data_7HVY
# 
_entry.id   7HVY 
# 
_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   7HVY         pdb_00007hvy 10.2210/pdb7hvy/pdb 
WWPDB D_1001407998 ?            ?                   
# 
_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                        7HVY 
_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,4R)-1-[(2-methoxyphenyl)acetyl]-4-methylpyrrolidine-3-carboxamide' 276.331   1   ?         ? ? ? 
3 non-polymer syn GLYCEROL                                                                92.094    1   ?         ? ? ? 
4 non-polymer syn 'ZINC ION'                                                              65.409    2   ?         ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                                    78.133    1   ?         ? ? ? 
6 water       nat water                                                                   18.015    309 ?         ? ? ? 
# 
_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,4R)-1-[(2-methoxyphenyl)acetyl]-4-methylpyrrolidine-3-carboxamide' A1BP2 
3 GLYCEROL                                                                GOL   
4 'ZINC ION'                                                              ZN    
5 'DIMETHYL SULFOXIDE'                                                    DMS   
6 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 
A1BP2 non-polymer         . '(3S,4R)-1-[(2-methoxyphenyl)acetyl]-4-methylpyrrolidine-3-carboxamide' ? 'C15 H20 N2 O3'  276.331 
ALA   'L-peptide linking' y ALANINE                                                                 ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                              ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                         ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                    ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                               ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                         ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                 ? 'C2 H5 N O2'     75.067  
GOL   non-polymer         . GLYCEROL                                                                
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS   'L-peptide linking' y HISTIDINE                                                               ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                   ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                              ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                 ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                  ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                              ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                           ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                 ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                  ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                               ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                              ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                  ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                              ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 146 GLU GLU C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BP2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BP2 
_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 A1BP2 1   201 201 A1BP2 LIG A . 
D 3 GOL   1   202 202 GOL   GOL A . 
E 4 ZN    1   203 1   ZN    ZN  A . 
F 4 ZN    1   201 1   ZN    ZN  C . 
G 5 DMS   1   202 1   DMS   DMS C . 
H 6 HOH   1   301 298 HOH   HOH A . 
H 6 HOH   2   302 165 HOH   HOH A . 
H 6 HOH   3   303 297 HOH   HOH A . 
H 6 HOH   4   304 263 HOH   HOH A . 
H 6 HOH   5   305 265 HOH   HOH A . 
H 6 HOH   6   306 305 HOH   HOH A . 
H 6 HOH   7   307 68  HOH   HOH A . 
H 6 HOH   8   308 171 HOH   HOH A . 
H 6 HOH   9   309 290 HOH   HOH A . 
H 6 HOH   10  310 299 HOH   HOH A . 
H 6 HOH   11  311 227 HOH   HOH A . 
H 6 HOH   12  312 193 HOH   HOH A . 
H 6 HOH   13  313 268 HOH   HOH A . 
H 6 HOH   14  314 99  HOH   HOH A . 
H 6 HOH   15  315 259 HOH   HOH A . 
H 6 HOH   16  316 314 HOH   HOH A . 
H 6 HOH   17  317 192 HOH   HOH A . 
H 6 HOH   18  318 252 HOH   HOH A . 
H 6 HOH   19  319 249 HOH   HOH A . 
H 6 HOH   20  320 147 HOH   HOH A . 
H 6 HOH   21  321 264 HOH   HOH A . 
H 6 HOH   22  322 167 HOH   HOH A . 
H 6 HOH   23  323 133 HOH   HOH A . 
H 6 HOH   24  324 18  HOH   HOH A . 
H 6 HOH   25  325 250 HOH   HOH A . 
H 6 HOH   26  326 164 HOH   HOH A . 
H 6 HOH   27  327 77  HOH   HOH A . 
H 6 HOH   28  328 8   HOH   HOH A . 
H 6 HOH   29  329 312 HOH   HOH A . 
H 6 HOH   30  330 121 HOH   HOH A . 
H 6 HOH   31  331 78  HOH   HOH A . 
H 6 HOH   32  332 262 HOH   HOH A . 
H 6 HOH   33  333 73  HOH   HOH A . 
H 6 HOH   34  334 123 HOH   HOH A . 
H 6 HOH   35  335 258 HOH   HOH A . 
H 6 HOH   36  336 230 HOH   HOH A . 
H 6 HOH   37  337 205 HOH   HOH A . 
H 6 HOH   38  338 291 HOH   HOH A . 
H 6 HOH   39  339 157 HOH   HOH A . 
H 6 HOH   40  340 248 HOH   HOH A . 
H 6 HOH   41  341 281 HOH   HOH A . 
H 6 HOH   42  342 44  HOH   HOH A . 
H 6 HOH   43  343 17  HOH   HOH A . 
H 6 HOH   44  344 53  HOH   HOH A . 
H 6 HOH   45  345 235 HOH   HOH A . 
H 6 HOH   46  346 179 HOH   HOH A . 
H 6 HOH   47  347 4   HOH   HOH A . 
H 6 HOH   48  348 61  HOH   HOH A . 
H 6 HOH   49  349 101 HOH   HOH A . 
H 6 HOH   50  350 31  HOH   HOH A . 
H 6 HOH   51  351 69  HOH   HOH A . 
H 6 HOH   52  352 304 HOH   HOH A . 
H 6 HOH   53  353 292 HOH   HOH A . 
H 6 HOH   54  354 124 HOH   HOH A . 
H 6 HOH   55  355 283 HOH   HOH A . 
H 6 HOH   56  356 26  HOH   HOH A . 
H 6 HOH   57  357 287 HOH   HOH A . 
H 6 HOH   58  358 138 HOH   HOH A . 
H 6 HOH   59  359 50  HOH   HOH A . 
H 6 HOH   60  360 104 HOH   HOH A . 
H 6 HOH   61  361 241 HOH   HOH A . 
H 6 HOH   62  362 118 HOH   HOH A . 
H 6 HOH   63  363 80  HOH   HOH A . 
H 6 HOH   64  364 137 HOH   HOH A . 
H 6 HOH   65  365 170 HOH   HOH A . 
H 6 HOH   66  366 52  HOH   HOH A . 
H 6 HOH   67  367 266 HOH   HOH A . 
H 6 HOH   68  368 6   HOH   HOH A . 
H 6 HOH   69  369 62  HOH   HOH A . 
H 6 HOH   70  370 55  HOH   HOH A . 
H 6 HOH   71  371 45  HOH   HOH A . 
H 6 HOH   72  372 16  HOH   HOH A . 
H 6 HOH   73  373 214 HOH   HOH A . 
H 6 HOH   74  374 13  HOH   HOH A . 
H 6 HOH   75  375 36  HOH   HOH A . 
H 6 HOH   76  376 156 HOH   HOH A . 
H 6 HOH   77  377 59  HOH   HOH A . 
H 6 HOH   78  378 43  HOH   HOH A . 
H 6 HOH   79  379 238 HOH   HOH A . 
H 6 HOH   80  380 109 HOH   HOH A . 
H 6 HOH   81  381 181 HOH   HOH A . 
H 6 HOH   82  382 51  HOH   HOH A . 
H 6 HOH   83  383 174 HOH   HOH A . 
H 6 HOH   84  384 92  HOH   HOH A . 
H 6 HOH   85  385 135 HOH   HOH A . 
H 6 HOH   86  386 131 HOH   HOH A . 
H 6 HOH   87  387 286 HOH   HOH A . 
H 6 HOH   88  388 296 HOH   HOH A . 
H 6 HOH   89  389 173 HOH   HOH A . 
H 6 HOH   90  390 218 HOH   HOH A . 
H 6 HOH   91  391 27  HOH   HOH A . 
H 6 HOH   92  392 232 HOH   HOH A . 
H 6 HOH   93  393 47  HOH   HOH A . 
H 6 HOH   94  394 163 HOH   HOH A . 
H 6 HOH   95  395 58  HOH   HOH A . 
H 6 HOH   96  396 64  HOH   HOH A . 
H 6 HOH   97  397 129 HOH   HOH A . 
H 6 HOH   98  398 177 HOH   HOH A . 
H 6 HOH   99  399 89  HOH   HOH A . 
H 6 HOH   100 400 93  HOH   HOH A . 
H 6 HOH   101 401 149 HOH   HOH A . 
H 6 HOH   102 402 140 HOH   HOH A . 
H 6 HOH   103 403 213 HOH   HOH A . 
H 6 HOH   104 404 40  HOH   HOH A . 
H 6 HOH   105 405 141 HOH   HOH A . 
H 6 HOH   106 406 288 HOH   HOH A . 
H 6 HOH   107 407 212 HOH   HOH A . 
H 6 HOH   108 408 25  HOH   HOH A . 
H 6 HOH   109 409 105 HOH   HOH A . 
H 6 HOH   110 410 70  HOH   HOH A . 
H 6 HOH   111 411 143 HOH   HOH A . 
H 6 HOH   112 412 289 HOH   HOH A . 
H 6 HOH   113 413 201 HOH   HOH A . 
H 6 HOH   114 414 107 HOH   HOH A . 
H 6 HOH   115 415 81  HOH   HOH A . 
H 6 HOH   116 416 224 HOH   HOH A . 
H 6 HOH   117 417 15  HOH   HOH A . 
H 6 HOH   118 418 236 HOH   HOH A . 
H 6 HOH   119 419 14  HOH   HOH A . 
H 6 HOH   120 420 72  HOH   HOH A . 
H 6 HOH   121 421 9   HOH   HOH A . 
H 6 HOH   122 422 189 HOH   HOH A . 
H 6 HOH   123 423 302 HOH   HOH A . 
H 6 HOH   124 424 60  HOH   HOH A . 
H 6 HOH   125 425 273 HOH   HOH A . 
H 6 HOH   126 426 146 HOH   HOH A . 
H 6 HOH   127 427 115 HOH   HOH A . 
H 6 HOH   128 428 114 HOH   HOH A . 
H 6 HOH   129 429 223 HOH   HOH A . 
H 6 HOH   130 430 282 HOH   HOH A . 
H 6 HOH   131 431 228 HOH   HOH A . 
H 6 HOH   132 432 301 HOH   HOH A . 
H 6 HOH   133 433 303 HOH   HOH A . 
H 6 HOH   134 434 295 HOH   HOH A . 
H 6 HOH   135 435 300 HOH   HOH A . 
H 6 HOH   136 436 275 HOH   HOH A . 
H 6 HOH   137 437 277 HOH   HOH A . 
H 6 HOH   138 438 294 HOH   HOH A . 
H 6 HOH   139 439 254 HOH   HOH A . 
H 6 HOH   140 440 279 HOH   HOH A . 
H 6 HOH   141 441 127 HOH   HOH A . 
H 6 HOH   142 442 216 HOH   HOH A . 
H 6 HOH   143 443 154 HOH   HOH A . 
H 6 HOH   144 444 158 HOH   HOH A . 
H 6 HOH   145 445 125 HOH   HOH A . 
H 6 HOH   146 446 270 HOH   HOH A . 
H 6 HOH   147 447 256 HOH   HOH A . 
H 6 HOH   148 448 196 HOH   HOH A . 
H 6 HOH   149 449 284 HOH   HOH A . 
H 6 HOH   150 450 231 HOH   HOH A . 
H 6 HOH   151 451 148 HOH   HOH A . 
H 6 HOH   152 452 108 HOH   HOH A . 
H 6 HOH   153 453 208 HOH   HOH A . 
H 6 HOH   154 454 76  HOH   HOH A . 
H 6 HOH   155 455 136 HOH   HOH A . 
H 6 HOH   156 456 274 HOH   HOH A . 
H 6 HOH   157 457 194 HOH   HOH A . 
H 6 HOH   158 458 185 HOH   HOH A . 
H 6 HOH   159 459 175 HOH   HOH A . 
I 6 HOH   1   301 220 HOH   HOH C . 
I 6 HOH   2   302 82  HOH   HOH C . 
I 6 HOH   3   303 106 HOH   HOH C . 
I 6 HOH   4   304 206 HOH   HOH C . 
I 6 HOH   5   305 85  HOH   HOH C . 
I 6 HOH   6   306 32  HOH   HOH C . 
I 6 HOH   7   307 63  HOH   HOH C . 
I 6 HOH   8   308 308 HOH   HOH C . 
I 6 HOH   9   309 139 HOH   HOH C . 
I 6 HOH   10  310 278 HOH   HOH C . 
I 6 HOH   11  311 3   HOH   HOH C . 
I 6 HOH   12  312 151 HOH   HOH C . 
I 6 HOH   13  313 225 HOH   HOH C . 
I 6 HOH   14  314 306 HOH   HOH C . 
I 6 HOH   15  315 222 HOH   HOH C . 
I 6 HOH   16  316 260 HOH   HOH C . 
I 6 HOH   17  317 30  HOH   HOH C . 
I 6 HOH   18  318 229 HOH   HOH C . 
I 6 HOH   19  319 71  HOH   HOH C . 
I 6 HOH   20  320 117 HOH   HOH C . 
I 6 HOH   21  321 183 HOH   HOH C . 
I 6 HOH   22  322 130 HOH   HOH C . 
I 6 HOH   23  323 195 HOH   HOH C . 
I 6 HOH   24  324 49  HOH   HOH C . 
I 6 HOH   25  325 255 HOH   HOH C . 
I 6 HOH   26  326 217 HOH   HOH C . 
I 6 HOH   27  327 128 HOH   HOH C . 
I 6 HOH   28  328 152 HOH   HOH C . 
I 6 HOH   29  329 88  HOH   HOH C . 
I 6 HOH   30  330 90  HOH   HOH C . 
I 6 HOH   31  331 21  HOH   HOH C . 
I 6 HOH   32  332 57  HOH   HOH C . 
I 6 HOH   33  333 200 HOH   HOH C . 
I 6 HOH   34  334 1   HOH   HOH C . 
I 6 HOH   35  335 11  HOH   HOH C . 
I 6 HOH   36  336 91  HOH   HOH C . 
I 6 HOH   37  337 199 HOH   HOH C . 
I 6 HOH   38  338 293 HOH   HOH C . 
I 6 HOH   39  339 41  HOH   HOH C . 
I 6 HOH   40  340 150 HOH   HOH C . 
I 6 HOH   41  341 178 HOH   HOH C . 
I 6 HOH   42  342 197 HOH   HOH C . 
I 6 HOH   43  343 83  HOH   HOH C . 
I 6 HOH   44  344 34  HOH   HOH C . 
I 6 HOH   45  345 10  HOH   HOH C . 
I 6 HOH   46  346 103 HOH   HOH C . 
I 6 HOH   47  347 261 HOH   HOH C . 
I 6 HOH   48  348 38  HOH   HOH C . 
I 6 HOH   49  349 134 HOH   HOH C . 
I 6 HOH   50  350 113 HOH   HOH C . 
I 6 HOH   51  351 202 HOH   HOH C . 
I 6 HOH   52  352 209 HOH   HOH C . 
I 6 HOH   53  353 219 HOH   HOH C . 
I 6 HOH   54  354 48  HOH   HOH C . 
I 6 HOH   55  355 67  HOH   HOH C . 
I 6 HOH   56  356 215 HOH   HOH C . 
I 6 HOH   57  357 87  HOH   HOH C . 
I 6 HOH   58  358 122 HOH   HOH C . 
I 6 HOH   59  359 111 HOH   HOH C . 
I 6 HOH   60  360 37  HOH   HOH C . 
I 6 HOH   61  361 280 HOH   HOH C . 
I 6 HOH   62  362 311 HOH   HOH C . 
I 6 HOH   63  363 56  HOH   HOH C . 
I 6 HOH   64  364 66  HOH   HOH C . 
I 6 HOH   65  365 253 HOH   HOH C . 
I 6 HOH   66  366 233 HOH   HOH C . 
I 6 HOH   67  367 191 HOH   HOH C . 
I 6 HOH   68  368 7   HOH   HOH C . 
I 6 HOH   69  369 246 HOH   HOH C . 
I 6 HOH   70  370 19  HOH   HOH C . 
I 6 HOH   71  371 313 HOH   HOH C . 
I 6 HOH   72  372 39  HOH   HOH C . 
I 6 HOH   73  373 23  HOH   HOH C . 
I 6 HOH   74  374 74  HOH   HOH C . 
I 6 HOH   75  375 169 HOH   HOH C . 
I 6 HOH   76  376 42  HOH   HOH C . 
I 6 HOH   77  377 168 HOH   HOH C . 
I 6 HOH   78  378 20  HOH   HOH C . 
I 6 HOH   79  379 5   HOH   HOH C . 
I 6 HOH   80  380 112 HOH   HOH C . 
I 6 HOH   81  381 54  HOH   HOH C . 
I 6 HOH   82  382 22  HOH   HOH C . 
I 6 HOH   83  383 29  HOH   HOH C . 
I 6 HOH   84  384 79  HOH   HOH C . 
I 6 HOH   85  385 186 HOH   HOH C . 
I 6 HOH   86  386 75  HOH   HOH C . 
I 6 HOH   87  387 166 HOH   HOH C . 
I 6 HOH   88  388 155 HOH   HOH C . 
I 6 HOH   89  389 84  HOH   HOH C . 
I 6 HOH   90  390 102 HOH   HOH C . 
I 6 HOH   91  391 276 HOH   HOH C . 
I 6 HOH   92  392 153 HOH   HOH C . 
I 6 HOH   93  393 269 HOH   HOH C . 
I 6 HOH   94  394 132 HOH   HOH C . 
I 6 HOH   95  395 35  HOH   HOH C . 
I 6 HOH   96  396 142 HOH   HOH C . 
I 6 HOH   97  397 207 HOH   HOH C . 
I 6 HOH   98  398 310 HOH   HOH C . 
I 6 HOH   99  399 180 HOH   HOH C . 
I 6 HOH   100 400 95  HOH   HOH C . 
I 6 HOH   101 401 159 HOH   HOH C . 
I 6 HOH   102 402 65  HOH   HOH C . 
I 6 HOH   103 403 28  HOH   HOH C . 
I 6 HOH   104 404 243 HOH   HOH C . 
I 6 HOH   105 405 100 HOH   HOH C . 
I 6 HOH   106 406 190 HOH   HOH C . 
I 6 HOH   107 407 182 HOH   HOH C . 
I 6 HOH   108 408 119 HOH   HOH C . 
I 6 HOH   109 409 237 HOH   HOH C . 
I 6 HOH   110 410 2   HOH   HOH C . 
I 6 HOH   111 411 24  HOH   HOH C . 
I 6 HOH   112 412 116 HOH   HOH C . 
I 6 HOH   113 413 46  HOH   HOH C . 
I 6 HOH   114 414 12  HOH   HOH C . 
I 6 HOH   115 415 210 HOH   HOH C . 
I 6 HOH   116 416 96  HOH   HOH C . 
I 6 HOH   117 417 211 HOH   HOH C . 
I 6 HOH   118 418 110 HOH   HOH C . 
I 6 HOH   119 419 172 HOH   HOH C . 
I 6 HOH   120 420 162 HOH   HOH C . 
I 6 HOH   121 421 234 HOH   HOH C . 
I 6 HOH   122 422 271 HOH   HOH C . 
I 6 HOH   123 423 161 HOH   HOH C . 
I 6 HOH   124 424 86  HOH   HOH C . 
I 6 HOH   125 425 309 HOH   HOH C . 
I 6 HOH   126 426 285 HOH   HOH C . 
