706 0.0060  0.0161  0.0257  122 GLY   C O   
2017 N  N   . ILE   B 117 ? 0.1775 0.1580 0.2676 0.0056  0.0196  0.0258  123 ILE   C N   
2018 C  CA  . ILE   B 117 ? 0.1837 0.1648 0.2742 0.0045  0.0183  0.0293  123 ILE   C CA  
2019 C  C   . ILE   B 117 ? 0.1778 0.1622 0.2707 0.0052  0.0192  0.0292  123 ILE   C C   
2020 O  O   . ILE   B 117 ? 0.1728 0.1598 0.2717 0.0056  0.0214  0.0275  123 ILE   C O   
2021 C  CB  . ILE   B 117 ? 0.2078 0.1903 0.3056 0.0024  0.0189  0.0334  123 ILE   C CB  
2022 C  CG1 . ILE   B 117 ? 0.2162 0.2012 0.3238 0.0026  0.0223  0.0329  123 ILE   C CG1 
2023 C  CG2 . ILE   B 117 ? 0.2171 0.1968 0.3123 0.0012  0.0174  0.0347  123 ILE   C CG2 
2024 C  CD1 . ILE   B 117 ? 0.2258 0.2127 0.3427 0.0011  0.0231  0.0378  123 ILE   C CD1 
2025 N  N   . VAL   B 118 ? 0.1790 0.1633 0.2674 0.0051  0.0177  0.0310  124 VAL   C N   
2026 C  CA  . VAL   B 118 ? 0.1708 0.1586 0.2613 0.0056  0.0191  0.0317  124 VAL   C CA  
2027 C  C   . VAL   B 118 ? 0.1765 0.1677 0.2778 0.0043  0.0213  0.0347  124 VAL   C C   
2028 O  O   . VAL   B 118 ? 0.1801 0.1711 0.2851 0.0028  0.0208  0.0381  124 VAL   C O   
2029 C  CB  . VAL   B 118 ? 0.1908 0.1778 0.2736 0.0054  0.0174  0.0336  124 VAL   C CB  
2030 C  CG1 . VAL   B 118 ? 0.1854 0.1766 0.2704 0.0058  0.0194  0.0354  124 VAL   C CG1 
2031 C  CG2 . VAL   B 118 ? 0.2013 0.1841 0.2742 0.0071  0.0158  0.0300  124 VAL   C CG2 
2032 N  N   . SER   B 119 ? 0.1669 0.1611 0.2738 0.0049  0.0237  0.0334  125 SER   C N   
2033 C  CA  . SER   B 119 ? 0.1786 0.1750 0.2963 0.0037  0.0261  0.0360  125 SER   C CA  
2034 C  C   . SER   B 119 ? 0.1851 0.1850 0.3059 0.0036  0.0279  0.0378  125 SER   C C   
2035 O  O   . SER   B 119 ? 0.1877 0.1891 0.3158 0.0025  0.0295  0.0421  125 SER   C O   
2036 C  CB  . SER   B 119 ? 0.1957 0.1913 0.3195 0.0036  0.0278  0.0321  125 SER   C CB  
2037 O  OG  . SER   B 119 ? 0.2012 0.1979 0.3360 0.0026  0.0304  0.0340  125 SER   C OG  
2038 N  N   . THR   B 120 ? 0.1727 0.1742 0.2890 0.0050  0.0281  0.0349  126 THR   C N   
2039 C  CA  . THR   B 120 ? 0.1694 0.1750 0.2896 0.0049  0.0305  0.0366  126 THR   C CA  
2040 C  C   . THR   B 120 ? 0.1781 0.1848 0.2885 0.0066  0.0301  0.0363  126 THR   C C   
2041 O  O   . THR   B 120 ? 0.1835 0.1873 0.2851 0.0080  0.0280  0.0336  126 THR   C O   
