data_7HZF
# 
_entry.id   7HZF 
# 
_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   7HZF         pdb_00007hzf 10.2210/pdb7hzf/pdb 
WWPDB D_1001408123 ?            ?                   
# 
_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                        7HZF 
_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-[(5-chloro-1,2-thiazol-4-yl)di(fluoro)acetyl]piperidine-3-carboxamide' 323.747   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                     65.409    2   ?         ? ? ? 
4 water       nat water                                                                          18.015    381 ?         ? ? ? 
# 
_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-[(5-chloro-1,2-thiazol-4-yl)di(fluoro)acetyl]piperidine-3-carboxamide' A1BN7 
3 'ZINC ION'                                                                     ZN    
4 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 
A1BN7 non-polymer         . '(3S)-1-[(5-chloro-1,2-thiazol-4-yl)di(fluoro)acetyl]piperidine-3-carboxamide' ? 
'C11 H12 Cl F2 N3 O2 S' 323.747 
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 
GLN   'L-peptide linking' y GLUTAMINE                                                                      ? 'C5 H10 N2 O3' 
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                ? 'C5 H9 N O4' 147.129 
GLY   'peptide linking'   y GLYCINE                                                                        ? 'C2 H5 N O2' 75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                      ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                          ? 'H2 O' 18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                     ? 'C6 H13 N O2' 131.173 
LEU   'L-peptide linking' y LEUCINE                                                                        ? 'C6 H13 N O2' 131.173 
LYS   'L-peptide linking' y LYSINE                                                                         ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                     ? 'C5 H11 N O2 S' 
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                  ? 'C9 H11 N O2' 165.189 
PRO   'L-peptide linking' y PROLINE                                                                        ? 'C5 H9 N O2' 115.130 
SER   'L-peptide linking' y SERINE                                                                         ? 'C3 H7 N O3' 105.093 
THR   'L-peptide linking' y THREONINE                                                                      ? 'C4 H9 N O3' 119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                     ? 'C11 H12 N2 O2' 
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                       ? 'C9 H11 N O3' 181.189 
VAL   'L-peptide linking' y VALINE                                                                         ? 'C5 H11 N O2' 117.146 
ZN    non-polymer         . 'ZINC ION'                                                                     ? 'Zn 2' 65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 ?   ?   ?   C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BN7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BN7 
_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 A1BN7 1   201 201 A1BN7 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 2 A1BN7 1   201 201 A1BN7 LIG C . 
F 3 ZN    1   202 1   ZN    ZN  C . 
G 4 HOH   1   301 61  HOH   HOH A . 
G 4 HOH   2   302 156 HOH   HOH A . 
G 4 HOH   3   303 95  HOH   HOH A . 
G 4 HOH   4   304 65  HOH   HOH A . 
G 4 HOH   5   305 240 HOH   HOH A . 
G 4 HOH   6   306 243 HOH   HOH A . 
G 4 HOH   7   307 166 HOH   HOH A . 
G 4 HOH   8   308 6   HOH   HOH A . 
G 4 HOH   9   309 84  HOH   HOH A . 
G 4 HOH   10  310 58  HOH   HOH A . 
G 4 HOH   11  311 164 HOH   HOH A . 
G 4 HOH   12  312 25  HOH   HOH A . 
G 4 HOH   13  313 144 HOH   HOH A . 
G 4 HOH   14  314 109 HOH   HOH A . 
G 4 HOH   15  315 66  HOH   HOH A . 
G 4 HOH   16  316 93  HOH   HOH A . 
G 4 HOH   17  317 183 HOH   HOH A . 
G 4 HOH   18  318 24  HOH   HOH A . 
G 4 HOH   19  319 273 HOH   HOH A . 
G 4 HOH   20  320 22  HOH   HOH A . 
G 4 HOH   21  321 63  HOH   HOH A . 
G 4 HOH   22  322 171 HOH   HOH A . 
G 4 HOH   23  323 176 HOH   HOH A . 
G 4 HOH   24  324 34  HOH   HOH A . 
G 4 HOH   25  325 5   HOH   HOH A . 
G 4 HOH   26  326 103 HOH   HOH A . 
G 4 HOH   27  327 7   HOH   HOH A . 
G 4 HOH   28  328 59  HOH   HOH A . 
G 4 HOH   29  329 116 HOH   HOH A . 
G 4 HOH   30  330 262 HOH   HOH A . 
G 4 HOH   31  331 30  HOH   HOH A . 
G 4 HOH   32  332 140 HOH   HOH A . 
G 4 HOH   33  333 13  HOH   HOH A . 
G 4 HOH   34  334 242 HOH   HOH A . 
G 4 HOH   35  335 22  HOH   HOH A . 
G 4 HOH   36  336 102 HOH   HOH A . 
G 4 HOH   37  337 60  HOH   HOH A . 
G 4 HOH   38  338 76  HOH   HOH A . 
G 4 HOH   39  339 232 HOH   HOH A . 
G 4 HOH   40  340 190 HOH   HOH A . 
G 4 HOH   41  341 33  HOH   HOH A . 
G 4 HOH   42  342 70  HOH   HOH A . 
G 4 HOH   43  343 56  HOH   HOH A . 
G 4 HOH   44  344 71  HOH   HOH A . 
G 4 HOH   45  345 85  HOH   HOH A . 
G 4 HOH   46  346 17  HOH   HOH A . 
G 4 HOH   47  347 128 HOH   HOH A . 
G 4 HOH   48  348 72  HOH   HOH A . 
G 4 HOH   49  349 14  HOH   HOH A . 
G 4 HOH   50  350 66  HOH   HOH A . 
G 4 HOH   51  351 23  HOH   HOH A . 
G 4 HOH   52  352 10  HOH   HOH A . 
G 4 HOH   53  353 157 HOH   HOH A . 
G 4 HOH   54  354 79  HOH   HOH A . 
G 4 HOH   55  355 26  HOH   HOH A . 
G 4 HOH   56  356 247 HOH   HOH A . 
G 4 HOH   57  357 264 HOH   HOH A . 
G 4 HOH   58  358 45  HOH   HOH A . 
G 4 HOH   59  359 88  HOH   HOH A . 
G 4 HOH   60  360 49  HOH   HOH A . 
G 4 HOH   61  361 119 HOH   HOH A . 
G 4 HOH   62  362 56  HOH   HOH A . 
G 4 HOH   63  363 101 HOH   HOH A . 
G 4 HOH   64  364 48  HOH   HOH A . 
G 4 HOH   65  365 115 HOH   HOH A . 
G 4 HOH   66  366 152 HOH   HOH A . 
G 4 HOH   67  367 10  HOH   HOH A . 
G 4 HOH   68  368 27  HOH   HOH A . 
G 4 HOH   69  369 35  HOH   HOH A . 
G 4 HOH   70  370 42  HOH   HOH A . 
G 4 HOH   71  371 18  HOH   HOH A . 
G 4 HOH   72  372 89  HOH   HOH A . 
G 4 HOH   73  373 19  HOH   HOH A . 
G 4 HOH   74  374 3   HOH   HOH A . 
G 4 HOH   75  375 14  HOH   HOH A . 
G 4 HOH   76  376 115 HOH   HOH A . 
G 4 HOH   77  377 84  HOH   HOH A . 
G 4 HOH   78  378 53  HOH   HOH A . 
G 4 HOH   79  379 75  HOH   HOH A . 
G 4 HOH   80  380 149 HOH   HOH A . 
G 4 HOH   81  381 76  HOH   HOH A . 
G 4 HOH   82  382 119 HOH   HOH A . 
G 4 HOH   83  383 141 HOH   HOH A . 
G 4 HOH   84  384 204 HOH   HOH A . 
G 4 HOH   85  385 73  HOH   HOH A . 
G 4 HOH   86  386 235 HOH   HOH A . 
G 4 HOH   87  387 29  HOH   HOH A . 
G 4 HOH   88  388 133 HOH   HOH A . 
G 4 HOH   89  389 92  HOH   HOH A . 
G 4 HOH   90  390 268 HOH   HOH A . 
G 4 HOH   91  391 99  HOH   HOH A . 
G 4 HOH   92  392 53  HOH   HOH A . 
G 4 HOH   93  393 47  HOH   HOH A . 
G 4 HOH   94  394 214 HOH   HOH A . 
G 4 HOH   95  395 113 HOH   HOH A . 
G 4 HOH   96  396 12  HOH   HOH A . 
G 4 HOH   97  397 272 HOH   HOH A . 
G 4 HOH   98  398 4   HOH   HOH A . 
G 4 HOH   99  399 112 HOH   HOH A . 
G 4 HOH   100 400 107 HOH   HOH A . 
G 4 HOH   101 401 60  HOH   HOH A . 
G 4 HOH   102 402 257 HOH   HOH A . 
G 4 HOH   103 403 23  HOH   HOH A . 
G 4 HOH   104 404 197 HOH   HOH A . 
G 4 HOH   105 405 255 HOH   HOH A . 
G 4 HOH   106 406 168 HOH   HOH A . 
G 4 HOH   107 407 223 HOH   HOH A . 
G 4 HOH   108 408 114 HOH   HOH A . 
G 4 HOH   109 409 228 HOH   HOH A . 
G 4 HOH   110 410 26  HOH   HOH A . 
G 4 HOH   111 411 269 HOH   HOH A . 
G 4 HOH   112 412 157 HOH   HOH A . 
G 4 HOH   113 413 253 HOH   HOH A . 
G 4 HOH   114 414 35  HOH   HOH A . 
G 4 HOH   115 415 91  HOH   HOH A . 
G 4 HOH   116 416 96  HOH   HOH A . 
G 4 HOH   117 417 106 HOH   HOH A . 
G 4 HOH   118 418 150 HOH   HOH A . 
G 4 HOH   119 419 245 HOH   HOH A . 
G 4 HOH   120 420 142 HOH   HOH A . 
G 4 HOH   121 421 111 HOH   HOH A . 
G 4 HOH   122 422 19  HOH   HOH A . 
G 4 HOH   123 423 261 HOH   HOH A . 
G 4 HOH   124 424 147 HOH   HOH A . 
G 4 HOH   125 425 104 HOH   HOH A . 
G 4 HOH   126 426 55  HOH   HOH A . 
G 4 HOH   127 427 85  HOH   HOH A . 
G 4 HOH   128 428 49  HOH   HOH A . 
G 4 HOH   129 429 202 HOH   HOH A . 
G 4 HOH   130 430 125 HOH   HOH A . 
G 4 HOH   131 431 16  HOH   HOH A . 
G 4 HOH   132 432 100 HOH   HOH A . 
G 4 HOH   133 433 52  HOH   HOH A . 
G 4 HOH   134 434 12  HOH   HOH A . 
G 4 HOH   135 435 40  HOH   HOH A . 
G 4 HOH   136 436 209 HOH   HOH A . 
G 4 HOH   137 437 77  HOH   HOH A . 
G 4 HOH   138 438 21  HOH   HOH A . 
G 4 HOH   139 439 102 HOH   HOH A . 
G 4 HOH   140 440 36  HOH   HOH A . 
G 4 HOH   141 441 165 HOH   HOH A . 
G 4 HOH   142 442 231 HOH   HOH A . 
G 4 HOH   143 443 114 HOH   HOH A . 
G 4 HOH   144 444 127 HOH   HOH A . 
G 4 HOH   145 445 251 HOH   HOH A . 
G 4 HOH   146 446 208 HOH   HOH A . 
G 4 HOH   147 447 8   HOH   HOH A . 
G 4 HOH   148 448 151 HOH   HOH A . 
G 4 HOH   149 449 15  HOH   HOH A . 
G 4 HOH   150 450 129 HOH   HOH A . 
G 4 HOH   151 451 38  HOH   HOH A . 
G 4 HOH   152 452 151 HOH   HOH A . 
G 4 HOH   153 453 158 HOH   HOH A . 
G 4 HOH   154 454 145 HOH   HOH A . 
G 4 HOH   155 455 61  HOH   HOH A . 
G 4 HOH   156 456 82  HOH   HOH A . 
G 4 HOH   157 457 126 HOH   HOH A . 
G 4 HOH   158 458 108 HOH   HOH A . 
G 4 HOH   159 459 177 HOH   HOH A . 
G 4 HOH   160 460 201 HOH   HOH A . 
G 4 HOH   161 461 136 HOH   HOH A . 
G 4 HOH   162 462 130 HOH   HOH A . 
G 4 HOH   163 463 174 HOH   HOH A . 
G 4 HOH   164 464 154 HOH   HOH A . 
G 4 HOH   165 465 178 HOH   HOH A . 
G 4 HOH   166 466 154 HOH   HOH A . 
G 4 HOH   167 467 57  HOH   HOH A . 
G 4 HOH   168 468 59  HOH   HOH A . 
G 4 HOH   169 469 24  HOH   HOH A . 
G 4 HOH   170 470 181 HOH   HOH A . 
G 4 HOH   171 471 271 HOH   HOH A . 
G 4 HOH   172 472 166 HOH   HOH A . 
G 4 HOH   173 473 138 HOH   HOH A . 
G 4 HOH   174 474 132 HOH   HOH A . 
G 4 HOH   175 475 226 HOH   HOH A . 
G 4 HOH   176 476 168 HOH   HOH A . 
G 4 HOH   177 477 146 HOH   HOH A . 
G 4 HOH   178 478 187 HOH   HOH A . 
G 4 HOH   179 479 32  HOH   HOH A . 
G 4 HOH   180 480 167 HOH   HOH A . 
G 4 HOH   181 481 136 HOH   HOH A . 
G 4 HOH   182 482 63  HOH   HOH A . 
G 4 HOH   183 483 92  HOH   HOH A . 
G 4 HOH   184 484 219 HOH   HOH A . 
G 4 HOH   185 485 82  HOH   HOH A . 
G 4 HOH   186 486 222 HOH   HOH A . 
G 4 HOH   187 487 90  HOH   HOH A . 
G 4 HOH   188 488 101 HOH   HOH A . 
G 4 HOH   189 489 270 HOH   HOH A . 
G 4 HOH   190 490 161 HOH   HOH A . 
G 4 HOH   191 491 206 HOH   HOH A . 
G 4 HOH   192 492 99  HOH   HOH A . 
G 4 HOH   193 493 193 HOH   HOH A . 
G 4 HOH   194 494 182 HOH   HOH A . 
G 4 HOH   195 495 227 HOH   HOH A . 
H 4 HOH   1   301 42  HOH   HOH C . 
H 4 HOH   2   302 89  HOH   HOH C . 
H 4 HOH   3   303 161 HOH   HOH C . 
H 4 HOH   4   304 34  HOH   HOH C . 
H 4 HOH   5   305 174 HOH   HOH C . 
H 4 HOH   6   306 143 HOH   HOH C . 
H 4 HOH   7   307 123 HOH   HOH C . 
H 4 HOH   8   308 171 HOH   HOH C . 
H 4 HOH   9   309 110 HOH   HOH C . 
H 4 HOH   10  310 135 HOH   HOH C . 
H 4 HOH   11  311 250 HOH   HOH C . 
H 4 HOH   12  312 241 HOH   HOH C . 
H 4 HOH   13  313 64  HOH   HOH C . 
H 4 HOH   14  314 2   HOH   HOH C . 
H 4 HOH   15  315 8   HOH   HOH C . 
H 4 HOH   16  316 69  HOH   HOH C . 
H 4 HOH   17  317 33  HOH   HOH C . 
H 4 HOH   18  318 120 HOH   HOH C . 
H 4 HOH   19  319 103 HOH   HOH C . 
H 4 HOH   20  320 121 HOH   HOH C . 
H 4 HOH   21  321 32  HOH   HOH C . 
H 4 HOH   22  322 137 HOH   HOH C . 
H 4 HOH   23  323 91  HOH   HOH C . 
H 4 HOH   24  324 51  HOH   HOH C . 
H 4 HOH   25  325 50  HOH   HOH C . 
H 4 HOH   26  326 233 HOH   HOH C . 
H 4 HOH   27  327 43  HOH   HOH C . 
H 4 HOH   28  328 20  HOH   HOH C . 
H 4 HOH   29  329 236 HOH   HOH C . 
H 4 HOH   30  330 28  HOH   HOH C . 
H 4 HOH   31  331 6   HOH   HOH C . 
H 4 HOH   32  332 80  HOH   HOH C . 
H 4 HOH   33  333 30  HOH   HOH C . 
H 4 HOH   34  334 195 HOH   HOH C . 
H 4 HOH   35  335 155 HOH   HOH C . 
H 4 HOH   36  336 259 HOH   HOH C . 
H 4 HOH   37  337 65  HOH   HOH C . 
H 4 HOH   38  338 170 HOH   HOH C . 
H 4 HOH   39  339 64  HOH   HOH C . 
H 4 HOH   40  340 78  HOH   HOH C . 
H 4 HOH   41  341 126 HOH   HOH C . 
H 4 HOH   42  342 11  HOH   HOH C . 
H 4 HOH   43  343 130 HOH   HOH C . 
H 4 HOH   44  344 13  HOH   HOH C . 
H 4 HOH   45  345 98  HOH   HOH C . 
H 4 HOH   46  346 248 HOH   HOH C . 
H 4 HOH   47  347 138 HOH   HOH C . 
H 4 HOH   48  348 122 HOH   HOH C . 
H 4 HOH   49  349 238 HOH   HOH C . 
H 4 HOH   50  350 237 HOH   HOH C . 
H 4 HOH   51  351 70  HOH   HOH C . 
H 4 HOH   52  352 110 HOH   HOH C . 
H 4 HOH   53  353 15  HOH   HOH C . 
H 4 HOH   54  354 46  HOH   HOH C . 
H 4 HOH   55  355 244 HOH   HOH C . 
H 4 HOH   56  356 124 HOH   HOH C . 
H 4 HOH   57  357 18  HOH   HOH C . 
H 4 HOH   58  358 73  HOH   HOH C . 
H 4 HOH   59  359 98  HOH   HOH C . 
H 4 HOH   60  360 39  HOH   HOH C . 
H 4 HOH   61  361 38  HOH   HOH C . 
H 4 HOH   62  362 210 HOH   HOH C . 
H 4 HOH   63  363 4   HOH   HOH C . 
H 4 HOH   64  364 39  HOH   HOH C . 
H 4 HOH   65  365 252 HOH   HOH C . 
H 4 HOH   66  366 74  HOH   HOH C . 
H 4 HOH   67  367 256 HOH   HOH C . 
H 4 HOH   68  368 67  HOH   HOH C . 
H 4 HOH   69  369 249 HOH   HOH C . 
H 4 HOH   70  370 29  HOH   HOH C . 
H 4 HOH   71  371 78  HOH   HOH C . 
H 4 HOH   72  372 109 HOH   HOH C . 
H 4 HOH   73  373 246 HOH   HOH C . 
H 4 HOH   74  374 169 HOH   HOH C . 
H 4 HOH   75  375 205 HOH   HOH C . 
H 4 HOH   76  376 80  HOH   HOH C . 
H 4 HOH   77  377 150 HOH   HOH C . 
H 4 HOH   78  378 7   HOH   HOH C . 
H 4 HOH   79  379 87  HOH   HOH C . 
H 4 HOH   80  380 260 HOH   HOH C . 
H 4 HOH   81  381 79  HOH   HOH C . 
H 4 HOH   82  382 86  HOH   HOH C . 
H 4 HOH   83  383 37  HOH   HOH C . 
H 4 HOH   84  384 148 HOH   HOH C . 
H 4 HOH   85  385 117 HOH   HOH C . 
H 4 HOH   86  386 54  HOH   HOH C . 
H 4 HOH   87  387 71  HOH   HOH C . 
H 4 HOH   88  388 62  HOH   HOH C . 
H 4 HOH   89  389 83  HOH   HOH C . 
H 4 HOH   90  390 97  HOH   HOH C . 
H 4 HOH   91  391 11  HOH   HOH C . 
H 4 HOH   92  392 194 HOH   HOH C . 
H 4 HOH   93  393 9   HOH   HOH C . 
H 4 HOH   94  394 230 HOH   HOH C . 
H 4 HOH   95  395 135 HOH   HOH C . 
H 4 HOH   96  396 267 HOH   HOH C . 
H 4 HOH   97  397 17  HOH   HOH C . 
H 4 HOH   98  398 148 HOH   HOH C . 
H 4 HOH   99  399 50  HOH   HOH C . 
H 4 HOH   100 400 1   HOH   HOH C . 
H 4 HOH   101 401 37  HOH   HOH C . 
H 4 HOH   102 402 83  HOH   HOH C . 
H 4 HOH   103 403 140 HOH   HOH C . 
H 4 HOH   104 404 127 HOH   HOH C . 
H 4 HOH   105 405 144 HOH   HOH C . 
H 4 HOH   106 406 44  HOH   HOH C . 
H 4 HOH   107 407 31  HOH   HOH C . 
H 4 HOH   108 408 229 HOH   HOH C . 
H 4 HOH   109 409 31  HOH   HOH C . 
H 4 HOH   110 410 175 HOH   HOH C . 
H 4 HOH   111 411 149 HOH   HOH C . 
H 4 HOH   112 412 234 HOH   HOH C . 
H 4 HOH   113 413 120 HOH   HOH C . 
H 4 HOH   114 414 44  HOH   HOH C . 
H 4 HOH   115 415 41  HOH   HOH C . 
H 4 HOH   116 416 124 HOH   HOH C . 
H 4 HOH   117 417 81  HOH   HOH C . 
H 4 HOH   118 418 54  HOH   HOH C . 
H 4 HOH   119 419 68  HOH   HOH C . 
H 4 HOH   120 420 45  HOH   HOH C . 
H 4 HOH   121 421 57  HOH   HOH C . 
H 4 HOH   122 422 48  HOH   HOH C . 
H 4 HOH   123 423 266 HOH   HOH C . 
H 4 HOH   124 424 137 HOH   HOH C . 
H 4 HOH   125 425 146 HOH   HOH C . 
H 4 HOH   126 426 117 HOH   HOH C . 
H 4 HOH   127 427 108 HOH   HOH C . 
H 4 HOH   128 428 40  HOH   HOH C . 
H 4 HOH   129 429 3   HOH   HOH C . 
H 4 HOH   130 430 263 HOH   HOH C . 
H 4 HOH   131 431 41  HOH   HOH C . 
H 4 HOH   132 432 52  HOH   HOH C . 
H 4 HOH   133 433 5   HOH   HOH C . 
H 4 HOH   134 434 254 HOH   HOH C . 
H 4 HOH   135 435 16  HOH   HOH C . 
H 4 HOH   136 436 134 HOH   HOH C . 
H 4 HOH   137 437 47  HOH   HOH C . 
H 4 HOH   138 438 95  HOH   HOH C . 
H 4 HOH   139 439 20  HOH   HOH C . 
H 4 HOH   140 440 200 HOH   HOH C . 
H 4 HOH   141 441 164 HOH   HOH C . 
H 4 HOH   142 442 107 HOH   HOH C . 
H 4 HOH   143 443 90  HOH   HOH C . 
H 4 HOH   144 444 118 HOH   HOH C . 
H 4 HOH   145 445 105 HOH   HOH C . 
H 4 HOH   146 446 152 HOH   HOH C . 
H 4 HOH   147 447 165 HOH   HOH C . 
H 4 HOH   148 448 131 HOH   HOH C . 
H 4 HOH   149 449 43  HOH   HOH C . 
H 4 HOH   150 450 139 HOH   HOH C . 
H 4 HOH   151 451 132 HOH   HOH C . 
H 4 HOH   152 452 27  HOH   HOH C . 
H 4 HOH   153 453 118 HOH   HOH C . 
H 4 HOH   154 454 185 HOH   HOH C . 
H 4 HOH   155 455 104 HOH   HOH C . 
H 4 HOH   156 456 116 HOH   HOH C . 
H 4 HOH   157 457 72  HOH   HOH C . 
H 4 HOH   158 458 9   HOH   HOH C . 
H 4 HOH   159 459 198 HOH   HOH C . 
H 4 HOH   160 460 153 HOH   HOH C . 
H 4 HOH   161 461 162 HOH   HOH C . 
H 4 HOH   162 462 239 HOH   HOH C . 
H 4 HOH   163 463 160 HOH   HOH C . 
H 4 HOH   164 464 93  HOH   HOH C . 
H 4 HOH   165 465 74  HOH   HOH C . 
H 4 HOH   166 466 188 HOH   HOH C . 
H 4 HOH   167 467 142 HOH   HOH C . 
H 4 HOH   168 468 159 HOH   HOH C . 
H 4 HOH   169 469 123 HOH   HOH C . 
H 4 HOH   170 470 199 HOH   HOH C . 
H 4 HOH   171 471 176 HOH   HOH C . 
H 4 HOH   172 472 169 HOH   HOH C . 
H 4 HOH   173 473 125 HOH   HOH C . 
H 4 HOH   174 474 105 HOH   HOH C . 
H 4 HOH   175 475 172 HOH   HOH C . 
H 4 HOH   176 476 25  HOH   HOH C . 
H 4 HOH   177 477 218 HOH   HOH C . 
H 4 HOH   178 478 196 HOH   HOH C . 
H 4 HOH   179 479 141 HOH   HOH C . 
H 4 HOH   180 480 211 HOH   HOH C . 
H 4 HOH   181 481 203 HOH   HOH C . 
H 4 HOH   182 482 189 HOH   HOH C . 
H 4 HOH   183 483 207 HOH   HOH C . 
H 4 HOH   184 484 163 HOH   HOH C . 
H 4 HOH   185 485 173 HOH   HOH C . 
H 4 HOH   186 486 155 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           7HZF 
_cell.length_a           72.759 
_cell.length_b           61.736 
_cell.length_c           65.666 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.94 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HZF 
_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          7HZF 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.32 
_exptl_crystal.density_percent_sol   46.91 
_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   2024-12-13 
_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                     7HZF 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.05 
_reflns.d_resolution_high            1.54 
_reflns.number_obs                   42755 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.167 
_reflns.pdbx_netI_over_sigmaI        7.2 
_reflns.pdbx_redundancy              6.8 
_reflns.pdbx_Rrim_I_all              0.181 
_reflns.pdbx_Rpim_I_all              0.069 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     291156 
_reflns.pdbx_chi_squared             0.89 
_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                  1.54 
_reflns_shell.d_res_low                   1.63 
_reflns_shell.number_measured_all         36917 
_reflns_shell.number_unique_obs           6222 
_reflns_shell.Rmerge_I_obs                1.743 
_reflns_shell.pdbx_chi_squared            0.78 
_reflns_shell.pdbx_redundancy             5.9 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.2 
_reflns_shell.pdbx_Rrim_I_all             1.913 
_reflns_shell.pdbx_Rpim_I_all             0.775 
_reflns_shell.pdbx_CC_half                0.407 
_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                                 7HZF 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     42674 
_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                             47.05 
_refine.ls_d_res_high                            1.543 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_R_factor_obs                          0.1837 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1825 
_refine.ls_R_factor_R_free                       0.2075 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.940 
_refine.ls_number_reflns_R_free                  2109 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.B_iso_mean                               20.78 
_refine.aniso_B[1][1]                            -0.09130 
_refine.aniso_B[2][2]                            0.87900 
_refine.aniso_B[3][3]                            -0.78760 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.42800 
_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             0.079 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.078 
_refine.pdbx_overall_SU_R_Blow_DPI               0.086 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.083 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HZF 
_refine_analyze.Luzzati_coordinate_error_obs    0.19 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             381 
_refine_hist.number_atoms_total               2571 
_refine_hist.d_res_high                       1.543 
_refine_hist.d_res_low                        47.05 
# 
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                  0.010 ? 2.00  2250 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.98  ? 2.00  3068 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  752  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  404  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2250 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.25  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           13.95 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  276  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  2061 '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                       1.54 
_refine_ls_shell.d_res_low                        1.55 
_refine_ls_shell.number_reflns_R_work             817 
_refine_ls_shell.R_factor_R_work                  0.2984 
_refine_ls_shell.percent_reflns_obs               94.82 
_refine_ls_shell.R_factor_R_free                  0.3836 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.33 
_refine_ls_shell.number_reflns_R_free             37 
_refine_ls_shell.number_reflns_all                854 
_refine_ls_shell.R_factor_all                     0.3020 
# 
_struct.entry_id                  7HZF 
_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-0036379-001 (A71EV2A-x4541)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HZF 
_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 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_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 7HZF A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HZF 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 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? ASP A 138 ? LEU A 140 ASP A 144 5 ? 5 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.361 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.122 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.5 ? 
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_555 105.3 ? 
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_555 117.2 ? 
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_555 109.1 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 101.6 ? 
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_555 113.0 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.4 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.5 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.3 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 108.4 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 99.6  ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 115.3 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N VAL B 26  ? N VAL C 32  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                   7HZF 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O A HOH 304 ? ? O A HOH 312 ? ? 1.28 
2  1 O A HOH 346 ? ? O A HOH 374 ? ? 1.44 
3  1 O C HOH 347 ? ? O C HOH 445 ? ? 1.54 
4  1 O C HOH 301 ? ? O C HOH 334 ? ? 1.64 
5  1 O A HOH 367 ? ? O A HOH 374 ? ? 1.66 
6  1 O A HOH 371 ? ? O A HOH 398 ? ? 1.83 
7  1 O C HOH 309 ? ? O C HOH 424 ? ? 1.99 
8  1 O C HOH 309 ? ? O C HOH 354 ? ? 2.09 
9  1 O A HOH 370 ? ? O A HOH 417 ? ? 2.11 
10 1 O A HOH 341 ? ? O A HOH 430 ? ? 2.16 
# 
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 19.6450 6.7434   18.3679 -0.0192 -0.0279 0.0006  -0.0033 0.0113 0.0019  0.4756 1.0499 0.3479 
-0.3240 -0.0689 -0.0518 -0.0084 -0.0000 0.0285 0.0374 0.0143 0.0542  0.0290 0.0257  -0.0059 
'X-RAY DIFFRACTION' 2 ? refined 15.1980 -23.9552 14.1953 -0.0167 -0.0260 -0.0021 0.0002  0.0043 -0.0019 0.4722 0.9020 0.4138 
0.3087  0.0110  0.0948  -0.0212 0.0172  0.0284 0.0103 0.0308 -0.0398 0.0010 -0.0144 -0.0096 
# 
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|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       495 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.51 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 146 ? A GLU 140 
2  1 Y 1 A ALA 147 ? A ALA 141 
3  1 Y 1 A MET 148 ? A MET 142 
4  1 Y 1 A GLU 149 ? A GLU 143 
5  1 Y 1 A GLN 150 ? A GLN 144 
6  1 Y 1 C GLU 146 ? B GLU 140 
7  1 Y 1 C ALA 147 ? B ALA 141 
8  1 Y 1 C MET 148 ? B MET 142 
9  1 Y 1 C GLU 149 ? B GLU 143 
10 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BN7 N1   N  N N 1   
A1BN7 C4   C  N N 2   
A1BN7 C5   C  N N 3   
A1BN7 C6   C  N N 4   
A1BN7 C7   C  Y N 5   
A1BN7 C8   C  Y N 6   
A1BN7 C10  C  N N 7   
A1BN7 CL   CL N N 8   
A1BN7 C9   C  Y N 9   
A1BN7 S    S  Y N 10  
A1BN7 N2   N  Y N 11  
A1BN7 F    F  N N 12  
A1BN7 F1   F  N N 13  
A1BN7 O1   O  N N 14  
A1BN7 C3   C  N N 15  
A1BN7 C2   C  N N 16  
A1BN7 C1   C  N S 17  
A1BN7 C    C  N N 18  
A1BN7 O    O  N N 19  
A1BN7 N    N  N N 20  
A1BN7 H8   H  N N 21  
A1BN7 H7   H  N N 22  
A1BN7 H9   H  N N 23  
A1BN7 H11  H  N N 24  
A1BN7 H10  H  N N 25  
A1BN7 H6   H  N N 26  
A1BN7 H5   H  N N 27  
A1BN7 H4   H  N N 28  
A1BN7 H3   H  N N 29  
A1BN7 H    H  N N 30  
A1BN7 H2   H  N N 31  
A1BN7 H1   H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CYS   N    N  N N 106 
CYS   CA   C  N R 107 
CYS   C    C  N N 108 
CYS   O    O  N N 109 
CYS   CB   C  N N 110 
CYS   SG   S  N N 111 
CYS   OXT  O  N N 112 
CYS   H    H  N N 113 
CYS   H2   H  N N 114 
CYS   HA   H  N N 115 
CYS   HB2  H  N N 116 
CYS   HB3  H  N N 117 
CYS   HG   H  N N 118 
CYS   HXT  H  N N 119 
GLN   N    N  N N 120 
GLN   CA   C  N S 121 
GLN   C    C  N N 122 
GLN   O    O  N N 123 
GLN   CB   C  N N 124 
GLN   CG   C  N N 125 
GLN   CD   C  N N 126 
GLN   OE1  O  N N 127 
GLN   NE2  N  N N 128 
GLN   OXT  O  N N 129 
GLN   H    H  N N 130 
GLN   H2   H  N N 131 
GLN   HA   H  N N 132 
GLN   HB2  H  N N 133 
GLN   HB3  H  N N 134 
GLN   HG2  H  N N 135 
GLN   HG3  H  N N 136 
GLN   HE21 H  N N 137 
GLN   HE22 H  N N 138 
GLN   HXT  H  N N 139 
GLU   N    N  N N 140 
GLU   CA   C  N S 141 
GLU   C    C  N N 142 
GLU   O    O  N N 143 
GLU   CB   C  N N 144 
GLU   CG   C  N N 145 
GLU   CD   C  N N 146 
GLU   OE1  O  N N 147 
GLU   OE2  O  N N 148 
GLU   OXT  O  N N 149 
GLU   H    H  N N 150 
GLU   H2   H  N N 151 
GLU   HA   H  N N 152 
GLU   HB2  H  N N 153 
GLU   HB3  H  N N 154 
GLU   HG2  H  N N 155 
GLU   HG3  H  N N 156 
GLU   HE2  H  N N 157 
GLU   HXT  H  N N 158 
GLY   N    N  N N 159 
GLY   CA   C  N N 160 
GLY   C    C  N N 161 
GLY   O    O  N N 162 
GLY   OXT  O  N N 163 
GLY   H    H  N N 164 
GLY   H2   H  N N 165 
GLY   HA2  H  N N 166 
GLY   HA3  H  N N 167 
GLY   HXT  H  N N 168 
HIS   N    N  N N 169 
HIS   CA   C  N S 170 
HIS   C    C  N N 171 
HIS   O    O  N N 172 
HIS   CB   C  N N 173 
HIS   CG   C  Y N 174 
HIS   ND1  N  Y N 175 
HIS   CD2  C  Y N 176 
HIS   CE1  C  Y N 177 
HIS   NE2  N  Y N 178 
HIS   OXT  O  N N 179 
HIS   H    H  N N 180 
HIS   H2   H  N N 181 
HIS   HA   H  N N 182 
HIS   HB2  H  N N 183 
HIS   HB3  H  N N 184 
HIS   HD1  H  N N 185 
HIS   HD2  H  N N 186 
HIS   HE1  H  N N 187 
HIS   HE2  H  N N 188 
HIS   HXT  H  N N 189 
HOH   O    O  N N 190 
HOH   H1   H  N N 191 
HOH   H2   H  N N 192 
ILE   N    N  N N 193 
ILE   CA   C  N S 194 
ILE   C    C  N N 195 
ILE   O    O  N N 196 
ILE   CB   C  N S 197 
ILE   CG1  C  N N 198 
ILE   CG2  C  N N 199 
ILE   CD1  C  N N 200 
ILE   OXT  O  N N 201 
ILE   H    H  N N 202 
ILE   H2   H  N N 203 
ILE   HA   H  N N 204 
ILE   HB   H  N N 205 
ILE   HG12 H  N N 206 
ILE   HG13 H  N N 207 
ILE   HG21 H  N N 208 
ILE   HG22 H  N N 209 
ILE   HG23 H  N N 210 
ILE   HD11 H  N N 211 
ILE   HD12 H  N N 212 
ILE   HD13 H  N N 213 
ILE   HXT  H  N N 214 
LEU   N    N  N N 215 
LEU   CA   C  N S 216 
LEU   C    C  N N 217 
LEU   O    O  N N 218 
LEU   CB   C  N N 219 
LEU   CG   C  N N 220 
LEU   CD1  C  N N 221 
LEU   CD2  C  N N 222 
LEU   OXT  O  N N 223 
LEU   H    H  N N 224 
LEU   H2   H  N N 225 
LEU   HA   H  N N 226 
LEU   HB2  H  N N 227 
LEU   HB3  H  N N 228 
LEU   HG   H  N N 229 
LEU   HD11 H  N N 230 
LEU   HD12 H  N N 231 
LEU   HD13 H  N N 232 
LEU   HD21 H  N N 233 
LEU   HD22 H  N N 234 
LEU   HD23 H  N N 235 
LEU   HXT  H  N N 236 
LYS   N    N  N N 237 
LYS   CA   C  N S 238 
LYS   C    C  N N 239 
LYS   O    O  N N 240 
LYS   CB   C  N N 241 
LYS   CG   C  N N 242 
LYS   CD   C  N N 243 
LYS   CE   C  N N 244 
LYS   NZ   N  N N 245 
LYS   OXT  O  N N 246 
LYS   H    H  N N 247 
LYS   H2   H  N N 248 
LYS   HA   H  N N 249 
LYS   HB2  H  N N 250 
LYS   HB3  H  N N 251 
LYS   HG2  H  N N 252 
LYS   HG3  H  N N 253 
LYS   HD2  H  N N 254 
LYS   HD3  H  N N 255 
LYS   HE2  H  N N 256 
LYS   HE3  H  N N 257 
LYS   HZ1  H  N N 258 
LYS   HZ2  H  N N 259 
LYS   HZ3  H  N N 260 
LYS   HXT  H  N N 261 
MET   N    N  N N 262 
MET   CA   C  N S 263 
MET   C    C  N N 264 
MET   O    O  N N 265 
MET   CB   C  N N 266 
MET   CG   C  N N 267 
MET   SD   S  N N 268 
MET   CE   C  N N 269 
MET   OXT  O  N N 270 
MET   H    H  N N 271 
MET   H2   H  N N 272 
MET   HA   H  N N 273 
MET   HB2  H  N N 274 
MET   HB3  H  N N 275 
MET   HG2  H  N N 276 
MET   HG3  H  N N 277 
MET   HE1  H  N N 278 
MET   HE2  H  N N 279 
MET   HE3  H  N N 280 
MET   HXT  H  N N 281 
PHE   N    N  N N 282 
PHE   CA   C  N S 283 
PHE   C    C  N N 284 
PHE   O    O  N N 285 
PHE   CB   C  N N 286 
PHE   CG   C  Y N 287 
PHE   CD1  C  Y N 288 
PHE   CD2  C  Y N 289 
PHE   CE1  C  Y N 290 
PHE   CE2  C  Y N 291 
PHE   CZ   C  Y N 292 
PHE   OXT  O  N N 293 
PHE   H    H  N N 294 
PHE   H2   H  N N 295 
PHE   HA   H  N N 296 
PHE   HB2  H  N N 297 
PHE   HB3  H  N N 298 
PHE   HD1  H  N N 299 
PHE   HD2  H  N N 300 
PHE   HE1  H  N N 301 
PHE   HE2  H  N N 302 
PHE   HZ   H  N N 303 
PHE   HXT  H  N N 304 
PRO   N    N  N N 305 
PRO   CA   C  N S 306 
PRO   C    C  N N 307 
PRO   O    O  N N 308 
PRO   CB   C  N N 309 
PRO   CG   C  N N 310 
PRO   CD   C  N N 311 
PRO   OXT  O  N N 312 
PRO   H    H  N N 313 
PRO   HA   H  N N 314 
PRO   HB2  H  N N 315 
PRO   HB3  H  N N 316 
PRO   HG2  H  N N 317 
PRO   HG3  H  N N 318 
PRO   HD2  H  N N 319 
PRO   HD3  H  N N 320 
PRO   HXT  H  N N 321 
SER   N    N  N N 322 
SER   CA   C  N S 323 
SER   C    C  N N 324 
SER   O    O  N N 325 
SER   CB   C  N N 326 
SER   OG   O  N N 327 
SER   OXT  O  N N 328 
SER   H    H  N N 329 
SER   H2   H  N N 330 
SER   HA   H  N N 331 
SER   HB2  H  N N 332 
SER   HB3  H  N N 333 
SER   HG   H  N N 334 
SER   HXT  H  N N 335 
THR   N    N  N N 336 
THR   CA   C  N S 337 
THR   C    C  N N 338 
THR   O    O  N N 339 
THR   CB   C  N R 340 
THR   OG1  O  N N 341 
THR   CG2  C  N N 342 
THR   OXT  O  N N 343 
THR   H    H  N N 344 
THR   H2   H  N N 345 
THR   HA   H  N N 346 
THR   HB   H  N N 347 
THR   HG1  H  N N 348 
THR   HG21 H  N N 349 
THR   HG22 H  N N 350 
THR   HG23 H  N N 351 
THR   HXT  H  N N 352 
TRP   N    N  N N 353 
TRP   CA   C  N S 354 
TRP   C    C  N N 355 
TRP   O    O  N N 356 
TRP   CB   C  N N 357 
TRP   CG   C  Y N 358 
TRP   CD1  C  Y N 359 
TRP   CD2  C  Y N 360 
TRP   NE1  N  Y N 361 
TRP   CE2  C  Y N 362 
TRP   CE3  C  Y N 363 
TRP   CZ2  C  Y N 364 
TRP   CZ3  C  Y N 365 
TRP   CH2  C  Y N 366 
TRP   OXT  O  N N 367 
TRP   H    H  N N 368 
TRP   H2   H  N N 369 
TRP   HA   H  N N 370 
TRP   HB2  H  N N 371 
TRP   HB3  H  N N 372 
TRP   HD1  H  N N 373 
TRP   HE1  H  N N 374 
TRP   HE3  H  N N 375 
TRP   HZ2  H  N N 376 
TRP   HZ3  H  N N 377 
TRP   HH2  H  N N 378 
TRP   HXT  H  N N 379 
TYR   N    N  N N 380 
TYR   CA   C  N S 381 
TYR   C    C  N N 382 
TYR   O    O  N N 383 
TYR   CB   C  N N 384 
TYR   CG   C  Y N 385 
TYR   CD1  C  Y N 386 
TYR   CD2  C  Y N 387 
TYR   CE1  C  Y N 388 
TYR   CE2  C  Y N 389 
TYR   CZ   C  Y N 390 
TYR   OH   O  N N 391 
TYR   OXT  O  N N 392 
TYR   H    H  N N 393 
TYR   H2   H  N N 394 
TYR   HA   H  N N 395 
TYR   HB2  H  N N 396 
TYR   HB3  H  N N 397 
TYR   HD1  H  N N 398 
TYR   HD2  H  N N 399 
TYR   HE1  H  N N 400 
TYR   HE2  H  N N 401 
TYR   HH   H  N N 402 
TYR   HXT  H  N N 403 
VAL   N    N  N N 404 
VAL   CA   C  N S 405 
VAL   C    C  N N 406 
VAL   O    O  N N 407 
VAL   CB   C  N N 408 
VAL   CG1  C  N N 409 
VAL   CG2  C  N N 410 
VAL   OXT  O  N N 411 
VAL   H    H  N N 412 
VAL   H2   H  N N 413 
VAL   HA   H  N N 414 
VAL   HB   H  N N 415 
VAL   HG11 H  N N 416 
VAL   HG12 H  N N 417 
VAL   HG13 H  N N 418 
VAL   HG21 H  N N 419 
VAL   HG22 H  N N 420 
VAL   HG23 H  N N 421 
VAL   HXT  H  N N 422 
ZN    ZN   ZN N N 423 
# 
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 
A1BN7 N   C    sing N N 1   
A1BN7 O   C    doub N N 2   
A1BN7 C   C1   sing N N 3   
A1BN7 C1  C2   sing N N 4   
A1BN7 C2  C3   sing N N 5   
A1BN7 C3  C4   sing N N 6   
A1BN7 C4  N1   sing N N 7   
A1BN7 N1  C5   sing N N 8   
A1BN7 O1  C5   doub N N 9   
A1BN7 C5  C6   sing N N 10  
A1BN7 F   C6   sing N N 11  
A1BN7 F1  C6   sing N N 12  
A1BN7 C6  C7   sing N N 13  
A1BN7 C7  C8   sing Y N 14  
A1BN7 C8  N2   doub Y N 15  
A1BN7 N2  S    sing Y N 16  
A1BN7 S   C9   sing Y N 17  
A1BN7 C7  C9   doub Y N 18  
A1BN7 C9  CL   sing N N 19  
A1BN7 C10 N1   sing N N 20  
A1BN7 C1  C10  sing N N 21  
A1BN7 C4  H8   sing N N 22  
A1BN7 C4  H7   sing N N 23  
A1BN7 C8  H9   sing N N 24  
A1BN7 C10 H11  sing N N 25  
A1BN7 C10 H10  sing N N 26  
A1BN7 C3  H6   sing N N 27  
A1BN7 C3  H5   sing N N 28  
A1BN7 C2  H4   sing N N 29  
A1BN7 C2  H3   sing N N 30  
A1BN7 C1  H    sing N N 31  
A1BN7 N   H2   sing N N 32  
A1BN7 N   H1   sing N N 33  
ALA   N   CA   sing N N 34  
ALA   N   H    sing N N 35  
ALA   N   H2   sing N N 36  
ALA   CA  C    sing N N 37  
ALA   CA  CB   sing N N 38  
ALA   CA  HA   sing N N 39  
ALA   C   O    doub N N 40  
ALA   C   OXT  sing N N 41  
ALA   CB  HB1  sing N N 42  
ALA   CB  HB2  sing N N 43  
ALA   CB  HB3  sing N N 44  
ALA   OXT HXT  sing N N 45  
ARG   N   CA   sing N N 46  
ARG   N   H    sing N N 47  
ARG   N   H2   sing N N 48  
ARG   CA  C    sing N N 49  
ARG   CA  CB   sing N N 50  
ARG   CA  HA   sing N N 51  
ARG   C   O    doub N N 52  
ARG   C   OXT  sing N N 53  
ARG   CB  CG   sing N N 54  
ARG   CB  HB2  sing N N 55  
ARG   CB  HB3  sing N N 56  
ARG   CG  CD   sing N N 57  
ARG   CG  HG2  sing N N 58  
ARG   CG  HG3  sing N N 59  
ARG   CD  NE   sing N N 60  
ARG   CD  HD2  sing N N 61  
ARG   CD  HD3  sing N N 62  
ARG   NE  CZ   sing N N 63  
ARG   NE  HE   sing N N 64  
ARG   CZ  NH1  sing N N 65  
ARG   CZ  NH2  doub N N 66  
ARG   NH1 HH11 sing N N 67  
ARG   NH1 HH12 sing N N 68  
ARG   NH2 HH21 sing N N 69  
ARG   NH2 HH22 sing N N 70  
ARG   OXT HXT  sing N N 71  
ASN   N   CA   sing N N 72  
ASN   N   H    sing N N 73  
ASN   N   H2   sing N N 74  
ASN   CA  C    sing N N 75  
ASN   CA  CB   sing N N 76  
ASN   CA  HA   sing N N 77  
ASN   C   O    doub N N 78  
ASN   C   OXT  sing N N 79  
ASN   CB  CG   sing N N 80  
ASN   CB  HB2  sing N N 81  
ASN   CB  HB3  sing N N 82  
ASN   CG  OD1  doub N N 83  
ASN   CG  ND2  sing N N 84  
ASN   ND2 HD21 sing N N 85  
ASN   ND2 HD22 sing N N 86  
ASN   OXT HXT  sing N N 87  
ASP   N   CA   sing N N 88  
ASP   N   H    sing N N 89  
ASP   N   H2   sing N N 90  
ASP   CA  C    sing N N 91  
ASP   CA  CB   sing N N 92  
ASP   CA  HA   sing N N 93  
ASP   C   O    doub N N 94  
ASP   C   OXT  sing N N 95  
ASP   CB  CG   sing N N 96  
ASP   CB  HB2  sing N N 97  
ASP   CB  HB3  sing N N 98  
ASP   CG  OD1  doub N N 99  
ASP   CG  OD2  sing N N 100 
ASP   OD2 HD2  sing N N 101 
ASP   OXT HXT  sing N N 102 
CYS   N   CA   sing N N 103 
CYS   N   H    sing N N 104 
CYS   N   H2   sing N N 105 
CYS   CA  C    sing N N 106 
CYS   CA  CB   sing N N 107 
CYS   CA  HA   sing N N 108 
CYS   C   O    doub N N 109 
CYS   C   OXT  sing N N 110 
CYS   CB  SG   sing N N 111 
CYS   CB  HB2  sing N N 112 
CYS   CB  HB3  sing N N 113 
CYS   SG  HG   sing N N 114 
CYS   OXT HXT  sing N N 115 
GLN   N   CA   sing N N 116 
GLN   N   H    sing N N 117 
GLN   N   H2   sing N N 118 
GLN   CA  C    sing N N 119 
GLN   CA  CB   sing N N 120 
GLN   CA  HA   sing N N 121 
GLN   C   O    doub N N 122 
GLN   C   OXT  sing N N 123 
GLN   CB  CG   sing N N 124 
GLN   CB  HB2  sing N N 125 
GLN   CB  HB3  sing N N 126 
GLN   CG  CD   sing N N 127 
GLN   CG  HG2  sing N N 128 
GLN   CG  HG3  sing N N 129 
GLN   CD  OE1  doub N N 130 
GLN   CD  NE2  sing N N 131 
GLN   NE2 HE21 sing N N 132 
GLN   NE2 HE22 sing N N 133 
GLN   OXT HXT  sing N N 134 
GLU   N   CA   sing N N 135 
GLU   N   H    sing N N 136 
GLU   N   H2   sing N N 137 
GLU   CA  C    sing N N 138 
GLU   CA  CB   sing N N 139 
GLU   CA  HA   sing N N 140 
GLU   C   O    doub N N 141 
GLU   C   OXT  sing N N 142 
GLU   CB  CG   sing N N 143 
GLU   CB  HB2  sing N N 144 
GLU   CB  HB3  sing N N 145 
GLU   CG  CD   sing N N 146 
GLU   CG  HG2  sing N N 147 
GLU   CG  HG3  sing N N 148 
GLU   CD  OE1  doub N N 149 
GLU   CD  OE2  sing N N 150 
GLU   OE2 HE2  sing N N 151 
GLU   OXT HXT  sing N N 152 
GLY   N   CA   sing N N 153 
GLY   N   H    sing N N 154 
GLY   N   H2   sing N N 155 
GLY   CA  C    sing N N 156 
GLY   CA  HA2  sing N N 157 
GLY   CA  HA3  sing N N 158 
GLY   C   O    doub N N 159 
GLY   C   OXT  sing N N 160 
GLY   OXT HXT  sing N N 161 
HIS   N   CA   sing N N 162 
HIS   N   H    sing N N 163 
HIS   N   H2   sing N N 164 
HIS   CA  C    sing N N 165 
HIS   CA  CB   sing N N 166 
HIS   CA  HA   sing N N 167 
HIS   C   O    doub N N 168 
HIS   C   OXT  sing N N 169 
HIS   CB  CG   sing N N 170 
HIS   CB  HB2  sing N N 171 
HIS   CB  HB3  sing N N 172 
HIS   CG  ND1  sing Y N 173 
HIS   CG  CD2  doub Y N 174 
HIS   ND1 CE1  doub Y N 175 
HIS   ND1 HD1  sing N N 176 
HIS   CD2 NE2  sing Y N 177 
HIS   CD2 HD2  sing N N 178 
HIS   CE1 NE2  sing Y N 179 
HIS   CE1 HE1  sing N N 180 
HIS   NE2 HE2  sing N N 181 
HIS   OXT HXT  sing N N 182 
HOH   O   H1   sing N N 183 
HOH   O   H2   sing N N 184 
ILE   N   CA   sing N N 185 
ILE   N   H    sing N N 186 
ILE   N   H2   sing N N 187 
ILE   CA  C    sing N N 188 
ILE   CA  CB   sing N N 189 
ILE   CA  HA   sing N N 190 
ILE   C   O    doub N N 191 
ILE   C   OXT  sing N N 192 
ILE   CB  CG1  sing N N 193 
ILE   CB  CG2  sing N N 194 
ILE   CB  HB   sing N N 195 
ILE   CG1 CD1  sing N N 196 
ILE   CG1 HG12 sing N N 197 
ILE   CG1 HG13 sing N N 198 
ILE   CG2 HG21 sing N N 199 
ILE   CG2 HG22 sing N N 200 
ILE   CG2 HG23 sing N N 201 
ILE   CD1 HD11 sing N N 202 
ILE   CD1 HD12 sing N N 203 
ILE   CD1 HD13 sing N N 204 
ILE   OXT HXT  sing N N 205 
LEU   N   CA   sing N N 206 
LEU   N   H    sing N N 207 
LEU   N   H2   sing N N 208 
LEU   CA  C    sing N N 209 
LEU   CA  CB   sing N N 210 
LEU   CA  HA   sing N N 211 
LEU   C   O    doub N N 212 
LEU   C   OXT  sing N N 213 
LEU   CB  CG   sing N N 214 
LEU   CB  HB2  sing N N 215 
LEU   CB  HB3  sing N N 216 
LEU   CG  CD1  sing N N 217 
LEU   CG  CD2  sing N N 218 
LEU   CG  HG   sing N N 219 
LEU   CD1 HD11 sing N N 220 
LEU   CD1 HD12 sing N N 221 
LEU   CD1 HD13 sing N N 222 
LEU   CD2 HD21 sing N N 223 
LEU   CD2 HD22 sing N N 224 
LEU   CD2 HD23 sing N N 225 
LEU   OXT HXT  sing N N 226 
LYS   N   CA   sing N N 227 
LYS   N   H    sing N N 228 
LYS   N   H2   sing N N 229 
LYS   CA  C    sing N N 230 
LYS   CA  CB   sing N N 231 
LYS   CA  HA   sing N N 232 
LYS   C   O    doub N N 233 
LYS   C   OXT  sing N N 234 
LYS   CB  CG   sing N N 235 
LYS   CB  HB2  sing N N 236 
LYS   CB  HB3  sing N N 237 
LYS   CG  CD   sing N N 238 
LYS   CG  HG2  sing N N 239 
LYS   CG  HG3  sing N N 240 
LYS   CD  CE   sing N N 241 
LYS   CD  HD2  sing N N 242 
LYS   CD  HD3  sing N N 243 
LYS   CE  NZ   sing N N 244 
LYS   CE  HE2  sing N N 245 
LYS   CE  HE3  sing N N 246 
LYS   NZ  HZ1  sing N N 247 
LYS   NZ  HZ2  sing N N 248 
LYS   NZ  HZ3  sing N N 249 
LYS   OXT HXT  sing N N 250 
MET   N   CA   sing N N 251 
MET   N   H    sing N N 252 
MET   N   H2   sing N N 253 
MET   CA  C    sing N N 254 
MET   CA  CB   sing N N 255 
MET   CA  HA   sing N N 256 
MET   C   O    doub N N 257 
MET   C   OXT  sing N N 258 
MET   CB  CG   sing N N 259 
MET   CB  HB2  sing N N 260 
MET   CB  HB3  sing N N 261 
MET   CG  SD   sing N N 262 
MET   CG  HG2  sing N N 263 
MET   CG  HG3  sing N N 264 
MET   SD  CE   sing N N 265 
MET   CE  HE1  sing N N 266 
MET   CE  HE2  sing N N 267 
MET   CE  HE3  sing N N 268 
MET   OXT HXT  sing N N 269 
PHE   N   CA   sing N N 270 
PHE   N   H    sing N N 271 
PHE   N   H2   sing N N 272 
PHE   CA  C    sing N N 273 
PHE   CA  CB   sing N N 274 
PHE   CA  HA   sing N N 275 
PHE   C   O    doub N N 276 
PHE   C   OXT  sing N N 277 
PHE   CB  CG   sing N N 278 
PHE   CB  HB2  sing N N 279 
PHE   CB  HB3  sing N N 280 
PHE   CG  CD1  doub Y N 281 
PHE   CG  CD2  sing Y N 282 
PHE   CD1 CE1  sing Y N 283 
PHE   CD1 HD1  sing N N 284 
PHE   CD2 CE2  doub Y N 285 
PHE   CD2 HD2  sing N N 286 
PHE   CE1 CZ   doub Y N 287 
PHE   CE1 HE1  sing N N 288 
PHE   CE2 CZ   sing Y N 289 
PHE   CE2 HE2  sing N N 290 
PHE   CZ  HZ   sing N N 291 
PHE   OXT HXT  sing N N 292 
PRO   N   CA   sing N N 293 
PRO   N   CD   sing N N 294 
PRO   N   H    sing N N 295 
PRO   CA  C    sing N N 296 
PRO   CA  CB   sing N N 297 
PRO   CA  HA   sing N N 298 
PRO   C   O    doub N N 299 
PRO   C   OXT  sing N N 300 
PRO   CB  CG   sing N N 301 
PRO   CB  HB2  sing N N 302 
PRO   CB  HB3  sing N N 303 
PRO   CG  CD   sing N N 304 
PRO   CG  HG2  sing N N 305 
PRO   CG  HG3  sing N N 306 
PRO   CD  HD2  sing N N 307 
PRO   CD  HD3  sing N N 308 
PRO   OXT HXT  sing N N 309 
SER   N   CA   sing N N 310 
SER   N   H    sing N N 311 
SER   N   H2   sing N N 312 
SER   CA  C    sing N N 313 
SER   CA  CB   sing N N 314 
SER   CA  HA   sing N N 315 
SER   C   O    doub N N 316 
SER   C   OXT  sing N N 317 
SER   CB  OG   sing N N 318 
SER   CB  HB2  sing N N 319 
SER   CB  HB3  sing N N 320 
SER   OG  HG   sing N N 321 
SER   OXT HXT  sing N N 322 
THR   N   CA   sing N N 323 
THR   N   H    sing N N 324 
THR   N   H2   sing N N 325 
THR   CA  C    sing N N 326 
THR   CA  CB   sing N N 327 
THR   CA  HA   sing N N 328 
THR   C   O    doub N N 329 
THR   C   OXT  sing N N 330 
THR   CB  OG1  sing N N 331 
THR   CB  CG2  sing N N 332 
THR   CB  HB   sing N N 333 
THR   OG1 HG1  sing N N 334 
THR   CG2 HG21 sing N N 335 
THR   CG2 HG22 sing N N 336 
THR   CG2 HG23 sing N N 337 
THR   OXT HXT  sing N N 338 
TRP   N   CA   sing N N 339 
TRP   N   H    sing N N 340 
TRP   N   H2   sing N N 341 
TRP   CA  C    sing N N 342 
TRP   CA  CB   sing N N 343 
TRP   CA  HA   sing N N 344 
TRP   C   O    doub N N 345 
TRP   C   OXT  sing N N 346 
TRP   CB  CG   sing N N 347 
TRP   CB  HB2  sing N N 348 
TRP   CB  HB3  sing N N 349 
TRP   CG  CD1  doub Y N 350 
TRP   CG  CD2  sing Y N 351 
TRP   CD1 NE1  sing Y N 352 
TRP   CD1 HD1  sing N N 353 
TRP   CD2 CE2  doub Y N 354 
TRP   CD2 CE3  sing Y N 355 
TRP   NE1 CE2  sing Y N 356 
TRP   NE1 HE1  sing N N 357 
TRP   CE2 CZ2  sing Y N 358 
TRP   CE3 CZ3  doub Y N 359 
TRP   CE3 HE3  sing N N 360 
TRP   CZ2 CH2  doub Y N 361 
TRP   CZ2 HZ2  sing N N 362 
TRP   CZ3 CH2  sing Y N 363 
TRP   CZ3 HZ3  sing N N 364 
TRP   CH2 HH2  sing N N 365 
TRP   OXT HXT  sing N N 366 
TYR   N   CA   sing N N 367 
TYR   N   H    sing N N 368 
TYR   N   H2   sing N N 369 
TYR   CA  C    sing N N 370 
TYR   CA  CB   sing N N 371 
TYR   CA  HA   sing N N 372 
TYR   C   O    doub N N 373 
TYR   C   OXT  sing N N 374 
TYR   CB  CG   sing N N 375 
TYR   CB  HB2  sing N N 376 
TYR   CB  HB3  sing N N 377 
TYR   CG  CD1  doub Y N 378 
TYR   CG  CD2  sing Y N 379 
TYR   CD1 CE1  sing Y N 380 
TYR   CD1 HD1  sing N N 381 
TYR   CD2 CE2  doub Y N 382 
TYR   CD2 HD2  sing N N 383 
TYR   CE1 CZ   doub Y N 384 
TYR   CE1 HE1  sing N N 385 
TYR   CE2 CZ   sing Y N 386 
TYR   CE2 HE2  sing N N 387 
TYR   CZ  OH   sing N N 388 
TYR   OH  HH   sing N N 389 
TYR   OXT HXT  sing N N 390 
VAL   N   CA   sing N N 391 
VAL   N   H    sing N N 392 
VAL   N   H2   sing N N 393 
VAL   CA  C    sing N N 394 
VAL   CA  CB   sing N N 395 
VAL   CA  HA   sing N N 396 
VAL   C   O    doub N N 397 
VAL   C   OXT  sing N N 398 
VAL   CB  CG1  sing N N 399 
VAL   CB  CG2  sing N N 400 
VAL   CB  HB   sing N N 401 
VAL   CG1 HG11 sing N N 402 
VAL   CG1 HG12 sing N N 403 
VAL   CG1 HG13 sing N N 404 
VAL   CG2 HG21 sing N N 405 
VAL   CG2 HG22 sing N N 406 
VAL   CG2 HG23 sing N N 407 
VAL   OXT HXT  sing N N 408 
# 
_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                    7HZF 
_atom_sites.fract_transf_matrix[1][1]   0.013744 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000706 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016198 
_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]   0.015249 
_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 
F  
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   ? 16.415 6.453   8.208  1.00 18.76  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.169 6.526   8.981  1.00 18.93  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 15.021 5.371   9.964  1.00 18.48  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.684 4.339   9.828  1.00 18.70  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 13.976 6.598   8.027  1.00 21.20  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.814 5.359   7.351  1.00 23.20  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.153 5.542   10.959 1.00 17.71  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.884 4.497   11.935 1.00 16.12  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.512 5.029   13.305 1.00 15.68  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.902 6.144   13.672 1.00 15.49  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.763 4.242   14.081 1.00 14.80  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.347 4.660   15.413 1.00 15.26  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.311 3.456   16.386 1.00 15.16  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.301 2.287   15.942 1.00 15.12  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.945 5.283   15.333 1.00 16.35  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.237 3.740   17.710 1.00 13.64  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 12.023 2.739   18.751 1.00 13.58  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.591 2.938   19.248 1.00 13.97  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.197 4.079   19.532 1.00 13.57  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 13.008 2.915   19.921 1.00 14.30  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.466 2.907   19.414 1.00 14.36  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.791 1.820   20.993 1.00 14.91  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.470 3.448   20.446 1.00 14.96  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.805  1.849   19.369 1.00 14.70  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.424  1.930   19.869 1.00 16.13  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.326  1.177   21.184 1.00 16.64  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.388  -0.041  21.184 1.00 17.27  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.461  1.349   18.848 1.00 16.39  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.416  2.177   17.588 1.00 17.35  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.620  3.306   17.505 1.00 19.09  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.204  1.854   16.494 1.00 19.41  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.618  4.107   16.368 1.00 20.51  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.217  2.647   15.357 1.00 21.15  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.401  3.758   15.288 1.00 22.45  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.440  4.558   14.170 1.00 25.09  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.200  1.889   22.309 1.00 17.14  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.172  1.247   23.633 1.00 18.04  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.042  1.864   24.436 1.00 18.84  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 6.965  3.079   24.542 1.00 19.65  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.556  1.392   24.359 1.00 19.97  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.092 2.828   24.275 1.00 19.81  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.474  0.946   25.815 1.00 22.21  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.090  1.045   24.913 1.00 19.20  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 4.945  1.559   25.662 1.00 19.50  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.164  2.566   24.832 1.00 20.59  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 3.947  2.316   23.645 1.00 21.26  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 3.876  3.760   25.373 1.00 20.12  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.206  4.778   24.557 1.00 20.79  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.174  5.827   24.049 1.00 18.80  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.791  6.990   23.887 1.00 18.70  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 2.013  5.403   25.280 1.00 24.62  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 0.897  4.415   25.394 1.00 30.81  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.287  4.025   24.394 1.00 33.85  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.650  3.958   26.607 1.00 31.83  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.417  5.419   23.735 1.00 17.02  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.431  6.368   23.264 1.00 16.54  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 7.025  5.932   21.927 1.00 15.28  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.133  4.729   21.655 1.00 15.25  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.600  6.437   24.278 1.00 16.36  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.186  6.976   25.630 1.00 17.19  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.558  8.209   25.747 1.00 18.54  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.415  6.250   26.792 1.00 18.43  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.202  8.728   26.990 1.00 19.83  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.032  6.742   28.038 1.00 19.60  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.394  7.970   28.128 1.00 21.03  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.019  8.490   29.349 1.00 23.12  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.454  6.924   21.119 1.00 14.34  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.159  6.726   19.863 1.00 13.60  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.473  7.534   20.010 1.00 14.29  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.422  8.724   20.290 1.00 15.01  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.308  7.273   18.690 1.00 14.36  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.071  7.502   17.380 1.00 15.33  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.165  7.851   16.210 1.00 16.56  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.741  8.874   15.322 1.00 18.66  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.293  8.626   14.139 1.00 22.13  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.443  7.369   13.715 1.00 20.61  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.755  9.625   13.393 1.00 22.34  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.627 6.876   19.881 1.00 14.06  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 11.942 7.539   20.011 1.00 14.29  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.520 7.675   18.610 1.00 14.54  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.702 6.667   17.932 1.00 14.55  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 12.910 6.696   20.884 1.00 14.87  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.218 7.484   21.160 1.00 14.60  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.239 6.248   22.196 1.00 14.88  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.865 8.895   18.186 1.00 13.21  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.440 9.113   16.852 1.00 13.48  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.659 10.041  16.955 1.00 13.00  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.826 10.753  17.964 1.00 13.55  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.389 9.750   15.897 1.00 15.41  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.313 8.751   15.524 1.00 17.63  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.779 11.012  16.502 1.00 16.33  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.460 10.146  15.862 1.00 12.31  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.509 11.181  15.823 1.00 12.43  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.808 12.537  15.809 1.00 12.86  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.885 12.741  15.006 1.00 13.16  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.302 11.086  14.520 1.00 12.32  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.129 9.827   14.432 1.00 14.02  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.690 8.830   13.851 1.00 14.83  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.329 9.862   14.995 1.00 14.88  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.216 13.472  16.677 1.00 12.04  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.561 14.801  16.727 1.00 11.49  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.592 15.490  15.342 1.00 11.99  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.608 16.146  14.952 1.00 13.38  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.222 15.674  17.792 1.00 13.55  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.461 16.963  18.142 1.00 13.70  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.380 17.849  18.979 1.00 14.97  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.754 19.082  19.496 1.00 16.12  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.680 20.224  18.826 1.00 15.99  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.122 20.298  17.570 1.00 16.27  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.193 21.315  19.416 1.00 15.34  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.702 15.337  14.591 1.00 11.74  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.802 16.013  13.267 1.00 12.72  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.861 15.428  12.202 1.00 14.01  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.632 16.068  11.165 1.00 16.14  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.270 16.092  12.744 1.00 12.83  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.864 14.798  12.258 1.00 13.86  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.470 13.902  13.129 1.00 14.26  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 19.050 14.358  10.986 1.00 14.95  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.934 12.919  12.369 1.00 15.18  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.692 13.146  11.070 1.00 15.01  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.273 14.248  12.467 1.00 13.44  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.328 13.597  11.549 1.00 13.37  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.874 13.616  12.071 1.00 15.24  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 11.976 13.008  11.458 1.00 15.51  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.776 12.157  11.285 1.00 13.25  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.182 12.022  10.655 1.00 14.14  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.529 10.548  10.395 1.00 15.27  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.249 12.776  9.327  1.00 14.44  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.635 14.291  13.227 1.00 14.78  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.290 14.324  13.796 1.00 14.91  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.304 14.997  12.831 1.00 15.60  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.659 15.975  12.184 1.00 15.55  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.302 15.067  15.120 1.00 15.40  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.079  14.467  12.760 1.00 16.17  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 8.040  15.003  11.874 1.00 17.62  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.194  16.087  12.575 1.00 18.63  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.300  16.280  13.795 1.00 18.74  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.116  13.835  11.425 1.00 20.06  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.361  13.387  12.560 1.00 20.82  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.871  12.697  10.783 1.00 20.66  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.272  16.738  11.823 1.00 19.75  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.326  17.701  12.409 1.00 21.07  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.494  17.008  13.511 1.00 18.93  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.306  17.574  14.586 1.00 18.95  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.373  18.220  11.316 1.00 24.77  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 5.028  19.082  10.289 1.00 33.19  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.951  20.054  10.643 1.00 36.91  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 4.851  19.112  8.945  1.00 35.74  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.329  20.618  9.506  1.00 38.16  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.685  20.091  8.457  1.00 38.05  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.065  15.757  13.264 1.00 18.58  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.299  15.007  14.251 1.00 18.84  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.088  14.696  15.519 1.00 17.67  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.524  14.747  16.602 1.00 18.53  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.733  13.716  13.668 1.00 22.04  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.402  13.951  13.059 1.00 28.77  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.590  14.724  13.599 1.00 29.93  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 1.186  13.348  11.901 1.00 30.80  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.385  14.369  15.404 1.00 15.70  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.229  14.127  16.587 1.00 15.22  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.274  15.375  17.479 1.00 