I 6 HOH   127 427 94  HOH   HOH C . 
I 6 HOH   128 428 272 HOH   HOH C . 
I 6 HOH   129 429 98  HOH   HOH C . 
I 6 HOH   130 430 247 HOH   HOH C . 
I 6 HOH   131 431 184 HOH   HOH C . 
I 6 HOH   132 432 226 HOH   HOH C . 
I 6 HOH   133 433 198 HOH   HOH C . 
I 6 HOH   134 434 203 HOH   HOH C . 
I 6 HOH   135 435 126 HOH   HOH C . 
I 6 HOH   136 436 257 HOH   HOH C . 
I 6 HOH   137 437 267 HOH   HOH C . 
I 6 HOH   138 438 307 HOH   HOH C . 
I 6 HOH   139 439 240 HOH   HOH C . 
I 6 HOH   140 440 239 HOH   HOH C . 
I 6 HOH   141 441 160 HOH   HOH C . 
I 6 HOH   142 442 244 HOH   HOH C . 
I 6 HOH   143 443 245 HOH   HOH C . 
I 6 HOH   144 444 120 HOH   HOH C . 
I 6 HOH   145 445 204 HOH   HOH C . 
I 6 HOH   146 446 221 HOH   HOH C . 
I 6 HOH   147 447 187 HOH   HOH C . 
I 6 HOH   148 448 251 HOH   HOH C . 
I 6 HOH   149 449 188 HOH   HOH C . 
I 6 HOH   150 450 242 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           7HVY 
_cell.length_a           86.689 
_cell.length_b           57.243 
_cell.length_c           64.794 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.91 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HVY 
_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          7HVY 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.52 
_exptl_crystal.density_percent_sol   51.18 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-14 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92201 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HVY 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             39.27 
_reflns.d_resolution_high            1.19 
_reflns.number_obs                   83867 
_reflns.percent_possible_obs         83.0 
_reflns.pdbx_Rmerge_I_obs            0.052 
_reflns.pdbx_netI_over_sigmaI        18.3 
_reflns.pdbx_redundancy              5.3 
_reflns.pdbx_Rrim_I_all              0.056 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     448515 
_reflns.pdbx_chi_squared             0.84 
_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                  1.19 
_reflns_shell.d_res_low                   1.21 
_reflns_shell.number_measured_all         1537 
_reflns_shell.number_unique_obs           1151 
_reflns_shell.Rmerge_I_obs                0.927 
_reflns_shell.pdbx_chi_squared            0.42 
_reflns_shell.pdbx_redundancy             1.3 
_reflns_shell.percent_possible_obs        23.1 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.4 
_reflns_shell.pdbx_Rrim_I_all             1.280 
_reflns_shell.pdbx_Rpim_I_all             0.879 
_reflns_shell.pdbx_CC_half                0.306 
_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                                 7HVY 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     83730 
_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                             39.27 
_refine.ls_d_res_high                            1.190 
_refine.ls_percent_reflns_obs                    82.8 
_refine.ls_R_factor_obs                          0.1972 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1965 
_refine.ls_R_factor_R_free                       0.2098 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  4189 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.937 
_refine.correlation_coeff_Fo_to_Fc_free          0.955 
_refine.B_iso_mean                               20.42 
_refine.aniso_B[1][1]                            -1.51420 
_refine.aniso_B[2][2]                            -0.21220 
_refine.aniso_B[3][3]                            1.72640 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.25590 
_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             0.046 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.046 
_refine.pdbx_overall_SU_R_Blow_DPI               0.048 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.048 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HVY 
_refine_analyze.Luzzati_coordinate_error_obs    0.17 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_refine_hist.number_atoms_solvent             309 
_refine_hist.number_atoms_total               2507 
_refine_hist.d_res_high                       1.190 
_refine_hist.d_res_low                        39.27 
# 
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                  0.014 ? 2.00  2277 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.14  ? 2.00  3105 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  766  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  408  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2277 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.00  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.58 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  283  '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  2053 '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                       1.19 
_refine_ls_shell.d_res_low                        1.22 
_refine_ls_shell.number_reflns_R_work             1589 
_refine_ls_shell.R_factor_R_work                  0.3527 
_refine_ls_shell.percent_reflns_obs               23.24 
_refine_ls_shell.R_factor_R_free                  0.4114 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.13 
_refine_ls_shell.number_reflns_R_free             86 
_refine_ls_shell.number_reflns_all                1675 
_refine_ls_shell.R_factor_all                     0.3557 
# 
_struct.entry_id                  7HVY 
_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-0032512-001 (A71EV2A-x3634)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HVY 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
# 
_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 7HVY A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HVY C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,H 
2 1 B,F,G,I   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 56  A ZN 203 1_555 ? ? ? ? ? ? ? 2.398 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 58  A ZN 203 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 116 A ZN 203 1_555 ? ? ? ? ? ? ? 2.172 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 E ZN . ZN ? ? A HIS 118 A ZN 203 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
# 
_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 ? E ZN . ? A ZN 203 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 107.7 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 104.2 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.6 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 105.3 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.5 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 120.7 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.6 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.6 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.9 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 105.5 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.3 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 115.3 ? 
# 
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 TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7HVY 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    423 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    455 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.11 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -105.86 41.12  
2 1 ASN C 14  ? ? -106.15 42.51  
3 1 SER C 105 ? ? -160.55 113.28 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 14.8740 8.0468   14.4030 -0.0142 -0.0241 0.0007 0.0129 0.0020 0.0054 1.5040 0.6892 0.7790 0.8308  
-0.6578 -0.4448 0.0185 0.0636 0.1181 0.0614 0.0436 0.0245 -0.0369 -0.0667 -0.0621 
'X-RAY DIFFRACTION' 2 ? refined 25.7861 -20.2377 17.7453 -0.0238 -0.0148 0.0171 0.0102 0.0031 0.0242 0.6461 0.8731 0.2328 -0.0257 
-0.1633 -0.1640 0.0206 0.0254 0.1285 0.0321 0.0392 0.0458 0.0351  0.0059  -0.0598 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BP2 N1   N  N N 1   
A1BP2 C4   C  Y N 2   
A1BP2 C5   C  Y N 3   
A1BP2 C6   C  Y N 4   
A1BP2 C7   C  N N 5   
A1BP2 C8   C  N N 6   
A1BP2 C10  C  N R 7   
A1BP2 C13  C  N N 8   
A1BP2 O2   O  N N 9   
A1BP2 C11  C  N N 10  
A1BP2 C9   C  N N 11  
A1BP2 C12  C  N R 12  
A1BP2 C14  C  N N 13  
A1BP2 N    N  N N 14  
A1BP2 O1   O  N N 15  
A1BP2 C1   C  Y N 16  
A1BP2 O    O  N N 17  
A1BP2 C    C  N N 18  
A1BP2 C3   C  Y N 19  
A1BP2 C2   C  Y N 20  
A1BP2 H14  H  N N 21  
A1BP2 H13  H  N N 22  
A1BP2 H7   H  N N 23  
A1BP2 H8   H  N N 24  
A1BP2 H9   H  N N 25  
A1BP2 H10  H  N N 26  
A1BP2 H    H  N N 27  
A1BP2 H15  H  N N 28  
A1BP2 H16  H  N N 29  
A1BP2 H17  H  N N 30  
A1BP2 H12  H  N N 31  
A1BP2 H11  H  N N 32  
A1BP2 H1   H  N N 33  
A1BP2 H19  H  N N 34  
A1BP2 H18  H  N N 35  
A1BP2 H2   H  N N 36  
A1BP2 H3   H  N N 37  
A1BP2 H4   H  N N 38  
A1BP2 H6   H  N N 39  
A1BP2 H5   H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CYS   N    N  N N 114 
CYS   CA   C  N R 115 
CYS   C    C  N N 116 
CYS   O    O  N N 117 
CYS   CB   C  N N 118 
CYS   SG   S  N N 119 
CYS   OXT  O  N N 120 
CYS   H    H  N N 121 
CYS   H2   H  N N 122 
CYS   HA   H  N N 123 
CYS   HB2  H  N N 124 
CYS   HB3  H  N N 125 
CYS   HG   H  N N 126 
CYS   HXT  H  N N 127 
DMS   S    S  N N 128 
DMS   O    O  N N 129 
DMS   C1   C  N N 130 
DMS   C2   C  N N 131 
DMS   H11  H  N N 132 
DMS   H12  H  N N 133 
DMS   H13  H  N N 134 
DMS   H21  H  N N 135 
DMS   H22  H  N N 136 
DMS   H23  H  N N 137 
GLN   N    N  N N 138 
GLN   CA   C  N S 139 
GLN   C    C  N N 140 
GLN   O    O  N N 141 
GLN   CB   C  N N 142 
GLN   CG   C  N N 143 
GLN   CD   C  N N 144 
GLN   OE1  O  N N 145 
GLN   NE2  N  N N 146 
GLN   OXT  O  N N 147 
GLN   H    H  N N 148 
GLN   H2   H  N N 149 
GLN   HA   H  N N 150 
GLN   HB2  H  N N 151 
GLN   HB3  H  N N 152 
GLN   HG2  H  N N 153 
GLN   HG3  H  N N 154 
GLN   HE21 H  N N 155 
GLN   HE22 H  N N 156 
GLN   HXT  H  N N 157 
GLU   N    N  N N 158 
GLU   CA   C  N S 159 
GLU   C    C  N N 160 
GLU   O    O  N N 161 
GLU   CB   C  N N 162 
GLU   CG   C  N N 163 
GLU   CD   C  N N 164 
GLU   OE1  O  N N 165 
GLU   OE2  O  N N 166 
GLU   OXT  O  N N 167 
GLU   H    H  N N 168 
GLU   H2   H  N N 169 
GLU   HA   H  N N 170 
GLU   HB2  H  N N 171 
GLU   HB3  H  N N 172 
GLU   HG2  H  N N 173 
GLU   HG3  H  N N 174 
GLU   HE2  H  N N 175 
GLU   HXT  H  N N 176 
GLY   N    N  N N 177 
GLY   CA   C  N N 178 
GLY   C    C  N N 179 
GLY   O    O  N N 180 
GLY   OXT  O  N N 181 
GLY   H    H  N N 182 
GLY   H2   H  N N 183 
GLY   HA2  H  N N 184 
GLY   HA3  H  N N 185 
GLY   HXT  H  N N 186 
GOL   C1   C  N N 187 
GOL   O1   O  N N 188 
GOL   C2   C  N N 189 
GOL   O2   O  N N 190 
GOL   C3   C  N N 191 
GOL   O3   O  N N 192 
GOL   H11  H  N N 193 
GOL   H12  H  N N 194 
GOL   HO1  H  N N 195 
GOL   H2   H  N N 196 
GOL   HO2  H  N N 197 
GOL   H31  H  N N 198 
GOL   H32  H  N N 199 
GOL   HO3  H  N N 200 
HIS   N    N  N N 201 
HIS   CA   C  N S 202 
HIS   C    C  N N 203 
HIS   O    O  N N 204 
HIS   CB   C  N N 205 
HIS   CG   C  Y N 206 
HIS   ND1  N  Y N 207 
HIS   CD2  C  Y N 208 
HIS   CE1  C  Y N 209 
HIS   NE2  N  Y N 210 
HIS   OXT  O  N N 211 
HIS   H    H  N N 212 
HIS   H2   H  N N 213 
HIS   HA   H  N N 214 
HIS   HB2  H  N N 215 
HIS   HB3  H  N N 216 
HIS   HD1  H  N N 217 
HIS   HD2  H  N N 218 
HIS   HE1  H  N N 219 
HIS   HE2  H  N N 220 
HIS   HXT  H  N N 221 
HOH   O    O  N N 222 
HOH   H1   H  N N 223 
HOH   H2   H  N N 224 
ILE   N    N  N N 225 
ILE   CA   C  N S 226 
ILE   C    C  N N 227 
ILE   O    O  N N 228 
ILE   CB   C  N S 229 
ILE   CG1  C  N N 230 
ILE   CG2  C  N N 231 
ILE   CD1  C  N N 232 
ILE   OXT  O  N N 233 
ILE   H    H  N N 234 
ILE   H2   H  N N 235 
ILE   HA   H  N N 236 
ILE   HB   H  N N 237 
ILE   HG12 H  N N 238 
ILE   HG13 H  N N 239 
ILE   HG21 H  N N 240 
ILE   HG22 H  N N 241 
ILE   HG23 H  N N 242 
ILE   HD11 H  N N 243 
ILE   HD12 H  N N 244 
ILE   HD13 H  N N 245 
ILE   HXT  H  N N 246 
LEU   N    N  N N 247 
LEU   CA   C  N S 248 
LEU   C    C  N N 249 
LEU   O    O  N N 250 
LEU   CB   C  N N 251 
LEU   CG   C  N N 252 
LEU   CD1  C  N N 253 
LEU   CD2  C  N N 254 
LEU   OXT  O  N N 255 
LEU   H    H  N N 256 
LEU   H2   H  N N 257 
LEU   HA   H  N N 258 
LEU   HB2  H  N N 259 
LEU   HB3  H  N N 260 
LEU   HG   H  N N 261 
LEU   HD11 H  N N 262 
LEU   HD12 H  N N 263 
LEU   HD13 H  N N 264 
LEU   HD21 H  N N 265 
LEU   HD22 H  N N 266 
LEU   HD23 H  N N 267 
LEU   HXT  H  N N 268 
LYS   N    N  N N 269 
LYS   CA   C  N S 270 
LYS   C    C  N N 271 
LYS   O    O  N N 272 
LYS   CB   C  N N 273 
LYS   CG   C  N N 274 
LYS   CD   C  N N 275 
LYS   CE   C  N N 276 
LYS   NZ   N  N N 277 
LYS   OXT  O  N N 278 
LYS   H    H  N N 279 
LYS   H2   H  N N 280 
LYS   HA   H  N N 281 
LYS   HB2  H  N N 282 
LYS   HB3  H  N N 283 
LYS   HG2  H  N N 284 
LYS   HG3  H  N N 285 
LYS   HD2  H  N N 286 
LYS   HD3  H  N N 287 
LYS   HE2  H  N N 288 
LYS   HE3  H  N N 289 
LYS   HZ1  H  N N 290 
LYS   HZ2  H  N N 291 
LYS   HZ3  H  N N 292 
LYS   HXT  H  N N 293 
MET   N    N  N N 294 
MET   CA   C  N S 295 
MET   C    C  N N 296 
MET   O    O  N N 297 
MET   CB   C  N N 298 
MET   CG   C  N N 299 
MET   SD   S  N N 300 
MET   CE   C  N N 301 
MET   OXT  O  N N 302 
MET   H    H  N N 303 
MET   H2   H  N N 304 
MET   HA   H  N N 305 
MET   HB2  H  N N 306 
MET   HB3  H  N N 307 
MET   HG2  H  N N 308 
MET   HG3  H  N N 309 
MET   HE1  H  N N 310 
MET   HE2  H  N N 311 
MET   HE3  H  N N 312 
MET   HXT  H  N N 313 
PHE   N    N  N N 314 
PHE   CA   C  N S 315 
PHE   C    C  N N 316 
PHE   O    O  N N 317 
PHE   CB   C  N N 318 
PHE   CG   C  Y N 319 
PHE   CD1  C  Y N 320 
PHE   CD2  C  Y N 321 
PHE   CE1  C  Y N 322 
PHE   CE2  C  Y N 323 
PHE   CZ   C  Y N 324 
PHE   OXT  O  N N 325 
PHE   H    H  N N 326 
PHE   H2   H  N N 327 
PHE   HA   H  N N 328 
PHE   HB2  H  N N 329 
PHE   HB3  H  N N 330 
PHE   HD1  H  N N 331 
PHE   HD2  H  N N 332 
PHE   HE1  H  N N 333 
PHE   HE2  H  N N 334 
PHE   HZ   H  N N 335 
PHE   HXT  H  N N 336 
PRO   N    N  N N 337 
PRO   CA   C  N S 338 
PRO   C    C  N N 339 
PRO   O    O  N N 340 
PRO   CB   C  N N 341 
PRO   CG   C  N N 342 
PRO   CD   C  N N 343 
PRO   OXT  O  N N 344 
PRO   H    H  N N 345 
PRO   HA   H  N N 346 
PRO   HB2  H  N N 347 
PRO   HB3  H  N N 348 
PRO   HG2  H  N N 349 
PRO   HG3  H  N N 350 
PRO   HD2  H  N N 351 
PRO   HD3  H  N N 352 
PRO   HXT  H  N N 353 
SER   N    N  N N 354 
SER   CA   C  N S 355 
SER   C    C  N N 356 
SER   O    O  N N 357 
SER   CB   C  N N 358 
SER   OG   O  N N 359 
SER   OXT  O  N N 360 
SER   H    H  N N 361 
SER   H2   H  N N 362 
SER   HA   H  N N 363 
SER   HB2  H  N N 364 
SER   HB3  H  N N 365 
SER   HG   H  N N 366 
SER   HXT  H  N N 367 
THR   N    N  N N 368 
THR   CA   C  N S 369 
THR   C    C  N N 370 
THR   O    O  N N 371 
THR   CB   C  N R 372 
THR   OG1  O  N N 373 
THR   CG2  C  N N 374 
THR   OXT  O  N N 375 
THR   H    H  N N 376 
THR   H2   H  N N 377 
THR   HA   H  N N 378 
THR   HB   H  N N 379 
THR   HG1  H  N N 380 
THR   HG21 H  N N 381 
THR   HG22 H  N N 382 
THR   HG23 H  N N 383 
THR   HXT  H  N N 384 
TRP   N    N  N N 385 
TRP   CA   C  N S 386 
TRP   C    C  N N 387 