2042 C  CB  . THR   B 120 ? 0.1777 0.1859 0.3065 0.0046  0.0324  0.0330  126 THR   C CB  
2043 O  OG1 . THR   B 120 ? 0.1839 0.1929 0.3078 0.0065  0.0312  0.0282  126 THR   C OG1 
2044 C  CG2 . THR   B 120 ? 0.1935 0.1997 0.3306 0.0031  0.0330  0.0317  126 THR   C CG2 
2045 N  N   . GLY   B 121 ? 0.2083 0.2188 0.3205 0.0064  0.0326  0.0392  127 GLY   C N   
2046 C  CA  . GLY   B 121 ? 0.2394 0.2512 0.3426 0.0083  0.0332  0.0387  127 GLY   C CA  
2047 C  C   . GLY   B 121 ? 0.2795 0.2968 0.3877 0.0081  0.0372  0.0415  127 GLY   C C   
2048 O  O   . GLY   B 121 ? 0.2904 0.3096 0.4078 0.0061  0.0389  0.0452  127 GLY   C O   
2049 N  N   . GLY   B 122 ? 0.3014 0.3210 0.4039 0.0103  0.0388  0.0400  128 GLY   C N   
2050 C  CA  . GLY   B 122 ? 0.3161 0.3417 0.4231 0.0102  0.0432  0.0428  128 GLY   C CA  
2051 C  C   . GLY   B 122 ? 0.3162 0.3461 0.4265 0.0126  0.0452  0.0387  128 GLY   C C   
2052 O  O   . GLY   B 122 ? 0.3108 0.3396 0.4231 0.0136  0.0429  0.0341  128 GLY   C O   
2053 N  N   . ASN   B 123 ? 0.3209 0.3563 0.4320 0.0134  0.0495  0.0407  129 ASN   C N   
2054 C  CA  . ASN   B 123 ? 0.3306 0.3715 0.4460 0.0160  0.0519  0.0376  129 ASN   C CA  
2055 C  C   . ASN   B 123 ? 0.3136 0.3511 0.4211 0.0196  0.0494  0.0322  129 ASN   C C   
2056 O  O   . ASN   B 123 ? 0.3274 0.3685 0.4409 0.0215  0.0492  0.0288  129 ASN   C O   
2057 C  CB  . ASN   B 123 ? 0.3810 0.4273 0.5124 0.0139  0.0525  0.0370  129 ASN   C CB  
2058 C  CG  . ASN   B 123 ? 0.4753 0.5281 0.6158 0.0119  0.0575  0.0419  129 ASN   C CG  
2059 O  OD1 . ASN   B 123 ? 0.5184 0.5713 0.6534 0.0115  0.0604  0.0467  129 ASN   C OD1 
2060 N  ND2 . ASN   B 123 ? 0.4845 0.5429 0.6389 0.0103  0.0584  0.0409  129 ASN   C ND2 
2061 N  N   . GLY   B 124 ? 0.2923 0.3231 0.3866 0.0206  0.0474  0.0316  130 GLY   C N   
2062 C  CA  . GLY   B 124 ? 0.2875 0.3136 0.3736 0.0240  0.0452  0.0268  130 GLY   C CA  
2063 C  C   . GLY   B 124 ? 0.2703 0.2930 0.3594 0.0237  0.0407  0.0239  130 GLY   C C   
2064 O  O   . GLY   B 124 ? 0.2689 0.2887 0.3538 0.0267  0.0390  0.0203  130 GLY   C O   
2065 N  N   . LEU   B 125 ? 0.2438 0.2665 0.3399 0.0203  0.0390  0.0255  131 LEU   C N   
2066 C  CA  . LEU   B 125 ? 0.2337 0.2531 0.3316 0.0199  0.0351  0.0227  131 LEU   C CA  
2067 C  C   . LEU   B 125 ? 0.2217 0.2350 0.3152 0.0174  0.0326  0.0245  131 LEU   C C   