14.89  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.122  15.270  18.702 1.00 15.87  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.681  13.792  16.168 1.00 14.81  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.850  12.398  15.605 1.00 19.61  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.215  11.464  16.141 1.00 19.57  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.607  12.249  14.601 1.00 19.66  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.496  16.548  16.870 1.00 14.61  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.547  17.803  17.621 1.00 15.52  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.184  18.159  18.234 1.00 16.89  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.138  18.727  19.335 1.00 17.76  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.084  18.942  16.738 1.00 15.85  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.586  18.953  16.658 1.00 15.70  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.365  18.538  15.615 1.00 16.55  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.484  19.474  17.648 1.00 15.73  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.702 18.743  15.914 1.00 16.46  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.797 19.299  17.162 1.00 16.42  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.307  19.997  18.930 1.00 16.97  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 11.915 19.687  17.898 1.00 16.47  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.412 20.439  19.628 1.00 17.16  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.698 20.243  19.129 1.00 16.42  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.075  17.801  17.561 1.00 16.74  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.729  18.076  18.120 1.00 18.90  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.367  17.142  19.288 1.00 19.53  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.391  17.391  20.018 1.00 20.70  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.691  17.952  17.030 1.00 19.86  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.076  16.023  19.416 1.00 18.57  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 2.856  15.065  20.494 1.00 18.54  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.153  14.903  21.317 1.00 17.61  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.434  13.841  21.830 1.00 17.19  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.393  13.727  19.897 1.00 19.27  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.031  13.824  19.255 1.00 23.45  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.011  13.859  19.949 1.00 24.77  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 0.979  13.891  17.922 1.00 23.15  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 4.925  15.994  21.473 1.00 17.02  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.215  15.999  22.157 1.00 16.92  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.153  15.612  23.635 1.00 17.45  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.313  16.119  24.386 1.00 19.07  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 6.820  17.412  22.052 1.00 16.76  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.178  17.625  22.715 1.00 17.29  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.261  16.773  22.007 1.00 17.56  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.586  19.114  22.646 1.00 17.88  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.052  14.705  24.053 1.00 16.83  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.196  14.318  25.452 1.00 17.65  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.510  14.915  25.994 1.00 18.52  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.547  15.516  27.072 1.00 19.78  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.189  12.770  25.590 1.00 18.33  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.566  12.351  27.007 1.00 19.26  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 5.808  12.214  25.214 1.00 19.44  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.591  14.763  25.227 1.00 17.65  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 10.919 15.229  25.632 1.00 17.02  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 11.821 15.305  24.401 1.00 15.48  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.696 14.479  23.508 1.00 15.21  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.527 14.211  26.635 1.00 17.41  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 12.993 14.403  26.967 1.00 17.96  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.534 15.287  27.856 1.00 19.14  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.093 13.669  26.413 1.00 17.37  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 14.910 15.155  27.876 1.00 19.73  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.272 14.145  27.025 1.00 18.38  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.193 12.643  25.469 1.00 18.21  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.534 13.624  26.721 1.00 18.38  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.439 12.127  25.174 1.00 18.71  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.592 12.622  25.791 1.00 18.35  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.712 16.284  24.365 1.00 15.06  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.699 16.386  23.293 1.00 14.48  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 14.993 16.979  23.826 1.00 14.56  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 14.981 17.757  24.783 1.00 15.61  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.186 17.158  22.061 1.00 14.03  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.598 18.533  22.369 1.00 15.69  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.571 19.670  22.623 1.00 19.72  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.208 20.568  23.424 1.00 23.13  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.683 19.670  22.045 1.00 17.70  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.119 16.633  23.192 1.00 13.37  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.405 17.157  23.618 1.00 13.82  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.320 17.282  22.388 1.00 13.83  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.775 16.265  21.865 1.00 13.70  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 17.980 16.243  24.705 1.00 16.43  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.254 16.736  25.380 1.00 22.95  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.013 17.507  24.741 1.00 24.26  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.503 16.338  26.540 1.00 25.18  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.556 18.532  21.902 1.00 14.49  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.420 18.781  20.742 0.50 14.76  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.398 18.721  20.723 0.50 15.09  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.818 18.246  20.984 1.00 14.86  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.469 17.786  20.053 1.00 15.19  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.530 20.278  20.452 0.50 15.91  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.405 20.178  20.268 0.50 17.18  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 18.267 20.838  20.150 0.50 16.99  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 19.948 21.006  21.277 0.50 19.37  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.308 18.359  22.232 1.00 14.99  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.671 17.892  22.530 1.00 15.97  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 22.830 16.380  22.377 1.00 15.40  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 23.947 15.933  22.206 1.00 15.75  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.145 18.362  23.908 1.00 19.79  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.623 17.569  24.955 1.00 24.81  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.736 15.612  22.421 1.00 13.57  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.771 14.137  22.233 1.00 13.00  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.242 13.694  20.858 1.00 13.37  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.273 12.485  20.558 1.00 13.58  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 20.925 13.443  23.330 1.00 13.33  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.489 13.657  24.736 1.00 13.96  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.649 13.012  25.830 1.00 14.13  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.639 11.555  25.682 1.00 13.08  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.421 10.691  26.675 1.00 15.10  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.272 11.126  27.928 1.00 14.21  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.437 9.378   26.438 1.00 14.56  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.679 14.634  20.060 1.00 13.32  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 19.991 14.323  18.794 1.00 13.34  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.803 13.360  19.045 1.00 12.81  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.539 12.501  18.187 1.00 12.88  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 20.935 13.760  17.701 1.00 14.49  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.248 13.524  16.345 1.00 13.74  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.467 14.393  15.920 1.00 13.69  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.515 12.463  15.710 1.00 13.58  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.082 13.489  20.190 1.00 12.11  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 16.914 12.626  20.461 1.00 11.93  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.641 13.431  20.652 1.00 12.72  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.645 14.543  21.202 1.00 12.64  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.099 11.785  21.744 1.00 12.21  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.127 10.671  21.706 1.00 13.29  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.128 9.935   23.059 1.00 14.59  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.838 9.660   20.555 1.00 13.93  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.527 12.820  20.253 1.00 13.00  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.201 13.366  20.503 1.00 12.74  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.287 12.165  20.771 1.00 12.53  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.400 11.110  20.102 1.00 12.18  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.683 14.199  19.320 1.00 13.07  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.278 14.822  19.493 1.00 14.61  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.171 16.162  18.779 1.00 15.88  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.147 13.887  18.990 1.00 13.97  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.395 12.318  21.752 1.00 12.12  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.408 11.290  22.116 1.00 13.01  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 9.027  11.915  22.016 1.00 14.77  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 8.801  13.012  22.550 1.00 15.53  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.653 10.722  23.551 1.00 14.05  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.560  9.704   23.943 1.00 14.85  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 12.044 10.082  23.649 1.00 15.15  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.122  11.228  21.331 1.00 14.94  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.732  11.658  21.160 1.00 16.16  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.791  10.564  21.701 1.00 17.27  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.192  9.393   21.863 1.00 16.25  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.429  11.971  19.692 1.00 17.46  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.568  10.835  18.848 1.00 19.02  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.532  10.948  21.972 1.00 17.19  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.564  9.987   22.489 1.00 18.22  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 2.797  9.290   21.360 1.00 19.53  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.588  9.864   20.291 1.00 19.93  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.599  10.668  23.457 1.00 19.66  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 1.940  11.735  22.805 1.00 23.04  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.343  8.051   21.602 1.00 20.36  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.601  7.298   20.576 1.00 22.40  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.274  6.819   21.159 1.00 24.69  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.161  6.681   22.374 1.00 25.42  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.394  6.056   20.125 1.00 24.10  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.514  5.183   21.244 1.00 25.55  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.790  6.387   19.598 1.00 24.04  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.707 6.527   20.306 1.00 26.27  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -1.981 5.988   20.773 1.00 28.07  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.882 4.445   20.896 1.00 28.63  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.538 3.850   21.755 1.00 30.48  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -3.130 6.398   19.826 1.00 30.73  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.764 6.059   18.486 1.00 32.59  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.468 7.875   19.914 1.00 31.23  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -1.088 3.804   20.035 1.00 27.81  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.927 2.353   20.073 1.00 28.07  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.260  1.940   20.972 1.00 27.99  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.219  2.687   21.135 1.00 26.70  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.736 1.813   18.665 1.00 28.56  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.176  0.757   21.557 1.00 28.78  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.202  0.224   22.450 1.00 30.44  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.398  -0.320  21.671 1.00 30.74  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.206  -1.084  20.726 1.00 31.59  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.581  -0.902  23.306 1.00 34.71  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.569  -1.595  24.242 1.00 41.75  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 1.808  -0.848  25.530 1.00 49.34  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 1.130  0.136   25.852 1.00 51.26  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 2.785  -1.314  26.307 1.00 51.20  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.609  0.077   22.062 1.00 29.82  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 4.843  -0.391  21.448 1.00 30.33  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.382  -1.577  22.230 1.00 31.29  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 5.259  -1.616  23.459 1.00 31.58  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.015  -2.521  21.552 1.00 31.02  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.493  -3.731  22.226 1.00 31.18  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 8.010  -3.897  22.198 1.00 29.39  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.472  -4.991  22.507 1.00 30.20  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 5.779  -4.977  21.687 1.00 33.57  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 3.976  -4.872  21.738 1.00 47.81  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.772  -2.847  21.847 1.00 27.00  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.239 -2.945  21.859 1.00 25.18  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.665 -2.973  23.373 1.00 24.60  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 9.929  -2.450  24.229 1.00 26.42  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 10.914 -1.749  21.086 1.00 25.35  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.188 -1.873  19.569 1.00 29.34  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 11.803 -2.888  19.158 1.00 29.58  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 10.884 -0.870  18.789 1.00 26.49  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 11.785 -3.629  23.698 1.00 21.93  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 12.342 -3.733  25.063 1.00 20.93  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.627 -2.894  25.099 1.00 18.69  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.444 -3.036  24.199 1.00 18.17  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 12.767 -5.205  25.357 1.00 23.65  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 11.597 -5.989  25.531 1.00 25.03  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 13.639 -5.343  26.635 1.00 23.88  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 13.817 -2.048  26.128 1.00 16.73  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 15.045 -1.255  26.236 1.00 15.53  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 16.049 -2.004  27.129 1.00 15.37  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.694 -2.469  28.235 1.00 15.99  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 14.757 0.150   26.857 1.00 15.88  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.637 0.912   26.100 1.00 17.32  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 16.043 0.992   26.857 1.00 15.88  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 13.954 1.175   24.562 1.00 19.23  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.290 -2.116  26.685 1.00 14.38  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.340 -2.736  27.489 1.00 14.32  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.676 -1.848  28.686 1.00 15.32  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.712 -0.621  28.567 1.00 15.42  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.598 -2.919  26.638 1.00 12.71  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 18.980 -2.468  29.827 1.00 15.44  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.410 -1.733  31.039 1.00 15.97  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.691 -2.458  31.468 1.00 17.78  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.658 -3.390  32.277 1.00 19.32  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.336 -1.817  32.141 1.00 16.39  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.976 -1.246  31.723 1.00 17.31  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.997 0.252   31.357 1.00 18.87  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.642 0.690   31.020 1.00 18.90  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.341 1.816   30.385 1.00 21.40  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.298 2.653   30.015 1.00 20.32  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 14.078 2.113   30.115 1.00 19.98  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 21.799 -2.125  30.816 1.00 17.53  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 23.055 -2.877  30.937 1.00 17.51  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.248 -1.970  30.618 1.00 18.42  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 24.078 -0.807  30.226 1.00 19.03  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 23.008 -4.052  29.957 1.00 17.57  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 23.012 -3.534  28.218 1.00 18.56  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.468 -2.556  30.688 1.00 19.00  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.659 -1.825  30.284 1.00 20.68  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.363 -2.540  29.141 1.00 20.07  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.578 -2.455  29.031 1.00 20.66  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 27.612 -1.586  31.467 1.00 24.94  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 28.225 -2.815  32.099 1.00 34.41  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 27.795 -3.948  31.754 1.00 34.40  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 29.157 -2.653  32.919 1.00 40.61  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.604 -3.231  28.258 1.00 18.70  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 27.196 -3.912  27.097 1.00 17.73  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 27.957 -2.942  26.231 1.00 17.30  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.497 -1.807  26.050 1.00 17.40  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 26.114 -4.594  26.269 1.00 18.61  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.495 -6.143  26.972 1.00 18.82  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 29.110 -3.380  25.691 1.00 15.28  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 29.892 -2.644  24.701 1.00 14.42  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 30.021 -3.378  23.361 1.00 14.37  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 30.907 -3.065  22.564 1.00 13.90  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 31.258 -2.216  25.213 1.00 16.81  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 31.178 -1.100  26.235 1.00 21.08  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.585 -0.636  26.539 1.00 24.71  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 33.088 -0.843  27.636 1.00 26.52  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.227 0.011   25.578 1.00 22.67  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 29.195 -4.427  23.156 1.00 13.71  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 29.107 -5.125  21.882 1.00 14.50  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.610 -5.287  21.579 1.00 13.85  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.772 -5.326  22.485 1.00 13.97  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 29.822 -6.496  21.879 1.00 16.50  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 29.162 -7.366  22.782 1.00 18.08  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 31.315 -6.405  22.221 1.00 17.88  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.300 -5.380  20.303 1.00 12.97  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 25.921 -5.554  19.865 1.00 13.17  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 25.853 -5.674  18.352 1.00 13.17  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 26.867 -5.929  17.699 1.00 13.11  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.654 -5.532  17.808 1.00 11.80  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.394 -5.658  16.363 1.00 12.21  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.534 -4.475  15.920 1.00 12.49  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.557 -4.161  16.589 1.00 13.37  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.695 -7.010  16.058 1.00 14.24  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.338 -7.115  14.586 1.00 14.95  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.586 -8.195  16.469 1.00 13.95  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 23.879 -3.820  14.782 1.00 11.86  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 23.031 -2.705  14.318 1.00 11.82  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.505 -2.947  12.927 1.00 12.34  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 23.129 -3.677  12.153 1.00 11.51  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.734 -1.314  14.400 1.00 11.87  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.762 -1.056  13.309 1.00 12.03  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 26.017 -1.645  13.354 1.00 13.48  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.496 -0.177  12.259 1.00 12.35  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 26.972 -1.389  12.375 1.00 13.99  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.433 0.049   11.248 1.00 13.47  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.683 -0.538  11.328 1.00 14.59  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.636 -0.305  10.354 1.00 15.66  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.377 -2.300  12.590 1.00 11.42  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.848 -2.412  11.236 1.00 11.66  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.358 -1.238  10.397 1.00 12.45  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.203 -0.079  10.781 1.00 12.51  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.304 -2.410  11.228 1.00 11.46  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.762 -2.526  9.828  1.00 12.84  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 18.962 -3.680  9.081  1.00 14.32  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 18.094 -1.462  9.229  1.00 13.57  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.507 -3.777  7.774  1.00 15.46  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.642 -1.543  7.924  1.00 15.14  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.847 -2.705  7.203  1.00 16.97  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.412 -2.796  5.909  1.00 19.82  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.921 -1.565  9.216  1.00 12.36  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.465 -0.583  8.278  1.00 12.20  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.584 -0.590  7.001  1.00 13.20  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.694 -1.497  6.156  1.00 14.23  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.920 -0.935  7.969  1.00 13.43  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.670 0.084   6.674  1.00 15.33  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.694 0.419   6.877  1.00 13.02  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.779 0.460   5.745  1.00 14.04  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.462 0.624   4.401  1.00 13.92  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.980 0.058   3.413  1.00 14.65  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.692 1.517   5.918  1.00 17.20  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.293 2.791   6.044  1.00 24.27  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.619 1.314   4.360  1.00 13.08  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.359 1.508   3.093  1.00 13.73  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 23.040 0.242   2.549  1.00 13.51  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.619 0.280   1.459  1.00 14.00  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.382 2.635   3.218  1.00 15.55  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.390 2.316   4.161  1.00 16.47  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.992 -0.861  3.316  1.00 13.28  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.480 -2.164  2.878  1.00 13.46  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.368 -3.259  3.026  1.00 15.00  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.619 -4.439  2.713  1.00 15.26  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.696 -2.536  3.751  1.00 14.60  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.927 -1.665  3.502  1.00 14.79  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.579 -2.016  2.170  1.00 16.19  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.771 -1.197  1.924  1.00 18.10  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.747 -0.004  1.330  1.00 19.27  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.604 0.494   0.867  1.00 18.90  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.875 0.684   1.153  1.00 18.60  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 21.183 -2.897  3.576  1.00 15.35  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 20.089 -3.826  3.898  1.00 17.03  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.632 -5.013  4.708  1.00 16.42  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.328 -6.186  4.432  1.00 16.75  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.372 -4.312  2.657  1.00 20.63  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 18.642 -3.215  1.915  1.00 26.02  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.492 -3.864  1.156  1.00 29.95  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.874 -2.911  0.249  1.00 32.58  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.099 -2.868  -1.063 1.00 35.35  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.922 -3.749  -1.635 1.00 36.35  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.540 -1.922  -1.806 1.00 33.79  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.513 -4.716  5.673  1.00 14.90  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 22.183 -5.794  6.440  1.00 15.21  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.403 -5.382  7.872  1.00 15.32  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.457 -4.192  8.177  1.00 15.18  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.598 -6.031  5.859  1.00 17.20  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.720 -7.085  4.747  1.00 25.97  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 25.206 -7.260  4.427  1.00 32.17  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 25.479 -8.495  3.593  1.00 38.67  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 25.169 -8.278  2.155  1.00 43.41  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.539 -6.381  8.755  1.00 14.45  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 22.917 -6.160  10.147 1.00 13.06  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.419 -6.461  10.286 1.00 13.49  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 24.967 -7.385  9.654  1.00 14.51  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 22.138 -7.082  11.086 1.00 12.96  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.661 -6.829  11.115 1.00 14.31  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 20.071 -6.096  12.129 1.00 17.51  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.691 -7.282  10.295 1.00 14.35  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.773 -6.122  11.875 1.00 16.61  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.505 -6.802  10.784 1.00 17.07  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 25.097 -5.685  11.149 1.00 12.65  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.519 -5.885  11.374 1.00 13.02  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.820 -5.943  12.869 1.00 13.22  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.304 -5.145  13.644 1.00 11.97  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.342 -4.704  10.796 1.00 13.75  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.344 -4.595  9.297  1.00 14.03  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 28.051 -5.507  8.506  1.00 15.34  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.665 -3.572  8.663  1.00 15.16  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 28.044 -5.413  7.108  1.00 15.65  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.682 -3.446  7.278  1.00 16.10  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.346 -4.386  6.501  1.00 17.30  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.349 -4.252  5.122  1.00 19.27  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.726 -6.824  13.302 1.00 13.70  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 28.164 -6.790  14.723 1.00 13.24  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 29.169 -5.608  14.965 1.00 14.14  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 29.970 -5.251  14.072 1.00 15.60  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.843 -8.157  14.901 1.00 13.95  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.444 -8.415  13.490 1.00 14.71  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.449 -7.833  12.505 1.00 13.19  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 29.147 -5.008  16.179 1.00 13.37  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 30.010 -3.859  16.496 1.00 13.41  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.517 -3.935  17.915 1.00 14.15  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 29.851 -4.496  18.798 1.00 14.00  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.285 -2.475  16.351 1.00 15.22  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.226 -2.012  14.893 1.00 16.14  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 27.890 -2.496  16.976 1.00 15.29  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.732 -3.370  18.137 1.00 13.92  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 32.273 -3.100  19.473 1.00 14.51  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 32.176 -1.562  19.560 1.00 14.51  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.607 -0.897  18.612 1.00 14.47  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.734 -3.517  19.559 1.00 17.59  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 33.706 -4.934  19.497 1.00 24.01  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.541 -1.005  20.613 1.00 13.60  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.357 0.448   20.678 1.00 13.10  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.843 1.045   21.993 1.00 14.18  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.923 0.357   23.011 1.00 15.47  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.877 0.848   20.409 1.00 12.96  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.819 0.083   21.205 1.00 13.31  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.326 -1.134  20.752 1.00 14.54  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.335 0.574   22.409 1.00 14.18  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.358 -1.842  21.486 1.00 14.55  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.338 -0.124  23.134 1.00 14.40  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.877 -1.335  22.674 1.00 14.93  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.203 2.326   21.958 1.00 14.07  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.668 3.022   23.153 1.00 13.90  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.532 3.362   24.101 1.00 14.68  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.378 3.438   23.698 1.00 15.49  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.404 4.299   22.762 1.00 14.98  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.520 5.158   22.059 1.00 17.74  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 31.852 3.551   25.385 1.00 14.69  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 30.859 3.961   26.376 1.00 15.50  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.275 5.337   25.987 1.00 15.66  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 30.984 6.171   25.398 1.00 15.88  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.522 4.000   27.771 1.00 18.10  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 31.791 2.586   28.257 1.00 21.43  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.316 2.594   29.690 1.00 27.85  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.264 1.180   30.201 1.00 34.27  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 32.579 1.083   31.660 1.00 38.52  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 29.000 5.604   26.343 1.00 15.15  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.403 6.909   26.008 1.00 15.26  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.255 8.082   26.500 1.00 15.54  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.660 8.115   27.678 1.00 15.35  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 27.050 6.890   26.749 1.00 16.47  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 26.792 5.477   27.119 1.00 17.74  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 28.067 4.722   27.087 1.00 15.18  ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.550 9.030   25.598 1.00 15.10  ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 30.411 10.164  25.951 1.00 16.98  ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 30.111 11.411  25.103 1.00 16.48  ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 29.263 11.355  24.206 1.00 15.62  ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 31.882 9.752   25.840 1.00 21.46  ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 32.245 9.624   24.478 1.00 27.16  ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 30.820 12.537  25.390 1.00 16.93  ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 30.669 13.810  24.668 1.00 18.16  ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 31.665 13.761  23.507 1.00 17.87  ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 32.878 13.658  23.753 1.00 18.47  ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 31.096 14.977  25.596 1.00 20.00  ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 30.032 15.617  26.444 1.00 24.54  ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 30.681 16.599  27.439 1.00 26.51  ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 29.078 16.428  25.571 1.00 25.75  ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 31.171 13.843  22.264 1.00 16.78  ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 32.006 13.732  21.069 1.00 17.64  ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 31.757 14.906  20.160 1.00 17.69  ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 30.599 15.258  19.937 1.00 16.93  ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 31.691 12.372  20.367 1.00 18.90  ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 32.148 11.207  21.266 1.00 21.04  ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 32.293 12.282  18.955 1.00 19.45  ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 31.789 9.873   20.825 1.00 23.82  ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 32.826 15.522  19.626 1.00 17.44  ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 32.682 16.655  18.710 1.00 18.27  ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 32.121 16.205  17.372 1.00 18.69  ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 32.620 15.244  16.780 1.00 19.64  ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 34.037 17.368  18.494 1.00 18.94  ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 33.851 18.754  17.912 1.00 22.66  ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 34.049 18.987  16.562 1.00 24.88  ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 33.339 19.780  18.683 1.00 25.30  ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 33.848 20.257  16.018 1.00 25.78  ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 33.104 21.042  18.129 1.00 26.79  ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 33.377 21.269  16.801 1.00 25.95  ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 31.037 16.870  16.920 1.00 17.00  ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 30.381 16.544  15.648 1.00 16.49  ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 30.420 17.792  14.767 1.00 17.57  ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 29.945 18.864  15.178 1.00 18.51  ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 28.890 16.071  15.884 1.00 16.79  ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 28.196 15.729  14.555 1.00 17.59  ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 28.835 14.868  16.828 1.00 16.40  ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 30.888 17.627  13.528 1.00 17.80  ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 30.992 18.705  12.548 1.00 19.00  ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 29.632 19.340  12.250 1.00 18.80  ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 28.606 18.669  12.348 1.00 17.63  ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 31.469 18.093  11.232 1.00 24.92  ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 32.955 17.914  11.132 1.00 35.42  ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 33.214 17.868  9.642  1.00 46.69  ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 33.604 18.909  9.063  1.00 50.29  ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 32.924 16.810  9.039  1.00 49.86  ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 29.635 20.610  11.788 1.00 18.71  ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 28.384 21.267  11.423 1.00 18.68  ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 27.684 20.515  10.276 1.00 18.75  ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 28.346 19.922  9.426  1.00 18.74  ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 28.640 22.714  10.994 1.00 19.91  ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 26.348 20.533  10.284 1.00 18.16  ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 25.513 19.931  9.246  1.00 17.73  ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 24.370 20.940  8.969  1.00 17.83  ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 24.338 22.028  9.590  1.00 17.66  ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 24.927 18.592  9.735  1.00 18.33  ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 23.964 18.783  10.762 1.00 18.54  ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 23.445 20.605  8.051  1.00 17.76  ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 22.317 21.521  7.830  1.00 19.13  ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 21.367 21.561  9.031  1.00 18.60  ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 20.549 22.474  9.131  1.00 19.03  ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 21.566 21.215  6.530  1.00 25.42  ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 20.765 19.939  6.588  1.00 36.17  ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 20.011 19.668  5.302  1.00 49.91  ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 18.769 19.510  5.345  1.00 52.33  ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 20.667 19.654  4.235  1.00 55.12  ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 21.482 20.587  9.964  1.00 17.79  ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 20.600 20.483  11.126 1.00 17.65  ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 21.147 21.088  12.386 1.00 16.95  ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 20.377 21.533  13.223 1.00 17.32  ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 20.272 19.017  11.403 1.00 17.90  ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 19.791 18.252  10.194 1.00 19.73  ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 20.621 17.344  9.545  1.00 21.91  ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 18.513 18.441  9.687  1.00 21.03  ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 20.166 16.602  8.461  1.00 23.54  ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 18.060 17.725  8.580  1.00 22.59  ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 18.884 16.799  7.982  1.00 24.37  ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 18.450 16.064  6.898  1.00 28.27  ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 22.458 21.097  12.536 1.00 16.64  ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 23.081 21.621  13.758 1.00 16.13  ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 24.380 22.326  13.441 1.00 17.01  ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 25.100 21.921  12.521 1.00 17.31  ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 23.461 20.460  14.732 1.00 15.22  ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 22.341 19.550  15.178 1.00 14.77  ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 21.387 19.984  16.082 1.00 14.51  ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 22.279 18.237  14.744 1.00 15.28  ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 20.414 19.124  16.572 1.00 14.81  ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 21.278 17.381  15.183 1.00 14.20  ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 20.372 17.814  16.128 1.00 13.94  ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 19.384 16.977  16.585 1.00 13.54  ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 24.760 23.321  14.256 1.00 17.36  ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 26.119 23.894  14.095 1.00 17.77  ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 27.143 22.898  14.672 1.00 18.06  ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 26.770 21.919  15.358 1.00 19.06  ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 26.072 25.169  14.952 1.00 19.13  ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 25.052 24.865  16.020 1.00 19.80  ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 24.040 23.890  15.416 1.00 17.69  ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 28.455 23.141  14.464 1.00 18.27  ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 29.491 22.277  15.054 1.00 18.92  ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 29.333 22.304  16.592 1.00 18.44  ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 29.058 23.363  17.143 1.00 18.99  ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 30.877 22.777  14.646 1.00 19.85  ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 29.332 21.136  17.240 1.00 18.18  ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 29.023 21.080  18.683 1.00 17.60  ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 29.470 19.759  19.297 1.00 17.15  ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 29.834 18.850  18.554 1.00 18.27  ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 27.496 21.252  18.860 1.00 17.13  ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 26.731 19.929  18.534 1.00 18.13  ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 25.334 20.124  18.003 1.00 18.97  ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 24.437 19.028  18.365 1.00 18.70  ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 24.425 17.832  17.792 1.00 17.77  ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 23.524 16.928  18.155 1.00 16.84  ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 25.289 17.543  16.823 1.00 16.56  ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 29.410 19.627  20.632 1.00 16.36  ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 29.642 18.317  21.252 1.00 16.96  ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 28.298 17.641  21.418 1.00 16.58  ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 27.369 18.243  21.959 1.00 18.12  ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 30.304 18.421  22.627 1.00 17.94  ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 31.750 18.836  22.555 1.00 19.49  ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 32.760 17.894  22.477 1.00 20.99  ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 32.104 20.178  22.565 1.00 21.22  ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 34.092 18.272  22.393 1.00 22.79  ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 33.426 20.573  22.458 1.00 22.91  ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 34.423 19.618  22.395 1.00 24.31  ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? 35.723 20.071  22.333 1.00 28.01  ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 28.166 16.436  20.884 1.00 15.63  ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 26.937 15.669  21.064 1.00 14.20  ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 27.194 14.752  22.287 1.00 14.37  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 28.229 14.079  22.342 1.00 15.74  ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 26.588 14.843  19.802 1.00 14.09  ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 25.341 13.948  20.019 1.00 13.56  ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 24.716 13.463  18.741 1.00 15.28  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 24.616 14.203  17.746 1.00 15.17  ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 24.219 12.210  18.762 1.00 13.58  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 26.299 14.741  23.263 1.00 13.39  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 26.466 13.914  24.473 1.00 13.79  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 25.802 12.537  24.316 1.00 14.51  ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 24.978 12.351  23.410 1.00 15.40  ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 25.886 14.647  25.681 1.00 15.87  ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 24.507 14.930  25.478 1.00 17.29  ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 26.159 11.581  25.201 1.00 13.53  ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 25.583 10.235  25.254 1.00 13.40  ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 25.772 9.478   23.908 1.00 13.40  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 24.914 8.673   23.532 1.00 14.01  ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 24.090 10.313  25.652 1.00 14.19  ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 23.871 10.920  27.017 1.00 16.04  ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 23.721 10.119  28.148 1.00 18.30  ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 23.776 12.224  27.388 1.00 15.78  ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 23.565 10.965  29.168 1.00 18.05  ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 23.599 12.244  28.755 1.00 17.35  ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 26.879 9.772   23.182 1.00 12.97  ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 27.142 9.169   21.866 1.00 12.05  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 28.185 8.043   22.002 1.00 12.56  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 29.152 8.182   22.743 1.00 12.70  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 27.715 10.271  20.932 1.00 12.29  ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 27.895 9.921   19.447 1.00 14.79  ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 26.572 9.467   18.796 1.00 16.68  ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 28.454 11.187  18.677 1.00 16.66  ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 27.950 6.932   21.302 1.00 11.58  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 28.813 5.735   21.331 1.00 13.18  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 29.363 5.509   19.938 1.00 14.24  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 28.582 5.410   19.009 1.00 15.02  ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 27.963 4.524   21.754 1.00 13.92  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 27.420 4.685   23.183 1.00 15.67  ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 26.276 3.392   23.698 1.00 16.46  ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 24.950 3.599   22.547 1.00 18.65  ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 30.694 5.431   19.760 1.00 13.37  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 31.261 5.236   18.420 1.00 13.99  ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 31.711 3.787   18.195 1.00 13.88  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 32.172 3.106   19.111 1.00 14.05  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 32.517 6.122   18.237 1.00 16.00  ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 32.304 7.627   18.127 1.00 21.21  ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 33.606 8.341   17.648 1.00 22.94  ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 31.200 7.990   17.141 1.00 22.70  ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 31.670 3.384   16.951 1.00 13.20  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 32.108 2.045   16.546 1.00 13.20  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 32.626 2.070   15.114 1.00 12.81  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 32.302 2.987   14.363 1.00 13.15  ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 30.926 1.078   16.620 1.00 14.23  ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 33.443 1.070   14.742 1.00 12.50  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 33.865 0.945   13.357 1.00 13.94  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 32.755 0.159   12.650 1.00 15.00  ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 32.402 -0.946  13.058 1.00 15.80  ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? 35.229 0.220   13.295 1.00 15.60  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? 35.651 -0.063  11.842 1.00 15.90  ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? 