TRP   O    O  N N 388 
TRP   CB   C  N N 389 
TRP   CG   C  Y N 390 
TRP   CD1  C  Y N 391 
TRP   CD2  C  Y N 392 
TRP   NE1  N  Y N 393 
TRP   CE2  C  Y N 394 
TRP   CE3  C  Y N 395 
TRP   CZ2  C  Y N 396 
TRP   CZ3  C  Y N 397 
TRP   CH2  C  Y N 398 
TRP   OXT  O  N N 399 
TRP   H    H  N N 400 
TRP   H2   H  N N 401 
TRP   HA   H  N N 402 
TRP   HB2  H  N N 403 
TRP   HB3  H  N N 404 
TRP   HD1  H  N N 405 
TRP   HE1  H  N N 406 
TRP   HE3  H  N N 407 
TRP   HZ2  H  N N 408 
TRP   HZ3  H  N N 409 
TRP   HH2  H  N N 410 
TRP   HXT  H  N N 411 
TYR   N    N  N N 412 
TYR   CA   C  N S 413 
TYR   C    C  N N 414 
TYR   O    O  N N 415 
TYR   CB   C  N N 416 
TYR   CG   C  Y N 417 
TYR   CD1  C  Y N 418 
TYR   CD2  C  Y N 419 
TYR   CE1  C  Y N 420 
TYR   CE2  C  Y N 421 
TYR   CZ   C  Y N 422 
TYR   OH   O  N N 423 
TYR   OXT  O  N N 424 
TYR   H    H  N N 425 
TYR   H2   H  N N 426 
TYR   HA   H  N N 427 
TYR   HB2  H  N N 428 
TYR   HB3  H  N N 429 
TYR   HD1  H  N N 430 
TYR   HD2  H  N N 431 
TYR   HE1  H  N N 432 
TYR   HE2  H  N N 433 
TYR   HH   H  N N 434 
TYR   HXT  H  N N 435 
VAL   N    N  N N 436 
VAL   CA   C  N S 437 
VAL   C    C  N N 438 
VAL   O    O  N N 439 
VAL   CB   C  N N 440 
VAL   CG1  C  N N 441 
VAL   CG2  C  N N 442 
VAL   OXT  O  N N 443 
VAL   H    H  N N 444 
VAL   H2   H  N N 445 
VAL   HA   H  N N 446 
VAL   HB   H  N N 447 
VAL   HG11 H  N N 448 
VAL   HG12 H  N N 449 
VAL   HG13 H  N N 450 
VAL   HG21 H  N N 451 
VAL   HG22 H  N N 452 
VAL   HG23 H  N N 453 
VAL   HXT  H  N N 454 
ZN    ZN   ZN N N 455 
# 
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 
A1BP2 C   O    sing N N 1   
A1BP2 O   C1   sing N N 2   
A1BP2 C1  C2   doub Y N 3   
A1BP2 C2  C3   sing Y N 4   
A1BP2 C3  C4   doub Y N 5   
A1BP2 C4  C5   sing Y N 6   
A1BP2 C5  C6   doub Y N 7   
A1BP2 C1  C6   sing Y N 8   
A1BP2 C6  C7   sing N N 9   
A1BP2 C7  C8   sing N N 10  
A1BP2 O1  C8   doub N N 11  
A1BP2 C8  N    sing N N 12  
A1BP2 N   C9   sing N N 13  
A1BP2 C9  C10  sing N N 14  
A1BP2 C10 C11  sing N N 15  
A1BP2 N1  C11  sing N N 16  
A1BP2 C11 O2   doub N N 17  
A1BP2 C12 C10  sing N N 18  
A1BP2 C13 C12  sing N N 19  
A1BP2 C14 C12  sing N N 20  
A1BP2 N   C14  sing N N 21  
A1BP2 N1  H14  sing N N 22  
A1BP2 N1  H13  sing N N 23  
A1BP2 C4  H7   sing N N 24  
A1BP2 C5  H8   sing N N 25  
A1BP2 C7  H9   sing N N 26  
A1BP2 C7  H10  sing N N 27  
A1BP2 C10 H    sing N N 28  
A1BP2 C13 H15  sing N N 29  
A1BP2 C13 H16  sing N N 30  
A1BP2 C13 H17  sing N N 31  
A1BP2 C9  H12  sing N N 32  
A1BP2 C9  H11  sing N N 33  
A1BP2 C12 H1   sing N N 34  
A1BP2 C14 H19  sing N N 35  
A1BP2 C14 H18  sing N N 36  
A1BP2 C   H2   sing N N 37  
A1BP2 C   H3   sing N N 38  
A1BP2 C   H4   sing N N 39  
A1BP2 C3  H6   sing N N 40  
A1BP2 C2  H5   sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
GOL   C1  O1   sing N N 179 
GOL   C1  C2   sing N N 180 
GOL   C1  H11  sing N N 181 
GOL   C1  H12  sing N N 182 
GOL   O1  HO1  sing N N 183 
GOL   C2  O2   sing N N 184 
GOL   C2  C3   sing N N 185 
GOL   C2  H2   sing N N 186 
GOL   O2  HO2  sing N N 187 
GOL   C3  O3   sing N N 188 
GOL   C3  H31  sing N N 189 
GOL   C3  H32  sing N N 190 
GOL   O3  HO3  sing N N 191 
HIS   N   CA   sing N N 192 
HIS   N   H    sing N N 193 
HIS   N   H2   sing N N 194 
HIS   CA  C    sing N N 195 
HIS   CA  CB   sing N N 196 
HIS   CA  HA   sing N N 197 
HIS   C   O    doub N N 198 
HIS   C   OXT  sing N N 199 
HIS   CB  CG   sing N N 200 
HIS   CB  HB2  sing N N 201 
HIS   CB  HB3  sing N N 202 
HIS   CG  ND1  sing Y N 203 
HIS   CG  CD2  doub Y N 204 
HIS   ND1 CE1  doub Y N 205 
HIS   ND1 HD1  sing N N 206 
HIS   CD2 NE2  sing Y N 207 
HIS   CD2 HD2  sing N N 208 
HIS   CE1 NE2  sing Y N 209 
HIS   CE1 HE1  sing N N 210 
HIS   NE2 HE2  sing N N 211 
HIS   OXT HXT  sing N N 212 
HOH   O   H1   sing N N 213 
HOH   O   H2   sing N N 214 
ILE   N   CA   sing N N 215 
ILE   N   H    sing N N 216 
ILE   N   H2   sing N N 217 
ILE   CA  C    sing N N 218 
ILE   CA  CB   sing N N 219 
ILE   CA  HA   sing N N 220 
ILE   C   O    doub N N 221 
ILE   C   OXT  sing N N 222 
ILE   CB  CG1  sing N N 223 
ILE   CB  CG2  sing N N 224 
ILE   CB  HB   sing N N 225 
ILE   CG1 CD1  sing N N 226 
ILE   CG1 HG12 sing N N 227 
ILE   CG1 HG13 sing N N 228 
ILE   CG2 HG21 sing N N 229 
ILE   CG2 HG22 sing N N 230 
ILE   CG2 HG23 sing N N 231 
ILE   CD1 HD11 sing N N 232 
ILE   CD1 HD12 sing N N 233 
ILE   CD1 HD13 sing N N 234 
ILE   OXT HXT  sing N N 235 
LEU   N   CA   sing N N 236 
LEU   N   H    sing N N 237 
LEU   N   H2   sing N N 238 
LEU   CA  C    sing N N 239 
LEU   CA  CB   sing N N 240 
LEU   CA  HA   sing N N 241 
LEU   C   O    doub N N 242 
LEU   C   OXT  sing N N 243 
LEU   CB  CG   sing N N 244 
LEU   CB  HB2  sing N N 245 
LEU   CB  HB3  sing N N 246 
LEU   CG  CD1  sing N N 247 
LEU   CG  CD2  sing N N 248 
LEU   CG  HG   sing N N 249 
LEU   CD1 HD11 sing N N 250 
LEU   CD1 HD12 sing N N 251 
LEU   CD1 HD13 sing N N 252 
LEU   CD2 HD21 sing N N 253 
LEU   CD2 HD22 sing N N 254 
LEU   CD2 HD23 sing N N 255 
LEU   OXT HXT  sing N N 256 
LYS   N   CA   sing N N 257 
LYS   N   H    sing N N 258 
LYS   N   H2   sing N N 259 
LYS   CA  C    sing N N 260 
LYS   CA  CB   sing N N 261 
LYS   CA  HA   sing N N 262 
LYS   C   O    doub N N 263 
LYS   C   OXT  sing N N 264 
LYS   CB  CG   sing N N 265 
LYS   CB  HB2  sing N N 266 
LYS   CB  HB3  sing N N 267 
LYS   CG  CD   sing N N 268 
LYS   CG  HG2  sing N N 269 
LYS   CG  HG3  sing N N 270 
LYS   CD  CE   sing N N 271 
LYS   CD  HD2  sing N N 272 
LYS   CD  HD3  sing N N 273 
LYS   CE  NZ   sing N N 274 
LYS   CE  HE2  sing N N 275 
LYS   CE  HE3  sing N N 276 
LYS   NZ  HZ1  sing N N 277 
LYS   NZ  HZ2  sing N N 278 
LYS   NZ  HZ3  sing N N 279 
LYS   OXT HXT  sing N N 280 
MET   N   CA   sing N N 281 
MET   N   H    sing N N 282 
MET   N   H2   sing N N 283 
MET   CA  C    sing N N 284 
MET   CA  CB   sing N N 285 
MET   CA  HA   sing N N 286 
MET   C   O    doub N N 287 
MET   C   OXT  sing N N 288 
MET   CB  CG   sing N N 289 
MET   CB  HB2  sing N N 290 
MET   CB  HB3  sing N N 291 
MET   CG  SD   sing N N 292 
MET   CG  HG2  sing N N 293 
MET   CG  HG3  sing N N 294 
MET   SD  CE   sing N N 295 
MET   CE  HE1  sing N N 296 
MET   CE  HE2  sing N N 297 
MET   CE  HE3  sing N N 298 
MET   OXT HXT  sing N N 299 
PHE   N   CA   sing N N 300 
PHE   N   H    sing N N 301 
PHE   N   H2   sing N N 302 
PHE   CA  C    sing N N 303 
PHE   CA  CB   sing N N 304 
PHE   CA  HA   sing N N 305 
PHE   C   O    doub N N 306 
PHE   C   OXT  sing N N 307 
PHE   CB  CG   sing N N 308 
PHE   CB  HB2  sing N N 309 
PHE   CB  HB3  sing N N 310 
PHE   CG  CD1  doub Y N 311 
PHE   CG  CD2  sing Y N 312 
PHE   CD1 CE1  sing Y N 313 
PHE   CD1 HD1  sing N N 314 
PHE   CD2 CE2  doub Y N 315 
PHE   CD2 HD2  sing N N 316 
PHE   CE1 CZ   doub Y N 317 
PHE   CE1 HE1  sing N N 318 
PHE   CE2 CZ   sing Y N 319 
PHE   CE2 HE2  sing N N 320 
PHE   CZ  HZ   sing N N 321 
PHE   OXT HXT  sing N N 322 
PRO   N   CA   sing N N 323 
PRO   N   CD   sing N N 324 
PRO   N   H    sing N N 325 
PRO   CA  C    sing N N 326 
PRO   CA  CB   sing N N 327 
PRO   CA  HA   sing N N 328 
PRO   C   O    doub N N 329 
PRO   C   OXT  sing N N 330 
PRO   CB  CG   sing N N 331 
PRO   CB  HB2  sing N N 332 
PRO   CB  HB3  sing N N 333 
PRO   CG  CD   sing N N 334 
PRO   CG  HG2  sing N N 335 
PRO   CG  HG3  sing N N 336 
PRO   CD  HD2  sing N N 337 
PRO   CD  HD3  sing N N 338 
PRO   OXT HXT  sing N N 339 
SER   N   CA   sing N N 340 
SER   N   H    sing N N 341 
SER   N   H2   sing N N 342 
SER   CA  C    sing N N 343 
SER   CA  CB   sing N N 344 
SER   CA  HA   sing N N 345 
SER   C   O    doub N N 346 
SER   C   OXT  sing N N 347 
SER   CB  OG   sing N N 348 
SER   CB  HB2  sing N N 349 
SER   CB  HB3  sing N N 350 
SER   OG  HG   sing N N 351 
SER   OXT HXT  sing N N 352 
THR   N   CA   sing N N 353 
THR   N   H    sing N N 354 
THR   N   H2   sing N N 355 
THR   CA  C    sing N N 356 
THR   CA  CB   sing N N 357 
THR   CA  HA   sing N N 358 
THR   C   O    doub N N 359 
THR   C   OXT  sing N N 360 
THR   CB  OG1  sing N N 361 
THR   CB  CG2  sing N N 362 
THR   CB  HB   sing N N 363 
THR   OG1 HG1  sing N N 364 
THR   CG2 HG21 sing N N 365 
THR   CG2 HG22 sing N N 366 
THR   CG2 HG23 sing N N 367 
THR   OXT HXT  sing N N 368 
TRP   N   CA   sing N N 369 
TRP   N   H    sing N N 370 
TRP   N   H2   sing N N 371 
TRP   CA  C    sing N N 372 
TRP   CA  CB   sing N N 373 
TRP   CA  HA   sing N N 374 
TRP   C   O    doub N N 375 
TRP   C   OXT  sing N N 376 
TRP   CB  CG   sing N N 377 
TRP   CB  HB2  sing N N 378 
TRP   CB  HB3  sing N N 379 
TRP   CG  CD1  doub Y N 380 
TRP   CG  CD2  sing Y N 381 
TRP   CD1 NE1  sing Y N 382 
TRP   CD1 HD1  sing N N 383 
TRP   CD2 CE2  doub Y N 384 
TRP   CD2 CE3  sing Y N 385 
TRP   NE1 CE2  sing Y N 386 
TRP   NE1 HE1  sing N N 387 
TRP   CE2 CZ2  sing Y N 388 
TRP   CE3 CZ3  doub Y N 389 
TRP   CE3 HE3  sing N N 390 
TRP   CZ2 CH2  doub Y N 391 
TRP   CZ2 HZ2  sing N N 392 
TRP   CZ3 CH2  sing Y N 393 
TRP   CZ3 HZ3  sing N N 394 
TRP   CH2 HH2  sing N N 395 
TRP   OXT HXT  sing N N 396 
TYR   N   CA   sing N N 397 
TYR   N   H    sing N N 398 
TYR   N   H2   sing N N 399 
TYR   CA  C    sing N N 400 
TYR   CA  CB   sing N N 401 
TYR   CA  HA   sing N N 402 
TYR   C   O    doub N N 403 
TYR   C   OXT  sing N N 404 
TYR   CB  CG   sing N N 405 
TYR   CB  HB2  sing N N 406 
TYR   CB  HB3  sing N N 407 
TYR   CG  CD1  doub Y N 408 
TYR   CG  CD2  sing Y N 409 
TYR   CD1 CE1  sing Y N 410 
TYR   CD1 HD1  sing N N 411 
TYR   CD2 CE2  doub Y N 412 
TYR   CD2 HD2  sing N N 413 
TYR   CE1 CZ   doub Y N 414 
TYR   CE1 HE1  sing N N 415 
TYR   CE2 CZ   sing Y N 416 
TYR   CE2 HE2  sing N N 417 
TYR   CZ  OH   sing N N 418 
TYR   OH  HH   sing N N 419 
TYR   OXT HXT  sing N N 420 
VAL   N   CA   sing N N 421 
VAL   N   H    sing N N 422 
VAL   N   H2   sing N N 423 
VAL   CA  C    sing N N 424 
VAL   CA  CB   sing N N 425 
VAL   CA  HA   sing N N 426 
VAL   C   O    doub N N 427 
VAL   C   OXT  sing N N 428 
VAL   CB  CG1  sing N N 429 
VAL   CB  CG2  sing N N 430 
VAL   CB  HB   sing N N 431 
VAL   CG1 HG11 sing N N 432 
VAL   CG1 HG12 sing N N 433 
VAL   CG1 HG13 sing N N 434 
VAL   CG2 HG21 sing N N 435 
VAL   CG2 HG22 sing N N 436 
VAL   CG2 HG23 sing N N 437 
VAL   OXT HXT  sing N N 438 
# 
_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                    7HVY 
_atom_sites.fract_transf_matrix[1][1]   0.011535 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000991 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017469 
_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]   0.015490 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.467 8.246   24.805 1.00 17.42 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.727 8.314   24.048 1.00 17.79 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 18.864 7.115   23.120 1.00 16.84 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.122 6.123   23.285 1.00 17.33 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 19.909 8.385   25.021 1.00 20.48 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.005 7.167   25.738 1.00 23.97 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.809 7.170   22.181 1.00 15.89 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.086 6.045   21.284 1.00 14.63 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.504 6.478   19.890 1.00 13.92 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.211 7.602   19.483 1.00 15.55 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.217 5.619   19.201 1.00 12.83 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.720 5.963   17.863 1.00 13.85 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.732 4.746   16.969 1.00 13.63 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.595 3.619   17.442 1.00 14.05 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.146 6.519   17.998 1.00 15.44 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.790 4.971   15.653 1.00 12.09 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.051 3.916   14.661 1.00 11.46 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.499 4.016   14.264 1.00 12.55 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.009 5.122   13.988 1.00 12.67 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.196 4.103   13.396 1.00 12.16 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.678 4.280   13.751 1.00 13.33 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.427 2.910   12.462 1.00 13.78 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.913 4.802   12.485 1.00 14.40 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.223 2.875   14.273 1.00 12.64 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.634 2.866   13.875 1.00 13.64 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.750 2.014   12.606 1.00 14.46 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.756 0.775   12.674 1.00 14.51 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.498 2.274   15.015 1.00 14.85 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.526 3.174   16.228 1.00 14.59 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.379 4.281   16.286 1.00 14.58 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.669 2.958   17.300 1.00 15.69 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.370 5.152   17.385 1.00 15.73 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.683 3.805   18.420 1.00 16.59 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.489 4.933   18.418 1.00 16.80 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.483 5.799   19.507 1.00 18.92 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.807 2.659   11.444 1.00 14.13 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.896 1.999   10.141 1.00 14.49 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.132 2.518   9.455  1.00 15.43 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.373 3.730   9.387  1.00 14.93 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.623 2.277   9.287  1.00 15.43 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.258 3.776   9.216  1.00 16.64 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.784 1.656   7.899  1.00 17.21 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.019 1.615   9.021  1.00 16.37 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.253 2.023   8.338  1.00 16.52 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.074 2.927   9.238  1.00 16.25 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.183 2.637   10.442 1.00 15.99 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.511 4.078   8.706  1.00 15.38 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.194 5.058   9.543  1.00 15.43 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.291 6.248   9.838  1.00 14.89 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.798 7.377   9.971  1.00 15.34 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.533 5.479   8.962  1.00 17.03 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.615 4.432   9.116  1.00 20.01 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.367 4.373   10.097 1.00 22.59 