2068 O  O   . LEU   B 125 ? 0.2336 0.2470 0.3273 0.0152  0.0337  0.0284  131 LEU   C O   
2069 C  CB  . LEU   B 125 ? 0.2459 0.2706 0.3566 0.0182  0.0354  0.0220  131 LEU   C CB  
2070 C  CG  . LEU   B 125 ? 0.2793 0.3115 0.3970 0.0202  0.0372  0.0204  131 LEU   C CG  
2071 C  CD1 . LEU   B 125 ? 0.3094 0.3470 0.4403 0.0173  0.0376  0.0202  131 LEU   C CD1 
2072 C  CD2 . LEU   B 125 ? 0.2907 0.3219 0.4039 0.0240  0.0349  0.0167  131 LEU   C CD2 
2073 N  N   . VAL   B 126 ? 0.1833 0.1919 0.2737 0.0177  0.0294  0.0221  132 VAL   C N   
2074 C  CA  . VAL   B 126 ? 0.1789 0.1826 0.2671 0.0152  0.0272  0.0237  132 VAL   C CA  
2075 C  C   . VAL   B 126 ? 0.1822 0.1859 0.2766 0.0144  0.0260  0.0216  132 VAL   C C   
2076 O  O   . VAL   B 126 ? 0.1854 0.1900 0.2800 0.0163  0.0250  0.0183  132 VAL   C O   
2077 C  CB  . VAL   B 126 ? 0.2070 0.2040 0.2837 0.0162  0.0246  0.0229  132 VAL   C CB  
2078 C  CG1 . VAL   B 126 ? 0.2364 0.2310 0.3089 0.0194  0.0235  0.0190  132 VAL   C CG1 
2079 C  CG2 . VAL   B 126 ? 0.2126 0.2055 0.2889 0.0135  0.0223  0.0246  132 VAL   C CG2 
2080 N  N   . GLY   B 127 ? 0.1702 0.1734 0.2701 0.0117  0.0262  0.0236  133 GLY   C N   
2081 C  CA  . GLY   B 127 ? 0.1630 0.1659 0.2682 0.0108  0.0256  0.0212  133 GLY   C CA  
2082 C  C   . GLY   B 127 ? 0.1771 0.1750 0.2790 0.0097  0.0241  0.0220  133 GLY   C C   
2083 O  O   . GLY   B 127 ? 0.1777 0.1741 0.2788 0.0085  0.0240  0.0256  133 GLY   C O   
2084 N  N   . PHE   B 128 ? 0.1692 0.1653 0.2694 0.0103  0.0228  0.0189  134 PHE   C N   
2085 C  CA  . PHE   B 128 ? 0.1701 0.1618 0.2672 0.0094  0.0219  0.0196  134 PHE   C CA  
2086 C  C   . PHE   B 128 ? 0.1674 0.1596 0.2707 0.0082  0.0233  0.0177  134 PHE   C C   
2087 O  O   . PHE   B 128 ? 0.1774 0.1714 0.2821 0.0087  0.0233  0.0141  134 PHE   C O   
2088 C  CB  . PHE   B 128 ? 0.1643 0.1526 0.2523 0.0112  0.0196  0.0179  134 PHE   C CB  
2089 C  CG  . PHE   B 128 ? 0.1730 0.1599 0.2543 0.0130  0.0184  0.0184  134 PHE   C CG  
2090 C  CD1 . PHE   B 128 ? 0.1799 0.1634 0.2564 0.0120  0.0175  0.0209  134 PHE   C CD1 
2091 C  CD2 . PHE   B 128 ? 0.1896 0.1788 0.2698 0.0156  0.0183  0.0161  134 PHE   C CD2 
2092 C  CE1 . PHE   B 128 ? 0.2008 0.1821 0.2703 0.0136  0.0166  0.0205  134 PHE   C CE1 
2093 C  CE2 . PHE   B 128 ? 0.2048 0.1922 0.2788 0.0176  0.0179  0.0161  134 PHE   C CE2 