36.271 1.067   14.017 1.00 17.08  ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 32.230 0.733   11.581 1.00 14.90  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 31.144 0.152   10.802 1.00 15.11  ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 30.687 1.153   9.757  1.00 15.20  ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 30.936 2.357   9.877  1.00 16.08  ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 30.109 0.664   8.679  1.00 14.29  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 29.601 1.500   7.603  1.00 14.41  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 28.338 2.245   7.991  1.00 13.90  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 27.421 1.676   8.597  1.00 14.97  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 29.315 0.649   6.360  1.00 14.82  ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 28.774 1.458   5.212  1.00 14.85  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 29.574 2.358   4.531  1.00 17.00  ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 27.505 1.527   4.719  1.00 16.18  ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 28.784 2.929   3.628  1.00 17.85  ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 27.530 2.447   3.694  1.00 17.63  ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 28.246 3.511   7.572  1.00 13.48  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 27.043 4.316   7.762  1.00 13.09  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 27.067 5.493   6.774  1.00 14.58  ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 28.151 6.007   6.419  1.00 16.11  ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 26.896 4.817   9.194  1.00 15.24  ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 27.870 5.795   9.515  1.00 19.08  ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 25.885 5.849   6.279  1.00 13.78  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 25.594 6.971   5.403  1.00 14.42  ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 24.463 7.791   6.079  1.00 15.95  ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 23.791 7.285   6.982  1.00 16.74  ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 25.175 6.476   3.996  1.00 15.99  ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 26.294 5.714   3.300  1.00 20.14  ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 25.956 5.086   1.956  1.00 21.77  ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 25.220 5.718   1.161  1.00 21.11  ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 26.431 3.957   1.696  1.00 22.86  ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 24.241 9.066   5.686  1.00 16.20  ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 23.237 9.890   6.417  1.00 16.30  ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 21.850 9.261   6.613  1.00 16.74  ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 21.292 9.338   7.718  1.00 17.19  ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 23.174 11.176  5.599  1.00 17.04  ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 24.606 11.302  5.032  1.00 17.59  ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 25.007 9.854   4.699  1.00 16.17  ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 21.351 8.580   5.579  1.00 16.39  ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 20.052 7.900   5.612  1.00 16.06  ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 19.987 6.707   6.557  1.00 14.87  ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 18.901 6.175   6.819  1.00 15.23  ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 21.153 6.253   7.091  1.00 14.26  ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 21.170 5.176   8.070  1.00 13.67  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 20.703 5.612   9.471  1.00 13.00  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 20.428 4.740   10.325 1.00 12.94  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 22.582 4.545   8.167  1.00 13.38  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 22.883 3.728   6.927  1.00 13.67  ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 21.955 3.128   6.382  1.00 14.64  ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 24.064 3.698   6.498  1.00 13.92  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 20.586 6.926   9.727  1.00 13.27  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 20.140 7.409   11.039 1.00 12.74  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 18.791 6.788   11.430 1.00 12.71  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.903 6.718   10.576 1.00 13.70  ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 20.062 8.937   11.063 1.00 13.20  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 21.684 9.746   11.195 1.00 15.22  ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 18.666 6.318   12.661 1.00 11.51  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.421 5.672   13.087 1.00 12.58  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.513 4.159   13.150 1.00 13.59  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 16.654 3.516   13.756 1.00 13.52  ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 18.534 3.569   12.504 1.00 13.37  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 18.739 2.114   12.587 1.00 13.39  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 19.020 1.714   14.025 1.00 12.73  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 19.766 2.401   14.714 1.00 12.60  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 18.400 0.622   14.498 1.00 12.44  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 18.568 0.199   15.874 1.00 12.25  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 19.876 -0.560  16.123 1.00 12.12  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 20.251 -1.419  15.314 1.00 12.72  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.315 -0.647  16.282 1.00 14.16  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 16.159 0.314   16.602 1.00 15.83  ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.581 -1.579  17.466 1.00 14.10  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 14.765 -0.445  16.881 1.00 17.84  ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 20.504 -0.290  17.286 1.00 11.54  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 21.613 -1.063  17.840 1.00 11.65  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 20.991 -1.891  18.999 1.00 12.83  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 20.293 -1.306  19.845 1.00 13.69  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 22.691 -0.108  18.415 1.00 12.48  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 23.812 -0.787  19.230 1.00 13.73  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 24.641 -1.761  18.359 1.00 14.00  ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 24.732 0.275   19.881 1.00 15.15  ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 21.218 -3.213  19.032 1.00 12.79  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 20.679 -4.100  20.059 1.00 14.04  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 21.771 -4.965  20.626 1.00 14.47  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 22.620 -5.468  19.881 1.00 14.98  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 19.680 -5.102  19.441 1.00 17.20  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 18.504 -4.546  18.703 1.00 22.80  ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.611 -5.699  18.232 1.00 24.90  ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 16.933 -6.226  19.405 1.00 25.83  ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 15.748 -5.813  19.828 1.00 25.12  ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 15.027 -4.976  19.092 1.00 22.81  ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 15.257 -6.260  20.975 1.00 23.70  ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 21.649 -5.298  21.903 1.00 14.16  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 22.495 -6.324  22.517 1.00 14.85  ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 21.531 -7.465  22.966 1.00 15.46  ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 20.326 -7.399  22.713 1.00 16.48  ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 23.239 -5.734  23.708 1.00 16.32  ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 22.126 -5.203  25.026 1.00 15.45  ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 22.054 -8.501  23.652 1.00 16.44  ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 21.215 -9.598  24.154 1.00 17.55  ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 20.140 -9.143  25.144 1.00 17.92  ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 19.200 -9.911  25.395 1.00 18.64  ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 22.061 -10.694 24.834 1.00 19.16  ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 22.845 -10.147 26.021 1.00 25.76  ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 23.801 -11.173 26.574 1.00 33.06  ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 25.028 -11.071 26.421 1.00 35.56  ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 23.254 -12.178 27.235 1.00 32.80  ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 20.246 -7.917  25.704 1.00 17.00  ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 19.274 -7.426  26.697 1.00 16.03  ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 18.157 -6.573  26.109 1.00 15.54  ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.157 -6.336  26.805 1.00 16.13  ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 19.971 -6.641  27.846 1.00 16.70  ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 21.104 -7.395  28.487 1.00 18.94  ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 22.435 -7.080  28.225 1.00 19.74  ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 21.072 -8.451  29.340 1.00 20.33  ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 23.166 -7.938  28.920 1.00 21.41  ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 22.395 -8.789  29.608 1.00 21.50  ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 18.317 -6.127  24.856 1.00 14.04  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.311 -5.308  24.206 1.00 14.28  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 17.916 -4.168  23.418 1.00 13.74  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 19.098 -4.203  23.062 1.00 14.46  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.102 -3.154  23.146 1.00 12.04  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.527 -1.993  22.366 1.00 12.38  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 18.483 -1.102  23.167 1.00 12.95  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 18.161 -0.740  24.307 1.00 13.96  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 16.293 -1.184  21.919 1.00 13.73  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 16.728 0.122   21.222 1.00 14.36  ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 15.424 -2.027  20.989 1.00 14.44  ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 19.665 -0.782  22.578 1.00 12.66  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 20.680 0.052   23.214 1.00 13.12  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 20.579 1.526   22.775 1.00 13.96  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 20.816 2.447   23.573 1.00 14.13  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 22.074 -0.521  22.856 1.00 13.22  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 23.201 0.410   23.297 1.00 14.20  ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 22.265 -1.909  23.453 1.00 13.34  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 20.334 1.725   21.479 1.00 12.17  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 20.292 3.079   20.928 1.00 11.98  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 19.993 3.105   19.440 1.00 12.50  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 19.642 2.079   18.852 1.00 12.84  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 20.127 4.293   18.804 1.00 11.96  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 19.874 4.384   17.354 1.00 12.39  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 21.037 5.068   16.642 1.00 11.72  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 21.690 5.921   17.221 1.00 11.45  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 18.548 5.144   17.062 1.00 12.61  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 18.488 6.496   17.776 1.00 13.08  ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.329 4.291   17.410 1.00 13.68  ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.273 7.379   17.241 1.00 15.64  ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 21.257 4.757   15.354 1.00 10.49  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 22.311 5.435   14.580 1.00 9.67   ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 22.038 6.958   14.560 1.00 10.85  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 20.896 7.364   14.374 1.00 11.44  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 22.388 4.878   13.144 1.00 10.88  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 23.386 5.689   12.317 1.00 11.84  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 22.779 3.386   13.154 1.00 11.40  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 23.074 7.771   14.807 1.00 11.46  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 22.898 9.217   14.858 1.00 12.08  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 24.029 9.959   14.122 1.00 13.01  ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 23.812 11.075  13.674 1.00 13.83  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 22.816 9.663   16.321 1.00 12.70  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 22.745 11.075  16.470 1.00 13.87  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 25.234 9.371   14.019 1.00 12.78  ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 26.340 10.032  13.289 1.00 13.56  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 27.125 8.961   12.462 1.00 14.17  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 26.898 7.754   12.624 1.00 13.88  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 27.328 10.771  14.276 1.00 15.54  ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 28.099 9.772   14.962 1.00 15.87  ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 26.642 11.740  15.255 1.00 15.30  ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 28.079 9.415   11.646 1.00 14.39  ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 28.960 8.487   10.952 1.00 15.79  ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 29.897 9.173   9.986  1.00 16.00  ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 29.848 10.396  9.843  1.00 15.82  ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 30.692 8.357   9.306  1.00 15.94  ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 31.542 8.785   8.209  1.00 16.47  ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 32.868 8.090   8.227  1.00 16.72  ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 33.315 7.670   9.297  1.00 16.05  ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 33.471 7.902   7.039  1.00 17.23  ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 34.806 7.318   6.917  1.00 17.99  ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 34.980 5.988   7.641  1.00 16.88  ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? 36.044 5.738   8.215  1.00 18.17  ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? 35.861 8.343   7.373  1.00 21.42  ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? 35.779 9.625   6.570  1.00 27.11  ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? 35.866 9.597   5.346  1.00 28.52  ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? 35.600 10.777  7.235  1.00 29.34  ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 33.953 5.138   7.608  1.00 15.27  ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 34.058 3.823   8.249  1.00 14.70  ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 33.725 3.796   9.722  1.00 15.65  ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 33.888 2.743   10.368 1.00 17.13  ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 33.175 4.906   10.255 1.00 14.27  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 32.696 4.946   11.637 1.00 14.20  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 31.161 5.026   11.653 1.00 13.41  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 30.550 5.485   10.690 1.00 13.78  ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 33.254 6.181   12.368 1.00 14.89  ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 34.768 6.147   12.578 1.00 17.44  ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? 35.314 7.525   12.972 1.00 19.50  ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? 35.131 5.109   13.683 1.00 17.65  ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 30.561 4.611   12.767 1.00 12.22  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 29.136 4.767   12.991 1.00 12.22  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 28.927 5.151   14.470 1.00 12.91  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 29.603 4.598   15.328 1.00 13.69  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 28.326 3.526   12.566 1.00 12.00  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 28.847 2.245   13.224 1.00 13.24  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 26.836 3.739   12.799 1.00 12.41  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 28.125 6.190   14.730 1.00 11.17  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 27.870 6.656   16.088 1.00 11.16  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 26.416 6.454   16.452 1.00 12.10  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 25.533 6.629   15.603 1.00 11.87  ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 26.171 6.020   17.695 1.00 12.32  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 24.825 5.675   18.171 1.00 12.31  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 24.455 6.528   19.379 1.00 11.59  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 25.233 6.649   20.336 1.00 11.42  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 24.759 4.188   18.608 1.00 11.43  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 25.284 3.201   17.589 1.00 11.23  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 24.461 2.717   16.582 1.00 11.43  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 26.588 2.718   17.668 1.00 11.68  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 24.932 1.794   15.657 1.00 12.29  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 27.057 1.785   16.735 1.00 12.48  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 26.232 1.351   15.723 1.00 12.03  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 23.234 7.074   19.340 1.00 11.43  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 22.690 7.835   20.454 1.00 12.15  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 22.167 6.797   21.469 1.00 12.37  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 21.259 6.004   21.149 1.00 13.07  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 21.543 8.722   19.975 1.00 12.73  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 22.750 6.776   22.680 1.00 11.44  ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 22.307 5.835   23.720 1.00 12.59  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 20.923 6.197   24.240 1.00 13.26  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 20.583 7.385   24.367 1.00 13.08  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 23.295 5.905   24.892 1.00 14.12  ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 23.075 4.859   25.986 1.00 20.00  ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 22.848 3.693   25.647 1.00 19.19  ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 23.098 5.232   27.188 1.00 23.59  ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 20.125 5.166   24.598 1.00 12.42  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 18.819 5.381   25.231 1.00 12.88  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 18.703 4.585   26.559 1.00 13.29  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.652 4.660   27.190 1.00 12.97  ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.617 5.060   24.320 1.00 14.45  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.594 5.958   23.072 1.00 15.35  ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.552 3.562   23.973 1.00 14.99  ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 19.737 3.810   26.960 1.00 12.88  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 19.634 2.938   28.146 1.00 12.29  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 19.473 3.680   29.450 1.00 14.48  ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 18.946 3.105   30.400 1.00 15.29  ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 20.866 2.007   28.237 1.00 12.26  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 20.994 1.044   27.072 1.00 14.22  ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 22.282 0.269   27.228 1.00 15.18  ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 23.408 1.122   26.877 1.00 14.34  ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 24.662 0.707   26.780 1.00 14.79  ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 24.976 -0.565  27.051 1.00 13.56  ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 25.604 1.536   26.363 1.00 14.86  ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 19.914 4.958   29.510 1.00 14.61  ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 19.772 5.727   30.753 1.00 15.41  ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 18.355 6.317   30.925 1.00 15.80  ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 18.055 6.861   31.992 1.00 16.25  ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 20.794 6.878   30.822 1.00 15.94  ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 20.633 7.896   29.697 1.00 20.78  ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 20.469 7.476   28.540 1.00 19.89  ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 20.673 9.128   29.985 1.00 21.09  ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.516 6.299   29.877 1.00 15.98  ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 16.170 6.897   29.941 1.00 14.91  ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 15.223 5.926   30.614 1.00 15.19  ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 14.439 5.229   29.956 1.00 14.29  ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 15.705 7.261   28.534 1.00 14.58  ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 16.668 8.222   27.778 1.00 15.62  ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 16.215 8.411   26.349 1.00 14.51  ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 16.794 9.571   28.493 1.00 17.38  ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 15.290 5.872   31.950 1.00 16.38  ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 14.510 4.867   32.685 1.00 16.84  ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 13.017 5.010   32.549 1.00 17.20  ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 12.296 4.005   32.653 1.00 17.26  ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 14.918 4.832   34.162 1.00 17.06  ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 16.415 4.741   34.431 1.00 18.87  ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 16.668 4.624   35.937 1.00 19.47  ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.076 3.570   33.661 1.00 19.61  ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 12.539 6.265   32.353 1.00 17.02  ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 11.120 6.562   32.255 1.00 17.69  ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 10.456 5.959   30.986 1.00 18.75  ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 9.224  5.909   30.918 1.00 19.06  ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 10.918 8.080   32.357 1.00 17.65  ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 11.731 8.888   31.379 1.00 17.96  ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 12.972 9.430   31.572 1.00 18.92  ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 11.368 9.195   30.028 1.00 18.08  ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 13.353 10.138  30.458 1.00 19.62  ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 12.390 10.004  29.492 1.00 18.86  ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 10.234 8.949   29.260 1.00 18.68  ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 12.342 10.507  28.194 1.00 19.09  ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 10.169 9.475   27.981 1.00 19.25  ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 11.213 10.250  27.464 1.00 19.60  ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 11.249 5.452   30.008 1.00 18.72  ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 10.656 4.858   28.794 1.00 20.99  ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 9.780  3.638   29.120 1.00 25.48  ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 8.856  3.341   28.365 1.00 25.02  ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 11.741 4.463   27.755 1.00 19.86  ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 12.423 5.619   27.013 1.00 19.03  ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 13.606 5.115   26.114 1.00 19.24  ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 11.421 6.392   26.147 1.00 18.48  ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 10.028 2.985   30.281 1.00 29.68  ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 9.309  1.801   30.762 1.00 34.86  ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 8.471  2.008   31.981 1.00 39.11  ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 7.704  1.103   32.307 1.00 40.57  ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 10.323 0.795   31.290 1.00 39.14  ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 11.142 0.178   30.250 1.00 48.47  ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 10.600 -0.075  29.149 1.00 50.95  ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 12.325 -0.062  30.515 1.00 52.41  ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 8.850  2.982   32.817 1.00 41.19  ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 8.233  3.118   34.123 1.00 43.68  ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 7.270  4.270   34.222 1.00 45.19  ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 6.207  4.099   34.827 1.00 46.41  ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 9.306  3.186   35.214 1.00 46.91  ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 10.087 4.487   35.267 1.00 52.94  ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 11.329 4.402   36.135 1.00 61.32  ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 11.753 5.455   36.666 1.00 63.43  ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 11.876 3.283   36.289 1.00 63.13  ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 19.415 -24.634 24.027 1.00 22.33  ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 20.559 -24.505 23.107 1.00 21.78  ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 20.590 -25.677 22.100 1.00 21.26  ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 19.924 -26.709 22.311 1.00 22.16  ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 21.872 -24.462 23.892 1.00 24.10  ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 22.073 -25.704 24.550 1.00 29.05  ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 21.354 -25.507 21.022 1.00 19.31  ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 21.513 -26.534 20.003 1.00 18.33  ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 21.738 -25.964 18.615 1.00 17.51  ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 21.380 -24.811 18.337 1.00 17.84  ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 22.364 -26.749 17.739 1.00 16.05  ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 22.667 -26.276 16.378 1.00 15.68  ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 22.604 -27.429 15.375 1.00 15.12  ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 22.626 -28.603 15.771 1.00 15.03  ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 24.087 -25.672 16.350 1.00 16.07  ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 22.533 -27.096 14.061 1.00 15.10  ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 22.638 -28.066 12.974 1.00 14.81  ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 24.032 -27.879 12.339 1.00 15.08  ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 24.430 -26.762 12.066 1.00 15.21  ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 21.538 -27.846 11.916 1.00 15.23  ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 20.171 -27.890 12.559 1.00 16.72  ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 21.642 -28.887 10.790 1.00 15.87  ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 19.095 -27.309 11.665 1.00 17.83  ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 24.757 -28.972 12.088 1.00 16.49  ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 26.089 -28.920 11.483 1.00 17.14  ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 26.036 -29.641 10.147 1.00 17.72  ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 25.892 -30.856 10.119 1.00 17.96  ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 27.112 -29.596 12.415 1.00 17.21  ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 27.303 -28.814 13.694 1.00 17.45  ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 28.138 -27.702 13.734 1.00 17.75  ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 26.599 -29.139 14.842 1.00 18.17  ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 28.263 -26.936 14.887 1.00 19.04  ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 26.706 -28.375 15.998 1.00 19.27  ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 27.570 -27.293 16.029 1.00 19.55  ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 27.655 -26.517 17.160 1.00 21.30  ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 26.125 -28.906 9.037  1.00 17.70  ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 26.011 -29.502 7.705  1.00 18.08  ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 27.089 -28.896 6.809  1.00 18.89  ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 27.194 -27.679 6.705  1.00 18.79  ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 24.570 -29.315 7.127  1.00 19.67  ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 24.089 -27.875 7.283  1.00 20.24  ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 24.497 -29.773 5.678  1.00 20.78  ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 27.980 -29.730 6.250  1.00 19.70  ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 29.060 -29.227 5.407  1.00 20.41  ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 29.942 -28.277 6.196  1.00 20.93  ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 30.242 -28.570 7.350  1.00 21.96  ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 30.219 -27.068 5.680  1.00 21.03  ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 30.994 -26.096 6.460  1.00 21.45  ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 30.108 -25.010 7.064  1.00 19.69  ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 30.552 -23.869 7.228  1.00 20.05  ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 32.144 -25.507 5.667  1.00 25.13  ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 33.209 -26.537 5.439  1.00 32.41  ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 33.865 -27.008 6.382  1.00 35.61  ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 33.365 -26.941 4.204  1.00 34.08  ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 28.880 -25.387 7.470  1.00 17.54  ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 27.930 -24.446 8.056  1.00 16.68  ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 27.441 -24.917 9.425  1.00 16.29  ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 27.315 -26.128 9.668  1.00 15.89  ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 26.671 -24.333 7.155  1.00 15.78  ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 26.969 -23.760 5.791  1.00 17.29  ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 27.629 -22.545 5.656  1.00 18.88  ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 26.599 -24.430 4.641  1.00 18.34  ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 27.887 -22.001 4.402  1.00 20.78  ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 26.873 -23.908 3.381  1.00 20.12  ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 27.507 -22.686 3.266  1.00 21.96  ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 27.778 -22.149 2.021  1.00 24.40  ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 27.128 -23.943 10.296 1.00 14.87  ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 26.525 -24.158 11.616 1.00 15.41  ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 25.236 -23.313 11.611 1.00 14.34  ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 25.310 -22.116 11.346 1.00 14.89  ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 27.484 -23.701 12.730 1.00 15.91  ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 26.841 -23.459 14.098 1.00 16.33  ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 27.869 -23.177 15.204 1.00 17.73  ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 27.438 -22.151 16.177 1.00 19.69  ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 26.918 -22.411 17.378 1.00 20.66  ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 26.736 -23.669 17.774 1.00 19.18  ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 26.576 -21.410 18.196 1.00 18.92  ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 24.058 -23.938 11.817 1.00 14.05  ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 22.762 -23.250 11.823 1.00 13.79  ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 22.322 -23.145 13.279 1.00 14.39  ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 22.193 -24.173 13.946 1.00 14.14  ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 21.701 -24.049 11.020 1.00 15.48  ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 20.409 -23.223 10.881 1.00 15.37  ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 22.237 -24.461 9.652  1.00 15.05  ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 22.059 -21.938 13.771 1.00 13.39  ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 21.623 -21.753 15.161 1.00 14.35  ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 20.431 -20.799 15.206 1.00 12.51  ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 20.206 -20.028 14.258 1.00 11.88  ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 22.772 -21.161 16.033 1.00 16.86  ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 23.847 -22.196 16.274 1.00 20.17  ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 23.359 -19.886 15.407 1.00 16.27  ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 19.723 -20.735 16.362 1.00 11.68  ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 18.697 -19.686 16.538 1.00 11.10  ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 19.443 -18.334 16.520 1.00 12.72  ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 20.451 -18.177 17.233 1.00 13.97  ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 18.040 -19.803 17.919 1.00 11.76  ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.213 -21.046 18.065 1.00 14.00  ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 17.679 -22.071 18.575 1.00 14.80  ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 15.971 -20.963 17.625 1.00 12.77  ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 18.974 -17.369 15.706 1.00 12.48  ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 19.651 -16.050 15.631 1.00 11.92  ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 19.774 -15.399 17.018 1.00 12.41  ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 20.818 -14.802 17.312 1.00 13.31  ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 18.911 -15.125 14.665 1.00 12.83  ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 19.659 -13.839 14.275 1.00 13.79  ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 18.691 -12.912 13.540 1.00 13.81  ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 19.289 -11.671 13.003 1.00 13.68  ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 19.436 -10.555 13.701 1.00 15.18  ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 19.131 -10.526 14.994 1.00 15.42  ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 19.901 -9.457  13.118 1.00 15.81  ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 18.736 -15.556 17.874 1.00 12.23  ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 18.805 -14.913 19.200 1.00 12.72  ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 19.842 -15.542 20.156 1.00 14.03  ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 20.197 -14.916 21.170 1.00 15.53  ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.413 -14.807 19.868 1.00 12.85  ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 16.827 -16.087 20.398 1.00 12.85  ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 16.122 -16.966 19.580 1.00 14.04  ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 16.773 -16.543 21.677 1.00 14.72  ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 15.730 -17.969 20.370 1.00 15.91  ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 16.096 -17.763 21.641 1.00 16.30  ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 20.346 -16.733 19.822 1.00 14.16  ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 21.364 -17.423 20.638 1.00 14.59  ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 22.753 -17.405 19.991 1.00 16.03  ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 23.689 -18.021 20.529 1.00 16.29  ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 20.919 -18.888 20.900 1.00 14.15  ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 19.571 -18.986 21.675 1.00 15.03  ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 19.225 -20.460 21.948 1.00 16.22  ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 19.634 -18.199 23.035 1.00 17.06  ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 22.894 -16.728 18.828 1.00 16.13  ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 24.187 -16.665 18.135 1.00 16.96  ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 25.267 -16.030 19.016 1.00 17.06  ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 24.998 -15.079 19.731 1.00 16.83  ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 24.057 -15.888 16.826 1.00 16.36  ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 26.476 -16.585 18.969 1.00 16.70  ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 27.609 -16.093 19.767 1.00 16.90  ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 28.431 -15.013 19.017 1.00 17.21  ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 28.242 -14.810 17.819 1.00 16.34  ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 28.536 -17.286 20.102 1.00 17.48  ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 29.172 -17.724 18.904 1.00 18.06  ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 27.821 -18.424 20.791 1.00 18.51  ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 29.421 -14.393 19.695 1.00 17.73  ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 30.359 -13.458 19.051 1.00 18.03  ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 31.059 -14.151 17.860 1.00 17.67  ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 31.180 -13.563 16.777 1.00 17.92  ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 31.421 -13.006 20.061 1.00 20.70  ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 30.890 -12.134 21.153 1.00 28.22  ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 29.974 -11.123 20.897 1.00 31.78  ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 31.205 -12.111 22.470 1.00 31.23  ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 29.763 -10.522 22.060 1.00 32.75  ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 30.475 -11.084 23.036 1.00 33.00  ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 31.466 -15.423 18.036 1.00 16.99  ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 32.129 -16.157 16.958 1.00 17.60  ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 31.210 -16.385 15.756 1.00 17.83  ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 31.678 -16.294 14.629 1.00 19.08  ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 32.691 -17.492 17.462 1.00 19.47  ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 33.515 -18.209 16.410 1.00 24.90  ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? 34.580 -17.719 16.002 1.00 26.00  ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 33.015 -19.347 15.899 1.00 25.69  ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 29.913 -16.692 15.981 1.00 17.00  ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 28.964 -16.864 14.881 1.00 16.73  ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 28.860 -15.571 14.039 1.00 16.99  ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 28.901 -15.618 12.813 1.00 17.50  ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 27.551 -17.189 15.434 1.00 15.57  ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 27.412 -18.601 15.981 1.00 17.25  ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 28.013 -19.542 15.376 1.00 16.95  ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 26.723 -18.765 17.031 1.00 17.31  ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 28.737 -14.415 14.706 1.00 16.26  ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 28.632 -13.141 14.008 1.00 16.67  ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 29.946 -12.772 13.290 1.00 18.11  ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 29.897 -12.128 12.242 1.00 18.71  ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 28.193 -12.030 14.975 1.00 16.63  ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 26.707 -11.998 15.177 1.00 15.72  ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 26.007 -12.467 16.254 1.00 16.24  ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 25.738 -11.420 14.280 1.00 14.79  ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 24.651 -12.223 16.075 1.00 16.15  ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 24.466 -11.583 14.870 1.00 16.00  ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 25.822 -10.816 13.017 1.00 15.25  ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 23.295 -11.128 14.259 1.00 16.17  ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 24.656 -10.352 12.422 1.00 16.61  ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 23.413 -10.550 13.026 1.00 16.25  ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 31.096 -13.185 13.833 1.00 17.58  ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 32.385 -12.890 13.185 1.00 18.43  ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 32.637 -13.801 11.951 1.00 19.36  ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 33.556 -13.531 11.173 1.00 19.88  ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 33.521 -13.063 14.182 1.00 18.59  ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 31.876 -14.916 11.832 1.00 17.85  ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 31.991 -15.864 10.721 1.00 18.50  ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 30.626 -15.998 10.026 1.00 18.52  ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 30.249 -17.071 9.572  1.00 18.06  ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 32.500 -17.210 11.241 1.00 20.01  ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 33.931 -17.103 11.734 1.00 24.04  ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? 34.893 -17.009 10.939 1.00 24.49  ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 34.107 -17.064 13.059 1.00 23.95  ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 29.898 -14.880 9.926  1.00 17.85  ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 28.541 -14.835 9.390  1.00 17.91  ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 28.438 -15.211 7.923  1.00 17.91  ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 29.179 -14.676 7.099  1.00 19.60  ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 27.982 -13.409 9.597  1.00 17.78  ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 26.545 -13.168 9.089  1.00 18.21  ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 25.534 -14.026 9.879  1.00 19.67  ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 26.174 -11.676 9.213  1.00 18.21  ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 27.476 -16.092 7.580  1.00 16.74  ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 27.184 -16.444 6.191  1.00 17.32  ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 25.845 -15.814 5.774  1.00 17.83  ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 25.736 -15.184 4.717  1.00 19.32  ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 27.151 -17.979 6.006  1.00 17.84  ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 26.608 -18.362 4.620  1.00 18.28  ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 28.546 -18.579 6.253  1.00 18.42  ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 24.845 -15.931 6.637  1.00 16.22  ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 23.496 -15.443 6.369  1.00 16.40  ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 22.717 -15.373 7.676  1.00 16.57  ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 22.911 -16.207 8.550  1.00 15.99  ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 22.777 -16.428 5.400  1.00 16.21  ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 21.289 -16.213 5.213  1.00 17.64  ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 20.679 -15.305 4.389  1.00 19.25  ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 20.223 -16.943 5.860  1.00 17.37  ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 19.300 -15.443 4.468  1.00 19.72  ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 19.001 -16.456 5.345  1.00 18.61  ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 20.186 -17.998 6.786  1.00 17.56  ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 17.757 -16.960 5.763  1.00 18.67  ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 18.961 -18.509 7.170  1.00 17.91  ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 17.765 -17.997 6.665  1.00 18.30  ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 21.841 -14.375 7.812  1.00 16.27  ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 20.957 -14.293 8.969  1.00 16.41  ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 19.629 -13.678 8.563  1.00 16.39  ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 19.572 -12.875 7.611  1.00 16.76  ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 21.591 -13.551 10.165 1.00 17.34  ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 22.170 -12.178 9.851  1.00 17.78  ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 21.186 -11.028 9.734  1.00 21.01  ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 21.476 -10.080 8.968  1.00 22.35  ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 20.126 -11.055 10.405 1.00 18.74  ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 18.561 -14.039 9.277  1.00 15.35  ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.244 -13.490 8.981  1.00 15.25  ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 16.448 -13.389 10.299 1.00 14.32  ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 16.025 -14.405 10.851 1.00 14.13  ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 16.553 -14.366 7.930  1.00 16.96  ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 15.228 -13.868 7.396  1.00 22.59  ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 14.543 -13.123 8.108  1.00 24.47  ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 14.863 -14.256 6.267  1.00 23.57  ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 16.276 -12.149 10.820 1.00 13.20  ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 15.529 -11.913 12.056 0.50 13.93  ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 15.553 -11.969 12.072 0.50 14.03  ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 14.093 -12.409 11.930 1.00 14.83  ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 13.529 -12.882 12.906 1.00 16.38  ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 15.465 -10.417 12.385 0.50 15.35  ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 15.608 -10.513 12.540 0.50 16.01  ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 16.754 -9.869  12.587 0.50 17.48  ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 15.024 -9.668  11.565 0.50 18.31  ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 13.495 -12.257 10.726 1.00 14.55  ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 12.090 -12.687 10.567 1.00 14.90  ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 11.911 -14.206 10.732 1.00 14.33  ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 10.790 -14.630 11.030 1.00 14.18  ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 11.499 -12.207 9.245  1.00 17.61  ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 11.920 -13.013 8.153  1.00 22.27  ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 12.986 -15.000 10.559 1.00 13.21  ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 12.943 -16.471 10.733 1.00 13.22  ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 13.588 -16.950 12.046 1.00 13.04  ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 13.569 -18.160 12.330 1.00 13.20  ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 13.664 -17.153 9.547  1.00 14.25  ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 12.964 -16.900 8.201  1.00 14.15  ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 13.703 -17.547 7.027  1.00 14.51  ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 13.708 -19.000 7.135  1.00 13.59  ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 13.767 -19.835 6.096  1.00 15.59  ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 13.791 -19.361 4.847  1.00 15.85  ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 13.714 -21.152 6.293  1.00 15.41  ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 14.232 -16.046 12.800 1.00 13.05  ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 15.047 -16.379 13.983 1.00 12.48  ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 16.175 -17.363 13.599 1.00 12.56  ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 16.515 -18.224 14.402 1.00 12.34  ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 14.209 -16.962 15.163 1.00 12.46  ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 15.025 -17.238 16.435 1.00 14.62  ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 15.861 -16.391 16.803 1.00 14.88  ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 14.807 -18.306 17.083 1.00 14.96  ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 16.803 -17.222 12.392 1.00 12.29  ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 17.924 -18.099 12.001 1.00 12.50  ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 19.198 -17.310 11.711 1.00 12.98  ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 19.162 -16.210 11.163 1.00 13.53  ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 17.587 -18.898 10.723 1.00 12.65  ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 16.541 -20.004 10.840 1.00 13.40  ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 16.393 -20.710 9.469  1.00 13.87  ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 16.907 -21.041 11.903 1.00 14.69  ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 20.329 -17.955 11.979 1.00 12.19  ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 21.639 -17.410 11.630 1.00 12.78  ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 22.514 -18.613 11.243 1.00 13.10  ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 22.439 -19.678 11.862 1.00 13.33  ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 22.270 -16.610 12.784 1.00 12.95  ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 23.672 -15.987 12.486 1.00 13.39  ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 23.866 -14.662 13.215 1.00 13.79  ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 24.844 -16.953 12.855 1.00 14.27  ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 23.324 -18.439 10.201 1.00 12.25  ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 24.239 -19.476 9.714  1.00 12.77  ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 25.643 -18.875 9.707  1.00 13.84  ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 25.854 -17.761 9.189  1.00 13.86  ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 23.858 -19.992 8.285  1.00 13.23  ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 24.879 -21.007 7.756  1.00 14.70  ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 22.454 -20.611 8.285  1.00 12.65  ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 26.581 -19.593 10.318 1.00 14.08  ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 27.987 -19.211 10.363 1.00 14.53  ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 28.846 -20.317 9.717  1.00 16.36  ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 28.398 -21.471 9.549  1.00 16.50  ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 28.428 -18.944 11.797 1.00 14.85  ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 28.313 -20.102 12.623 1.00 17.04  ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 30.090 -19.959 9.348  1.00 16.95  ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 30.987 -20.934 8.718  1.00 19.10  ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 31.829 -21.677 9.764  1.00 22.07  ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 32.153 -21.115 10.814 1.00 22.95  ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 31.887 -20.240 7.702  1.00 20.95  ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 32.650 -19.234 8.339  1.00 24.35  ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 32.207 -22.940 9.463  1.00 22.97  ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 33.005 -23.749 10.395 1.00 25.26  ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 34.248 -24.290 9.676  1.00 27.87  ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 34.238 -24.399 8.448  1.00 28.46  ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 32.192 -24.981 10.854 1.00 26.70  ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 31.943 -25.811 9.724  1.00 29.22  ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 30.860 -24.621 11.504 1.00 26.89  ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? 35.285 -24.671 10.426 1.00 29.31  ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? 36.469 -25.292 9.824  1.00 31.38  ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? 36.258 -26.820 9.694  1.00 32.58  ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? 36.793 -27.442 8.765  1.00 33.94  ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? 37.735 -24.989 10.639 1.00 33.73  ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? 37.479 -25.299 12.011 1.00 36.16  ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? 38.173 -23.535 10.524 1.00 34.46  ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? 35.501 -27.430 10.622 1.00 31.51  ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? 35.251 -28.863 10.589 1.00 31.49  ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 34.022 -29.212 9.743  1.00 31.05  ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 33.086 -28.416 9.647  1.00 31.36  ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? 35.087 -29.401 12.005 1.00 32.04  ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 34.015 -30.403 9.151  1.00 29.90  ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 32.924 -30.865 8.297  1.00 29.32  ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 31.758 -31.388 9.130  1.00 27.88  ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 31.953 -32.210 10.021 1.00 28.92  ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 33.434 -31.979 7.364  1.00 31.85  ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 32.358 -32.606 6.473  1.00 37.51  ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 32.058 -31.780 5.233  1.00 44.57  ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 32.762 -30.810 4.896  1.00 47.51  ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 31.012 -32.166 4.512  1.00 45.12  ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 30.559 -30.912 8.835  1.00 25.20  ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 29.360 -31.345 9.538  1.00 24.02  ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 28.703 -32.484 8.795  1.00 22.65  ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 28.702 -32.509 7.558  1.00 23.56  ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 28.101 -33.406 9.550  1.00 20.54  ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 27.514 -34.599 8.972  1.00 20.67  ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 26.015 -34.717 9.136  1.00 19.37  ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 25.502 -35.823 8.962  1.00 20.04  ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 28.215 -35.837 9.505  1.00 22.82  ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 29.989 -35.854 9.175  1.00 26.75  ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 25.302 -33.643 9.524  1.00 17.07  ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 23.830 -33.731 9.613  1.00 16.78  ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 23.244 -33.747 8.196  1.00 18.75  ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 23.744 -33.048 7.302  1.00 20.10  ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 23.207 -32.546 10.407 1.00 16.31  ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 23.456 -32.596 11.904 1.00 21.68  ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 23.719 -33.707 12.434 1.00 20.75  ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 23.420 -31.527 12.548 1.00 21.32  ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 22.201 -34.539 7.975  1.00 18.23  ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 21.534 -34.574 6.671  1.00 18.74  ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 20.313 -33.685 6.773  1.00 17.04  ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 19.562 -33.852 7.720  1.00 17.56  ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 21.067 -36.014 6.354  1.00 22.46  ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 22.235 -36.794 6.025  1.00 25.67  ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 20.068 -36.078 5.168  1.00 23.78  ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 20.066 -32.794 5.786  1.00 15.94  ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 18.887 -31.940 5.830  1.00 15.37  ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 17.752 -32.613 5.035  1.00 15.12  ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 17.980 -33.070 3.897  1.00 15.68  ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 19.162 -30.529 5.231  1.00 16.96  ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 20.379 -29.850 5.888  1.00 18.61  ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 17.902 -29.621 5.372  1.00 17.05  ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 20.221 -29.602 7.419  1.00 20.50  ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 16.551 -32.672 5.610  1.00 14.01  ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 15.403 -33.225 4.900  1.00 13.98  ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 14.990 -32.302 3.757  1.00 13.02  ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 15.004 -31.089 3.930  1.00 13.41  ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 14.233 -33.345 5.853  1.00 13.60  ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 14.566 -32.874 2.619  1.00 12.92  ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 14.060 -32.129 1.447  1.00 12.75  ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 12.721 -32.789 1.150  1.00 13.43  ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 12.655 -33.793 0.420  1.00 14.17  ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 15.057 -32.248 0.282  1.00 13.48  ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 16.446 -31.716 0.609  1.00 14.39  ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 16.482 -30.217 0.991  1.00 13.30  ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 17.883 -29.807 1.215  1.00 14.49  ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 18.258 -28.710 1.854  1.00 16.95  ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.353 -27.860 2.310  1.00 15.86  ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 19.550 -28.438 2.022  1.00 17.73  ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 11.651 -32.287 1.810  1.00 13.43  ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 10.351 -32.958 1.810  1.00 13.53  ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 9.233  -32.008 2.304  1.00 15.34  ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 9.511  -30.883 2.733  1.00 15.31  ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 10.448 -34.161 2.752  1.00 13.94  ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 10.627 -33.676 4.499  1.00 13.65  ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 7.980  -32.521 2.343  1.00 15.02  ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 6.855  -31.793 2.918  1.00 15.80  ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 6.236  -32.615 4.070  1.00 15.52  ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 5.027  -32.553 4.304  1.00 15.14  ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 5.816  -31.411 1.870  1.00 18.49  ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 5.112  -32.563 1.200  1.00 22.11  ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 5.442  -33.740 1.514  1.00 21.42  ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 4.224  -32.302 0.365  1.00 25.31  ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 7.059  -33.373 4.821  1.00 14.34  ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 6.576  -34.127 5.987  1.00 13.60  ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 5.899  -33.213 6.975  1.00 12.58  ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 6.303  -32.057 7.142  1.00 12.12  ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 7.716  -34.855 6.688  1.00 15.02  ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 8.281  -36.350 5.846  1.00 16.77  ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 4.912  -33.777 7.676  1.00 11.25  ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 4.215  -33.135 8.782  1.00 11.86  ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 4.224  -34.035 10.041 1.00 12.81  ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 3.415  -33.809 10.938 1.00 12.91  ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 2.775  -32.739 8.415  1.00 12.68  ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 2.751  -31.476 7.522  1.00 13.05  ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 1.324  -31.069 7.266  1.00 16.50  ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 0.797  -31.211 6.139  1.00 17.73  ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 0.666  -30.581 8.313  1.00 15.88  ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 5.110  -35.047 10.108 1.00 13.69  ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 5.233  -35.888 11.303 1.00 15.46  ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 6.751  -36.084 11.520 1.00 15.21  ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 7.548  -36.173 10.560 1.00 15.63  ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 4.469  -37.242 11.197 1.00 20.16  ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 5.134  -38.084 10.246 1.00 23.29  ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 3.008  -37.082 10.751 1.00 21.13  ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 7.152  -36.060 12.781 1.00 13.44  ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 8.576  -36.152 13.107 1.00 12.64  ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 8.811  -36.333 14.581 1.00 11.91  ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 7.876  -36.615 15.316 1.00 13.63  ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 10.062 -36.186 15.008 1.00 11.05  ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 10.417 -36.352 16.426 1.00 11.44  ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 11.303 -35.166 16.808 1.00 11.51  ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 12.253 -34.867 16.079 1.00 11.87  ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 11.187 -37.691 16.629 1.00 12.34  ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 11.652 -37.838 18.084 1.00 13.11  ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 10.325 -38.889 16.232 1.00 12.69  ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 11.052 -34.529 17.978 1.00 11.46  ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 11.945 -33.428 18.398 1.00 12.23  ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 12.585 -33.700 19.735 1.00 12.26  ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 12.013 -34.434 20.537 1.00 12.18  ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 11.261 -32.022 18.390 1.00 12.81  ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 10.342 -31.775 19.565 1.00 12.90  ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 9.071  -32.327 19.605 1.00 14.76  ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 10.714 -30.917 20.597 1.00 13.51  ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 8.193  -32.054 20.658 1.00 15.35  ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 9.866  -30.679 21.683 1.00 13.86  ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 8.598  -31.232 21.696 1.00 15.49  ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 7.753  -30.943 22.734 1.00 17.26  ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 13.769 -33.090 19.983 1.00 12.23  ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 14.403 -33.241 21.269 1.00 12.11  ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 13.970 -32.073 22.174 1.00 12.64  ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 14.111 -30.901 21.794 1.00 13.26  ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 15.936 -33.267 21.154 1.00 12.68  ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 16.585 -33.414 22.515 1.00 13.99  ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 16.428 -34.577 23.261 1.00 15.62  ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.302 -32.368 23.081 1.00 16.18  ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 16.993 -34.710 24.527 1.00 17.16  ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 17.883 -32.493 24.340 1.00 17.02  ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 17.713 -33.662 25.065 1.00 18.75  ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 18.266 -33.787 26.318 1.00 21.91  ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 13.502 -32.414 23.381 1.00 12.76  ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 13.058 -31.439 24.393 1.00 13.43  ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 14.041 -31.485 25.594 1.00 14.88  ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 13.975 -32.409 26.424 1.00 15.90  ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 11.625 -31.746 24.814 1.00 14.34  ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 11.024 -30.729 26.197 1.00 15.96  ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 14.977 -30.514 25.661 1.00 14.70  ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 15.975 -30.531 26.735 1.00 16.42  ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 15.397 -30.358 28.127 1.00 16.39  ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 15.923 -30.958 29.072 1.00 17.26  ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 17.101 -29.526 26.504 1.00 21.10  ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 16.550 -28.235 26.467 1.00 26.66  ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 14.271 -29.640 28.267 1.00 15.81  ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 13.660 -29.451 29.607 1.00 16.55  ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 12.979 -30.700 30.191 1.00 17.44  ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 12.519 -30.701 31.350 1.00 18.28  ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 12.691 -28.280 29.582 1.00 16.98  ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 11.598 -28.561 28.732 1.00 18.24  ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 12.903 -31.773 29.394 1.00 16.19  ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 12.398 -33.073 29.835 1.00 15.92  ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 13.457 -34.183 29.577 1.00 16.20  ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 13.196 -35.347 29.875 1.00 16.57  ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 11.110 -33.391 29.070 1.00 17.16  ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 9.942  -32.483 29.432 1.00 18.05  ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 9.381  -32.836 30.800 1.00 20.54  ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 8.263  -31.968 31.174 1.00 23.86  ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 8.386  -30.805 31.805 1.00 27.14  ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 9.584  -30.361 32.171 1.00 26.65  ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 7.310  -30.082 32.091 1.00 27.08  ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 14.631 -33.832 28.957 1.00 16.68  ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 15.701 -34.763 28.539 1.00 18.90  ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 15.080 -35.926 27.774 1.00 20.38  ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 15.377 -37.085 28.053 1.00 22.15  ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 16.538 -35.242 29.749 1.00 22.61  ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 17.209 -34.145 30.570 1.00 28.35  ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 18.522 -33.565 30.073 1.00 35.28  ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 19.087 -32.636 31.060 1.00 40.00  ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 19.014 -31.312 30.980 1.00 42.13  ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 18.476 -30.733 29.914 1.00 41.35  ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 19.545 -30.553 31.933 1.00 42.86  ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 14.124 -35.612 26.862 1.00 18.89  ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 13.388 -36.655 26.157 1.00 18.42  ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 13.084 -36.220 24.727 1.00 15.32  ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 12.985 -35.021 24.457 1.00 14.41  ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 11.987 -36.855 26.825 1.00 22.09  ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 11.883 -37.924 27.892 1.00 32.77  ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 10.417 -38.061 28.276 1.00 40.20  ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 10.114 -39.279 29.128 1.00 47.08  ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 10.434 -39.054 30.569 1.00 50.02  ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 12.864 -37.191 23.850 1.00 14.93  ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 12.374 -36.958 22.498 1.00 13.82  ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 10.868 -37.203 22.476 1.00 15.62  ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 10.367 -38.135 23.144 1.00 17.01  ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 13.046 -37.887 21.485 1.00 14.50  ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 14.521 -37.670 21.329 1.00 14.84  ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 15.040 -36.934 20.271 1.00 17.97  ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 15.544 -38.128 22.079 1.00 15.39  ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 16.354 -36.971 20.417 1.00 16.31  ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 16.701 -37.653 21.495 1.00 17.60  ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 10.140 -36.416 21.672 1.00 14.11  ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 8.692  -36.604 21.538 1.00 13.77  ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 8.283  -36.693 20.076 1.00 13.62  ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 8.694  -35.848 19.262 1.00 12.93  ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 7.918  -35.429 22.154 1.00 13.96  ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 8.045  -35.315 23.653 1.00 14.80  ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 7.353  -36.174 24.494 1.00 16.47  ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 8.793  -34.295 24.239 1.00 15.21  ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 7.441  -36.058 25.881 1.00 17.97  ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 8.878  -34.167 25.626 1.00 17.10  ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 8.212  -35.061 26.442 1.00 19.48  ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 8.269  -34.915 27.823 1.00 22.75  ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 7.443  -37.680 19.734 1.00 13.64  ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 6.921  -37.751 18.354 1.00 13.18  ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 5.758  -36.748 18.217 1.00 14.83  ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 4.915  -36.677 19.134 1.00 16.08  ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 6.456  -39.224 18.233 1.00 14.19  ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 6.081  -39.604 19.641 1.00 14.77  ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 6.933  -38.781 20.596 1.00 13.24  ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 5.704  -35.961 17.117 1.00 13.78  ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 4.609  -34.972 16.966 1.00 14.12  ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 4.198  -34.822 15.497 1.00 14.15  ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 4.996  -35.083 14.614 1.00 14.83  ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 5.055  -33.557 17.439 1.00 16.05  ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 5.155  -33.457 18.962 1.00 16.87  ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 6.351  -33.108 16.753 1.00 15.86  ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 2.950  -34.362 15.268 1.00 13.54  ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 2.501  -33.864 13.978 1.00 13.55  ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 2.796  -32.325 14.042 1.00 13.06  ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 2.677  -31.691 15.106 1.00 13.43  ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 0.989  -34.051 13.797 1.00 15.44  ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 0.672  -35.425 13.693 1.00 21.41  ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 3.172  -31.741 12.920 1.00 11.28  ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 3.481  -30.311 12.862 1.00 11.66  ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 2.904  -29.662 11.612 1.00 13.04  ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 2.610  -30.372 10.634 1.00 13.92  ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 4.990  -30.023 13.037 1.00 11.71  ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 5.920  -30.755 12.074 1.00 11.12  ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 6.404  -32.020 12.371 1.00 11.10  ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 6.326  -30.159 10.881 1.00 11.93  ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 7.275  -32.680 11.488 1.00 12.07  ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 7.167  -30.822 9.997  1.00 12.58  ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 7.657  -32.073 10.314 1.00 12.57  ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 2.650  -28.328 11.680 1.00 11.66  ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 1.983  -27.614 10.575 1.00 12.39  ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 2.897  -27.276 9.393  1.00 13.39  ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 4.084  -27.618 9.400  1.00 13.70  ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 1.281  -26.369 11.113 1.00 12.49  ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 2.225  -25.404 11.554 1.00 15.67  ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 2.322  -26.663 8.335  1.00 12.78  ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 3.142  -26.263 7.181  1.00 14.45  ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 3.866  -24.951 7.530  1.00 15.57  ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 3.298  -24.116 8.246  1.00 17.80  ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 2.217  -26.048 5.977  1.00 16.81  ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 1.482  -27.341 5.596  1.00 21.37  ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 0.564  -27.121 4.405  1.00 29.48  ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 0.602  -28.332 3.515  1.00 36.87  ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? 2.017  -28.742 3.275  1.00 41.00  ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 5.087  -24.709 7.020  1.00 15.06  ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 5.783  -23.434 7.342  1.00 15.53  ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 4.952  -22.205 6.970  1.00 17.22  ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 4.417  -22.113 5.851  1.00 18.23  ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 7.068  -23.487 6.519  1.00 16.57  ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 7.236  -24.908 6.147  1.00 17.53  ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 5.897  -25.574 6.147  1.00 14.67  ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 4.794  -21.292 7.918  1.00 16.91  ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 3.930  -20.140 7.690  1.00 18.09  ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 4.309  -18.964 8.597  1.00 17.22  ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 5.247  -19.078 9.410  1.00 15.98  ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 2.464  -20.541 7.905  1.00 20.96  ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 2.169  -20.755 9.281  1.00 24.11  ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 3.622  -17.816 8.409  1.00 17.14  ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 3.808  -16.613 9.197  1.00 16.98  ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 2.929  -16.761 10.440 1.00 17.50  ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 1.699  -16.860 10.304 1.00 18.70  ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 3.283  -15.403 8.396  1.00 18.27  ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 4.260  -14.714 7.463  1.00 22.87  ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 3.510  -13.689 6.566  1.00 25.17  ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 5.304  -13.952 8.254  1.00 23.64  ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 3.535  -16.752 11.634 1.00 16.65  ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 2.843  -16.945 12.903 1.00 17.83  ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 3.204  -15.856 13.877 1.00 18.30  ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 4.368  -15.504 13.990 1.00 17.46  ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 3.195  -18.335 13.472 1.00 20.04  ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 2.602  -19.429 12.565 1.00 22.18  ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 2.714  -18.509 14.936 1.00 21.42  ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 2.952  -20.783 12.896 1.00 24.82  ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 2.209  -15.328 14.609 1.00 19.70  ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 2.451  -14.269 15.583 1.00 21.30  ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 3.239  -14.769 16.791 1.00 20.56  ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 2.916  -15.819 17.369 1.00 21.42  ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 1.116  -13.640 16.054 1.00 23.65  ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 1.335  -12.271 16.663 1.00 26.39  ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 1.320  -12.098 18.031 1.00 28.94  ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 1.694  -11.194 15.873 1.00 28.58  ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 1.555  -10.841 18.594 1.00 29.70  ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 1.956  -9.948  16.435 1.00 30.28  ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 1.874  -9.778  17.792 1.00 30.29  ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 4.299  -14.043 17.144 1.00 19.80  ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 5.151  -14.359 18.292 1.00 19.22  ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 5.194  -13.149 19.230 1.00 19.63  ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 5.546  -12.042 18.808 1.00 19.08  ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 6.582  -14.707 17.838 1.00 18.54  ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 7.471  -15.045 19.043 1.00 18.30  ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 6.561  -15.870 16.854 1.00 18.16  ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 4.926  -13.384 20.523 1.00 20.04  ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 4.947  -12.331 21.554 1.00 20.38  ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 6.302  -11.643 21.650 1.00 20.04  ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 7.327  -12.274 21.384 1.00 20.85  ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 4.673  -12.975 22.927 1.00 22.85  ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 3.263  -13.521 23.114 1.00 27.95  ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 2.116  -12.538 23.301 1.00 33.58  ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 0.951  -12.978 23.175 1.00 34.23  ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 2.366  -11.340 23.568 1.00 33.48  ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 6.328  -10.405 22.131 1.00 19.58  ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 7.583  -9.671  22.318 1.00 19.91  ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 8.479  -10.379 23.330 1.00 18.77  ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 8.005  -11.055 24.248 1.00 18.55  ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 7.310  -8.246  22.812 1.00 20.81  ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 9.793  -10.253 23.130 1.00 17.68  ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 10.796 -10.798 24.044 1.00 17.34  ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 11.933 -9.739  24.138 1.00 18.94  ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 11.838 -8.677  23.493 1.00 19.96  ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 11.339 -12.139 23.524 1.00 16.33  ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 12.117 -11.949 22.352 1.00 15.94  ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 12.986 -10.002 24.905 1.00 19.20  ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 14.129 -9.068  24.931 1.00 19.83  ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 14.894 -9.077  23.601 1.00 19.87  ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 15.665 -8.153  23.354 1.00 20.43  ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 15.067 -9.335  26.104 1.00 21.34  ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 15.829 -10.639 25.995 1.00 25.12  ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 15.160 -11.797 26.715 1.00 32.80  ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 15.880 -12.496 27.462 1.00 36.61  ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 13.934 -12.017 26.533 1.00 29.68  ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 14.670 -10.089 22.732 1.00 19.34  ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 15.353 -10.233 21.448 1.00 19.05  ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 14.606 -9.608  20.284 1.00 19.02  ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 15.230 -9.174  19.310 1.00 20.23  ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 15.589 -11.731 21.162 1.00 18.76  ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 16.262 -12.442 22.306 1.00 18.65  ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 17.601 -12.221 22.593 1.00 20.70  ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 15.577 -13.357 23.075 1.00 19.97  ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 18.237 -12.894 23.623 1.00 22.46  ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 16.204 -14.044 24.107 1.00 22.02  ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 17.540 -13.810 24.375 1.00 23.98  ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 18.225 -14.464 25.368 1.00 27.05  ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 13.282 -9.619  20.330 1.00 18.02  ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 12.485 -9.083  19.234 1.00 17.58  ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 11.227 -8.399  19.756 1.00 19.33  ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 10.648 -8.842  20.749 1.00 19.40  ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 12.002 -10.228 18.303 1.00 16.85  ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 13.056 -11.168 17.747 1.00 16.47  ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 13.212 -12.452 18.258 1.00 17.01  ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 13.873 -10.791 16.680 1.00 16.69  ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 14.161 -13.331 17.747 1.00 16.65  ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 14.798 -11.683 16.130 1.00 16.78  ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 14.960 -12.947 16.687 1.00 16.81  ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 15.898 -13.812 16.169 1.00 15.27  ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 10.690 -7.398  19.028 1.00 20.74  ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 9.356  -6.886  19.396 1.00 21.10  ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 8.292  -7.913  18.977 1.00 21.38  ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 8.602  -8.874  18.230 1.00 20.92  ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 9.226  -5.590  18.566 1.00 22.40  ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 10.099 -5.833  17.381 1.00 23.10  ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 11.218 -6.779  17.794 1.00 21.32  ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 7.020  -7.728  19.375 1.00 21.86  ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 5.933  -8.628  18.935 1.00 22.47  ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 5.863  -8.553  17.398 1.00 22.32  ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 6.032  -7.462  16.841 1.00 23.20  ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 4.605  -8.195  19.551 1.00 22.99  ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 5.810  -9.701  16.724 1.00 21.11  ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 5.916  -9.692  15.265 1.00 20.66  ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 5.441  -11.008 14.684 1.00 20.44  ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 5.191  -11.951 15.432 1.00 20.97  ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 7.412  -9.467  14.894 1.00 19.67  ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 8.271  -10.763 15.044 1.00 18.32  ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 9.725  -10.538 15.333 1.00 17.21  ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 10.615 -11.610 14.852 1.00 15.33  ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 10.737 -12.813 15.427 1.00 17.74  ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 11.612 -13.698 14.955 1.00 15.18  ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 9.993  -13.132 16.490 1.00 17.80  ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 5.330  -11.084 13.345 1.00 20.57  ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 5.046  -12.359 12.714 1.00 21.04  ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 6.416  -12.976 12.342 1.00 18.00  ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 7.258  -12.339 11.681 1.00 18.21  ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 4.199  -12.181 11.449 1.00 23.54  ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 2.755  -11.857 11.750 1.00 27.48  ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 1.816  -12.862 11.903 1.00 29.68  ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 2.334  -10.547 11.910 1.00 30.98  ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 0.486  -12.574 12.210 1.00 32.55  ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 1.014  -10.247 12.226 1.00 32.83  ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 0.091  -11.265 12.369 1.00 34.82  ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? -1.234 -11.019 12.662 1.00 39.02  ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 6.649  -14.195 12.804 1.00 14.56  ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 7.883  -14.914 12.447 1.00 13.92  ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 7.519  -15.787 11.242 1.00 14.52  ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 6.475  -16.447 11.257 1.00 15.67  ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 8.372  -15.765 13.645 1.00 14.12  ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 9.597  -16.650 13.271 1.00 15.28  ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 10.352 -17.171 14.475 1.00 17.16  ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 10.573 -16.450 15.462 1.00 16.43  ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 10.826 -18.436 14.384 1.00 14.25  ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 8.326  -15.754 10.182 1.00 12.23  ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 8.040  -16.546 8.976  1.00 13.04  ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 8.699  -17.936 9.020  1.00 13.11  ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 9.591  -18.158 9.845  1.00 13.29  ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 8.498  -15.794 7.726  1.00 14.72  ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 9.899  -15.542 7.779  1.00 16.04  ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 8.236  -18.858 8.148  1.00 12.17  ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 8.770  -20.215 8.008  1.00 12.22  ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 8.683  -21.010 9.331  1.00 14.25  ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 9.552  -21.835 9.620  1.00 14.69  ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 10.225 -20.141 7.470  1.00 11.42  ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 10.321 -19.503 6.104  1.00 14.98  ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 10.312 -20.267 4.948  1.00 17.84  ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 10.380 -18.192 5.759  1.00 16.30  ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 10.384 -19.403 3.936  1.00 17.91  ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 10.435 -18.139 4.375  1.00 17.78  ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 7.652  -20.719 10.153 1.00 14.07  ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 7.498  -21.367 11.465 1.00 13.53  ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 6.423  -22.462 11.393 1.00 14.21  ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 5.403  -22.297 10.718 1.00 14.52  ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 7.087  -20.288 12.508 1.00 13.51  ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 7.026  -20.672 13.973 1.00 15.53  ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 8.407  -21.113 14.478 1.00 16.13  ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 6.597  -19.455 14.811 1.00 17.72  ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 6.654  -23.567 12.094 1.00 13.10  ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 5.695  -24.680 12.105 1.00 13.16  ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 5.339  -24.971 13.548 1.00 13.68  ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 6.229  -24.986 14.401 1.00 14.82  ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 6.344  -25.920 11.474 1.00 13.38  ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 6.773  -25.657 10.046 1.00 16.13  ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 7.814  -26.993 9.426  1.00 17.23  ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 9.268  -26.849 10.465 1.00 14.25  ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 4.062  -25.193 13.832 1.00 12.53  ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 3.641  -25.465 15.215 1.00 12.17  ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 3.244  -26.937 15.445 1.00 13.01  ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 2.723  -27.614 14.548 1.00 12.63  ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 2.427  -24.608 15.626 1.00 12.94  ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 2.613  -23.096 15.617 1.00 14.98  ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 1.310  -22.393 16.162 1.00 16.03  ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 3.811  -22.687 16.467 1.00 17.25  ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 3.454  -27.406 16.676 1.00 12.94  ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 3.027  -28.745 17.127 1.00 13.79  ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 2.481  -28.604 18.563 1.00 13.48  ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 2.823  -27.644 19.263 1.00 13.80  ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 4.201  -29.717 17.148 1.00 14.62  ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 1.640  -29.548 18.994 1.00 13.42  ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 1.176  -29.604 20.375 1.00 13.50  ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 2.267  -30.354 21.137 1.00 15.28  ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 2.496  -31.541 20.880 1.00 15.62  ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? -0.208 -30.323 20.461 1.00 13.81  ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? -0.634 -30.496 21.928 1.00 14.32  ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? -1.258 -29.519 19.681 1.00 14.54  ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 2.969  -29.656 22.020 1.00 15.80  ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 4.041  -30.279 22.777 1.00 17.40  ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 4.686  -29.332 23.762 1.00 17.21  ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 4.452  -28.111 23.734 1.00 17.76  ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 5.474  -29.899 24.664 1.00 16.46  ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 6.105  -29.111 25.700 1.00 16.49  ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 7.355  -28.383 25.207 1.00 16.36  ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 8.192  -28.960 24.506 1.00 16.78  ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 6.463  -29.999 26.903 1.00 17.73  ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 7.112  -29.238 28.012 1.00 20.14  ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 6.392  -28.328 28.779 1.00 22.66  ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 8.414  -29.213 28.401 1.00 20.42  ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 7.269  -27.803 29.630 1.00 22.85  ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 8.499  -28.332 29.454 1.00 22.22  ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 7.510  -27.131 25.648 1.00 15.65  ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 8.715  -26.376 25.392 1.00 16.34  ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 8.843  -25.249 26.413 1.00 17.14  ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 7.836  -24.697 26.869 1.00 17.38  ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 8.747  -25.831 23.961 1.00 18.81  ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 7.799  -24.800 23.781 1.00 24.32  ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 10.094 -24.944 26.773 1.00 15.90  ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 10.497 -23.856 27.660 1.00 16.65  ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 11.609 -23.071 26.912 1.00 16.19  ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 12.177 -23.568 25.918 1.00 14.84  ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 10.994 -24.410 29.016 1.00 18.66  ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 9.886  -25.113 29.787 1.00 21.68  ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 10.293 -25.788 31.089 1.00 27.07  ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 11.106 -25.199 31.829 1.00 30.94  ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 9.789  -26.895 31.379 1.00 26.86  ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 11.930 -21.834 27.319 1.00 16.76  ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 12.909 -21.045 26.528 1.00 16.42  ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 14.244 -21.749 26.218 1.00 16.44  ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 14.760 -21.646 25.084 1.00 16.70  ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 13.101 -19.787 27.374 1.00 17.51  ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 11.743 -19.610 28.041 1.00 18.58  ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 11.324 -21.032 28.398 1.00 17.18  ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 14.789 -22.480 27.204 1.00 15.45  ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 16.049 -23.218 27.053 1.00 16.13  ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 15.993 -24.376 26.062 1.00 15.86  ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 17.028 -24.956 25.706 1.00 15.61  ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 14.776 -24.726 25.601 1.00 14.70  ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 14.605 -25.772 24.592 1.00 14.46  ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 14.977 -25.320 23.176 1.00 13.32  ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 15.119 -26.169 22.281 1.00 13.87  ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 13.151 -26.321 24.610 1.00 15.27  ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 12.912 -27.166 25.856 1.00 17.03  ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 13.864 -27.809 26.324 1.00 17.18  ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 11.786 -27.155 26.375 1.00 16.53  ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 15.118 -23.985 22.943 1.00 12.30  ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 15.449 -23.486 21.597 1.00 13.04  ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 16.730 -24.134 21.078 1.00 13.69  ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 17.674 -24.257 21.841 1.00 14.08  ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 15.568 -21.967 21.618 1.00 14.21  ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 13.960 -21.111 21.667 1.00 17.30  ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 16.734 -24.577 19.820 1.00 12.78  ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 17.902 -25.247 19.275 1.00 12.41  ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 17.779 -26.758 19.187 1.00 13.64  ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 18.550 -27.408 18.468 1.00 14.32  ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 16.795 -27.335 19.900 1.00 12.88  ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 16.553 -28.772 19.809 1.00 12.80  ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 16.130 -29.133 18.391 1.00 12.80  ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 15.344 -28.411 17.785 1.00 12.59  ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 16.650 -30.250 17.857 1.00 12.66  ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 16.347 -30.620 16.476 1.00 13.67  ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 14.996 -31.321 16.339 1.00 12.63  ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 14.646 -32.165 17.181 1.00 13.77  ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.530 -31.476 15.938 1.00 17.16  ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 18.696 -30.536 15.519 1.00 20.41  ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.145 -32.406 14.787 1.00 18.93  ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 20.008 -31.291 15.100 1.00 22.61  ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 14.297 -31.039 15.221 1.00 11.55  ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 13.094 -31.764 14.798 1.00 11.66  ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 13.571 -32.583 13.567 1.00 13.05  ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 14.196 -32.015 12.659 1.00 13.32  ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 11.999 -30.771 14.348 1.00 11.11  ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 10.782 -31.389 13.627 1.00 12.48  ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 9.991  -32.374 14.547 1.00 12.68  ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 9.851  -30.274 13.087 1.00 13.20  ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 13.325 -33.908 13.576 1.00 13.51  ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 13.769 -34.784 12.494 1.00 13.84  ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 12.588 -35.586 11.965 1.00 14.27  ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 11.757 -36.031 12.765 1.00 15.61  ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 14.768 -35.846 13.032 1.00 15.57  ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 16.103 -35.377 13.541 1.00 22.00  ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 17.002 -36.570 13.940 1.00 26.35  ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 17.251 -37.450 12.801 1.00 29.18  ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 18.297 -37.333 11.977 1.00 31.10  ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 19.243 -36.441 12.220 1.00 30.25  ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 18.435 -38.159 10.946 1.00 32.43  ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 12.546 -35.843 10.642 1.00 13.67  ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 11.572 -36.751 10.046 1.00 14.86  ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 12.363 -37.934 9.463  1.00 16.40  ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 13.597 -38.012 9.627  1.00 16.14  ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 10.769 -36.048 8.955  1.00 14.84  ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 11.799 -35.508 7.565  1.00 14.70  ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 11.671 -38.853 8.757  1.00 17.44  ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 12.360 -39.993 8.143  1.00 18.56  ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 13.422 -39.580 7.092  1.00 19.42  ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 14.284 -40.400 6.747  1.00 21.73  ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 11.341 -40.938 7.487  1.00 20.56  ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 10.602 -40.304 6.322  1.00 23.76  ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 9.591  -41.268 5.749  1.00 33.18  ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 8.379  -41.120 5.953  1.00 35.29  ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 10.071 -42.276 5.028  1.00 35.42  ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 13.397 -38.310 6.618  1.00 17.78  ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 14.340 -37.842 5.601  1.00 16.99  ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 15.550 -37.107 6.145  1.00 17.88  ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 16.486 -36.864 5.388  1.00 18.99  ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 13.627 -36.953 4.553  1.00 16.74  ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 12.437 -37.604 3.916  1.00 17.51  ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 11.154 -37.244 4.260  1.00 17.33  ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 12.386 -38.589 2.979  1.00 18.83  ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 10.354 -38.011 3.531  1.00 19.48  ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 11.048 -38.838 2.738  1.00 20.58  ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 15.524 -36.719 7.425  1.00 16.73  ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 16.635 -35.967 7.998  1.00 15.30  ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 16.165 -34.836 8.884  1.00 13.56  ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 15.012 -34.821 9.347  1.00 13.52  ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 17.040 -33.852 9.070  1.00 12.69  ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 16.732 -32.687 9.902  1.00 12.91  ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 15.746 -31.751 9.232  1.00 13.00  ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 15.996 -31.326 8.085  1.00 13.23  ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 18.044 -31.938 10.243 1.00 13.97  ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 17.741 -30.633 10.994 1.00 14.63  ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 18.985 -32.847 11.060 1.00 14.80  ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 14.644 -31.396 9.933  1.00 12.10  ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 13.606 -30.499 9.411  1.00 12.24  ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 13.798 -29.058 9.843  1.00 12.92  ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 13.528 -28.135 9.075  1.00 12.41  ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 12.209 -31.018 9.886  1.00 12.43  ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 11.095 -30.027 9.570  1.00 12.89  ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 11.905 -32.373 9.279  1.00 12.99  ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 14.172 -28.894 11.108 1.00 13.07  ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 14.334 -27.562 11.675 1.00 13.28  ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 14.724 -27.597 13.134 1.00 13.46  ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 15.119 -28.651 13.655 1.00 13.96  ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 14.667 -26.434 13.793 1.00 12.54  ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 15.047 -26.370 15.211 1.00 13.03  ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 13.986 -25.673 16.038 1.00 12.39  ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 13.297 -24.802 15.537 1.00 11.92  ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 16.413 -25.651 15.398 1.00 13.95  ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 16.436 -24.277 14.717 1.00 14.56  ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.578 -26.503 14.923 1.00 15.33  ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 17.723 -23.428 15.120 1.00 15.56  ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 13.865 -26.019 17.349 1.00 11.35  ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 12.899 -25.323 18.217 1.00 11.47  ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 13.216 -23.815 18.249 1.00 11.90  ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 14.378 -23.442 18.365 1.00 12.61  ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 12.927 -25.907 19.657 1.00 12.15  ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 12.038 -25.085 20.571 1.00 11.83  ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 12.495 -27.382 19.642 1.00 13.52  ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 12.190 -22.956 18.107 1.00 12.10  ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 12.408 -21.521 18.073 1.00 11.84  ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 11.396 -20.745 18.929 1.00 13.77  ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 11.711 -19.649 19.405 1.00 14.93  ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 12.395 -21.040 16.622 1.00 12.15  ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 12.469 -19.620 16.509 1.00 13.48  ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 10.193 -21.288 19.144 1.00 13.61  ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 9.184  -20.601 19.977 1.00 14.74  ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 8.420  -21.636 20.836 1.00 14.91  ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 8.523  -22.851 20.619 1.00 14.64  ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 8.150  -19.828 19.093 1.00 16.13  ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 7.274  -20.766 18.439 1.00 16.47  ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 8.777  -18.870 18.083 1.00 16.77  ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 7.618  -21.149 21.774 1.00 16.11  ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 6.739  -22.017 22.544 1.00 17.96  ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 5.844  -21.251 23.484 1.00 18.60  ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 6.024  -20.056 23.685 1.00 17.93  ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 4.867  -21.927 24.033 1.00 20.22  ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 3.920  -21.288 24.951 1.00 21.78  ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 2.541  -21.910 24.842 1.00 22.11  ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 2.182  -22.425 23.786 1.00 20.84  ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 1.785  -21.919 25.961 1.00 22.76  ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 0.435  -22.506 26.031 1.00 23.17  ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 0.356  -23.950 25.485 1.00 21.36  ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? -0.641 -24.314 24.853 1.00 21.48  ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? -0.555 -21.630 25.293 1.00 26.93  ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? -0.630 -20.211 25.762 1.00 34.20  ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? -0.659 -19.920 26.957 1.00 37.14  ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? -0.712 -19.309 24.808 1.00 36.47  ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 1.417  -24.740 25.667 1.00 19.41  ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 1.390  -26.127 25.213 1.00 18.67  ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 1.601  -26.339 23.724 1.00 17.41  ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 1.309  -27.425 23.223 1.00 17.24  ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 2.119  -25.314 23.019 1.00 16.43  ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 2.476  -25.407 21.615 1.00 16.69  ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 3.989  -25.171 21.505 1.00 17.40  ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 4.552  -24.398 22.287 1.00 20.69  ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 1.722  -24.356 20.790 1.00 17.20  ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 0.189  -24.430 20.897 1.00 19.96  ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? -0.437 -23.097 20.516 1.00 22.68  ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? -0.330 -25.512 20.003 1.00 20.55  ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 4.654  -25.841 20.567 1.00 13.50  ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 6.077  -25.656 20.346 1.00 13.38  ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 6.193  -25.273 18.867 1.00 13.80  ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 5.492  -25.827 17.991 1.00 13.76  ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 6.888  -26.930 20.717 1.00 14.47  ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 6.316  -28.195 20.067 1.00 15.55  ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 8.392  -26.771 20.413 1.00 14.23  ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 7.064  -24.302 18.598 1.00 13.22  ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 7.259  -23.852 17.228 1.00 12.81  ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 8.674  -24.132 16.757 1.00 12.53  ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 9.624  -24.011 17.532 1.00 12.48  ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 8.797  -24.569 15.493 1.00 11.59  ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 10.078 -24.944 14.881 1.00 11.74  ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 10.370 -24.081 13.669 1.00 12.52  ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 9.505  -23.889 12.808 1.00 12.65  ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 10.050 -26.413 14.400 1.00 11.68  ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 9.588  -27.403 15.453 1.00 11.49  ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 10.481 -27.929 16.369 1.00 12.50  ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 8.274  -27.843 15.485 1.00 12.05  ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 10.055 -28.852 17.314 1.00 12.76  ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 7.843  -28.744 16.454 1.00 12.53  ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 8.738  -29.244 17.369 1.00 12.41  ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 11.622 -23.571 13.599 1.00 11.53  ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 12.068 -22.802 12.444 1.00 11.56  ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 12.455 -23.810 11.375 1.00 12.69  ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 13.365 -24.621 11.584 1.00 12.49  ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 13.264 -21.934 12.824 1.00 10.94  ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 11.761 -23.773 10.234 1.00 13.08  ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 12.070 -24.685 9.131  1.00 12.93  ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 13.392 -24.365 8.482  1.00 13.00  ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 13.734 -23.191 8.341  1.00 14.12  ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 10.952 -24.560 8.062  1.00 14.09  ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 11.037 -25.579 6.943  1.00 20.32  ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 11.234 -26.759 7.244  1.00 18.51  ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 10.924 -25.177 5.760  1.00 20.65  ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 14.131 -25.406 8.038  1.00 11.83  ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 15.380 -25.209 7.271  1.00 12.42  ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 15.331 -25.975 5.931  1.00 13.05  ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 16.287 -25.911 5.174  1.00 13.86  ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 16.672 -25.576 8.052  1.00 13.24  ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 16.832 -24.700 9.316  1.00 14.53  ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 16.737 -27.088 8.364  1.00 12.43  ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 14.244 -26.712 5.624  1.00 12.52  ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 14.187 -27.563 4.437  1.00 11.82  ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 14.232 -26.799 3.123  1.00 13.01  ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 14.613 -27.382 2.112  1.00 14.01  ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 12.923 -28.441 4.464  1.00 11.12  ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 12.895 -29.406 5.635  1.00 11.28  ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 11.558 -30.130 5.596  1.00 11.85  ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 10.489 -29.247 6.086  1.00 12.38  ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 9.236  -29.628 6.301  1.00 13.10  ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 8.856  -30.866 6.026  1.00 11.86  ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 8.347  -28.768 6.786  1.00 14.16  ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 13.819 -25.521 3.121  1.00 12.99  ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 13.865 -24.715 1.894  1.00 13.26  ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 15.261 -24.160 1.589  1.00 14.69  ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 15.471 -23.639 0.483  1.00 16.06  ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 12.862 -23.559 1.939  1.00 14.77  ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 13.150 -22.551 3.039  1.00 18.68  ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 13.421 -22.986 4.189  1.00 19.18  ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 13.084 -21.310 2.755  1.00 18.95  ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 16.198 -24.210 2.556  1.00 14.12  ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.536 -23.640 2.379  1.00 14.66  ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 18.418 -24.600 1.631  1.00 14.72  ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 19.260 -25.300 2.221  1.00 14.94  ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 18.136 -23.280 3.758  1.00 15.08  ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.276 -22.335 4.604  1.00 16.47  ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 17.894 -22.177 5.993  1.00 16.83  ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.117 -20.972 3.933  1.00 16.61  ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 18.221 -24.664 0.303  1.00 14.38  ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 18.923 -25.684 -0.493 1.00 14.87  ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 20.422 -25.507 -0.528 1.00 16.04  ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 21.139 -26.492 -0.741 1.00 17.42  ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 18.375 -25.735 -1.921 1.00 14.56  ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 16.873 -25.816 -2.072 1.00 15.65  ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 16.497 -25.940 -3.527 1.00 16.44  ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 16.257 -26.943 -1.231 1.00 16.90  ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 20.902 -24.252 -0.358 1.00 15.74  ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 22.333 -23.947 -0.416 1.00 17.03  ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 23.128 -24.548 0.771  1.00 19.01  ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 24.363 -24.599 0.707  1.00 19.91  ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 22.512 -22.421 -0.508 1.00 17.02  ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 21.822 -21.648 0.577  1.00 16.87  ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 20.570 -21.095 0.547  1.00 16.63  ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 22.368 -21.350 1.874  1.00 16.60  ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 20.329 -20.420 1.728  1.00 16.97  ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 21.424 -20.562 2.554  1.00 16.89  ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 23.610 -21.607 2.490  1.00 17.47  ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 21.636 -20.123 3.862  1.00 17.78  ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 23.846 -21.093 3.759  1.00 18.41  ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 22.860 -20.370 4.430  1.00 18.22  ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 22.446 -25.031 1.829  1.00 18.79  ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 23.159 -25.642 2.965  1.00 19.39  ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 23.989 -26.871 2.508  1.00 23.13  ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 24.990 -27.182 3.144  1.00 22.59  ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 22.163 -26.076 4.041  1.00 17.64  ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 21.539 -24.951 4.859  1.00 18.37  ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 20.511 -25.529 5.861  1.00 18.27  ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 22.621 -24.139 5.613  1.00 18.85  ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 23.572 -27.535 1.404  1.00 26.29  ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 24.234 -28.711 0.857  1.00 30.93  ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 25.237 -28.432 -0.231 1.00 35.64  ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 25.768 -29.389 -0.790 1.00 37.27  ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 23.189 -29.698 0.333  1.00 33.95  ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 22.454 -30.358 1.458  1.00 38.82  ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 23.095 -30.650 2.493  1.00 39.88  ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 21.244 -30.575 1.320  1.00 42.12  ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 25.567 -27.168 -0.503 1.00 37.53  ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 26.577 -26.837 -1.504 1.00 40.55  ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 27.562 -25.783 -0.980 1.00 42.46  ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 28.312 -25.179 -1.765 1.00 43.81  ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 25.911 -26.373 -2.805 1.00 44.10  ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 24.929 -25.238 -2.618 1.00 50.98  ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 23.863 -25.171 -3.695 1.00 59.76  ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 23.552 -24.048 -4.159 1.00 60.99  ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 23.339 -26.244 -4.074 1.00 62.24  ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1BN7 C 2 .   ? 25.330 13.879  10.614 1.00 16.24  ? 201 A1BN7 A N1  1 
HETATM 2156 C  C4  . A1BN7 C 2 .   ? 24.383 14.658  9.802  1.00 16.09  ? 201 A1BN7 A C4  1 
HETATM 2157 C  C5  . A1BN7 C 2 .   ? 26.060 12.830  10.180 1.00 18.15  ? 201 A1BN7 A C5  1 
HETATM 2158 C  C6  . A1BN7 C 2 .   ? 25.854 12.322  8.735  1.00 21.21  ? 201 A1BN7 A C6  1 
HETATM 2159 C  C7  . A1BN7 C 2 .   ? 26.569 11.039  8.386  1.00 22.42  ? 201 A1BN7 A C7  1 
HETATM 2160 C  C8  . A1BN7 C 2 .   ? 27.596 10.943  7.431  1.00 22.88  ? 201 A1BN7 A C8  1 
HETATM 2161 C  C10 . A1BN7 C 2 .   ? 25.409 14.312  12.013 1.00 15.25  ? 201 A1BN7 A C10 1 
HETATM 2162 CL CL  . A1BN7 C 2 .   ? 24.984 9.351   9.955  1.00 27.20  ? 201 A1BN7 A CL  1 
HETATM 2163 C  C9  . A1BN7 C 2 .   ? 26.206 9.805   8.850  1.00 23.99  ? 201 A1BN7 A C9  1 
HETATM 2164 S  S   . A1BN7 C 2 .   ? 27.126 8.601   8.116  1.00 23.05  ? 201 A1BN7 A S   1 
HETATM 2165 N  N2  . A1BN7 C 2 .   ? 28.000 9.675   7.178  1.00 22.45  ? 201 A1BN7 A N2  1 
HETATM 2166 F  F   . A1BN7 C 2 .   ? 26.246 13.332  7.898  1.00 21.54  ? 201 A1BN7 A F   1 
HETATM 2167 F  F1  . A1BN7 C 2 .   ? 24.514 12.171  8.522  1.00 22.38  ? 201 A1BN7 A F1  1 
HETATM 2168 O  O1  . A1BN7 C 2 .   ? 26.887 12.258  10.873 1.00 16.71  ? 201 A1BN7 A O1  1 
HETATM 2169 C  C3  . A1BN7 C 2 .   ? 22.982 14.590  10.398 1.00 15.92  ? 201 A1BN7 A C3  1 
HETATM 2170 C  C2  . A1BN7 C 2 .   ? 23.003 15.029  11.865 1.00 16.13  ? 201 A1BN7 A C2  1 
HETATM 2171 C  C1  . A1BN7 C 2 .   ? 24.023 14.202  12.661 1.00 15.33  ? 201 A1BN7 A C1  1 
HETATM 2172 C  C   . A1BN7 C 2 .   ? 24.101 14.648  14.110 1.00 15.30  ? 201 A1BN7 A C   1 
HETATM 2173 O  O   . A1BN7 C 2 .   ? 24.540 15.762  14.406 1.00 15.32  ? 201 A1BN7 A O   1 
HETATM 2174 N  N   . A1BN7 C 2 .   ? 23.739 13.745  15.015 1.00 14.89  ? 201 A1BN7 A N   1 
HETATM 2175 ZN ZN  . ZN    D 3 .   ? 23.251 -5.524  27.074 1.00 18.34  2 202 ZN    A ZN  1 
HETATM 2176 N  N1  . A1BN7 E 2 .   ? 10.626 -16.860 22.621 1.00 16.32  ? 201 A1BN7 C N1  1 
HETATM 2177 C  C4  . A1BN7 E 2 .   ? 11.640 -16.088 23.355 1.00 15.71  ? 201 A1BN7 C C4  1 
HETATM 2178 C  C5  . A1BN7 E 2 .   ? 9.903  -17.886 23.107 1.00 18.85  ? 201 A1BN7 C C5  1 
HETATM 2179 C  C6  . A1BN7 E 2 .   ? 10.200 -18.416 24.530 1.00 21.96  ? 201 A1BN7 C C6  1 
HETATM 2180 C  C7  . A1BN7 E 2 .   ? 9.445  -19.676 24.910 1.00 23.38  ? 201 A1BN7 C C7  1 
HETATM 2181 C  C8  . A1BN7 E 2 .   ? 8.497  -19.756 25.945 1.00 23.39  ? 201 A1BN7 C C8  1 
HETATM 2182 C  C10 . A1BN7 E 2 .   ? 10.418 -16.405 21.245 1.00 14.24  ? 201 A1BN7 C C10 1 
HETATM 2183 CL CL  . A1BN7 E 2 .   ? 10.792 -21.415 23.170 1.00 29.77  ? 201 A1BN7 C CL  1 