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.678 3.551   8.167  1.00 20.30 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.022 5.966   10.108 1.00 13.92 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.058 7.002   10.451 1.00 13.39 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.381 6.673   11.777 1.00 13.34 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.120 5.488   12.105 1.00 13.93 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.967 7.062   9.364  1.00 14.06 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.476 7.435   7.992  1.00 15.41 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.087 8.661   7.755  1.00 16.57 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.296 6.584   6.920  1.00 16.98 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.520 9.021   6.479  1.00 17.00 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.708 6.941   5.638  1.00 17.48 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.322 8.150   5.423  1.00 18.34 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.744 8.513   4.149  1.00 22.76 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.024 7.729   12.514 1.00 12.42 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.221 7.665   13.736 1.00 12.69 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 24.989 8.535   13.463 1.00 12.68 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.139 9.738   13.155 1.00 12.85 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.042 8.217   14.950 1.00 12.74 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.221 8.555   16.178 1.00 14.25 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.144 8.945   17.364 1.00 14.46 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.580 10.032  18.183 1.00 15.58 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.894 9.851   19.307 1.00 17.77 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.625 8.618   19.740 1.00 17.75 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.431 10.897  19.984 1.00 16.83 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.792 7.928   13.521 1.00 11.92 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.529 8.664   13.263 1.00 11.29 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.841 8.870   14.587 1.00 12.47 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.527 7.863   15.300 1.00 12.79 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.596 7.851   12.343 1.00 11.78 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.363 8.692   11.961 1.00 12.67 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.312 7.333   11.087 1.00 13.38 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.598 10.130  14.957 1.00 11.59 ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 20.946 10.463  16.236 0.50 11.88 ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.003 10.459  16.255 0.50 13.90 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.849 11.452  16.026 1.00 12.65 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.696 12.076  14.944 1.00 13.65 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 21.958 11.076  17.265 0.50 10.99 ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.145 11.131  17.127 0.50 17.31 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 22.872 9.995   17.797 0.50 11.30 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.748 11.337  18.572 0.50 18.20 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.716 12.313  16.680 0.50 8.41  ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.439 10.340  17.083 0.50 19.21 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 18.996 11.638  17.057 1.00 12.31 ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 17.980 12.707  16.986 1.00 13.01 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.794 14.028  16.988 1.00 13.42 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.699 14.203  17.812 1.00 13.79 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.085 12.718  18.251 1.00 13.15 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.232 11.476  18.373 1.00 13.88 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.664 10.480  18.994 1.00 14.64 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.067 11.544  17.718 1.00 15.69 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.416 14.967  16.122 1.00 12.46 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.181 16.245  16.071 1.00 14.16 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.137 16.920  17.419 1.00 15.71 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.128 17.494  17.855 1.00 16.05 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.559 17.129  15.002 1.00 14.55 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.376 18.439  14.717 1.00 14.72 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.621 19.305  13.720 1.00 15.99 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.354 20.516  13.265 1.00 16.91 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.333 21.681  13.905 1.00 19.42 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.751 21.786  15.086 1.00 18.79 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 19.940 22.751  13.379 1.00 20.56 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 17.978 16.822  18.128 1.00 14.69 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 17.847 17.537  19.400 1.00 15.89 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.721 16.947  20.524 1.00 16.34 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 18.865 17.588  21.571 1.00 18.41 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.359 17.685  19.823 1.00 17.72 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.698 16.440  20.335 1.00 16.45 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.070 15.560  19.475 1.00 15.99 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.497 16.012  21.605 1.00 17.38 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.551 14.582  20.239 1.00 16.27 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.783 14.812  21.527 1.00 17.67 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.255 15.733  20.348 1.00 15.57 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.133 15.066  21.326 1.00 15.05 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.592 15.014  20.869 1.00 16.96 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.419 14.388  21.518 1.00 17.49 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.616 13.652  21.627 1.00 15.45 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.203 13.657  22.229 1.00 16.55 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.738 12.219  22.471 1.00 17.00 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.157 14.434  23.575 1.00 18.54 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 21.922 15.670  19.734 1.00 16.43 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.295 15.625  19.239 1.00 15.91 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.256 16.290  20.233 1.00 16.51 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 23.922 17.317  20.848 1.00 17.66 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.393 16.312  17.879 1.00 15.77 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.449 15.697  20.355 1.00 16.10 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.499 16.208  21.267 1.00 16.37 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.438 17.179  20.544 1.00 16.65 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.371 17.344  19.298 1.00 15.92 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.354 15.036  21.793 1.00 18.41 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.101 14.484  20.696 1.00 18.53 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.505 13.925  22.448 1.00 19.13 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.355 17.869  21.296 1.00 17.54 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.342 18.702  20.659 1.00 17.97 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.206 17.883  19.709 1.00 17.24 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.481 18.362  18.613 1.00 17.01 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.246 19.379  21.730 1.00 19.76 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.496 20.020  21.130 1.00 26.66 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.427 21.171  20.363 1.00 31.20 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.774 19.552  21.078 1.00 31.05 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.670 21.469  20.008 1.00 32.47 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.525 20.500  20.367 1.00 33.79 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.571 16.636  20.085 1.00 16.87 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.382 15.828  19.192 1.00 16.87 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.637 15.537  17.877 1.00 15.92 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.232 15.564  16.812 1.00 16.54 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.823 14.509  19.828 1.00 18.40 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.791 13.761  18.942 1.00 26.01 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 33.954 14.192  18.762 1.00 29.19 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.322 12.695  18.292 1.00 28.23 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.310 15.323  17.954 1.00 14.81 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.507 15.121  16.738 1.00 14.53 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.572 16.368  15.827 1.00 13.92 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.803 16.246  14.616 1.00 14.17 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.037 14.845  17.081 1.00 14.07 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.758 13.482  17.685 1.00 15.38 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.421 12.495  17.267 1.00 14.75 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 25.927 13.408  18.593 1.00 15.26 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.359 17.560  16.401 1.00 13.82 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.416 18.798  15.617 1.00 14.13 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.820 19.058  15.056 1.00 14.99 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 29.928 19.619  13.965 1.00 15.20 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 27.942 20.002  16.489 1.00 14.90 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.444 20.070  16.611 1.00 14.97 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.688 19.742  17.692 1.00 17.38 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.521 20.501  15.593 1.00 15.58 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.357 19.993  17.440 1.00 16.53 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.221 20.418  16.136 1.00 15.85 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.674 20.916  14.264 1.00 17.47 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.082 20.797  15.395 1.00 17.49 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.561 21.232  13.528 1.00 17.97 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.297 21.232  14.100 1.00 18.05 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.866 18.664  15.792 1.00 13.96 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.230 18.887  15.310 1.00 14.72 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.662 17.870  14.246 1.00 15.86 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.718 18.024  13.631 1.00 17.24 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.190 18.855  16.503 1.00 16.48 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.869 16.801  14.046 1.00 15.04 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.155 15.744  13.042 1.00 15.53 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.927 15.553  12.165 1.00 14.71 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.535 14.423  11.827 1.00 14.69 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.547 14.421  13.750 1.00 16.60 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.896 14.601  14.409 1.00 18.43 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 34.923 14.529  13.718 1.00 20.98 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 33.921 14.910  15.715 1.00 19.36 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.276 16.655  11.819 1.00 14.08 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 28.982 16.598  11.145 1.00 13.81 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.044 16.128  9.720  1.00 15.32 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.896 16.600  8.946  1.00 16.64 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.362 18.021  11.187 1.00 14.26 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 26.979 18.149  10.564 1.00 15.36 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 25.939 17.397  11.430 1.00 15.25 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.550 19.624  10.468 1.00 18.16 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.131 15.247  9.328  1.00 14.14 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 27.951 14.820  7.930  1.00 14.49 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.712 15.515  7.336  1.00 15.33 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.762 16.041  6.219  1.00 16.41 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.838 13.284  7.847  1.00 13.70 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.460 12.849  6.408  1.00 16.14 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.142 12.624  8.328  1.00 15.74 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.566 15.475  8.056  1.00 14.45 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.308 16.006  7.530  1.00 14.43 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.325 16.210  8.671  1.00 14.41 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.371 15.442  9.648  1.00 14.31 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.710 14.996  6.507  1.00 15.68 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.309 15.241  6.032  1.00 16.70 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.906 16.084  5.035  1.00 18.71 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.108 14.655  6.573  1.00 16.43 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.530 16.028  4.900  1.00 20.39 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.020 15.136  5.812  1.00 18.64 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.856 13.730  7.587  1.00 16.62 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.697 14.691  6.021  1.00 19.79 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.557 13.268  7.769  1.00 17.54 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.493 13.774  7.020  1.00 18.83 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.508 17.253  8.609  1.00 15.28 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.488 17.462  9.617  1.00 14.88 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.268 18.084  8.973  1.00 16.28 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.381 18.888  8.019  1.00 17.23 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 21.983 18.285  10.792 1.00 16.48 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.593 19.639  10.416 1.00 17.57 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.636 20.810  10.192 1.00 18.35 