2094 C  CZ  . PHE   B 128 ? 0.2090 0.1920 0.2772 0.0166  0.0172  0.0180  134 PHE   C CZ  
2095 N  N   . ALA   B 129 ? 0.1572 0.1476 0.2637 0.0067  0.0244  0.0199  135 ALA   C N   
2096 C  CA  . ALA   B 129 ? 0.1674 0.1572 0.2788 0.0059  0.0263  0.0178  135 ALA   C CA  
2097 C  C   . ALA   B 129 ? 0.1793 0.1664 0.2830 0.0067  0.0252  0.0159  135 ALA   C C   
2098 O  O   . ALA   B 129 ? 0.1770 0.1616 0.2764 0.0066  0.0242  0.0185  135 ALA   C O   
2099 C  CB  . ALA   B 129 ? 0.1711 0.1603 0.2897 0.0046  0.0283  0.0215  135 ALA   C CB  
2100 N  N   . ASP   B 130 ? 0.1747 0.1624 0.2765 0.0072  0.0251  0.0116  136 ASP   C N   
2101 C  CA  . ASP   B 130 ? 0.1828 0.1681 0.2766 0.0081  0.0241  0.0101  136 ASP   C CA  
2102 C  C   . ASP   B 130 ? 0.1915 0.1747 0.2870 0.0070  0.0268  0.0108  136 ASP   C C   
2103 O  O   . ASP   B 130 ? 0.2004 0.1843 0.3035 0.0060  0.0296  0.0100  136 ASP   C O   
2104 C  CB  . ASP   B 130 ? 0.1987 0.1862 0.2905 0.0087  0.0232  0.0052  136 ASP   C CB  
2105 C  CG  . ASP   B 130 ? 0.2437 0.2293 0.3261 0.0098  0.0217  0.0040  136 ASP   C CG  
2106 O  OD1 . ASP   B 130 ? 0.2491 0.2323 0.3253 0.0110  0.0200  0.0066  136 ASP   C OD1 
2107 O  OD2 . ASP   B 130 ? 0.2961 0.2820 0.3771 0.0093  0.0226  0.0005  136 ASP   C OD2 
2108 N  N   . VAL   B 131 ? 0.1799 0.1605 0.2687 0.0073  0.0264  0.0123  137 VAL   C N   
2109 C  CA  . VAL   B 131 ? 0.1803 0.1595 0.2703 0.0066  0.0294  0.0129  137 VAL   C CA  
2110 C  C   . VAL   B 131 ? 0.1947 0.1723 0.2755 0.0073  0.0294  0.0108  137 VAL   C C   
2111 O  O   . VAL   B 131 ? 0.2008 0.1773 0.2810 0.0069  0.0324  0.0112  137 VAL   C O   
2112 C  CB  . VAL   B 131 ? 0.1895 0.1677 0.2824 0.0055  0.0297  0.0181  137 VAL   C CB  
2113 C  CG1 . VAL   B 131 ? 0.1837 0.1639 0.2853 0.0047  0.0297  0.0206  137 VAL   C CG1 
2114 C  CG2 . VAL   B 131 ? 0.1919 0.1674 0.2767 0.0057  0.0264  0.0203  137 VAL   C CG2 
2115 N  N   . ARG   B 132 ? 0.1924 0.1701 0.2661 0.0087  0.0262  0.0090  138 ARG   C N   
2116 C  CA  . ARG   B 132 ? 0.1964 0.1727 0.2605 0.0096  0.0256  0.0082  138 ARG   C CA  
2117 C  C   . ARG   B 132 ? 0.2096 0.1868 0.2718 0.0092  0.0282  0.0040  138 ARG   C C   
2118 O  O   . ARG   B 132 ? 0.2344 0.2103 0.2884 0.0097  0.0288  0.0041  138 ARG   C O   
2119 C  CB  . ARG   B 132 ? 0.1960 0.1726 0.2541 0.0115  0.0213  0.0077  138 ARG   C CB  