HETATM 2184 C  C9  . A1BN7 E 2 .   ? 9.694  -20.912 24.385 1.00 25.76  ? 201 A1BN7 C C9  1 
HETATM 2185 S  S   . A1BN7 E 2 .   ? 8.764  -22.071 25.176 1.00 25.11  ? 201 A1BN7 C S   1 
HETATM 2186 N  N2  . A1BN7 E 2 .   ? 8.046  -20.995 26.210 1.00 22.83  ? 201 A1BN7 C N2  1 
HETATM 2187 F  F   . A1BN7 E 2 .   ? 9.922  -17.412 25.416 1.00 23.24  ? 201 A1BN7 C F   1 
HETATM 2188 F  F1  . A1BN7 E 2 .   ? 11.546 -18.629 24.628 1.00 22.30  ? 201 A1BN7 C F1  1 
HETATM 2189 O  O1  . A1BN7 E 2 .   ? 9.006  -18.419 22.482 1.00 16.60  ? 201 A1BN7 C O1  1 
HETATM 2190 C  C3  . A1BN7 E 2 .   ? 12.978 -16.151 22.634 1.00 15.00  ? 201 A1BN7 C C3  1 
HETATM 2191 C  C2  . A1BN7 E 2 .   ? 12.825 -15.718 21.172 1.00 14.47  ? 201 A1BN7 C C2  1 
HETATM 2192 C  C1  . A1BN7 E 2 .   ? 11.723 -16.526 20.459 1.00 13.70  ? 201 A1BN7 C C1  1 
HETATM 2193 C  C   . A1BN7 E 2 .   ? 11.499 -16.036 19.038 1.00 13.46  ? 201 A1BN7 C C   1 
HETATM 2194 O  O   . A1BN7 E 2 .   ? 11.067 -14.899 18.817 1.00 13.06  ? 201 A1BN7 C O   1 
HETATM 2195 N  N   . A1BN7 E 2 .   ? 11.731 -16.922 18.076 1.00 14.25  ? 201 A1BN7 C N   1 
HETATM 2196 ZN ZN  . ZN    F 3 .   ? 10.511 -35.728 5.599  1.00 15.76  2 202 ZN    C ZN  1 
HETATM 2197 O  O   . HOH   G 4 .   ? 11.639 -1.866  27.958 1.00 25.99  ? 301 HOH   A O   1 
HETATM 2198 O  O   . HOH   G 4 .   ? 12.752 -4.657  20.618 1.00 33.36  ? 302 HOH   A O   1 
HETATM 2199 O  O   . HOH   G 4 .   ? 14.672 22.196  24.621 1.00 21.74  ? 303 HOH   A O   1 
HETATM 2200 O  O   . HOH   G 4 .   ? 24.025 7.597   27.209 1.00 238.96 ? 304 HOH   A O   1 
HETATM 2201 O  O   . HOH   G 4 .   ? -1.877 15.547  20.297 1.00 26.06  ? 305 HOH   A O   1 
HETATM 2202 O  O   . HOH   G 4 .   ? 31.767 7.353   23.262 1.00 25.71  ? 306 HOH   A O   1 
HETATM 2203 O  O   . HOH   G 4 .   ? 16.370 19.423  4.418  1.00 66.23  ? 307 HOH   A O   1 
HETATM 2204 O  O   . HOH   G 4 .   ? 6.995  -1.778  25.356 1.00 47.32  ? 308 HOH   A O   1 
HETATM 2205 O  O   . HOH   G 4 .   ? 11.095 21.456  24.606 1.00 30.03  ? 309 HOH   A O   1 
HETATM 2206 O  O   . HOH   G 4 .   ? 5.065  6.361   35.378 1.00 57.93  ? 310 HOH   A O   1 
HETATM 2207 O  O   . HOH   G 4 .   ? 12.998 13.233  16.729 1.00 137.46 ? 311 HOH   A O   1 
HETATM 2208 O  O   . HOH   G 4 .   ? 23.844 7.382   28.459 1.00 21.21  ? 312 HOH   A O   1 
HETATM 2209 O  O   . HOH   G 4 .   ? 35.659 20.536  8.884  1.00 55.35  ? 313 HOH   A O   1 
HETATM 2210 O  O   . HOH   G 4 .   ? 17.900 -7.797  21.784 1.00 22.98  ? 314 HOH   A O   1 
HETATM 2211 O  O   . HOH   G 4 .   ? 21.372 10.267  32.251 1.00 53.82  ? 315 HOH   A O   1 
HETATM 2212 O  O   . HOH   G 4 .   ? 16.989 20.741  22.789 1.00 21.87  ? 316 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 4 .   ? 31.088 -1.995  29.758 1.00 43.29  ? 317 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 4 .   ? 6.259  3.318   28.929 1.00 35.68  ? 318 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 4 .   ? 15.010 -3.975  30.324 1.00 36.32  ? 319 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 4 .   ? 6.922  15.509  29.184 1.00 40.21  ? 320 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 4 .   ? 18.781 -11.560 27.461 1.00 27.43  ? 321 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 4 .   ? 16.263 18.691  26.945 1.00 36.54  ? 322 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 4 .   ? 34.944 14.902  24.941 1.00 29.55  ? 323 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 4 .   ? 15.046 8.575   13.413 1.00 14.30  ? 324 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 4 .   ? 7.073  7.324   31.709 1.00 30.92  ? 325 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 4 .   ? 22.667 6.455   1.609  1.00 21.17  ? 326 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 4 .   ? 23.950 3.918   29.389 1.00 19.55  ? 327 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 4 .   ? 28.503 -6.118  3.541  1.00 23.31  ? 328 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 4 .   ? 16.199 -0.656  4.776  1.00 26.66  ? 329 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 4 .   ? 12.270 3.604   8.726  1.00 40.92  ? 330 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 4 .   ? 12.308 18.024  12.861 1.00 34.45  ? 331 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 4 .   ? 23.656 16.573  27.467 1.00 44.54  ? 332 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 4 .   ? 34.557 -0.781  16.703 1.00 13.84  ? 333 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 4 .   ? 30.423 20.396  7.716  1.00 35.72  ? 334 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 4 .   ? 23.760 1.803   -0.805 1.00 14.47  ? 335 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 4 .   ? 4.060  20.234  15.167 1.00 31.76  ? 336 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 4 .   ? 27.019 19.211  15.053 1.00 14.58  ? 337 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 4 .   ? 30.549 -0.291  32.919 1.00 103.05 ? 338 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 4 .   ? 3.944  19.955  21.476 1.00 26.63  ? 339 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 4 .   ? 34.907 13.763  16.440 1.00 27.54  ? 340 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 4 .   ? 5.084  10.961  12.365 1.00 32.46  ? 341 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 4 .   ? 28.064 3.025   -0.314 1.00 21.97  ? 342 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 4 .   ? 32.245 2.866   4.978  1.00 26.58  ? 343 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 4 .   ? 5.051  3.017   21.050 1.00 23.17  ? 344 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 4 .   ? 9.008  3.967   11.973 1.00 34.86  ? 345 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 4 .   ? 23.524 10.985  21.495 1.00 13.80  ? 346 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 4 .   ? 29.635 25.927  16.273 1.00 37.85  ? 347 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 4 .   ? 4.113  9.881   17.975 1.00 32.74  ? 348 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 4 .   ? 25.491 17.909  12.930 1.00 13.37  ? 349 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 4 .   ? 17.310 2.140   9.364  1.00 18.04  ? 350 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 4 .   ? 29.799 7.114   4.481  1.00 35.94  ? 351 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 4 .   ? 25.371 1.640   30.014 1.00 20.01  ? 352 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 4 .   ? 6.228  -2.619  18.785 1.00 36.48  ? 353 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 4 .   ? 25.199 4.152   -1.135 1.00 21.14  ? 354 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 4 .   ? 4.123  4.102   28.130 1.00 32.98  ? 355 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 4 .   ? 16.484 -7.393  29.299 1.00 26.20  ? 356 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 4 .   ? 37.057 7.407   4.080  1.00 36.33  ? 357 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 4 .   ? 13.514 18.707  14.692 1.00 24.69  ? 358 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 4 .   ? 23.795 14.768  29.959 1.00 51.10  ? 359 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 4 .   ? 20.120 2.120   9.355  1.00 14.45  ? 360 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 4 .   ? 16.889 4.426   5.897  1.00 27.40  ? 361 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 4 .   ? 22.256 -5.966  0.359  1.00 43.27  ? 362 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 4 .   ? 22.186 -8.227  19.409 1.00 27.04  ? 363 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 4 .   ? 11.305 -0.364  15.851 1.00 24.83  ? 364 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 4 .   ? 3.418  18.101  23.669 1.00 28.72  ? 365 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 4 .   ? -0.104 14.379  22.734 1.00 60.05  ? 366 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 4 .   ? 21.499 9.890   23.403 1.00 12.36  ? 367 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 4 .   ? 22.068 8.697   2.827  1.00 19.82  ? 368 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 4 .   ? 30.437 -5.758  26.533 1.00 27.43  ? 369 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 4 .   ? 24.810 -9.105  23.228 1.00 38.17  ? 370 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 4 .   ? 28.352 0.934   26.858 1.00 17.89  ? 371 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 4 .   ? 34.062 0.431   8.697  1.00 17.94  ? 372 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 4 .   ? 20.222 11.873  8.565  1.00 18.96  ? 373 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 4 .   ? 22.784 10.663  22.688 1.00 74.27  ? 374 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 4 .   ? 17.795 20.444  13.821 1.00 22.11  ? 375 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 4 .   ? 16.527 8.922   6.758  1.00 21.12  ? 376 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 4 .   ? 29.006 -7.673  25.628 1.00 63.00  ? 377 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 4 .   ? 17.150 18.491  15.593 1.00 14.82  ? 378 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 4 .   ? 35.461 14.558  20.233 1.00 20.55  ? 379 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 4 .   ? 34.572 3.663   26.314 1.00 25.48  ? 380 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 4 .   ? 30.796 5.350   7.822  1.00 20.69  ? 381 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 4 .   ? 17.270 0.309   2.459  1.00 32.28  ? 382 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 4 .   ? 31.823 13.133  14.974 1.00 40.01  ? 383 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 4 .   ? 21.225 25.170  9.937  1.00 22.47  ? 384 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 4 .   ? 29.779 6.433   30.030 1.00 29.50  ? 385 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 4 .   ? 29.262 13.873  11.243 1.00 29.65  ? 386 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 4 .   ? 29.789 -2.197  8.342  1.00 20.90  ? 387 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 4 .   ? 20.604 -7.612  1.916  1.00 39.56  ? 388 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 4 .   ? 29.016 22.105  22.098 1.00 28.48  ? 389 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 4 .   ? 27.788 24.975  19.201 1.00 41.15  ? 390 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 4 .   ? 34.848 -6.297  21.797 1.00 38.86  ? 391 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 4 .   ? 22.905 -11.353 30.888 1.00 52.34  ? 392 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 4 .   ? 15.338 12.271  30.469 1.00 42.69  ? 393 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 4 .   ? -2.524 2.904   24.513 1.00 62.20  ? 394 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 4 .   ? 17.563 16.405  28.730 1.00 47.31  ? 395 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 4 .   ? 18.432 -5.229  30.659 1.00 24.43  ? 396 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 4 .   ? 14.953 -4.327  16.223 1.00 30.44  ? 397 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 4 .   ? 29.381 1.228   25.373 1.00 69.97  ? 398 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 4 .   ? 6.725  16.364  8.933  1.00 25.83  ? 399 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 4 .   ? 27.895 16.323  10.701 1.00 23.08  ? 400 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 4 .   ? 28.300 17.133  8.445  1.00 35.18  ? 401 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 4 .   ? 2.423  1.417   28.186 1.00 38.57  ? 402 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 4 .   ? 30.684 -3.142  12.062 1.00 27.66  ? 403 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 4 .   ? 29.345 25.769  13.421 1.00 24.30  ? 404 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 4 .   ? 20.257 20.451  24.424 1.00 32.45  ? 405 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 4 .   ? 26.107 8.551   0.925  1.00 49.02  ? 406 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 4 .   ? 4.905  6.044   13.659 1.00 51.62  ? 407 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 4 .   ? 23.665 18.197  6.295  1.00 35.29  ? 408 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 4 .   ? 27.817 11.950  27.662 1.00 22.51  ? 409 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 4 .   ? 33.117 -2.625  15.428 1.00 20.36  ? 410 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 4 .   ? 4.658  11.142  29.605 1.00 52.22  ? 411 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 4 .   ? 25.224 -5.404  32.233 1.00 40.41  ? 412 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 4 .   ? -0.376 10.305  21.558 1.00 40.10  ? 413 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 4 .   ? 3.823  14.693  10.475 1.00 27.76  ? 414 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 4 .   ? 31.517 14.817  12.691 1.00 24.28  ? 415 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 4 .   ? 19.820 13.841  29.128 1.00 26.55  ? 416 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 4 .   ? 26.448 -7.968  23.917 1.00 38.41  ? 417 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 4 .   ? 26.934 19.208  24.770 1.00 39.78  ? 418 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 4 .   ? 18.568 10.284  31.805 1.00 31.16  ? 419 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 4 .   ? 33.993 16.314  14.315 1.00 32.18  ? 420 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 4 .   ? 2.640  8.632   26.157 1.00 30.98  ? 421 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 4 .   ? 32.009 8.991   4.617  1.00 38.63  ? 422 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 4 .   ? 25.301 20.466  21.972 1.00 34.27  ? 423 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 4 .   ? 16.194 -0.678  12.834 1.00 21.30  ? 424 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 4 .   ? 5.141  3.223   12.647 1.00 51.25  ? 425 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 4 .   ? 19.837 -4.651  15.207 1.00 23.28  ? 426 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 4 .   ? 32.624 12.490  27.900 1.00 32.51  ? 427 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 4 .   ? 32.053 22.494  11.365 1.00 22.43  ? 428 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 4 .   ? 2.296  14.056  24.833 1.00 55.10  ? 429 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 4 .   ? 4.771  10.533  14.456 1.00 33.01  ? 430 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 4 .   ? 15.032 23.209  16.947 1.00 21.55  ? 431 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 4 .   ? 31.878 -7.032  18.091 1.00 34.64  ? 432 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 4 .   ? 30.310 -2.056  3.527  1.00 36.05  ? 433 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 4 .   ? 12.062 18.451  26.527 1.00 25.39  ? 434 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 4 .   ? 3.555  2.431   19.067 1.00 30.24  ? 435 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 4 .   ? 10.537 6.778   11.462 1.00 37.74  ? 436 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 4 .   ? 32.712 5.600   4.764  1.00 29.98  ? 437 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 4 .   ? 23.016 20.789  20.540 1.00 22.82  ? 438 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 4 .   ? 11.150 2.061   12.501 1.00 22.73  ? 439 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 4 .   ? 13.234 8.560   11.145 1.00 18.76  ? 440 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 4 .   ? 36.110 -0.806  28.590 1.00 48.96  ? 441 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 4 .   ? 17.958 22.523  16.114 1.00 33.75  ? 442 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 4 .   ? 11.707 15.795  9.118  1.00 50.66  ? 443 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 4 .   ? 16.013 -5.578  4.948  1.00 57.12  ? 444 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 4 .   ? 20.704 13.685  6.722  1.00 33.16  ? 445 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 4 .   ? 19.631 -9.786  20.568 1.00 27.65  ? 446 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 4 .   ? 31.226 10.472  14.021 1.00 40.97  ? 447 HOH   A O   1 
HETATM 2344 O  O   . HOH   G 4 .   ? 8.219  -2.371  17.433 1.00 21.98  ? 448 HOH   A O   1 
HETATM 2345 O  O   . HOH   G 4 .   ? 15.884 8.347   34.146 1.00 40.05  ? 449 HOH   A O   1 
HETATM 2346 O  O   . HOH   G 4 .   ? 8.703  -2.779  27.369 1.00 48.95  ? 450 HOH   A O   1 
HETATM 2347 O  O   . HOH   G 4 .   ? 12.049 -2.884  15.761 1.00 47.25  ? 451 HOH   A O   1 
HETATM 2348 O  O   . HOH   G 4 .   ? 0.897  17.172  23.393 1.00 59.84  ? 452 HOH   A O   1 
HETATM 2349 O  O   . HOH   G 4 .   ? 16.304 10.104  32.349 1.00 36.40  ? 453 HOH   A O   1 
HETATM 2350 O  O   . HOH   G 4 .   ? 19.615 11.486  4.374  1.00 36.76  ? 454 HOH   A O   1 
HETATM 2351 O  O   . HOH   G 4 .   ? 20.475 24.440  22.308 1.00 66.95  ? 455 HOH   A O   1 
HETATM 2352 O  O   . HOH   G 4 .   ? 1.710  16.162  9.643  1.00 45.63  ? 456 HOH   A O   1 
HETATM 2353 O  O   . HOH   G 4 .   ? 18.097 10.852  6.760  1.00 25.36  ? 457 HOH   A O   1 
HETATM 2354 O  O   . HOH   G 4 .   ? 35.764 23.099  20.237 1.00 50.28  ? 458 HOH   A O   1 
HETATM 2355 O  O   . HOH   G 4 .   ? 25.945 22.122  5.799  1.00 46.58  ? 459 HOH   A O   1 
HETATM 2356 O  O   . HOH   G 4 .   ? 25.692 18.352  26.924 1.00 47.49  ? 460 HOH   A O   1 
HETATM 2357 O  O   . HOH   G 4 .   ? 13.873 21.596  14.845 1.00 22.50  ? 461 HOH   A O   1 
HETATM 2358 O  O   . HOH   G 4 .   ? 23.844 20.613  27.037 1.00 59.34  ? 462 HOH   A O   1 
HETATM 2359 O  O   . HOH   G 4 .   ? 7.846  -6.809  26.324 1.00 47.11  ? 463 HOH   A O   1 
HETATM 2360 O  O   . HOH   G 4 .   ? 33.141 0.653   6.177  1.00 27.64  ? 464 HOH   A O   1 
HETATM 2361 O  O   . HOH   G 4 .   ? 6.492  -0.164  28.656 1.00 51.11  ? 465 HOH   A O   1 
HETATM 2362 O  O   . HOH   G 4 .   ? 8.980  17.914  8.788  1.00 49.38  ? 466 HOH   A O   1 
HETATM 2363 O  O   . HOH   G 4 .   ? 17.821 12.938  30.501 1.00 41.17  ? 467 HOH   A O   1 
HETATM 2364 O  O   . HOH   G 4 .   ? 28.081 1.831   29.506 1.00 29.14  ? 468 HOH   A O   1 
HETATM 2365 O  O   . HOH   G 4 .   ? 2.294  20.980  12.167 1.00 40.33  ? 469 HOH   A O   1 
HETATM 2366 O  O   . HOH   G 4 .   ? 6.700  19.143  26.849 1.00 56.74  ? 470 HOH   A O   1 
HETATM 2367 O  O   . HOH   G 4 .   ? 23.158 22.888  18.808 1.00 27.56  ? 471 HOH   A O   1 
HETATM 2368 O  O   . HOH   G 4 .   ? 31.123 -2.849  5.858  1.00 35.57  ? 472 HOH   A O   1 
HETATM 2369 O  O   . HOH   G 4 .   ? 33.749 -2.291  9.268  1.00 24.65  ? 473 HOH   A O   1 
HETATM 2370 O  O   . HOH   G 4 .   ? 9.248  21.863  12.325 1.00 30.89  ? 474 HOH   A O   1 
HETATM 2371 O  O   . HOH   G 4 .   ? 4.693  -0.545  17.450 1.00 40.74  ? 475 HOH   A O   1 
HETATM 2372 O  O   . HOH   G 4 .   ? 18.007 -8.258  1.500  1.00 59.22  ? 476 HOH   A O   1 
HETATM 2373 O  O   . HOH   G 4 .   ? 16.246 12.593  5.566  1.00 31.24  ? 477 HOH   A O   1 
HETATM 2374 O  O   . HOH   G 4 .   ? 2.799  3.976   16.985 1.00 35.57  ? 478 HOH   A O   1 
HETATM 2375 O  O   . HOH   G 4 .   ? 16.591 -3.556  13.951 1.00 31.28  ? 479 HOH   A O   1 
HETATM 2376 O  O   . HOH   G 4 .   ? 23.018 10.844  1.677  1.00 33.75  ? 480 HOH   A O   1 
HETATM 2377 O  O   . HOH   G 4 .   ? 28.532 4.269   30.672 1.00 30.97  ? 481 HOH   A O   1 
HETATM 2378 O  O   . HOH   G 4 .   ? 13.347 9.827   8.412  1.00 38.97  ? 482 HOH   A O   1 
HETATM 2379 O  O   . HOH   G 4 .   ? 20.701 -7.290  -0.845 1.00 49.92  ? 483 HOH   A O   1 
HETATM 2380 O  O   . HOH   G 4 .   ? 3.314  8.068   16.151 1.00 48.95  ? 484 HOH   A O   1 
HETATM 2381 O  O   . HOH   G 4 .   ? 31.405 -3.788  9.604  1.00 27.10  ? 485 HOH   A O   1 
HETATM 2382 O  O   . HOH   G 4 .   ? 31.810 25.355  12.216 1.00 29.97  ? 486 HOH   A O   1 
HETATM 2383 O  O   . HOH   G 4 .   ? 11.639 -4.682  30.225 1.00 54.69  ? 487 HOH   A O   1 
HETATM 2384 O  O   . HOH   G 4 .   ? 21.158 24.077  17.488 1.00 28.15  ? 488 HOH   A O   1 
HETATM 2385 O  O   . HOH   G 4 .   ? 25.035 24.540  19.823 1.00 34.89  ? 489 HOH   A O   1 
HETATM 2386 O  O   . HOH   G 4 .   ? -3.858 0.433   25.348 1.00 59.62  ? 490 HOH   A O   1 
HETATM 2387 O  O   . HOH   G 4 .   ? 30.223 20.400  25.708 1.00 52.97  ? 491 HOH   A O   1 
HETATM 2388 O  O   . HOH   G 4 .   ? 25.534 14.805  5.476  1.00 44.75  ? 492 HOH   A O   1 
HETATM 2389 O  O   . HOH   G 4 .   ? 29.179 -9.155  6.847  1.00 50.99  ? 493 HOH   A O   1 
HETATM 2390 O  O   . HOH   G 4 .   ? 22.161 13.242  2.456  1.00 59.00  ? 494 HOH   A O   1 
HETATM 2391 O  O   . HOH   G 4 .   ? 2.695  13.667  31.483 1.00 64.35  ? 495 HOH   A O   1 
HETATM 2392 O  O   . HOH   H 4 .   ? 30.816 -28.113 9.520  1.00 63.11  ? 301 HOH   C O   1 
HETATM 2393 O  O   . HOH   H 4 .   ? 12.790 -14.245 4.995  1.00 47.06  ? 302 HOH   C O   1 
HETATM 2394 O  O   . HOH   H 4 .   ? 2.547  -23.173 10.375 1.00 30.75  ? 303 HOH   C O   1 
HETATM 2395 O  O   . HOH   H 4 .   ? 13.479 -24.750 31.352 1.00 28.54  ? 304 HOH   C O   1 
HETATM 2396 O  O   . HOH   H 4 .   ? 35.513 -15.399 15.839 1.00 35.84  ? 305 HOH   C O   1 
HETATM 2397 O  O   . HOH   H 4 .   ? -2.220 -8.717  12.980 1.00 46.35  ? 306 HOH   C O   1 
HETATM 2398 O  O   . HOH   H 4 .   ? 22.142 -32.606 3.802  1.00 25.79  ? 307 HOH   C O   1 
HETATM 2399 O  O   . HOH   H 4 .   ? 17.190 -15.899 27.192 1.00 37.13  ? 308 HOH   C O   1 
HETATM 2400 O  O   . HOH   H 4 .   ? 1.807  -32.767 18.735 1.00 71.95  ? 309 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 4 .   ? 14.952 -14.063 29.272 1.00 47.60  ? 310 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 4 .   ? 2.754  -31.159 3.799  1.00 34.22  ? 311 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 4 .   ? 4.353  -36.202 21.615 1.00 27.89  ? 312 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 4 .   ? 24.660 -37.347 10.885 1.00 33.38  ? 313 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 4 .   ? 23.440 -31.217 15.128 1.00 21.48  ? 314 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 4 .   ? 9.997  -22.960 4.764  1.00 23.64  ? 315 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 4 .   ? 22.774 -36.136 12.374 1.00 30.92  ? 316 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 4 .   ? 17.169 -37.957 3.120  1.00 34.36  ? 317 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 4 .   ? 19.910 -8.449  7.651  1.00 37.51  ? 318 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 4 .   ? 10.487 -27.540 33.840 1.00 27.42  ? 319 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 4 .   ? 23.765 -9.316  7.894  1.00 20.89  ? 320 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 4 .   ? 20.386 -22.395 18.738 1.00 14.15  ? 321 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 4 .   ? 31.071 -10.441 10.577 1.00 31.28  ? 322 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 4 .   ? 16.047 -38.983 9.906  1.00 40.26  ? 323 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 4 .   ? 26.391 -22.662 -0.180 1.00 38.17  ? 324 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 4 .   ? 9.826  -26.234 3.557  1.00 14.86  ? 325 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 4 .   ? 0.134  -15.479 22.660 1.00 31.07  ? 326 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 4 .   ? 10.385 -12.796 20.489 1.00 13.54  ? 327 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 4 .   ? 8.358  -28.472 2.996  1.00 19.18  ? 328 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 4 .   ? 4.925  -31.107 -1.937 1.00 29.91  ? 329 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 4 .   ? 12.394 -29.407 33.706 1.00 20.46  ? 330 HOH   C O   1 
HETATM 2422 O  O   . HOH   H 4 .   ? 12.619 -6.458  22.186 1.00 34.97  ? 331 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 4 .   ? 7.189  -36.976 29.182 1.00 37.93  ? 332 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 4 .   ? 8.459  -11.562 18.447 1.00 17.52  ? 333 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 4 .   ? 29.263 -27.965 10.021 1.00 22.14  ? 334 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 4 .   ? 14.309 -19.878 0.816  1.00 34.13  ? 335 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 4 .   ? 7.231  -39.064 7.282  1.00 37.78  ? 336 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 4 .   ? 30.801 -21.400 13.140 1.00 33.99  ? 337 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 4 .   ? 13.261 -14.589 25.975 1.00 40.52  ? 338 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 4 .   ? 26.078 -33.190 5.918  1.00 39.83  ? 339 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 4 .   ? 6.408  -23.093 28.538 1.00 42.97  ? 340 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 4 .   ? 18.155 -11.736 5.586  1.00 35.97  ? 341 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 4 .   ? 11.636 -36.000 -0.815 1.00 31.20  ? 342 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 4 .   ? 0.608  -17.064 18.131 1.00 29.77  ? 343 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 4 .   ? 3.796  -9.102  22.930 1.00 29.43  ? 344 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 4 .   ? 21.995 -12.337 17.231 1.00 22.21  ? 345 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 4 .   ? 27.590 -27.628 2.429  1.00 29.95  ? 346 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 4 .   ? 23.983 -12.619 19.094 1.00 26.22  ? 347 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 4 .   ? 17.755 -9.981  9.546  1.00 18.88  ? 348 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 4 .   ? 11.237 -36.160 31.612 1.00 33.20  ? 349 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 4 .   ? -0.716 -17.358 11.508 1.00 29.08  ? 350 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 4 .   ? 5.524  -17.900 25.310 1.00 42.73  ? 351 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 4 .   ? 31.185 -10.824 16.569 1.00 21.50  ? 352 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 4 .   ? 10.475 -13.845 5.696  1.00 50.12  ? 353 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 4 .   ? 0.862  -31.740 17.173 1.00 14.82  ? 354 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 4 .   ? 25.033 -36.894 6.471  1.00 52.36  ? 355 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 4 .   ? 3.552  -23.591 3.695  1.00 23.31  ? 356 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 4 .   ? 26.303 -34.658 12.305 1.00 78.61  ? 357 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 4 .   ? 18.220 -28.794 22.930 1.00 18.38  ? 358 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 4 .   ? 27.561 -15.037 2.647  1.00 38.05  ? 359 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 4 .   ? 29.448 -34.281 5.556  1.00 59.36  ? 360 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 4 .   ? 30.364 -20.221 19.187 1.00 24.47  ? 361 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 4 .   ? 16.527 -13.848 4.057  1.00 34.98  ? 362 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 4 .   ? 13.000 -20.727 9.443  1.00 12.56  ? 363 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 4 .   ? 11.250 -19.665 11.529 1.00 12.86  ? 364 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 4 .   ? 20.641 -28.587 -2.544 1.00 30.78  ? 365 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 4 .   ? 15.449 -28.833 23.150 1.00 15.31  ? 366 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 4 .   ? 29.614 -26.273 3.044  1.00 36.38  ? 367 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 4 .   ? 15.673 -18.843 24.212 1.00 19.40  ? 368 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 4 .   ? 5.698  -10.377 25.726 1.00 42.54  ? 369 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 4 .   ? 1.324  -29.556 25.087 1.00 34.51  ? 370 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 4 .   ? 0.877  -33.863 20.682 1.00 26.66  ? 371 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 4 .   ? 26.334 -21.689 21.022 1.00 41.45  ? 372 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 4 .   ? 21.968 -14.871 23.413 1.00 34.51  ? 373 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 4 .   ? 13.036 -27.133 -0.263 1.00 135.50 ? 374 HOH   C O   1 
HETATM 2466 O  O   . HOH   H 4 .   ? 4.640  -30.533 31.164 1.00 69.15  ? 375 HOH   C O   1 
HETATM 2467 O  O   . HOH   H 4 .   ? 14.417 -22.502 30.044 1.00 21.10  ? 376 HOH   C O   1 
HETATM 2468 O  O   . HOH   H 4 .   ? 20.653 -29.326 18.141 1.00 27.44  ? 377 HOH   C O   1 
HETATM 2469 O  O   . HOH   H 4 .   ? 3.637  -36.236 6.941  1.00 23.40  ? 378 HOH   C O   1 
HETATM 2470 O  O   . HOH   H 4 .   ? 8.627  -38.648 9.594  1.00 32.60  ? 379 HOH   C O   1 
HETATM 2471 O  O   . HOH   H 4 .   ? 30.480 -20.536 16.520 1.00 33.05  ? 380 HOH   C O   1 
HETATM 2472 O  O   . HOH   H 4 .   ? 19.487 -22.229 25.589 1.00 26.68  ? 381 HOH   C O   1 
HETATM 2473 O  O   . HOH   H 4 .   ? 14.799 -35.850 16.972 1.00 20.62  ? 382 HOH   C O   1 
HETATM 2474 O  O   . HOH   H 4 .   ? 18.194 -12.317 17.040 1.00 14.67  ? 383 HOH   C O   1 
HETATM 2475 O  O   . HOH   H 4 .   ? 14.382 -10.280 8.598  1.00 31.30  ? 384 HOH   C O   1 
HETATM 2476 O  O   . HOH   H 4 .   ? 17.857 -10.160 18.611 1.00 31.47  ? 385 HOH   C O   1 
HETATM 2477 O  O   . HOH   H 4 .   ? 5.784  -32.799 29.933 1.00 46.61  ? 386 HOH   C O   1 
HETATM 2478 O  O   . HOH   H 4 .   ? 19.773 -31.412 27.065 1.00 30.79  ? 387 HOH   C O   1 
HETATM 2479 O  O   . HOH   H 4 .   ? 6.490  -18.359 5.870  1.00 18.19  ? 388 HOH   C O   1 
HETATM 2480 O  O   . HOH   H 4 .   ? 6.985  -5.597  14.815 1.00 37.64  ? 389 HOH   C O   1 
HETATM 2481 O  O   . HOH   H 4 .   ? 4.247  -24.454 26.301 1.00 37.75  ? 390 HOH   C O   1 
HETATM 2482 O  O   . HOH   H 4 .   ? 5.660  -32.806 24.557 1.00 20.29  ? 391 HOH   C O   1 
HETATM 2483 O  O   . HOH   H 4 .   ? 10.087 -22.512 32.330 1.00 44.56  ? 392 HOH   C O   1 
HETATM 2484 O  O   . HOH   H 4 .   ? 5.483  -29.264 7.334  1.00 15.24  ? 393 HOH   C O   1 
HETATM 2485 O  O   . HOH   H 4 .   ? 8.164  -14.555 22.999 1.00 23.08  ? 394 HOH   C O   1 
HETATM 2486 O  O   . HOH   H 4 .   ? 28.434 -9.851  18.769 1.00 45.61  ? 395 HOH   C O   1 
HETATM 2487 O  O   . HOH   H 4 .   ? 19.450 -27.212 25.401 1.00 35.66  ? 396 HOH   C O   1 
HETATM 2488 O  O   . HOH   H 4 .   ? 24.475 -15.103 22.606 1.00 45.29  ? 397 HOH   C O   1 
HETATM 2489 O  O   . HOH   H 4 .   ? 8.288  -39.704 24.472 1.00 34.36  ? 398 HOH   C O   1 
HETATM 2490 O  O   . HOH   H 4 .   ? 1.916  -17.623 6.029  1.00 35.34  ? 399 HOH   C O   1 
HETATM 2491 O  O   . HOH   H 4 .   ? 7.911  -35.082 0.602  1.00 19.47  ? 400 HOH   C O   1 
HETATM 2492 O  O   . HOH   H 4 .   ? -0.536 -16.307 14.084 1.00 24.20  ? 401 HOH   C O   1 
HETATM 2493 O  O   . HOH   H 4 .   ? 14.065 -16.655 3.642  1.00 25.21  ? 402 HOH   C O   1 
HETATM 2494 O  O   . HOH   H 4 .   ? 24.786 -23.865 20.017 1.00 26.78  ? 403 HOH   C O   1 
HETATM 2495 O  O   . HOH   H 4 .   ? 16.889 -8.029  14.930 1.00 30.86  ? 404 HOH   C O   1 
HETATM 2496 O  O   . HOH   H 4 .   ? 15.028 -7.462  16.876 1.00 44.51  ? 405 HOH   C O   1 
HETATM 2497 O  O   . HOH   H 4 .   ? 15.325 -35.640 1.786  1.00 20.48  ? 406 HOH   C O   1 
HETATM 2498 O  O   . HOH   H 4 .   ? 19.485 -7.355  15.205 1.00 17.77  ? 407 HOH   C O   1 
HETATM 2499 O  O   . HOH   H 4 .   ? 32.090 -16.582 20.732 1.00 23.11  ? 408 HOH   C O   1 
HETATM 2500 O  O   . HOH   H 4 .   ? 9.389  -39.852 0.445  1.00 47.70  ? 409 HOH   C O   1 
HETATM 2501 O  O   . HOH   H 4 .   ? 0.466  -11.261 25.910 1.00 42.73  ? 410 HOH   C O   1 
HETATM 2502 O  O   . HOH   H 4 .   ? 18.989 -31.530 19.274 1.00 20.28  ? 411 HOH   C O   1 
HETATM 2503 O  O   . HOH   H 4 .   ? 6.602  -16.609 22.745 1.00 28.72  ? 412 HOH   C O   1 
HETATM 2504 O  O   . HOH   H 4 .   ? 10.522 -15.215 3.526  1.00 50.09  ? 413 HOH   C O   1 
HETATM 2505 O  O   . HOH   H 4 .   ? 23.939 -29.067 18.952 1.00 23.85  ? 414 HOH   C O   1 
HETATM 2506 O  O   . HOH   H 4 .   ? 22.284 -12.170 5.744  1.00 26.46  ? 415 HOH   C O   1 
HETATM 2507 O  O   . HOH   H 4 .   ? 18.354 -18.111 2.059  1.00 37.91  ? 416 HOH   C O   1 
HETATM 2508 O  O   . HOH   H 4 .   ? 8.690  -13.735 25.557 1.00 30.33  ? 417 HOH   C O   1 
HETATM 2509 O  O   . HOH   H 4 .   ? 5.837  -8.602  11.625 1.00 45.43  ? 418 HOH   C O   1 
HETATM 2510 O  O   . HOH   H 4 .   ? 29.076 -14.836 22.706 1.00 31.55  ? 419 HOH   C O   1 
HETATM 2511 O  O   . HOH   H 4 .   ? 31.287 -22.055 4.871  1.00 34.84  ? 420 HOH   C O   1 
HETATM 2512 O  O   . HOH   H 4 .   ? 32.629 -16.795 6.469  1.00 50.07  ? 421 HOH   C O   1 
HETATM 2513 O  O   . HOH   H 4 .   ? 36.606 -32.073 9.015  1.00 48.38  ? 422 HOH   C O   1 
HETATM 2514 O  O   . HOH   H 4 .   ? 23.752 -13.474 3.075  1.00 43.65  ? 423 HOH   C O   1 
HETATM 2515 O  O   . HOH   H 4 .   ? 1.250  -34.459 17.856 1.00 20.80  ? 424 HOH   C O   1 
HETATM 2516 O  O   . HOH   H 4 .   ? 20.955 -11.904 21.178 1.00 25.06  ? 425 HOH   C O   1 
HETATM 2517 O  O   . HOH   H 4 .   ? 13.643 -42.446 4.488  1.00 46.77  ? 426 HOH   C O   1 
HETATM 2518 O  O   . HOH   H 4 .   ? 28.607 -33.352 12.624 1.00 29.25  ? 427 HOH   C O   1 
HETATM 2519 O  O   . HOH   H 4 .   ? 26.334 -33.079 14.018 1.00 26.02  ? 428 HOH   C O   1 
HETATM 2520 O  O   . HOH   H 4 .   ? 12.006 -9.823  12.702 1.00 26.36  ? 429 HOH   C O   1 
HETATM 2521 O  O   . HOH   H 4 .   ? 4.625  -29.138 4.979  1.00 39.31  ? 430 HOH   C O   1 
HETATM 2522 O  O   . HOH   H 4 .   ? 4.390  -16.360 21.418 1.00 25.97  ? 431 HOH   C O   1 
HETATM 2523 O  O   . HOH   H 4 .   ? 31.024 -28.827 12.014 1.00 26.76  ? 432 HOH   C O   1 
HETATM 2524 O  O   . HOH   H 4 .   ? 4.178  -18.232 19.054 1.00 38.07  ? 433 HOH   C O   1 
HETATM 2525 O  O   . HOH   H 4 .   ? 4.072  -33.809 22.533 1.00 31.26  ? 434 HOH   C O   1 
HETATM 2526 O  O   . HOH   H 4 .   ? 9.271  -9.870  11.190 1.00 50.70  ? 435 HOH   C O   1 
HETATM 2527 O  O   . HOH   H 4 .   ? 22.403 -22.459 20.767 1.00 18.73  ? 436 HOH   C O   1 
HETATM 2528 O  O   . HOH   H 4 .   ? 12.161 -39.240 12.949 1.00 33.39  ? 437 HOH   C O   1 
HETATM 2529 O  O   . HOH   H 4 .   ? 20.167 -8.872  17.604 1.00 30.24  ? 438 HOH   C O   1 
HETATM 2530 O  O   . HOH   H 4 .   ? 4.278  -20.673 19.722 1.00 37.71  ? 439 HOH   C O   1 
HETATM 2531 O  O   . HOH   H 4 .   ? 17.922 -38.860 24.274 1.00 35.56  ? 440 HOH   C O   1 
HETATM 2532 O  O   . HOH   H 4 .   ? 17.712 -20.167 25.807 1.00 33.35  ? 441 HOH   C O   1 
HETATM 2533 O  O   . HOH   H 4 .   ? 30.873 -8.999  18.413 1.00 48.44  ? 442 HOH   C O   1 
HETATM 2534 O  O   . HOH   H 4 .   ? -0.494 -36.014 16.824 1.00 31.13  ? 443 HOH   C O   1 
HETATM 2535 O  O   . HOH   H 4 .   ? -0.288 -18.717 21.491 1.00 43.08  ? 444 HOH   C O   1 
HETATM 2536 O  O   . HOH   H 4 .   ? 22.463 -12.649 19.360 1.00 37.54  ? 445 HOH   C O   1 
HETATM 2537 O  O   . HOH   H 4 .   ? 6.934  -36.496 2.929  1.00 24.48  ? 446 HOH   C O   1 
HETATM 2538 O  O   . HOH   H 4 .   ? 6.937  -20.176 4.284  1.00 39.53  ? 447 HOH   C O   1 
HETATM 2539 O  O   . HOH   H 4 .   ? 12.120 -16.952 1.610  1.00 51.08  ? 448 HOH   C O   1 
HETATM 2540 O  O   . HOH   H 4 .   ? 31.594 -26.241 -2.631 1.00 52.18  ? 449 HOH   C O   1 
HETATM 2541 O  O   . HOH   H 4 .   ? -0.048 -34.705 10.262 1.00 56.31  ? 450 HOH   C O   1 
HETATM 2542 O  O   . HOH   H 4 .   ? 4.806  -38.480 6.689  1.00 50.04  ? 451 HOH   C O   1 
HETATM 2543 O  O   . HOH   H 4 .   ? 10.387 -10.023 27.419 1.00 44.04  ? 452 HOH   C O   1 
HETATM 2544 O  O   . HOH   H 4 .   ? 17.175 -34.899 18.163 1.00 30.32  ? 453 HOH   C O   1 
HETATM 2545 O  O   . HOH   H 4 .   ? 30.604 -31.245 13.324 1.00 39.20  ? 454 HOH   C O   1 
HETATM 2546 O  O   . HOH   H 4 .   ? 33.081 -9.264  19.960 1.00 60.29  ? 455 HOH   C O   1 
HETATM 2547 O  O   . HOH   H 4 .   ? 5.724  -27.868 3.060  1.00 27.83  ? 456 HOH   C O   1 
HETATM 2548 O  O   . HOH   H 4 .   ? 4.041  -28.110 32.369 1.00 56.86  ? 457 HOH   C O   1 
HETATM 2549 O  O   . HOH   H 4 .   ? 17.779 -9.869  29.574 1.00 38.15  ? 458 HOH   C O   1 
HETATM 2550 O  O   . HOH   H 4 .   ? 2.763  -28.951 27.554 1.00 38.68  ? 459 HOH   C O   1 
HETATM 2551 O  O   . HOH   H 4 .   ? 10.797 -14.306 26.477 1.00 31.75  ? 460 HOH   C O   1 
HETATM 2552 O  O   . HOH   H 4 .   ? 29.129 -22.065 21.066 1.00 32.53  ? 461 HOH   C O   1 
HETATM 2553 O  O   . HOH   H 4 .   ? 2.185  -17.245 22.833 1.00 37.38  ? 462 HOH   C O   1 
HETATM 2554 O  O   . HOH   H 4 .   ? 15.024 -16.930 25.935 1.00 27.05  ? 463 HOH   C O   1 
HETATM 2555 O  O   . HOH   H 4 .   ? 8.465  -23.987 2.721  1.00 32.28  ? 464 HOH   C O   1 
HETATM 2556 O  O   . HOH   H 4 .   ? -1.728 -13.272 26.296 1.00 50.36  ? 465 HOH   C O   1 
HETATM 2557 O  O   . HOH   H 4 .   ? 8.479  -21.876 30.218 1.00 40.75  ? 466 HOH   C O   1 
HETATM 2558 O  O   . HOH   H 4 .   ? 16.023 -17.672 1.669  1.00 37.40  ? 467 HOH   C O   1 
HETATM 2559 O  O   . HOH   H 4 .   ? 32.557 -19.319 20.920 1.00 26.09  ? 468 HOH   C O   1 
HETATM 2560 O  O   . HOH   H 4 .   ? 31.826 -27.022 13.819 1.00 33.41  ? 469 HOH   C O   1 
HETATM 2561 O  O   . HOH   H 4 .   ? 33.028 -9.149  12.223 1.00 35.76  ? 470 HOH   C O   1 
HETATM 2562 O  O   . HOH   H 4 .   ? 20.185 -18.260 26.541 1.00 40.62  ? 471 HOH   C O   1 
HETATM 2563 O  O   . HOH   H 4 .   ? 5.439  -25.042 2.603  1.00 34.64  ? 472 HOH   C O   1 
HETATM 2564 O  O   . HOH   H 4 .   ? 24.702 -10.959 6.014  1.00 43.22  ? 473 HOH   C O   1 
HETATM 2565 O  O   . HOH   H 4 .   ? 22.803 -21.237 23.581 1.00 39.33  ? 474 HOH   C O   1 
HETATM 2566 O  O   . HOH   H 4 .   ? 13.464 -20.227 31.362 1.00 35.80  ? 475 HOH   C O   1 
HETATM 2567 O  O   . HOH   H 4 .   ? 25.952 -32.985 16.504 1.00 48.51  ? 476 HOH   C O   1 
HETATM 2568 O  O   . HOH   H 4 .   ? 5.446  -39.777 23.436 1.00 28.55  ? 477 HOH   C O   1 
HETATM 2569 O  O   . HOH   H 4 .   ? 2.003  -19.920 19.791 1.00 52.47  ? 478 HOH   C O   1 
HETATM 2570 O  O   . HOH   H 4 .   ? 29.891 -8.442  9.172  1.00 32.00  ? 479 HOH   C O   1 
HETATM 2571 O  O   . HOH   H 4 .   ? 27.821 -31.242 17.993 1.00 46.68  ? 480 HOH   C O   1 
HETATM 2572 O  O   . HOH   H 4 .   ? 30.065 -30.642 15.958 1.00 52.47  ? 481 HOH   C O   1 
HETATM 2573 O  O   . HOH   H 4 .   ? 26.801 -24.407 23.586 1.00 42.65  ? 482 HOH   C O   1 
HETATM 2574 O  O   . HOH   H 4 .   ? 35.584 -9.999  8.222  1.00 46.08  ? 483 HOH   C O   1 
HETATM 2575 O  O   . HOH   H 4 .   ? 14.842 -18.419 30.324 1.00 39.36  ? 484 HOH   C O   1 
HETATM 2576 O  O   . HOH   H 4 .   ? 9.836  -16.498 28.710 1.00 45.48  ? 485 HOH   C O   1 
HETATM 2577 O  O   . HOH   H 4 .   ? 35.648 -10.163 15.631 1.00 33.07  ? 486 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   ? 0.2394 0.2251 0.2483 0.0006  -0.0069 0.0045  7   SER   A N   
2    C  CA  . SER   A 1   ? 0.2377 0.2255 0.2561 -0.0013 -0.0083 0.0040  7   SER   A CA  
3    C  C   . SER   A 1   ? 0.2308 0.2185 0.2528 -0.0030 -0.0072 0.0024  7   SER   A C   
4    O  O   . SER   A 1   ? 0.2360 0.2216 0.2528 -0.0024 -0.0069 0.0012  7   SER   A O   
5    C  CB  . SER   A 1   ? 0.2663 0.2530 0.2862 -0.0007 -0.0136 0.0035  7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.2942 0.2776 0.3098 -0.0003 -0.0174 0.0012  7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.2176 0.2073 0.2482 -0.0046 -0.0060 0.0025  8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.1964 0.1855 0.2306 -0.0060 -0.0043 0.0016  8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.1881 0.1791 0.2284 -0.0069 -0.0003 0.0026  8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.1855 0.1779 0.2252 -0.0065 0.0017  0.0036  8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.1754 0.1657 0.2214 -0.0081 0.0013  0.0023  9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.1794 0.1703 0.2299 -0.0085 0.0057  0.0034  9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.1790 0.1673 0.2296 -0.0089 0.0089  0.0034  9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.1794 0.1658 0.2295 -0.0094 0.0072  0.0025  9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.1890 0.1822 0.2500 -0.0092 0.0052  0.0041  9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.1600 0.1474 0.2107 -0.0084 0.0138  0.0044  10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.1603 0.1446 0.2112 -0.0084 0.0178  0.0051  10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.1615 0.1465 0.2230 -0.0092 0.0209  0.0065  10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.1549 0.1417 0.2191 -0.0088 0.0223  0.0070  10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.1732 0.1551 0.2149 -0.0065 0.0211  0.0055  10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.1766 0.1590 0.2100 -0.0056 0.0180  0.0043  10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.1829 0.1605 0.2232 -0.0059 0.0255  0.0067  10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.1870 0.1684 0.2129 -0.0039 0.0196  0.0041  10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.1688 0.1524 0.2373 -0.0105 0.0223  0.0070  11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.1826 0.1671 0.2633 -0.0113 0.0260  0.0086  11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.1912 0.1711 0.2701 -0.0105 0.0330  0.0106  11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.1999 0.1770 0.2791 -0.0113 0.0334  0.0107  11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.1810 0.1678 0.2740 -0.0137 0.0217  0.0078  11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.1915 0.1821 0.2857 -0.0139 0.0149  0.0063  11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.2098 0.2040 0.3116 -0.0136 0.0148  0.0071  11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.2204 0.2103 0.3069 -0.0138 0.0091  0.0043  11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.2269 0.2240 0.3286 -0.0133 0.0088  0.0061  11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.2419 0.2343 0.3274 -0.0133 0.0035  0.0033  11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.2546 0.2505 0.3477 -0.0131 0.0032  0.0043  11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.2882 0.2859 0.3793 -0.0123 -0.0022 0.0037  11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.1990 0.1774 0.2749 -0.0086 0.0387  0.0121  12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.2138 0.1867 0.2851 -0.0070 0.0458  0.0142  12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.2214 0.1942 0.3003 -0.0062 0.0524  0.0164  12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.2313 0.2059 0.3093 -0.0051 0.0524  0.0158  12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.2452 0.2142 0.2994 -0.0042 0.0460  0.0135  12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.2441 0.2155 0.2931 -0.0032 0.0434  0.0119  12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.2781 0.2405 0.3254 -0.0016 0.0534  0.0159  12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.2235 0.1944 0.3117 -0.0068 0.0581  0.0188  13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.2244 0.1952 0.3213 -0.0059 0.0654  0.0213  13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.2317 0.2093 0.3414 -0.0073 0.0618  0.0203  13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.2355 0.2178 0.3543 -0.0100 0.0549  0.0188  13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.2260 0.2039 0.3345 -0.0051 0.0652  0.0208  14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.2287 0.2128 0.3485 -0.0061 0.0613  0.0200  14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.2067 0.1919 0.3156 -0.0053 0.0553  0.0174  14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.2034 0.1911 0.3162 -0.0045 0.0548  0.0172  14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.2735 0.2581 0.4039 -0.0046 0.0690  0.0224  14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.3458 0.3318 0.4930 -0.0063 0.0736  0.0250  14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.3775 0.3689 0.5398 -0.0093 0.0681  0.0244  14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.3616 0.3420 0.5059 -0.0043 0.0834  0.0278  14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.1889 0.1723 0.2854 -0.0056 0.0506  0.0156  15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.1857 0.1701 0.2725 -0.0050 0.0454  0.0134  15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.1690 0.1563 0.2554 -0.0070 0.0375  0.0117  15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.1686 0.1551 0.2556 -0.0083 0.0362  0.0116  15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.1909 0.1697 0.2611 -0.0027 0.0477  0.0127  15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.2042 0.1785 0.2706 0.0000  0.0551  0.0138  15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.2193 0.1948 0.2904 0.0010  0.0569  0.0139  15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.2249 0.1930 0.2822 0.0021  0.0606  0.0150  15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.2389 0.2092 0.3052 0.0040  0.0641  0.0147  15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.2433 0.2061 0.2953 0.0053  0.0677  0.0161  15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.2594 0.2233 0.3161 0.0062  0.0696  0.0158  15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.2901 0.2480 0.3404 0.0097  0.0769  0.0166  15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.1568 0.1468 0.2411 -0.0070 0.0326  0.0104  16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.1479 0.1398 0.2289 -0.0081 0.0257  0.0090  16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.1611 0.1517 0.2302 -0.0068 0.0248  0.0079  16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.1702 0.1609 0.2391 -0.0059 0.0261  0.0080  16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.1527 0.1490 0.2438 -0.0089 0.0210  0.0090  16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.1666 0.1641 0.2519 -0.0091 0.0145  0.0077  16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.1781 0.1789 0.2722 -0.0095 0.0093  0.0078  16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.2065 0.2079 0.2948 -0.0084 0.0057  0.0077  16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.2526 0.2536 0.3348 -0.0082 0.0005  0.0069  16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.2343 0.2341 0.3146 -0.0090 -0.0021 0.0055  16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.2568 0.2579 0.3340 -0.0069 -0.0016 0.0074  16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.1616 0.1507 0.2218 -0.0068 0.0230  0.0069  17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.1680 0.1563 0.2187 -0.0059 0.0219  0.0059  17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.1707 0.1615 0.2204 -0.0065 0.0168  0.0053  17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.1711 0.1619 0.2199 -0.0071 0.0145  0.0050  17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.1794 0.1644 0.2211 -0.0049 0.0235  0.0054  17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.1787 0.1633 0.2127 -0.0039 0.0222  0.0041  17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.1809 0.1622 0.2223 -0.0038 0.0290  0.0064  17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.1535 0.1456 0.2026 -0.0063 0.0155  0.0053  18  VAL   A N   
86   C  CA  . VAL   A 12  ? 0.1571 0.1508 0.2043 -0.0064 0.0115  0.0053  18  VAL   A CA  
87   C  C   . VAL   A 12  ? 0.1527 0.1464 0.1950 -0.0060 0.0118  0.0050  18  VAL   A C   
88   O  O   . VAL   A 12  ? 0.1603 0.1527 0.2020 -0.0057 0.0141  0.0046  18  VAL   A O   
89   C  CB  . VAL   A 12  ? 0.1787 0.1743 0.2326 -0.0066 0.0091  0.0062  18  VAL   A CB  
90   C  CG1 . VAL   A 12  ? 0.2045 0.2008 0.2644 -0.0073 0.0073  0.0061  18  VAL   A CG1 
91   C  CG2 . VAL   A 12  ? 0.1886 0.1845 0.2472 -0.0061 0.0115  0.0069  18  VAL   A CG2 
92   N  N   . ASN   A 13  ? 0.1446 0.1391 0.1839 -0.0058 0.0095  0.0054  19  ASN   A N   
93   C  CA  . ASN   A 13  ? 0.1467 0.1416 0.1841 -0.0057 0.0100  0.0055  19  ASN   A CA  
94   C  C   . ASN   A 13  ? 0.1506 0.1454 0.1925 -0.0057 0.0105  0.0064  19  ASN   A C   
95   O  O   . ASN   A 13  ? 0.1532 0.1486 0.1984 -0.0055 0.0091  0.0075  19  ASN   A O   
96   C  CB  . ASN   A 13  ? 0.1461 0.1416 0.1803 -0.0053 0.0084  0.0064  19  ASN   A CB  
97   C  CG  . ASN   A 13  ? 0.1692 0.1646 0.1988 -0.0049 0.0080  0.0057  19  ASN   A CG  
98   O  OD1 . ASN   A 13  ? 0.1803 0.1749 0.2082 -0.0046 0.0065  0.0054  19  ASN   A OD1 
99   N  ND2 . ASN   A 13  ? 0.1805 0.1764 0.2084 -0.0048 0.0091  0.0051  19  ASN   A ND2 
100  N  N   . ARG   A 14  ? 0.1405 0.1343 0.1828 -0.0059 0.0123  0.0057  20  ARG   A N   
101  C  CA  . ARG   A 14  ? 0.1322 0.1253 0.1789 -0.0057 0.0131  0.0063  20  ARG   A CA  
102  C  C   . ARG   A 14  ? 0.1378 0.1317 0.1859 -0.0055 0.0116  0.0084  20  ARG   A C   
103  O  O   . ARG   A 14  ? 0.1542 0.1479 0.2062 -0.0049 0.0113  0.0097  20  ARG   A O   
104  C  CB  . ARG   A 14  ? 0.1594 0.1504 0.2051 -0.0060 0.0147  0.0047  20  ARG   A CB  
105  C  CG  . ARG   A 14  ? 0.1605 0.1496 0.2103 -0.0056 0.0162  0.0049  20  ARG   A CG  
106  C  CD  . ARG   A 14  ? 0.1780 0.1646 0.2262 -0.0060 0.0167  0.0028  20  ARG   A CD  
107  N  NE  . ARG   A 14  ? 0.1927 0.1762 0.2436 -0.0054 0.0184  0.0023  20  ARG   A NE  
108  C  CZ  . ARG   A 14  ? 0.1899 0.1728 0.2449 -0.0056 0.0184  0.0037  20  ARG   A CZ  
109  N  NH1 . ARG   A 14  ? 0.1922 0.1773 0.2487 -0.0062 0.0171  0.0060  20  ARG   A NH1 
110  N  NH2 . ARG   A 14  ? 0.1822 0.1616 0.2392 -0.0050 0.0201  0.0028  20  ARG   A NH2 
111  N  N   . HIS   A 15  ? 0.1357 0.1301 0.1804 -0.0056 0.0109  0.0090  21  HIS   A N   
112  C  CA  . HIS   A 15  ? 0.1483 0.1424 0.1926 -0.0048 0.0102  0.0115  21  HIS   A CA  
113  C  C   . HIS   A 15  ? 0.1650 0.1593 0.2080 -0.0036 0.0075  0.0126  21  HIS   A C   
114  O  O   . HIS   A 15  ? 0.1926 0.1859 0.2347 -0.0024 0.0065  0.0148  21  HIS   A O   
115  C  CB  . HIS   A 15  ? 0.1506 0.1449 0.1921 -0.0050 0.0113  0.0123  21  HIS   A CB  
116  C  CG  . HIS   A 15  ? 0.1649 0.1601 0.2014 -0.0045 0.0105  0.0120  21  HIS   A CG  
117  N  ND1 . HIS   A 15  ? 0.1700 0.1663 0.2055 -0.0051 0.0107  0.0099  21  HIS   A ND1 
118  C  CD2 . HIS   A 15  ? 0.1806 0.1751 0.2122 -0.0030 0.0099  0.0135  21  HIS   A CD2 
119  C  CE1 . HIS   A 15  ? 0.1831 0.1796 0.2141 -0.0042 0.0102  0.0102  21  HIS   A CE1 
120  N  NE2 . HIS   A 15  ? 0.1823 0.1775 0.2105 -0.0029 0.0097  0.0122  21  HIS   A NE2 
121  N  N   . LEU   A 16  ? 0.1575 0.1526 0.2004 -0.0038 0.0061  0.0112  22  LEU   A N   
122  C  CA  . LEU   A 16  ? 0.1567 0.1520 0.1994 -0.0030 0.0026  0.0115  22  LEU   A CA  
123  C  C   . LEU   A 16  ? 0.1774 0.1739 0.2279 -0.0033 0.0019  0.0111  22  LEU   A C   
124  O  O   . LEU   A 16  ? 0.1797 0.1769 0.2325 -0.0029 -0.0016 0.0110  22  LEU   A O   
125  C  CB  . LEU   A 16  ? 0.1569 0.1519 0.1947 -0.0030 0.0014  0.0102  22  LEU   A CB  
126  C  CG  . LEU   A 16  ? 0.1709 0.1648 0.2014 -0.0023 0.0024  0.0107  22  LEU   A CG  
127  C  CD1 . LEU   A 16  ? 0.1872 0.1803 0.2128 -0.0020 0.0012  0.0093  22  LEU   A CD1 
128  C  CD2 . LEU   A 16  ? 0.1766 0.1689 0.2033 -0.0005 0.0014  0.0130  22  LEU   A CD2 
129  N  N   . ALA   A 17  ? 0.1699 0.1666 0.2250 -0.0039 0.0051  0.0108  23  ALA   A N   
130  C  CA  . ALA   A 17  ? 0.1685 0.1663 0.2317 -0.0039 0.0055  0.0108  23  ALA   A CA  
131  C  C   . ALA   A 17  ? 0.1753 0.1741 0.2435 -0.0026 0.0025  0.0124  23  ALA   A C   
132  O  O   . ALA   A 17  ? 0.1758 0.1735 0.2415 -0.0016 0.0019  0.0139  23  ALA   A O   
133  C  CB  . ALA   A 17  ? 0.1745 0.1711 0.2397 -0.0040 0.0099  0.0102  23  ALA   A CB  
134  N  N   . THR   A 18  ? 0.1792 0.1801 0.2550 -0.0027 0.0005  0.0123  24  THR   A N   
135  C  CA  . THR   A 18  ? 0.1951 0.1974 0.2769 -0.0012 -0.0034 0.0136  24  THR   A CA  
136  C  C   . THR   A 18  ? 0.2047 0.2079 0.2953 -0.0005 -0.0005 0.0147  24  THR   A C   
137  O  O   . THR   A 18  ? 0.2059 0.2084 0.2979 -0.0011 0.0047  0.0141  24  THR   A O   
138  C  CB  . THR   A 18  ? 0.2234 0.2278 0.3109 -0.0018 -0.0079 0.0126  24  THR   A CB  
139  O  OG1 . THR   A 18  ? 0.2293 0.2356 0.3262 -0.0031 -0.0043 0.0120  24  THR   A OG1 
140  C  CG2 . THR   A 18  ? 0.2345 0.2372 0.3132 -0.0023 -0.0107 0.0112  24  THR   A CG2 
141  N  N   . HIS   A 19  ? 0.2163 0.2209 0.3130 0.0012  -0.0039 0.0163  25  HIS   A N   
142  C  CA  . HIS   A 19  ? 0.2294 0.2351 0.3359 0.0023  -0.0013 0.0174  25  HIS   A CA  
143  C  C   . HIS   A 19  ? 0.1984 0.2065 0.3146 0.0012  0.0022  0.0165  25  HIS   A C   
144  O  O   . HIS   A 19  ? 0.1980 0.2051 0.3171 0.0015  0.0079  0.0166  25  HIS   A O   
145  C  CB  . HIS   A 19  ? 0.2737 0.2812 0.3863 0.0045  -0.0068 0.0192  25  HIS   A CB  
146  C  CG  . HIS   A 19  ? 0.3844 0.3888 0.4880 0.0063  -0.0092 0.0210  25  HIS   A CG  
147  N  ND1 . HIS   A 19  ? 0.4347 0.4356 0.5321 0.0064  -0.0047 0.0218  25  HIS   A ND1 
148  C  CD2 . HIS   A 19  ? 0.4181 0.4219 0.5179 0.0083  -0.0154 0.0222  25  HIS   A CD2 
149  C  CE1 . HIS   A 19  ? 0.4536 0.4520 0.5444 0.0082  -0.0076 0.0238  25  HIS   A CE1 
150  N  NE2 . HIS   A 19  ? 0.4516 0.4514 0.5426 0.0097  -0.0140 0.0242  25  HIS   A NE2 
151  N  N   . ASN   A 20  ? 0.1918 0.2023 0.3119 -0.0001 -0.0007 0.0155  26  ASN   A N   
152  C  CA  . ASN   A 20  ? 0.1913 0.2037 0.3210 -0.0013 0.0031  0.0150  26  ASN   A CA  
153  C  C   . ASN   A 20  ? 0.1799 0.1891 0.3023 -0.0022 0.0098  0.0141  26  ASN   A C   
154  O  O   . ASN   A 20  ? 0.1890 0.1981 0.3171 -0.0020 0.0155  0.0145  26  ASN   A O   
155  C  CB  . ASN   A 20  ? 0.2289 0.2439 0.3647 -0.0028 -0.0017 0.0141  26  ASN   A CB  
156  C  CG  . ASN   A 20  ? 0.3079 0.3271 0.4582 -0.0019 -0.0061 0.0149  26  ASN   A CG  
157  O  OD1 . ASN   A 20  ? 0.3185 0.3398 0.4790 -0.0007 -0.0026 0.0164  26  ASN   A OD1 
158  N  ND2 . ASN   A 20  ? 0.3329 0.3533 0.4838 -0.0022 -0.0141 0.0139  26  ASN   A ND2 
159  N  N   . ASP   A 21  ? 0.1602 0.1666 0.2698 -0.0030 0.0092  0.0130  27  ASP   A N   
160  C  CA  . ASP   A 21  ? 0.1577 0.1610 0.2595 -0.0034 0.0144  0.0119  27  ASP   A CA  
161  C  C   . ASP   A 21  ? 0.1547 0.1556 0.2555 -0.0020 0.0192  0.0122  27  ASP   A C   
162  O  O   . ASP   A 21  ? 0.1679 0.1666 0.2683 -0.0016 0.0246  0.0118  27  ASP   A O   
163  C  CB  . ASP   A 21  ? 0.1574 0.1586 0.2468 -0.0041 0.0122  0.0109  27  ASP   A CB  
164  C  CG  . ASP   A 21  ? 0.2184 0.2204 0.3061 -0.0053 0.0090  0.0100  27  ASP   A CG  
165  O  OD1 . ASP   A 21  ? 0.2160 0.2185 0.3091 -0.0061 0.0107  0.0098  27  ASP   A OD1 
166  O  OD2 . ASP   A 21  ? 0.2216 0.2231 0.3024 -0.0053 0.0051  0.0097  27  ASP   A OD2 
167  N  N   . TRP   A 22  ? 0.1517 0.1521 0.2513 -0.0011 0.0173  0.0129  28  TRP   A N   
168  C  CA  . TRP   A 22  ? 0.1644 0.1619 0.2632 0.0002  0.0212  0.0128  28  TRP   A CA  
169  C  C   . TRP   A 22  ? 0.1778 0.1764 0.2874 0.0017  0.0250  0.0138  28  TRP   A C   
170  O  O   . TRP   A 22  ? 0.1906 0.1857 0.2985 0.0028  0.0303  0.0132  28  TRP   A O   
171  C  CB  . TRP   A 22  ? 0.1699 0.1664 0.2658 0.0008  0.0184  0.0137  28  TRP   A CB  
172  C  CG  . TRP   A 22  ? 0.1724 0.1665 0.2578 -0.0004 0.0177  0.0125  28  TRP   A CG  
173  C  CD1 . TRP   A 22  ? 0.1845 0.1795 0.2648 -0.0011 0.0139  0.0130  28  TRP   A CD1 
174  C  CD2 . TRP   A 22  ? 0.1760 0.1663 0.2554 -0.0006 0.0207  0.0108  28  TRP   A CD2 
175  N  NE1 . TRP   A 22  ? 0.1866 0.1792 0.2595 -0.0020 0.0149  0.0118  28  TRP   A NE1 
176  C  CE2 . TRP   A 22  ? 0.1871 0.1770 0.2596 -0.0019 0.0186  0.0103  28  TRP   A CE2 
177  C  CE3 . TRP   A 22  ? 0.1930 0.1799 0.2718 0.0002  0.0250  0.0093  28  TRP   A CE3 
178  C  CZ2 . TRP   A 22  ? 0.1907 0.1777 0.2576 -0.0025 0.0199  0.0084  28  TRP   A CZ2 
179  C  CZ3 . TRP   A 22  ? 0.1991 0.1822 0.2707 -0.0003 0.0259  0.0071  28  TRP   A CZ3 
180  C  CH2 . TRP   A 22  ? 0.1913 0.1749 0.2578 -0.0018 0.0231  0.0066  28  TRP   A CH2 
181  N  N   . ALA   A 23  ? 0.1707 0.1737 0.2915 0.0018  0.0224  0.0152  29  ALA   A N   
182  C  CA  . ALA   A 23  ? 0.1932 0.1981 0.3268 0.0032  0.0263  0.0165  29  ALA   A CA  
183  C  C   . ALA   A 23  ? 0.2007 0.2049 0.3364 0.0028  0.0323  0.0162  29  ALA   A C   
184  O  O   . ALA   A 23  ? 0.2125 0.2170 0.3571 0.0043  0.0377  0.0172  29  ALA   A O   
185  C  CB  . ALA   A 23  ? 0.1994 0.2097 0.3454 0.0035  0.0209  0.0180  29  ALA   A CB  
186  N  N   . ASN   A 24  ? 0.1913 0.1945 0.3198 0.0010  0.0316  0.0151  30  ASN   A N   
187  C  CA  . ASN   A 24  ? 0.1914 0.1930 0.3200 0.0007  0.0372  0.0151  30  ASN   A CA  
188  C  C   . ASN   A 24  ? 0.1869 0.1829 0.2993 0.0008  0.0395  0.0133  30  ASN   A C   
189  O  O   . ASN   A 24  ? 0.1835 0.1779 0.2918 0.0001  0.0414  0.0131  30  ASN   A O   
190  C  CB  . ASN   A 24  ? 0.1967 0.2021 0.3333 -0.0014 0.0340  0.0155  30  ASN   A CB  
191  C  CG  . ASN   A 24  ? 0.2419 0.2529 0.3962 -0.0014 0.0318  0.0169  30  ASN   A CG  
192  O  OD1 . ASN   A 24  ? 0.2545 0.2667 0.4201 -0.0005 0.0374  0.0185  30  ASN   A OD1 
193  N  ND2 . ASN   A 24  ? 0.2361 0.2504 0.3931 -0.0021 0.0236  0.0166  30  ASN   A ND2 
194  N  N   . LEU   A 25  ? 0.1834 0.1762 0.2872 0.0018  0.0392  0.0121  31  LEU   A N   
195  C  CA  . LEU   A 25  ? 0.1885 0.1764 0.2780 0.0019  0.0399  0.0101  31  LEU   A CA  
196  C  C   . LEU   A 25  ? 0.1989 0.1819 0.2824 0.0035  0.0464  0.0096  31  LEU   A C   
197  O  O   . LEU   A 25  ? 0.2189 0.1997 0.3059 0.0056  0.0520  0.0103  31  LEU   A O   
198  C  CB  . LEU   A 25  ? 0.1887 0.1743 0.2737 0.0026  0.0385  0.0090  31  LEU   A CB  
199  C  CG  . LEU   A 25  ? 0.2013 0.1821 0.2734 0.0026  0.0382  0.0065  31  LEU   A CG  
200  C  CD1 . LEU   A 25  ? 0.2057 0.1888 0.2729 0.0005  0.0333  0.0060  31  LEU   A CD1 
201  C  CD2 . LEU   A 25  ? 0.2102 0.1884 0.2806 0.0032  0.0373  0.0054  31  LEU   A CD2 
202  N  N   . VAL   A 26  ? 0.1949 0.1756 0.2687 0.0030  0.0459  0.0086  32  VAL   A N   
203  C  CA  . VAL   A 26  ? 0.2103 0.1851 0.2750 0.0050  0.0514  0.0081  32  VAL   A CA  
204  C  C   . VAL   A 26  ? 0.2276 0.1976 0.2785 0.0058  0.0493  0.0052  32  VAL   A C   
205  O  O   . VAL   A 26  ? 0.2479 0.2120 0.2914 0.0083  0.0529  0.0039  32  VAL   A O   
206  C  CB  . VAL   A 26  ? 0.2190 0.1942 0.2831 0.0041  0.0524  0.0093  32  VAL   A CB  
207  C  CG1 . VAL   A 26  ? 0.2374 0.2055 0.2891 0.0066  0.0575  0.0088  32  VAL   A CG1 
208  C  CG2 . VAL   A 26  ? 0.2267 0.2060 0.3059 0.0033  0.0550  0.0119  32  VAL   A CG2 
209  N  N   . TRP   A 27  ? 0.2167 0.1892 0.2647 0.0038  0.0433  0.0041  33  TRP   A N   
210  C  CA  . TRP   A 27  ? 0.2134 0.1826 0.2509 0.0041  0.0404  0.0014  33  TRP   A CA  
211  C  C   . TRP   A 27  ? 0.1915 0.1653 0.2313 0.0016  0.0344  0.0012  33  TRP   A C   
212  O  O   . TRP   A 27  ? 0.1852 0.1633 0.2295 0.0001  0.0324  0.0027  33  TRP   A O   
213  C  CB  . TRP   A 27  ? 0.2232 0.1884 0.2500 0.0054  0.0416  0.0006  33  TRP   A CB  
214  C  CG  . TRP   A 27  ? 0.2341 0.1970 0.2512 0.0055  0.0373  -0.0022 33  TRP   A CG  
215  C  CD1 . TRP   A 27  ? 0.2534 0.2110 0.2626 0.0071  0.0368  -0.0050 33  TRP   A CD1 
216  C  CD2 . TRP   A 27  ? 0.2262 0.1923 0.2416 0.0039  0.0327  -0.0026 33  TRP   A CD2 
217  N  NE1 . TRP   A 27  ? 0.2627 0.2206 0.2665 0.0064  0.0317  -0.0072 33  TRP   A NE1 
218  C  CE2 . TRP   A 27  ? 0.2426 0.2057 0.2500 0.0046  0.0295  -0.0055 33  TRP   A CE2 
219  C  CE3 . TRP   A 27  ? 0.2337 0.2046 0.2534 0.0022  0.0308  -0.0009 33  TRP   A CE3 
220  C  CZ2 . TRP   A 27  ? 0.2425 0.2081 0.2477 0.0037  0.0249  -0.0064 33  TRP   A CZ2 
221  C  CZ3 . TRP   A 27  ? 0.2408 0.2133 0.2568 0.0015  0.0268  -0.0018 33  TRP   A CZ3 
222  C  CH2 . TRP   A 27  ? 0.2392 0.2094 0.2487 0.0022  0.0240  -0.0043 33  TRP   A CH2 
223  N  N   . GLU   A 28  ? 0.1876 0.1602 0.2243 0.0013  0.0317  -0.0007 34  GLU   A N   
224  C  CA  . GLU   A 28  ? 0.1785 0.1548 0.2168 -0.0008 0.0270  -0.0007 34  GLU   A CA  
225  C  C   . GLU   A 28  ? 0.1824 0.1560 0.2147 -0.0009 0.0246  -0.0035 34  GLU   A C   