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 21.986 21.759  9.435  1.00 20.30 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.529 20.804  10.776 1.00 18.42 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.088 17.786  9.518  1.00 15.91 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.844 18.337  9.009  1.00 15.94 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.878 18.529  10.162 1.00 15.91 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.346 17.554  10.713 1.00 16.08 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.255 17.414  7.913  1.00 17.50 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.004 17.909  7.220  1.00 21.74 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.166 18.513  7.893  1.00 25.67 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.836 17.624  6.017  1.00 25.49 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.653 19.792  10.553 1.00 16.80 ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.778 20.115  11.660 0.50 17.78 ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.778 20.083  11.675 0.50 18.67 ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.330 19.668  11.386 1.00 18.88 ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.645 19.181  12.307 1.00 18.74 ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.870 21.618  11.950 0.50 18.46 ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 15.882 21.562  12.052 0.50 22.11 ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 14.859 22.045  12.841 0.50 19.19 ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.647 22.364  10.909 0.50 27.24 ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.859 19.799  10.131 1.00 18.52 ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.481 19.384  9.816  1.00 19.34 ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.239 17.898  10.021 1.00 18.26 ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.098 17.514  10.216 1.00 19.23 ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.087 19.761  8.395  1.00 21.25 ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.688 18.936  7.411  1.00 26.94 ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.294 17.071  10.001 1.00 16.14 ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.187 15.620  10.224 1.00 15.83 ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.653 15.182  11.638 1.00 15.78 ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.539 13.991  11.977 1.00 14.52 ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.061 14.888  9.178  1.00 16.56 ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.520 15.042  7.743  1.00 17.67 ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.388 14.362  6.693  1.00 17.08 ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.315 12.900  6.853  1.00 15.46 ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.474 12.026  5.866  1.00 16.68 ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.726 12.447  4.627  1.00 19.05 ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.353 10.716  6.097  1.00 16.14 ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.205 16.103  12.463 1.00 14.77 ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.831 15.795  13.740 1.00 13.61 ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 15.962 14.784  13.605 1.00 13.95 ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.175 13.953  14.501 1.00 14.51 ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.808 15.322  14.806 1.00 15.10 ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.396 15.118  16.186 1.00 15.47 ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.225 15.945  16.635 1.00 15.96 ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.003 14.127  16.872 1.00 16.01 ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.765 14.899  12.537 1.00 13.23 ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.881 13.953  12.342 1.00 12.36 ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.239 14.665  12.215 1.00 12.63 ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.315 15.778  11.641 1.00 13.87 ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.689 13.126  11.062 1.00 13.31 ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.577 12.029  11.101 1.00 14.66 ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.508 11.324  9.753  1.00 15.90 ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.793 11.015  12.277 1.00 15.62 ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.290 14.011  12.703 1.00 12.23 ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.663 14.487  12.495 1.00 11.96 ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.524 13.246  12.357 1.00 12.39 ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.316 12.218  13.050 1.00 12.62 ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.112 15.335  13.697 1.00 12.82 ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.561 15.898  13.613 1.00 13.91 ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.661 17.273  14.301 1.00 14.72 ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.588 14.958  14.271 1.00 14.40 ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.500 13.314  11.443 1.00 12.20 ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.433 12.219  11.196 1.00 11.94 ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.843 12.735  11.347 1.00 12.04 ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.188 13.797  10.781 1.00 13.03 ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.222 11.615  9.783  1.00 11.86 ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.267 10.520  9.532  1.00 13.38 ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.778 11.076  9.638  1.00 13.59 ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.663 12.062  12.166 1.00 12.52 ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.071 12.412  12.342 1.00 12.05 ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 28.949 11.242  11.927 1.00 13.36 ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.465 10.104  11.712 1.00 13.69 ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.348 12.792  13.796 1.00 13.92 ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 27.998 11.730  14.672 1.00 14.53 ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.236 11.513  11.702 1.00 14.26 ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.165 10.467  11.288 1.00 14.94 ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.787 9.757   12.503 1.00 17.41 ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 31.976 10.369  13.570 1.00 19.02 ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.253 11.084  10.417 1.00 18.09 ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 32.964 12.063  11.159 1.00 19.99 ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.154 8.464   12.322 1.00 17.46 ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.730 7.675   13.413 1.00 19.02 ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.071 7.086   12.973 1.00 21.44 ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.299 6.852   11.768 1.00 20.52 ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.810 6.496   13.808 1.00 20.02 ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.667 5.598   12.702 1.00 20.60 ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.407 6.945   14.241 1.00 20.68 ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.949 6.820   13.951 1.00 22.79 ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.223 6.186   13.622 1.00 24.78 ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.008 4.662   13.460 1.00 25.09 ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.537 4.066   12.510 1.00 27.33 ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.251 6.535   14.703 1.00 28.65 ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.782 6.018   15.923 1.00 32.27 ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.431 8.031   14.855 1.00 29.13 ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.199 4.065   14.347 1.00 24.25 ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.923 2.624   14.277 1.00 25.09 ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.723 2.316   13.361 1.00 24.34 ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.790 3.110   13.307 1.00 23.20 ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.632 2.083   15.678 1.00 27.20 ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.717 1.152   12.703 1.00 22.68 ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.626 0.726   11.838 1.00 22.75 ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.497 0.164   12.684 1.00 21.71 ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.744 -0.526  13.687 1.00 23.16 ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.105 -0.320  10.828 1.00 25.75 ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.890 0.304   9.650  1.00 30.85 ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.282 -0.750  8.639  1.00 37.10 ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.108 -1.622  8.909  1.00 36.77 ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.683 -0.704  7.456  1.00 40.21 ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.249 0.478   12.318 1.00 18.27 ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.090 -0.024  13.040 1.00 17.79 ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.489 -1.289  12.461 1.00 17.39 ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.803 -1.692  11.335 1.00 18.46 ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.555 -1.862  13.221 1.00 16.35 ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.955 -3.161  12.832 1.00 17.81 ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.524 -3.119  12.385 1.00 17.31 ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.978 -4.178  11.994 1.00 18.31 ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.116 -4.209  13.936 1.00 18.90 ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.833 -4.641  14.273 1.00 22.82 ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.861 -1.978  12.518 1.00 15.11 ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.481 -1.896  12.073 1.00 14.86 ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.422 -1.816  10.552 1.00 15.82 ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.332 -1.265  9.901  1.00 17.24 ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.814 -0.643  12.681 1.00 14.23 ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.695 -0.689  14.193 1.00 15.75 ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.350 -1.792  14.734 1.00 16.25 ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.889 0.380   14.855 1.00 16.07 ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.375 -2.347  9.986  1.00 16.46 ? 52  THR   A N   1 
ATOM   360  C  CA  A THR   A 1 46  ? 22.109 -2.239  8.554  0.50 17.77 ? 52  THR   A CA  1 
ATOM   361  C  CA  B THR   A 1 46  ? 22.119 -2.260  8.544  0.50 16.82 ? 52  THR   A CA  1 
ATOM   362  C  C   . THR   A 1 46  ? 20.767 -1.536  8.364  1.00 16.01 ? 52  THR   A C   1 
ATOM   363  O  O   . THR   A 1 46  ? 19.843 -1.702  9.187  1.00 17.18 ? 52  THR   A O   1 
ATOM   364  C  CB  A THR   A 1 46  ? 22.185 -3.616  7.915  0.50 21.81 ? 52  THR   A CB  1 
ATOM   365  C  CB  B THR   A 1 46  ? 22.043 -3.660  7.914  0.50 18.29 ? 52  THR   A CB  1 
ATOM   366  O  OG1 A THR   A 1 46  ? 23.576 -3.921  7.744  0.50 23.27 ? 52  THR   A OG1 1 
ATOM   367  O  OG1 B THR   A 1 46  ? 20.931 -4.313  8.460  0.50 19.11 ? 52  THR   A OG1 1 
ATOM   368  C  CG2 A THR   A 1 46  ? 21.458 -3.702  6.579  0.50 23.82 ? 52  THR   A CG2 1 
ATOM   369  C  CG2 B THR   A 1 46  ? 23.287 -4.538  8.195  0.50 18.17 ? 52  THR   A CG2 1 
ATOM   370  N  N   . ILE   A 1 47  ? 20.647 -0.705  7.314  1.00 15.65 ? 53  ILE   A N   1 
ATOM   371  C  CA  . ILE   A 1 47  ? 19.410 0.039   7.082  1.00 14.45 ? 53  ILE   A CA  1 
ATOM   372  C  C   . ILE   A 1 47  ? 18.444 -0.749  6.190  1.00 15.55 ? 53  ILE   A C   1 
ATOM   373  O  O   . ILE   A 1 47  ? 18.846 -1.313  5.149  1.00 16.49 ? 53  ILE   A O   1 
ATOM   374  C  CB  . ILE   A 1 47  ? 19.735 1.401   6.419  1.00 14.61 ? 53  ILE   A CB  1 
ATOM   375  C  CG1 . ILE   A 1 47  ? 20.790 2.194   7.207  1.00 15.64 ? 53  ILE   A CG1 1 
ATOM   376  C  CG2 . ILE   A 1 47  ? 18.423 2.236   6.256  1.00 14.85 ? 53  ILE   A CG2 1 
ATOM   377  C  CD1 . ILE   A 1 47  ? 20.409 2.485   8.681  1.00 16.26 ? 53  ILE   A CD1 1 
ATOM   378  N  N   . ALA   A 1 48  ? 17.183 -0.799  6.575  1.00 14.21 ? 54  ALA   A N   1 
ATOM   379  C  CA  . ALA   A 1 48  ? 16.151 -1.442  5.785  1.00 14.57 ? 54  ALA   A CA  1 
ATOM   380  C  C   . ALA   A 1 48  ? 15.919 -0.609  4.517  1.00 15.84 ? 54  ALA   A C   1 
ATOM   381  O  O   . ALA   A 1 48  ? 15.847 0.645   4.536  1.00 15.41 ? 54  ALA   A O   1 
ATOM   382  C  CB  . ALA   A 1 48  ? 14.861 -1.499  6.595  1.00 14.57 ? 54  ALA   A CB  1 
ATOM   383  N  N   . ARG   A 1 49  ? 15.722 -1.336  3.388  1.00 17.24 ? 55  ARG   A N   1 
ATOM   384  C  CA  . ARG   A 1 49  ? 15.403 -0.690  2.113  1.00 18.36 ? 55  ARG   A CA  1 
ATOM   385  C  C   . ARG   A 1 49  ? 14.165 -1.439  1.618  1.00 20.59 ? 55  ARG   A C   1 
ATOM   386  O  O   . ARG   A 1 49  ? 14.236 -2.383  0.817  1.00 22.10 ? 55  ARG   A O   1 
ATOM   387  C  CB  . ARG   A 1 49  ? 16.605 -0.778  1.122  1.00 19.13 ? 55  ARG   A CB  1 
ATOM   388  C  CG  . ARG   A 1 49  ? 17.908 -0.178  1.666  1.00 19.27 ? 55  ARG   A CG  1 
ATOM   389  C  CD  . ARG   A 1 49  ? 17.858 1.347   1.880  1.00 17.72 ? 55  ARG   A CD  1 
ATOM   390  N  NE  . ARG   A 1 49  ? 19.164 1.848   2.361  1.00 16.83 ? 55  ARG   A NE  1 
ATOM   391  C  CZ  . ARG   A 1 49  ? 19.340 3.009   2.978  1.00 18.16 ? 55  ARG   A CZ  1 
ATOM   392  N  NH1 . ARG   A 1 49  ? 18.326 3.852   3.126  1.00 17.06 ? 55  ARG   A NH1 1 
ATOM   393  N  NH2 . ARG   A 1 49  ? 20.532 3.345   3.449  1.00 20.08 ? 55  ARG   A NH2 1 
ATOM   394  N  N   . CYS   A 1 50  ? 13.030 -1.025  2.144  1.00 20.27 ? 56  CYS   A N   1 
ATOM   395  C  CA  . CYS   A 1 50  ? 11.780 -1.744  1.977  1.00 21.97 ? 56  CYS   A CA  1 
ATOM   396  C  C   . CYS   A 1 50  ? 10.575 -0.825  2.179  1.00 22.55 ? 56  CYS   A C   1 
ATOM   397  O  O   . CYS   A 1 50  ? 10.664 0.352   2.465  1.00 23.41 ? 56  CYS   A O   1 
ATOM   398  C  CB  . CYS   A 1 50  ? 11.752 -2.858  3.012  1.00 22.59 ? 56  CYS   A CB  1 
ATOM   399  S  SG  . CYS   A 1 50  ? 11.627 -2.215  4.701  1.00 19.92 ? 56  CYS   A SG  1 
ATOM   400  N  N   . ASP   A 1 51  ? 9.364  -1.478  2.105  1.00 24.71 ? 57  ASP   A N   1 
ATOM   401  C  CA  . ASP   A 1 51  ? 8.102  -0.796  2.307  1.00 27.23 ? 57  ASP   A CA  1 
ATOM   402  C  C   . ASP   A 1 51  ? 7.329  -1.388  3.498  1.00 25.99 ? 57  ASP   A C   1 
ATOM   403  O  O   . ASP   A 1 51  ? 6.101  -1.364  3.513  1.00 26.71 ? 57  ASP   A O   1 
ATOM   404  C  CB  . ASP   A 1 51  ? 7.215  -0.867  1.033  1.00 34.37 ? 57  ASP   A CB  1 
ATOM   405  C  CG  . ASP   A 1 51  ? 6.897  -2.255  0.538  1.00 46.49 ? 57  ASP   A CG  1 
ATOM   406  O  OD1 . ASP   A 1 51  ? 7.252  -3.226  1.228  1.00 49.25 ? 57  ASP   A OD1 1 
ATOM   407  O  OD2 . ASP   A 1 51  ? 6.276  -2.373  -0.553 1.00 51.36 ? 57  ASP   A OD2 1 
ATOM   408  N  N   . CYS   A 1 52  ? 8.035  -1.916  4.494  1.00 23.44 ? 58  CYS   A N   1 
ATOM   409  C  CA  . CYS   A 1 52  ? 7.342  -2.478  5.677  1.00 21.06 ? 58  CYS   A CA  1 