2120 C  CG  . ARG   B 132 ? 0.2002 0.1744 0.2576 0.0122  0.0192  0.0114  138 ARG   C CG  
2121 C  CD  . ARG   B 132 ? 0.1988 0.1736 0.2517 0.0147  0.0155  0.0105  138 ARG   C CD  
2122 N  NE  . ARG   B 132 ? 0.1905 0.1703 0.2494 0.0150  0.0149  0.0075  138 ARG   C NE  
2123 C  CZ  . ARG   B 132 ? 0.2287 0.2108 0.2869 0.0172  0.0121  0.0066  138 ARG   C CZ  
2124 N  NH1 . ARG   B 132 ? 0.2033 0.1831 0.2548 0.0197  0.0097  0.0082  138 ARG   C NH1 
2125 N  NH2 . ARG   B 132 ? 0.2170 0.2040 0.2820 0.0170  0.0120  0.0043  138 ARG   C NH2 
2126 N  N   . ASP   B 133 ? 0.1997 0.1789 0.2687 0.0084  0.0297  0.0002  139 ASP   C N   
2127 C  CA  . ASP   B 133 ? 0.2159 0.1953 0.2832 0.0078  0.0324  -0.0047 139 ASP   C CA  
2128 C  C   . ASP   B 133 ? 0.2249 0.2024 0.2963 0.0072  0.0380  -0.0039 139 ASP   C C   
2129 O  O   . ASP   B 133 ? 0.2420 0.2189 0.3109 0.0070  0.0411  -0.0081 139 ASP   C O   
2130 C  CB  . ASP   B 133 ? 0.2265 0.2081 0.3000 0.0069  0.0316  -0.0096 139 ASP   C CB  
2131 C  CG  . ASP   B 133 ? 0.2774 0.2589 0.3633 0.0060  0.0339  -0.0080 139 ASP   C CG  
2132 O  OD1 . ASP   B 133 ? 0.2470 0.2285 0.3361 0.0063  0.0332  -0.0028 139 ASP   C OD1 
2133 O  OD2 . ASP   B 133 ? 0.3019 0.2830 0.3941 0.0049  0.0365  -0.0118 139 ASP   C OD2 
2134 N  N   . LEU   B 134 ? 0.2096 0.1867 0.2879 0.0069  0.0392  0.0012  140 LEU   C N   
2135 C  CA  . LEU   B 134 ? 0.2078 0.1842 0.2926 0.0065  0.0444  0.0027  140 LEU   C CA  
2136 C  C   . LEU   B 134 ? 0.2266 0.2019 0.3041 0.0067  0.0462  0.0053  140 LEU   C C   
2137 O  O   . LEU   B 134 ? 0.2350 0.2102 0.3152 0.0062  0.0460  0.0108  140 LEU   C O   
2138 C  CB  . LEU   B 134 ? 0.1997 0.1770 0.2954 0.0060  0.0441  0.0075  140 LEU   C CB  
2139 C  CG  . LEU   B 134 ? 0.2226 0.2010 0.3255 0.0057  0.0426  0.0060  140 LEU   C CG  
2140 C  CD1 . LEU   B 134 ? 0.2292 0.2088 0.3411 0.0052  0.0419  0.0116  140 LEU   C CD1 
2141 C  CD2 . LEU   B 134 ? 0.2370 0.2146 0.3454 0.0055  0.0465  0.0007  140 LEU   C CD2 
2142 N  N   . LEU   B 135 ? 0.2313 0.2059 0.2992 0.0072  0.0476  0.0016  141 LEU   C N   
2143 C  CA  . LEU   B 135 ? 0.2497 0.2233 0.3091 0.0074  0.0492  0.0045  141 LEU   C CA  
2144 C  C   . LEU   B 135 ? 0.2481 0.2220 0.3142 0.0069  0.0548  0.0079  141 LEU   C C   
2145 O  O   . LEU   B 135 ? 0.2540 0.2275 0.3171 0.0065  0.0554  0.0127  141 LEU   C O   