226  O  O   . GLU   A 28  ? 0.1987 0.1674 0.2272 0.0004  0.0259  -0.0056 34  GLU   A O   
227  C  CB  . GLU   A 28  ? 0.1689 0.1485 0.2157 -0.0018 0.0258  0.0012  34  GLU   A CB  
228  C  CG  . GLU   A 28  ? 0.1899 0.1666 0.2396 -0.0008 0.0278  0.0008  34  GLU   A CG  
229  C  CD  . GLU   A 28  ? 0.2429 0.2165 0.2898 -0.0012 0.0263  -0.0013 34  GLU   A CD  
230  O  OE1 . GLU   A 28  ? 0.2879 0.2570 0.3338 0.0002  0.0286  -0.0028 34  GLU   A OE1 
231  O  OE2 . GLU   A 28  ? 0.2169 0.1924 0.2631 -0.0028 0.0231  -0.0016 34  GLU   A OE2 
232  N  N   . ASP   A 29  ? 0.1665 0.1431 0.1984 -0.0024 0.0211  -0.0036 35  ASP   A N   
233  C  CA  . ASP   A 29  ? 0.1737 0.1488 0.2025 -0.0028 0.0183  -0.0062 35  ASP   A CA  
234  C  C   . ASP   A 29  ? 0.1707 0.1503 0.2045 -0.0049 0.0156  -0.0050 35  ASP   A C   
235  O  O   . ASP   A 29  ? 0.1682 0.1510 0.2013 -0.0052 0.0145  -0.0039 35  ASP   A O   
236  C  CB  . ASP   A 29  ? 0.2104 0.1830 0.2307 -0.0014 0.0176  -0.0080 35  ASP   A CB  
237  C  CG  . ASP   A 29  ? 0.2950 0.2655 0.3116 -0.0014 0.0139  -0.0113 35  ASP   A CG  
238  O  OD1 . ASP   A 29  ? 0.3088 0.2816 0.3313 -0.0033 0.0115  -0.0117 35  ASP   A OD1 
239  O  OD2 . ASP   A 29  ? 0.3275 0.2938 0.3356 0.0006  0.0133  -0.0134 35  ASP   A OD2 
240  N  N   . SER   A 30  ? 0.1774 0.1568 0.2162 -0.0060 0.0151  -0.0049 36  SER   A N   
241  C  CA  A SER   A 30  ? 0.1780 0.1610 0.2217 -0.0077 0.0136  -0.0033 36  SER   A CA  
242  C  CA  B SER   A 30  ? 0.1823 0.1654 0.2258 -0.0076 0.0137  -0.0032 36  SER   A CA  
243  C  C   . SER   A 30  ? 0.1792 0.1640 0.2216 -0.0083 0.0112  -0.0048 36  SER   A C   
244  O  O   . SER   A 30  ? 0.1814 0.1698 0.2259 -0.0090 0.0107  -0.0030 36  SER   A O   
245  C  CB  A SER   A 30  ? 0.1915 0.1726 0.2405 -0.0086 0.0140  -0.0032 36  SER   A CB  
246  C  CB  B SER   A 30  ? 0.2073 0.1890 0.2565 -0.0086 0.0142  -0.0026 36  SER   A CB  
247  O  OG  A SER   A 30  ? 0.2049 0.1846 0.2559 -0.0078 0.0161  -0.0015 36  SER   A OG  
248  O  OG  B SER   A 30  ? 0.2365 0.2144 0.2852 -0.0089 0.0131  -0.0059 36  SER   A OG  
249  N  N   . SER   A 31  ? 0.1830 0.1648 0.2216 -0.0078 0.0094  -0.0082 37  SER   A N   
250  C  CA  . SER   A 31  ? 0.1949 0.1786 0.2332 -0.0082 0.0063  -0.0098 37  SER   A CA  
251  C  C   . SER   A 31  ? 0.1881 0.1746 0.2225 -0.0071 0.0062  -0.0086 37  SER   A C   
252  O  O   . SER   A 31  ? 0.1909 0.1804 0.2272 -0.0075 0.0042  -0.0089 37  SER   A O   
253  C  CB  . SER   A 31  ? 0.2459 0.2253 0.2805 -0.0075 0.0034  -0.0140 37  SER   A CB  
254  O  OG  . SER   A 31  ? 0.3140 0.2899 0.3389 -0.0050 0.0038  -0.0153 37  SER   A OG  
255  N  N   . ARG   A 32  ? 0.1667 0.1521 0.1967 -0.0059 0.0085  -0.0073 38  ARG   A N   
256  C  CA  . ARG   A 32  ? 0.1600 0.1472 0.1866 -0.0050 0.0087  -0.0060 38  ARG   A CA  
257  C  C   . ARG   A 32  ? 0.1627 0.1529 0.1925 -0.0057 0.0102  -0.0030 38  ARG   A C   
258  O  O   . ARG   A 32  ? 0.1658 0.1572 0.1931 -0.0051 0.0103  -0.0021 38  ARG   A O   
259  C  CB  . ARG   A 32  ? 0.1680 0.1511 0.1873 -0.0030 0.0104  -0.0067 38  ARG   A CB  
260  C  CG  . ARG   A 32  ? 0.1795 0.1585 0.1924 -0.0014 0.0086  -0.0097 38  ARG   A CG  
261  C  CD  . ARG   A 32  ? 0.1862 0.1601 0.1907 0.0011  0.0112  -0.0098 38  ARG   A CD  
262  N  NE  . ARG   A 32  ? 0.1733 0.1484 0.1753 0.0018  0.0120  -0.0080 38  ARG   A NE  
263  C  CZ  . ARG   A 32  ? 0.2031 0.1739 0.1968 0.0043  0.0135  -0.0080 38  ARG   A CZ  
264  N  NH1 . ARG   A 32  ? 0.1964 0.1612 0.1822 0.0066  0.0141  -0.0098 38  ARG   A NH1 
265  N  NH2 . ARG   A 32  ? 0.1964 0.1681 0.1888 0.0047  0.0143  -0.0062 38  ARG   A NH2 
266  N  N   . ASP   A 33  ? 0.1604 0.1511 0.1948 -0.0066 0.0112  -0.0016 39  ASP   A N   
267  C  CA  . ASP   A 33  ? 0.1593 0.1518 0.1957 -0.0067 0.0120  0.0010  39  ASP   A CA  
268  C  C   . ASP   A 33  ? 0.1536 0.1452 0.1879 -0.0059 0.0130  0.0013  39  ASP   A C   
269  O  O   . ASP   A 33  ? 0.1541 0.1472 0.1882 -0.0059 0.0125  0.0026  39  ASP   A O   
270  C  CB  . ASP   A 33  ? 0.1729 0.1683 0.2094 -0.0069 0.0112  0.0023  39  ASP   A CB  
271  C  CG  . ASP   A 33  ? 0.1631 0.1593 0.1998 -0.0066 0.0114  0.0047  39  ASP   A CG  
272  O  OD1 . ASP   A 33  ? 0.1618 0.1572 0.2011 -0.0067 0.0118  0.0058  39  ASP   A OD1 
273  O  OD2 . ASP   A 33  ? 0.1617 0.1589 0.1955 -0.0060 0.0109  0.0052  39  ASP   A OD2 
274  N  N   . LEU   A 34  ? 0.1462 0.1349 0.1791 -0.0052 0.0146  0.0003  40  LEU   A N   
275  C  CA  . LEU   A 34  ? 0.1443 0.1321 0.1770 -0.0046 0.0164  0.0010  40  LEU   A CA  
276  C  C   . LEU   A 34  ? 0.1532 0.1399 0.1904 -0.0043 0.0186  0.0016  40  LEU   A C   
277  O  O   . LEU   A 34  ? 0.1528 0.1374 0.1901 -0.0039 0.0195  0.0007  40  LEU   A O   
278  C  CB  . LEU   A 34  ? 0.1508 0.1357 0.1775 -0.0033 0.0178  -0.0002 40  LEU   A CB  
279  C  CG  . LEU   A 34  ? 0.1656 0.1513 0.1880 -0.0030 0.0161  -0.0005 40  LEU   A CG  
280  C  CD1 . LEU   A 34  ? 0.1858 0.1674 0.2014 -0.0012 0.0177  -0.0013 40  LEU   A CD1 
281  C  CD2 . LEU   A 34  ? 0.1721 0.1602 0.1969 -0.0037 0.0154  0.0010  40  LEU   A CD2 
282  N  N   . LEU   A 35  ? 0.1550 0.1429 0.1963 -0.0043 0.0194  0.0031  41  LEU   A N   
283  C  CA  . LEU   A 35  ? 0.1499 0.1373 0.1970 -0.0038 0.0219  0.0039  41  LEU   A CA  
284  C  C   . LEU   A 35  ? 0.1462 0.1338 0.1960 -0.0037 0.0238  0.0048  41  LEU   A C   
285  O  O   . LEU   A 35  ? 0.1411 0.1303 0.1912 -0.0046 0.0217  0.0052  41  LEU   A O   
286  C  CB  . LEU   A 35  ? 0.1511 0.1411 0.2046 -0.0043 0.0199  0.0053  41  LEU   A CB  
287  C  CG  . LEU   A 35  ? 0.1679 0.1581 0.2292 -0.0035 0.0221  0.0064  41  LEU   A CG  
288  C  CD1 . LEU   A 35  ? 0.1826 0.1733 0.2473 -0.0032 0.0207  0.0072  41  LEU   A CD1 
289  C  CD2 . LEU   A 35  ? 0.1565 0.1494 0.2249 -0.0039 0.0214  0.0077  41  LEU   A CD2 
290  N  N   . VAL   A 36  ? 0.1412 0.1265 0.1930 -0.0026 0.0281  0.0051  42  VAL   A N   
291  C  CA  . VAL   A 36  ? 0.1510 0.1362 0.2073 -0.0025 0.0312  0.0064  42  VAL   A CA  
292  C  C   . VAL   A 36  ? 0.1691 0.1559 0.2360 -0.0022 0.0334  0.0078  42  VAL   A C   
293  O  O   . VAL   A 36  ? 0.1794 0.1644 0.2461 -0.0009 0.0359  0.0076  42  VAL   A O   
294  C  CB  . VAL   A 36  ? 0.1686 0.1487 0.2167 -0.0009 0.0357  0.0061  42  VAL   A CB  
295  C  CG1 . VAL   A 36  ? 0.1770 0.1565 0.2310 -0.0008 0.0401  0.0080  42  VAL   A CG1 
296  C  CG2 . VAL   A 36  ? 0.1862 0.1650 0.2245 -0.0009 0.0329  0.0048  42  VAL   A CG2 
297  N  N   . SER   A 37  ? 0.1669 0.1572 0.2434 -0.0034 0.0323  0.0091  43  SER   A N   
298  C  CA  . SER   A 37  ? 0.1772 0.1701 0.2665 -0.0032 0.0339  0.0106  43  SER   A CA  
299  C  C   . SER   A 37  ? 0.1888 0.1817 0.2856 -0.0036 0.0380  0.0119  43  SER   A C   
300  O  O   . SER   A 37  ? 0.1777 0.1691 0.2706 -0.0044 0.0381  0.0118  43  SER   A O   
301  C  CB  . SER   A 37  ? 0.1900 0.1874 0.2860 -0.0042 0.0276  0.0108  43  SER   A CB  
302  O  OG  . SER   A 37  ? 0.2090 0.2081 0.3057 -0.0058 0.0232  0.0104  43  SER   A OG  
303  N  N   . SER   A 38  ? 0.1832 0.1779 0.2919 -0.0029 0.0417  0.0135  44  SER   A N   
304  C  CA  . SER   A 38  ? 0.1930 0.1879 0.3113 -0.0033 0.0465  0.0153  44  SER   A CA  
305  C  C   . SER   A 38  ? 0.2032 0.2036 0.3355 -0.0057 0.0412  0.0156  44  SER   A C   
306  O  O   . SER   A 38  ? 0.2052 0.2094 0.3425 -0.0062 0.0351  0.0150  44  SER   A O   
307  C  CB  . SER   A 38  ? 0.2095 0.2032 0.3341 -0.0011 0.0543  0.0170  44  SER   A CB  
308  O  OG  . SER   A 38  ? 0.2478 0.2457 0.3820 -0.0007 0.0517  0.0173  44  SER   A OG  
309  N  N   . THR   A 39  ? 0.2116 0.2117 0.3503 -0.0072 0.0435  0.0165  45  THR   A N   
310  C  CA  . THR   A 39  ? 0.2312 0.2360 0.3839 -0.0097 0.0380  0.0162  45  THR   A CA  
311  C  C   . THR   A 39  ? 0.2539 0.2604 0.4240 -0.0103 0.0439  0.0186  45  THR   A C   
312  O  O   . THR   A 39  ? 0.2651 0.2678 0.4328 -0.0089 0.0528  0.0205  45  THR   A O   
313  C  CB  . THR   A 39  ? 0.2560 0.2585 0.4013 -0.0115 0.0339  0.0147  45  THR   A CB  
314  O  OG1 . THR   A 39  ? 0.2769 0.2750 0.4188 -0.0113 0.0412  0.0161  45  THR   A OG1 
315  C  CG2 . THR   A 39  ? 0.2614 0.2621 0.3899 -0.0108 0.0290  0.0127  45  THR   A CG2 
316  N  N   . THR   A 40  ? 0.2663 0.2782 0.4537 -0.0122 0.0390  0.0185  46  THR   A N   
317  C  CA  . THR   A 40  ? 0.2818 0.2961 0.4888 -0.0133 0.0443  0.0207  46  THR   A CA  
318  C  C   . THR   A 40  ? 0.2891 0.3008 0.4980 -0.0158 0.0452  0.0207  46  THR   A C   
319  O  O   . THR   A 40  ? 0.3097 0.3201 0.5281 -0.0162 0.0533  0.0233  46  THR   A O   
320  C  CB  . THR   A 40  ? 0.3063 0.3282 0.5333 -0.0142 0.0381  0.0205  46  THR   A CB  
321  O  OG1 . THR   A 40  ? 0.3302 0.3536 0.5544 -0.0159 0.0267  0.0176  46  THR   A OG1 
322  C  CG2 . THR   A 40  ? 0.3112 0.3354 0.5399 -0.0114 0.0395  0.0215  46  THR   A CG2 
323  N  N   . ALA   A 41  ? 0.2820 0.2925 0.4821 -0.0174 0.0373  0.0180  47  ALA   A N   
324  C  CA  . ALA   A 41  ? 0.2861 0.2934 0.4870 -0.0197 0.0375  0.0176  47  ALA   A CA  
325  C  C   . ALA   A 41  ? 0.2941 0.2943 0.4752 -0.0181 0.0430  0.0182  47  ALA   A C   
326  O  O   . ALA   A 41  ? 0.2839 0.2821 0.4486 -0.0159 0.0427  0.0175  47  ALA   A O   
327  C  CB  . ALA   A 41  ? 0.2915 0.3004 0.4932 -0.0218 0.0261  0.0142  47  ALA   A CB  
328  N  N   . GLN   A 42  ? 0.3046 0.3008 0.4880 -0.0192 0.0479  0.0196  48  GLN   A N   
329  C  CA  . GLN   A 42  ? 0.3338 0.3230 0.4998 -0.0175 0.0532  0.0205  48  GLN   A CA  
330  C  C   . GLN   A 42  ? 0.3429 0.3299 0.4951 -0.0180 0.0456  0.0175  48  GLN   A C   
331  O  O   . GLN   A 42  ? 0.3509 0.3392 0.5103 -0.0206 0.0394  0.0155  48  GLN   A O   
332  C  CB  . GLN   A 42  ? 0.3862 0.3716 0.5610 -0.0184 0.0615  0.0236  48  GLN   A CB  
333  C  CG  . GLN   A 42  ? 0.4840 0.4613 0.6411 -0.0163 0.0669  0.0249  48  GLN   A CG  
334  C  CD  . GLN   A 42  ? 0.5854 0.5588 0.7304 -0.0123 0.0753  0.0273  48  GLN   A CD  
335  O  OE1 . GLN   A 42  ? 0.6068 0.5828 0.7579 -0.0110 0.0789  0.0284  48  GLN   A OE1 
336  N  NE2 . GLN   A 42  ? 0.6172 0.5836 0.7444 -0.0098 0.0784  0.0279  48  GLN   A NE2 
337  N  N   . GLY   A 43  ? 0.3386 0.3224 0.4720 -0.0155 0.0462  0.0169  49  GLY   A N   
338  C  CA  . GLY   A 43  ? 0.3502 0.3320 0.4702 -0.0155 0.0404  0.0145  49  GLY   A CA  
339  C  C   . GLY   A 43  ? 0.3670 0.3424 0.4794 -0.0148 0.0450  0.0158  49  GLY   A C   
340  O  O   . GLY   A 43  ? 0.3730 0.3446 0.4823 -0.0130 0.0531  0.0186  49  GLY   A O   
341  N  N   . CYS   A 44  ? 0.3657 0.3392 0.4739 -0.0159 0.0402  0.0139  50  CYS   A N   
342  C  CA  . CYS   A 44  ? 0.3718 0.3390 0.4738 -0.0153 0.0443  0.0153  50  CYS   A CA  
343  C  C   . CYS   A 44  ? 0.3561 0.3204 0.4403 -0.0131 0.0417  0.0139  50  CYS   A C   
344  O  O   . CYS   A 44  ? 0.3697 0.3290 0.4489 -0.0125 0.0434  0.0146  50  CYS   A O   
345  C  CB  . CYS   A 44  ? 0.3982 0.3641 0.5130 -0.0184 0.0428  0.0149  50  CYS   A CB  
346  S  SG  . CYS   A 44  ? 0.5692 0.5391 0.7083 -0.0212 0.0459  0.0166  50  CYS   A SG  
347  N  N   . ASP   A 45  ? 0.3275 0.2950 0.4033 -0.0117 0.0378  0.0122  51  ASP   A N   
348  C  CA  . ASP   A 45  ? 0.3102 0.2757 0.3709 -0.0096 0.0356  0.0111  51  ASP   A CA  
349  C  C   . ASP   A 45  ? 0.3076 0.2683 0.3586 -0.0066 0.0422  0.0135  51  ASP   A C   
350  O  O   . ASP   A 45  ? 0.3300 0.2900 0.3840 -0.0059 0.0476  0.0154  51  ASP   A O   
351  C  CB  . ASP   A 45  ? 0.3124 0.2826 0.3683 -0.0091 0.0302  0.0089  51  ASP   A CB  
352  C  CG  . ASP   A 45  ? 0.3617 0.3346 0.4187 -0.0105 0.0231  0.0064  51  ASP   A CG  
353  O  OD1 . ASP   A 45  ? 0.3672 0.3372 0.4196 -0.0103 0.0211  0.0053  51  ASP   A OD1 
354  O  OD2 . ASP   A 45  ? 0.3229 0.3000 0.3834 -0.0111 0.0195  0.0054  51  ASP   A OD2 
355  N  N   . THR   A 46  ? 0.2789 0.2360 0.3185 -0.0046 0.0418  0.0134  52  THR   A N   
356  C  CA  . THR   A 46  ? 0.2718 0.2236 0.3000 -0.0011 0.0466  0.0153  52  THR   A CA  
357  C  C   . THR   A 46  ? 0.2463 0.2002 0.2636 0.0009  0.0424  0.0134  52  THR   A C   
358  O  O   . THR   A 46  ? 0.2394 0.1959 0.2551 0.0004  0.0372  0.0114  52  THR   A O   
359  C  CB  . THR   A 46  ? 0.3097 0.2557 0.3334 -0.0001 0.0483  0.0167  52  THR   A CB  
360  O  OG1 . THR   A 46  ? 0.3247 0.2678 0.3585 -0.0018 0.0531  0.0189  52  THR   A OG1 
361  C  CG2 . THR   A 46  ? 0.3193 0.2597 0.3283 0.0043  0.0512  0.0183  52  THR   A CG2 
362  N  N   . ILE   A 47  ? 0.2246 0.1768 0.2345 0.0034  0.0449  0.0139  53  ILE   A N   
363  C  CA  . ILE   A 47  ? 0.2118 0.1658 0.2127 0.0052  0.0407  0.0118  53  ILE   A CA  
364  C  C   . ILE   A 47  ? 0.2154 0.1642 0.2042 0.0086  0.0411  0.0125  53  ILE   A C   
365  O  O   . ILE   A 47  ? 0.2273 0.1698 0.2104 0.0110  0.0463  0.0149  53  ILE   A O   
366  C  CB  . ILE   A 47  ? 0.2166 0.1712 0.2157 0.0060  0.0420  0.0113  53  ILE   A CB  
367  C  CG1 . ILE   A 47  ? 0.2292 0.1884 0.2406 0.0032  0.0423  0.0111  53  ILE   A CG1 
368  C  CG2 . ILE   A 47  ? 0.2182 0.1750 0.2102 0.0072  0.0369  0.0088  53  ILE   A CG2 
369  C  CD1 . ILE   A 47  ? 0.2490 0.2146 0.2669 0.0005  0.0360  0.0091  53  ILE   A CD1 
370  N  N   . ALA   A 48  ? 0.2036 0.1547 0.1883 0.0092  0.0360  0.0108  54  ALA   A N   
371  C  CA  . ALA   A 48  ? 0.2077 0.1548 0.1817 0.0128  0.0353  0.0113  54  ALA   A CA  
372  C  C   . ALA   A 48  ? 0.2244 0.1687 0.1888 0.0158  0.0355  0.0107  54  ALA   A C   
373  O  O   . ALA   A 48  ? 0.2239 0.1717 0.1902 0.0148  0.0334  0.0088  54  ALA   A O   
374  C  CB  . ALA   A 48  ? 0.1858 0.1371 0.1598 0.0126  0.0296  0.0094  54  ALA   A CB  
375  N  N   . ARG   A 49  ? 0.2319 0.1694 0.1855 0.0197  0.0375  0.0123  55  ARG   A N   
376  C  CA  . ARG   A 49  ? 0.2438 0.1774 0.1857 0.0233  0.0369  0.0115  55  ARG   A CA  
377  C  C   . ARG   A 49  ? 0.2704 0.2018 0.2033 0.0268  0.0329  0.0113  55  ARG   A C   
378  O  O   . ARG   A 49  ? 0.2951 0.2194 0.2194 0.0302  0.0360  0.0139  55  ARG   A O   
379  C  CB  . ARG   A 49  ? 0.2537 0.1795 0.1895 0.0256  0.0443  0.0141  55  ARG   A CB  
380  C  CG  . ARG   A 49  ? 0.2610 0.1891 0.2077 0.0223  0.0490  0.0148  55  ARG   A CG  
381  C  CD  . ARG   A 49  ? 0.2775 0.2110 0.2284 0.0205  0.0456  0.0117  55  ARG   A CD  
382  N  NE  . ARG   A 49  ? 0.2738 0.2091 0.2351 0.0180  0.0503  0.0128  55  ARG   A NE  
383  C  CZ  . ARG   A 49  ? 0.3011 0.2417 0.2702 0.0155  0.0483  0.0109  55  ARG   A CZ  
384  N  NH1 . ARG   A 49  ? 0.2866 0.2312 0.2544 0.0150  0.0420  0.0079  55  ARG   A NH1 
385  N  NH2 . ARG   A 49  ? 0.2793 0.2215 0.2584 0.0137  0.0526  0.0123  55  ARG   A NH2 
386  N  N   . CYS   A 50  ? 0.2640 0.2018 0.2004 0.0259  0.0264  0.0087  56  CYS   A N   
387  C  CA  . CYS   A 50  ? 0.2653 0.2030 0.1971 0.0286  0.0221  0.0086  56  CYS   A CA  
388  C  C   . CYS   A 50  ? 0.2736 0.2180 0.2084 0.0282  0.0150  0.0052  56  CYS   A C   
389  O  O   . CYS   A 50  ? 0.2780 0.2267 0.2185 0.0255  0.0137  0.0032  56  CYS   A O   
390  C  CB  . CYS   A 50  ? 0.2632 0.2024 0.2018 0.0269  0.0235  0.0101  56  CYS   A CB  
391  S  SG  . CYS   A 50  ? 0.2678 0.2165 0.2208 0.0217  0.0210  0.0081  56  CYS   A SG  
392  N  N   . ASP   A 51  ? 0.2812 0.2268 0.2138 0.0307  0.0106  0.0049  57  ASP   A N   
393  C  CA  . ASP   A 51  ? 0.2983 0.2510 0.2366 0.0300  0.0042  0.0020  57  ASP   A CA  
394  C  C   . ASP   A 51  ? 0.2859 0.2442 0.2327 0.0288  0.0031  0.0025  57  ASP   A C   
395  O  O   . ASP   A 51  ? 0.2908 0.2536 0.2406 0.0300  -0.0017 0.0012  57  ASP   A O   
396  C  CB  . ASP   A 51  ? 0.3560 0.3062 0.2854 0.0343  -0.0012 0.0004  57  ASP   A CB  
397  C  CG  . ASP   A 51  ? 0.4802 0.4259 0.4014 0.0389  -0.0023 0.0023  57  ASP   A CG  
398  O  OD1 . ASP   A 51  ? 0.4810 0.4240 0.4021 0.0391  0.0022  0.0052  57  ASP   A OD1 
399  O  OD2 . ASP   A 51  ? 0.5610 0.5057 0.4762 0.0425  -0.0081 0.0008  57  ASP   A OD2 
400  N  N   . CYS   A 52  ? 0.2671 0.2252 0.2183 0.0266  0.0075  0.0042  58  CYS   A N   
401  C  CA  . CYS   A 52  ? 0.2510 0.2134 0.2091 0.0257  0.0069  0.0044  58  CYS   A CA  
402  C  C   . CYS   A 52  ? 0.2400 0.2105 0.2069 0.0235  0.0036  0.0024  58  CYS   A C   
403  O  O   . CYS   A 52  ? 0.2393 0.2121 0.2096 0.0209  0.0036  0.0012  58  CYS   A O   
404  C  CB  . CYS   A 52  ? 0.2618 0.2221 0.2231 0.0232  0.0114  0.0058  58  CYS   A CB  
405  S  SG  . CYS   A 52  ? 0.2700 0.2210 0.2240 0.0256  0.0157  0.0087  58  CYS   A SG  
406  N  N   . GLN   A 53  ? 0.2117 0.1863 0.1827 0.0248  0.0013  0.0022  59  GLN   A N   
407  C  CA  . GLN   A 53  ? 0.1951 0.1772 0.1755 0.0229  -0.0005 0.0010  59  GLN   A CA  
408  C  C   . GLN   A 53  ? 0.1924 0.1763 0.1771 0.0223  0.0020  0.0018  59  GLN   A C   
409  O  O   . GLN   A 53  ? 0.1824 0.1719 0.1739 0.0220  0.0011  0.0014  59  GLN   A O   
410  C  CB  . GLN   A 53  ? 0.2228 0.2094 0.2064 0.0250  -0.0054 -0.0003 59  GLN   A CB  
411  C  CG  . GLN   A 53  ? 0.2779 0.2639 0.2591 0.0247  -0.0086 -0.0021 59  GLN   A CG  
412  C  CD  . GLN   A 53  ? 0.3200 0.3115 0.3072 0.0261  -0.0143 -0.0038 59  GLN   A CD  
413  O  OE1 . GLN   A 53  ? 0.3455 0.3347 0.3273 0.0293  -0.0184 -0.0046 59  GLN   A OE1 
414  N  NE2 . GLN   A 53  ? 0.2879 0.2865 0.2867 0.0237  -0.0145 -0.0043 59  GLN   A NE2 
415  N  N   . THR   A 54  ? 0.1874 0.1658 0.1678 0.0224  0.0051  0.0030  60  THR   A N   
416  C  CA  . THR   A 54  ? 0.1966 0.1750 0.1794 0.0216  0.0072  0.0033  60  THR   A CA  
417  C  C   . THR   A 54  ? 0.1903 0.1643 0.1717 0.0189  0.0099  0.0035  60  THR   A C   
418  O  O   . THR   A 54  ? 0.1943 0.1643 0.1721 0.0187  0.0110  0.0042  60  THR   A O   
419  C  CB  . THR   A 54  ? 0.2236 0.1994 0.2039 0.0250  0.0076  0.0042  60  THR   A CB  
420  O  OG1 . THR   A 54  ? 0.2483 0.2169 0.2219 0.0264  0.0089  0.0054  60  THR   A OG1 
421  C  CG2 . THR   A 54  ? 0.2385 0.2190 0.2217 0.0281  0.0046  0.0041  60  THR   A CG2 
422  N  N   . GLY   A 55  ? 0.1780 0.1527 0.1621 0.0172  0.0108  0.0030  61  GLY   A N   
423  C  CA  . GLY   A 55  ? 0.1816 0.1529 0.1660 0.0146  0.0124  0.0029  61  GLY   A CA  
424  C  C   . GLY   A 55  ? 0.1807 0.1528 0.1670 0.0135  0.0123  0.0019  61  GLY   A C   
425  O  O   . GLY   A 55  ? 0.1794 0.1532 0.1654 0.0154  0.0121  0.0016  61  GLY   A O   
426  N  N   . VAL   A 56  ? 0.1634 0.1338 0.1512 0.0109  0.0124  0.0013  62  VAL   A N   
427  C  CA  . VAL   A 56  ? 0.1687 0.1385 0.1567 0.0101  0.0116  0.0001  62  VAL   A CA  
428  C  C   . VAL   A 56  ? 0.1701 0.1427 0.1616 0.0075  0.0106  -0.0002 62  VAL   A C   
429  O  O   . VAL   A 56  ? 0.1805 0.1527 0.1747 0.0057  0.0110  0.0002  62  VAL   A O   
430  C  CB  . VAL   A 56  ? 0.1971 0.1605 0.1835 0.0099  0.0118  -0.0007 62  VAL   A CB  
431  C  CG1 . VAL   A 56  ? 0.2069 0.1688 0.1923 0.0092  0.0101  -0.0025 62  VAL   A CG1 
432  C  CG2 . VAL   A 56  ? 0.1956 0.1558 0.1785 0.0129  0.0130  -0.0002 62  VAL   A CG2 
433  N  N   . TYR   A 57  ? 0.1614 0.1365 0.1526 0.0076  0.0098  -0.0006 63  TYR   A N   
434  C  CA  . TYR   A 57  ? 0.1592 0.1364 0.1533 0.0054  0.0087  -0.0007 63  TYR   A CA  
435  C  C   . TYR   A 57  ? 0.1676 0.1422 0.1593 0.0053  0.0069  -0.0018 63  TYR   A C   
436  O  O   . TYR   A 57  ? 0.1594 0.1315 0.1463 0.0073  0.0070  -0.0026 63  TYR   A O   
437  C  CB  . TYR   A 57  ? 0.1573 0.1398 0.1537 0.0054  0.0092  0.0003  63  TYR   A CB  
438  C  CG  . TYR   A 57  ? 0.1594 0.1436 0.1539 0.0071  0.0099  0.0007  63  TYR   A CG  
439  C  CD1 . TYR   A 57  ? 0.1780 0.1629 0.1712 0.0094  0.0112  0.0009  63  TYR   A CD1 
440  C  CD2 . TYR   A 57  ? 0.1633 0.1483 0.1575 0.0066  0.0095  0.0011  63  TYR   A CD2 
441  C  CE1 . TYR   A 57  ? 0.1842 0.1707 0.1766 0.0112  0.0128  0.0016  63  TYR   A CE1 
442  C  CE2 . TYR   A 57  ? 0.1781 0.1638 0.1699 0.0085  0.0112  0.0019  63  TYR   A CE2 
443  C  CZ  . TYR   A 57  ? 0.1920 0.1788 0.1834 0.0107  0.0131  0.0022  63  TYR   A CZ  
444  O  OH  . TYR   A 57  ? 0.2058 0.1935 0.1957 0.0128  0.0157  0.0033  63  TYR   A OH  
445  N  N   . TYR   A 58  ? 0.1547 0.1297 0.1493 0.0033  0.0051  -0.0021 64  TYR   A N   
446  C  CA  . TYR   A 58  ? 0.1597 0.1321 0.1514 0.0035  0.0024  -0.0034 64  TYR   A CA  
447  C  C   . TYR   A 58  ? 0.1695 0.1446 0.1588 0.0045  0.0027  -0.0023 64  TYR   A C   
448  O  O   . TYR   A 58  ? 0.1676 0.1464 0.1611 0.0034  0.0033  -0.0010 64  TYR   A O   
449  C  CB  . TYR   A 58  ? 0.1557 0.1270 0.1526 0.0010  -0.0003 -0.0042 64  TYR   A CB  
450  C  CG  . TYR   A 58  ? 0.1753 0.1437 0.1687 0.0015  -0.0043 -0.0060 64  TYR   A CG  
451  C  CD1 . TYR   A 58  ? 0.1979 0.1609 0.1854 0.0029  -0.0060 -0.0081 64  TYR   A CD1 
452  C  CD2 . TYR   A 58  ? 0.1834 0.1537 0.1784 0.0010  -0.0066 -0.0055 64  TYR   A CD2 
453  C  CE1 . TYR   A 58  ? 0.2153 0.1745 0.1976 0.0039  -0.0102 -0.0100 64  TYR   A CE1 
454  C  CE2 . TYR   A 58  ? 0.2060 0.1730 0.1962 0.0021  -0.0109 -0.0071 64  TYR   A CE2 
455  C  CZ  . TYR   A 58  ? 0.2334 0.1947 0.2169 0.0035  -0.0128 -0.0095 64  TYR   A CZ  
456  O  OH  . TYR   A 58  ? 0.2730 0.2301 0.2500 0.0050  -0.0176 -0.0115 64  TYR   A OH  
457  N  N   . CYS   A 59  ? 0.1717 0.1440 0.1539 0.0069  0.0025  -0.0029 65  CYS   A N   
458  C  CA  . CYS   A 59  ? 0.1705 0.1440 0.1491 0.0085  0.0035  -0.0015 65  CYS   A CA  
459  C  C   . CYS   A 59  ? 0.1866 0.1556 0.1593 0.0093  -0.0002 -0.0027 65  CYS   A C   
460  O  O   . CYS   A 59  ? 0.2039 0.1676 0.1690 0.0113  -0.0014 -0.0045 65  CYS   A O   
461  C  CB  . CYS   A 59  ? 0.1875 0.1609 0.1619 0.0113  0.0072  -0.0007 65  CYS   A CB  
462  S  SG  . CYS   A 59  ? 0.2132 0.1867 0.1824 0.0139  0.0099  0.0015  65  CYS   A SG  
463  N  N   . SER   A 60  ? 0.1825 0.1534 0.1587 0.0079  -0.0023 -0.0020 66  SER   A N   
464  C  CA  . SER   A 60  ? 0.1985 0.1654 0.1698 0.0087  -0.0069 -0.0032 66  SER   A CA  
465  C  C   . SER   A 60  ? 0.2020 0.1649 0.1618 0.0124  -0.0060 -0.0026 66  SER   A C   
466  O  O   . SER   A 60  ? 0.2158 0.1730 0.1677 0.0142  -0.0100 -0.0048 66  SER   A O   
467  C  CB  . SER   A 60  ? 0.2351 0.2051 0.2132 0.0068  -0.0093 -0.0023 66  SER   A CB  
468  O  OG  . SER   A 60  ? 0.3231 0.2966 0.3025 0.0071  -0.0058 0.0006  66  SER   A OG  
469  N  N   . SER   A 61  ? 0.1911 0.1564 0.1496 0.0139  -0.0008 0.0001  67  SER   A N   
470  C  CA  . SER   A 61  ? 0.2043 0.1655 0.1519 0.0178  0.0015  0.0014  67  SER   A CA  
471  C  C   . SER   A 61  ? 0.2063 0.1622 0.1450 0.0207  0.0027  -0.0004 67  SER   A C   
472  O  O   . SER   A 61  ? 0.2174 0.1688 0.1455 0.0246  0.0050  0.0004  67  SER   A O   
473  C  CB  . SER   A 61  ? 0.2247 0.1903 0.1757 0.0182  0.0073  0.0052  67  SER   A CB  
474  O  OG  . SER   A 61  ? 0.2328 0.2026 0.1905 0.0173  0.0111  0.0056  67  SER   A OG  
475  N  N   . ARG   A 62  ? 0.2020 0.1580 0.1446 0.0192  0.0017  -0.0028 68  ARG   A N   
476  C  CA  . ARG   A 62  ? 0.2088 0.1591 0.1436 0.0218  0.0022  -0.0050 68  ARG   A CA  
477  C  C   . ARG   A 62  ? 0.2295 0.1756 0.1649 0.0200  -0.0038 -0.0089 68  ARG   A C   
478  O  O   . ARG   A 62  ? 0.2367 0.1771 0.1661 0.0217  -0.0042 -0.0113 68  ARG   A O   
479  C  CB  . ARG   A 62  ? 0.2201 0.1744 0.1604 0.0219  0.0074  -0.0036 68  ARG   A CB  
480  C  CG  . ARG   A 62  ? 0.2211 0.1791 0.1619 0.0240  0.0134  -0.0001 68  ARG   A CG  
481  C  CD  . ARG   A 62  ? 0.2451 0.1968 0.1733 0.0288  0.0164  0.0000  68  ARG   A CD  
482  N  NE  . ARG   A 62  ? 0.2674 0.2227 0.1976 0.0307  0.0230  0.0038  68  ARG   A NE  
483  C  CZ  . ARG   A 62  ? 0.2825 0.2385 0.2112 0.0312  0.0249  0.0066  68  ARG   A CZ  
484  N  NH1 . ARG   A 62  ? 0.2805 0.2334 0.2044 0.0305  0.0202  0.0059  68  ARG   A NH1 
485  N  NH2 . ARG   A 62  ? 0.2718 0.2311 0.2040 0.0327  0.0315  0.0102  68  ARG   A NH2 
486  N  N   . ARG   A 63  ? 0.2301 0.1791 0.1740 0.0164  -0.0078 -0.0094 69  ARG   A N   
487  C  CA  . ARG   A 63  ? 0.2508 0.1972 0.1992 0.0139  -0.0128 -0.0125 69  ARG   A CA  
488  C  C   . ARG   A 63  ? 0.2425 0.1879 0.1934 0.0135  -0.0102 -0.0134 69  ARG   A C   
489  O  O   . ARG   A 63  ? 0.2497 0.1891 0.1976 0.0137  -0.0128 -0.0164 69  ARG   A O   
490  C  CB  . ARG   A 63  ? 0.3018 0.2407 0.2413 0.0156  -0.0188 -0.0159 69  ARG   A CB  
491  C  CG  . ARG   A 63  ? 0.3705 0.3101 0.3081 0.0160  -0.0226 -0.0152 69  ARG   A CG  
492  C  CD  . ARG   A 63  ? 0.4232 0.3568 0.3581 0.0159  -0.0309 -0.0193 69  ARG   A CD  
493  N  NE  . ARG   A 63  ? 0.4583 0.3911 0.3884 0.0175  -0.0353 -0.0189 69  ARG   A NE  
494  C  CZ  . ARG   A 63  ? 0.5010 0.4267 0.4155 0.0219  -0.0377 -0.0199 69  ARG   A CZ  
495  N  NH1 . ARG   A 63  ? 0.5201 0.4388 0.4224 0.0252  -0.0357 -0.0217 69  ARG   A NH1 
496  N  NH2 . ARG   A 63  ? 0.4829 0.4079 0.3931 0.0236  -0.0415 -0.0190 69  ARG   A NH2 
497  N  N   . LYS   A 64  ? 0.2199 0.1706 0.1756 0.0132  -0.0051 -0.0107 70  LYS   A N   
498  C  CA  . LYS   A 64  ? 0.2237 0.1733 0.1808 0.0136  -0.0023 -0.0110 70  LYS   A CA  
499  C  C   . LYS   A 64  ? 0.2199 0.1759 0.1862 0.0115  0.0005  -0.0087 70  LYS   A C   
500  O  O   . LYS   A 64  ? 0.2150 0.1764 0.1852 0.0106  0.0015  -0.0066 70  LYS   A O   
501  C  CB  . LYS   A 64  ? 0.2521 0.2002 0.2014 0.0176  0.0017  -0.0103 70  LYS   A CB  
502  C  CG  . LYS   A 64  ? 0.3695 0.3091 0.3080 0.0207  0.0005  -0.0132 70  LYS   A CG  
503  C  CD  . LYS   A 64  ? 0.4499 0.3893 0.3831 0.0248  0.0060  -0.0117 70  LYS   A CD  
504  C  CE  . LYS   A 64  ? 0.5386 0.4692 0.4617 0.0282  0.0059  -0.0146 70  LYS   A CE  
505  N  NZ  . LYS   A 64  ? 0.6048 0.5289 0.5155 0.0309  0.0039  -0.0162 70  LYS   A NZ  
506  N  N   . HIS   A 65  ? 0.2085 0.1630 0.1774 0.0111  0.0016  -0.0090 71  HIS   A N   
507  C  CA  . HIS   A 65  ? 0.1874 0.1465 0.1624 0.0102  0.0043  -0.0069 71  HIS   A CA  
508  C  C   . HIS   A 65  ? 0.1934 0.1537 0.1656 0.0133  0.0076  -0.0058 71  HIS   A C   
509  O  O   . HIS   A 65  ? 0.2096 0.1655 0.1761 0.0158  0.0083  -0.0069 71  HIS   A O   
510  C  CB  . HIS   A 65  ? 0.1856 0.1419 0.1649 0.0083  0.0039  -0.0074 71  HIS   A CB  
511  C  CG  . HIS   A 65  ? 0.2010 0.1569 0.1859 0.0051  0.0011  -0.0081 71  HIS   A CG  
512  N  ND1 . HIS   A 65  ? 0.2379 0.1979 0.2297 0.0029  0.0022  -0.0064 71  HIS   A ND1 
513  C  CD2 . HIS   A 65  ? 0.2027 0.1546 0.1879 0.0039  -0.0026 -0.0105 71  HIS   A CD2 
514  C  CE1 . HIS   A 65  ? 0.2252 0.1840 0.2221 0.0005  -0.0004 -0.0075 71  HIS   A CE1 
515  N  NE2 . HIS   A 65  ? 0.2336 0.1879 0.2273 0.0009  -0.0038 -0.0100 71  HIS   A NE2 
516  N  N   . TYR   A 66  ? 0.1792 0.1455 0.1558 0.0132  0.0095  -0.0037 72  TYR   A N   
517  C  CA  . TYR   A 66  ? 0.1833 0.1519 0.1596 0.0159  0.0122  -0.0026 72  TYR   A CA  
518  C  C   . TYR   A 66  ? 0.1834 0.1547 0.1642 0.0156  0.0126  -0.0014 72  TYR   A C   
519  O  O   . TYR   A 66  ? 0.1654 0.1396 0.1500 0.0134  0.0118  -0.0008 72  TYR   A O   
520  C  CB  . TYR   A 66  ? 0.1903 0.1640 0.1680 0.0168  0.0139  -0.0011 72  TYR   A CB  
521  C  CG  . TYR   A 66  ? 0.1969 0.1676 0.1684 0.0183  0.0145  -0.0016 72  TYR   A CG  
522  C  CD1 . TYR   A 66  ? 0.2169 0.1836 0.1823 0.0218  0.0164  -0.0023 72  TYR   A CD1 
523  C  CD2 . TYR   A 66  ? 0.2113 0.1827 0.1822 0.0169  0.0133  -0.0013 72  TYR   A CD2 
524  C  CE1 . TYR   A 66  ? 0.2248 0.1874 0.1823 0.0238  0.0172  -0.0028 72  TYR   A CE1 
525  C  CE2 . TYR   A 66  ? 0.2269 0.1946 0.1902 0.0190  0.0138  -0.0015 72  TYR   A CE2 
526  C  CZ  . TYR   A 66  ? 0.2461 0.2091 0.2021 0.0225  0.0157  -0.0024 72  TYR   A CZ  
527  O  OH  . TYR   A 66  ? 0.2757 0.2341 0.2225 0.0251  0.0164  -0.0026 72  TYR   A OH  
528  N  N   . PRO   A 67  ? 0.1901 0.1606 0.1700 0.0182  0.0138  -0.0011 73  PRO   A N   
529  C  CA  . PRO   A 67  ? 0.1823 0.1555 0.1654 0.0186  0.0137  0.0001  73  PRO   A CA  
530  C  C   . PRO   A 67  ? 0.1896 0.1701 0.1777 0.0189  0.0137  0.0012  73  PRO   A C   
531  O  O   . PRO   A 67  ? 0.2066 0.1900 0.1961 0.0201  0.0151  0.0015  73  PRO   A O   
532  C  CB  . PRO   A 67  ? 0.1935 0.1629 0.1737 0.0217  0.0146  0.0002  73  PRO   A CB  
533  C  CG  . PRO   A 67  ? 0.2043 0.1727 0.1819 0.0237  0.0161  -0.0006 73  PRO   A CG  
534  C  CD  . PRO   A 67  ? 0.1862 0.1532 0.1618 0.0213  0.0152  -0.0017 73  PRO   A CD  
535  N  N   . VAL   A 68  ? 0.1779 0.1612 0.1689 0.0180  0.0124  0.0017  74  VAL   A N   
536  C  CA  . VAL   A 68  ? 0.1744 0.1642 0.1711 0.0178  0.0116  0.0022  74  VAL   A CA  
537  C  C   . VAL   A 68  ? 0.1831 0.1740 0.1806 0.0191  0.0096  0.0023  74  VAL   A C   
538  O  O   . VAL   A 68  ? 0.1841 0.1706 0.1771 0.0192  0.0091  0.0024  74  VAL   A O   
539  C  CB  . VAL   A 68  ? 0.1957 0.1877 0.1950 0.0146  0.0111  0.0020  74  VAL   A CB  
540  C  CG1 . VAL   A 68  ? 0.2070 0.1997 0.2066 0.0140  0.0128  0.0023  74  VAL   A CG1 
541  C  CG2 . VAL   A 68  ? 0.1988 0.1869 0.1952 0.0126  0.0105  0.0016  74  VAL   A CG2 
542  N  N   . SER   A 69  ? 0.1763 0.1730 0.1797 0.0202  0.0084  0.0025  75  SER   A N   
543  C  CA  . SER   A 69  ? 0.1826 0.1812 0.1875 0.0212  0.0052  0.0022  75  SER   A CA  
544  C  C   . SER   A 69  ? 0.1795 0.1822 0.1896 0.0183  0.0039  0.0015  75  SER   A C   
545  O  O   . SER   A 69  ? 0.1757 0.1824 0.1918 0.0172  0.0054  0.0018  75  SER   A O   
546  C  CB  . SER   A 69  ? 0.2186 0.2213 0.2286 0.0243  0.0041  0.0026  75  SER   A CB  
547  O  OG  . SER   A 69  ? 0.3033 0.3014 0.3078 0.0270  0.0054  0.0032  75  SER   A OG  
548  N  N   . PHE   A 70  ? 0.1696 0.1703 0.1768 0.0172  0.0019  0.0006  76  PHE   A N   
549  C  CA  . PHE   A 70  ? 0.1609 0.1644 0.1725 0.0145  0.0009  -0.0003 76  PHE   A CA  
550  C  C   . PHE   A 70  ? 0.1741 0.1785 0.1863 0.0152  -0.0033 -0.0018 76  PHE   A C   
551  O  O   . PHE   A 70  ? 0.1935 0.1946 0.1996 0.0177  -0.0052 -0.0021 76  PHE   A O   
552  C  CB  . PHE   A 70  ? 0.1616 0.1614 0.1695 0.0120  0.0030  -0.0002 76  PHE   A CB  
553  C  CG  . PHE   A 70  ? 0.1708 0.1644 0.1707 0.0127  0.0038  0.0000  76  PHE   A CG  
554  C  CD1 . PHE   A 70  ? 0.1887 0.1786 0.1850 0.0134  0.0059  0.0009  76  PHE   A CD1 
555  C  CD2 . PHE   A 70  ? 0.1838 0.1748 0.1802 0.0127  0.0026  -0.0008 76  PHE   A CD2 
556  C  CE1 . PHE   A 70  ? 0.1927 0.1769 0.1832 0.0138  0.0072  0.0014  76  PHE   A CE1 
557  C  CE2 . PHE   A 70  ? 0.1909 0.1759 0.1803 0.0135  0.0045  -0.0001 76  PHE   A CE2 
558  C  CZ  . PHE   A 70  ? 0.1994 0.1812 0.1866 0.0139  0.0068  0.0012  76  PHE   A CZ  
559  N  N   . SER   A 71  ? 0.1691 0.1773 0.1882 0.0132  -0.0048 -0.0029 77  SER   A N   
560  C  CA  . SER   A 71  ? 0.1665 0.1752 0.1864 0.0136  -0.0096 -0.0050 77  SER   A CA  
561  C  C   . SER   A 71  ? 0.1815 0.1841 0.1924 0.0133  -0.0099 -0.0060 77  SER   A C   
562  O  O   . SER   A 71  ? 0.1937 0.1934 0.2014 0.0117  -0.0062 -0.0051 77  SER   A O   
563  C  CB  . SER   A 71  ? 0.1745 0.1889 0.2059 0.0112  -0.0110 -0.0059 77  SER   A CB  
564  O  OG  . SER   A 71  ? 0.2093 0.2229 0.2417 0.0082  -0.0077 -0.0053 77  SER   A OG  
565  N  N   . LYS   A 72  ? 0.1838 0.1841 0.1903 0.0152  -0.0142 -0.0080 78  LYS   A N   
566  C  CA  . LYS   A 72  ? 0.1994 0.1933 0.1965 0.0154  -0.0142 -0.0091 78  LYS   A CA  
567  C  C   . LYS   A 72  ? 0.1994 0.1942 0.2013 0.0120  -0.0129 -0.0100 78  LYS   A C   
568  O  O   . LYS   A 72  ? 0.1970 0.1972 0.2092 0.0098  -0.0144 -0.0108 78  LYS   A O   
569  C  CB  . LYS   A 72  ? 0.2351 0.2263 0.2262 0.0186  -0.0199 -0.0114 78  LYS   A CB  
570  C  CG  . LYS   A 72  ? 0.2809 0.2691 0.2644 0.0226  -0.0203 -0.0099 78  LYS   A CG  
571  C  CD  . LYS   A 72  ? 0.3664 0.3504 0.3412 0.0264  -0.0261 -0.0120 78  LYS   A CD  
572  C  CE  . LYS   A 72  ? 0.4528 0.4318 0.4176 0.0305  -0.0249 -0.0097 78  LYS   A CE  
573  N  NZ  . LYS   A 72  ? 0.5127 0.4854 0.4653 0.0351  -0.0299 -0.0112 78  LYS   A NZ  
574  N  N   . PRO   A 73  ? 0.1968 0.1865 0.1921 0.0115  -0.0099 -0.0099 79  PRO   A N   
575  C  CA  . PRO   A 73  ? 0.1966 0.1867 0.1963 0.0086  -0.0087 -0.0106 79  PRO   A CA  
576  C  C   . PRO   A 73  ? 0.1982 0.1899 0.2025 0.0078  -0.0135 -0.0137 79  PRO   A C   
577  O  O   . PRO   A 73  ? 0.1989 0.1873 0.1971 0.0102  -0.0177 -0.0161 79  PRO   A O   
578  C  CB  . PRO   A 73  ? 0.2173 0.2006 0.2077 0.0095  -0.0056 -0.0104 79  PRO   A CB  
579  C  CG  . PRO   A 73  ? 0.2371 0.2170 0.2199 0.0121  -0.0037 -0.0086 79  PRO   A CG  
580  C  CD  . PRO   A 73  ? 0.2032 0.1861 0.1873 0.0138  -0.0072 -0.0087 79  PRO   A CD  
581  N  N   . SER   A 74  ? 0.1874 0.1837 0.2025 0.0048  -0.0132 -0.0136 80  SER   A N   
582  C  CA  . SER   A 74  ? 0.2083 0.2065 0.2303 0.0035  -0.0177 -0.0165 80  SER   A CA  
583  C  C   . SER   A 74  ? 0.1986 0.1985 0.2291 0.0001  -0.0153 -0.0160 80  SER   A C   
584  O  O   . SER   A 74  ? 0.1876 0.1877 0.2182 -0.0010 -0.0105 -0.0134 80  SER   A O   
585  C  CB  . SER   A 74  ? 0.2606 0.2645 0.2905 0.0042  -0.0216 -0.0169 80  SER   A CB  
586  O  OG  . SER   A 74  ? 0.3275 0.3372 0.3671 0.0024  -0.0180 -0.0140 80  SER   A OG  
587  N  N   . LEU   A 75  ? 0.2014 0.2025 0.2395 -0.0016 -0.0190 -0.0186 81  LEU   A N   
588  C  CA  . LEU   A 75  ? 0.2136 0.2159 0.2606 -0.0048 -0.0170 -0.0182 81  LEU   A CA  
589  C  C   . LEU   A 75  ? 0.2033 0.2128 0.2629 -0.0064 -0.0156 -0.0158 81  LEU   A C   
590  O  O   . LEU   A 75  ? 0.2070 0.2205 0.2741 -0.0064 -0.0194 -0.0171 81  LEU   A O   
591  C  CB  . LEU   A 75  ? 0.2368 0.2365 0.2866 -0.0058 -0.0221 -0.0225 81  LEU   A CB  
592  C  CG  . LEU   A 75  ? 0.3001 0.2921 0.3401 -0.0050 -0.0219 -0.0247 81  LEU   A CG  
593  C  CD1 . LEU   A 75  ? 0.3255 0.3145 0.3674 -0.0054 -0.0282 -0.0297 81  LEU   A CD1 
594  C  CD2 . LEU   A 75  ? 0.3147 0.3059 0.3579 -0.0071 -0.0165 -0.0224 81  LEU   A CD2 
595  N  N   . ILE   A 76  ? 0.1883 0.1991 0.2503 -0.0076 -0.0101 -0.0122 82  ILE   A N   
596  C  CA  . ILE   A 76  ? 0.1940 0.2105 0.2658 -0.0085 -0.0074 -0.0093 82  ILE   A CA  
597  C  C   . ILE   A 76  ? 0.1923 0.2088 0.2708 -0.0110 -0.0038 -0.0073 82  ILE   A C   
598  O  O   . ILE   A 76  ? 0.1860 0.1986 0.2585 -0.0112 -0.0015 -0.0065 82  ILE   A O   
599  C  CB  . ILE   A 76  ? 0.2120 0.2292 0.2770 -0.0064 -0.0041 -0.0065 82  ILE   A CB  
600  C  CG1 . ILE   A 76  ? 0.2407 0.2581 0.3007 -0.0038 -0.0076 -0.0082 82  ILE   A CG1 
601  C  CG2 . ILE   A 76  ? 0.2152 0.2365 0.2873 -0.0068 0.0002  -0.0031 82  ILE   A CG2 
602  C  CD1 . ILE   A 76  ? 0.2785 0.2952 0.3312 -0.0017 -0.0051 -0.0062 82  ILE   A CD1 
603  N  N   . PHE   A 77  ? 0.1835 0.2043 0.2749 -0.0127 -0.0031 -0.0064 83  PHE   A N   
604  C  CA  . PHE   A 77  ? 0.1919 0.2122 0.2900 -0.0149 0.0010  -0.0039 83  PHE   A CA  
605  C  C   . PHE   A 77  ? 0.1991 0.2191 0.2921 -0.0137 0.0068  0.0005  83  PHE   A C   
606  O  O   . PHE   A 77  ? 0.2104 0.2333 0.3028 -0.0121 0.0087  0.0024  83  PHE   A O   
607  C  CB  . PHE   A 77  ? 0.1934 0.2183 0.3079 -0.0170 0.0008  -0.0036 83  PHE   A CB  
608  C  CG  . PHE   A 77  ? 0.2389 0.2616 0.3604 -0.0196 0.0041  -0.0019 83  PHE   A CG  
609  C  CD1 . PHE   A 77  ? 0.2650 0.2891 0.3911 -0.0198 0.0106  0.0030  83  PHE   A CD1 
610  C  CD2 . PHE   A 77  ? 0.2738 0.2921 0.3952 -0.0212 0.0011  -0.0050 83  PHE   A CD2 
611  C  CE1 . PHE   A 77  ? 0.2754 0.2969 0.4072 -0.0217 0.0139  0.0051  83  PHE   A CE1 
612  C  CE2 . PHE   A 77  ? 0.2917 0.3073 0.4189 -0.0233 0.0044  -0.0031 83  PHE   A CE2 
613  C  CZ  . PHE   A 77  ? 0.2786 0.2960 0.4114 -0.0236 0.0107  0.0020  83  PHE   A CZ  
614  N  N   . VAL   A 78  ? 0.1805 0.1965 0.2690 -0.0142 0.0091  0.0019  84  VAL   A N   
615  C  CA  . VAL   A 78  ? 0.1764 0.1912 0.2590 -0.0128 0.0137  0.0058  84  VAL   A CA  
616  C  C   . VAL   A 78  ? 0.1884 0.2020 0.2771 -0.0142 0.0174  0.0088  84  VAL   A C   
617  O  O   . VAL   A 78  ? 0.2005 0.2112 0.2915 -0.0157 0.0165  0.0077  84  VAL   A O   
618  C  CB  . VAL   A 78  ? 0.1854 0.1962 0.2562 -0.0115 0.0126  0.0050  84  VAL   A CB  
619  C  CG1 . VAL   A 78  ? 0.1980 0.2075 0.2628 -0.0100 0.0161  0.0084  84  VAL   A CG1 
620  C  CG2 . VAL   A 78  ? 0.1824 0.1935 0.2470 -0.0102 0.0095  0.0023  84  VAL   A CG2 
621  N  N   . GLU   A 79  ? 0.1905 0.2054 0.2805 -0.0131 0.0221  0.0127  85  GLU   A N   
622  C  CA  . GLU   A 79  ? 0.2047 0.2179 0.2994 -0.0138 0.0268  0.0165  85  GLU   A CA  
623  C  C   . GLU   A 79  ? 0.2063 0.2143 0.2937 -0.0134 0.0270  0.0175  85  GLU   A C   
624  O  O   . GLU   A 79  ? 0.1954 0.2017 0.2729 -0.0120 0.0249  0.0164  85  GLU   A O   
625  C  CB  . GLU   A 79  ? 0.2804 0.2944 0.3722 -0.0114 0.0320  0.0207  85  GLU   A CB  
626  C  CG  . GLU   A 79  ? 0.4080 0.4270 0.5109 -0.0118 0.0343  0.0216  85  GLU   A CG  
627  C  CD  . GLU   A 79  ? 0.5521 0.5695 0.6524 -0.0095 0.0414  0.0269  85  GLU   A CD  
628  O  OE1 . GLU   A 79  ? 0.5957 0.6120 0.7033 -0.0106 0.0459  0.0302  85  GLU   A OE1 
629  O  OE2 . GLU   A 79  ? 0.5960 0.6125 0.6858 -0.0065 0.0426  0.0277  85  GLU   A OE2 
630  N  N   . ALA   A 80  ? 0.2040 0.2097 0.2971 -0.0146 0.0299  0.0200  86  ALA   A N   
631  C  CA  . ALA   A 80  ? 0.2074 0.2083 0.2942 -0.0138 0.0302  0.0214  86  ALA   A CA  
632  C  C   . ALA   A 80  ? 0.2128 0.2119 0.2879 -0.0106 0.0319  0.0243  86  ALA   A C   
633  O  O   . ALA   A 80  ? 0.2129 0.2131 0.2860 -0.0090 0.0350  0.0268  86  ALA   A O   
634  C  CB  . ALA   A 80  ? 0.2212 0.2193 0.3161 -0.0152 0.0337  0.0242  86  ALA   A CB  
635  N  N   . SER   A 81  ? 0.2087 0.2049 0.2766 -0.0095 0.0296  0.0238  87  SER   A N   
636  C  CA  . SER   A 81  ? 0.2074 0.2014 0.2646 -0.0065 0.0297  0.0259  87  SER   A CA  
637  C  C   . SER   A 81  ? 0.2106 0.2007 0.2663 -0.0059 0.0293  0.0275  87  SER   A C   
638  O  O   . SER   A 81  ? 0.2063 0.1954 0.2692 -0.0078 0.0295  0.0269  87  SER   A O   
639  C  CB  . SER   A 81  ? 0.2166 0.2123 0.2676 -0.0058 0.0258  0.0227  87  SER   A CB  
640  O  OG  . SER   A 81  ? 0.2190 0.2143 0.2709 -0.0069 0.0226  0.0198  87  SER   A OG  
641  N  N   . GLU   A 82  ? 0.2134 0.2010 0.2602 -0.0032 0.0284  0.0293  88  GLU   A N   
642  C  CA  . GLU   A 82  ? 0.2322 0.2166 0.2783 -0.0023 0.0273  0.0308  88  GLU   A CA  
643  C  C   . GLU   A 82  ? 0.2239 0.2094 0.2733 -0.0038 0.0237  0.0270  88  GLU   A C   
644  O  O   . GLU   A 82  ? 0.2294 0.2126 0.2810 -0.0035 0.0233  0.0277  88  GLU   A O   
645  C  CB  . GLU   A 82  ? 0.3162 0.2975 0.3522 0.0013  0.0264  0.0336  88  GLU   A CB  
646  C  CG  . GLU   A 82  ? 0.4538 0.4366 0.4839 0.0022  0.0219  0.0308  88  GLU   A CG  
647  C  CD  . GLU   A 82  ? 0.6323 0.6117 0.6524 0.0058  0.0198  0.0330  88  GLU   A CD  
648  O  OE1 . GLU   A 82  ? 0.6633 0.6425 0.6825 0.0066  0.0154  0.0319  88  GLU   A OE1 
649  O  OE2 . GLU   A 82  ? 0.7015 0.6780 0.7148 0.0081  0.0226  0.0360  88  GLU   A OE2 
650  N  N   . TYR   A 83  ? 0.2125 0.2011 0.2621 -0.0050 0.0216  0.0233  89  TYR   A N   
651  C  CA  . TYR   A 83  ? 0.2100 0.1993 0.2615 -0.0059 0.0191  0.0199  89  TYR   A CA  
652  C  C   . TYR   A 83  ? 0.1989 0.1884 0.2566 -0.0082 0.0194  0.0172  89  TYR   A C   
653  O  O   . TYR   A 83  ? 0.2035 0.1916 0.2630 -0.0085 0.0185  0.0153  89  TYR   A O   
654  C  CB  . TYR   A 83  ? 0.2139 0.2054 0.2609 -0.0055 0.0167  0.0177  89  TYR   A CB  
655  C  CG  . TYR   A 83  ? 0.2395 0.2304 0.2798 -0.0033 0.0154  0.0196  89  TYR   A CG  
656  C  CD1 . TYR   A 83  ? 0.2684 0.2600 0.3039 -0.0024 0.0161  0.0201  89  TYR   A CD1 
657  C  CD2 . TYR   A 83  ? 0.2568 0.2464 0.2958 -0.0018 0.0133  0.0206  89  TYR   A CD2 
658  C  CE1 . TYR   A 83  ? 0.2921 0.2822 0.3202 -0.0002 0.0144  0.0211  89  TYR   A CE1 
659  C  CE2 . TYR   A 83  ? 0.2791 0.2677 0.3115 0.0003  0.0111  0.0217  89  TYR   A CE2 
660  C  CZ  . TYR   A 83  ? 0.3037 0.2921 0.3300 0.0012  0.0116  0.0218  89  TYR   A CZ  
661  O  OH  . TYR   A 83  ? 0.3564 0.3429 0.3750 0.0035  0.0090  0.0224  89  TYR   A OH  
662  N  N   . TYR   A 84  ? 0.1934 0.1844 0.2545 -0.0096 0.0206  0.0168  90  TYR   A N   
663  C  CA  . TYR   A 84  ? 0.1850 0.1760 0.2519 -0.0117 0.0198  0.0135  90  TYR   A CA  
664  C  C   . TYR   A 84  ? 0.1935 0.1851 0.2678 -0.0133 0.0219  0.0149  90  TYR   A C   
665  O  O   . TYR   A 84  ? 0.1968 0.1902 0.2709 -0.0127 0.0241  0.0176  90  TYR   A O   
666  C  CB  . TYR   A 84  ? 0.1733 0.1670 0.2378 -0.0120 0.0173  0.0100  90  TYR   A CB  
667  C  CG  . TYR   A 84  ? 0.1699 0.1633 0.2280 -0.0107 0.0157  0.0086  90  TYR   A CG  
668  C  CD1 . TYR   A 84  ? 0.1676 0.1585 0.2253 -0.0105 0.0150  0.0067  90  TYR   A CD1 
669  C  CD2 . TYR   A 84  ? 0.1774 0.1728 0.2305 -0.0095 0.0152  0.0092  90  TYR   A CD2 
670  C  CE1 . TYR   A 84  ? 0.1729 0.1637 0.2261 -0.0094 0.0143  0.0056  90  TYR   A CE1 
671  C  CE2 . TYR   A 84  ? 0.1653 0.1603 0.2139 -0.0086 0.0139  0.0080  90  TYR   A CE2 
672  C  CZ  . TYR   A 84  ? 0.1625 0.1555 0.2117 -0.0086 0.0137  0.0063  90  TYR   A CZ  
673  O  OH  . TYR   A 84  ? 0.1586 0.1513 0.2048 -0.0078 0.0133  0.0055  90  TYR   A OH  
674  N  N   . PRO   A 85  ? 0.1962 0.1862 0.2774 -0.0154 0.0213  0.0127  91  PRO   A N   
675  C  CA  . PRO   A 85  ? 0.1978 0.1891 0.2885 -0.0174 0.0228  0.0134  91  PRO   A CA  
676  C  C   . PRO   A 85  ? 0.1993 0.1952 0.2917 -0.0181 0.0206  0.0108  91  PRO   A C   
677  O  O   . PRO   A 85  ? 0.2138 0.2107 0.2995 -0.0170 0.0177  0.0081  91  PRO   A O   
678  C  CB  . PRO   A 85  ? 0.2141 0.2017 0.3112 -0.0194 0.0216  0.0107  91  PRO   A CB  
679  C  CG  . PRO   A 85  ? 0.2256 0.2113 0.3156 -0.0184 0.0184  0.0069  91  PRO   A CG  
680  C  CD  . PRO   A 85  ? 0.2015 0.1883 0.2825 -0.0158 0.0191  0.0091  91  PRO   A CD  
681  N  N   . ALA   A 86  ? 0.1979 0.1964 0.2999 -0.0197 0.0219  0.0115  92  ALA   A N   
682  C  CA  . ALA   A 86  ? 0.2035 0.2067 0.3088 -0.0202 0.0193  0.0090  92  ALA   A CA  
683  C  C   . ALA   A 86  ? 0.1983 0.2002 0.3023 -0.0209 0.0136  0.0033  92  ALA   A C   
684  O  O   . ALA   A 86  ? 0.2055 0.2037 0.3125 -0.0223 0.0123  0.0013  92  ALA   A O   
685  C  CB  . ALA   A 86  ? 0.2097 0.2160 0.3286 -0.0221 0.0216  0.0107  92  ALA   A CB  
686  N  N   . ARG   A 87  ? 0.1964 0.2003 0.2939 -0.0195 0.0106  0.0010  93  ARG   A N   
687  C  CA  . ARG   A 87  ? 0.1915 0.1929 0.2844 -0.0193 0.0057  -0.0040 93  ARG   A CA  
688  C  C   . ARG   A 87  ? 0.1864 0.1906 0.2745 -0.0177 0.0027  -0.0059 93  ARG   A C   
689  O  O   . ARG   A 87  ? 0.1995 0.2075 0.2872 -0.0167 0.0046  -0.0033 93  ARG   A O   
690  C  CB  . ARG   A 87  ? 0.1903 0.1868 0.2737 -0.0179 0.0067  -0.0040 93  ARG   A CB  
691  C  CG  . ARG   A 87  ? 0.2059 0.2035 0.2796 -0.0156 0.0079  -0.0023 93  ARG   A CG  
692  C  CD  . ARG   A 87  ? 0.2190 0.2139 0.2878 -0.0145 0.0104  -0.0002 93  ARG   A CD  
693  N  NE  . ARG   A 87  ? 0.2186 0.2131 0.2787 -0.0127 0.0099  -0.0007 93  ARG   A NE  
694  C  CZ  . ARG   A 87  ? 0.2073 0.2043 0.2637 -0.0115 0.0104  0.0009  93  ARG   A CZ  
695  N  NH1 . ARG   A 87  ? 0.1980 0.1941 0.2479 -0.0102 0.0102  0.0004  93  ARG   A NH1 
696  N  NH2 . ARG   A 87  ? 0.1899 0.1900 0.2492 -0.0117 0.0116  0.0031  93  ARG   A NH2 
697  N  N   . TYR   A 88  ? 0.1788 0.1806 0.2622 -0.0171 -0.0019 -0.0103 94  TYR   A N   
698  C  CA  . TYR   A 88  ? 0.1881 0.1914 0.2647 -0.0149 -0.0045 -0.0116 94  TYR   A CA  
699  C  C   . TYR   A 88  ? 0.1885 0.1885 0.2530 -0.0128 -0.0026 -0.0109 94  TYR   A C   
700  O  O   . TYR   A 88  ? 0.2111 0.2063 0.2710 -0.0126 -0.0024 -0.0123 94  TYR   A O   
701  C  CB  . TYR   A 88  ? 0.2011 0.2030 0.2774 -0.0147 -0.0106 -0.0165 94  TYR   A CB  
702  C  CG  . TYR   A 88  ? 0.2147 0.2211 0.3046 -0.0166 -0.0136 -0.0176 94  TYR   A CG  
703  C  CD1 . TYR   A 88  ? 0.2306 0.2425 0.3244 -0.0157 -0.0153 -0.0171 94  TYR   A CD1 
704  C  CD2 . TYR   A 88  ? 0.2336 0.2389 0.3336 -0.0194 -0.0145 -0.0190 94  TYR   A CD2 
705  C  CE1 . TYR   A 88  ? 0.2469 0.2638 0.3553 -0.0176 -0.0178 -0.0179 94  TYR   A CE1 
706  C  CE2 . TYR   A 88  ? 0.2486 0.2585 0.3634 -0.0216 -0.0170 -0.0198 94  TYR   A CE2 
707  C  CZ  . TYR   A 88  ? 0.2627 0.2787 0.3822 -0.0206 -0.0187 -0.0193 94  TYR   A CZ  
708  O  OH  . TYR   A 88  ? 0.3024 0.3233 0.4386 -0.0229 -0.0212 -0.0201 94  TYR   A OH  
709  N  N   . GLN   A 89  ? 0.1771 0.1794 0.2373 -0.0114 -0.0009 -0.0087 95  GLN   A N   
710  C  CA  . GLN   A 89  ? 0.1633 0.1627 0.2135 -0.0096 0.0007  -0.0080 95  GLN   A CA  
711  C  C   . GLN   A 89  ? 0.1683 0.1662 0.2115 -0.0076 -0.0024 -0.0106 95  GLN   A C   
712  O  O   . GLN   A 89  ? 0.1839 0.1850 0.2291 -0.0070 -0.0045 -0.0109 95  GLN   A O   
713  C  CB  . GLN   A 89  ? 0.1615 0.1632 0.2105 -0.0090 0.0040  -0.0044 95  GLN   A CB  
714  C  CG  . GLN   A 89  ? 0.1586 0.1576 0.1991 -0.0075 0.0051  -0.0040 95  GLN   A CG  
715  C  CD  . GLN   A 89  ? 0.1803 0.1804 0.2200 -0.0073 0.0076  -0.0010 95  GLN   A CD  
716  O  OE1 . GLN   A 89  ? 0.1774 0.1782 0.2209 -0.0082 0.0092  0.0010  95  GLN   A OE1 
717  N  NE2 . GLN   A 89  ? 0.1608 0.1602 0.1950 -0.0060 0.0079  -0.0006 95  GLN   A NE2 
718  N  N   . SER   A 90  ? 0.1603 0.1531 0.1954 -0.0062 -0.0025 -0.0122 96  SER   A N   
719  C  CA  . SER   A 90  ? 0.1691 0.1592 0.1956 -0.0038 -0.0050 -0.0143 96  SER   A CA  
720  C  C   . SER   A 90  ? 0.1805 0.1702 0.2005 -0.0021 -0.0023 -0.0120 96  SER   A C   
721  O  O   . SER   A 90  ? 0.1910 0.1817 0.2125 -0.0028 0.0012  -0.0095 96  SER   A O   
722  C  CB  . SER   A 90  ? 0.1998 0.1835 0.2198 -0.0027 -0.0059 -0.0173 96  SER   A CB  
723  O  OG  . SER   A 90  ? 0.2195 0.2003 0.2372 -0.0027 -0.0015 -0.0157 96  SER   A OG  
724  N  N   . HIS   A 91  ? 0.1711 0.1589 0.1840 0.0004  -0.0042 -0.0130 97  HIS   A N   
725  C  CA  . HIS   A 91  ? 0.1721 0.1584 0.1786 0.0022  -0.0017 -0.0111 97  HIS   A CA  
726  C  C   . HIS   A 91  ? 0.1688 0.1599 0.1805 0.0011  0.0000  -0.0084 97  HIS   A C   
727  O  O   . HIS   A 91  ? 0.1778 0.1678 0.1869 0.0014  0.0029  -0.0065 97  HIS   A O   
728  C  CB  . HIS   A 91  ? 0.1854 0.1669 0.1866 0.0027  0.0023  -0.0103 97  HIS   A CB  
729  C  CG  . HIS   A 91  ? 0.2135 0.1889 0.2072 0.0045  0.0014  -0.0129 97  HIS   A CG  
730  N  ND1 . HIS   A 91  ? 0.2474 0.2175 0.2303 0.0078  0.0018  -0.0132 97  HIS   A ND1 
731  C  CD2 . HIS   A 91  ? 0.2105 0.1837 0.2052 0.0039  0.0004  -0.0151 97  HIS   A CD2 
732  C  CE1 . HIS   A 91  ? 0.2481 0.2128 0.2249 0.0092  0.0009  -0.0158 97  HIS   A CE1 
733  N  NE2 . HIS   A 91  ? 0.2362 0.2026 0.2202 0.0068  -0.0001 -0.0173 97  HIS   A NE2 
734  N  N   . LEU   A 92  ? 0.1591 0.1552 0.1785 0.0000  -0.0017 -0.0083 98  LEU   A N   
735  C  CA  . LEU   A 92  ? 0.1447 0.1447 0.1682 -0.0006 0.0003  -0.0058 98  LEU   A CA  
736  C  C   . LEU   A 92  ? 0.1509 0.1529 0.1736 0.0014  -0.0014 -0.0058 98  LEU   A C   
737  O  O   . LEU   A 92  ? 0.1517 0.1549 0.1761 0.0022  -0.0049 -0.0076 98  LEU   A O   
738  C  CB  . LEU   A 92  ? 0.1434 0.1472 0.1762 -0.0027 0.0006  -0.0052 98  LEU   A CB  
739  C  CG  . LEU   A 92  ? 0.1731 0.1798 0.2091 -0.0030 0.0035  -0.0025 98  LEU   A CG  
740  C  CD1 . LEU   A 92  ? 0.1997 0.2038 0.2305 -0.0029 0.0059  -0.0009 98  LEU   A CD1 
741  C  CD2 . LEU   A 92  ? 0.1929 0.2024 0.2378 -0.0050 0.0045  -0.0015 98  LEU   A CD2 
742  N  N   . MET   A 93  ? 0.1393 0.1412 0.1595 0.0022  0.0008  -0.0040 99  MET   A N   
743  C  CA  . MET   A 93  ? 0.1595 0.1627 0.1784 0.0044  0.0000  -0.0036 99  MET   A CA  
744  C  C   . MET   A 93  ? 0.1701 0.1770 0.1942 0.0041  0.0021  -0.0018 99  MET   A C   
745  O  O   . MET   A 93  ? 0.1808 0.1865 0.2034 0.0033  0.0047  -0.0006 99  MET   A O   
746  C  CB  . MET   A 93  ? 0.1734 0.1717 0.1838 0.0060  0.0013  -0.0030 99  MET   A CB  
747  C  CG  . MET   A 93  ? 0.1992 0.1929 0.2031 0.0070  0.0003  -0.0043 99  MET   A CG  
748  S  SD  . MET   A 93  ? 0.2143 0.2018 0.2094 0.0086  0.0032  -0.0029 99  MET   A SD  
749  C  CE  . MET   A 93  ? 0.2406 0.2283 0.2395 0.0058  0.0066  -0.0016 99  MET   A CE  
750  N  N   . LEU   A 94  ? 0.1556 0.1668 0.1857 0.0049  0.0010  -0.0018 100 LEU   A N   
751  C  CA  . LEU   A 94  ? 0.1610 0.1752 0.1955 0.0051  0.0040  0.0002  100 LEU   A CA  
752  C  C   . LEU   A 94  ? 0.1608 0.1746 0.1919 0.0078  0.0048  0.0009  100 LEU   A C   
753  O  O   . LEU   A 94  ? 0.1636 0.1772 0.1931 0.0097  0.0023  0.0000  100 LEU   A O   
754  C  CB  . LEU   A 94  ? 0.1808 0.2007 0.2266 0.0043  0.0035  0.0003  100 LEU   A CB  
755  C  CG  . LEU   A 94  ? 0.2446 0.2652 0.2960 0.0014  0.0036  0.0001  100 LEU   A CG  
756  C  CD1 . LEU   A 94  ? 0.2603 0.2867 0.3246 0.0006  0.0045  0.0010  100 LEU   A CD1 
757  C  CD2 . LEU   A 94  ? 0.2659 0.2836 0.3131 0.0003  0.0071  0.0018  100 LEU   A CD2 
758  N  N   . ALA   A 95  ? 0.1527 0.1662 0.1828 0.0083  0.0082  0.0024  101 ALA   A N   
759  C  CA  . ALA   A 95  ? 0.1540 0.1665 0.1809 0.0111  0.0095  0.0030  101 ALA   A CA  
760  C  C   . ALA   A 95  ? 0.1479 0.1619 0.1769 0.0118  0.0134  0.0048  101 ALA   A C   
761  O  O   . ALA   A 95  ? 0.1517 0.1659 0.1820 0.0103  0.0152  0.0057  101 ALA   A O   
762  C  CB  . ALA   A 95  ? 0.1723 0.1788 0.1898 0.0114  0.0096  0.0026  101 ALA   A CB  
763  N  N   . VAL   A 96  ? 0.1438 0.1583 0.1727 0.0147  0.0150  0.0054  102 VAL   A N   
764  C  CA  . VAL   A 96  ? 0.1622 0.1766 0.1908 0.0162  0.0195  0.0071  102 VAL   A CA  
765  C  C   . VAL   A 96  ? 0.1818 0.1893 0.1990 0.0167  0.0202  0.0065  102 VAL   A C   
766  O  O   . VAL   A 96  ? 0.1949 0.1987 0.2067 0.0178  0.0188  0.0054  102 VAL   A O   
767  C  CB  . VAL   A 96  ? 0.1804 0.1981 0.2143 0.0193  0.0212  0.0078  102 VAL   A CB  
768  C  CG1 . VAL   A 96  ? 0.1855 0.2018 0.2170 0.0217  0.0267  0.0096  102 VAL   A CG1 
769  C  CG2 . VAL   A 96  ? 0.1924 0.2174 0.2392 0.0184  0.0195  0.0080  102 VAL   A CG2 
770  N  N   . GLY   A 97  ? 0.1823 0.1877 0.1962 0.0161  0.0222  0.0074  103 GLY   A N   
771  C  CA  . GLY   A 97  ? 0.1904 0.1895 0.1943 0.0164  0.0220  0.0066  103 GLY   A CA  
772  C  C   . GLY   A 97  ? 0.1927 0.1906 0.1944 0.0157  0.0235  0.0079  103 GLY   A C   
773  O  O   . GLY   A 97  ? 0.2003 0.2021 0.2085 0.0141  0.0243  0.0092  103 GLY   A O   
774  N  N   . HIS   A 98  ? 0.1861 0.1784 0.1785 0.0172  0.0240  0.0075  104 HIS   A N   
775  C  CA  . HIS   A 98  ? 0.1898 0.1799 0.1779 0.0172  0.0250  0.0087  104 HIS   A CA  
776  C  C   . HIS   A 98  ? 0.1830 0.1729 0.1722 0.0142  0.0213  0.0081  104 HIS   A C   
777  O  O   . HIS   A 98  ? 0.1975 0.1857 0.1856 0.0127  0.0178  0.0061  104 HIS   A O   
778  C  CB  . HIS   A 98  ? 0.2012 0.1843 0.1775 0.0203  0.0256  0.0080  104 HIS   A CB  
779  C  CG  . HIS   A 98  ? 0.2049 0.1846 0.1747 0.0210  0.0261  0.0093  104 HIS   A CG  
780  N  ND1 . HIS   A 98  ? 0.2313 0.2124 0.2021 0.0226  0.0310  0.0125  104 HIS   A ND1 
781  C  CD2 . HIS   A 98  ? 0.2254 0.2006 0.1885 0.0205  0.0220  0.0080  104 HIS   A CD2 
782  C  CE1 . HIS   A 98  ? 0.2461 0.2229 0.2093 0.0232  0.0300  0.0131  104 HIS   A CE1 
783  N  NE2 . HIS   A 98  ? 0.2460 0.2194 0.2045 0.0221  0.0242  0.0103  104 HIS   A NE2 
784  N  N   . SER   A 99  ? 0.1765 0.1677 0.1679 0.0134  0.0226  0.0100  105 SER   A N   
785  C  CA  . SER   A 99  ? 0.1715 0.1622 0.1636 0.0110  0.0196  0.0098  105 SER   A CA  
786  C  C   . SER   A 99  ? 0.1911 0.1811 0.1819 0.0117  0.0219  0.0125  105 SER   A C   
787  O  O   . SER   A 99  ? 0.2087 0.2006 0.2025 0.0127  0.0263  0.0148  105 SER   A O   
788  C  CB  . SER   A 99  ? 0.1944 0.1893 0.1953 0.0080  0.0179  0.0090  105 SER   A CB  
789  O  OG  . SER   A 99  ? 0.2390 0.2383 0.2476 0.0073  0.0203  0.0106  105 SER   A OG  
790  N  N   . GLU   A 100 ? 0.1835 0.1703 0.1698 0.0114  0.0191  0.0123  106 GLU   A N   
791  C  CA  . GLU   A 100 ? 0.1931 0.1781 0.1769 0.0121  0.0201  0.0148  106 GLU   A CA  
792  C  C   . GLU   A 100 ? 0.2100 0.1966 0.1994 0.0093  0.0167  0.0142  106 GLU   A C   
793  O  O   . GLU   A 100 ? 0.2185 0.2063 0.2111 0.0074  0.0135  0.0118  106 GLU   A O   
794  C  CB  . GLU   A 100 ? 0.2194 0.1978 0.1903 0.0156  0.0192  0.0148  106 GLU   A CB  
795  C  CG  . GLU   A 100 ? 0.2748 0.2509 0.2394 0.0189  0.0234  0.0155  106 GLU   A CG  
796  C  CD  . GLU   A 100 ? 0.3030 0.2714 0.2527 0.0228  0.0224  0.0149  106 GLU   A CD  
797  O  OE1 . GLU   A 100 ? 0.2981 0.2626 0.2413 0.0241  0.0205  0.0160  106 GLU   A OE1 
798  O  OE2 . GLU   A 100 ? 0.3197 0.2852 0.2637 0.0250  0.0233  0.0133  106 GLU   A OE2 
799  N  N   . PRO   A 101 ? 0.2127 0.1991 0.2036 0.0092  0.0178  0.0167  107 PRO   A N   
800  C  CA  . PRO   A 101 ? 0.2114 0.1994 0.2085 0.0067  0.0151  0.0162  107 PRO   A CA  
801  C  C   . PRO   A 101 ? 0.2179 0.2046 0.2135 0.0061  0.0100  0.0137  107 PRO   A C   
802  O  O   . PRO   A 101 ? 0.2205 0.2097 0.2229 0.0037  0.0085  0.0123  107 PRO   A O   
803  C  CB  . PRO   A 101 ? 0.2217 0.2079 0.2178 0.0077  0.0170  0.0195  107 PRO   A CB  
804  C  CG  . PRO   A 101 ? 0.2290 0.2152 0.2241 0.0093  0.0226  0.0220  107 PRO   A CG  
805  C  CD  . PRO   A 101 ? 0.2138 0.1985 0.2020 0.0113  0.0224  0.0202  107 PRO   A CD  
806  N  N   . GLY   A 102 ? 0.2177 0.2003 0.2047 0.0083  0.0074  0.0131  108 GLY   A N   
807  C  CA  . GLY   A 102 ? 0.2142 0.1953 0.2007 0.0077  0.0021  0.0107  108 GLY   A CA  
808  C  C   . GLY   A 102 ? 0.1975 0.1800 0.1874 0.0060  0.0012  0.0079  108 GLY   A C   
809  O  O   . GLY   A 102 ? 0.2014 0.1834 0.1939 0.0048  -0.0025 0.0061  108 GLY   A O   
810  N  N   . ASP   A 103 ? 0.1891 0.1731 0.1795 0.0059  0.0046  0.0079  109 ASP   A N   
811  C  CA  . ASP   A 103 ? 0.1805 0.1653 0.1736 0.0047  0.0042  0.0057  109 ASP   A CA  
812  C  C   . ASP   A 103 ? 0.1681 0.1563 0.1697 0.0020  0.0044  0.0054  109 ASP   A C   
813  O  O   . ASP   A 103 ? 0.1666 0.1547 0.1703 0.0011  0.0038  0.0039  109 ASP   A O   
814  C  CB  . ASP   A 103 ? 0.1774 0.1627 0.1682 0.0060  0.0075  0.0059  109 ASP   A CB  
815  C  CG  . ASP   A 103 ? 0.1857 0.1665 0.1671 0.0089  0.0073  0.0054  109 ASP   A CG  
816  O  OD1 . ASP   A 103 ? 0.2007 0.1776 0.1778 0.0093  0.0037  0.0037  109 ASP   A OD1 
817  O  OD2 . ASP   A 103 ? 0.1899 0.1707 0.1684 0.0109  0.0110  0.0067  109 ASP   A OD2 
818  N  N   . CYS   A 104 ? 0.1692 0.1596 0.1754 0.0011  0.0053  0.0069  110 CYS   A N   
819  C  CA  . CYS   A 104 ? 0.1595 0.1521 0.1724 -0.0009 0.0057  0.0064  110 CYS   A CA  
820  C  C   . CYS   A 104 ? 0.1587 0.1502 0.1740 -0.0019 0.0035  0.0051  110 CYS   A C   
821  O  O   . CYS   A 104 ? 0.1719 0.1620 0.1866 -0.0015 0.0007  0.0050  110 CYS   A O   
822  C  CB  . CYS   A 104 ? 0.1636 0.1576 0.1804 -0.0015 0.0067  0.0079  110 CYS   A CB  
823  S  SG  . CYS   A 104 ? 0.1880 0.1841 0.2064 -0.0014 0.0100  0.0092  110 CYS   A SG  
824  N  N   . GLY   A 105 ? 0.1424 0.1344 0.1606 -0.0029 0.0046  0.0041  111 GLY   A N   
825  C  CA  . GLY   A 105 ? 0.1550 0.1460 0.1768 -0.0039 0.0035  0.0033  111 GLY   A CA  
826  C  C   . GLY   A 105 ? 0.1695 0.1581 0.1886 -0.0037 0.0031  0.0021  111 GLY   A C   
827  O  O   . GLY   A 105 ? 0.1677 0.1554 0.1906 -0.0047 0.0033  0.0016  111 GLY   A O   
828  N  N   . GLY   A 106 ? 0.1692 0.1567 0.1822 -0.0023 0.0029  0.0018  112 GLY   A N   
829  C  CA  . GLY   A 106 ? 0.1714 0.1561 0.1815 -0.0018 0.0027  0.0006  112 GLY   A CA  
830  C  C   . GLY   A 106 ? 0.1625 0.1473 0.1740 -0.0021 0.0053  0.0007  112 GLY   A C   
831  O  O   . GLY   A 106 ? 0.1600 0.1470 0.1715 -0.0017 0.0070  0.0014  112 GLY   A O   
832  N  N   . ILE   A 107 ? 0.1593 0.1414 0.1721 -0.0027 0.0056  0.0002  113 ILE   A N   
833  C  CA  . ILE   A 107 ? 0.1572 0.1383 0.1700 -0.0025 0.0083  0.0007  113 ILE   A CA  
834  C  C   . ILE   A 107 ? 0.1577 0.1377 0.1649 -0.0005 0.0091  0.0006  113 ILE   A C   
835  O  O   . ILE   A 107 ? 0.1670 0.1451 0.1712 0.0004  0.0080  -0.0002 113 ILE   A O   
836  C  CB  . ILE   A 107 ? 0.1807 0.1590 0.1982 -0.0038 0.0090  0.0007  113 ILE   A CB  
837  C  CG1 . ILE   A 107 ? 0.1989 0.1792 0.2233 -0.0053 0.0097  0.0014  113 ILE   A CG1 
838  C  CG2 . ILE   A 107 ? 0.1818 0.1569 0.1969 -0.0029 0.0120  0.0015  113 ILE   A CG2 
839  C  CD1 . ILE   A 107 ? 0.2225 0.2007 0.2545 -0.0070 0.0106  0.0017  113 ILE   A CD1 
840  N  N   . LEU   A 108 ? 0.1506 0.1314 0.1564 0.0004  0.0107  0.0012  114 LEU   A N   
841  C  CA  . LEU   A 108 ? 0.1539 0.1335 0.1553 0.0025  0.0113  0.0013  114 LEU   A CA  
842  C  C   . LEU   A 108 ? 0.1706 0.1460 0.1709 0.0028  0.0134  0.0020  114 LEU   A C   
843  O  O   . LEU   A 108 ? 0.1810 0.1561 0.1828 0.0022  0.0150  0.0026  114 LEU   A O   
844  C  CB  . LEU   A 108 ? 0.1634 0.1465 0.1643 0.0035  0.0110  0.0014  114 LEU   A CB  
845  C  CG  . LEU   A 108 ? 0.1807 0.1631 0.1779 0.0060  0.0109  0.0015  114 LEU   A CG  
846  C  CD1 . LEU   A 108 ? 0.1847 0.1669 0.1804 0.0075  0.0106  0.0014  114 LEU   A CD1 
847  C  CD2 . LEU   A 108 ? 0.1972 0.1831 0.1954 0.0065  0.0096  0.0011  114 LEU   A CD2 
848  N  N   . ARG   A 109 ? 0.1722 0.1440 0.1698 0.0040  0.0140  0.0022  115 ARG   A N   
849  C  CA  . ARG   A 109 ? 0.1901 0.1570 0.1864 0.0045  0.0166  0.0034  115 ARG   A CA  
850  C  C   . ARG   A 109 ? 0.1982 0.1628 0.1887 0.0075  0.0169  0.0039  115 ARG   A C   
851  O  O   . ARG   A 109 ? 0.2050 0.1702 0.1940 0.0086  0.0154  0.0032  115 ARG   A O   
852  C  CB  . ARG   A 109 ? 0.2301 0.1934 0.2301 0.0028  0.0170  0.0032  115 ARG   A CB  
853  C  CG  . ARG   A 109 ? 0.2980 0.2632 0.3049 0.0000  0.0159  0.0024  115 ARG   A CG  
854  C  CD  . ARG   A 109 ? 0.3247 0.2858 0.3358 -0.0016 0.0157  0.0019  115 ARG   A CD  
855  N  NE  . ARG   A 109 ? 0.3369 0.2944 0.3503 -0.0018 0.0199  0.0039  115 ARG   A NE  
856  C  CZ  . ARG   A 109 ? 0.3253 0.2834 0.3459 -0.0036 0.0220  0.0049  115 ARG   A CZ  
857  N  NH1 . ARG   A 109 ? 0.2925 0.2547 0.3196 -0.0056 0.0195  0.0039  115 ARG   A NH1 
858  N  NH2 . ARG   A 109 ? 0.3082 0.2626 0.3297 -0.0032 0.0269  0.0073  115 ARG   A NH2 
859  N  N   . CYS   A 110 ? 0.1968 0.1577 0.1836 0.0090  0.0193  0.0054  116 CYS   A N   
860  C  CA  . CYS   A 110 ? 0.2087 0.1660 0.1896 0.0122  0.0197  0.0064  116 CYS   A CA  
861  C  C   . CYS   A 110 ? 0.2188 0.1692 0.1995 0.0120  0.0234  0.0081  116 CYS   A C   
862  O  O   . CYS   A 110 ? 0.2301 0.1796 0.2165 0.0092  0.0251  0.0083  116 CYS   A O   
863  C  CB  . CYS   A 110 ? 0.2290 0.1868 0.2044 0.0149  0.0190  0.0068  116 CYS   A CB  
864  S  SG  . CYS   A 110 ? 0.2202 0.1740 0.1927 0.0148  0.0226  0.0083  116 CYS   A SG  
865  N  N   . GLN   A 111 ? 0.2348 0.1802 0.2098 0.0149  0.0248  0.0097  117 GLN   A N   
866  C  CA  . GLN   A 111 ? 0.2513 0.1894 0.2262 0.0149  0.0289  0.0118  117 GLN   A CA  
867  C  C   . GLN   A 111 ? 0.2567 0.1923 0.2319 0.0143  0.0331  0.0138  117 GLN   A C   
868  O  O   . GLN   A 111 ? 0.2665 0.1970 0.2448 0.0133  0.0373  0.0156  117 GLN   A O   
869  C  CB  . GLN   A 111 ? 0.2759 0.2087 0.2434 0.0190  0.0298  0.0136  117 GLN   A CB  
870  C  CG  . GLN   A 111 ? 0.3624 0.2952 0.3213 0.0227  0.0290  0.0145  117 GLN   A CG  
871  C  CD  . GLN   A 111 ? 0.4587 0.3870 0.4104 0.0271  0.0287  0.0161  117 GLN   A CD  
872  O  OE1 . GLN   A 111 ? 0.4897 0.4218 0.4397 0.0294  0.0247  0.0149  117 GLN   A OE1 
873  N  NE2 . GLN   A 111 ? 0.4593 0.3795 0.4076 0.0285  0.0331  0.0190  117 GLN   A NE2 
874  N  N   . HIS   A 112 ? 0.2448 0.1838 0.2175 0.0149  0.0324  0.0133  118 HIS   A N   
875  C  CA  . HIS   A 112 ? 0.2338 0.1699 0.2055 0.0149  0.0368  0.0152  118 HIS   A CA  
876  C  C   . HIS   A 112 ? 0.2230 0.1632 0.2044 0.0111  0.0375  0.0142  118 HIS   A C   
877  O  O   . HIS   A 112 ? 0.2307 0.1683 0.2137 0.0108  0.0422  0.0160  118 HIS   A O   
878  C  CB  . HIS   A 112 ? 0.2460 0.1812 0.2074 0.0185  0.0360  0.0152  118 HIS   A CB  
879  C  CG  . HIS   A 112 ? 0.2788 0.2102 0.2304 0.0228  0.0345  0.0161  118 HIS   A CG  
880  N  ND1 . HIS   A 112 ? 0.2882 0.2242 0.2377 0.0243  0.0287  0.0139  118 HIS   A ND1 
881  C  CD2 . HIS   A 112 ? 0.3015 0.2251 0.2460 0.0260  0.0381  0.0190  118 HIS   A CD2 