ATOM   410  C  C   . CYS   A 1 52  ? 6.587  -1.385  6.423  1.00 20.65 ? 58  CYS   A C   1 
ATOM   411  O  O   . CYS   A 1 52  ? 7.048  -0.247  6.564  1.00 21.78 ? 58  CYS   A O   1 
ATOM   412  C  CB  . CYS   A 1 52  ? 8.340  -3.181  6.597  1.00 21.35 ? 58  CYS   A CB  1 
ATOM   413  S  SG  . CYS   A 1 52  ? 9.078  -4.750  5.980  1.00 21.28 ? 58  CYS   A SG  1 
ATOM   414  N  N   . GLN   A 1 53  ? 5.416  -1.752  6.936  1.00 17.97 ? 59  GLN   A N   1 
ATOM   415  C  CA  A GLN   A 1 53  ? 4.549  -0.897  7.799  0.50 17.36 ? 59  GLN   A CA  1 
ATOM   416  C  CA  B GLN   A 1 53  ? 4.679  -0.860  7.799  0.50 17.46 ? 59  GLN   A CA  1 
ATOM   417  C  C   . GLN   A 1 53  ? 4.291  -1.595  9.163  1.00 15.65 ? 59  GLN   A C   1 
ATOM   418  O  O   . GLN   A 1 53  ? 3.414  -1.181  9.914  1.00 16.17 ? 59  GLN   A O   1 
ATOM   419  C  CB  A GLN   A 1 53  ? 3.185  -0.440  7.172  0.50 19.14 ? 59  GLN   A CB  1 
ATOM   420  C  CB  B GLN   A 1 53  ? 3.559  -0.182  7.013  0.50 19.41 ? 59  GLN   A CB  1 
ATOM   421  C  CG  A GLN   A 1 53  ? 3.158  0.889   6.311  0.50 17.60 ? 59  GLN   A CG  1 
ATOM   422  C  CG  B GLN   A 1 53  ? 4.116  0.633   5.777  0.50 17.84 ? 59  GLN   A CG  1 
ATOM   423  C  CD  A GLN   A 1 53  ? 1.732  1.382   6.009  0.50 22.79 ? 59  GLN   A CD  1 
ATOM   424  C  CD  B GLN   A 1 53  ? 5.041  1.791   6.183  0.50 17.53 ? 59  GLN   A CD  1 
ATOM   425  O  OE1 A GLN   A 1 53  ? 1.186  1.192   4.910  0.50 24.54 ? 59  GLN   A OE1 1 
ATOM   426  O  OE1 B GLN   A 1 53  ? 6.019  2.195   5.486  0.50 17.28 ? 59  GLN   A OE1 1 
ATOM   427  N  NE2 A GLN   A 1 53  ? 1.100  2.061   6.949  0.50 18.13 ? 59  GLN   A NE2 1 
ATOM   428  N  NE2 B GLN   A 1 53  ? 4.761  2.352   7.354  0.50 18.18 ? 59  GLN   A NE2 1 
ATOM   429  N  N   . THR   A 1 54  ? 5.019  -2.703  9.442  1.00 14.18 ? 60  THR   A N   1 
ATOM   430  C  CA  . THR   A 1 54  ? 5.008  -3.401  10.703 1.00 14.59 ? 60  THR   A CA  1 
ATOM   431  C  C   . THR   A 1 54  ? 6.468  -3.658  11.113 1.00 14.34 ? 60  THR   A C   1 
ATOM   432  O  O   . THR   A 1 54  ? 7.354  -3.828  10.244 1.00 15.61 ? 60  THR   A O   1 
ATOM   433  C  CB  . THR   A 1 54  ? 4.217  -4.683  10.727 1.00 17.90 ? 60  THR   A CB  1 
ATOM   434  O  OG1 . THR   A 1 54  ? 4.829  -5.641  9.904  1.00 24.23 ? 60  THR   A OG1 1 
ATOM   435  C  CG2 . THR   A 1 54  ? 2.810  -4.503  10.283 1.00 18.35 ? 60  THR   A CG2 1 
ATOM   436  N  N   . GLY   A 1 55  ? 6.735  -3.576  12.387 1.00 13.83 ? 61  GLY   A N   1 
ATOM   437  C  CA  . GLY   A 1 55  ? 8.093  -3.795  12.892 1.00 13.32 ? 61  GLY   A CA  1 
ATOM   438  C  C   . GLY   A 1 55  ? 8.104  -3.860  14.395 1.00 12.02 ? 61  GLY   A C   1 
ATOM   439  O  O   . GLY   A 1 55  ? 7.058  -4.049  15.017 1.00 12.81 ? 61  GLY   A O   1 
ATOM   440  N  N   . VAL   A 1 56  ? 9.261  -3.600  14.998 1.00 12.04 ? 62  VAL   A N   1 
ATOM   441  C  CA  . VAL   A 1 56  ? 9.439  -3.686  16.431 1.00 10.81 ? 62  VAL   A CA  1 
ATOM   442  C  C   . VAL   A 1 56  ? 10.285 -2.505  16.857 1.00 10.93 ? 62  VAL   A C   1 
ATOM   443  O  O   . VAL   A 1 56  ? 11.254 -2.178  16.176 1.00 12.09 ? 62  VAL   A O   1 
ATOM   444  C  CB  . VAL   A 1 56  ? 10.149 -5.009  16.790 1.00 13.27 ? 62  VAL   A CB  1 
ATOM   445  C  CG1 . VAL   A 1 56  ? 10.527 -5.066  18.252 1.00 16.13 ? 62  VAL   A CG1 1 
ATOM   446  C  CG2 . VAL   A 1 56  ? 9.244  -6.201  16.446 1.00 14.15 ? 62  VAL   A CG2 1 
ATOM   447  N  N   . TYR   A 1 57  ? 9.912  -1.824  17.955 1.00 10.51 ? 63  TYR   A N   1 
ATOM   448  C  CA  . TYR   A 1 57  ? 10.762 -0.723  18.462 1.00 10.91 ? 63  TYR   A CA  1 
ATOM   449  C  C   . TYR   A 1 57  ? 11.205 -0.958  19.899 1.00 11.24 ? 63  TYR   A C   1 
ATOM   450  O  O   . TYR   A 1 57  ? 10.500 -1.586  20.673 1.00 11.70 ? 63  TYR   A O   1 
ATOM   451  C  CB  . TYR   A 1 57  ? 10.063 0.667   18.321 1.00 10.66 ? 63  TYR   A CB  1 
ATOM   452  C  CG  . TYR   A 1 57  ? 9.060  1.031   19.396 1.00 11.23 ? 63  TYR   A CG  1 
ATOM   453  C  CD1 . TYR   A 1 57  ? 7.786  0.478   19.394 1.00 12.21 ? 63  TYR   A CD1 1 
ATOM   454  C  CD2 . TYR   A 1 57  ? 9.383  1.934   20.410 1.00 12.05 ? 63  TYR   A CD2 1 
ATOM   455  C  CE1 . TYR   A 1 57  ? 6.849  0.814   20.361 1.00 13.35 ? 63  TYR   A CE1 1 
ATOM   456  C  CE2 . TYR   A 1 57  ? 8.435  2.284   21.386 1.00 13.02 ? 63  TYR   A CE2 1 
ATOM   457  C  CZ  . TYR   A 1 57  ? 7.193  1.695   21.351 1.00 13.43 ? 63  TYR   A CZ  1 
ATOM   458  O  OH  . TYR   A 1 57  ? 6.223  1.936   22.326 1.00 16.62 ? 63  TYR   A OH  1 
ATOM   459  N  N   . TYR   A 1 58  ? 12.305 -0.326  20.274 1.00 11.19 ? 64  TYR   A N   1 
ATOM   460  C  CA  . TYR   A 1 58  ? 12.787 -0.351  21.650 1.00 10.68 ? 64  TYR   A CA  1 
ATOM   461  C  C   . TYR   A 1 58  ? 12.298 0.856   22.445 1.00 11.33 ? 64  TYR   A C   1 
ATOM   462  O  O   . TYR   A 1 58  ? 12.532 2.005   22.058 1.00 11.42 ? 64  TYR   A O   1 
ATOM   463  C  CB  . TYR   A 1 58  ? 14.344 -0.398  21.703 1.00 11.69 ? 64  TYR   A CB  1 
ATOM   464  C  CG  . TYR   A 1 58  ? 14.834 -0.546  23.132 1.00 12.49 ? 64  TYR   A CG  1 
ATOM   465  C  CD1 . TYR   A 1 58  ? 14.512 -1.657  23.874 1.00 12.76 ? 64  TYR   A CD1 1 
ATOM   466  C  CD2 . TYR   A 1 58  ? 15.560 0.473   23.758 1.00 12.67 ? 64  TYR   A CD2 1 
ATOM   467  C  CE1 . TYR   A 1 58  ? 14.883 -1.758  25.214 1.00 14.26 ? 64  TYR   A CE1 1 
ATOM   468  C  CE2 . TYR   A 1 58  ? 15.917 0.387   25.093 1.00 13.39 ? 64  TYR   A CE2 1 
ATOM   469  C  CZ  . TYR   A 1 58  ? 15.617 -0.756  25.799 1.00 15.05 ? 64  TYR   A CZ  1 
ATOM   470  O  OH  . TYR   A 1 58  ? 15.964 -0.921  27.132 1.00 16.93 ? 64  TYR   A OH  1 
ATOM   471  N  N   . CYS   A 1 59  ? 11.709 0.561   23.586 1.00 11.06 ? 65  CYS   A N   1 
ATOM   472  C  CA  . CYS   A 1 59  ? 11.148 1.561   24.512 1.00 11.76 ? 65  CYS   A CA  1 
ATOM   473  C  C   . CYS   A 1 59  ? 11.974 1.553   25.811 1.00 11.89 ? 65  CYS   A C   1 
ATOM   474  O  O   . CYS   A 1 59  ? 11.798 0.658   26.673 1.00 12.77 ? 65  CYS   A O   1 
ATOM   475  C  CB  . CYS   A 1 59  ? 9.692  1.214   24.785 1.00 11.64 ? 65  CYS   A CB  1 
ATOM   476  S  SG  . CYS   A 1 59  ? 8.905  2.310   26.011 1.00 13.47 ? 65  CYS   A SG  1 
ATOM   477  N  N   . SER   A 1 60  ? 12.878 2.538   25.987 1.00 11.96 ? 66  SER   A N   1 
ATOM   478  C  CA  . SER   A 1 60  ? 13.740 2.546   27.185 1.00 12.98 ? 66  SER   A CA  1 
ATOM   479  C  C   . SER   A 1 60  ? 12.959 2.741   28.494 1.00 13.06 ? 66  SER   A C   1 
ATOM   480  O  O   . SER   A 1 60  ? 13.377 2.186   29.507 1.00 14.55 ? 66  SER   A O   1 
ATOM   481  C  CB  . SER   A 1 60  ? 14.852 3.589   27.048 1.00 15.45 ? 66  SER   A CB  1 
ATOM   482  O  OG  . SER   A 1 60  ? 14.367 4.910   27.110 1.00 17.22 ? 66  SER   A OG  1 
ATOM   483  N  N   . SER   A 1 61  ? 11.806 3.458   28.460 1.00 12.56 ? 67  SER   A N   1 
ATOM   484  C  CA  . SER   A 1 61  ? 10.985 3.653   29.650 1.00 12.13 ? 67  SER   A CA  1 
ATOM   485  C  C   . SER   A 1 61  ? 10.220 2.415   30.118 1.00 12.61 ? 67  SER   A C   1 
ATOM   486  O  O   . SER   A 1 61  ? 9.556  2.468   31.132 1.00 13.24 ? 67  SER   A O   1 
ATOM   487  C  CB  . SER   A 1 61  ? 10.033 4.837   29.466 1.00 13.25 ? 67  SER   A CB  1 
ATOM   488  O  OG  . SER   A 1 61  ? 9.078  4.608   28.461 1.00 14.31 ? 67  SER   A OG  1 
ATOM   489  N  N   . ARG   A 1 62  ? 10.322 1.309   29.340 1.00 13.10 ? 68  ARG   A N   1 
ATOM   490  C  CA  . ARG   A 1 62  ? 9.756  0.017   29.747 1.00 13.57 ? 68  ARG   A CA  1 
ATOM   491  C  C   . ARG   A 1 62  ? 10.825 -1.095  29.697 1.00 14.26 ? 68  ARG   A C   1 
ATOM   492  O  O   . ARG   A 1 62  ? 10.498 -2.264  29.975 1.00 14.53 ? 68  ARG   A O   1 
ATOM   493  C  CB  . ARG   A 1 62  ? 8.600  -0.361  28.793 1.00 14.15 ? 68  ARG   A CB  1 
ATOM   494  C  CG  . ARG   A 1 62  ? 7.420  0.592   28.945 1.00 13.80 ? 68  ARG   A CG  1 
ATOM   495  C  CD  . ARG   A 1 62  ? 6.651  0.249   30.193 1.00 14.66 ? 68  ARG   A CD  1 
ATOM   496  N  NE  . ARG   A 1 62  ? 5.477  1.124   30.352 1.00 17.49 ? 68  ARG   A NE  1 
ATOM   497  C  CZ  . ARG   A 1 62  ? 5.491  2.288   30.989 1.00 15.74 ? 68  ARG   A CZ  1 
ATOM   498  N  NH1 . ARG   A 1 62  ? 6.621  2.746   31.539 1.00 16.46 ? 68  ARG   A NH1 1 
ATOM   499  N  NH2 . ARG   A 1 62  ? 4.360  2.997   31.128 1.00 17.07 ? 68  ARG   A NH2 1 
ATOM   500  N  N   . ARG   A 1 63  ? 12.050 -0.796  29.228 1.00 15.18 ? 69  ARG   A N   1 
ATOM   501  C  CA  . ARG   A 1 63  ? 13.111 -1.817  28.979 1.00 16.02 ? 69  ARG   A CA  1 
ATOM   502  C  C   . ARG   A 1 63  ? 12.548 -2.962  28.118 1.00 18.21 ? 69  ARG   A C   1 
ATOM   503  O  O   . ARG   A 1 63  ? 12.825 -4.146  28.393 1.00 20.57 ? 69  ARG   A O   1 
ATOM   504  C  CB  . ARG   A 1 63  ? 13.645 -2.395  30.288 1.00 20.51 ? 69  ARG   A CB  1 
ATOM   505  C  CG  . ARG   A 1 63  ? 14.808 -1.688  30.726 1.00 22.45 ? 69  ARG   A CG  1 
ATOM   506  C  CD  . ARG   A 1 63  ? 15.469 -2.488  31.834 1.00 22.54 ? 69  ARG   A CD  1 
ATOM   507  N  NE  . ARG   A 1 63  ? 16.180 -1.503  32.609 1.00 23.49 ? 69  ARG   A NE  1 
ATOM   508  C  CZ  . ARG   A 1 63  ? 15.819 -1.072  33.802 1.00 19.71 ? 69  ARG   A CZ  1 
ATOM   509  N  NH1 . ARG   A 1 63  ? 14.772 -1.615  34.430 1.00 21.51 ? 69  ARG   A NH1 1 
ATOM   510  N  NH2 . ARG   A 1 63  ? 16.525 -0.134  34.406 1.00 20.97 ? 69  ARG   A NH2 1 
ATOM   511  N  N   . LYS   A 1 64  ? 11.772 -2.636  27.102 1.00 15.41 ? 70  LYS   A N   1 
ATOM   512  C  CA  . LYS   A 1 64  ? 11.112 -3.637  26.295 1.00 15.48 ? 70  LYS   A CA  1 
ATOM   513  C  C   . LYS   A 1 64  ? 11.059 -3.253  24.840 1.00 15.24 ? 70  LYS   A C   1 
ATOM   514  O  O   . LYS   A 1 64  ? 10.988 -2.063  24.488 1.00 14.30 ? 70  LYS   A O   1 
ATOM   515  C  CB  . LYS   A 1 64  ? 9.649  -3.808  26.815 1.00 17.57 ? 70  LYS   A CB  1 
ATOM   516  C  CG  . LYS   A 1 64  ? 9.552  -4.792  27.990 1.00 27.07 ? 70  LYS   A CG  1 
ATOM   517  C  CD  . LYS   A 1 64  ? 8.123  -5.138  28.292 1.00 35.70 ? 70  LYS   A CD  1 
ATOM   518  C  CE  . LYS   A 1 64  ? 8.024  -5.885  29.611 1.00 41.03 ? 70  LYS   A CE  1 
ATOM   519  N  NZ  . LYS   A 1 64  ? 8.563  -5.068  30.745 1.00 44.94 ? 70  LYS   A NZ  1 
ATOM   520  N  N   . HIS   A 1 65  ? 11.038 -4.266  23.979 1.00 13.80 ? 71  HIS   A N   1 
ATOM   521  C  CA  . HIS   A 1 65  ? 10.788 -4.129  22.543 1.00 13.70 ? 71  HIS   A CA  1 
ATOM   522  C  C   . HIS   A 1 65  ? 9.315  -4.472  22.285 1.00 14.71 ? 71  HIS   A C   1 
ATOM   523  O  O   . HIS   A 1 65  ? 8.804  -5.493  22.803 1.00 18.08 ? 71  HIS   A O   1 
ATOM   524  C  CB  . HIS   A 1 65  ? 11.682 -5.119  21.775 1.00 12.46 ? 71  HIS   A CB  1 
ATOM   525  C  CG  . HIS   A 1 65  ? 13.126 -4.732  21.792 1.00 13.35 ? 71  HIS   A CG  1 
ATOM   526  N  ND1 . HIS   A 1 65  ? 13.987 -5.099  22.827 1.00 15.50 ? 71  HIS   A ND1 1 
ATOM   527  C  CD2 . HIS   A 1 65  ? 13.837 -4.093  20.838 1.00 14.61 ? 71  HIS   A CD2 1 
ATOM   528  C  CE1 . HIS   A 1 65  ? 15.185 -4.655  22.446 1.00 15.98 ? 71  HIS   A CE1 1 
ATOM   529  N  NE2 . HIS   A 1 65  ? 15.152 -4.081  21.269 1.00 16.75 ? 71  HIS   A NE2 1 
ATOM   530  N  N   . TYR   A 1 66  ? 8.599  -3.637  21.514 1.00 12.75 ? 72  TYR   A N   1 
ATOM   531  C  CA  . TYR   A 1 66  ? 7.179  -3.860  21.242 1.00 13.34 ? 72  TYR   A CA  1 
ATOM   532  C  C   . TYR   A 1 66  ? 6.934  -3.945  19.752 1.00 12.38 ? 72  TYR   A C   1 
ATOM   533  O  O   . TYR   A 1 66  ? 7.452  -3.126  18.976 1.00 12.68 ? 72  TYR   A O   1 
ATOM   534  C  CB  . TYR   A 1 66  ? 6.358  -2.621  21.729 1.00 13.70 ? 72  TYR   A CB  1 
ATOM   535  C  CG  . TYR   A 1 66  ? 6.308  -2.472  23.234 1.00 13.63 ? 72  TYR   A CG  1 
ATOM   536  C  CD1 . TYR   A 1 66  ? 5.519  -3.325  24.013 1.00 14.87 ? 72  TYR   A CD1 1 
ATOM   537  C  CD2 . TYR   A 1 66  ? 7.019  -1.473  23.871 1.00 13.47 ? 72  TYR   A CD2 1 
ATOM   538  C  CE1 . TYR   A 1 66  ? 5.443  -3.191  25.399 1.00 16.28 ? 72  TYR   A CE1 1 
ATOM   539  C  CE2 . TYR   A 1 66  ? 6.945  -1.314  25.262 1.00 14.70 ? 72  TYR   A CE2 1 
ATOM   540  C  CZ  . TYR   A 1 66  ? 6.138  -2.162  26.017 1.00 15.83 ? 72  TYR   A CZ  1 
ATOM   541  O  OH  . TYR   A 1 66  ? 6.055  -1.975  27.394 1.00 18.60 ? 72  TYR   A OH  1 
ATOM   542  N  N   . PRO   A 1 67  ? 6.111  -4.907  19.332 1.00 12.77 ? 73  PRO   A N   1 
ATOM   543  C  CA  . PRO   A 1 67  ? 5.692  -4.919  17.923 1.00 12.56 ? 73  PRO   A CA  1 
ATOM   544  C  C   . PRO   A 1 67  ? 4.707  -3.789  17.643 1.00 13.95 ? 73  PRO   A C   1 
ATOM   545  O  O   . PRO   A 1 67  ? 3.811  -3.540  18.480 1.00 17.03 ? 73  PRO   A O   1 
ATOM   546  C  CB  . PRO   A 1 67  ? 5.006  -6.285  17.730 1.00 15.28 ? 73  PRO   A CB  1 
ATOM   547  C  CG  . PRO   A 1 67  ? 4.630  -6.711  19.106 1.00 17.40 ? 73  PRO   A CG  1 
ATOM   548  C  CD  . PRO   A 1 67  ? 5.499  -5.999  20.115 1.00 14.50 ? 73  PRO   A CD  1 
ATOM   549  N  N   . VAL   A 1 68  ? 4.818  -3.165  16.504 1.00 12.29 ? 74  VAL   A N   1 
ATOM   550  C  CA  . VAL   A 1 68  ? 3.920  -2.052  16.146 1.00 14.31 ? 74  VAL   A CA  1 
ATOM   551  C  C   . VAL   A 1 68  ? 3.585  -2.071  14.674 1.00 13.49 ? 74  VAL   A C   1 
ATOM   552  O  O   . VAL   A 1 68  ? 4.390  -2.442  13.831 1.00 14.06 ? 74  VAL   A O   1 
ATOM   553  C  CB  . VAL   A 1 68  ? 4.498  -0.677  16.490 1.00 18.55 ? 74  VAL   A CB  1 
ATOM   554  C  CG1 . VAL   A 1 68  ? 4.393  -0.428  17.991 1.00 20.43 ? 74  VAL   A CG1 1 
ATOM   555  C  CG2 . VAL   A 1 68  ? 5.911  -0.532  15.960 1.00 18.94 ? 74  VAL   A CG2 1 
ATOM   556  N  N   . SER   A 1 69  ? 2.400  -1.510  14.345 1.00 14.13 ? 75  SER   A N   1 
ATOM   557  C  CA  . SER   A 1 69  ? 1.997  -1.126  12.992 1.00 14.37 ? 75  SER   A CA  1 
ATOM   558  C  C   . SER   A 1 69  ? 2.191  0.382   12.908 1.00 14.13 ? 75  SER   A C   1 
ATOM   559  O  O   . SER   A 1 69  ? 1.768  1.092   13.853 1.00 14.93 ? 75  SER   A O   1 
ATOM   560  C  CB  . SER   A 1 69  ? 0.507  -1.380  12.812 1.00 18.68 ? 75  SER   A CB  1 
ATOM   561  O  OG  . SER   A 1 69  ? 0.266  -2.776  12.878 1.00 26.28 ? 75  SER   A OG  1 
ATOM   562  N  N   . PHE   A 1 70  ? 2.798  0.890   11.860 1.00 14.48 ? 76  PHE   A N   1 
ATOM   563  C  CA  . PHE   A 1 70  ? 3.086  2.313   11.770 1.00 15.08 ? 76  PHE   A CA  1 
ATOM   564  C  C   . PHE   A 1 70  ? 2.689  2.892   10.431 1.00 15.62 ? 76  PHE   A C   1 
ATOM   565  O  O   . PHE   A 1 70  ? 2.621  2.174   9.432  1.00 17.25 ? 76  PHE   A O   1 
ATOM   566  C  CB  . PHE   A 1 70  ? 4.581  2.596   12.115 1.00 15.26 ? 76  PHE   A CB  1 
ATOM   567  C  CG  . PHE   A 1 70  ? 5.620  1.788   11.343 1.00 14.19 ? 76  PHE   A CG  1 
ATOM   568  C  CD1 . PHE   A 1 70  ? 6.049  0.557   11.803 1.00 13.90 ? 76  PHE   A CD1 1 
ATOM   569  C  CD2 . PHE   A 1 70  ? 6.202  2.293   10.183 1.00 14.12 ? 76  PHE   A CD2 1 
ATOM   570  C  CE1 . PHE   A 1 70  ? 6.989  -0.175  11.098 1.00 14.27 ? 76  PHE   A CE1 1 
ATOM   571  C  CE2 . PHE   A 1 70  ? 7.156  1.543   9.482  1.00 15.32 ? 76  PHE   A CE2 1 
ATOM   572  C  CZ  . PHE   A 1 70  ? 7.523  0.310   9.929  1.00 14.21 ? 76  PHE   A CZ  1 
ATOM   573  N  N   . SER   A 1 71  ? 2.379  4.187   10.395 1.00 15.85 ? 77  SER   A N   1 
ATOM   574  C  CA  . SER   A 1 71  ? 1.948  4.859   9.178  1.00 16.46 ? 77  SER   A CA  1 
ATOM   575  C  C   . SER   A 1 71  ? 3.126  5.094   8.216  1.00 16.30 ? 77  SER   A C   1 
ATOM   576  O  O   . SER   A 1 71  ? 4.292  5.013   8.618  1.00 16.61 ? 77  SER   A O   1 