2146 C  CB  . LEU   B 135 ? 0.2703 0.2435 0.3170 0.0080  0.0496  0.0001  141 LEU   C CB  
2147 C  CG  . LEU   B 135 ? 0.3061 0.2803 0.3470 0.0085  0.0439  -0.0037 141 LEU   C CG  
2148 C  CD1 . LEU   B 135 ? 0.3295 0.3038 0.3571 0.0090  0.0435  -0.0071 141 LEU   C CD1 
2149 C  CD2 . LEU   B 135 ? 0.2969 0.2709 0.3374 0.0090  0.0382  0.0005  141 LEU   C CD2 
2150 N  N   . TRP   B 136 ? 0.2389 0.2136 0.3150 0.0071  0.0589  0.0057  142 TRP   C N   
2151 C  CA  . TRP   B 136 ? 0.2553 0.2313 0.3400 0.0071  0.0646  0.0088  142 TRP   C CA  
2152 C  C   . TRP   B 136 ? 0.2611 0.2387 0.3538 0.0060  0.0623  0.0161  142 TRP   C C   
2153 O  O   . TRP   B 136 ? 0.2800 0.2594 0.3791 0.0057  0.0663  0.0199  142 TRP   C O   
2154 C  CB  . TRP   B 136 ? 0.2508 0.2269 0.3455 0.0080  0.0693  0.0047  142 TRP   C CB  
2155 C  CG  . TRP   B 136 ? 0.2483 0.2243 0.3514 0.0077  0.0657  0.0041  142 TRP   C CG  
2156 C  CD1 . TRP   B 136 ? 0.2665 0.2412 0.3673 0.0076  0.0634  -0.0014 142 TRP   C CD1 
2157 C  CD2 . TRP   B 136 ? 0.2484 0.2263 0.3641 0.0073  0.0644  0.0094  142 TRP   C CD2 
2158 N  NE1 . TRP   B 136 ? 0.2660 0.2413 0.3772 0.0072  0.0610  0.0005  142 TRP   C NE1 
2159 C  CE2 . TRP   B 136 ? 0.2575 0.2347 0.3773 0.0072  0.0616  0.0072  142 TRP   C CE2 
2160 C  CE3 . TRP   B 136 ? 0.2468 0.2272 0.3709 0.0070  0.0652  0.0160  142 TRP   C CE3 
2161 C  CZ2 . TRP   B 136 ? 0.2515 0.2302 0.3824 0.0068  0.0598  0.0116  142 TRP   C CZ2 
2162 C  CZ3 . TRP   B 136 ? 0.2518 0.2341 0.3871 0.0066  0.0629  0.0201  142 TRP   C CZ3 
2163 C  CH2 . TRP   B 136 ? 0.2464 0.2277 0.3843 0.0066  0.0603  0.0181  142 TRP   C CH2 
2164 N  N   . LEU   B 137 ? 0.2523 0.2294 0.3449 0.0053  0.0561  0.0180  143 LEU   C N   
2165 C  CA  . LEU   B 137 ? 0.2540 0.2322 0.3527 0.0038  0.0534  0.0243  143 LEU   C CA  
2166 C  C   . LEU   B 137 ? 0.2854 0.2627 0.3780 0.0027  0.0537  0.0282  143 LEU   C C   
2167 O  O   . LEU   B 137 ? 0.2943 0.2730 0.3936 0.0011  0.0532  0.0334  143 LEU   C O   
2168 C  CB  . LEU   B 137 ? 0.2453 0.2225 0.3425 0.0034  0.0471  0.0248  143 LEU   C CB  
2169 C  CG  . LEU   B 137 ? 0.2462 0.2249 0.3516 0.0039  0.0464  0.0231  143 LEU   C CG  
2170 C  CD1 . LEU   B 137 ? 0.2496 0.2275 0.3511 0.0037  0.0408  0.0231  143 LEU   C CD1 
2171 C  CD2 . LEU   B 137 ? 0.2453 0.2268 0.3638 0.0032  0.0479  0.0276  143 LEU   C CD2 