882  C  CE1 . HIS   A 112 ? 0.3135 0.2449 0.2549 0.0283  0.0284  0.0154  118 HIS   A CE1 
883  N  NE2 . HIS   A 112 ? 0.3188 0.2422 0.2561 0.0296  0.0339  0.0186  118 HIS   A NE2 
884  N  N   . GLY   A 113 ? 0.1999 0.1461 0.1875 0.0086  0.0331  0.0117  119 GLY   A N   
885  C  CA  . GLY   A 113 ? 0.1985 0.1488 0.1952 0.0053  0.0328  0.0108  119 GLY   A CA  
886  C  C   . GLY   A 113 ? 0.1893 0.1461 0.1868 0.0045  0.0282  0.0085  119 GLY   A C   
887  O  O   . GLY   A 113 ? 0.1992 0.1579 0.1925 0.0058  0.0249  0.0073  119 GLY   A O   
888  N  N   . VAL   A 114 ? 0.1646 0.1247 0.1682 0.0025  0.0282  0.0080  120 VAL   A N   
889  C  CA  . VAL   A 114 ? 0.1666 0.1323 0.1716 0.0016  0.0243  0.0062  120 VAL   A CA  
890  C  C   . VAL   A 114 ? 0.1756 0.1423 0.1741 0.0037  0.0236  0.0057  120 VAL   A C   
891  O  O   . VAL   A 114 ? 0.1906 0.1544 0.1856 0.0050  0.0265  0.0065  120 VAL   A O   
892  C  CB  . VAL   A 114 ? 0.1799 0.1483 0.1936 -0.0009 0.0247  0.0062  120 VAL   A CB  
893  C  CG1 . VAL   A 114 ? 0.1859 0.1593 0.2004 -0.0014 0.0214  0.0048  120 VAL   A CG1 
894  C  CG2 . VAL   A 114 ? 0.1864 0.1544 0.2077 -0.0031 0.0238  0.0060  120 VAL   A CG2 
895  N  N   . VAL   A 115 ? 0.1714 0.1415 0.1681 0.0041  0.0199  0.0043  121 VAL   A N   
896  C  CA  . VAL   A 115 ? 0.1781 0.1498 0.1705 0.0058  0.0182  0.0035  121 VAL   A CA  
897  C  C   . VAL   A 115 ? 0.1860 0.1618 0.1827 0.0041  0.0167  0.0024  121 VAL   A C   
898  O  O   . VAL   A 115 ? 0.1890 0.1646 0.1833 0.0048  0.0164  0.0016  121 VAL   A O   
899  C  CB  . VAL   A 115 ? 0.1798 0.1531 0.1696 0.0073  0.0154  0.0029  121 VAL   A CB  
900  C  CG1 . VAL   A 115 ? 0.1917 0.1680 0.1800 0.0084  0.0126  0.0016  121 VAL   A CG1 
901  C  CG2 . VAL   A 115 ? 0.1846 0.1531 0.1692 0.0096  0.0168  0.0041  121 VAL   A CG2 
902  N  N   . GLY   A 116 ? 0.1604 0.1395 0.1626 0.0021  0.0155  0.0022  122 GLY   A N   
903  C  CA  . GLY   A 116 ? 0.1554 0.1381 0.1616 0.0007  0.0142  0.0016  122 GLY   A CA  
904  C  C   . GLY   A 116 ? 0.1598 0.1449 0.1703 -0.0008 0.0129  0.0018  122 GLY   A C   
905  O  O   . GLY   A 116 ? 0.1644 0.1482 0.1751 -0.0010 0.0127  0.0019  122 GLY   A O   
906  N  N   . ILE   A 117 ? 0.1510 0.1391 0.1644 -0.0017 0.0117  0.0016  123 ILE   A N   
907  C  CA  . ILE   A 117 ? 0.1552 0.1448 0.1708 -0.0025 0.0103  0.0020  123 ILE   A CA  
908  C  C   . ILE   A 117 ? 0.1459 0.1382 0.1612 -0.0021 0.0095  0.0021  123 ILE   A C   
909  O  O   . ILE   A 117 ? 0.1416 0.1355 0.1579 -0.0021 0.0097  0.0019  123 ILE   A O   
910  C  CB  . ILE   A 117 ? 0.1562 0.1462 0.1767 -0.0038 0.0103  0.0024  123 ILE   A CB  
911  C  CG1 . ILE   A 117 ? 0.1612 0.1521 0.1838 -0.0041 0.0113  0.0025  123 ILE   A CG1 
912  C  CG2 . ILE   A 117 ? 0.1696 0.1574 0.1928 -0.0044 0.0112  0.0026  123 ILE   A CG2 
913  C  CD1 . ILE   A 117 ? 0.1915 0.1832 0.2196 -0.0050 0.0110  0.0032  123 ILE   A CD1 
914  N  N   . VAL   A 118 ? 0.1307 0.1233 0.1446 -0.0016 0.0086  0.0025  124 VAL   A N   
915  C  CA  . VAL   A 118 ? 0.1196 0.1144 0.1335 -0.0011 0.0089  0.0033  124 VAL   A CA  
916  C  C   . VAL   A 118 ? 0.1327 0.1290 0.1506 -0.0022 0.0092  0.0040  124 VAL   A C   
917  O  O   . VAL   A 118 ? 0.1398 0.1353 0.1594 -0.0030 0.0086  0.0043  124 VAL   A O   
918  C  CB  . VAL   A 118 ? 0.1366 0.1301 0.1468 0.0001  0.0085  0.0037  124 VAL   A CB  
919  C  CG1 . VAL   A 118 ? 0.1481 0.1434 0.1584 0.0009  0.0099  0.0052  124 VAL   A CG1 
920  C  CG2 . VAL   A 118 ? 0.1452 0.1366 0.1514 0.0014  0.0084  0.0028  124 VAL   A CG2 
921  N  N   . SER   A 119 ? 0.1387 0.1373 0.1592 -0.0023 0.0099  0.0043  125 SER   A N   
922  C  CA  . SER   A 119 ? 0.1450 0.1444 0.1697 -0.0035 0.0103  0.0048  125 SER   A CA  
923  C  C   . SER   A 119 ? 0.1551 0.1566 0.1826 -0.0034 0.0116  0.0062  125 SER   A C   
924  O  O   . SER   A 119 ? 0.1646 0.1660 0.1948 -0.0040 0.0124  0.0075  125 SER   A O   
925  C  CB  . SER   A 119 ? 0.1522 0.1514 0.1788 -0.0042 0.0099  0.0032  125 SER   A CB  
926  O  OG  . SER   A 119 ? 0.1656 0.1650 0.1962 -0.0053 0.0102  0.0033  125 SER   A OG  
927  N  N   . THR   A 120 ? 0.1515 0.1548 0.1791 -0.0025 0.0123  0.0063  126 THR   A N   
928  C  CA  . THR   A 120 ? 0.1594 0.1648 0.1911 -0.0024 0.0144  0.0080  126 THR   A CA  
929  C  C   . THR   A 120 ? 0.1681 0.1739 0.1965 -0.0002 0.0160  0.0089  126 THR   A C   
930  O  O   . THR   A 120 ? 0.1664 0.1709 0.1900 0.0008  0.0149  0.0078  126 THR   A O   
931  C  CB  . THR   A 120 ? 0.1809 0.1893 0.2203 -0.0037 0.0138  0.0069  126 THR   A CB  
932  O  OG1 . THR   A 120 ? 0.1846 0.1947 0.2238 -0.0027 0.0125  0.0055  126 THR   A OG1 
933  C  CG2 . THR   A 120 ? 0.1775 0.1847 0.2191 -0.0054 0.0121  0.0054  126 THR   A CG2 
934  N  N   . GLY   A 121 ? 0.1693 0.1767 0.2009 0.0004  0.0191  0.0110  127 GLY   A N   
935  C  CA  . GLY   A 121 ? 0.1877 0.1955 0.2169 0.0027  0.0213  0.0120  127 GLY   A CA  
936  C  C   . GLY   A 121 ? 0.1886 0.1978 0.2218 0.0035  0.0258  0.0149  127 GLY   A C   
937  O  O   . GLY   A 121 ? 0.1844 0.1940 0.2224 0.0020  0.0270  0.0164  127 GLY   A O   
938  N  N   . GLY   A 122 ? 0.1889 0.1978 0.2190 0.0061  0.0287  0.0160  128 GLY   A N   
939  C  CA  . GLY   A 122 ? 0.1948 0.2041 0.2269 0.0077  0.0343  0.0194  128 GLY   A CA  
940  C  C   . GLY   A 122 ? 0.1950 0.2079 0.2326 0.0094  0.0370  0.0198  128 GLY   A C   
941  O  O   . GLY   A 122 ? 0.1832 0.1998 0.2268 0.0084  0.0340  0.0176  128 GLY   A O   
942  N  N   . ASN   A 123 ? 0.2031 0.2142 0.2374 0.0123  0.0427  0.0226  129 ASN   A N   
943  C  CA  . ASN   A 123 ? 0.2094 0.2241 0.2499 0.0144  0.0466  0.0237  129 ASN   A CA  
944  C  C   . ASN   A 123 ? 0.1955 0.2113 0.2345 0.0155  0.0432  0.0208  129 ASN   A C   
945  O  O   . ASN   A 123 ? 0.2066 0.2279 0.2561 0.0157  0.0436  0.0206  129 ASN   A O   
946  C  CB  . ASN   A 123 ? 0.2449 0.2662 0.3026 0.0121  0.0487  0.0253  129 ASN   A CB  
947  C  CG  . ASN   A 123 ? 0.3171 0.3365 0.3765 0.0114  0.0532  0.0289  129 ASN   A CG  
948  O  OD1 . ASN   A 123 ? 0.3386 0.3540 0.3911 0.0144  0.0592  0.0321  129 ASN   A OD1 
949  N  ND2 . ASN   A 123 ? 0.3420 0.3633 0.4097 0.0077  0.0506  0.0284  129 ASN   A ND2 
950  N  N   . GLY   A 124 ? 0.1809 0.1916 0.2078 0.0163  0.0399  0.0185  130 GLY   A N   
951  C  CA  . GLY   A 124 ? 0.1744 0.1850 0.1990 0.0175  0.0371  0.0161  130 GLY   A CA  
952  C  C   . GLY   A 124 ? 0.1840 0.1973 0.2134 0.0148  0.0314  0.0135  130 GLY   A C   
953  O  O   . GLY   A 124 ? 0.2032 0.2165 0.2312 0.0160  0.0292  0.0118  130 GLY   A O   
954  N  N   . LEU   A 125 ? 0.1647 0.1794 0.1981 0.0116  0.0290  0.0132  131 LEU   A N   
955  C  CA  . LEU   A 125 ? 0.1628 0.1786 0.1982 0.0095  0.0239  0.0107  131 LEU   A CA  
956  C  C   . LEU   A 125 ? 0.1571 0.1681 0.1843 0.0081  0.0215  0.0096  131 LEU   A C   
957  O  O   . LEU   A 125 ? 0.1642 0.1724 0.1871 0.0081  0.0231  0.0108  131 LEU   A O   
958  C  CB  . LEU   A 125 ? 0.1660 0.1866 0.2129 0.0070  0.0227  0.0107  131 LEU   A CB  
959  C  CG  . LEU   A 125 ? 0.1927 0.2192 0.2509 0.0078  0.0238  0.0113  131 LEU   A CG  
960  C  CD1 . LEU   A 125 ? 0.2132 0.2438 0.2837 0.0051  0.0232  0.0116  131 LEU   A CD1 
961  C  CD2 . LEU   A 125 ? 0.1950 0.2227 0.2529 0.0092  0.0198  0.0091  131 LEU   A CD2 
962  N  N   . VAL   A 126 ? 0.1430 0.1530 0.1685 0.0072  0.0179  0.0075  132 VAL   A N   
963  C  CA  . VAL   A 126 ? 0.1458 0.1523 0.1664 0.0056  0.0158  0.0065  132 VAL   A CA  
964  C  C   . VAL   A 126 ? 0.1531 0.1607 0.1769 0.0040  0.0129  0.0049  132 VAL   A C   
965  O  O   . VAL   A 126 ? 0.1620 0.1710 0.1872 0.0050  0.0115  0.0039  132 VAL   A O   
966  C  CB  . VAL   A 126 ? 0.1473 0.1490 0.1594 0.0069  0.0153  0.0057  132 VAL   A CB  
967  C  CG1 . VAL   A 126 ? 0.1638 0.1650 0.1743 0.0085  0.0146  0.0047  132 VAL   A CG1 
968  C  CG2 . VAL   A 126 ? 0.1544 0.1533 0.1640 0.0051  0.0132  0.0049  132 VAL   A CG2 
969  N  N   . GLY   A 127 ? 0.1307 0.1378 0.1559 0.0020  0.0121  0.0046  133 GLY   A N   
970  C  CA  . GLY   A 127 ? 0.1300 0.1371 0.1568 0.0008  0.0098  0.0030  133 GLY   A CA  
971  C  C   . GLY   A 127 ? 0.1448 0.1481 0.1668 0.0002  0.0092  0.0024  133 GLY   A C   
972  O  O   . GLY   A 127 ? 0.1429 0.1446 0.1634 -0.0003 0.0101  0.0033  133 GLY   A O   
973  N  N   . PHE   A 128 ? 0.1490 0.1506 0.1685 0.0006  0.0079  0.0010  134 PHE   A N   
974  C  CA  . PHE   A 128 ? 0.1514 0.1492 0.1670 0.0003  0.0082  0.0007  134 PHE   A CA  
975  C  C   . PHE   A 128 ? 0.1426 0.1392 0.1584 -0.0003 0.0077  -0.0004 134 PHE   A C   
976  O  O   . PHE   A 128 ? 0.1407 0.1375 0.1558 0.0006  0.0061  -0.0017 134 PHE   A O   
977  C  CB  . PHE   A 128 ? 0.1428 0.1379 0.1535 0.0019  0.0084  0.0006  134 PHE   A CB  
978  C  CG  . PHE   A 128 ? 0.1406 0.1360 0.1500 0.0030  0.0088  0.0012  134 PHE   A CG  
979  C  CD1 . PHE   A 128 ? 0.1443 0.1378 0.1522 0.0025  0.0094  0.0016  134 PHE   A CD1 
980  C  CD2 . PHE   A 128 ? 0.1456 0.1430 0.1553 0.0047  0.0084  0.0012  134 PHE   A CD2 
981  C  CE1 . PHE   A 128 ? 0.1563 0.1490 0.1617 0.0039  0.0097  0.0018  134 PHE   A CE1 
982  C  CE2 . PHE   A 128 ? 0.1563 0.1534 0.1644 0.0062  0.0093  0.0017  134 PHE   A CE2 
983  C  CZ  . PHE   A 128 ? 0.1525 0.1469 0.1578 0.0058  0.0101  0.0019  134 PHE   A CZ  
984  N  N   . ALA   A 129 ? 0.1409 0.1359 0.1574 -0.0014 0.0087  -0.0001 135 ALA   A N   
985  C  CA  . ALA   A 129 ? 0.1511 0.1439 0.1668 -0.0015 0.0090  -0.0011 135 ALA   A CA  
986  C  C   . ALA   A 129 ? 0.1570 0.1459 0.1670 0.0000  0.0101  -0.0013 135 ALA   A C   
987  O  O   . ALA   A 129 ? 0.1664 0.1540 0.1763 -0.0002 0.0117  -0.0002 135 ALA   A O   
988  C  CB  . ALA   A 129 ? 0.1574 0.1498 0.1765 -0.0029 0.0103  -0.0004 135 ALA   A CB  
989  N  N   . ASP   A 130 ? 0.1474 0.1343 0.1529 0.0015  0.0091  -0.0026 136 ASP   A N   
990  C  CA  . ASP   A 130 ? 0.1657 0.1480 0.1645 0.0035  0.0107  -0.0023 136 ASP   A CA  
991  C  C   . ASP   A 130 ? 0.1757 0.1545 0.1738 0.0033  0.0140  -0.0017 136 ASP   A C   
992  O  O   . ASP   A 130 ? 0.1726 0.1515 0.1729 0.0025  0.0142  -0.0026 136 ASP   A O   
993  C  CB  . ASP   A 130 ? 0.1877 0.1681 0.1807 0.0057  0.0082  -0.0040 136 ASP   A CB  
994  C  CG  . ASP   A 130 ? 0.2670 0.2419 0.2511 0.0086  0.0096  -0.0033 136 ASP   A CG  
995  O  OD1 . ASP   A 130 ? 0.2571 0.2312 0.2407 0.0089  0.0114  -0.0016 136 ASP   A OD1 
996  O  OD2 . ASP   A 130 ? 0.3162 0.2868 0.2934 0.0106  0.0092  -0.0045 136 ASP   A OD2 
997  N  N   . VAL   A 131 ? 0.1670 0.1425 0.1625 0.0042  0.0171  -0.0003 137 VAL   A N   
998  C  CA  . VAL   A 131 ? 0.1739 0.1459 0.1694 0.0044  0.0212  0.0006  137 VAL   A CA  
999  C  C   . VAL   A 131 ? 0.1842 0.1499 0.1707 0.0073  0.0241  0.0014  137 VAL   A C   
1000 O  O   . VAL   A 131 ? 0.1816 0.1437 0.1674 0.0080  0.0285  0.0026  137 VAL   A O   
1001 C  CB  . VAL   A 131 ? 0.1906 0.1644 0.1942 0.0023  0.0232  0.0023  137 VAL   A CB  
1002 C  CG1 . VAL   A 131 ? 0.1980 0.1768 0.2086 0.0001  0.0206  0.0018  137 VAL   A CG1 
1003 C  CG2 . VAL   A 131 ? 0.1977 0.1706 0.2013 0.0022  0.0238  0.0035  137 VAL   A CG2 
1004 N  N   . ARG   A 132 ? 0.1817 0.1460 0.1617 0.0093  0.0220  0.0011  138 ARG   A N   
1005 C  CA  . ARG   A 132 ? 0.1795 0.1372 0.1501 0.0125  0.0248  0.0024  138 ARG   A CA  
1006 C  C   . ARG   A 132 ? 0.2121 0.1642 0.1739 0.0152  0.0262  0.0015  138 ARG   A C   
1007 O  O   . ARG   A 132 ? 0.2270 0.1727 0.1814 0.0178  0.0306  0.0033  138 ARG   A O   
1008 C  CB  . ARG   A 132 ? 0.1809 0.1384 0.1466 0.0143  0.0214  0.0022  138 ARG   A CB  
1009 C  CG  . ARG   A 132 ? 0.2024 0.1634 0.1745 0.0125  0.0209  0.0033  138 ARG   A CG  
1010 C  CD  . ARG   A 132 ? 0.2161 0.1771 0.1836 0.0148  0.0176  0.0030  138 ARG   A CD  
1011 N  NE  . ARG   A 132 ? 0.2028 0.1691 0.1730 0.0144  0.0127  0.0007  138 ARG   A NE  
1012 C  CZ  . ARG   A 132 ? 0.2079 0.1765 0.1776 0.0158  0.0090  0.0001  138 ARG   A CZ  
1013 N  NH1 . ARG   A 132 ? 0.1948 0.1603 0.1599 0.0183  0.0096  0.0016  138 ARG   A NH1 
1014 N  NH2 . ARG   A 132 ? 0.2053 0.1793 0.1801 0.0149  0.0052  -0.0017 138 ARG   A NH2 
1015 N  N   . ASP   A 133 ? 0.2130 0.1669 0.1751 0.0147  0.0229  -0.0012 139 ASP   A N   
1016 C  CA  . ASP   A 133 ? 0.2283 0.1761 0.1810 0.0175  0.0238  -0.0027 139 ASP   A CA  
1017 C  C   . ASP   A 133 ? 0.2332 0.1786 0.1885 0.0171  0.0298  -0.0015 139 ASP   A C   
1018 O  O   . ASP   A 133 ? 0.2439 0.1830 0.1905 0.0199  0.0320  -0.0024 139 ASP   A O   
1019 C  CB  . ASP   A 133 ? 0.2345 0.1843 0.1869 0.0172  0.0176  -0.0064 139 ASP   A CB  
1020 C  CG  . ASP   A 133 ? 0.2896 0.2458 0.2541 0.0132  0.0165  -0.0071 139 ASP   A CG  
1021 O  OD1 . ASP   A 133 ? 0.2736 0.2352 0.2470 0.0106  0.0170  -0.0054 139 ASP   A OD1 
1022 O  OD2 . ASP   A 133 ? 0.2940 0.2490 0.2585 0.0130  0.0151  -0.0095 139 ASP   A OD2 
1023 N  N   . LEU   A 134 ? 0.2298 0.1802 0.1971 0.0138  0.0320  0.0001  140 LEU   A N   
1024 C  CA  . LEU   A 134 ? 0.2149 0.1643 0.1873 0.0133  0.0372  0.0012  140 LEU   A CA  
1025 C  C   . LEU   A 134 ? 0.2210 0.1654 0.1908 0.0151  0.0441  0.0044  140 LEU   A C   
1026 O  O   . LEU   A 134 ? 0.2054 0.1526 0.1848 0.0131  0.0467  0.0067  140 LEU   A O   
1027 C  CB  . LEU   A 134 ? 0.2036 0.1604 0.1900 0.0094  0.0358  0.0017  140 LEU   A CB  
1028 C  CG  . LEU   A 134 ? 0.2142 0.1757 0.2035 0.0076  0.0298  -0.0008 140 LEU   A CG  
1029 C  CD1 . LEU   A 134 ? 0.1941 0.1619 0.1952 0.0044  0.0286  0.0002  140 LEU   A CD1 
1030 C  CD2 . LEU   A 134 ? 0.2389 0.1973 0.2241 0.0088  0.0293  -0.0032 140 LEU   A CD2 
1031 N  N   . LEU   A 135 ? 0.2431 0.1794 0.1998 0.0192  0.0471  0.0044  141 LEU   A N   
1032 C  CA  . LEU   A 135 ? 0.2522 0.1827 0.2050 0.0215  0.0544  0.0079  141 LEU   A CA  
1033 C  C   . LEU   A 135 ? 0.2530 0.1842 0.2163 0.0203  0.0615  0.0104  141 LEU   A C   
1034 O  O   . LEU   A 135 ? 0.2531 0.1825 0.2202 0.0203  0.0670  0.0138  141 LEU   A O   
1035 C  CB  . LEU   A 135 ? 0.2643 0.1851 0.1988 0.0269  0.0562  0.0076  141 LEU   A CB  
1036 C  CG  . LEU   A 135 ? 0.2910 0.2109 0.2152 0.0286  0.0485  0.0048  141 LEU   A CG  
1037 C  CD1 . LEU   A 135 ? 0.3086 0.2177 0.2136 0.0345  0.0504  0.0047  141 LEU   A CD1 
1038 C  CD2 . LEU   A 135 ? 0.2972 0.2217 0.2263 0.0267  0.0450  0.0060  141 LEU   A CD2 
1039 N  N   . TRP   A 136 ? 0.2483 0.1817 0.2168 0.0195  0.0616  0.0089  142 TRP   A N   
1040 C  CA  . TRP   A 136 ? 0.2528 0.1873 0.2321 0.0187  0.0681  0.0111  142 TRP   A CA  
1041 C  C   . TRP   A 136 ? 0.2577 0.2001 0.2547 0.0144  0.0672  0.0129  142 TRP   A C   
1042 O  O   . TRP   A 136 ? 0.2576 0.2011 0.2655 0.0137  0.0728  0.0153  142 TRP   A O   
1043 C  CB  . TRP   A 136 ? 0.2521 0.1867 0.2318 0.0193  0.0676  0.0088  142 TRP   A CB  
1044 C  CG  . TRP   A 136 ? 0.2526 0.1933 0.2365 0.0164  0.0593  0.0057  142 TRP   A CG  
1045 C  CD1 . TRP   A 136 ? 0.2682 0.2077 0.2428 0.0171  0.0532  0.0023  142 TRP   A CD1 
1046 C  CD2 . TRP   A 136 ? 0.2464 0.1954 0.2452 0.0125  0.0561  0.0059  142 TRP   A CD2 
1047 N  NE1 . TRP   A 136 ? 0.2718 0.2181 0.2554 0.0138  0.0476  0.0007  142 TRP   A NE1 
1048 C  CE2 . TRP   A 136 ? 0.2558 0.2077 0.2532 0.0112  0.0493  0.0029  142 TRP   A CE2 
1049 C  CE3 . TRP   A 136 ? 0.2475 0.2015 0.2610 0.0103  0.0585  0.0082  142 TRP   A CE3 
1050 C  CZ2 . TRP   A 136 ? 0.2527 0.2116 0.2611 0.0080  0.0453  0.0027  142 TRP   A CZ2 
1051 C  CZ3 . TRP   A 136 ? 0.2487 0.2097 0.2729 0.0072  0.0536  0.0076  142 TRP   A CZ3 
1052 C  CH2 . TRP   A 136 ? 0.2537 0.2167 0.2745 0.0063  0.0474  0.0050  142 TRP   A CH2 
1053 N  N   . LEU   A 137 ? 0.2548 0.2021 0.2545 0.0117  0.0605  0.0118  143 LEU   A N   
1054 C  CA  . LEU   A 137 ? 0.2765 0.2301 0.2911 0.0079  0.0589  0.0129  143 LEU   A CA  
1055 C  C   . LEU   A 137 ? 0.3324 0.2834 0.3522 0.0079  0.0650  0.0162  143 LEU   A C   
1056 O  O   . LEU   A 137 ? 0.3204 0.2757 0.3547 0.0051  0.0655  0.0173  143 LEU   A O   
1057 C  CB  . LEU   A 137 ? 0.2608 0.2187 0.2750 0.0058  0.0511  0.0110  143 LEU   A CB  
1058 C  CG  . LEU   A 137 ? 0.2487 0.2111 0.2633 0.0047  0.0451  0.0083  143 LEU   A CG  
1059 C  CD1 . LEU   A 137 ? 0.2508 0.2166 0.2636 0.0033  0.0388  0.0070  143 LEU   A CD1 
1060 C  CD2 . LEU   A 137 ? 0.2358 0.2032 0.2632 0.0025  0.0448  0.0086  143 LEU   A CD2 
1061 N  N   . ASP   A 138 ? 0.3920 0.3355 0.4002 0.0111  0.0698  0.0178  144 ASP   A N   
1062 C  CA  . ASP   A 138 ? 0.4579 0.3973 0.4692 0.0116  0.0767  0.0215  144 ASP   A CA  
1063 C  C   . ASP   A 138 ? 0.5152 0.4481 0.5228 0.0150  0.0863  0.0242  144 ASP   A C   
1064 O  O   . ASP   A 138 ? 0.5328 0.4627 0.5459 0.0150  0.0931  0.0278  144 ASP   A O   
1065 C  CB  . ASP   A 138 ? 0.5186 0.4524 0.5163 0.0139  0.0758  0.0219  144 ASP   A CB  
1066 C  CG  . ASP   A 138 ? 0.6343 0.5725 0.6347 0.0113  0.0684  0.0202  144 ASP   A CG  
1067 O  OD1 . ASP   A 138 ? 0.6591 0.6030 0.6736 0.0074  0.0662  0.0200  144 ASP   A OD1 
1068 O  OD2 . ASP   A 138 ? 0.6890 0.6250 0.6774 0.0132  0.0646  0.0189  144 ASP   A OD2 
1069 N  N   . GLU   A 139 ? 0.5473 0.4759 0.5419 0.0185  0.0870  0.0227  145 GLU   A N   
1070 C  CA  . GLU   A 139 ? 0.5844 0.5046 0.5706 0.0229  0.0965  0.0252  145 GLU   A CA  
1071 C  C   . GLU   A 139 ? 0.6007 0.5223 0.5941 0.0233  0.1007  0.0251  145 GLU   A C   
1072 O  O   . GLU   A 139 ? 0.6158 0.5340 0.6138 0.0250  0.1103  0.0286  145 GLU   A O   
1073 C  CB  . GLU   A 139 ? 0.6358 0.5473 0.5991 0.0278  0.0954  0.0239  145 GLU   A CB  
1074 C  CG  . GLU   A 139 ? 0.7149 0.6269 0.6696 0.0288  0.0888  0.0193  145 GLU   A CG  
1075 C  CD  . GLU   A 139 ? 0.8304 0.7352 0.7643 0.0330  0.0849  0.0173  145 GLU   A CD  
1076 O  OE1 . GLU   A 139 ? 0.8616 0.7631 0.7853 0.0354  0.0824  0.0140  145 GLU   A OE1 
1077 O  OE2 . GLU   A 139 ? 0.8561 0.7584 0.7842 0.0339  0.0842  0.0189  145 GLU   A OE2 
1078 N  N   . SER   B 1   ? 0.2952 0.2632 0.2899 0.0015  -0.0153 -0.0056 7   SER   C N   
1079 C  CA  . SER   B 1   ? 0.2836 0.2556 0.2882 0.0025  -0.0165 -0.0059 7   SER   C CA  
1080 C  C   . SER   B 1   ? 0.2747 0.2491 0.2840 0.0035  -0.0151 -0.0050 7   SER   C C   
1081 O  O   . SER   B 1   ? 0.2884 0.2605 0.2931 0.0035  -0.0147 -0.0039 7   SER   C O   
1082 C  CB  . SER   B 1   ? 0.3128 0.2833 0.3194 0.0024  -0.0219 -0.0061 7   SER   C CB  
1083 O  OG  . SER   B 1   ? 0.3778 0.3450 0.3812 0.0027  -0.0254 -0.0045 7   SER   C OG  
1084 N  N   . GLY   B 2   ? 0.2457 0.2241 0.2636 0.0041  -0.0141 -0.0057 8   GLY   C N   
1085 C  CA  . GLY   B 2   ? 0.2311 0.2115 0.2537 0.0048  -0.0124 -0.0056 8   GLY   C CA  
1086 C  C   . GLY   B 2   ? 0.2175 0.2021 0.2459 0.0045  -0.0087 -0.0066 8   GLY   C C   
1087 O  O   . GLY   B 2   ? 0.2217 0.2073 0.2491 0.0036  -0.0071 -0.0068 8   GLY   C O   
1088 N  N   . ALA   B 3   ? 0.1963 0.1830 0.2307 0.0049  -0.0074 -0.0073 9   ALA   C N   
1089 C  CA  . ALA   B 3   ? 0.1890 0.1790 0.2279 0.0039  -0.0036 -0.0084 9   ALA   C CA  
1090 C  C   . ALA   B 3   ? 0.1812 0.1718 0.2216 0.0039  -0.0007 -0.0090 9   ALA   C C   
1091 O  O   . ALA   B 3   ? 0.1806 0.1693 0.2211 0.0050  -0.0022 -0.0089 9   ALA   C O   
1092 C  CB  . ALA   B 3   ? 0.1901 0.1828 0.2376 0.0039  -0.0045 -0.0098 9   ALA   C CB  
1093 N  N   . ILE   B 4   ? 0.1801 0.1726 0.2210 0.0023  0.0033  -0.0097 10  ILE   C N   
1094 C  CA  . ILE   B 4   ? 0.1759 0.1688 0.2181 0.0017  0.0066  -0.0111 10  ILE   C CA  
1095 C  C   . ILE   B 4   ? 0.1753 0.1712 0.2265 0.0013  0.0089  -0.0134 10  ILE   C C   
1096 O  O   . ILE   B 4   ? 0.1759 0.1735 0.2287 0.0000  0.0099  -0.0135 10  ILE   C O   
1097 C  CB  . ILE   B 4   ? 0.1836 0.1762 0.2188 -0.0005 0.0095  -0.0103 10  ILE   C CB  
1098 C  CG1 . ILE   B 4   ? 0.2054 0.1962 0.2338 -0.0002 0.0075  -0.0083 10  ILE   C CG1 
1099 C  CG2 . ILE   B 4   ? 0.1918 0.1840 0.2271 -0.0017 0.0131  -0.0120 10  ILE   C CG2 
1100 C  CD1 . ILE   B 4   ? 0.2211 0.2123 0.2441 -0.0021 0.0091  -0.0070 10  ILE   C CD1 
1101 N  N   . TYR   B 5   ? 0.1909 0.1871 0.2484 0.0023  0.0101  -0.0153 11  TYR   C N   
1102 C  CA  . TYR   B 5   ? 0.1947 0.1942 0.2622 0.0020  0.0129  -0.0181 11  TYR   C CA  
1103 C  C   . TYR   B 5   ? 0.2025 0.2016 0.2690 0.0003  0.0186  -0.0203 11  TYR   C C   
1104 O  O   . TYR   B 5   ? 0.2061 0.2032 0.2731 0.0015  0.0189  -0.0212 11  TYR   C O   
1105 C  CB  . TYR   B 5   ? 0.1919 0.1922 0.2698 0.0050  0.0092  -0.0189 11  TYR   C CB  
1106 C  CG  . TYR   B 5   ? 0.1947 0.1953 0.2732 0.0060  0.0036  -0.0170 11  TYR   C CG  
1107 C  CD1 . TYR   B 5   ? 0.1954 0.1993 0.2797 0.0050  0.0034  -0.0177 11  TYR   C CD1 
1108 C  CD2 . TYR   B 5   ? 0.2073 0.2041 0.2791 0.0073  -0.0013 -0.0146 11  TYR   C CD2 
1109 C  CE1 . TYR   B 5   ? 0.2121 0.2156 0.2957 0.0054  -0.0018 -0.0163 11  TYR   C CE1 
1110 C  CE2 . TYR   B 5   ? 0.2219 0.2181 0.2922 0.0076  -0.0061 -0.0131 11  TYR   C CE2 
1111 C  CZ  . TYR   B 5   ? 0.2223 0.2218 0.2988 0.0068  -0.0066 -0.0141 11  TYR   C CZ  
1112 O  OH  . TYR   B 5   ? 0.2456 0.2440 0.3198 0.0067  -0.0113 -0.0130 11  TYR   C OH  
1113 N  N   . VAL   B 6   ? 0.2027 0.2030 0.2669 -0.0028 0.0231  -0.0211 12  VAL   C N   
1114 C  CA  . VAL   B 6   ? 0.2091 0.2082 0.2697 -0.0052 0.0288  -0.0233 12  VAL   C CA  
1115 C  C   . VAL   B 6   ? 0.2166 0.2185 0.2827 -0.0077 0.0341  -0.0259 12  VAL   C C   
1116 O  O   . VAL   B 6   ? 0.2155 0.2185 0.2800 -0.0095 0.0341  -0.0245 12  VAL   C O   
1117 C  CB  . VAL   B 6   ? 0.2347 0.2308 0.2818 -0.0076 0.0288  -0.0210 12  VAL   C CB  
1118 C  CG1 . VAL   B 6   ? 0.2434 0.2399 0.2858 -0.0087 0.0266  -0.0180 12  VAL   C CG1 
1119 C  CG2 . VAL   B 6   ? 0.2510 0.2455 0.2930 -0.0110 0.0344  -0.0232 12  VAL   C CG2 
1120 N  N   . GLY   B 7   ? 0.2239 0.2270 0.2978 -0.0077 0.0387  -0.0298 13  GLY   C N   
1121 C  CA  . GLY   B 7   ? 0.2299 0.2359 0.3099 -0.0103 0.0446  -0.0328 13  GLY   C CA  
1122 C  C   . GLY   B 7   ? 0.2317 0.2419 0.3216 -0.0092 0.0418  -0.0322 13  GLY   C C   
1123 O  O   . GLY   B 7   ? 0.2416 0.2533 0.3393 -0.0054 0.0365  -0.0315 13  GLY   C O   
1124 N  N   . ASN   B 8   ? 0.2333 0.2446 0.3212 -0.0126 0.0444  -0.0317 14  ASN   C N   
1125 C  CA  . ASN   B 8   ? 0.2345 0.2494 0.3311 -0.0119 0.0414  -0.0310 14  ASN   C CA  
1126 C  C   . ASN   B 8   ? 0.2162 0.2285 0.3035 -0.0121 0.0362  -0.0268 14  ASN   C C   
1127 O  O   . ASN   B 8   ? 0.2195 0.2332 0.3092 -0.0137 0.0357  -0.0260 14  ASN   C O   
1128 C  CB  . ASN   B 8   ? 0.2774 0.2958 0.3816 -0.0153 0.0477  -0.0340 14  ASN   C CB  
1129 C  CG  . ASN   B 8   ? 0.3636 0.3859 0.4818 -0.0139 0.0518  -0.0387 14  ASN   C CG  
1130 O  OD1 . ASN   B 8   ? 0.3987 0.4244 0.5300 -0.0100 0.0477  -0.0395 14  ASN   C OD1 
1131 N  ND2 . ASN   B 8   ? 0.3860 0.4073 0.5016 -0.0170 0.0597  -0.0417 14  ASN   C ND2 
1132 N  N   . TYR   B 9   ? 0.1933 0.2021 0.2711 -0.0104 0.0324  -0.0242 15  TYR   C N   
1133 C  CA  . TYR   B 9   ? 0.1860 0.1923 0.2555 -0.0103 0.0279  -0.0205 15  TYR   C CA  
1134 C  C   . TYR   B 9   ? 0.1812 0.1867 0.2509 -0.0065 0.0217  -0.0190 15  TYR   C C   
1135 O  O   . TYR   B 9   ? 0.1759 0.1809 0.2470 -0.0044 0.0209  -0.0198 15  TYR   C O   
1136 C  CB  . TYR   B 9   ? 0.1803 0.1827 0.2365 -0.0125 0.0295  -0.0184 15  TYR   C CB  
1137 C  CG  . TYR   B 9   ? 0.2010 0.2026 0.2533 -0.0170 0.0351  -0.0190 15  TYR   C CG  
1138 C  CD1 . TYR   B 9   ? 0.2200 0.2224 0.2748 -0.0192 0.0362  -0.0187 15  TYR   C CD1 
1139 C  CD2 . TYR   B 9   ? 0.2173 0.2168 0.2626 -0.0194 0.0392  -0.0200 15  TYR   C CD2 
1140 C  CE1 . TYR   B 9   ? 0.2463 0.2471 0.2963 -0.0238 0.0415  -0.0189 15  TYR   C CE1 
1141 C  CE2 . TYR   B 9   ? 0.2423 0.2401 0.2822 -0.0241 0.0443  -0.0205 15  TYR   C CE2 
1142 C  CZ  . TYR   B 9   ? 0.2646 0.2630 0.3067 -0.0263 0.0455  -0.0198 15  TYR   C CZ  
1143 O  OH  . TYR   B 9   ? 0.2985 0.2944 0.3340 -0.0315 0.0508  -0.0199 15  TYR   C OH  
1144 N  N   . ARG   B 10  ? 0.1643 0.1689 0.2317 -0.0059 0.0176  -0.0169 16  ARG   C N   
1145 C  CA  . ARG   B 10  ? 0.1725 0.1755 0.2375 -0.0032 0.0121  -0.0152 16  ARG   C CA  
1146 C  C   . ARG   B 10  ? 0.1635 0.1634 0.2181 -0.0040 0.0113  -0.0126 16  ARG   C C   
1147 O  O   . ARG   B 10  ? 0.1708 0.1705 0.2245 -0.0057 0.0120  -0.0119 16  ARG   C O   
1148 C  CB  . ARG   B 10  ? 0.1756 0.1804 0.2484 -0.0020 0.0080  -0.0158 16  ARG   C CB  
1149 C  CG  . ARG   B 10  ? 0.1837 0.1856 0.2511 -0.0003 0.0026  -0.0139 16  ARG   C CG  
1150 C  CD  . ARG   B 10  ? 0.1985 0.2019 0.2732 0.0006  -0.0020 -0.0146 16  ARG   C CD  
1151 N  NE  . ARG   B 10  ? 0.2261 0.2268 0.2951 0.0002  -0.0054 -0.0135 16  ARG   C NE  
1152 C  CZ  . ARG   B 10  ? 0.2415 0.2390 0.3047 0.0016  -0.0096 -0.0124 16  ARG   C CZ  
1153 N  NH1 . ARG   B 10  ? 0.2235 0.2198 0.2856 0.0033  -0.0115 -0.0118 16  ARG   C NH1 
1154 N  NH2 . ARG   B 10  ? 0.2219 0.2168 0.2799 0.0009  -0.0118 -0.0120 16  ARG   C NH2 
1155 N  N   . VAL   B 11  ? 0.1628 0.1605 0.2105 -0.0030 0.0101  -0.0112 17  VAL   C N   
1156 C  CA  . VAL   B 11  ? 0.1628 0.1584 0.2026 -0.0034 0.0093  -0.0089 17  VAL   C CA  
1157 C  C   . VAL   B 11  ? 0.1715 0.1656 0.2097 -0.0013 0.0053  -0.0082 17  VAL   C C   
1158 O  O   . VAL   B 11  ? 0.1687 0.1622 0.2065 0.0002  0.0037  -0.0084 17  VAL   C O   
1159 C  CB  . VAL   B 11  ? 0.1866 0.1812 0.2202 -0.0041 0.0110  -0.0082 17  VAL   C CB  
1160 C  CG1 . VAL   B 11  ? 0.1879 0.1810 0.2152 -0.0046 0.0101  -0.0058 17  VAL   C CG1 
1161 C  CG2 . VAL   B 11  ? 0.1808 0.1761 0.2150 -0.0063 0.0152  -0.0095 17  VAL   C CG2 
1162 N  N   . VAL   B 12  ? 0.1597 0.1528 0.1964 -0.0014 0.0040  -0.0074 18  VAL   C N   
1163 C  CA  . VAL   B 12  ? 0.1733 0.1645 0.2074 0.0001  0.0009  -0.0071 18  VAL   C CA  
1164 C  C   . VAL   B 12  ? 0.1522 0.1416 0.1814 0.0000  0.0013  -0.0058 18  VAL   C C   
1165 O  O   . VAL   B 12  ? 0.1443 0.1338 0.1733 -0.0011 0.0030  -0.0049 18  VAL   C O   
1166 C  CB  . VAL   B 12  ? 0.2036 0.1948 0.2422 0.0001  -0.0017 -0.0083 18  VAL   C CB  
1167 C  CG1 . VAL   B 12  ? 0.2430 0.2359 0.2874 0.0009  -0.0032 -0.0094 18  VAL   C CG1 
1168 C  CG2 . VAL   B 12  ? 0.1948 0.1866 0.2367 -0.0015 -0.0002 -0.0086 18  VAL   C CG2 
1169 N  N   . ASN   B 13  ? 0.1436 0.1310 0.1691 0.0011  -0.0004 -0.0058 19  ASN   C N   
1170 C  CA  . ASN   B 13  ? 0.1377 0.1236 0.1606 0.0013  0.0002  -0.0052 19  ASN   C CA  
1171 C  C   . ASN   B 13  ? 0.1576 0.1423 0.1833 0.0006  -0.0002 -0.0057 19  ASN   C C   
1172 O  O   . ASN   B 13  ? 0.1730 0.1572 0.2006 0.0003  -0.0019 -0.0071 19  ASN   C O   
1173 C  CB  . ASN   B 13  ? 0.1481 0.1318 0.1670 0.0022  -0.0008 -0.0059 19  ASN   C CB  
1174 C  CG  . ASN   B 13  ? 0.1774 0.1615 0.1931 0.0026  -0.0003 -0.0053 19  ASN   C CG  
1175 O  OD1 . ASN   B 13  ? 0.1882 0.1716 0.2026 0.0026  -0.0017 -0.0056 19  ASN   C OD1 
1176 N  ND2 . ASN   B 13  ? 0.1618 0.1469 0.1766 0.0028  0.0014  -0.0045 19  ASN   C ND2 
1177 N  N   . ARG   B 14  ? 0.1548 0.1389 0.1807 0.0001  0.0011  -0.0046 20  ARG   C N   
1178 C  CA  . ARG   B 14  ? 0.1474 0.1296 0.1757 -0.0008 0.0010  -0.0049 20  ARG   C CA  
1179 C  C   . ARG   B 14  ? 0.1548 0.1344 0.1824 -0.0002 -0.0006 -0.0067 20  ARG   C C   
1180 O  O   . ARG   B 14  ? 0.1655 0.1444 0.1957 -0.0014 -0.0017 -0.0079 20  ARG   C O   
1181 C  CB  . ARG   B 14  ? 0.1596 0.1404 0.1874 -0.0012 0.0021  -0.0028 20  ARG   C CB  
1182 C  CG  . ARG   B 14  ? 0.1719 0.1503 0.2019 -0.0028 0.0023  -0.0025 20  ARG   C CG  
1183 C  CD  . ARG   B 14  ? 0.1735 0.1491 0.2022 -0.0026 0.0025  -0.0001 20  ARG   C CD  
1184 N  NE  . ARG   B 14  ? 0.1725 0.1448 0.2024 -0.0044 0.0028  0.0008  20  ARG   C NE  
1185 C  CZ  . ARG   B 14  ? 0.1922 0.1610 0.2236 -0.0041 0.0021  -0.0002 20  ARG   C CZ  
1186 N  NH1 . ARG   B 14  ? 0.1954 0.1635 0.2269 -0.0022 0.0013  -0.0025 20  ARG   C NH1 
1187 N  NH2 . ARG   B 14  ? 0.2012 0.1663 0.2333 -0.0060 0.0024  0.0010  20  ARG   C NH2 
1188 N  N   . HIS   B 15  ? 0.1542 0.1324 0.1781 0.0012  -0.0007 -0.0072 21  HIS   C N   
1189 C  CA  . HIS   B 15  ? 0.1622 0.1371 0.1839 0.0013  -0.0017 -0.0093 21  HIS   C CA  
1190 C  C   . HIS   B 15  ? 0.1793 0.1540 0.1998 0.0005  -0.0044 -0.0107 21  HIS   C C   
1191 O  O   . HIS   B 15  ? 0.1999 0.1716 0.2183 -0.0002 -0.0059 -0.0125 21  HIS   C O   
1192 C  CB  . HIS   B 15  ? 0.1656 0.1388 0.1838 0.0026  -0.0002 -0.0099 21  HIS   C CB  
1193 C  CG  . HIS   B 15  ? 0.1664 0.1408 0.1808 0.0031  0.0000  -0.0099 21  HIS   C CG  
1194 N  ND1 . HIS   B 15  ? 0.1802 0.1578 0.1954 0.0036  0.0011  -0.0081 21  HIS   C ND1 
1195 C  CD2 . HIS   B 15  ? 0.1928 0.1649 0.2017 0.0027  -0.0006 -0.0114 21  HIS   C CD2 
1196 C  CE1 . HIS   B 15  ? 0.2053 0.1826 0.2163 0.0036  0.0012  -0.0085 21  HIS   C CE1 
1197 N  NE2 . HIS   B 15  ? 0.2128 0.1867 0.2196 0.0030  0.0002  -0.0104 21  HIS   C NE2 
1198 N  N   . LEU   B 16  ? 0.1795 0.1572 0.2015 0.0005  -0.0053 -0.0099 22  LEU   C N   
1199 C  CA  . LEU   B 16  ? 0.1848 0.1626 0.2070 0.0001  -0.0086 -0.0108 22  LEU   C CA  
1200 C  C   . LEU   B 16  ? 0.1994 0.1802 0.2292 -0.0008 -0.0096 -0.0110 22  LEU   C C   
1201 O  O   . LEU   B 16  ? 0.2016 0.1833 0.2339 -0.0008 -0.0128 -0.0115 22  LEU   C O   
1202 C  CB  . LEU   B 16  ? 0.1802 0.1584 0.1991 0.0010  -0.0090 -0.0099 22  LEU   C CB  
1203 C  CG  . LEU   B 16  ? 0.1948 0.1701 0.2062 0.0014  -0.0077 -0.0099 22  LEU   C CG  
1204 C  CD1 . LEU   B 16  ? 0.2109 0.1862 0.2190 0.0018  -0.0082 -0.0089 22  LEU   C CD1 
1205 C  CD2 . LEU   B 16  ? 0.2238 0.1947 0.2299 0.0005  -0.0092 -0.0118 22  LEU   C CD2 
1206 N  N   . ALA   B 17  ? 0.1989 0.1812 0.2327 -0.0015 -0.0070 -0.0104 23  ALA   C N   
1207 C  CA  . ALA   B 17  ? 0.2058 0.1913 0.2472 -0.0028 -0.0069 -0.0109 23  ALA   C CA  
1208 C  C   . ALA   B 17  ? 0.2061 0.1911 0.2509 -0.0040 -0.0102 -0.0126 23  ALA   C C   
1209 O  O   . ALA   B 17  ? 0.2056 0.1870 0.2468 -0.0045 -0.0112 -0.0133 23  ALA   C O   
1210 C  CB  . ALA   B 17  ? 0.1976 0.1834 0.2404 -0.0041 -0.0034 -0.0099 23  ALA   C CB  
1211 N  N   . THR   B 18  ? 0.1979 0.1864 0.2500 -0.0044 -0.0118 -0.0134 24  THR   C N   
1212 C  CA  . THR   B 18  ? 0.1987 0.1876 0.2556 -0.0056 -0.0157 -0.0150 24  THR   C CA  
1213 C  C   . THR   B 18  ? 0.1998 0.1906 0.2637 -0.0080 -0.0136 -0.0158 24  THR   C C   
1214 O  O   . THR   B 18  ? 0.1881 0.1798 0.2530 -0.0088 -0.0092 -0.0150 24  THR   C O   
1215 C  CB  . THR   B 18  ? 0.2028 0.1953 0.2663 -0.0046 -0.0191 -0.0153 24  THR   C CB  
1216 O  OG1 . THR   B 18  ? 0.2055 0.2030 0.2778 -0.0048 -0.0157 -0.0156 24  THR   C OG1 
1217 C  CG2 . THR   B 18  ? 0.2187 0.2090 0.2755 -0.0026 -0.0212 -0.0142 24  THR   C CG2 
1218 N  N   . HIS   B 19  ? 0.2047 0.1958 0.2732 -0.0097 -0.0170 -0.0174 25  HIS   C N   
1219 C  CA  . HIS   B 19  ? 0.2051 0.1983 0.2815 -0.0125 -0.0152 -0.0184 25  HIS   C CA  
1220 C  C   . HIS   B 19  ? 0.1956 0.1947 0.2810 -0.0128 -0.0115 -0.0184 25  HIS   C C   
1221 O  O   . HIS   B 19  ? 0.1980 0.1975 0.2851 -0.0148 -0.0069 -0.0181 25  HIS   C O   
1222 C  CB  . HIS   B 19  ? 0.2371 0.2310 0.3186 -0.0141 -0.0203 -0.0203 25  HIS   C CB  
1223 C  CG  . HIS   B 19  ? 0.3373 0.3249 0.4100 -0.0147 -0.0232 -0.0209 25  HIS   C CG  
1224 N  ND1 . HIS   B 19  ? 0.3864 0.3689 0.4522 -0.0152 -0.0199 -0.0205 25  HIS   C ND1 
1225 C  CD2 . HIS   B 19  ? 0.3769 0.3625 0.4471 -0.0152 -0.0289 -0.0221 25  HIS   C CD2 
1226 C  CE1 . HIS   B 19  ? 0.4024 0.3799 0.4619 -0.0158 -0.0231 -0.0219 25  HIS   C CE1 
1227 N  NE2 . HIS   B 19  ? 0.4047 0.3836 0.4657 -0.0161 -0.0285 -0.0229 25  HIS   C NE2 
1228 N  N   . ASN   B 20  ? 0.1841 0.1869 0.2744 -0.0108 -0.0134 -0.0187 26  ASN   C N   
1229 C  CA  . ASN   B 20  ? 0.1870 0.1952 0.2863 -0.0110 -0.0095 -0.0194 26  ASN   C CA  
1230 C  C   . ASN   B 20  ? 0.1927 0.1993 0.2854 -0.0109 -0.0037 -0.0180 26  ASN   C C   
1231 O  O   . ASN   B 20  ? 0.2062 0.2154 0.3034 -0.0129 0.0013  -0.0187 26  ASN   C O   
1232 C  CB  . ASN   B 20  ? 0.2073 0.2190 0.3135 -0.0084 -0.0130 -0.0200 26  ASN   C CB  
1233 C  CG  . ASN   B 20  ? 0.2704 0.2879 0.3879 -0.0085 -0.0087 -0.0215 26  ASN   C CG  
1234 O  OD1 . ASN   B 20  ? 0.2793 0.3012 0.4075 -0.0107 -0.0069 -0.0234 26  ASN   C OD1 
1235 N  ND2 . ASN   B 20  ? 0.2811 0.2985 0.3963 -0.0065 -0.0063 -0.0211 26  ASN   C ND2 
1236 N  N   . ASP   B 21  ? 0.1871 0.1897 0.2691 -0.0091 -0.0042 -0.0163 27  ASP   C N   
1237 C  CA  . ASP   B 21  ? 0.1864 0.1874 0.2619 -0.0092 0.0004  -0.0148 27  ASP   C CA  
1238 C  C   . ASP   B 21  ? 0.1911 0.1900 0.2643 -0.0121 0.0038  -0.0140 27  ASP   C C   
1239 O  O   . ASP   B 21  ? 0.1975 0.1970 0.2703 -0.0139 0.0083  -0.0135 27  ASP   C O   
1240 C  CB  . ASP   B 21  ? 0.1764 0.1735 0.2417 -0.0070 -0.0014 -0.0131 27  ASP   C CB  
1241 C  CG  . ASP   B 21  ? 0.1973 0.1955 0.2626 -0.0045 -0.0036 -0.0132 27  ASP   C CG  
1242 O  OD1 . ASP   B 21  ? 0.1904 0.1919 0.2617 -0.0042 -0.0019 -0.0141 27  ASP   C OD1 
1243 O  OD2 . ASP   B 21  ? 0.2011 0.1963 0.2603 -0.0030 -0.0068 -0.0126 27  ASP   C OD2 
1244 N  N   . TRP   B 22  ? 0.1838 0.1794 0.2547 -0.0128 0.0015  -0.0138 28  TRP   C N   
1245 C  CA  . TRP   B 22  ? 0.1907 0.1831 0.2594 -0.0154 0.0041  -0.0127 28  TRP   C CA  
1246 C  C   . TRP   B 22  ? 0.2051 0.2007 0.2822 -0.0188 0.0070  -0.0140 28  TRP   C C   
1247 O  O   . TRP   B 22  ? 0.2142 0.2077 0.2888 -0.0215 0.0109  -0.0128 28  TRP   C O   
1248 C  CB  . TRP   B 22  ? 0.1932 0.1808 0.2580 -0.0151 0.0011  -0.0126 28  TRP   C CB  
1249 C  CG  . TRP   B 22  ? 0.1859 0.1694 0.2419 -0.0128 0.0006  -0.0109 28  TRP   C CG  
1250 C  CD1 . TRP   B 22  ? 0.1942 0.1766 0.2462 -0.0102 -0.0022 -0.0114 28  TRP   C CD1 
1251 C  CD2 . TRP   B 22  ? 0.1771 0.1570 0.2277 -0.0130 0.0029  -0.0084 28  TRP   C CD2 
1252 N  NE1 . TRP   B 22  ? 0.1963 0.1754 0.2419 -0.0087 -0.0012 -0.0097 28  TRP   C NE1 
1253 C  CE2 . TRP   B 22  ? 0.1951 0.1728 0.2401 -0.0102 0.0015  -0.0078 28  TRP   C CE2 
1254 C  CE3 . TRP   B 22  ? 0.1837 0.1621 0.2335 -0.0155 0.0059  -0.0066 28  TRP   C CE3 
1255 C  CZ2 . TRP   B 22  ? 0.1998 0.1744 0.2402 -0.0095 0.0025  -0.0054 28  TRP   C CZ2 
1256 C  CZ3 . TRP   B 22  ? 0.2044 0.1787 0.2481 -0.0149 0.0065  -0.0039 28  TRP   C CZ3 
1257 C  CH2 . TRP   B 22  ? 0.2015 0.1744 0.2414 -0.0117 0.0046  -0.0033 28  TRP   C CH2 
1258 N  N   . ALA   B 23  ? 0.1936 0.1940 0.2805 -0.0189 0.0053  -0.0164 29  ALA   C N   
1259 C  CA  . ALA   B 23  ? 0.1996 0.2041 0.2964 -0.0222 0.0084  -0.0181 29  ALA   C CA  
1260 C  C   . ALA   B 23  ? 0.2094 0.2174 0.3088 -0.0230 0.0140  -0.0186 29  ALA   C C   
1261 O  O   . ALA   B 23  ? 0.2128 0.2237 0.3189 -0.0263 0.0184  -0.0200 29  ALA   C O   
1262 C  CB  . ALA   B 23  ? 0.1964 0.2056 0.3044 -0.0219 0.0042  -0.0206 29  ALA   C CB  
1263 N  N   . ASN   B 24  ? 0.1919 0.1998 0.2865 -0.0201 0.0140  -0.0179 30  ASN   C N   
1264 C  CA  . ASN   B 24  ? 0.1989 0.2093 0.2946 -0.0207 0.0191  -0.0187 30  ASN   C CA  
1265 C  C   . ASN   B 24  ? 0.2053 0.2107 0.2877 -0.0204 0.0207  -0.0161 30  ASN   C C   
1266 O  O   . ASN   B 24  ? 0.2000 0.2062 0.2801 -0.0192 0.0223  -0.0163 30  ASN   C O   
1267 C  CB  . ASN   B 24  ? 0.2136 0.2287 0.3178 -0.0175 0.0172  -0.0208 30  ASN   C CB  
1268 C  CG  . ASN   B 24  ? 0.2579 0.2786 0.3769 -0.0181 0.0158  -0.0234 30  ASN   C CG  
1269 O  OD1 . ASN   B 24  ? 0.2594 0.2840 0.3871 -0.0208 0.0208  -0.0256 30  ASN   C OD1 
1270 N  ND2 . ASN   B 24  ? 0.2557 0.2768 0.3778 -0.0160 0.0090  -0.0234 30  ASN   C ND2 
1271 N  N   . LEU   B 25  ? 0.2012 0.2015 0.2755 -0.0216 0.0199  -0.0136 31  LEU   C N   
1272 C  CA  . LEU   B 25  ? 0.2073 0.2031 0.2702 -0.0211 0.0201  -0.0107 31  LEU   C CA  
1273 C  C   . LEU   B 25  ? 0.2092 0.2042 0.2672 -0.0239 0.0252  -0.0101 31  LEU   C C   
1274 O  O   . LEU   B 25  ? 0.2302 0.2250 0.2895 -0.0278 0.0293  -0.0105 31  LEU   C O   
1275 C  CB  . LEU   B 25  ? 0.2091 0.1995 0.2669 -0.0220 0.0182  -0.0083 31  LEU   C CB  
1276 C  CG  . LEU   B 25  ? 0.2196 0.2052 0.2670 -0.0213 0.0175  -0.0050 31  LEU   C CG  
1277 C  CD1 . LEU   B 25  ? 0.2386 0.2250 0.2836 -0.0172 0.0143  -0.0048 31  LEU   C CD1 
1278 C  CD2 . LEU   B 25  ? 0.2225 0.2026 0.2668 -0.0222 0.0159  -0.0029 31  LEU   C CD2 
1279 N  N   . VAL   B 26  ? 0.1968 0.1910 0.2482 -0.0224 0.0251  -0.0091 32  VAL   C N   
1280 C  CA  . VAL   B 26  ? 0.2071 0.1995 0.2514 -0.0253 0.0293  -0.0084 32  VAL   C CA  
1281 C  C   . VAL   B 26  ? 0.2191 0.2061 0.2524 -0.0256 0.0270  -0.0043 32  VAL   C C   
1282 O  O   . VAL   B 26  ? 0.2414 0.2246 0.2680 -0.0293 0.0292  -0.0023 32  VAL   C O   
1283 C  CB  . VAL   B 26  ? 0.2123 0.2076 0.2578 -0.0238 0.0308  -0.0105 32  VAL   C CB  
1284 C  CG1 . VAL   B 26  ? 0.2221 0.2145 0.2578 -0.0269 0.0345  -0.0096 32  VAL   C CG1 
1285 C  CG2 . VAL   B 26  ? 0.2138 0.2144 0.2715 -0.0236 0.0334  -0.0145 32  VAL   C CG2 
1286 N  N   . TRP   B 27  ? 0.1993 0.1858 0.2312 -0.0219 0.0225  -0.0031 33  TRP   C N   
1287 C  CA  . TRP   B 27  ? 0.2056 0.1880 0.2295 -0.0214 0.0199  0.0004  33  TRP   C CA  
1288 C  C   . TRP   B 27  ? 0.2070 0.1898 0.2329 -0.0172 0.0155  0.0006  33  TRP   C C   
1289 O  O   . TRP   B 27  ? 0.1971 0.1831 0.2272 -0.0148 0.0146  -0.0015 33  TRP   C O   
1290 C  CB  . TRP   B 27  ? 0.2056 0.1878 0.2226 -0.0224 0.0210  0.0012  33  TRP   C CB  
1291 C  CG  . TRP   B 27  ? 0.2267 0.2062 0.2372 -0.0213 0.0175  0.0045  33  TRP   C CG  
1292 C  CD1 . TRP   B 27  ? 0.2509 0.2257 0.2548 -0.0233 0.0163  0.0081  33  TRP   C CD1 
1293 C  CD2 . TRP   B 27  ? 0.2228 0.2040 0.2333 -0.0179 0.0146  0.0046  33  TRP   C CD2 
1294 N  NE1 . TRP   B 27  ? 0.2579 0.2322 0.2590 -0.0212 0.0125  0.0104  33  TRP   C NE1 
1295 C  CE2 . TRP   B 27  ? 0.2413 0.2196 0.2463 -0.0180 0.0119  0.0081  33  TRP   C CE2 
1296 C  CE3 . TRP   B 27  ? 0.2227 0.2074 0.2373 -0.0151 0.0141  0.0023  33  TRP   C CE3 
1297 C  CZ2 . TRP   B 27  ? 0.2417 0.2215 0.2463 -0.0154 0.0090  0.0089  33  TRP   C CZ2 
1298 C  CZ3 . TRP   B 27  ? 0.2275 0.2128 0.2402 -0.0129 0.0115  0.0032  33  TRP   C CZ3 
1299 C  CH2 . TRP   B 27  ? 0.2346 0.2178 0.2429 -0.0131 0.0092  0.0063  33  TRP   C CH2 
1300 N  N   . GLU   B 28  ? 0.2053 0.1845 0.2283 -0.0164 0.0130  0.0032  34  GLU   C N   
1301 C  CA  . GLU   B 28  ? 0.2066 0.1859 0.2309 -0.0126 0.0097  0.0032  34  GLU   C CA  
1302 C  C   . GLU   B 28  ? 0.2089 0.1849 0.2288 -0.0119 0.0077  0.0064  34  GLU   C C   
1303 O  O   . GLU   B 28  ? 0.2160 0.1884 0.2326 -0.0142 0.0078  0.0090  34  GLU   C O   
1304 C  CB  . GLU   B 28  ? 0.2169 0.1957 0.2463 -0.0115 0.0085  0.0014  34  GLU   C CB  
1305 C  CG  . GLU   B 28  ? 0.2234 0.1985 0.2535 -0.0138 0.0091  0.0023  34  GLU   C CG  
1306 C  CD  . GLU   B 28  ? 0.2670 0.2371 0.2943 -0.0131 0.0073  0.0050  34  GLU   C CD  
1307 O  OE1 . GLU   B 28  ? 0.2857 0.2519 0.3113 -0.0157 0.0080  0.0069  34  GLU   C OE1 
1308 O  OE2 . GLU   B 28  ? 0.2384 0.2082 0.2654 -0.0100 0.0052  0.0052  34  GLU   C OE2 
1309 N  N   . ASP   B 29  ? 0.1953 0.1725 0.2156 -0.0088 0.0057  0.0064  35  ASP   C N   
1310 C  CA  . ASP   B 29  ? 0.1952 0.1703 0.2137 -0.0076 0.0035  0.0092  35  ASP   C CA  
1311 C  C   . ASP   B 29  ? 0.1820 0.1580 0.2040 -0.0040 0.0021  0.0078  35  ASP   C C   
1312 O  O   . ASP   B 29  ? 0.1785 0.1576 0.2007 -0.0027 0.0022  0.0064  35  ASP   C O   
1313 C  CB  . ASP   B 29  ? 0.2180 0.1944 0.2320 -0.0088 0.0032  0.0110  35  ASP   C CB  
1314 C  CG  . ASP   B 29  ? 0.2903 0.2650 0.3028 -0.0081 0.0002  0.0143  35  ASP   C CG  
1315 O  OD1 . ASP   B 29  ? 0.3131 0.2869 0.3296 -0.0053 -0.0015 0.0147  35  ASP   C OD1 
1316 O  OD2 . ASP   B 29  ? 0.3046 0.2788 0.3121 -0.0103 -0.0005 0.0165  35  ASP   C OD2 
1317 N  N   . SER   B 30  ? 0.1682 0.1408 0.1926 -0.0028 0.0012  0.0080  36  SER   C N   
1318 C  CA  A SER   B 30  ? 0.1764 0.1490 0.2037 0.0002  0.0006  0.0062  36  SER   C CA  
1319 C  CA  B SER   B 30  ? 0.1777 0.1504 0.2049 0.0002  0.0007  0.0061  36  SER   C CA  
1320 C  C   . SER   B 30  ? 0.1869 0.1618 0.2148 0.0021  -0.0003 0.0074  36  SER   C C   
1321 O  O   . SER   B 30  ? 0.2054 0.1824 0.2347 0.0040  0.0003  0.0054  36  SER   C O   
1322 C  CB  A SER   B 30  ? 0.1952 0.1630 0.2249 0.0011  0.0000  0.0064  36  SER   C CB  
1323 C  CB  B SER   B 30  ? 0.2035 0.1716 0.2332 0.0010  0.0003  0.0058  36  SER   C CB  
1324 O  OG  A SER   B 30  ? 0.2229 0.1885 0.2527 -0.0008 0.0008  0.0051  36  SER   C OG  
1325 O  OG  B SER   B 30  ? 0.2336 0.1986 0.2636 0.0009  -0.0012 0.0093  36  SER   C OG  
1326 N  N   . SER   B 31  ? 0.1839 0.1583 0.2106 0.0014  -0.0019 0.0108  37  SER   C N   
1327 C  CA  . SER   B 31  ? 0.1868 0.1639 0.2154 0.0030  -0.0033 0.0120  37  SER   C CA  
1328 C  C   . SER   B 31  ? 0.1786 0.1604 0.2053 0.0026  -0.0023 0.0106  37  SER   C C   
1329 O  O   . SER   B 31  ? 0.1749 0.1595 0.2042 0.0041  -0.0027 0.0104  37  SER   C O   
1330 C  CB  . SER   B 31  ? 0.2221 0.1974 0.2496 0.0021  -0.0062 0.0162  37  SER   C CB  
1331 O  OG  . SER   B 31  ? 0.2829 0.2589 0.3043 -0.0012 -0.0063 0.0177  37  SER   C OG  
1332 N  N   . ARG   B 32  ? 0.1655 0.1479 0.1885 0.0005  -0.0007 0.0094  38  ARG   C N   
1333 C  CA  . ARG   B 32  ? 0.1652 0.1510 0.1863 0.0000  0.0003  0.0079  38  ARG   C CA  
1334 C  C   . ARG   B 32  ? 0.1624 0.1488 0.1842 0.0010  0.0018  0.0048  38  ARG   C C   
1335 O  O   . ARG   B 32  ? 0.1642 0.1527 0.1847 0.0008  0.0024  0.0037  38  ARG   C O   
1336 C  CB  . ARG   B 32  ? 0.1796 0.1655 0.1964 -0.0030 0.0010  0.0087  38  ARG   C CB  
1337 C  CG  . ARG   B 32  ? 0.1797 0.1646 0.1935 -0.0047 -0.0009 0.0119  38  ARG   C CG  
1338 C  CD  . ARG   B 32  ? 0.1864 0.1705 0.1944 -0.0082 0.0005  0.0122  38  ARG   C CD  
1339 N  NE  . ARG   B 32  ? 0.1742 0.1611 0.1810 -0.0086 0.0020  0.0101  38  ARG   C NE  
1340 C  CZ  . ARG   B 32  ? 0.2013 0.1881 0.2030 -0.0114 0.0028  0.0102  38  ARG   C CZ  
1341 N  NH1 . ARG   B 32  ? 0.2073 0.1913 0.2036 -0.0143 0.0022  0.0124  38  ARG   C NH1 
1342 N  NH2 . ARG   B 32  ? 0.1985 0.1873 0.1998 -0.0114 0.0040  0.0081  38  ARG   C NH2 
1343 N  N   . ASP   B 33  ? 0.1628 0.1469 0.1862 0.0017  0.0020  0.0035  39  ASP   C N   
1344 C  CA  . ASP   B 33  ? 0.1556 0.1395 0.1790 0.0020  0.0025  0.0008  39  ASP   C CA  
1345 C  C   . ASP   B 33  ? 0.1564 0.1418 0.1788 0.0005  0.0030  0.0002  39  ASP   C C   
1346 O  O   . ASP   B 33  ? 0.1536 0.1397 0.1755 0.0009  0.0029  -0.0014 39  ASP   C O   
1347 C  CB  . ASP   B 33  ? 0.1554 0.1401 0.1779 0.0036  0.0029  -0.0007 39  ASP   C CB  
1348 C  CG  . ASP   B 33  ? 0.1837 0.1671 0.2046 0.0036  0.0027  -0.0031 39  ASP   C CG  
1349 O  OD1 . ASP   B 33  ? 0.1874 0.1686 0.2092 0.0033  0.0021  -0.0041 39  ASP   C OD1 
1350 O  OD2 . ASP   B 33  ? 0.1886 0.1727 0.2070 0.0037  0.0029  -0.0038 39  ASP   C OD2 
1351 N  N   . LEU   B 34  ? 0.1531 0.1384 0.1753 -0.0015 0.0037  0.0013  40  LEU   C N   
1352 C  CA  . LEU   B 34  ? 0.1551 0.1420 0.1779 -0.0030 0.0049  0.0002  40  LEU   C CA  
1353 C  C   . LEU   B 34  ? 0.1606 0.1466 0.1860 -0.0046 0.0057  -0.0004 40  LEU   C C   
1354 O  O   . LEU   B 34  ? 0.1685 0.1523 0.1933 -0.0057 0.0059  0.0010  40  LEU   C O   
1355 C  CB  . LEU   B 34  ? 0.1576 0.1456 0.1774 -0.0046 0.0061  0.0013  40  LEU   C CB  
1356 C  CG  . LEU   B 34  ? 0.1674 0.1568 0.1850 -0.0037 0.0056  0.0015  40  LEU   C CG  
1357 C  CD1 . LEU   B 34  ? 0.1744 0.1642 0.1885 -0.0061 0.0069  0.0022  40  LEU   C CD1 
1358 C  CD2 . LEU   B 34  ? 0.1829 0.1732 0.2018 -0.0024 0.0055  -0.0006 40  LEU   C CD2 
1359 N  N   . LEU   B 35  ? 0.1488 0.1367 0.1775 -0.0049 0.0063  -0.0024 41  LEU   C N   
1360 C  CA  . LEU   B 35  ? 0.1549 0.1431 0.1875 -0.0068 0.0076  -0.0034 41  LEU   C CA  
1361 C  C   . LEU   B 35  ? 0.1568 0.1481 0.1927 -0.0074 0.0094  -0.0052 41  LEU   C C   
1362 O  O   . LEU   B 35  ? 0.1591 0.1516 0.1958 -0.0057 0.0083  -0.0061 41  LEU   C O   
1363 C  CB  . LEU   B 35  ? 0.1561 0.1435 0.1923 -0.0062 0.0056  -0.0047 41  LEU   C CB  
1364 C  CG  . LEU   B 35  ? 0.1595 0.1478 0.2012 -0.0085 0.0068  -0.0059 41  LEU   C CG  
1365 C  CD1 . LEU   B 35  ? 0.1652 0.1508 0.2080 -0.0087 0.0050  -0.0061 41  LEU   C CD1 
1366 C  CD2 . LEU   B 35  ? 0.1672 0.1594 0.2156 -0.0082 0.0065  -0.0083 41  LEU   C CD2 
1367 N  N   . VAL   B 36  ? 0.1453 0.1373 0.1829 -0.0101 0.0125  -0.0056 42  VAL   C N   
1368 C  CA  . VAL   B 36  ? 0.1495 0.1443 0.1914 -0.0108 0.0152  -0.0079 42  VAL   C CA  
1369 C  C   . VAL   B 36  ? 0.1598 0.1566 0.2093 -0.0124 0.0167  -0.0096 42  VAL   C C   
1370 O  O   . VAL   B 36  ? 0.1611 0.1562 0.2094 -0.0149 0.0181  -0.0087 42  VAL   C O   
1371 C  CB  . VAL   B 36  ? 0.1575 0.1515 0.1938 -0.0132 0.0188  -0.0074 42  VAL   C CB  
1372 C  CG1 . VAL   B 36  ? 0.1735 0.1702 0.2149 -0.0141 0.0226  -0.0104 42  VAL   C CG1 
1373 C  CG2 . VAL   B 36  ? 0.1529 0.1455 0.1825 -0.0118 0.0170  -0.0057 42  VAL   C CG2 
1374 N  N   . SER   B 37  ? 0.1590 0.1591 0.2167 -0.0110 0.0159  -0.0120 43  SER   C N   
1375 C  CA  . SER   B 37  ? 0.1604 0.1636 0.2279 -0.0124 0.0171  -0.0141 43  SER   C CA  
1376 C  C   . SER   B 37  ? 0.1801 0.1870 0.2546 -0.0127 0.0209  -0.0168 43  SER   C C   
1377 O  O   . SER   B 37  ? 0.1826 0.1893 0.2550 -0.0111 0.0213  -0.0172 43  SER   C O   
1378 C  CB  . SER   B 37  ? 0.1625 0.1666 0.2352 -0.0103 0.0120  -0.0146 43  SER   C CB  
1379 O  OG  . SER   B 37  ? 0.1893 0.1943 0.2637 -0.0072 0.0087  -0.0151 43  SER   C OG  
1380 N  N   . SER   B 38  ? 0.1834 0.1936 0.2670 -0.0148 0.0238  -0.0190 44  SER   C N   
1381 C  CA  . SER   B 38  ? 0.2065 0.2206 0.2986 -0.0151 0.0282  -0.0222 44  SER   C CA  
1382 C  C   . SER   B 38  ? 0.2386 0.2568 0.3432 -0.0117 0.0243  -0.0241 44  SER   C C   
1383 O  O   . SER   B 38  ? 0.2481 0.2671 0.3568 -0.0107 0.0192  -0.0235 44  SER   C O   
1384 C  CB  . SER   B 38  ? 0.2280 0.2438 0.3240 -0.0195 0.0343  -0.0239 44  SER   C CB  
1385 O  OG  . SER   B 38  ? 0.2680 0.2859 0.3713 -0.0203 0.0320  -0.0240 44  SER   C OG  
1386 N  N   . THR   B 39  ? 0.2472 0.2675 0.3579 -0.0102 0.0265  -0.0264 45  THR   C N   
1387 C  CA  . THR   B 39  ? 0.2709 0.2947 0.3942 -0.0067 0.0223  -0.0279 45  THR   C CA  
1388 C  C   . THR   B 39  ? 0.2973 0.3264 0.4350 -0.0072 0.0277  -0.0320 45  THR   C C   
1389 O  O   . THR   B 39  ? 0.3058 0.3346 0.4407 -0.0100 0.0350  -0.0338 45  THR   C O   
1390 C  CB  . THR   B 39  ? 0.2919 0.3125 0.4100 -0.0033 0.0192  -0.0268 45  THR   C CB  
1391 O  OG1 . THR   B 39  ? 0.3250 0.3448 0.4405 -0.0041 0.0252  -0.0285 45  THR   C OG1 
1392 C  CG2 . THR   B 39  ? 0.3007 0.3163 0.4048 -0.0027 0.0149  -0.0232 45  THR   C CG2 
1393 N  N   . THR   B 40  ? 0.3090 0.3427 0.4619 -0.0047 0.0241  -0.0336 46  THR   C N   
1394 C  CA  . THR   B 40  ? 0.3280 0.3673 0.4971 -0.0046 0.0290  -0.0379 46  THR   C CA  
1395 C  C   . THR   B 40  ? 0.3430 0.3809 0.5140 -0.0012 0.0297  -0.0392 46  THR   C C   
1396 O  O   . THR   B 40  ? 0.3570 0.3971 0.5354 -0.0018 0.0367  -0.0430 46  THR   C O   
1397 C  CB  . THR   B 40  ? 0.3496 0.3953 0.5364 -0.0034 0.0245  -0.0391 46  THR   C CB  
1398 O  OG1 . THR   B 40  ? 0.3815 0.4251 0.5673 0.0002  0.0148  -0.0364 46  THR   C OG1 
1399 C  CG2 . THR   B 40  ? 0.3579 0.4058 0.5456 -0.0075 0.0259  -0.0391 46  THR   C CG2 
1400 N  N   . ALA   B 41  ? 0.3331 0.3668 0.4975 0.0021  0.0228  -0.0362 47  ALA   C N   
1401 C  CA  . ALA   B 41  ? 0.3332 0.3645 0.4987 0.0052  0.0228  -0.0370 47  ALA   C CA  
1402 C  C   . ALA   B 41  ? 0.3349 0.3606 0.4842 0.0034  0.0273  -0.0364 47  ALA   C C   
1403 O  O   . ALA   B 41  ? 0.3446 0.3673 0.4798 0.0011  0.0270  -0.0337 47  ALA   C O   
1404 C  CB  . ALA   B 41  ? 0.3406 0.3697 0.5070 0.0092  0.0132  -0.0341 47  ALA   C CB  
1405 N  N   . GLN   B 42  ? 0.3199 0.3443 0.4716 0.0046  0.0312  -0.0389 48  GLN   C N   
1406 C  CA  . GLN   B 42  ? 0.3191 0.3384 0.4564 0.0027  0.0354  -0.0387 48  GLN   C CA  
1407 C  C   . GLN   B 42  ? 0.3063 0.3202 0.4327 0.0048  0.0292  -0.0349 48  GLN   C C   
1408 O  O   . GLN   B 42  ? 0.3178 0.3307 0.4502 0.0085  0.0241  -0.0342 48  GLN   C O   
1409 C  CB  . GLN   B 42  ? 0.3487 0.3681 0.4932 0.0030  0.0423  -0.0435 48  GLN   C CB  
1410 C  CG  . GLN   B 42  ? 0.4272 0.4409 0.5571 0.0008  0.0465  -0.0439 48  GLN   C CG  
1411 C  CD  . GLN   B 42  ? 0.5203 0.5335 0.6395 -0.0046 0.0531  -0.0446 48  GLN   C CD  
1412 O  OE1 . GLN   B 42  ? 0.5548 0.5718 0.6784 -0.0071 0.0562  -0.0456 48  GLN   C OE1 
1413 N  NE2 . GLN   B 42  ? 0.5338 0.5419 0.6385 -0.0070 0.0553  -0.0442 48  GLN   C NE2 
1414 N  N   . GLY   B 43  ? 0.2788 0.2892 0.3895 0.0024  0.0295  -0.0325 49  GLY   C N   
1415 C  CA  . GLY   B 43  ? 0.2690 0.2747 0.3691 0.0037  0.0246  -0.0291 49  GLY   C CA  
1416 C  C   . GLY   B 43  ? 0.2549 0.2568 0.3491 0.0032  0.0281  -0.0305 49  GLY   C C   
1417 O  O   . GLY   B 43  ? 0.2674 0.2692 0.3586 0.0003  0.0346  -0.0330 49  GLY   C O   
1418 N  N   . CYS   B 44  ? 0.2303 0.2285 0.3217 0.0056  0.0239  -0.0287 50  CYS   C N   
1419 C  CA  . CYS   B 44  ? 0.2349 0.2289 0.3216 0.0053  0.0266  -0.0301 50  CYS   C CA  
1420 C  C   . CYS   B 44  ? 0.2244 0.2144 0.2970 0.0040  0.0244  -0.0270 50  CYS   C C   
1421 O  O   . CYS   B 44  ? 0.2353 0.2214 0.3046 0.0041  0.0251  -0.0276 50  CYS   C O   
1422 C  CB  . CYS   B 44  ? 0.2591 0.2516 0.3566 0.0090  0.0247  -0.0315 50  CYS   C CB  
1423 S  SG  . CYS   B 44  ? 0.3004 0.2984 0.4174 0.0108  0.0280  -0.0359 50  CYS   C SG  
1424 N  N   . ASP   B 45  ? 0.1976 0.1884 0.2626 0.0028  0.0218  -0.0239 51  ASP   C N   
1425 C  CA  . ASP   B 45  ? 0.1989 0.1867 0.2519 0.0014  0.0202  -0.0213 51  ASP   C CA  
1426 C  C   . ASP   B 45  ? 0.2266 0.2136 0.2722 -0.0022 0.0251  -0.0227 51  ASP   C C   
1427 O  O   . ASP   B 45  ? 0.2427 0.2319 0.2890 -0.0043 0.0289  -0.0242 51  ASP   C O   
1428 C  CB  . ASP   B 45  ? 0.1942 0.1832 0.2423 0.0013  0.0164  -0.0179 51  ASP   C CB  
1429 C  CG  . ASP   B 45  ? 0.2615 0.2497 0.3127 0.0041  0.0109  -0.0160 51  ASP   C CG  
1430 O  OD1 . ASP   B 45  ? 0.2495 0.2350 0.3039 0.0061  0.0090  -0.0162 51  ASP   C OD1 
1431 O  OD2 . ASP   B 45  ? 0.2569 0.2464 0.3069 0.0042  0.0084  -0.0144 51  ASP   C OD2 
1432 N  N   . THR   B 46  ? 0.2235 0.2073 0.2617 -0.0033 0.0251  -0.0222 52  THR   C N   
1433 C  CA  . THR   B 46  ? 0.2331 0.2158 0.2631 -0.0071 0.0288  -0.0232 52  THR   C CA  
1434 C  C   . THR   B 46  ? 0.2141 0.1975 0.2357 -0.0086 0.0260  -0.0196 52  THR   C C   
1435 O  O   . THR   B 46  ? 0.2214 0.2042 0.2415 -0.0072 0.0222  -0.0173 52  THR   C O   
1436 C  CB  . THR   B 46  ? 0.2827 0.2612 0.3097 -0.0077 0.0301  -0.0249 52  THR   C CB  
1437 O  OG1 . THR   B 46  ? 0.3208 0.2984 0.3561 -0.0065 0.0338  -0.0289 52  THR   C OG1 
1438 C  CG2 . THR   B 46  ? 0.3035 0.2803 0.3198 -0.0121 0.0323  -0.0253 52  THR   C CG2 
1439 N  N   . ILE   B 47  ? 0.2017 0.1861 0.2178 -0.0117 0.0278  -0.0192 53  ILE   C N   
1440 C  CA  . ILE   B 47  ? 0.1965 0.1816 0.2060 -0.0129 0.0247  -0.0158 53  ILE   C CA  
1441 C  C   . ILE   B 47  ? 0.1968 0.1797 0.1981 -0.0158 0.0249  -0.0156 53  ILE   C C   
1442 O  O   . ILE   B 47  ? 0.2058 0.1868 0.2032 -0.0187 0.0285  -0.0180 53  ILE   C O   
1443 C  CB  . ILE   B 47  ? 0.2166 0.2033 0.2245 -0.0146 0.0255  -0.0146 53  ILE   C CB  
1444 C  CG1 . ILE   B 47  ? 0.2340 0.2229 0.2503 -0.0125 0.0258  -0.0152 53  ILE   C CG1 
1445 C  CG2 . ILE   B 47  ? 0.2193 0.2066 0.2219 -0.0151 0.0218  -0.0108 53  ILE   C CG2 
1446 C  CD1 . ILE   B 47  ? 0.2561 0.2461 0.2767 -0.0089 0.0213  -0.0133 53  ILE   C CD1 
1447 N  N   . ALA   B 48  ? 0.1835 0.1668 0.1822 -0.0153 0.0214  -0.0132 54  ALA   C N   
1448 C  CA  . ALA   B 48  ? 0.1858 0.1678 0.1776 -0.0182 0.0209  -0.0128 54  ALA   C CA  
1449 C  C   . ALA   B 48  ? 0.1757 0.1581 0.1611 -0.0215 0.0207  -0.0114 54  ALA   C C   
1450 O  O   . ALA   B 48  ? 0.1795 0.1638 0.1661 -0.0207 0.0191  -0.0092 54  ALA   C O   
1451 C  CB  . ALA   B 48  ? 0.1805 0.1636 0.1725 -0.0170 0.0173  -0.0104 54  ALA   C CB  
1452 N  N   . ARG   B 49  ? 0.1775 0.1576 0.1558 -0.0253 0.0218  -0.0126 55  ARG   C N   
1453 C  CA  . ARG   B 49  ? 0.1782 0.1577 0.1485 -0.0291 0.0209  -0.0109 55  ARG   C CA  
1454 C  C   . ARG   B 49  ? 0.1885 0.1677 0.1540 -0.0314 0.0179  -0.0100 55  ARG   C C   
1455 O  O   . ARG   B 49  ? 0.2007 0.1768 0.1610 -0.0344 0.0198  -0.0125 55  ARG   C O   
1456 C  CB  . ARG   B 49  ? 0.1902 0.1666 0.1555 -0.0324 0.0258  -0.0138 55  ARG   C CB  
1457 C  CG  . ARG   B 49  ? 0.1991 0.1766 0.1710 -0.0303 0.0292  -0.0152 55  ARG   C CG  
1458 C  CD  . ARG   B 49  ? 0.1837 0.1635 0.1579 -0.0289 0.0266  -0.0117 55  ARG   C CD  
1459 N  NE  . ARG   B 49  ? 0.1964 0.1771 0.1770 -0.0276 0.0302  -0.0136 55  ARG   C NE  
1460 C  CZ  . ARG   B 49  ? 0.2252 0.2080 0.2108 -0.0255 0.0287  -0.0117 55  ARG   C CZ  
1461 N  NH1 . ARG   B 49  ? 0.2114 0.1952 0.1962 -0.0244 0.0240  -0.0080 55  ARG   C NH1 
1462 N  NH2 . ARG   B 49  ? 0.2326 0.2165 0.2246 -0.0247 0.0319  -0.0137 55  ARG   C NH2 
1463 N  N   . CYS   B 50  ? 0.1865 0.1689 0.1549 -0.0298 0.0135  -0.0067 56  CYS   C N   
1464 C  CA  . CYS   B 50  ? 0.1879 0.1713 0.1549 -0.0312 0.0106  -0.0060 56  CYS   C CA  
1465 C  C   . CYS   B 50  ? 0.2082 0.1958 0.1790 -0.0297 0.0059  -0.0022 56  CYS   C C   
1466 O  O   . CYS   B 50  ? 0.2060 0.1952 0.1805 -0.0272 0.0052  -0.0004 56  CYS   C O   
1467 C  CB  . CYS   B 50  ? 0.1920 0.1746 0.1632 -0.0293 0.0122  -0.0081 56  CYS   C CB  
1468 S  SG  . CYS   B 50  ? 0.1843 0.1697 0.1646 -0.0240 0.0115  -0.0066 56  CYS   C SG  
1469 N  N   . ASP   B 51  ? 0.2033 0.1929 0.1745 -0.0310 0.0031  -0.0014 57  ASP   C N   
1470 C  CA  . ASP   B 51  ? 0.2097 0.2039 0.1868 -0.0294 -0.0007 0.0016  57  ASP   C CA  
1471 C  C   . ASP   B 51  ? 0.2036 0.1999 0.1862 -0.0279 0.0000  0.0007  57  ASP   C C   
1472 O  O   . ASP   B 51  ? 0.1963 0.1963 0.1827 -0.0282 -0.0027 0.0021  57  ASP   C O   
1473 C  CB  . ASP   B 51  ? 0.2443 0.2399 0.2181 -0.0325 -0.0053 0.0039  57  ASP   C CB  
1474 C  CG  . ASP   B 51  ? 0.2920 0.2868 0.2613 -0.0366 -0.0064 0.0027  57  ASP   C CG  
1475 O  OD1 . ASP   B 51  ? 0.2844 0.2769 0.2527 -0.0371 -0.0031 -0.0003 57  ASP   C OD1 
1476 O  OD2 . ASP   B 51  ? 0.3329 0.3290 0.2998 -0.0394 -0.0109 0.0047  57  ASP   C OD2 
1477 N  N   . CYS   B 52  ? 0.1893 0.1829 0.1726 -0.0263 0.0034  -0.0015 58  CYS   C N   
1478 C  CA  . CYS   B 52  ? 0.1784 0.1727 0.1656 -0.0250 0.0042  -0.0020 58  CYS   C CA  
1479 C  C   . CYS   B 52  ? 0.1620 0.1605 0.1553 -0.0224 0.0029  0.0000  58  CYS   C C   
1480 O  O   . CYS   B 52  ? 0.1551 0.1547 0.1505 -0.0202 0.0024  0.0011  58  CYS   C O   
1481 C  CB  . CYS   B 52  ? 0.1978 0.1880 0.1848 -0.0232 0.0073  -0.0040 58  CYS   C CB  
1482 S  SG  . CYS   B 52  ? 0.2235 0.2083 0.2053 -0.0260 0.0096  -0.0071 58  CYS   C SG  
1483 N  N   . GLN   B 53  ? 0.1435 0.1441 0.1398 -0.0230 0.0028  0.0000  59  GLN   C N   
1484 C  CA  . GLN   B 53  ? 0.1481 0.1523 0.1504 -0.0208 0.0028  0.0011  59  GLN   C CA  
1485 C  C   . GLN   B 53  ? 0.1608 0.1628 0.1630 -0.0204 0.0054  0.0000  59  GLN   C C   
1486 O  O   . GLN   B 53  ? 0.1599 0.1647 0.1661 -0.0199 0.0061  0.0005  59  GLN   C O   
1487 C  CB  . GLN   B 53  ? 0.1549 0.1648 0.1622 -0.0221 0.0002  0.0025  59  GLN   C CB  
1488 C  CG  . GLN   B 53  ? 0.1584 0.1703 0.1669 -0.0214 -0.0029 0.0044  59  GLN   C CG  
1489 C  CD  . GLN   B 53  ? 0.1979 0.2157 0.2132 -0.0222 -0.0061 0.0059  59  GLN   C CD  
1490 O  OE1 . GLN   B 53  ? 0.2136 0.2325 0.2274 -0.0249 -0.0096 0.0069  59  GLN   C OE1 
1491 N  NE2 . GLN   B 53  ? 0.1863 0.2079 0.2094 -0.0199 -0.0049 0.0059  59  GLN   C NE2 
1492 N  N   . THR   B 54  ? 0.1753 0.1720 0.1730 -0.0208 0.0069  -0.0013 60  THR   C N   
1493 C  CA  . THR   B 54  ? 0.1991 0.1924 0.1958 -0.0204 0.0088  -0.0017 60  THR   C CA  
1494 C  C   . THR   B 54  ? 0.1984 0.1867 0.1926 -0.0183 0.0094  -0.0025 60  THR   C C   
1495 O  O   . THR   B 54  ? 0.2048 0.1916 0.1976 -0.0184 0.0094  -0.0035 60  THR   C O   
1496 C  CB  . THR   B 54  ? 0.2598 0.2514 0.2547 -0.0238 0.0094  -0.0024 60  THR   C CB  
1497 O  OG1 . THR   B 54  ? 0.3022 0.2896 0.2932 -0.0252 0.0094  -0.0038 60  THR   C OG1 
1498 C  CG2 . THR   B 54  ? 0.2690 0.2663 0.2675 -0.0264 0.0083  -0.0018 60  THR   C CG2 
1499 N  N   . GLY   B 55  ? 0.1769 0.1629 0.1709 -0.0163 0.0100  -0.0021 61  GLY   C N   
1500 C  CA  . GLY   B 55  ? 0.1684 0.1503 0.1615 -0.0140 0.0098  -0.0026 61  GLY   C CA  
1501 C  C   . GLY   B 55  ? 0.1608 0.1394 0.1523 -0.0127 0.0097  -0.0018 61  GLY   C C   
1502 O  O   . GLY   B 55  ? 0.1832 0.1616 0.1731 -0.0142 0.0104  -0.0011 61  GLY   C O   
1503 N  N   . VAL   B 56  ? 0.1507 0.1265 0.1426 -0.0104 0.0086  -0.0019 62  VAL   C N   
1504 C  CA  . VAL   B 56  ? 0.1579 0.1297 0.1472 -0.0093 0.0076  -0.0008 62  VAL   C CA  
1505 C  C   . VAL   B 56  ? 0.1576 0.1308 0.1489 -0.0068 0.0063  -0.0008 62  VAL   C C   
1506 O  O   . VAL   B 56  ? 0.1606 0.1350 0.1555 -0.0055 0.0058  -0.0017 62  VAL   C O   
1507 C  CB  . VAL   B 56  ? 0.1719 0.1373 0.1598 -0.0090 0.0066  -0.0008 62  VAL   C CB  
1508 C  CG1 . VAL   B 56  ? 0.1844 0.1449 0.1687 -0.0080 0.0045  0.0008  62  VAL   C CG1 
1509 C  CG2 . VAL   B 56  ? 0.1777 0.1410 0.1634 -0.0117 0.0080  -0.0010 62  VAL   C CG2 
1510 N  N   . TYR   B 57  ? 0.1580 0.1307 0.1468 -0.0065 0.0060  -0.0001 63  TYR   C N   
1511 C  CA  . TYR   B 57  ? 0.1669 0.1403 0.1573 -0.0045 0.0045  -0.0003 63  TYR   C CA  
1512 C  C   . TYR   B 57  ? 0.1705 0.1386 0.1567 -0.0039 0.0022  0.0006  63  TYR   C C   
1513 O  O   . TYR   B 57  ? 0.1726 0.1368 0.1533 -0.0055 0.0024  0.0015  63  TYR   C O   
1514 C  CB  . TYR   B 57  ? 0.1723 0.1502 0.1642 -0.0043 0.0057  -0.0006 63  TYR   C CB  
1515 C  CG  . TYR   B 57  ? 0.1751 0.1520 0.1631 -0.0054 0.0071  -0.0004 63  TYR   C CG  
1516 C  CD1 . TYR   B 57  ? 0.1987 0.1766 0.1854 -0.0074 0.0094  -0.0003 63  TYR   C CD1 
1517 C  CD2 . TYR   B 57  ? 0.1842 0.1593 0.1697 -0.0046 0.0065  -0.0008 63  TYR   C CD2 
1518 C  CE1 . TYR   B 57  ? 0.2074 0.1848 0.1911 -0.0086 0.0116  -0.0005 63  TYR   C CE1 
1519 C  CE2 . TYR   B 57  ? 0.1906 0.1644 0.1717 -0.0059 0.0085  -0.0011 63  TYR   C CE2 
1520 C  CZ  . TYR   B 57  ? 0.2110 0.1861 0.1914 -0.0079 0.0114  -0.0010 63  TYR   C CZ  
1521 O  OH  . TYR   B 57  ? 0.2350 0.2092 0.2118 -0.0094 0.0143  -0.0018 63  TYR   C OH  
1522 N  N   . TYR   B 58  ? 0.1694 0.1373 0.1579 -0.0021 -0.0003 0.0003  64  TYR   C N   
1523 C  CA  . TYR   B 58  ? 0.1710 0.1338 0.1552 -0.0017 -0.0033 0.0013  64  TYR   C CA  
1524 C  C   . TYR   B 58  ? 0.1790 0.1422 0.1591 -0.0023 -0.0028 0.0010  64  TYR   C C   
1525 O  O   . TYR   B 58  ? 0.1842 0.1513 0.1682 -0.0015 -0.0021 -0.0002 64  TYR   C O   
1526 C  CB  . TYR   B 58  ? 0.1767 0.1390 0.1662 0.0004  -0.0068 0.0011  64  TYR   C CB  
1527 C  CG  . TYR   B 58  ? 0.1965 0.1535 0.1814 0.0006  -0.0111 0.0025  64  TYR   C CG  
1528 C  CD1 . TYR   B 58  ? 0.2214 0.1719 0.2003 -0.0003 -0.0130 0.0044  64  TYR   C CD1 
1529 C  CD2 . TYR   B 58  ? 0.2240 0.1816 0.2094 0.0013  -0.0135 0.0020  64  TYR   C CD2 
1530 C  CE1 . TYR   B 58  ? 0.2447 0.1895 0.2179 -0.0005 -0.0175 0.0061  64  TYR   C CE1 
1531 C  CE2 . TYR   B 58  ? 0.2381 0.1904 0.2183 0.0010  -0.0181 0.0033  64  TYR   C CE2 
1532 C  CZ  . TYR   B 58  ? 0.2644 0.2102 0.2380 0.0001  -0.0202 0.0055  64  TYR   C CZ  
1533 O  OH  . TYR   B 58  ? 0.3085 0.2483 0.2756 -0.0005 -0.0253 0.0072  64  TYR   C OH  
1534 N  N   . CYS   B 59  ? 0.1848 0.1431 0.1567 -0.0041 -0.0030 0.0019  65  CYS   C N   
1535 C  CA  . CYS   B 59  ? 0.1955 0.1528 0.1620 -0.0051 -0.0018 0.0012  65  CYS   C CA  
1536 C  C   . CYS   B 59  ? 0.2180 0.1692 0.1782 -0.0053 -0.0063 0.0021  65  CYS   C C   
1537 O  O   . CYS   B 59  ? 0.2356 0.1805 0.1880 -0.0070 -0.0079 0.0038  65  CYS   C O   
1538 C  CB  . CYS   B 59  ? 0.2089 0.1656 0.1703 -0.0077 0.0024  0.0011  65  CYS   C CB  