ATOM   577  C  CB  . SER   A 1 71  ? 1.218  6.172   9.532  1.00 18.86 ? 77  SER   A CB  1 
ATOM   578  O  OG  . SER   A 1 71  ? 2.076  7.100   10.192 1.00 19.97 ? 77  SER   A OG  1 
ATOM   579  N  N   . LYS   A 1 72  ? 2.835  5.421   6.988  1.00 16.87 ? 78  LYS   A N   1 
ATOM   580  C  CA  . LYS   A 1 72  ? 3.894  5.718   6.026  1.00 17.33 ? 78  LYS   A CA  1 
ATOM   581  C  C   . LYS   A 1 72  ? 4.510  7.078   6.323  1.00 18.12 ? 78  LYS   A C   1 
ATOM   582  O  O   . LYS   A 1 72  ? 3.823  7.949   6.876  1.00 19.01 ? 78  LYS   A O   1 
ATOM   583  C  CB  . LYS   A 1 72  ? 3.309  5.675   4.602  1.00 19.36 ? 78  LYS   A CB  1 
ATOM   584  C  CG  . LYS   A 1 72  ? 2.922  4.271   4.196  1.00 23.58 ? 78  LYS   A CG  1 
ATOM   585  C  CD  . LYS   A 1 72  ? 2.493  4.223   2.717  1.00 30.47 ? 78  LYS   A CD  1 
ATOM   586  C  CE  . LYS   A 1 72  ? 2.276  2.820   2.209  1.00 37.33 ? 78  LYS   A CE  1 
ATOM   587  N  NZ  . LYS   A 1 72  ? 2.262  2.787   0.713  1.00 41.82 ? 78  LYS   A NZ  1 
ATOM   588  N  N   . PRO   A 1 73  ? 5.782  7.308   5.989  1.00 17.29 ? 79  PRO   A N   1 
ATOM   589  C  CA  . PRO   A 1 73  ? 6.412  8.599   6.311  1.00 17.74 ? 79  PRO   A CA  1 
ATOM   590  C  C   . PRO   A 1 73  ? 5.635  9.785   5.734  1.00 19.21 ? 79  PRO   A C   1 
ATOM   591  O  O   . PRO   A 1 73  ? 5.262  9.764   4.556  1.00 21.11 ? 79  PRO   A O   1 
ATOM   592  C  CB  . PRO   A 1 73  ? 7.842  8.475   5.729  1.00 20.04 ? 79  PRO   A CB  1 
ATOM   593  C  CG  . PRO   A 1 73  ? 7.959  7.120   5.156  1.00 23.63 ? 79  PRO   A CG  1 
ATOM   594  C  CD  . PRO   A 1 73  ? 6.701  6.365   5.307  1.00 19.07 ? 79  PRO   A CD  1 
ATOM   595  N  N   . SER   A 1 74  ? 5.328  10.753  6.591  1.00 18.15 ? 80  SER   A N   1 
ATOM   596  C  CA  . SER   A 1 74  ? 4.469  11.872  6.204  1.00 21.34 ? 80  SER   A CA  1 
ATOM   597  C  C   . SER   A 1 74  ? 4.853  13.145  6.951  1.00 19.26 ? 80  SER   A C   1 
ATOM   598  O  O   . SER   A 1 74  ? 5.664  13.137  7.874  1.00 18.93 ? 80  SER   A O   1 
ATOM   599  C  CB  . SER   A 1 74  ? 3.013  11.519  6.515  1.00 28.87 ? 80  SER   A CB  1 
ATOM   600  O  OG  . SER   A 1 74  ? 2.652  10.329  5.830  1.00 39.88 ? 80  SER   A OG  1 
ATOM   601  N  N   . LEU   A 1 75  ? 4.151  14.252  6.589  1.00 21.40 ? 81  LEU   A N   1 
ATOM   602  C  CA  . LEU   A 1 75  ? 4.338  15.552  7.209  1.00 23.63 ? 81  LEU   A CA  1 
ATOM   603  C  C   . LEU   A 1 75  ? 3.242  15.679  8.272  1.00 24.47 ? 81  LEU   A C   1 
ATOM   604  O  O   . LEU   A 1 75  ? 2.027  15.705  7.948  1.00 26.94 ? 81  LEU   A O   1 
ATOM   605  C  CB  . LEU   A 1 75  ? 4.148  16.624  6.116  1.00 25.54 ? 81  LEU   A CB  1 
ATOM   606  C  CG  . LEU   A 1 75  ? 4.508  18.054  6.467  1.00 28.82 ? 81  LEU   A CG  1 
ATOM   607  C  CD1 . LEU   A 1 75  ? 5.987  18.215  6.738  1.00 28.78 ? 81  LEU   A CD1 1 
ATOM   608  C  CD2 . LEU   A 1 75  ? 4.146  19.012  5.313  1.00 30.25 ? 81  LEU   A CD2 1 
ATOM   609  N  N   . ILE   A 1 76  ? 3.637  15.685  9.539  1.00 22.97 ? 82  ILE   A N   1 
ATOM   610  C  CA  . ILE   A 1 76  ? 2.728  15.673  10.692 1.00 24.53 ? 82  ILE   A CA  1 
ATOM   611  C  C   . ILE   A 1 76  ? 2.989  16.839  11.636 1.00 26.21 ? 82  ILE   A C   1 
ATOM   612  O  O   . ILE   A 1 76  ? 4.144  17.235  11.874 1.00 24.78 ? 82  ILE   A O   1 
ATOM   613  C  CB  . ILE   A 1 76  ? 2.955  14.347  11.450 1.00 25.73 ? 82  ILE   A CB  1 
ATOM   614  C  CG1 . ILE   A 1 76  ? 2.686  13.135  10.496 1.00 28.77 ? 82  ILE   A CG1 1 
ATOM   615  C  CG2 . ILE   A 1 76  ? 2.161  14.293  12.799 1.00 27.64 ? 82  ILE   A CG2 1 
ATOM   616  C  CD1 . ILE   A 1 76  ? 2.758  11.851  11.048 1.00 29.69 ? 82  ILE   A CD1 1 
ATOM   617  N  N   . PHE   A 1 77  ? 1.915  17.434  12.157 1.00 27.94 ? 83  PHE   A N   1 
ATOM   618  C  CA  . PHE   A 1 77  ? 2.058  18.544  13.085 1.00 28.01 ? 83  PHE   A CA  1 
ATOM   619  C  C   . PHE   A 1 77  ? 2.434  17.982  14.440 1.00 28.80 ? 83  PHE   A C   1 
ATOM   620  O  O   . PHE   A 1 77  ? 1.786  17.074  14.938 1.00 30.96 ? 83  PHE   A O   1 
ATOM   621  C  CB  . PHE   A 1 77  ? 0.737  19.341  13.189 1.00 28.97 ? 83  PHE   A CB  1 
ATOM   622  C  CG  . PHE   A 1 77  ? 0.949  20.645  13.890 1.00 31.87 ? 83  PHE   A CG  1 
ATOM   623  C  CD1 . PHE   A 1 77  ? 1.631  21.677  13.269 1.00 33.66 ? 83  PHE   A CD1 1 
ATOM   624  C  CD2 . PHE   A 1 77  ? 0.527  20.818  15.196 1.00 34.23 ? 83  PHE   A CD2 1 
ATOM   625  C  CE1 . PHE   A 1 77  ? 1.849  22.871  13.922 1.00 35.86 ? 83  PHE   A CE1 1 
ATOM   626  C  CE2 . PHE   A 1 77  ? 0.722  22.030  15.843 1.00 34.75 ? 83  PHE   A CE2 1 
ATOM   627  C  CZ  . PHE   A 1 77  ? 1.372  23.047  15.201 1.00 35.47 ? 83  PHE   A CZ  1 
ATOM   628  N  N   . VAL   A 1 78  ? 3.531  18.494  15.027 1.00 27.19 ? 84  VAL   A N   1 
ATOM   629  C  CA  . VAL   A 1 78  ? 3.981  18.030  16.329 1.00 26.36 ? 84  VAL   A CA  1 
ATOM   630  C  C   . VAL   A 1 78  ? 3.897  19.194  17.327 1.00 28.13 ? 84  VAL   A C   1 
ATOM   631  O  O   . VAL   A 1 78  ? 4.370  20.261  17.005 1.00 28.38 ? 84  VAL   A O   1 
ATOM   632  C  CB  . VAL   A 1 78  ? 5.445  17.504  16.220 1.00 24.26 ? 84  VAL   A CB  1 
ATOM   633  C  CG1 . VAL   A 1 78  ? 5.927  16.991  17.576 1.00 24.66 ? 84  VAL   A CG1 1 
ATOM   634  C  CG2 . VAL   A 1 78  ? 5.518  16.391  15.151 1.00 24.53 ? 84  VAL   A CG2 1 
ATOM   635  N  N   . GLU   A 1 79  ? 3.381  18.940  18.532 1.00 29.82 ? 85  GLU   A N   1 
ATOM   636  C  CA  . GLU   A 1 79  ? 3.238  19.973  19.564 1.00 32.74 ? 85  GLU   A CA  1 
ATOM   637  C  C   . GLU   A 1 79  ? 4.595  20.440  20.080 1.00 34.37 ? 85  GLU   A C   1 
ATOM   638  O  O   . GLU   A 1 79  ? 5.582  19.712  19.990 1.00 34.52 ? 85  GLU   A O   1 
ATOM   639  C  CB  . GLU   A 1 79  ? 2.411  19.428  20.745 1.00 36.57 ? 85  GLU   A CB  1 
ATOM   640  C  CG  . GLU   A 1 79  ? 0.940  19.202  20.420 1.00 46.15 ? 85  GLU   A CG  1 
ATOM   641  C  CD  . GLU   A 1 79  ? 0.240  20.402  19.817 1.00 57.42 ? 85  GLU   A CD  1 
ATOM   642  O  OE1 . GLU   A 1 79  ? 0.431  21.536  20.317 1.00 60.20 ? 85  GLU   A OE1 1 
ATOM   643  O  OE2 . GLU   A 1 79  ? -0.481 20.206  18.815 1.00 61.70 ? 85  GLU   A OE2 1 
ATOM   644  N  N   . ALA   A 1 80  ? 4.606  21.634  20.702 1.00 35.05 ? 86  ALA   A N   1 
ATOM   645  C  CA  . ALA   A 1 80  ? 5.808  22.229  21.277 1.00 36.00 ? 86  ALA   A CA  1 
ATOM   646  C  C   . ALA   A 1 80  ? 6.387  21.342  22.337 1.00 36.36 ? 86  ALA   A C   1 
ATOM   647  O  O   . ALA   A 1 80  ? 5.668  20.654  23.072 1.00 37.34 ? 86  ALA   A O   1 
ATOM   648  C  CB  . ALA   A 1 80  ? 5.492  23.583  21.878 1.00 36.81 ? 86  ALA   A CB  1 
ATOM   649  N  N   . SER   A 1 81  ? 7.713  21.270  22.345 1.00 35.96 ? 87  SER   A N   1 
ATOM   650  C  CA  . SER   A 1 81  ? 8.423  20.492  23.347 1.00 35.60 ? 87  SER   A CA  1 
ATOM   651  C  C   . SER   A 1 81  ? 9.543  21.398  23.929 1.00 35.13 ? 87  SER   A C   1 
ATOM   652  O  O   . SER   A 1 81  ? 9.683  22.555  23.525 1.00 34.83 ? 87  SER   A O   1 
ATOM   653  C  CB  . SER   A 1 81  ? 9.048  19.261  22.692 1.00 37.09 ? 87  SER   A CB  1 
ATOM   654  O  OG  . SER   A 1 81  ? 10.067 19.702  21.811 1.00 37.80 ? 87  SER   A OG  1 
ATOM   655  N  N   . GLU   A 1 82  ? 10.438 20.823  24.769 1.00 35.20 ? 88  GLU   A N   1 
ATOM   656  C  CA  . GLU   A 1 82  ? 11.611 21.578  25.258 1.00 34.74 ? 88  GLU   A CA  1 
ATOM   657  C  C   . GLU   A 1 82  ? 12.586 21.881  24.083 1.00 31.59 ? 88  GLU   A C   1 
ATOM   658  O  O   . GLU   A 1 82  ? 13.394 22.806  24.176 1.00 30.59 ? 88  GLU   A O   1 
ATOM   659  C  CB  . GLU   A 1 82  ? 12.406 20.711  26.269 1.00 38.39 ? 88  GLU   A CB  1 
ATOM   660  C  CG  . GLU   A 1 82  ? 11.548 19.929  27.246 1.00 46.56 ? 88  GLU   A CG  1 
ATOM   661  C  CD  . GLU   A 1 82  ? 12.295 18.762  27.855 1.00 54.16 ? 88  GLU   A CD  1 
ATOM   662  O  OE1 . GLU   A 1 82  ? 11.890 17.596  27.622 1.00 55.82 ? 88  GLU   A OE1 1 
ATOM   663  O  OE2 . GLU   A 1 82  ? 13.312 19.017  28.541 1.00 55.59 ? 88  GLU   A OE2 1 
ATOM   664  N  N   . TYR   A 1 83  ? 12.512 21.114  22.976 1.00 29.76 ? 89  TYR   A N   1 
ATOM   665  C  CA  . TYR   A 1 83  ? 13.506 21.260  21.900 1.00 27.30 ? 89  TYR   A CA  1 
ATOM   666  C  C   . TYR   A 1 83  ? 13.055 21.924  20.627 1.00 25.91 ? 89  TYR   A C   1 
ATOM   667  O  O   . TYR   A 1 83  ? 13.884 22.387  19.857 1.00 26.07 ? 89  TYR   A O   1 
ATOM   668  C  CB  . TYR   A 1 83  ? 14.063 19.893  21.558 1.00 26.78 ? 89  TYR   A CB  1 
ATOM   669  C  CG  . TYR   A 1 83  ? 14.674 19.212  22.759 1.00 27.48 ? 89  TYR   A CG  1 
ATOM   670  C  CD1 . TYR   A 1 83  ? 15.964 19.511  23.170 1.00 29.97 ? 89  TYR   A CD1 1 
ATOM   671  C  CD2 . TYR   A 1 83  ? 13.939 18.328  23.526 1.00 30.01 ? 89  TYR   A CD2 1 
ATOM   672  C  CE1 . TYR   A 1 83  ? 16.537 18.870  24.261 1.00 31.47 ? 89  TYR   A CE1 1 
ATOM   673  C  CE2 . TYR   A 1 83  ? 14.498 17.687  24.621 1.00 31.60 ? 89  TYR   A CE2 1 
ATOM   674  C  CZ  . TYR   A 1 83  ? 15.779 17.999  25.018 1.00 33.35 ? 89  TYR   A CZ  1 
ATOM   675  O  OH  . TYR   A 1 83  ? 16.328 17.318  26.078 1.00 36.92 ? 89  TYR   A OH  1 
ATOM   676  N  N   . TYR   A 1 84  ? 11.728 21.947  20.379 1.00 26.40 ? 90  TYR   A N   1 
ATOM   677  C  CA  . TYR   A 1 84  ? 11.233 22.582  19.152 1.00 25.24 ? 90  TYR   A CA  1 
ATOM   678  C  C   . TYR   A 1 84  ? 9.901  23.280  19.491 1.00 27.68 ? 90  TYR   A C   1 
ATOM   679  O  O   . TYR   A 1 84  ? 9.134  22.731  20.297 1.00 28.84 ? 90  TYR   A O   1 
ATOM   680  C  CB  . TYR   A 1 84  ? 10.905 21.521  18.057 1.00 24.80 ? 90  TYR   A CB  1 
ATOM   681  C  CG  . TYR   A 1 84  ? 12.072 20.719  17.504 1.00 22.03 ? 90  TYR   A CG  1 
ATOM   682  C  CD1 . TYR   A 1 84  ? 13.014 21.304  16.676 1.00 21.31 ? 90  TYR   A CD1 1 
ATOM   683  C  CD2 . TYR   A 1 84  ? 12.228 19.386  17.823 1.00 20.35 ? 90  TYR   A CD2 1 
ATOM   684  C  CE1 . TYR   A 1 84  ? 14.085 20.561  16.169 1.00 20.03 ? 90  TYR   A CE1 1 
ATOM   685  C  CE2 . TYR   A 1 84  ? 13.271 18.634  17.312 1.00 19.27 ? 90  TYR   A CE2 1 
ATOM   686  C  CZ  . TYR   A 1 84  ? 14.221 19.241  16.531 1.00 18.93 ? 90  TYR   A CZ  1 
ATOM   687  O  OH  . TYR   A 1 84  ? 15.280 18.496  16.034 1.00 16.86 ? 90  TYR   A OH  1 
ATOM   688  N  N   . PRO   A 1 85  ? 9.558  24.312  18.743 1.00 29.42 ? 91  PRO   A N   1 
ATOM   689  C  CA  . PRO   A 1 85  ? 8.196  24.881  18.872 1.00 31.55 ? 91  PRO   A CA  1 
ATOM   690  C  C   . PRO   A 1 85  ? 7.201  23.913  18.198 1.00 33.53 ? 91  PRO   A C   1 
ATOM   691  O  O   . PRO   A 1 85  ? 7.621  22.943  17.522 1.00 33.30 ? 91  PRO   A O   1 
ATOM   692  C  CB  . PRO   A 1 85  ? 8.303  26.199  18.085 1.00 33.32 ? 91  PRO   A CB  1 
ATOM   693  C  CG  . PRO   A 1 85  ? 9.310  25.913  17.031 1.00 33.08 ? 91  PRO   A CG  1 
ATOM   694  C  CD  . PRO   A 1 85  ? 10.334 24.983  17.669 1.00 29.41 ? 91  PRO   A CD  1 
ATOM   695  N  N   . ALA   A 1 86  ? 5.884  24.184  18.294 1.00 34.50 ? 92  ALA   A N   1 
ATOM   696  C  CA  . ALA   A 1 86  ? 4.888  23.374  17.582 1.00 34.13 ? 92  ALA   A CA  1 
ATOM   697  C  C   . ALA   A 1 86  ? 5.127  23.650  16.079 1.00 32.94 ? 92  ALA   A C   1 
ATOM   698  O  O   . ALA   A 1 86  ? 5.391  24.777  15.692 1.00 34.17 ? 92  ALA   A O   1 
ATOM   699  C  CB  . ALA   A 1 86  ? 3.474  23.792  17.993 1.00 34.49 ? 92  ALA   A CB  1 
ATOM   700  N  N   . ARG   A 1 87  ? 5.256  22.579  15.277 1.00 31.44 ? 93  ARG   A N   1 
ATOM   701  C  CA  . ARG   A 1 87  ? 5.609  22.737  13.870 1.00 29.56 ? 93  ARG   A CA  1 
ATOM   702  C  C   . ARG   A 1 87  ? 5.290  21.425  13.125 1.00 27.88 ? 93  ARG   A C   1 
ATOM   703  O  O   . ARG   A 1 87  ? 4.980  20.427  13.750 1.00 29.94 ? 93  ARG   A O   1 
ATOM   704  C  CB  . ARG   A 1 87  ? 7.138  22.984  13.758 1.00 30.38 ? 93  ARG   A CB  1 
ATOM   705  C  CG  . ARG   A 1 87  ? 7.981  21.686  14.011 1.00 29.95 ? 93  ARG   A CG  1 
ATOM   706  C  CD  . ARG   A 1 87  ? 9.444  21.939  14.152 1.00 28.01 ? 93  ARG   A CD  1 
ATOM   707  N  NE  . ARG   A 1 87  ? 10.382 20.813  13.856 1.00 26.58 ? 93  ARG   A NE  1 
ATOM   708  C  CZ  . ARG   A 1 87  ? 10.383 19.605  14.398 1.00 26.04 ? 93  ARG   A CZ  1 
ATOM   709  N  NH1 . ARG   A 1 87  ? 9.417  19.246  15.234 1.00 27.75 ? 93  ARG   A NH1 1 
ATOM   710  N  NH2 . ARG   A 1 87  ? 11.346 18.729  14.095 1.00 20.64 ? 93  ARG   A NH2 1 
ATOM   711  N  N   . TYR   A 1 88  ? 5.453  21.445  11.796 1.00 27.13 ? 94  TYR   A N   1 
ATOM   712  C  CA  . TYR   A 1 88  ? 5.338  20.252  10.974 1.00 27.67 ? 94  TYR   A CA  1 
ATOM   713  C  C   . TYR   A 1 88  ? 6.690  19.581  10.894 1.00 24.93 ? 94  TYR   A C   1 
ATOM   714  O  O   . TYR   A 1 88  ? 7.691  20.205  10.556 1.00 25.76 ? 94  TYR   A O   1 
ATOM   715  C  CB  . TYR   A 1 88  ? 4.882  20.587  9.552  1.00 28.66 ? 94  TYR   A CB  1 
ATOM   716  C  CG  . TYR   A 1 88  ? 3.407  20.917  9.508  1.00 29.72 ? 94  TYR   A CG  1 
ATOM   717  C  CD1 . TYR   A 1 88  ? 2.450  19.912  9.489  1.00 30.60 ? 94  TYR   A CD1 1 
ATOM   718  C  CD2 . TYR   A 1 88  ? 2.962  22.226  9.605  1.00 30.83 ? 94  TYR   A CD2 1 
ATOM   719  C  CE1 . TYR   A 1 88  ? 1.096  20.198  9.538  1.00 32.34 ? 94  TYR   A CE1 1 
ATOM   720  C  CE2 . TYR   A 1 88  ? 1.607  22.522  9.663  1.00 32.58 ? 94  TYR   A CE2 1 
ATOM   721  C  CZ  . TYR   A 1 88  ? 0.676  21.503  9.622  1.00 33.54 ? 94  TYR   A CZ  1 
ATOM   722  O  OH  . TYR   A 1 88  ? -0.678 21.742  9.661  1.00 37.26 ? 94  TYR   A OH  1 
ATOM   723  N  N   . GLN   A 1 89  ? 6.718  18.269  11.190 1.00 22.12 ? 95  GLN   A N   1 
ATOM   724  C  CA  . GLN   A 1 89  ? 7.922  17.424  11.082 1.00 19.80 ? 95  GLN   A CA  1 
ATOM   725  C  C   . GLN   A 1 89  ? 7.707  16.517  9.872  1.00 18.92 ? 95  GLN   A C   1 
ATOM   726  O  O   . GLN   A 1 89  ? 6.638  15.902  9.739  1.00 19.25 ? 95  GLN   A O   1 
ATOM   727  C  CB  . GLN   A 1 89  ? 8.177  16.643  12.372 1.00 19.58 ? 95  GLN   A CB  1 
ATOM   728  C  CG  . GLN   A 1 89  ? 9.384  15.744  12.253 1.00 18.12 ? 95  GLN   A CG  1 
ATOM   729  C  CD  . GLN   A 1 89  ? 9.937  15.287  13.593 1.00 17.63 ? 95  GLN   A CD  1 
ATOM   730  O  OE1 . GLN   A 1 89  ? 9.973  16.014  14.579 1.00 18.95 ? 95  GLN   A OE1 1 
ATOM   731  N  NE2 . GLN   A 1 89  ? 10.428 14.041  13.634 1.00 16.23 ? 95  GLN   A NE2 1 
ATOM   732  N  N   . SER   A 1 90  ? 8.708  16.395  9.022  1.00 16.68 ? 96  SER   A N   1 
ATOM   733  C  CA  . SER   A 1 90  ? 8.603  15.584  7.823  1.00 17.63 ? 96  SER   A CA  1 
ATOM   734  C  C   . SER   A 1 90  ? 9.190  14.187  8.042  1.00 16.77 ? 96  SER   A C   1 
ATOM   735  O  O   . SER   A 1 90  ? 9.969  13.978  8.995  1.00 17.26 ? 96  SER   A O   1 
ATOM   736  C  CB  . SER   A 1 90  ? 9.306  16.290  6.670  1.00 21.18 ? 96  SER   A CB  1 
ATOM   737  O  OG  . SER   A 1 90  ? 10.691 16.416  6.955  1.00 24.07 ? 96  SER   A OG  1 
ATOM   738  N  N   . HIS   A 1 91  ? 8.796  13.252  7.144  1.00 17.40 ? 97  HIS   A N   1 
ATOM   739  C  CA  . HIS   A 1 91  ? 9.287  11.875  7.122  1.00 16.40 ? 97  HIS   A CA  1 
ATOM   740  C  C   . HIS   A 1 91  ? 9.027  11.194  8.481  1.00 16.18 ? 97  HIS   A C   1 
ATOM   741  O  O   . HIS   A 1 91  ? 9.839  10.352  8.922  1.00 16.24 ? 97  HIS   A O   1 
ATOM   742  C  CB  . HIS   A 1 91  ? 10.798 11.820  6.735  1.00 17.85 ? 97  HIS   A CB  1 
ATOM   743  C  CG  . HIS   A 1 91  ? 11.086 12.388  5.361  1.00 18.83 ? 97  HIS   A CG  1 