2172 N  N   . ASP   B 138 ? 0.2906 0.2656 0.3709 0.0034  0.0543  0.0260  144 ASP   C N   
2173 C  CA  . ASP   B 138 ? 0.3154 0.2887 0.3888 0.0025  0.0546  0.0300  144 ASP   C CA  
2174 C  C   . ASP   B 138 ? 0.3655 0.3410 0.4416 0.0021  0.0615  0.0319  144 ASP   C C   
2175 O  O   . ASP   B 138 ? 0.3744 0.3487 0.4452 0.0011  0.0625  0.0357  144 ASP   C O   
2176 C  CB  . ASP   B 138 ? 0.3209 0.2913 0.3797 0.0037  0.0523  0.0276  144 ASP   C CB  
2177 C  CG  . ASP   B 138 ? 0.3490 0.3173 0.4043 0.0043  0.0456  0.0265  144 ASP   C CG  
2178 O  OD1 . ASP   B 138 ? 0.3450 0.3134 0.4074 0.0034  0.0426  0.0284  144 ASP   C OD1 
2179 O  OD2 . ASP   B 138 ? 0.3788 0.3459 0.4243 0.0057  0.0434  0.0238  144 ASP   C OD2 
2180 N  N   . GLU   B 139 ? 0.3925 0.3708 0.4768 0.0031  0.0667  0.0295  145 GLU   C N   
2181 C  CA  . GLU   B 139 ? 0.4516 0.4324 0.5389 0.0033  0.0743  0.0310  145 GLU   C CA  
2182 C  C   . GLU   B 139 ? 0.4945 0.4792 0.5978 0.0039  0.0788  0.0316  145 GLU   C C   
2183 O  O   . GLU   B 139 ? 0.4992 0.4845 0.6108 0.0041  0.0758  0.0309  145 GLU   C O   
2184 C  CB  . GLU   B 139 ? 0.5161 0.4952 0.5904 0.0050  0.0780  0.0256  145 GLU   C CB  
2185 C  CG  . GLU   B 139 ? 0.6205 0.5988 0.6952 0.0066  0.0783  0.0183  145 GLU   C CG  
2186 C  CD  . GLU   B 139 ? 0.7564 0.7322 0.8154 0.0074  0.0767  0.0128  145 GLU   C CD  
2187 O  OE1 . GLU   B 139 ? 0.7842 0.7594 0.8412 0.0085  0.0798  0.0062  145 GLU   C OE1 
2188 O  OE2 . GLU   B 139 ? 0.8153 0.7896 0.8643 0.0069  0.0721  0.0151  145 GLU   C OE2 
2189 N  N   . GLU   B 140 ? 0.5214 0.5089 0.6290 0.0044  0.0864  0.0330  146 GLU   C N   
2190 C  CA  . GLU   B 140 ? 0.5468 0.5384 0.6700 0.0057  0.0921  0.0337  146 GLU   C CA  
2191 C  C   . GLU   B 140 ? 0.5714 0.5669 0.7095 0.0040  0.0884  0.0402  146 GLU   C C   
2192 O  O   . GLU   B 140 ? 0.5913 0.5909 0.7368 0.0026  0.0908  0.0459  146 GLU   C O   
2193 C  CB  . GLU   B 140 ? 0.5793 0.5690 0.7039 0.0083  0.0947  0.0265  146 GLU   C CB  
2194 C  CG  . GLU   B 140 ? 0.6686 0.6612 0.8114 0.0097  0.0974  0.0277  146 GLU   C CG  
2195 C  CD  . GLU   B 140 ? 0.7525 0.7482 0.9044 0.0119  0.1071  0.0278  146 GLU   C CD  
2196 O  OE1 . GLU   B 140 ? 0.7766 0.7716 0.9373 0.0143  0.1110  0.0244  146 GLU   C OE1 
2197 O  OE2 . GLU   B 140 ? 0.7827 0.7814 0.9336 0.0112  0.1110  0.0316  146 GLU   C OE2 