1539 S  SG  . CYS   B 59  ? 0.2329 0.1871 0.1864 -0.0095 0.0048  -0.0004 65  CYS   C SG  
1540 N  N   . SER   B 60  ? 0.2142 0.1667 0.1776 -0.0039 -0.0088 0.0012  66  SER   C N   
1541 C  CA  . SER   B 60  ? 0.2395 0.1867 0.1978 -0.0042 -0.0140 0.0021  66  SER   C CA  
1542 C  C   . SER   B 60  ? 0.2452 0.1864 0.1910 -0.0070 -0.0135 0.0022  66  SER   C C   
1543 O  O   . SER   B 60  ? 0.2610 0.1956 0.1992 -0.0082 -0.0179 0.0041  66  SER   C O   
1544 C  CB  . SER   B 60  ? 0.2955 0.2457 0.2605 -0.0024 -0.0168 0.0009  66  SER   C CB  
1545 O  OG  . SER   B 60  ? 0.3649 0.3179 0.3300 -0.0028 -0.0134 -0.0012 66  SER   C OG  
1546 N  N   . SER   B 61  ? 0.2382 0.1812 0.1814 -0.0084 -0.0081 0.0004  67  SER   C N   
1547 C  CA  . SER   B 61  ? 0.2537 0.1908 0.1844 -0.0116 -0.0064 -0.0002 67  SER   C CA  
1548 C  C   . SER   B 61  ? 0.2698 0.2014 0.1914 -0.0143 -0.0052 0.0018  67  SER   C C   
1549 O  O   . SER   B 61  ? 0.2865 0.2120 0.1961 -0.0176 -0.0037 0.0016  67  SER   C O   
1550 C  CB  . SER   B 61  ? 0.2574 0.1983 0.1897 -0.0119 -0.0005 -0.0032 67  SER   C CB  
1551 O  OG  . SER   B 61  ? 0.2695 0.2156 0.2079 -0.0115 0.0042  -0.0035 67  SER   C OG  
1552 N  N   . ARG   B 62  ? 0.2518 0.1848 0.1785 -0.0134 -0.0056 0.0036  68  ARG   C N   
1553 C  CA  . ARG   B 62  ? 0.2529 0.1801 0.1719 -0.0159 -0.0052 0.0058  68  ARG   C CA  
1554 C  C   . ARG   B 62  ? 0.2569 0.1805 0.1782 -0.0142 -0.0113 0.0087  68  ARG   C C   
1555 O  O   . ARG   B 62  ? 0.2653 0.1833 0.1810 -0.0159 -0.0119 0.0110  68  ARG   C O   
1556 C  CB  . ARG   B 62  ? 0.2653 0.1976 0.1892 -0.0166 0.0009  0.0049  68  ARG   C CB  
1557 C  CG  . ARG   B 62  ? 0.2761 0.2114 0.1983 -0.0184 0.0072  0.0022  68  ARG   C CG  
1558 C  CD  . ARG   B 62  ? 0.3149 0.2426 0.2230 -0.0228 0.0095  0.0026  68  ARG   C CD  
1559 N  NE  . ARG   B 62  ? 0.3562 0.2869 0.2636 -0.0245 0.0163  -0.0005 68  ARG   C NE  
1560 C  CZ  . ARG   B 62  ? 0.3990 0.3290 0.3033 -0.0245 0.0174  -0.0030 68  ARG   C CZ  
1561 N  NH1 . ARG   B 62  ? 0.3951 0.3216 0.2960 -0.0234 0.0119  -0.0025 68  ARG   C NH1 
1562 N  NH2 . ARG   B 62  ? 0.3969 0.3299 0.3021 -0.0259 0.0242  -0.0062 68  ARG   C NH2 
1563 N  N   . ARG   B 63  ? 0.2586 0.1858 0.1894 -0.0108 -0.0155 0.0084  69  ARG   C N   
1564 C  CA  . ARG   B 63  ? 0.2853 0.2109 0.2220 -0.0084 -0.0207 0.0103  69  ARG   C CA  
1565 C  C   . ARG   B 63  ? 0.3031 0.2288 0.2426 -0.0086 -0.0180 0.0111  69  ARG   C C   
1566 O  O   . ARG   B 63  ? 0.3285 0.2479 0.2651 -0.0088 -0.0212 0.0136  69  ARG   C O   
1567 C  CB  . ARG   B 63  ? 0.3380 0.2548 0.2662 -0.0093 -0.0276 0.0132  69  ARG   C CB  
1568 C  CG  . ARG   B 63  ? 0.4122 0.3282 0.3367 -0.0097 -0.0311 0.0124  69  ARG   C CG  
1569 C  CD  . ARG   B 63  ? 0.4943 0.4155 0.4306 -0.0064 -0.0353 0.0114  69  ARG   C CD  
1570 N  NE  . ARG   B 63  ? 0.5570 0.4756 0.4872 -0.0077 -0.0392 0.0110  69  ARG   C NE  
1571 C  CZ  . ARG   B 63  ? 0.5818 0.5049 0.5139 -0.0078 -0.0366 0.0081  69  ARG   C CZ  
1572 N  NH1 . ARG   B 63  ? 0.5667 0.4972 0.5073 -0.0064 -0.0308 0.0057  69  ARG   C NH1 
1573 N  NH2 . ARG   B 63  ? 0.5944 0.5141 0.5200 -0.0094 -0.0405 0.0077  69  ARG   C NH2 
1574 N  N   . LYS   B 64  ? 0.2804 0.2126 0.2248 -0.0088 -0.0122 0.0090  70  LYS   C N   
1575 C  CA  . LYS   B 64  ? 0.2738 0.2061 0.2199 -0.0096 -0.0094 0.0094  70  LYS   C CA  
1576 C  C   . LYS   B 64  ? 0.2282 0.1692 0.1846 -0.0081 -0.0060 0.0071  70  LYS   C C   
1577 O  O   . LYS   B 64  ? 0.2137 0.1602 0.1736 -0.0073 -0.0044 0.0054  70  LYS   C O   
1578 C  CB  . LYS   B 64  ? 0.3241 0.2541 0.2612 -0.0135 -0.0049 0.0097  70  LYS   C CB  
1579 C  CG  . LYS   B 64  ? 0.4664 0.3865 0.3922 -0.0163 -0.0067 0.0126  70  LYS   C CG  
1580 C  CD  . LYS   B 64  ? 0.5627 0.4826 0.4823 -0.0204 -0.0007 0.0121  70  LYS   C CD  
1581 C  CE  . LYS   B 64  ? 0.6566 0.5668 0.5654 -0.0239 -0.0012 0.0150  70  LYS   C CE  
1582 N  NZ  . LYS   B 64  ? 0.7010 0.6030 0.5964 -0.0262 -0.0035 0.0166  70  LYS   C NZ  
1583 N  N   . HIS   B 65  ? 0.2220 0.1633 0.1821 -0.0081 -0.0049 0.0072  71  HIS   C N   
1584 C  CA  . HIS   B 65  ? 0.2031 0.1513 0.1705 -0.0077 -0.0016 0.0053  71  HIS   C CA  
1585 C  C   . HIS   B 65  ? 0.2265 0.1761 0.1908 -0.0108 0.0026  0.0051  71  HIS   C C   
1586 O  O   . HIS   B 65  ? 0.2482 0.1922 0.2060 -0.0131 0.0030  0.0066  71  HIS   C O   
1587 C  CB  . HIS   B 65  ? 0.2100 0.1576 0.1832 -0.0063 -0.0026 0.0049  71  HIS   C CB  
1588 C  CG  . HIS   B 65  ? 0.2124 0.1601 0.1914 -0.0032 -0.0060 0.0046  71  HIS   C CG  
1589 N  ND1 . HIS   B 65  ? 0.2474 0.2012 0.2342 -0.0016 -0.0050 0.0026  71  HIS   C ND1 
1590 C  CD2 . HIS   B 65  ? 0.2211 0.1636 0.1998 -0.0017 -0.0105 0.0060  71  HIS   C CD2 
1591 C  CE1 . HIS   B 65  ? 0.2252 0.1778 0.2167 0.0008  -0.0082 0.0025  71  HIS   C CE1 
1592 N  NE2 . HIS   B 65  ? 0.2450 0.1912 0.2324 0.0010  -0.0119 0.0046  71  HIS   C NE2 
1593 N  N   . TYR   B 66  ? 0.2033 0.1601 0.1726 -0.0108 0.0054  0.0035  72  TYR   C N   
1594 C  CA  . TYR   B 66  ? 0.1983 0.1578 0.1670 -0.0135 0.0091  0.0032  72  TYR   C CA  
1595 C  C   . TYR   B 66  ? 0.1923 0.1573 0.1677 -0.0136 0.0101  0.0021  72  TYR   C C   
1596 O  O   . TYR   B 66  ? 0.1804 0.1499 0.1609 -0.0116 0.0095  0.0012  72  TYR   C O   
1597 C  CB  . TYR   B 66  ? 0.1997 0.1628 0.1680 -0.0140 0.0117  0.0023  72  TYR   C CB  
1598 C  CG  . TYR   B 66  ? 0.2150 0.1725 0.1748 -0.0151 0.0117  0.0029  72  TYR   C CG  
1599 C  CD1 . TYR   B 66  ? 0.2403 0.1929 0.1928 -0.0185 0.0136  0.0039  72  TYR   C CD1 
1600 C  CD2 . TYR   B 66  ? 0.2210 0.1777 0.1794 -0.0134 0.0100  0.0025  72  TYR   C CD2 
1601 C  CE1 . TYR   B 66  ? 0.2644 0.2110 0.2074 -0.0201 0.0138  0.0045  72  TYR   C CE1 
1602 C  CE2 . TYR   B 66  ? 0.2499 0.2009 0.1991 -0.0150 0.0099  0.0029  72  TYR   C CE2 
1603 C  CZ  . TYR   B 66  ? 0.2844 0.2301 0.2254 -0.0184 0.0118  0.0040  72  TYR   C CZ  
1604 O  OH  . TYR   B 66  ? 0.3316 0.2708 0.2618 -0.0206 0.0119  0.0044  72  TYR   C OH  
1605 N  N   . PRO   B 67  ? 0.1930 0.1574 0.1677 -0.0161 0.0117  0.0022  73  PRO   C N   
1606 C  CA  . PRO   B 67  ? 0.1837 0.1533 0.1637 -0.0168 0.0124  0.0012  73  PRO   C CA  
1607 C  C   . PRO   B 67  ? 0.2009 0.1777 0.1850 -0.0175 0.0143  0.0006  73  PRO   C C   
1608 O  O   . PRO   B 67  ? 0.2172 0.1942 0.1996 -0.0191 0.0165  0.0007  73  PRO   C O   
1609 C  CB  . PRO   B 67  ? 0.1988 0.1642 0.1761 -0.0197 0.0131  0.0015  73  PRO   C CB  
1610 C  CG  . PRO   B 67  ? 0.2099 0.1705 0.1810 -0.0215 0.0142  0.0028  73  PRO   C CG  
1611 C  CD  . PRO   B 67  ? 0.1920 0.1505 0.1604 -0.0190 0.0127  0.0034  73  PRO   C CD  
1612 N  N   . VAL   B 68  ? 0.1840 0.1664 0.1734 -0.0164 0.0135  0.0000  74  VAL   C N   
1613 C  CA  . VAL   B 68  ? 0.1842 0.1733 0.1789 -0.0166 0.0146  -0.0003 74  VAL   C CA  
1614 C  C   . VAL   B 68  ? 0.1815 0.1754 0.1807 -0.0172 0.0132  -0.0004 74  VAL   C C   
1615 O  O   . VAL   B 68  ? 0.1911 0.1833 0.1890 -0.0169 0.0117  -0.0006 74  VAL   C O   
1616 C  CB  . VAL   B 68  ? 0.2076 0.1983 0.2040 -0.0138 0.0144  -0.0005 74  VAL   C CB  
1617 C  CG1 . VAL   B 68  ? 0.2208 0.2076 0.2125 -0.0137 0.0160  -0.0006 74  VAL   C CG1 
1618 C  CG2 . VAL   B 68  ? 0.2054 0.1950 0.2020 -0.0115 0.0120  -0.0004 74  VAL   C CG2 
1619 N  N   . SER   B 69  ? 0.1699 0.1698 0.1746 -0.0182 0.0137  -0.0004 75  SER   C N   
1620 C  CA  . SER   B 69  ? 0.1669 0.1718 0.1762 -0.0185 0.0115  -0.0001 75  SER   C CA  
1621 C  C   . SER   B 69  ? 0.1587 0.1660 0.1715 -0.0153 0.0107  0.0003  75  SER   C C   
1622 O  O   . SER   B 69  ? 0.1629 0.1704 0.1770 -0.0138 0.0125  -0.0001 75  SER   C O   
1623 C  CB  . SER   B 69  ? 0.1870 0.1976 0.2021 -0.0209 0.0118  -0.0001 75  SER   C CB  
1624 O  OG  . SER   B 69  ? 0.2644 0.2726 0.2764 -0.0242 0.0125  -0.0005 75  SER   C OG  
1625 N  N   . PHE   B 70  ? 0.1355 0.1439 0.1491 -0.0146 0.0081  0.0010  76  PHE   C N   
1626 C  CA  . PHE   B 70  ? 0.1389 0.1488 0.1555 -0.0119 0.0071  0.0017  76  PHE   C CA  
1627 C  C   . PHE   B 70  ? 0.1538 0.1676 0.1742 -0.0123 0.0040  0.0031  76  PHE   C C   
1628 O  O   . PHE   B 70  ? 0.1654 0.1796 0.1840 -0.0149 0.0023  0.0035  76  PHE   C O   
1629 C  CB  . PHE   B 70  ? 0.1424 0.1477 0.1547 -0.0101 0.0072  0.0014  76  PHE   C CB  
1630 C  CG  . PHE   B 70  ? 0.1376 0.1398 0.1452 -0.0114 0.0064  0.0012  76  PHE   C CG  
1631 C  CD1 . PHE   B 70  ? 0.1399 0.1382 0.1436 -0.0124 0.0076  0.0002  76  PHE   C CD1 
1632 C  CD2 . PHE   B 70  ? 0.1478 0.1505 0.1550 -0.0116 0.0047  0.0019  76  PHE   C CD2 
1633 C  CE1 . PHE   B 70  ? 0.1542 0.1497 0.1547 -0.0133 0.0074  -0.0005 76  PHE   C CE1 
1634 C  CE2 . PHE   B 70  ? 0.1585 0.1582 0.1613 -0.0130 0.0049  0.0011  76  PHE   C CE2 
1635 C  CZ  . PHE   B 70  ? 0.1604 0.1568 0.1605 -0.0137 0.0064  -0.0003 76  PHE   C CZ  
1636 N  N   . SER   B 71  ? 0.1337 0.1499 0.1593 -0.0100 0.0030  0.0039  77  SER   C N   
1637 C  CA  . SER   B 71  ? 0.1403 0.1600 0.1703 -0.0102 -0.0007 0.0058  77  SER   C CA  
1638 C  C   . SER   B 71  ? 0.1559 0.1724 0.1803 -0.0108 -0.0031 0.0072  77  SER   C C   
1639 O  O   . SER   B 71  ? 0.1634 0.1756 0.1817 -0.0110 -0.0015 0.0063  77  SER   C O   
1640 C  CB  . SER   B 71  ? 0.1376 0.1607 0.1763 -0.0073 -0.0007 0.0062  77  SER   C CB  
1641 O  OG  . SER   B 71  ? 0.1796 0.1992 0.2166 -0.0048 0.0002  0.0060  77  SER   C OG  
1642 N  N   . LYS   B 72  ? 0.1469 0.1654 0.1735 -0.0114 -0.0071 0.0094  78  LYS   C N   
1643 C  CA  . LYS   B 72  ? 0.1713 0.1862 0.1914 -0.0126 -0.0092 0.0109  78  LYS   C CA  
1644 C  C   . LYS   B 72  ? 0.1857 0.1986 0.2073 -0.0097 -0.0087 0.0116  78  LYS   C C   
1645 O  O   . LYS   B 72  ? 0.2108 0.2259 0.2396 -0.0070 -0.0087 0.0118  78  LYS   C O   
1646 C  CB  . LYS   B 72  ? 0.2003 0.2173 0.2213 -0.0147 -0.0142 0.0135  78  LYS   C CB  
1647 C  CG  . LYS   B 72  ? 0.2578 0.2769 0.2774 -0.0180 -0.0150 0.0127  78  LYS   C CG  
1648 C  CD  . LYS   B 72  ? 0.3595 0.3808 0.3799 -0.0203 -0.0208 0.0153  78  LYS   C CD  
1649 C  CE  . LYS   B 72  ? 0.4565 0.4758 0.4684 -0.0250 -0.0215 0.0144  78  LYS   C CE  
1650 N  NZ  . LYS   B 72  ? 0.5144 0.5274 0.5162 -0.0260 -0.0178 0.0127  78  LYS   C NZ  
1651 N  N   . PRO   B 73  ? 0.1829 0.1914 0.1980 -0.0104 -0.0080 0.0117  79  PRO   C N   
1652 C  CA  . PRO   B 73  ? 0.1891 0.1954 0.2057 -0.0080 -0.0076 0.0123  79  PRO   C CA  
1653 C  C   . PRO   B 73  ? 0.2083 0.2159 0.2302 -0.0067 -0.0113 0.0151  79  PRO   C C   
1654 O  O   . PRO   B 73  ? 0.2216 0.2294 0.2418 -0.0086 -0.0151 0.0177  79  PRO   C O   
1655 C  CB  . PRO   B 73  ? 0.2062 0.2083 0.2152 -0.0101 -0.0066 0.0123  79  PRO   C CB  
1656 C  CG  . PRO   B 73  ? 0.2201 0.2218 0.2241 -0.0127 -0.0052 0.0106  79  PRO   C CG  
1657 C  CD  . PRO   B 73  ? 0.1818 0.1871 0.1886 -0.0135 -0.0071 0.0109  79  PRO   C CD  
1658 N  N   . SER   B 74  ? 0.2019 0.2101 0.2303 -0.0034 -0.0104 0.0147  80  SER   C N   
1659 C  CA  . SER   B 74  ? 0.2142 0.2235 0.2495 -0.0015 -0.0137 0.0171  80  SER   C CA  
1660 C  C   . SER   B 74  ? 0.2025 0.2098 0.2420 0.0017  -0.0119 0.0162  80  SER   C C   
1661 O  O   . SER   B 74  ? 0.1885 0.1937 0.2251 0.0021  -0.0084 0.0138  80  SER   C O   
1662 C  CB  . SER   B 74  ? 0.2459 0.2611 0.2894 -0.0009 -0.0151 0.0170  80  SER   C CB  
1663 O  OG  . SER   B 74  ? 0.2832 0.3009 0.3319 0.0011  -0.0109 0.0139  80  SER   C OG  
1664 N  N   . LEU   B 75  ? 0.1991 0.2066 0.2456 0.0039  -0.0148 0.0183  81  LEU   C N   
1665 C  CA  . LEU   B 75  ? 0.1962 0.2014 0.2476 0.0070  -0.0134 0.0174  81  LEU   C CA  
1666 C  C   . LEU   B 75  ? 0.1986 0.2080 0.2583 0.0094  -0.0103 0.0144  81  LEU   C C   
1667 O  O   . LEU   B 75  ? 0.2096 0.2237 0.2773 0.0103  -0.0120 0.0150  81  LEU   C O   
1668 C  CB  . LEU   B 75  ? 0.2115 0.2150 0.2677 0.0084  -0.0181 0.0212  81  LEU   C CB  
1669 C  CG  . LEU   B 75  ? 0.2744 0.2716 0.3229 0.0066  -0.0203 0.0240  81  LEU   C CG  
1670 C  CD1 . LEU   B 75  ? 0.3028 0.2982 0.3555 0.0075  -0.0262 0.0286  81  LEU   C CD1 
1671 C  CD2 . LEU   B 75  ? 0.2859 0.2789 0.3333 0.0078  -0.0168 0.0220  81  LEU   C CD2 
1672 N  N   . ILE   B 76  ? 0.1891 0.1968 0.2470 0.0102  -0.0059 0.0110  82  ILE   C N   
1673 C  CA  . ILE   B 76  ? 0.2013 0.2118 0.2645 0.0117  -0.0019 0.0077  82  ILE   C CA  
1674 C  C   . ILE   B 76  ? 0.2078 0.2148 0.2729 0.0141  0.0007  0.0054  82  ILE   C C   
1675 O  O   . ILE   B 76  ? 0.2008 0.2030 0.2596 0.0135  0.0010  0.0052  82  ILE   C O   
1676 C  CB  . ILE   B 76  ? 0.2313 0.2427 0.2876 0.0094  0.0010  0.0056  82  ILE   C CB  
1677 C  CG1 . ILE   B 76  ? 0.2572 0.2724 0.3130 0.0071  -0.0013 0.0074  82  ILE   C CG1 
1678 C  CG2 . ILE   B 76  ? 0.2475 0.2600 0.3062 0.0103  0.0057  0.0020  82  ILE   C CG2 
1679 C  CD1 . ILE   B 76  ? 0.2929 0.3081 0.3421 0.0048  0.0008  0.0060  82  ILE   C CD1 
1680 N  N   . PHE   B 77  ? 0.2218 0.2309 0.2959 0.0165  0.0029  0.0034  83  PHE   C N   
1681 C  CA  . PHE   B 77  ? 0.2426 0.2479 0.3186 0.0186  0.0059  0.0006  83  PHE   C CA  
1682 C  C   . PHE   B 77  ? 0.2370 0.2396 0.3045 0.0170  0.0101  -0.0028 83  PHE   C C   
1683 O  O   . PHE   B 77  ? 0.2479 0.2531 0.3127 0.0155  0.0126  -0.0044 83  PHE   C O   
1684 C  CB  . PHE   B 77  ? 0.2670 0.2757 0.3558 0.0215  0.0079  -0.0012 83  PHE   C CB  
1685 C  CG  . PHE   B 77  ? 0.3023 0.3061 0.3944 0.0241  0.0097  -0.0033 83  PHE   C CG  
1686 C  CD1 . PHE   B 77  ? 0.3356 0.3376 0.4266 0.0244  0.0154  -0.0081 83  PHE   C CD1 
1687 C  CD2 . PHE   B 77  ? 0.3307 0.3304 0.4248 0.0256  0.0057  -0.0004 83  PHE   C CD2 
1688 C  CE1 . PHE   B 77  ? 0.3461 0.3428 0.4394 0.0264  0.0172  -0.0104 83  PHE   C CE1 
1689 C  CE2 . PHE   B 77  ? 0.3531 0.3475 0.4498 0.0277  0.0074  -0.0025 83  PHE   C CE2 
1690 C  CZ  . PHE   B 77  ? 0.3537 0.3468 0.4503 0.0281  0.0131  -0.0076 83  PHE   C CZ  
1691 N  N   . VAL   B 78  ? 0.2309 0.2279 0.2934 0.0171  0.0103  -0.0037 84  VAL   C N   
1692 C  CA  . VAL   B 78  ? 0.2275 0.2211 0.2817 0.0157  0.0132  -0.0067 84  VAL   C CA  
1693 C  C   . VAL   B 78  ? 0.2335 0.2228 0.2896 0.0173  0.0158  -0.0099 84  VAL   C C   
1694 O  O   . VAL   B 78  ? 0.2267 0.2127 0.2854 0.0186  0.0140  -0.0090 84  VAL   C O   
1695 C  CB  . VAL   B 78  ? 0.2226 0.2134 0.2685 0.0137  0.0106  -0.0050 84  VAL   C CB  
1696 C  CG1 . VAL   B 78  ? 0.2233 0.2107 0.2613 0.0122  0.0126  -0.0079 84  VAL   C CG1 
1697 C  CG2 . VAL   B 78  ? 0.2172 0.2116 0.2612 0.0120  0.0084  -0.0023 84  VAL   C CG2 
1698 N  N   . GLU   B 79  ? 0.2400 0.2284 0.2931 0.0167  0.0202  -0.0137 85  GLU   C N   
1699 C  CA  . GLU   B 79  ? 0.2458 0.2295 0.2991 0.0176  0.0235  -0.0177 85  GLU   C CA  
1700 C  C   . GLU   B 79  ? 0.2455 0.2232 0.2927 0.0169  0.0214  -0.0177 85  GLU   C C   
1701 O  O   . GLU   B 79  ? 0.2582 0.2354 0.2986 0.0149  0.0186  -0.0159 85  GLU   C O   
1702 C  CB  . GLU   B 79  ? 0.2795 0.2624 0.3264 0.0157  0.0284  -0.0215 85  GLU   C CB  
1703 C  CG  . GLU   B 79  ? 0.3401 0.3284 0.3935 0.0161  0.0321  -0.0227 85  GLU   C CG  
1704 C  CD  . GLU   B 79  ? 0.4068 0.3967 0.4723 0.0190  0.0357  -0.0253 85  GLU   C CD  
1705 O  OE1 . GLU   B 79  ? 0.4104 0.4063 0.4840 0.0196  0.0379  -0.0256 85  GLU   C OE1 
1706 O  OE2 . GLU   B 79  ? 0.4064 0.3917 0.4739 0.0207  0.0363  -0.0272 85  GLU   C OE2 
1707 N  N   . ALA   B 80  ? 0.2404 0.2136 0.2901 0.0182  0.0230  -0.0203 86  ALA   C N   
1708 C  CA  . ALA   B 80  ? 0.2483 0.2155 0.2926 0.0171  0.0212  -0.0208 86  ALA   C CA  
1709 C  C   . ALA   B 80  ? 0.2385 0.2033 0.2714 0.0141  0.0216  -0.0228 86  ALA   C C   
1710 O  O   . ALA   B 80  ? 0.2370 0.2024 0.2656 0.0130  0.0248  -0.0252 86  ALA   C O   
1711 C  CB  . ALA   B 80  ? 0.2599 0.2221 0.3088 0.0190  0.0235  -0.0239 86  ALA   C CB  
1712 N  N   . SER   B 81  ? 0.2271 0.1893 0.2554 0.0125  0.0183  -0.0216 87  SER   C N   
1713 C  CA  . SER   B 81  ? 0.2269 0.1865 0.2455 0.0097  0.0174  -0.0232 87  SER   C CA  
1714 C  C   . SER   B 81  ? 0.2492 0.2038 0.2665 0.0088  0.0152  -0.0241 87  SER   C C   
1715 O  O   . SER   B 81  ? 0.2606 0.2137 0.2842 0.0103  0.0150  -0.0234 87  SER   C O   
1716 C  CB  . SER   B 81  ? 0.2138 0.1774 0.2294 0.0085  0.0145  -0.0201 87  SER   C CB  
1717 O  OG  . SER   B 81  ? 0.2072 0.1722 0.2264 0.0086  0.0113  -0.0170 87  SER   C OG  
1718 N  N   . GLU   B 82  ? 0.2560 0.2078 0.2657 0.0063  0.0134  -0.0254 88  GLU   C N   
1719 C  CA  . GLU   B 82  ? 0.2654 0.2133 0.2748 0.0050  0.0109  -0.0261 88  GLU   C CA  
1720 C  C   . GLU   B 82  ? 0.2631 0.2141 0.2778 0.0051  0.0078  -0.0223 88  GLU   C C   
1721 O  O   . GLU   B 82  ? 0.2705 0.2186 0.2870 0.0043  0.0064  -0.0224 88  GLU   C O   
1722 C  CB  . GLU   B 82  ? 0.2887 0.2330 0.2891 0.0021  0.0091  -0.0285 88  GLU   C CB  
1723 C  CG  . GLU   B 82  ? 0.3364 0.2844 0.3338 0.0009  0.0056  -0.0261 88  GLU   C CG  
1724 C  CD  . GLU   B 82  ? 0.4355 0.3842 0.4265 0.0005  0.0070  -0.0263 88  GLU   C CD  
1725 O  OE1 . GLU   B 82  ? 0.4867 0.4338 0.4706 -0.0016 0.0042  -0.0266 88  GLU   C OE1 
1726 O  OE2 . GLU   B 82  ? 0.3945 0.3454 0.3878 0.0020  0.0107  -0.0262 88  GLU   C OE2 
1727 N  N   . TYR   B 83  ? 0.2539 0.2102 0.2706 0.0058  0.0071  -0.0191 89  TYR   C N   
1728 C  CA  . TYR   B 83  ? 0.2481 0.2073 0.2686 0.0054  0.0049  -0.0157 89  TYR   C CA  
1729 C  C   . TYR   B 83  ? 0.2454 0.2054 0.2719 0.0071  0.0055  -0.0131 89  TYR   C C   
1730 O  O   . TYR   B 83  ? 0.2600 0.2196 0.2889 0.0063  0.0040  -0.0109 89  TYR   C O   
1731 C  CB  . TYR   B 83  ? 0.2434 0.2074 0.2620 0.0048  0.0038  -0.0139 89  TYR   C CB  
1732 C  CG  . TYR   B 83  ? 0.2443 0.2072 0.2569 0.0033  0.0024  -0.0158 89  TYR   C CG  
1733 C  CD1 . TYR   B 83  ? 0.2711 0.2325 0.2830 0.0016  -0.0003 -0.0166 89  TYR   C CD1 
1734 C  CD2 . TYR   B 83  ? 0.2626 0.2258 0.2704 0.0034  0.0035  -0.0166 89  TYR   C CD2 
1735 C  CE1 . TYR   B 83  ? 0.2953 0.2558 0.3021 0.0002  -0.0026 -0.0178 89  TYR   C CE1 
1736 C  CE2 . TYR   B 83  ? 0.2913 0.2528 0.2927 0.0018  0.0016  -0.0177 89  TYR   C CE2 
1737 C  CZ  . TYR   B 83  ? 0.3167 0.2767 0.3176 0.0003  -0.0018 -0.0182 89  TYR   C CZ  
1738 O  OH  . TYR   B 83  ? 0.3583 0.3164 0.3533 -0.0012 -0.0048 -0.0190 89  TYR   C OH  
1739 N  N   . TYR   B 84  ? 0.2315 0.1925 0.2605 0.0092  0.0074  -0.0132 90  TYR   C N   
1740 C  CA  . TYR   B 84  ? 0.2237 0.1856 0.2589 0.0110  0.0071  -0.0104 90  TYR   C CA  
1741 C  C   . TYR   B 84  ? 0.2447 0.2052 0.2845 0.0136  0.0096  -0.0124 90  TYR   C C   
1742 O  O   . TYR   B 84  ? 0.2460 0.2073 0.2840 0.0140  0.0122  -0.0153 90  TYR   C O   
1743 C  CB  . TYR   B 84  ? 0.2123 0.1798 0.2481 0.0111  0.0062  -0.0073 90  TYR   C CB  
1744 C  CG  . TYR   B 84  ? 0.2081 0.1778 0.2400 0.0088  0.0046  -0.0058 90  TYR   C CG  
1745 C  CD1 . TYR   B 84  ? 0.2153 0.1878 0.2433 0.0080  0.0050  -0.0067 90  TYR   C CD1 
1746 C  CD2 . TYR   B 84  ? 0.2110 0.1799 0.2434 0.0074  0.0030  -0.0034 90  TYR   C CD2 
1747 C  CE1 . TYR   B 84  ? 0.2107 0.1853 0.2366 0.0063  0.0037  -0.0056 90  TYR   C CE1 
1748 C  CE2 . TYR   B 84  ? 0.2121 0.1835 0.2420 0.0054  0.0023  -0.0024 90  TYR   C CE2 
1749 C  CZ  . TYR   B 84  ? 0.2124 0.1867 0.2396 0.0050  0.0026  -0.0037 90  TYR   C CZ  
1750 O  OH  . TYR   B 84  ? 0.1925 0.1690 0.2185 0.0034  0.0021  -0.0031 90  TYR   C OH  
1751 N  N   . PRO   B 85  ? 0.2610 0.2196 0.3073 0.0155  0.0088  -0.0105 91  PRO   C N   
1752 C  CA  . PRO   B 85  ? 0.2633 0.2219 0.3164 0.0185  0.0111  -0.0122 91  PRO   C CA  
1753 C  C   . PRO   B 85  ? 0.2635 0.2289 0.3199 0.0196  0.0111  -0.0105 91  PRO   C C   
1754 O  O   . PRO   B 85  ? 0.2575 0.2265 0.3107 0.0180  0.0090  -0.0075 91  PRO   C O   
1755 C  CB  . PRO   B 85  ? 0.2791 0.2335 0.3385 0.0202  0.0090  -0.0097 91  PRO   C CB  
1756 C  CG  . PRO   B 85  ? 0.2890 0.2437 0.3448 0.0180  0.0054  -0.0053 91  PRO   C CG  
1757 C  CD  . PRO   B 85  ? 0.2685 0.2251 0.3164 0.0149  0.0058  -0.0066 91  PRO   C CD  
1758 N  N   . ALA   B 86  ? 0.2666 0.2338 0.3301 0.0221  0.0137  -0.0123 92  ALA   C N   
1759 C  CA  . ALA   B 86  ? 0.2705 0.2446 0.3387 0.0229  0.0135  -0.0106 92  ALA   C CA  
1760 C  C   . ALA   B 86  ? 0.2670 0.2426 0.3385 0.0233  0.0085  -0.0052 92  ALA   C C   
1761 O  O   . ALA   B 86  ? 0.2785 0.2499 0.3533 0.0244  0.0062  -0.0033 92  ALA   C O   
1762 C  CB  . ALA   B 86  ? 0.2733 0.2491 0.3511 0.0258  0.0171  -0.0136 92  ALA   C CB  
1763 N  N   . ARG   B 87  ? 0.2510 0.2314 0.3196 0.0216  0.0067  -0.0026 93  ARG   C N   
1764 C  CA  . ARG   B 87  ? 0.2452 0.2260 0.3139 0.0209  0.0019  0.0024  93  ARG   C CA  
1765 C  C   . ARG   B 87  ? 0.2408 0.2276 0.3081 0.0195  0.0007  0.0041  93  ARG   C C   
1766 O  O   . ARG   B 87  ? 0.2470 0.2371 0.3126 0.0188  0.0036  0.0016  93  ARG   C O   
1767 C  CB  . ARG   B 87  ? 0.2370 0.2131 0.2974 0.0184  0.0007  0.0035  93  ARG   C CB  
1768 C  CG  . ARG   B 87  ? 0.2218 0.2003 0.2739 0.0155  0.0017  0.0027  93  ARG   C CG  
1769 C  CD  . ARG   B 87  ? 0.2110 0.1856 0.2571 0.0135  0.0022  0.0015  93  ARG   C CD  
1770 N  NE  . ARG   B 87  ? 0.1886 0.1652 0.2287 0.0108  0.0016  0.0025  93  ARG   C NE  
1771 C  CZ  . ARG   B 87  ? 0.2193 0.1989 0.2561 0.0100  0.0029  0.0008  93  ARG   C CZ  
1772 N  NH1 . ARG   B 87  ? 0.1879 0.1687 0.2203 0.0079  0.0024  0.0015  93  ARG   C NH1 
1773 N  NH2 . ARG   B 87  ? 0.2192 0.2001 0.2569 0.0113  0.0050  -0.0018 93  ARG   C NH2 
1774 N  N   . TYR   B 88  ? 0.2423 0.2298 0.3094 0.0186  -0.0035 0.0085  94  TYR   C N   
1775 C  CA  . TYR   B 88  ? 0.2477 0.2400 0.3119 0.0166  -0.0048 0.0100  94  TYR   C CA  
1776 C  C   . TYR   B 88  ? 0.2134 0.2034 0.2670 0.0133  -0.0047 0.0104  94  TYR   C C   
1777 O  O   . TYR   B 88  ? 0.2187 0.2044 0.2687 0.0122  -0.0063 0.0124  94  TYR   C O   
1778 C  CB  . TYR   B 88  ? 0.2774 0.2713 0.3459 0.0168  -0.0098 0.0143  94  TYR   C CB  
1779 C  CG  . TYR   B 88  ? 0.3217 0.3198 0.4024 0.0200  -0.0102 0.0139  94  TYR   C CG  
1780 C  CD1 . TYR   B 88  ? 0.3461 0.3508 0.4307 0.0197  -0.0095 0.0129  94  TYR   C CD1 
1781 C  CD2 . TYR   B 88  ? 0.3642 0.3595 0.4534 0.0233  -0.0111 0.0141  94  TYR   C CD2 
1782 C  CE1 . TYR   B 88  ? 0.3767 0.3860 0.4741 0.0225  -0.0094 0.0121  94  TYR   C CE1 
1783 C  CE2 . TYR   B 88  ? 0.3819 0.3815 0.4841 0.0265  -0.0110 0.0132  94  TYR   C CE2 
1784 C  CZ  . TYR   B 88  ? 0.4031 0.4101 0.5097 0.0260  -0.0101 0.0122  94  TYR   C CZ  
1785 O  OH  . TYR   B 88  ? 0.4499 0.4621 0.5708 0.0290  -0.0098 0.0110  94  TYR   C OH  
1786 N  N   . GLN   B 89  ? 0.1703 0.1631 0.2197 0.0119  -0.0025 0.0084  95  GLN   C N   
1787 C  CA  . GLN   B 89  ? 0.1655 0.1568 0.2066 0.0091  -0.0022 0.0086  95  GLN   C CA  
1788 C  C   . GLN   B 89  ? 0.1730 0.1670 0.2118 0.0071  -0.0045 0.0111  95  GLN   C C   
1789 O  O   . GLN   B 89  ? 0.1852 0.1832 0.2269 0.0074  -0.0048 0.0111  95  GLN   C O   
1790 C  CB  . GLN   B 89  ? 0.1688 0.1608 0.2067 0.0087  0.0009  0.0051  95  GLN   C CB  
1791 C  CG  . GLN   B 89  ? 0.1860 0.1773 0.2173 0.0063  0.0010  0.0051  95  GLN   C CG  
1792 C  CD  . GLN   B 89  ? 0.2111 0.2014 0.2393 0.0062  0.0030  0.0022  95  GLN   C CD  
1793 O  OE1 . GLN   B 89  ? 0.2024 0.1904 0.2313 0.0072  0.0040  0.0003  95  GLN   C OE1 
1794 N  NE2 . GLN   B 89  ? 0.1752 0.1667 0.1997 0.0047  0.0033  0.0019  95  GLN   C NE2 
1795 N  N   . SER   B 90  ? 0.1466 0.1381 0.1799 0.0048  -0.0059 0.0132  96  SER   C N   
1796 C  CA  . SER   B 90  ? 0.1577 0.1507 0.1871 0.0023  -0.0079 0.0154  96  SER   C CA  
1797 C  C   . SER   B 90  ? 0.1599 0.1542 0.1839 0.0002  -0.0056 0.0134  96  SER   C C   
1798 O  O   . SER   B 90  ? 0.1629 0.1564 0.1859 0.0005  -0.0030 0.0109  96  SER   C O   
1799 C  CB  . SER   B 90  ? 0.1816 0.1706 0.2068 0.0003  -0.0104 0.0187  96  SER   C CB  
1800 O  OG  . SER   B 90  ? 0.2008 0.1865 0.2219 -0.0011 -0.0080 0.0176  96  SER   C OG  
1801 N  N   . HIS   B 91  ? 0.1484 0.1445 0.1693 -0.0020 -0.0069 0.0144  97  HIS   C N   
1802 C  CA  . HIS   B 91  ? 0.1505 0.1473 0.1665 -0.0041 -0.0049 0.0126  97  HIS   C CA  
1803 C  C   . HIS   B 91  ? 0.1747 0.1736 0.1931 -0.0025 -0.0024 0.0097  97  HIS   C C   
1804 O  O   . HIS   B 91  ? 0.1816 0.1795 0.1969 -0.0033 -0.0003 0.0079  97  HIS   C O   
1805 C  CB  . HIS   B 91  ? 0.1433 0.1367 0.1540 -0.0060 -0.0031 0.0122  97  HIS   C CB  
1806 C  CG  . HIS   B 91  ? 0.1908 0.1814 0.1969 -0.0085 -0.0051 0.0150  97  HIS   C CG  
1807 N  ND1 . HIS   B 91  ? 0.2295 0.2194 0.2291 -0.0120 -0.0054 0.0157  97  HIS   C ND1 
1808 C  CD2 . HIS   B 91  ? 0.2083 0.1960 0.2149 -0.0083 -0.0068 0.0175  97  HIS   C CD2 
1809 C  CE1 . HIS   B 91  ? 0.2329 0.2194 0.2283 -0.0139 -0.0073 0.0186  97  HIS   C CE1 
1810 N  NE2 . HIS   B 91  ? 0.2302 0.2153 0.2299 -0.0118 -0.0084 0.0199  97  HIS   C NE2 
1811 N  N   . LEU   B 92  ? 0.1698 0.1709 0.1938 -0.0004 -0.0026 0.0094  98  LEU   C N   
1812 C  CA  . LEU   B 92  ? 0.1622 0.1645 0.1874 0.0006  0.0000  0.0069  98  LEU   C CA  
1813 C  C   . LEU   B 92  ? 0.1694 0.1752 0.1955 -0.0005 0.0000  0.0068  98  LEU   C C   
1814 O  O   . LEU   B 92  ? 0.1712 0.1798 0.2009 -0.0009 -0.0023 0.0084  98  LEU   C O   
1815 C  CB  . LEU   B 92  ? 0.1602 0.1624 0.1906 0.0033  0.0009  0.0059  98  LEU   C CB  
1816 C  CG  . LEU   B 92  ? 0.1859 0.1880 0.2161 0.0041  0.0038  0.0032  98  LEU   C CG  
1817 C  CD1 . LEU   B 92  ? 0.1966 0.1953 0.2210 0.0034  0.0047  0.0019  98  LEU   C CD1 
1818 C  CD2 . LEU   B 92  ? 0.2122 0.2137 0.2472 0.0064  0.0050  0.0021  98  LEU   C CD2 
1819 N  N   . MET   B 93  ? 0.1563 0.1617 0.1796 -0.0013 0.0021  0.0050  99  MET   C N   
1820 C  CA  . MET   B 93  ? 0.1561 0.1642 0.1798 -0.0028 0.0025  0.0047  99  MET   C CA  
1821 C  C   . MET   B 93  ? 0.1622 0.1704 0.1870 -0.0019 0.0053  0.0028  99  MET   C C   
1822 O  O   . MET   B 93  ? 0.1789 0.1838 0.2002 -0.0013 0.0067  0.0016  99  MET   C O   
1823 C  CB  . MET   B 93  ? 0.1615 0.1677 0.1793 -0.0051 0.0025  0.0044  99  MET   C CB  
1824 C  CG  . MET   B 93  ? 0.1975 0.2028 0.2126 -0.0065 0.0005  0.0059  99  MET   C CG  
1825 S  SD  . MET   B 93  ? 0.2147 0.2169 0.2231 -0.0089 0.0018  0.0045  99  MET   C SD  
1826 C  CE  . MET   B 93  ? 0.1781 0.1772 0.1861 -0.0068 0.0039  0.0028  99  MET   C CE  
1827 N  N   . LEU   B 94  ? 0.1449 0.1568 0.1743 -0.0023 0.0061  0.0026  100 LEU   C N   
1828 C  CA  . LEU   B 94  ? 0.1403 0.1521 0.1699 -0.0021 0.0095  0.0006  100 LEU   C CA  
1829 C  C   . LEU   B 94  ? 0.1520 0.1639 0.1785 -0.0047 0.0109  0.0002  100 LEU   C C   
1830 O  O   . LEU   B 94  ? 0.1460 0.1603 0.1736 -0.0065 0.0094  0.0011  100 LEU   C O   
1831 C  CB  . LEU   B 94  ? 0.1458 0.1618 0.1841 -0.0007 0.0109  0.0000  100 LEU   C CB  
1832 C  CG  . LEU   B 94  ? 0.1704 0.1859 0.2130 0.0021  0.0101  0.0001  100 LEU   C CG  
1833 C  CD1 . LEU   B 94  ? 0.1790 0.1986 0.2314 0.0037  0.0122  -0.0013 100 LEU   C CD1 
1834 C  CD2 . LEU   B 94  ? 0.2030 0.2131 0.2394 0.0030  0.0114  -0.0012 100 LEU   C CD2 
1835 N  N   . ALA   B 95  ? 0.1535 0.1623 0.1756 -0.0052 0.0137  -0.0012 101 ALA   C N   
1836 C  CA  . ALA   B 95  ? 0.1658 0.1737 0.1845 -0.0078 0.0155  -0.0016 101 ALA   C CA  
1837 C  C   . ALA   B 95  ? 0.1625 0.1695 0.1803 -0.0081 0.0194  -0.0033 101 ALA   C C   
1838 O  O   . ALA   B 95  ? 0.1672 0.1727 0.1846 -0.0064 0.0205  -0.0043 101 ALA   C O   
1839 C  CB  . ALA   B 95  ? 0.1809 0.1831 0.1917 -0.0086 0.0144  -0.0012 101 ALA   C CB  
1840 N  N   . VAL   B 96  ? 0.1617 0.1694 0.1788 -0.0108 0.0219  -0.0037 102 VAL   C N   
1841 C  CA  . VAL   B 96  ? 0.1643 0.1702 0.1785 -0.0120 0.0263  -0.0053 102 VAL   C CA  
1842 C  C   . VAL   B 96  ? 0.1933 0.1912 0.1961 -0.0130 0.0258  -0.0047 102 VAL   C C   
1843 O  O   . VAL   B 96  ? 0.1999 0.1951 0.1986 -0.0148 0.0246  -0.0035 102 VAL   C O   
1844 C  CB  . VAL   B 96  ? 0.1653 0.1754 0.1840 -0.0150 0.0294  -0.0059 102 VAL   C CB  
1845 C  CG1 . VAL   B 96  ? 0.1744 0.1816 0.1882 -0.0171 0.0348  -0.0076 102 VAL   C CG1 
1846 C  CG2 . VAL   B 96  ? 0.1673 0.1859 0.1990 -0.0136 0.0290  -0.0063 102 VAL   C CG2 
1847 N  N   . GLY   B 97  ? 0.2029 0.1967 0.2009 -0.0118 0.0262  -0.0055 103 GLY   C N   
1848 C  CA  . GLY   B 97  ? 0.2290 0.2153 0.2167 -0.0126 0.0247  -0.0047 103 GLY   C CA  
1849 C  C   . GLY   B 97  ? 0.2295 0.2120 0.2126 -0.0114 0.0249  -0.0059 103 GLY   C C   
1850 O  O   . GLY   B 97  ? 0.2336 0.2192 0.2219 -0.0096 0.0261  -0.0074 103 GLY   C O   
1851 N  N   . HIS   B 98  ? 0.2256 0.2011 0.1988 -0.0127 0.0236  -0.0052 104 HIS   C N   
1852 C  CA  . HIS   B 98  ? 0.2295 0.2005 0.1965 -0.0124 0.0234  -0.0063 104 HIS   C CA  
1853 C  C   . HIS   B 98  ? 0.2270 0.1980 0.1967 -0.0095 0.0190  -0.0059 104 HIS   C C   
1854 O  O   . HIS   B 98  ? 0.2320 0.2026 0.2031 -0.0085 0.0153  -0.0042 104 HIS   C O   
1855 C  CB  . HIS   B 98  ? 0.2521 0.2149 0.2066 -0.0152 0.0229  -0.0053 104 HIS   C CB  
1856 C  CG  . HIS   B 98  ? 0.2870 0.2445 0.2337 -0.0155 0.0221  -0.0064 104 HIS   C CG  
1857 N  ND1 . HIS   B 98  ? 0.3195 0.2771 0.2644 -0.0166 0.0269  -0.0092 104 HIS   C ND1 
1858 C  CD2 . HIS   B 98  ? 0.2940 0.2465 0.2353 -0.0148 0.0171  -0.0053 104 HIS   C CD2 
1859 C  CE1 . HIS   B 98  ? 0.3264 0.2783 0.2634 -0.0169 0.0246  -0.0098 104 HIS   C CE1 
1860 N  NE2 . HIS   B 98  ? 0.3203 0.2691 0.2549 -0.0159 0.0183  -0.0072 104 HIS   C NE2 
1861 N  N   . SER   B 99  ? 0.2179 0.1888 0.1881 -0.0084 0.0198  -0.0078 105 SER   C N   
1862 C  CA  . SER   B 99  ? 0.2263 0.1964 0.1980 -0.0063 0.0159  -0.0077 105 SER   C CA  
1863 C  C   . SER   B 99  ? 0.2389 0.2059 0.2065 -0.0065 0.0172  -0.0100 105 SER   C C   
1864 O  O   . SER   B 99  ? 0.2414 0.2094 0.2096 -0.0071 0.0218  -0.0122 105 SER   C O   
1865 C  CB  . SER   B 99  ? 0.2522 0.2283 0.2343 -0.0039 0.0149  -0.0072 105 SER   C CB  
1866 O  OG  . SER   B 99  ? 0.3187 0.2985 0.3067 -0.0029 0.0179  -0.0087 105 SER   C OG  
1867 N  N   . GLU   B 100 ? 0.2257 0.1889 0.1896 -0.0061 0.0132  -0.0098 106 GLU   C N   
1868 C  CA  . GLU   B 100 ? 0.2377 0.1973 0.1974 -0.0064 0.0132  -0.0120 106 GLU   C CA  
1869 C  C   . GLU   B 100 ? 0.2291 0.1906 0.1953 -0.0042 0.0094  -0.0117 106 GLU   C C   
1870 O  O   . GLU   B 100 ? 0.2092 0.1738 0.1810 -0.0029 0.0067  -0.0097 106 GLU   C O   
1871 C  CB  . GLU   B 100 ? 0.2702 0.2221 0.2168 -0.0092 0.0113  -0.0118 106 GLU   C CB  
1872 C  CG  . GLU   B 100 ? 0.3118 0.2611 0.2509 -0.0121 0.0158  -0.0122 106 GLU   C CG  
1873 C  CD  . GLU   B 100 ? 0.3878 0.3286 0.3123 -0.0155 0.0138  -0.0113 106 GLU   C CD  
1874 O  OE1 . GLU   B 100 ? 0.4404 0.3766 0.3587 -0.0162 0.0109  -0.0122 106 GLU   C OE1 
1875 O  OE2 . GLU   B 100 ? 0.3878 0.3262 0.3067 -0.0176 0.0151  -0.0097 106 GLU   C OE2 
1876 N  N   . PRO   B 101 ? 0.2370 0.1968 0.2030 -0.0039 0.0095  -0.0138 107 PRO   C N   
1877 C  CA  . PRO   B 101 ? 0.2297 0.1916 0.2027 -0.0021 0.0064  -0.0135 107 PRO   C CA  
1878 C  C   . PRO   B 101 ? 0.2297 0.1916 0.2035 -0.0019 0.0012  -0.0114 107 PRO   C C   
1879 O  O   . PRO   B 101 ? 0.2291 0.1949 0.2107 -0.0004 -0.0001 -0.0104 107 PRO   C O   
1880 C  CB  . PRO   B 101 ? 0.2457 0.2039 0.2155 -0.0027 0.0070  -0.0163 107 PRO   C CB  
1881 C  CG  . PRO   B 101 ? 0.2608 0.2178 0.2272 -0.0035 0.0126  -0.0186 107 PRO   C CG  
1882 C  CD  . PRO   B 101 ? 0.2454 0.2016 0.2058 -0.0052 0.0131  -0.0169 107 PRO   C CD  
1883 N  N   . GLY   B 102 ? 0.2214 0.1785 0.1870 -0.0035 -0.0018 -0.0109 108 GLY   C N   
1884 C  CA  . GLY   B 102 ? 0.2297 0.1864 0.1967 -0.0032 -0.0071 -0.0090 108 GLY   C CA  
1885 C  C   . GLY   B 102 ? 0.2234 0.1835 0.1957 -0.0020 -0.0071 -0.0069 108 GLY   C C   
1886 O  O   . GLY   B 102 ? 0.2187 0.1795 0.1949 -0.0012 -0.0108 -0.0057 108 GLY   C O   
1887 N  N   . ASP   B 103 ? 0.2077 0.1701 0.1806 -0.0021 -0.0029 -0.0067 109 ASP   C N   
1888 C  CA  . ASP   B 103 ? 0.2022 0.1675 0.1795 -0.0014 -0.0026 -0.0050 109 ASP   C CA  
1889 C  C   . ASP   B 103 ? 0.1829 0.1535 0.1697 0.0003  -0.0023 -0.0050 109 ASP   C C   
1890 O  O   . ASP   B 103 ? 0.1880 0.1607 0.1784 0.0007  -0.0024 -0.0040 109 ASP   C O   
1891 C  CB  . ASP   B 103 ? 0.2133 0.1792 0.1879 -0.0025 0.0015  -0.0049 109 ASP   C CB  
1892 C  CG  . ASP   B 103 ? 0.2408 0.2009 0.2054 -0.0047 0.0012  -0.0043 109 ASP   C CG  
1893 O  OD1 . ASP   B 103 ? 0.2453 0.2013 0.2063 -0.0049 -0.0030 -0.0030 109 ASP   C OD1 
1894 O  OD2 . ASP   B 103 ? 0.2361 0.1954 0.1965 -0.0063 0.0051  -0.0051 109 ASP   C OD2 
1895 N  N   . CYS   B 104 ? 0.1683 0.1405 0.1585 0.0009  -0.0016 -0.0062 110 CYS   C N   
1896 C  CA  . CYS   B 104 ? 0.1738 0.1502 0.1716 0.0019  -0.0012 -0.0059 110 CYS   C CA  
1897 C  C   . CYS   B 104 ? 0.1805 0.1577 0.1821 0.0023  -0.0038 -0.0053 110 CYS   C C   
1898 O  O   . CYS   B 104 ? 0.1865 0.1614 0.1871 0.0023  -0.0069 -0.0056 110 CYS   C O   
1899 C  CB  . CYS   B 104 ? 0.1877 0.1642 0.1878 0.0023  -0.0007 -0.0071 110 CYS   C CB  
1900 S  SG  . CYS   B 104 ? 0.2266 0.2040 0.2268 0.0027  0.0031  -0.0079 110 CYS   C SG  
1901 N  N   . GLY   B 105 ? 0.1664 0.1467 0.1724 0.0026  -0.0025 -0.0047 111 GLY   C N   
1902 C  CA  . GLY   B 105 ? 0.1600 0.1412 0.1704 0.0029  -0.0040 -0.0047 111 GLY   C CA  
1903 C  C   . GLY   B 105 ? 0.1763 0.1564 0.1854 0.0030  -0.0042 -0.0040 111 GLY   C C   
1904 O  O   . GLY   B 105 ? 0.1830 0.1643 0.1968 0.0034  -0.0043 -0.0043 111 GLY   C O   
1905 N  N   . GLY   B 106 ? 0.1695 0.1472 0.1726 0.0024  -0.0038 -0.0033 112 GLY   C N   
1906 C  CA  . GLY   B 106 ? 0.1697 0.1457 0.1711 0.0021  -0.0038 -0.0026 112 GLY   C CA  
1907 C  C   . GLY   B 106 ? 0.1675 0.1466 0.1721 0.0017  -0.0011 -0.0027 112 GLY   C C   
1908 O  O   . GLY   B 106 ? 0.1639 0.1457 0.1688 0.0012  0.0009  -0.0028 112 GLY   C O   
1909 N  N   . ILE   B 107 ? 0.1653 0.1436 0.1721 0.0019  -0.0013 -0.0029 113 ILE   C N   
1910 C  CA  . ILE   B 107 ? 0.1767 0.1573 0.1855 0.0011  0.0013  -0.0035 113 ILE   C CA  
1911 C  C   . ILE   B 107 ? 0.1651 0.1452 0.1696 -0.0004 0.0028  -0.0028 113 ILE   C C   
1912 O  O   . ILE   B 107 ? 0.1818 0.1586 0.1827 -0.0007 0.0020  -0.0021 113 ILE   C O   
1913 C  CB  . ILE   B 107 ? 0.2194 0.1993 0.2331 0.0019  0.0011  -0.0046 113 ILE   C CB  
1914 C  CG1 . ILE   B 107 ? 0.2577 0.2404 0.2774 0.0027  0.0011  -0.0057 113 ILE   C CG1 
1915 C  CG2 . ILE   B 107 ? 0.2420 0.2219 0.2554 0.0007  0.0037  -0.0054 113 ILE   C CG2 
1916 C  CD1 . ILE   B 107 ? 0.2832 0.2659 0.3099 0.0037  0.0012  -0.0074 113 ILE   C CD1 
1917 N  N   . LEU   B 108 ? 0.1503 0.1333 0.1551 -0.0016 0.0047  -0.0029 114 LEU   C N   
1918 C  CA  . LEU   B 108 ? 0.1525 0.1359 0.1548 -0.0034 0.0060  -0.0026 114 LEU   C CA  
1919 C  C   . LEU   B 108 ? 0.1699 0.1529 0.1732 -0.0043 0.0071  -0.0037 114 LEU   C C   
1920 O  O   . LEU   B 108 ? 0.1720 0.1567 0.1774 -0.0044 0.0079  -0.0045 114 LEU   C O   
1921 C  CB  . LEU   B 108 ? 0.1441 0.1314 0.1467 -0.0042 0.0066  -0.0019 114 LEU   C CB  
1922 C  CG  . LEU   B 108 ? 0.1613 0.1501 0.1626 -0.0063 0.0074  -0.0016 114 LEU   C CG  
1923 C  CD1 . LEU   B 108 ? 0.1653 0.1522 0.1641 -0.0073 0.0079  -0.0013 114 LEU   C CD1 
1924 C  CD2 . LEU   B 108 ? 0.1684 0.1614 0.1717 -0.0067 0.0072  -0.0006 114 LEU   C CD2 
1925 N  N   . ARG   B 109 ? 0.1772 0.1573 0.1786 -0.0052 0.0075  -0.0041 115 ARG   C N   
1926 C  CA  . ARG   B 109 ? 0.1817 0.1604 0.1838 -0.0062 0.0090  -0.0057 115 ARG   C CA  
1927 C  C   . ARG   B 109 ? 0.1885 0.1668 0.1870 -0.0088 0.0099  -0.0057 115 ARG   C C   
1928 O  O   . ARG   B 109 ? 0.2066 0.1837 0.2029 -0.0094 0.0093  -0.0046 115 ARG   C O   
1929 C  CB  . ARG   B 109 ? 0.2044 0.1787 0.2086 -0.0046 0.0084  -0.0065 115 ARG   C CB  
1930 C  CG  . ARG   B 109 ? 0.2842 0.2586 0.2933 -0.0020 0.0070  -0.0068 115 ARG   C CG  
1931 C  CD  . ARG   B 109 ? 0.3395 0.3096 0.3519 -0.0003 0.0059  -0.0075 115 ARG   C CD  
1932 N  NE  . ARG   B 109 ? 0.3752 0.3441 0.3894 -0.0011 0.0088  -0.0099 115 ARG   C NE  
1933 C  CZ  . ARG   B 109 ? 0.3971 0.3676 0.4170 -0.0005 0.0108  -0.0123 115 ARG   C CZ  
1934 N  NH1 . ARG   B 109 ? 0.3836 0.3571 0.4088 0.0012  0.0100  -0.0125 115 ARG   C NH1 
1935 N  NH2 . ARG   B 109 ? 0.4143 0.3832 0.4348 -0.0016 0.0141  -0.0149 115 ARG   C NH2 
1936 N  N   . CYS   B 110 ? 0.1811 0.1599 0.1785 -0.0108 0.0114  -0.0071 116 CYS   C N   
1937 C  CA  . CYS   B 110 ? 0.1976 0.1753 0.1916 -0.0137 0.0120  -0.0076 116 CYS   C CA  
1938 C  C   . CYS   B 110 ? 0.2186 0.1919 0.2125 -0.0141 0.0139  -0.0101 116 CYS   C C   
1939 O  O   . CYS   B 110 ? 0.2147 0.1864 0.2122 -0.0119 0.0146  -0.0113 116 CYS   C O   
1940 C  CB  . CYS   B 110 ? 0.1968 0.1782 0.1887 -0.0161 0.0118  -0.0071 116 CYS   C CB  
1941 S  SG  . CYS   B 110 ? 0.1954 0.1769 0.1863 -0.0170 0.0135  -0.0088 116 CYS   C SG  
1942 N  N   . GLN   B 111 ? 0.2337 0.2051 0.2240 -0.0171 0.0148  -0.0112 117 GLN   C N   
1943 C  CA  . GLN   B 111 ? 0.2495 0.2161 0.2396 -0.0177 0.0171  -0.0141 117 GLN   C CA  
1944 C  C   . GLN   B 111 ? 0.2598 0.2269 0.2509 -0.0177 0.0196  -0.0166 117 GLN   C C   
1945 O  O   . GLN   B 111 ? 0.2898 0.2532 0.2829 -0.0172 0.0221  -0.0195 117 GLN   C O   
1946 C  CB  . GLN   B 111 ? 0.2771 0.2415 0.2624 -0.0216 0.0176  -0.0151 117 GLN   C CB  
1947 C  CG  . GLN   B 111 ? 0.3179 0.2858 0.2989 -0.0250 0.0173  -0.0151 117 GLN   C CG  
1948 C  CD  . GLN   B 111 ? 0.4394 0.4053 0.4160 -0.0290 0.0172  -0.0161 117 GLN   C CD  
1949 O  OE1 . GLN   B 111 ? 0.4653 0.4343 0.4413 -0.0307 0.0150  -0.0142 117 GLN   C OE1 
1950 N  NE2 . GLN   B 111 ? 0.4704 0.4311 0.4445 -0.0306 0.0197  -0.0194 117 GLN   C NE2 
1951 N  N   . HIS   B 112 ? 0.2380 0.2094 0.2283 -0.0182 0.0193  -0.0156 118 HIS   C N   
1952 C  CA  . HIS   B 112 ? 0.2278 0.1996 0.2180 -0.0189 0.0221  -0.0177 118 HIS   C CA  
1953 C  C   . HIS   B 112 ? 0.2363 0.2099 0.2330 -0.0156 0.0225  -0.0176 118 HIS   C C   
1954 O  O   . HIS   B 112 ? 0.2499 0.2236 0.2480 -0.0162 0.0255  -0.0198 118 HIS   C O   
1955 C  CB  . HIS   B 112 ? 0.2260 0.2002 0.2100 -0.0223 0.0215  -0.0165 118 HIS   C CB  
1956 C  CG  . HIS   B 112 ? 0.2382 0.2111 0.2159 -0.0260 0.0205  -0.0166 118 HIS   C CG  
1957 N  ND1 . HIS   B 112 ? 0.2352 0.2112 0.2121 -0.0267 0.0169  -0.0136 118 HIS   C ND1 
1958 C  CD2 . HIS   B 112 ? 0.2579 0.2270 0.2307 -0.0293 0.0228  -0.0195 118 HIS   C CD2 
1959 C  CE1 . HIS   B 112 ? 0.2647 0.2389 0.2365 -0.0304 0.0166  -0.0146 118 HIS   C CE1 
1960 N  NE2 . HIS   B 112 ? 0.2812 0.2510 0.2497 -0.0322 0.0200  -0.0181 118 HIS   C NE2 
1961 N  N   . GLY   B 113 ? 0.2200 0.1950 0.2205 -0.0127 0.0196  -0.0153 119 GLY   C N   
1962 C  CA  . GLY   B 113 ? 0.1994 0.1762 0.2059 -0.0099 0.0192  -0.0151 119 GLY   C CA  
1963 C  C   . GLY   B 113 ? 0.1763 0.1561 0.1829 -0.0086 0.0161  -0.0121 119 GLY   C C   
1964 O  O   . GLY   B 113 ? 0.1768 0.1568 0.1800 -0.0092 0.0142  -0.0101 119 GLY   C O   
1965 N  N   . VAL   B 114 ? 0.1632 0.1451 0.1738 -0.0072 0.0160  -0.0120 120 VAL   C N   
1966 C  CA  . VAL   B 114 ? 0.1652 0.1494 0.1761 -0.0060 0.0134  -0.0096 120 VAL   C CA  
1967 C  C   . VAL   B 114 ? 0.1671 0.1533 0.1736 -0.0080 0.0133  -0.0080 120 VAL   C C   
1968 O  O   . VAL   B 114 ? 0.1703 0.1571 0.1752 -0.0099 0.0151  -0.0086 120 VAL   C O   
1969 C  CB  . VAL   B 114 ? 0.1761 0.1616 0.1930 -0.0042 0.0133  -0.0103 120 VAL   C CB  
1970 C  CG1 . VAL   B 114 ? 0.1840 0.1714 0.2006 -0.0033 0.0110  -0.0082 120 VAL   C CG1 
1971 C  CG2 . VAL   B 114 ? 0.1854 0.1690 0.2078 -0.0017 0.0122  -0.0113 120 VAL   C CG2 
1972 N  N   . VAL   B 115 ? 0.1558 0.1431 0.1606 -0.0076 0.0111  -0.0060 121 VAL   C N   
1973 C  CA  . VAL   B 115 ? 0.1578 0.1473 0.1601 -0.0090 0.0102  -0.0042 121 VAL   C CA  
1974 C  C   . VAL   B 115 ? 0.1651 0.1562 0.1698 -0.0075 0.0091  -0.0029 121 VAL   C C   
1975 O  O   . VAL   B 115 ? 0.1586 0.1507 0.1621 -0.0086 0.0088  -0.0018 121 VAL   C O   
1976 C  CB  . VAL   B 115 ? 0.1604 0.1505 0.1611 -0.0095 0.0090  -0.0031 121 VAL   C CB  
1977 C  CG1 . VAL   B 115 ? 0.1653 0.1584 0.1660 -0.0101 0.0075  -0.0012 121 VAL   C CG1 
1978 C  CG2 . VAL   B 115 ? 0.1691 0.1574 0.1670 -0.0116 0.0100  -0.0043 121 VAL   C CG2 
1979 N  N   . GLY   B 116 ? 0.1662 0.1568 0.1734 -0.0053 0.0082  -0.0030 122 GLY   C N   
1980 C  CA  . GLY   B 116 ? 0.1679 0.1594 0.1771 -0.0039 0.0072  -0.0022 122 GLY   C CA  
1981 C  C   . GLY   B 116 ? 0.1703 0.1605 0.1807 -0.0020 0.0061  -0.0026 122 GLY   C C   
1982 O  O   . GLY   B 116 ? 0.1773 0.1657 0.1875 -0.0015 0.0058  -0.0033 122 GLY   C O   
1983 N  N   . ILE   B 117 ? 0.1582 0.1488 0.1696 -0.0010 0.0052  -0.0022 123 ILE   C N   
1984 C  CA  . ILE   B 117 ? 0.1651 0.1537 0.1762 0.0004  0.0039  -0.0027 123 ILE   C CA  
1985 C  C   . ILE   B 117 ? 0.1576 0.1462 0.1670 0.0008  0.0039  -0.0023 123 ILE   C C   
1986 O  O   . ILE   B 117 ? 0.1506 0.1410 0.1613 0.0007  0.0045  -0.0016 123 ILE   C O   
1987 C  CB  . ILE   B 117 ? 0.1758 0.1641 0.1902 0.0010  0.0029  -0.0035 123 ILE   C CB  
1988 C  CG1 . ILE   B 117 ? 0.1825 0.1721 0.1986 0.0007  0.0035  -0.0031 123 ILE   C CG1 
1989 C  CG2 . ILE   B 117 ? 0.1922 0.1805 0.2097 0.0010  0.0030  -0.0045 123 ILE   C CG2 
1990 C  CD1 . ILE   B 117 ? 0.1942 0.1833 0.2137 0.0010  0.0025  -0.0040 123 ILE   C CD1 
1991 N  N   . VAL   B 118 ? 0.1462 0.1325 0.1526 0.0011  0.0033  -0.0026 124 VAL   C N   
1992 C  CA  . VAL   B 118 ? 0.1484 0.1344 0.1531 0.0013  0.0043  -0.0029 124 VAL   C CA  
1993 C  C   . VAL   B 118 ? 0.1530 0.1392 0.1601 0.0021  0.0040  -0.0034 124 VAL   C C   
1994 O  O   . VAL   B 118 ? 0.1621 0.1471 0.1701 0.0024  0.0025  -0.0039 124 VAL   C O   
1995 C  CB  . VAL   B 118 ? 0.1600 0.1422 0.1593 0.0009  0.0038  -0.0034 124 VAL   C CB  
1996 C  CG1 . VAL   B 118 ? 0.1569 0.1385 0.1541 0.0008  0.0056  -0.0043 124 VAL   C CG1 
1997 C  CG2 . VAL   B 118 ? 0.1787 0.1599 0.1753 -0.0002 0.0042  -0.0026 124 VAL   C CG2 
1998 N  N   . SER   B 119 ? 0.1543 0.1421 0.1634 0.0026  0.0054  -0.0033 125 SER   C N   
1999 C  CA  . SER   B 119 ? 0.1503 0.1376 0.1621 0.0034  0.0052  -0.0037 125 SER   C CA  
2000 C  C   . SER   B 119 ? 0.1749 0.1616 0.1869 0.0042  0.0070  -0.0049 125 SER   C C   
2001 O  O   . SER   B 119 ? 0.1900 0.1746 0.2026 0.0048  0.0070  -0.0061 125 SER   C O   
2002 C  CB  . SER   B 119 ? 0.1522 0.1417 0.1677 0.0034  0.0048  -0.0022 125 SER   C CB  
2003 O  OG  . SER   B 119 ? 0.1686 0.1570 0.1867 0.0042  0.0045  -0.0021 125 SER   C OG  
2004 N  N   . THR   B 120 ? 0.1722 0.1606 0.1843 0.0040  0.0088  -0.0050 126 THR   C N   
2005 C  CA  . THR   B 120 ? 0.1861 0.1745 0.1995 0.0046  0.0114  -0.0067 126 THR   C CA  
2006 C  C   . THR   B 120 ? 0.1896 0.1779 0.1992 0.0033  0.0137  -0.0075 126 THR   C C   
2007 O  O   . THR   B 120 ? 0.1870 0.1756 0.1938 0.0020  0.0130  -0.0064 126 THR   C O   
2008 C  CB  . THR   B 120 ? 0.1999 0.1919 0.2211 0.0060  0.0118  -0.0058 126 THR   C CB  
2009 O  OG1 . THR   B 120 ? 0.2022 0.1981 0.2255 0.0053  0.0118  -0.0045 126 THR   C OG1 
2010 C  CG2 . THR   B 120 ? 0.2071 0.1987 0.2315 0.0069  0.0094  -0.0043 126 THR   C CG2 
2011 N  N   . GLY   B 121 ? 0.2049 0.1925 0.2145 0.0033  0.0169  -0.0097 127 GLY   C N   
2012 C  CA  . GLY   B 121 ? 0.2295 0.2172 0.2358 0.0016  0.0200  -0.0106 127 GLY   C CA  
2013 C  C   . GLY   B 121 ? 0.2373 0.2246 0.2449 0.0018  0.0244  -0.0135 127 GLY   C C   
2014 O  O   . GLY   B 121 ? 0.2285 0.2144 0.2383 0.0033  0.0249  -0.0150 127 GLY   C O   
2015 N  N   . GLY   B 122 ? 0.2574 0.2463 0.2646 0.0002  0.0281  -0.0144 128 GLY   C N   
2016 C  CA  . GLY   B 122 ? 0.2767 0.2655 0.2855 0.0000  0.0334  -0.0178 128 GLY   C CA  
2017 C  C   . GLY   B 122 ? 0.2771 0.2711 0.2917 -0.0010 0.0371  -0.0181 128 GLY   C C   
2018 O  O   . GLY   B 122 ? 0.2574 0.2563 0.2782 -0.0006 0.0348  -0.0158 128 GLY   C O   
2019 N  N   . ASN   B 123 ? 0.2867 0.2794 0.2986 -0.0029 0.0429  -0.0212 129 ASN   C N   
2020 C  CA  . ASN   B 123 ? 0.2882 0.2861 0.3061 -0.0044 0.0474  -0.0222 129 ASN   C CA  
2021 C  C   . ASN   B 123 ? 0.2655 0.2650 0.2810 -0.0066 0.0451  -0.0191 129 ASN   C C   
2022 O  O   . ASN   B 123 ? 0.2619 0.2679 0.2866 -0.0068 0.0460  -0.0186 129 ASN   C O   
2023 C  CB  . ASN   B 123 ? 0.3279 0.3332 0.3620 -0.0013 0.0482  -0.0229 129 ASN   C CB  
2024 C  CG  . ASN   B 123 ? 0.4188 0.4229 0.4577 0.0011  0.0510  -0.0262 129 ASN   C CG  
2025 O  OD1 . ASN   B 123 ? 0.4605 0.4593 0.4916 -0.0003 0.0553  -0.0294 129 ASN   C OD1 
2026 N  ND2 . ASN   B 123 ? 0.4417 0.4505 0.4936 0.0047  0.0486  -0.0254 129 ASN   C ND2 
2027 N  N   . GLY   B 124 ? 0.2466 0.2404 0.2506 -0.0082 0.0418  -0.0171 130 GLY   C N   
2028 C  CA  . GLY   B 124 ? 0.2380 0.2321 0.2392 -0.0103 0.0399  -0.0145 130 GLY   C CA  
2029 C  C   . GLY   B 124 ? 0.2182 0.2167 0.2265 -0.0084 0.0349  -0.0119 130 GLY   C C   
2030 O  O   . GLY   B 124 ? 0.2156 0.2155 0.2239 -0.0102 0.0340  -0.0103 130 GLY   C O   
2031 N  N   . LEU   B 125 ? 0.2037 0.2036 0.2171 -0.0053 0.0318  -0.0114 131 LEU   C N   
2032 C  CA  . LEU   B 125 ? 0.2044 0.2072 0.2224 -0.0039 0.0271  -0.0090 131 LEU   C CA  
2033 C  C   . LEU   B 125 ? 0.2171 0.2150 0.2290 -0.0028 0.0235  -0.0080 131 LEU   C C   
2034 O  O   . LEU   B 125 ? 0.2612 0.2554 0.2696 -0.0020 0.0241  -0.0094 131 LEU   C O   
2035 C  CB  . LEU   B 125 ? 0.2050 0.2137 0.2348 -0.0015 0.0265  -0.0090 131 LEU   C CB  
2036 C  CG  . LEU   B 125 ? 0.2350 0.2497 0.2738 -0.0021 0.0299  -0.0102 131 LEU   C CG  
2037 C  CD1 . LEU   B 125 ? 0.2641 0.2831 0.3146 0.0010  0.0298  -0.0109 131 LEU   C CD1 
2038 C  CD2 . LEU   B 125 ? 0.2403 0.2588 0.2815 -0.0041 0.0280  -0.0083 131 LEU   C CD2 
2039 N  N   . VAL   B 126 ? 0.1682 0.1660 0.1789 -0.0030 0.0200  -0.0059 132 VAL   C N   
2040 C  CA  . VAL   B 126 ? 0.1691 0.1633 0.1760 -0.0020 0.0168  -0.0051 132 VAL   C CA  
2041 C  C   . VAL   B 126 ? 0.1713 0.1690 0.1840 -0.0008 0.0142  -0.0036 132 VAL   C C   
2042 O  O   . VAL   B 126 ? 0.1686 0.1697 0.1845 -0.0017 0.0137  -0.0026 132 VAL   C O   
2043 C  CB  . VAL   B 126 ? 0.1869 0.1766 0.1862 -0.0035 0.0156  -0.0044 132 VAL   C CB  
2044 C  CG1 . VAL   B 126 ? 0.1999 0.1913 0.1997 -0.0053 0.0156  -0.0033 132 VAL   C CG1 
2045 C  CG2 . VAL   B 126 ? 0.1854 0.1724 0.1830 -0.0023 0.0122  -0.0038 132 VAL   C CG2 
2046 N  N   . GLY   B 127 ? 0.1641 0.1605 0.1777 0.0007  0.0125  -0.0035 133 GLY   C N   
2047 C  CA  . GLY   B 127 ? 0.1568 0.1555 0.1743 0.0014  0.0102  -0.0019 133 GLY   C CA  
2048 C  C   . GLY   B 127 ? 0.1554 0.1514 0.1694 0.0011  0.0083  -0.0013 133 GLY   C C   
2049 O  O   . GLY   B 127 ? 0.1568 0.1496 0.1677 0.0015  0.0081  -0.0022 133 GLY   C O   
2050 N  N   . PHE   B 128 ? 0.1428 0.1403 0.1574 0.0002  0.0070  0.0000  134 PHE   C N   
2051 C  CA  . PHE   B 128 ? 0.1461 0.1417 0.1583 -0.0003 0.0060  0.0001  134 PHE   C CA  
2052 C  C   . PHE   B 128 ? 0.1551 0.1515 0.1692 -0.0004 0.0049  0.0013  134 PHE   C C   
2053 O  O   . PHE   B 128 ? 0.1554 0.1540 0.1711 -0.0011 0.0041  0.0026  134 PHE   C O   
2054 C  CB  . PHE   B 128 ? 0.1461 0.1416 0.1559 -0.0020 0.0061  0.0002  134 PHE   C CB  
2055 C  CG  . PHE   B 128 ? 0.1450 0.1391 0.1523 -0.0024 0.0071  -0.0005 134 PHE   C CG  
2056 C  CD1 . PHE   B 128 ? 0.1601 0.1507 0.1643 -0.0020 0.0069  -0.0011 134 PHE   C CD1 
2057 C  CD2 . PHE   B 128 ? 0.1511 0.1475 0.1592 -0.0036 0.0081  -0.0002 134 PHE   C CD2 
2058 C  CE1 . PHE   B 128 ? 0.1653 0.1537 0.1660 -0.0029 0.0076  -0.0013 134 PHE   C CE1 
2059 C  CE2 . PHE   B 128 ? 0.1587 0.1534 0.1639 -0.0045 0.0095  -0.0007 134 PHE   C CE2 
2060 C  CZ  . PHE   B 128 ? 0.1601 0.1504 0.1609 -0.0043 0.0092  -0.0011 134 PHE   C CZ  
2061 N  N   . ALA   B 129 ? 0.1432 0.1377 0.1570 -0.0001 0.0046  0.0009  135 ALA   C N   
2062 C  CA  . ALA   B 129 ? 0.1435 0.1379 0.1579 -0.0008 0.0040  0.0020  135 ALA   C CA  
2063 C  C   . ALA   B 129 ? 0.1586 0.1532 0.1704 -0.0029 0.0045  0.0020  135 ALA   C C   
2064 O  O   . ALA   B 129 ? 0.1566 0.1502 0.1678 -0.0030 0.0054  0.0006  135 ALA   C O   
2065 C  CB  . ALA   B 129 ? 0.1358 0.1284 0.1514 -0.0002 0.0040  0.0013  135 ALA   C CB  
2066 N  N   . ASP   B 130 ? 0.1637 0.1592 0.1741 -0.0044 0.0038  0.0036  136 ASP   C N   
2067 C  CA  . ASP   B 130 ? 0.1632 0.1581 0.1699 -0.0069 0.0046  0.0033  136 ASP   C CA  
2068 C  C   . ASP   B 130 ? 0.1650 0.1582 0.1706 -0.0080 0.0061  0.0026  136 ASP   C C   
2069 O  O   . ASP   B 130 ? 0.1792 0.1716 0.1857 -0.0078 0.0056  0.0037  136 ASP   C O   
2070 C  CB  . ASP   B 130 ? 0.1782 0.1742 0.1828 -0.0087 0.0027  0.0054  136 ASP   C CB  
2071 C  CG  . ASP   B 130 ? 0.2591 0.2542 0.2586 -0.0118 0.0034  0.0048  136 ASP   C CG  
2072 O  OD1 . ASP   B 130 ? 0.2366 0.2314 0.2355 -0.0120 0.0049  0.0029  136 ASP   C OD1 
2073 O  OD2 . ASP   B 130 ? 0.2650 0.2590 0.2605 -0.0141 0.0024  0.0063  136 ASP   C OD2 
2074 N  N   . VAL   B 131 ? 0.1510 0.1435 0.1550 -0.0093 0.0081  0.0008  137 VAL   C N   
2075 C  CA  . VAL   B 131 ? 0.1591 0.1503 0.1625 -0.0109 0.0105  -0.0003 137 VAL   C CA  
2076 C  C   . VAL   B 131 ? 0.1693 0.1592 0.1672 -0.0142 0.0123  -0.0010 137 VAL   C C   
2077 O  O   . VAL   B 131 ? 0.1804 0.1691 0.1771 -0.0161 0.0150  -0.0023 137 VAL   C O   
2078 C  CB  . VAL   B 131 ? 0.1678 0.1592 0.1762 -0.0092 0.0120  -0.0027 137 VAL   C CB  
2079 C  CG1 . VAL   B 131 ? 0.1825 0.1744 0.1950 -0.0067 0.0100  -0.0022 137 VAL   C CG1 
2080 C  CG2 . VAL   B 131 ? 0.1574 0.1485 0.1664 -0.0086 0.0127  -0.0046 137 VAL   C CG2 
2081 N  N   . ARG   B 132 ? 0.1638 0.1538 0.1583 -0.0152 0.0110  -0.0005 138 ARG   C N   
2082 C  CA  . ARG   B 132 ? 0.1573 0.1457 0.1460 -0.0186 0.0126  -0.0016 138 ARG   C CA  
2083 C  C   . ARG   B 132 ? 0.1752 0.1616 0.1575 -0.0221 0.0128  -0.0001 138 ARG   C C   
2084 O  O   . ARG   B 132 ? 0.1905 0.1747 0.1672 -0.0253 0.0154  -0.0018 138 ARG   C O   
2085 C  CB  . ARG   B 132 ? 0.1489 0.1379 0.1355 -0.0192 0.0106  -0.0011 138 ARG   C CB  
2086 C  CG  . ARG   B 132 ? 0.1494 0.1391 0.1404 -0.0167 0.0110  -0.0026 138 ARG   C CG  
2087 C  CD  . ARG   B 132 ? 0.1569 0.1474 0.1460 -0.0179 0.0091  -0.0019 138 ARG   C CD  
2088 N  NE  . ARG   B 132 ? 0.1618 0.1552 0.1536 -0.0167 0.0060  0.0007  138 ARG   C NE  
2089 C  CZ  . ARG   B 132 ? 0.1699 0.1654 0.1626 -0.0171 0.0041  0.0016  138 ARG   C CZ  
2090 N  NH1 . ARG   B 132 ? 0.1553 0.1499 0.1454 -0.0192 0.0047  0.0003  138 ARG   C NH1 
2091 N  NH2 . ARG   B 132 ? 0.1809 0.1794 0.1777 -0.0156 0.0019  0.0036  138 ARG   C NH2 
2092 N  N   . ASP   B 133 ? 0.1748 0.1615 0.1573 -0.0216 0.0100  0.0030  139 ASP   C N   
2093 C  CA  . ASP   B 133 ? 0.1815 0.1654 0.1571 -0.0251 0.0096  0.0051  139 ASP   C CA  
2094 C  C   . ASP   B 133 ? 0.2002 0.1823 0.1757 -0.0263 0.0135  0.0038  139 ASP   C C   
2095 O  O   . ASP   B 133 ? 0.2210 0.1999 0.1893 -0.0300 0.0143  0.0051  139 ASP   C O   
2096 C  CB  . ASP   B 133 ? 0.2003 0.1844 0.1765 -0.0241 0.0048  0.0092  139 ASP   C CB  
2097 C  CG  . ASP   B 133 ? 0.2469 0.2322 0.2307 -0.0204 0.0043  0.0098  139 ASP   C CG  
2098 O  OD1 . ASP   B 133 ? 0.2504 0.2381 0.2402 -0.0174 0.0055  0.0076  139 ASP   C OD1 
2099 O  OD2 . ASP   B 133 ? 0.2512 0.2346 0.2343 -0.0206 0.0024  0.0125  139 ASP   C OD2 
2100 N  N   . LEU   B 134 ? 0.1898 0.1737 0.1729 -0.0235 0.0157  0.0015  140 LEU   C N   
2101 C  CA  . LEU   B 134 ? 0.1963 0.1795 0.1814 -0.0245 0.0193  0.0002  140 LEU   C CA  
2102 C  C   . LEU   B 134 ? 0.1979 0.1802 0.1811 -0.0270 0.0244  -0.0034 140 LEU   C C   
2103 O  O   . LEU   B 134 ? 0.1977 0.1821 0.1879 -0.0251 0.0269  -0.0066 140 LEU   C O   
2104 C  CB  . LEU   B 134 ? 0.1975 0.1832 0.1922 -0.0205 0.0187  -0.0007 140 LEU   C CB  
2105 C  CG  . LEU   B 134 ? 0.2142 0.2004 0.2111 -0.0178 0.0143  0.0021  140 LEU   C CG  
2106 C  CD1 . LEU   B 134 ? 0.2154 0.2036 0.2203 -0.0144 0.0140  0.0006  140 LEU   C CD1 
2107 C  CD2 . LEU   B 134 ? 0.2181 0.2017 0.2115 -0.0196 0.0131  0.0052  140 LEU   C CD2 
2108 N  N   . LEU   B 135 ? 0.1980 0.1771 0.1715 -0.0316 0.0259  -0.0030 141 LEU   C N   
2109 C  CA  . LEU   B 135 ? 0.2056 0.1834 0.1761 -0.0345 0.0314  -0.0070 141 LEU   C CA  
2110 C  C   . LEU   B 135 ? 0.2181 0.1968 0.1944 -0.0350 0.0369  -0.0101 141 LEU   C C   
2111 O  O   . LEU   B 135 ? 0.2345 0.2137 0.2136 -0.0354 0.0416  -0.0143 141 LEU   C O   
2112 C  CB  . LEU   B 135 ? 0.2076 0.1809 0.1647 -0.0399 0.0319  -0.0059 141 LEU   C CB  
2113 C  CG  . LEU   B 135 ? 0.2236 0.1961 0.1749 -0.0402 0.0259  -0.0026 141 LEU   C CG  
2114 C  CD1 . LEU   B 135 ? 0.2398 0.2075 0.1772 -0.0461 0.0263  -0.0019 141 LEU   C CD1 
2115 C  CD2 . LEU   B 135 ? 0.2366 0.2121 0.1934 -0.0368 0.0241  -0.0041 141 LEU   C CD2 
2116 N  N   . TRP   B 136 ? 0.2134 0.1923 0.1922 -0.0351 0.0366  -0.0082 142 TRP   C N   
2117 C  CA  . TRP   B 136 ? 0.2273 0.2075 0.2123 -0.0360 0.0418  -0.0109 142 TRP   C CA  
2118 C  C   . TRP   B 136 ? 0.2461 0.2311 0.2450 -0.0314 0.0422  -0.0140 142 TRP   C C   
2119 O  O   . TRP   B 136 ? 0.2544 0.2414 0.2606 -0.0320 0.0467  -0.0172 142 TRP   C O   
2120 C  CB  . TRP   B 136 ? 0.2281 0.2068 0.2116 -0.0376 0.0406  -0.0077 142 TRP   C CB  
2121 C  CG  . TRP   B 136 ? 0.2245 0.2043 0.2120 -0.0336 0.0343  -0.0043 142 TRP   C CG  
2122 C  CD1 . TRP   B 136 ? 0.2243 0.2019 0.2059 -0.0331 0.0291  -0.0001 142 TRP   C CD1 
2123 C  CD2 . TRP   B 136 ? 0.2162 0.1996 0.2150 -0.0295 0.0328  -0.0052 142 TRP   C CD2 
2124 N  NE1 . TRP   B 136 ? 0.2256 0.2051 0.2142 -0.0290 0.0252  0.0013  142 TRP   C NE1 
2125 C  CE2 . TRP   B 136 ? 0.2202 0.2029 0.2185 -0.0270 0.0273  -0.0017 142 TRP   C CE2 
2126 C  CE3 . TRP   B 136 ? 0.2225 0.2096 0.2319 -0.0280 0.0354  -0.0086 142 TRP   C CE3 
2127 C  CZ2 . TRP   B 136 ? 0.2280 0.2130 0.2346 -0.0233 0.0247  -0.0019 142 TRP   C CZ2 
2128 C  CZ3 . TRP   B 136 ? 0.2307 0.2202 0.2484 -0.0245 0.0321  -0.0082 142 TRP   C CZ3 
2129 C  CH2 . TRP   B 136 ? 0.2296 0.2177 0.2450 -0.0224 0.0270  -0.0050 142 TRP   C CH2 
2130 N  N   . LEU   B 137 ? 0.2415 0.2282 0.2442 -0.0271 0.0374  -0.0131 143 LEU   C N   
2131 C  CA  . LEU   B 137 ? 0.2441 0.2343 0.2585 -0.0230 0.0370  -0.0155 143 LEU   C CA  
2132 C  C   . LEU   B 137 ? 0.2898 0.2806 0.3084 -0.0235 0.0421  -0.0201 143 LEU   C C   
2133 O  O   . LEU   B 137 ? 0.2782 0.2720 0.3080 -0.0210 0.0430  -0.0225 143 LEU   C O   
2134 C  CB  . LEU   B 137 ? 0.2216 0.2122 0.2365 -0.0192 0.0315  -0.0136 143 LEU   C CB  
2135 C  CG  . LEU   B 137 ? 0.2308 0.2217 0.2454 -0.0175 0.0268  -0.0101 143 LEU   C CG  
2136 C  CD1 . LEU   B 137 ? 0.2295 0.2206 0.2439 -0.0144 0.0226  -0.0089 143 LEU   C CD1 
2137 C  CD2 . LEU   B 137 ? 0.2334 0.2263 0.2564 -0.0161 0.0266  -0.0108 143 LEU   C CD2 
2138 N  N   . ASP   B 138 ? 0.3337 0.3214 0.3436 -0.0267 0.0452  -0.0213 144 ASP   C N   
2139 C  CA  . ASP   B 138 ? 0.3918 0.3791 0.4044 -0.0276 0.0506  -0.0260 144 ASP   C CA  
2140 C  C   . ASP   B 138 ? 0.4517 0.4386 0.4638 -0.0317 0.0579  -0.0291 144 ASP   C C   
2141 O  O   . ASP   B 138 ? 0.4721 0.4583 0.4859 -0.0328 0.0633  -0.0336 144 ASP   C O   
2142 C  CB  . ASP   B 138 ? 0.4343 0.4181 0.4375 -0.0289 0.0501  -0.0262 144 ASP   C CB  
2143 C  CG  . ASP   B 138 ? 0.4946 0.4792 0.5013 -0.0246 0.0447  -0.0247 144 ASP   C CG  
2144 O  OD1 . ASP   B 138 ? 0.5035 0.4906 0.5211 -0.0206 0.0435  -0.0256 144 ASP   C OD1 
2145 O  OD2 . ASP   B 138 ? 0.5398 0.5224 0.5383 -0.0255 0.0415  -0.0225 144 ASP   C OD2 
2146 N  N   . GLU   B 139 ? 0.4761 0.4632 0.4865 -0.0341 0.0586  -0.0273 145 GLU   C N   
2147 C  CA  . GLU   B 139 ? 0.5147 0.5014 0.5246 -0.0386 0.0661  -0.0302 145 GLU   C CA  
2148 C  C   . GLU   B 139 ? 0.5342 0.5248 0.5544 -0.0379 0.0665  -0.0298 145 GLU   C C   
2149 O  O   . GLU   B 139 ? 0.5518 0.5419 0.5708 -0.0422 0.0722  -0.0312 145 GLU   C O   
2150 C  CB  . GLU   B 139 ? 0.5672 0.5483 0.5599 -0.0447 0.0678  -0.0282 145 GLU   C CB  
2151 C  CG  . GLU   B 139 ? 0.6577 0.6366 0.6426 -0.0449 0.0611  -0.0221 145 GLU   C CG  
2152 C  CD  . GLU   B 139 ? 0.7766 0.7497 0.7444 -0.0494 0.0598  -0.0195 145 GLU   C CD  
2153 O  OE1 . GLU   B 139 ? 0.7960 0.7659 0.7555 -0.0524 0.0579  -0.0155 145 GLU   C OE1 
2154 O  OE2 . GLU   B 139 ? 0.8102 0.7816 0.7729 -0.0500 0.0602  -0.0213 145 GLU   C OE2 
2155 N  N1  . A1BN7 C .   ? 0.1931 0.1943 0.2294 -0.0033 0.0200  0.0157  201 A1BN7 A N1  
2156 C  C4  . A1BN7 C .   ? 0.1933 0.1914 0.2268 -0.0026 0.0202  0.0178  201 A1BN7 A C4  
2157 C  C5  . A1BN7 C .   ? 0.2182 0.2202 0.2512 -0.0017 0.0210  0.0159  201 A1BN7 A C5  
2158 C  C6  . A1BN7 C .   ? 0.2609 0.2598 0.2851 0.0010  0.0225  0.0180  201 A1BN7 A C6  
2159 C  C7  . A1BN7 C .   ? 0.2777 0.2768 0.2974 0.0029  0.0235  0.0175  201 A1BN7 A C7  
2160 C  C8  . A1BN7 C .   ? 0.2841 0.2829 0.3023 0.0051  0.0278  0.0200  201 A1BN7 A C8  
2161 C  C10 . A1BN7 C .   ? 0.1780 0.1808 0.2204 -0.0054 0.0182  0.0132  201 A1BN7 A C10 
2162 CL CL  . A1BN7 C .   ? 0.3396 0.3381 0.3557 0.0015  0.0163  0.0119  201 A1BN7 A CL  
2163 C  C9  . A1BN7 C .   ? 0.2990 0.2977 0.3149 0.0032  0.0207  0.0149  201 A1BN7 A C9  
2164 S  S   . A1BN7 C .   ? 0.2891 0.2870 0.2996 0.0060  0.0230  0.0152  201 A1BN7 A S   
2165 N  N2  . A1BN7 C .   ? 0.2807 0.2788 0.2937 0.0070  0.0281  0.0190  201 A1BN7 A N2  
2166 F  F   . A1BN7 C .   ? 0.2651 0.2628 0.2906 0.0016  0.0260  0.0213  201 A1BN7 A F   
2167 F  F1  . A1BN7 C .   ? 0.2784 0.2746 0.2974 0.0014  0.0194  0.0173  201 A1BN7 A F1  
2168 O  O1  . A1BN7 C .   ? 0.1980 0.2027 0.2341 -0.0021 0.0207  0.0144  201 A1BN7 A O1  
2169 C  C3  . A1BN7 C .   ? 0.1919 0.1889 0.2242 -0.0031 0.0168  0.0159  201 A1BN7 A C3  
2170 C  C2  . A1BN7 C .   ? 0.1920 0.1905 0.2304 -0.0052 0.0159  0.0135  201 A1BN7 A C2  
2171 C  C1  . A1BN7 C .   ? 0.1807 0.1817 0.2202 -0.0057 0.0156  0.0114  201 A1BN7 A C1  
2172 C  C   . A1BN7 C .   ? 0.1787 0.1802 0.2225 -0.0073 0.0142  0.0087  201 A1BN7 A C   
2173 O  O   . A1BN7 C .   ? 0.1770 0.1785 0.2264 -0.0086 0.0147  0.0086  201 A1BN7 A O   
2174 N  N   . A1BN7 C .   ? 0.1747 0.1759 0.2152 -0.0070 0.0125  0.0065  201 A1BN7 A N   
2176 N  N1  . A1BN7 E .   ? 0.2117 0.1875 0.2208 0.0061  0.0129  -0.0136 201 A1BN7 C N1  
2177 C  C4  . A1BN7 E .   ? 0.2068 0.1779 0.2122 0.0054  0.0116  -0.0155 201 A1BN7 C C4  
2178 C  C5  . A1BN7 E .   ? 0.2445 0.2214 0.2504 0.0051  0.0148  -0.0139 201 A1BN7 C C5  
2179 C  C6  . A1BN7 E .   ? 0.2887 0.2610 0.2848 0.0030  0.0155  -0.0157 201 A1BN7 C C6  
2180 C  C7  . A1BN7 E .   ? 0.3076 0.2808 0.2998 0.0016  0.0174  -0.0153 201 A1BN7 C C7  
2181 C  C8  . A1BN7 E .   ? 0.3097 0.2812 0.2978 0.0003  0.0218  -0.0176 201 A1BN7 C C8  
2182 C  C10 . A1BN7 E .   ? 0.1818 0.1609 0.1985 0.0075  0.0117  -0.0114 201 A1BN7 C C10 
2183 CL CL  . A1BN7 E .   ? 0.3865 0.3635 0.3811 0.0017  0.0109  -0.0101 201 A1BN7 C CL  
2184 C  C9  . A1BN7 E .   ? 0.3375 0.3124 0.3287 0.0010  0.0153  -0.0128 201 A1BN7 C C9  
2185 S  S   . A1BN7 E .   ? 0.3316 0.3056 0.3169 -0.0012 0.0184  -0.0131 201 A1BN7 C S   
2186 N  N2  . A1BN7 E .   ? 0.3040 0.2758 0.2878 -0.0015 0.0229  -0.0166 201 A1BN7 C N2  
2187 F  F   . A1BN7 E .   ? 0.3065 0.2755 0.3009 0.0030  0.0181  -0.0188 201 A1BN7 C F   
2188 F  F1  . A1BN7 E .   ? 0.2950 0.2650 0.2874 0.0023  0.0116  -0.0149 201 A1BN7 C F1  
2189 O  O1  . A1BN7 E .   ? 0.2133 0.1942 0.2232 0.0055  0.0158  -0.0126 201 A1BN7 C O1  
2190 C  C3  . A1BN7 E .   ? 0.1973 0.1688 0.2037 0.0050  0.0078  -0.0136 201 A1BN7 C C3  
2191 C  C2  . A1BN7 E .   ? 0.1871 0.1618 0.2007 0.0062  0.0073  -0.0113 201 A1BN7 C C2  
2192 C  C1  . A1BN7 E .   ? 0.1752 0.1541 0.1914 0.0068  0.0084  -0.0095 201 A1BN7 C C1  
2193 C  C   . A1BN7 E .   ? 0.1694 0.1506 0.1913 0.0076  0.0074  -0.0070 201 A1BN7 C C   
2194 O  O   . A1BN7 E .   ? 0.1633 0.1434 0.1895 0.0089  0.0078  -0.0070 201 A1BN7 C O   
2195 N  N   . A1BN7 E .   ? 0.1786 0.1625 0.2004 0.0068  0.0062  -0.0049 201 A1BN7 C N   
# 