2198 N  N1  . A1BPY C .   ? 0.3646 0.3286 0.4481 0.0089  0.0542  -0.0187 201 A1BPY A N1  
2199 N  N3  . A1BPY C .   ? 0.2508 0.2044 0.3844 0.0243  0.0473  0.0092  201 A1BPY A N3  
2200 C  C4  . A1BPY C .   ? 0.5490 0.4978 0.6683 0.0147  0.0807  -0.0354 201 A1BPY A C4  
2201 C  C5  . A1BPY C .   ? 0.5960 0.5408 0.7234 0.0146  0.0906  -0.0434 201 A1BPY A C5  
2202 C  C6  . A1BPY C .   ? 0.5899 0.5393 0.7150 0.0121  0.0960  -0.0490 201 A1BPY A C6  
2203 C  C7  . A1BPY C .   ? 0.5804 0.5380 0.6943 0.0098  0.0905  -0.0454 201 A1BPY A C7  
2204 C  C8  . A1BPY C .   ? 0.5372 0.4978 0.6433 0.0100  0.0805  -0.0372 201 A1BPY A C8  
2205 C  C10 . A1BPY C .   ? 0.3300 0.2783 0.4349 0.0134  0.0635  -0.0245 201 A1BPY A C10 
2206 C  C13 . A1BPY C .   ? 0.3101 0.2442 0.4245 0.0143  0.0602  -0.0216 201 A1BPY A C13 
2207 C  C15 . A1BPY C .   ? 0.2880 0.2319 0.4175 0.0223  0.0557  -0.0053 201 A1BPY A C15 
2208 C  C17 . A1BPY C .   ? 0.2986 0.2434 0.4351 0.0245  0.0617  -0.0076 201 A1BPY A C17 
2209 O  O1  . A1BPY C .   ? 0.2807 0.2250 0.4349 0.0287  0.0571  0.0074  201 A1BPY A O1  
2210 C  C16 . A1BPY C .   ? 0.2719 0.2190 0.4119 0.0255  0.0533  0.0043  201 A1BPY A C16 
2211 C  C14 . A1BPY C .   ? 0.2950 0.2302 0.4208 0.0189  0.0582  -0.0128 201 A1BPY A C14 
2212 C  C12 . A1BPY C .   ? 0.3103 0.2456 0.4299 0.0160  0.0662  -0.0244 201 A1BPY A C12 
2213 N  N2  . A1BPY C .   ? 0.3088 0.2520 0.4336 0.0202  0.0637  -0.0165 201 A1BPY A N2  
2214 C  C11 . A1BPY C .   ? 0.3115 0.2610 0.4302 0.0192  0.0626  -0.0165 201 A1BPY A C11 
2215 O  O   . A1BPY C .   ? 0.3010 0.2572 0.4250 0.0222  0.0612  -0.0102 201 A1BPY A O   
2216 C  C9  . A1BPY C .   ? 0.3571 0.3123 0.4550 0.0121  0.0615  -0.0231 201 A1BPY A C9  
2217 N  N   . A1BPY C .   ? 0.3508 0.3097 0.4394 0.0105  0.0544  -0.0189 201 A1BPY A N   
2218 C  C   . A1BPY C .   ? 0.3446 0.3022 0.4290 0.0103  0.0482  -0.0154 201 A1BPY A C   
2219 C  C2  . A1BPY C .   ? 0.4081 0.3667 0.5072 0.0115  0.0664  -0.0262 201 A1BPY A C2  
2220 C  C1  . A1BPY C .   ? 0.3819 0.3463 0.4713 0.0093  0.0612  -0.0230 201 A1BPY A C1  
2221 C  C3  . A1BPY C .   ? 0.4983 0.4545 0.6070 0.0124  0.0758  -0.0327 201 A1BPY A C3  
2222 CL CL1 . A1BPY C .   ? 0.6105 0.5746 0.7194 0.0053  0.0969  -0.0524 201 A1BPY A CL1 
2223 CL CL  . A1BPY C .   ? 0.6439 0.5775 0.7858 0.0172  0.0972  -0.0471 201 A1BPY A CL  
# 