ATOM   744  N  ND1 . HIS   A 1 91  ? 11.215 11.567  4.262  1.00 21.92 ? 97  HIS   A ND1 1 
ATOM   745  C  CD2 . HIS   A 1 91  ? 11.233 13.670  4.975  1.00 21.31 ? 97  HIS   A CD2 1 
ATOM   746  C  CE1 . HIS   A 1 91  ? 11.485 12.372  3.234  1.00 21.77 ? 97  HIS   A CE1 1 
ATOM   747  N  NE2 . HIS   A 1 91  ? 11.508 13.642  3.612  1.00 22.79 ? 97  HIS   A NE2 1 
ATOM   748  N  N   . LEU   A 1 92  ? 7.898  11.493  9.102  1.00 14.92 ? 98  LEU   A N   1 
ATOM   749  C  CA  . LEU   A 1 92  ? 7.546  10.964  10.421 1.00 15.58 ? 98  LEU   A CA  1 
ATOM   750  C  C   . LEU   A 1 92  ? 6.476  9.881   10.245 1.00 15.34 ? 98  LEU   A C   1 
ATOM   751  O  O   . LEU   A 1 92  ? 5.566  10.023  9.426  1.00 16.50 ? 98  LEU   A O   1 
ATOM   752  C  CB  . LEU   A 1 92  ? 6.979  12.111  11.310 1.00 16.83 ? 98  LEU   A CB  1 
ATOM   753  C  CG  . LEU   A 1 92  ? 6.672  11.708  12.775 1.00 20.13 ? 98  LEU   A CG  1 
ATOM   754  C  CD1 . LEU   A 1 92  ? 7.926  11.404  13.521 1.00 20.03 ? 98  LEU   A CD1 1 
ATOM   755  C  CD2 . LEU   A 1 92  ? 5.992  12.889  13.539 1.00 23.18 ? 98  LEU   A CD2 1 
ATOM   756  N  N   . MET   A 1 93  ? 6.613  8.786   11.007 1.00 14.89 ? 99  MET   A N   1 
ATOM   757  C  CA  . MET   A 1 93  ? 5.650  7.662   10.972 1.00 14.18 ? 99  MET   A CA  1 
ATOM   758  C  C   . MET   A 1 93  ? 5.058  7.519   12.385 1.00 15.56 ? 99  MET   A C   1 
ATOM   759  O  O   . MET   A 1 93  ? 5.827  7.505   13.360 1.00 16.11 ? 99  MET   A O   1 
ATOM   760  C  CB  . MET   A 1 93  ? 6.409  6.384   10.611 1.00 14.74 ? 99  MET   A CB  1 
ATOM   761  C  CG  . MET   A 1 93  ? 7.040  6.480   9.214  1.00 16.33 ? 99  MET   A CG  1 
ATOM   762  S  SD  . MET   A 1 93  ? 8.136  5.095   8.720  1.00 18.38 ? 99  MET   A SD  1 
ATOM   763  C  CE  . MET   A 1 93  ? 9.353  5.238   9.992  1.00 21.68 ? 99  MET   A CE  1 
ATOM   764  N  N   . LEU   A 1 94  ? 3.726  7.354   12.531 1.00 15.11 ? 100 LEU   A N   1 
ATOM   765  C  CA  . LEU   A 1 94  ? 3.130  7.238   13.847 1.00 15.92 ? 100 LEU   A CA  1 
ATOM   766  C  C   . LEU   A 1 94  ? 2.632  5.824   14.112 1.00 15.13 ? 100 LEU   A C   1 
ATOM   767  O  O   . LEU   A 1 94  ? 2.185  5.118   13.182 1.00 15.95 ? 100 LEU   A O   1 
ATOM   768  C  CB  . LEU   A 1 94  ? 1.933  8.201   14.011 1.00 18.48 ? 100 LEU   A CB  1 
ATOM   769  C  CG  . LEU   A 1 94  ? 2.219  9.675   13.945 1.00 23.20 ? 100 LEU   A CG  1 
ATOM   770  C  CD1 . LEU   A 1 94  ? 0.952  10.500  14.301 1.00 24.55 ? 100 LEU   A CD1 1 
ATOM   771  C  CD2 . LEU   A 1 94  ? 3.280  10.086  14.940 1.00 25.35 ? 100 LEU   A CD2 1 
ATOM   772  N  N   . ALA   A 1 95  ? 2.628  5.435   15.387 1.00 14.77 ? 101 ALA   A N   1 
ATOM   773  C  CA  . ALA   A 1 95  ? 2.123  4.120   15.806 1.00 14.31 ? 101 ALA   A CA  1 
ATOM   774  C  C   . ALA   A 1 95  ? 1.510  4.304   17.202 1.00 14.41 ? 101 ALA   A C   1 
ATOM   775  O  O   . ALA   A 1 95  ? 1.799  5.297   17.900 1.00 15.08 ? 101 ALA   A O   1 
ATOM   776  C  CB  . ALA   A 1 95  ? 3.298  3.097   15.941 1.00 14.87 ? 101 ALA   A CB  1 
ATOM   777  N  N   . VAL   A 1 96  ? 0.712  3.327   17.606 1.00 13.91 ? 102 VAL   A N   1 
ATOM   778  C  CA  . VAL   A 1 96  ? 0.194  3.260   18.946 1.00 13.89 ? 102 VAL   A CA  1 
ATOM   779  C  C   . VAL   A 1 96  ? 1.230  2.441   19.787 1.00 15.76 ? 102 VAL   A C   1 
ATOM   780  O  O   . VAL   A 1 96  ? 1.584  1.324   19.451 1.00 18.44 ? 102 VAL   A O   1 
ATOM   781  C  CB  . VAL   A 1 96  ? -1.155 2.536   18.943 1.00 14.07 ? 102 VAL   A CB  1 
ATOM   782  C  CG1 . VAL   A 1 96  ? -1.652 2.303   20.376 1.00 16.02 ? 102 VAL   A CG1 1 
ATOM   783  C  CG2 . VAL   A 1 96  ? -2.162 3.349   18.139 1.00 15.36 ? 102 VAL   A CG2 1 
ATOM   784  N  N   . GLY   A 1 97  ? 1.751  3.101   20.786 1.00 16.68 ? 103 GLY   A N   1 
ATOM   785  C  CA  . GLY   A 1 97  ? 2.781  2.483   21.629 1.00 17.51 ? 103 GLY   A CA  1 
ATOM   786  C  C   . GLY   A 1 97  ? 3.177  3.435   22.712 1.00 16.87 ? 103 GLY   A C   1 
ATOM   787  O  O   . GLY   A 1 97  ? 2.986  4.654   22.614 1.00 18.05 ? 103 GLY   A O   1 
ATOM   788  N  N   . HIS   A 1 98  ? 3.724  2.877   23.819 1.00 18.17 ? 104 HIS   A N   1 
ATOM   789  C  CA  . HIS   A 1 98  ? 4.161  3.724   24.898 1.00 19.84 ? 104 HIS   A CA  1 
ATOM   790  C  C   . HIS   A 1 98  ? 5.425  4.486   24.552 1.00 18.96 ? 104 HIS   A C   1 
ATOM   791  O  O   . HIS   A 1 98  ? 6.390  3.921   23.989 1.00 17.89 ? 104 HIS   A O   1 
ATOM   792  C  CB  . HIS   A 1 98  ? 4.404  2.912   26.195 1.00 19.55 ? 104 HIS   A CB  1 
ATOM   793  C  CG  . HIS   A 1 98  ? 4.789  3.809   27.332 1.00 19.64 ? 104 HIS   A CG  1 
ATOM   794  N  ND1 . HIS   A 1 98  ? 3.868  4.692   27.895 1.00 19.64 ? 104 HIS   A ND1 1 
ATOM   795  C  CD2 . HIS   A 1 98  ? 6.004  4.031   27.915 1.00 20.90 ? 104 HIS   A CD2 1 
ATOM   796  C  CE1 . HIS   A 1 98  ? 4.567  5.416   28.784 1.00 20.92 ? 104 HIS   A CE1 1 
ATOM   797  N  NE2 . HIS   A 1 98  ? 5.846  5.015   28.847 1.00 20.99 ? 104 HIS   A NE2 1 
ATOM   798  N  N   . SER   A 1 99  ? 5.443  5.715   24.874 1.00 19.80 ? 105 SER   A N   1 
ATOM   799  C  CA  . SER   A 1 99  ? 6.608  6.517   24.804 1.00 17.27 ? 105 SER   A CA  1 
ATOM   800  C  C   . SER   A 1 99  ? 6.589  7.625   25.821 1.00 19.11 ? 105 SER   A C   1 
ATOM   801  O  O   . SER   A 1 99  ? 5.491  8.096   26.160 1.00 21.40 ? 105 SER   A O   1 
ATOM   802  C  CB  . SER   A 1 99  ? 6.950  6.989   23.392 1.00 19.79 ? 105 SER   A CB  1 
ATOM   803  O  OG  . SER   A 1 99  ? 5.949  7.859   22.891 1.00 20.27 ? 105 SER   A OG  1 
ATOM   804  N  N   . GLU   A 1 100 ? 7.834  8.094   26.215 1.00 17.43 ? 106 GLU   A N   1 
ATOM   805  C  CA  . GLU   A 1 100 ? 8.205  9.228   27.082 1.00 18.21 ? 106 GLU   A CA  1 
ATOM   806  C  C   . GLU   A 1 100 ? 9.342  9.996   26.442 1.00 20.03 ? 106 GLU   A C   1 
ATOM   807  O  O   . GLU   A 1 100 ? 10.025 9.502   25.515 1.00 19.24 ? 106 GLU   A O   1 
ATOM   808  C  CB  . GLU   A 1 100 ? 8.576  8.747   28.507 1.00 18.34 ? 106 GLU   A CB  1 
ATOM   809  C  CG  . GLU   A 1 100 ? 7.397  8.072   29.154 1.00 19.96 ? 106 GLU   A CG  1 
ATOM   810  C  CD  . GLU   A 1 100 ? 7.637  7.427   30.518 1.00 20.93 ? 106 GLU   A CD  1 
ATOM   811  O  OE1 . GLU   A 1 100 ? 8.409  8.016   31.301 1.00 26.70 ? 106 GLU   A OE1 1 
ATOM   812  O  OE2 . GLU   A 1 100 ? 7.061  6.367   30.818 1.00 20.61 ? 106 GLU   A OE2 1 
ATOM   813  N  N   . PRO   A 1 101 ? 9.538  11.263  26.792 1.00 20.74 ? 107 PRO   A N   1 
ATOM   814  C  CA  . PRO   A 1 101 ? 10.524 12.088  26.052 1.00 20.91 ? 107 PRO   A CA  1 
ATOM   815  C  C   . PRO   A 1 101 ? 11.935 11.449  25.873 1.00 20.46 ? 107 PRO   A C   1 
ATOM   816  O  O   . PRO   A 1 101 ? 12.505 11.442  24.742 1.00 20.65 ? 107 PRO   A O   1 
ATOM   817  C  CB  . PRO   A 1 101 ? 10.491 13.432  26.830 1.00 22.18 ? 107 PRO   A CB  1 
ATOM   818  C  CG  . PRO   A 1 101 ? 9.075  13.486  27.357 1.00 23.73 ? 107 PRO   A CG  1 
ATOM   819  C  CD  . PRO   A 1 101 ? 8.741  12.071  27.752 1.00 21.65 ? 107 PRO   A CD  1 
ATOM   820  N  N   . GLY   A 1 102 ? 12.478 10.819  26.917 1.00 19.18 ? 108 GLY   A N   1 
ATOM   821  C  CA  . GLY   A 1 102 ? 13.786 10.165  26.882 1.00 17.79 ? 108 GLY   A CA  1 
ATOM   822  C  C   . GLY   A 1 102 ? 13.844 8.854   26.106 1.00 15.75 ? 108 GLY   A C   1 
ATOM   823  O  O   . GLY   A 1 102 ? 14.916 8.252   25.976 1.00 15.83 ? 108 GLY   A O   1 
ATOM   824  N  N   . ASP   A 1 103 ? 12.695 8.397   25.586 1.00 14.99 ? 109 ASP   A N   1 
ATOM   825  C  CA  . ASP   A 1 103 ? 12.679 7.247   24.679 1.00 14.93 ? 109 ASP   A CA  1 
ATOM   826  C  C   . ASP   A 1 103 ? 13.206 7.596   23.282 1.00 13.76 ? 109 ASP   A C   1 
ATOM   827  O  O   . ASP   A 1 103 ? 13.482 6.685   22.474 1.00 13.31 ? 109 ASP   A O   1 
ATOM   828  C  CB  . ASP   A 1 103 ? 11.255 6.650   24.575 1.00 13.71 ? 109 ASP   A CB  1 
ATOM   829  C  CG  . ASP   A 1 103 ? 10.884 5.900   25.823 1.00 14.35 ? 109 ASP   A CG  1 
ATOM   830  O  OD1 . ASP   A 1 103 ? 11.759 5.272   26.390 1.00 14.03 ? 109 ASP   A OD1 1 
ATOM   831  O  OD2 . ASP   A 1 103 ? 9.686  5.958   26.230 1.00 15.12 ? 109 ASP   A OD2 1 
ATOM   832  N  N   . CYS   A 1 104 ? 13.376 8.906   22.964 1.00 13.45 ? 110 CYS   A N   1 
ATOM   833  C  CA  . CYS   A 1 104 ? 13.951 9.287   21.646 1.00 13.96 ? 110 CYS   A CA  1 
ATOM   834  C  C   . CYS   A 1 104 ? 15.285 8.605   21.448 1.00 13.61 ? 110 CYS   A C   1 
ATOM   835  O  O   . CYS   A 1 104 ? 16.108 8.489   22.355 1.00 14.24 ? 110 CYS   A O   1 
ATOM   836  C  CB  . CYS   A 1 104 ? 14.096 10.804  21.582 1.00 15.33 ? 110 CYS   A CB  1 
ATOM   837  S  SG  . CYS   A 1 104 ? 12.521 11.665  21.303 1.00 16.93 ? 110 CYS   A SG  1 
ATOM   838  N  N   . GLY   A 1 105 ? 15.459 8.033   20.251 1.00 12.62 ? 111 GLY   A N   1 
ATOM   839  C  CA  . GLY   A 1 105 ? 16.688 7.363   19.897 1.00 12.70 ? 111 GLY   A CA  1 
ATOM   840  C  C   . GLY   A 1 105 ? 16.534 5.851   19.812 1.00 12.41 ? 111 GLY   A C   1 
ATOM   841  O  O   . GLY   A 1 105 ? 17.405 5.159   19.272 1.00 13.53 ? 111 GLY   A O   1 
ATOM   842  N  N   . GLY   A 1 106 ? 15.463 5.319   20.411 1.00 12.82 ? 112 GLY   A N   1 
ATOM   843  C  CA  . GLY   A 1 106 ? 15.216 3.883   20.320 1.00 12.12 ? 112 GLY   A CA  1 
ATOM   844  C  C   . GLY   A 1 106 ? 14.992 3.445   18.869 1.00 11.06 ? 112 GLY   A C   1 
ATOM   845  O  O   . GLY   A 1 106 ? 14.296 4.145   18.116 1.00 11.66 ? 112 GLY   A O   1 
ATOM   846  N  N   . ILE   A 1 107 ? 15.554 2.303   18.485 1.00 11.51 ? 113 ILE   A N   1 
ATOM   847  C  CA  . ILE   A 1 107 ? 15.402 1.843   17.099 1.00 11.63 ? 113 ILE   A CA  1 
ATOM   848  C  C   . ILE   A 1 107 ? 14.089 1.172   16.813 1.00 10.93 ? 113 ILE   A C   1 
ATOM   849  O  O   . ILE   A 1 107 ? 13.610 0.344   17.596 1.00 11.20 ? 113 ILE   A O   1 
ATOM   850  C  CB  . ILE   A 1 107 ? 16.584 0.878   16.775 1.00 11.83 ? 113 ILE   A CB  1 
ATOM   851  C  CG1 . ILE   A 1 107 ? 17.841 1.742   16.497 1.00 13.21 ? 113 ILE   A CG1 1 
ATOM   852  C  CG2 . ILE   A 1 107 ? 16.324 -0.033  15.552 1.00 13.00 ? 113 ILE   A CG2 1 
ATOM   853  C  CD1 . ILE   A 1 107 ? 19.112 0.917   16.407 1.00 15.77 ? 113 ILE   A CD1 1 
ATOM   854  N  N   . LEU   A 1 108 ? 13.510 1.520   15.647 1.00 10.34 ? 114 LEU   A N   1 
ATOM   855  C  CA  . LEU   A 1 108 ? 12.421 0.776   15.013 1.00 10.36 ? 114 LEU   A CA  1 
ATOM   856  C  C   . LEU   A 1 108 ? 13.059 -0.080  13.900 1.00 10.42 ? 114 LEU   A C   1 
ATOM   857  O  O   . LEU   A 1 108 ? 13.835 0.455   13.079 1.00 11.39 ? 114 LEU   A O   1 
ATOM   858  C  CB  . LEU   A 1 108 ? 11.415 1.772   14.382 1.00 10.89 ? 114 LEU   A CB  1 
ATOM   859  C  CG  . LEU   A 1 108 ? 10.344 1.133   13.476 1.00 11.46 ? 114 LEU   A CG  1 
ATOM   860  C  CD1 . LEU   A 1 108 ? 9.365  0.322   14.307 1.00 12.90 ? 114 LEU   A CD1 1 
ATOM   861  C  CD2 . LEU   A 1 108 ? 9.545  2.224   12.697 1.00 13.79 ? 114 LEU   A CD2 1 
ATOM   862  N  N   . ARG   A 1 109 ? 12.734 -1.355  13.842 1.00 11.32 ? 115 ARG   A N   1 
ATOM   863  C  CA  . ARG   A 1 109 ? 13.325 -2.279  12.841 1.00 11.29 ? 115 ARG   A CA  1 
ATOM   864  C  C   . ARG   A 1 109 ? 12.295 -3.221  12.297 1.00 12.38 ? 115 ARG   A C   1 
ATOM   865  O  O   . ARG   A 1 109 ? 11.254 -3.497  12.914 1.00 12.43 ? 115 ARG   A O   1 
ATOM   866  C  CB  . ARG   A 1 109 ? 14.516 -3.058  13.490 1.00 12.60 ? 115 ARG   A CB  1 
ATOM   867  C  CG  . ARG   A 1 109 ? 14.031 -4.047  14.552 1.00 13.45 ? 115 ARG   A CG  1 
ATOM   868  C  CD  . ARG   A 1 109 ? 15.252 -4.809  15.108 1.00 14.93 ? 115 ARG   A CD  1 
ATOM   869  N  NE  . ARG   A 1 109 ? 16.037 -3.931  15.967 1.00 15.88 ? 115 ARG   A NE  1 
ATOM   870  C  CZ  . ARG   A 1 109 ? 17.333 -3.708  15.840 1.00 15.68 ? 115 ARG   A CZ  1 
ATOM   871  N  NH1 . ARG   A 1 109 ? 17.998 -4.166  14.775 1.00 16.05 ? 115 ARG   A NH1 1 
ATOM   872  N  NH2 . ARG   A 1 109 ? 17.979 -2.975  16.742 1.00 16.58 ? 115 ARG   A NH2 1 
ATOM   873  N  N   . CYS   A 1 110 ? 12.600 -3.767  11.116 1.00 13.89 ? 116 CYS   A N   1 
ATOM   874  C  CA  . CYS   A 1 110 ? 11.797 -4.820  10.474 1.00 17.22 ? 116 CYS   A CA  1 
ATOM   875  C  C   . CYS   A 1 110 ? 12.752 -5.967  10.092 1.00 20.20 ? 116 CYS   A C   1 
ATOM   876  O  O   . CYS   A 1 110 ? 13.912 -5.958  10.451 1.00 20.00 ? 116 CYS   A O   1 
ATOM   877  C  CB  . CYS   A 1 110 ? 11.080 -4.225  9.283  1.00 17.86 ? 116 CYS   A CB  1 
ATOM   878  S  SG  . CYS   A 1 110 ? 12.203 -3.755  7.913  1.00 17.87 ? 116 CYS   A SG  1 
ATOM   879  N  N   . GLN   A 1 111 ? 12.246 -7.028  9.366  1.00 24.07 ? 117 GLN   A N   1 
ATOM   880  C  CA  . GLN   A 1 111 ? 13.140 -8.129  8.954  1.00 25.92 ? 117 GLN   A CA  1 
ATOM   881  C  C   . GLN   A 1 111 ? 14.297 -7.686  8.044  1.00 25.62 ? 117 GLN   A C   1 
ATOM   882  O  O   . GLN   A 1 111 ? 15.308 -8.376  7.967  1.00 28.87 ? 117 GLN   A O   1 
ATOM   883  C  CB  . GLN   A 1 111 ? 12.394 -9.281  8.228  1.00 28.67 ? 117 GLN   A CB  1 
ATOM   884  C  CG  . GLN   A 1 111 ? 11.676 -8.782  6.976  1.00 35.21 ? 117 GLN   A CG  1 
ATOM   885  C  CD  . GLN   A 1 111 ? 10.189 -8.777  7.177  1.00 41.28 ? 117 GLN   A CD  1 
ATOM   886  O  OE1 . GLN   A 1 111 ? 9.421  -9.422  6.433  1.00 42.23 ? 117 GLN   A OE1 1 
ATOM   887  N  NE2 . GLN   A 1 111 ? 9.739  -8.088  8.224  1.00 40.83 ? 117 GLN   A NE2 1 
ATOM   888  N  N   . HIS   A 1 112 ? 14.166 -6.507  7.405  1.00 21.69 ? 118 HIS   A N   1 
ATOM   889  C  CA  . HIS   A 1 112 ? 15.194 -5.994  6.464  1.00 20.55 ? 118 HIS   A CA  1 
ATOM   890  C  C   . HIS   A 1 112 ? 16.285 -5.178  7.123  1.00 20.20 ? 118 HIS   A C   1 
ATOM   891  O  O   . HIS   A 1 112 ? 17.301 -4.859  6.502  1.00 22.02 ? 118 HIS   A O   1 
ATOM   892  C  CB  . HIS   A 1 112 ? 14.526 -5.178  5.359  1.00 19.43 ? 118 HIS   A CB  1 
ATOM   893  C  CG  . HIS   A 1 112 ? 13.459 -5.973  4.660  1.00 20.69 ? 118 HIS   A CG  1 
ATOM   894  N  ND1 . HIS   A 1 112 ? 12.128 -5.691  4.832  1.00 21.87 ? 118 HIS   A ND1 1 
ATOM   895  C  CD2 . HIS   A 1 112 ? 13.583 -7.042  3.823  1.00 24.01 ? 118 HIS   A CD2 1 
ATOM   896  C  CE1 . HIS   A 1 112 ? 11.468 -6.605  4.114  1.00 24.95 ? 118 HIS   A CE1 1 
ATOM   897  N  NE2 . HIS   A 1 112 ? 12.320 -7.427  3.487  1.00 26.52 ? 118 HIS   A NE2 1 
ATOM   898  N  N   . GLY   A 1 113 ? 16.034 -4.720  8.364  1.00 18.33 ? 119 GLY   A N   1 
ATOM   899  C  CA  . GLY   A 1 113 ? 17.014 -3.900  9.041  1.00 16.92 ? 119 GLY   A CA  1 
ATOM   900  C  C   . GLY   A 1 113 ? 16.354 -2.745  9.794  1.00 14.58 ? 119 GLY   A C   1 
ATOM   901  O  O   . GLY   A 1 113 ? 15.164 -2.783  10.125 1.00 15.19 ? 119 GLY   A O   1 
ATOM   902  N  N   . VAL   A 1 114 ? 17.167 -1.723  10.063 1.00 12.88 ? 120 VAL   A N   1 
ATOM   903  C  CA  . VAL   A 1 114 ? 16.702 -0.532  10.818 1.00 12.83 ? 120 VAL   A CA  1 
ATOM   904  C  C   . VAL   A 1 114 ? 15.844 0.377   9.934  1.00 11.58 ? 120 VAL   A C   1 
ATOM   905  O  O   . VAL   A 1 114 ? 16.269 0.739   8.811  1.00 12.43 ? 120 VAL   A O   1 
ATOM   906  C  CB  . VAL   A 1 114 ? 17.924 0.235   11.400 1.00 12.83 ? 120 VAL   A CB  1 
ATOM   907  C  CG1 . VAL   A 1 114 ? 17.482 1.541   12.089 1.00 13.82 ? 120 VAL   A CG1 1 
ATOM   908  C  CG2 . VAL   A 1 114 ? 18.695 -0.655  12.389 1.00 14.12 ? 120 VAL   A CG2 1 
ATOM   909  N  N   . VAL   A 1 115 ? 14.697 0.770   10.430 1.00 11.10 ? 121 VAL   A N   1 
ATOM   910  C  CA  . VAL   A 1 115 ? 13.746 1.582   9.710  1.00 12.23 ? 121 VAL   A CA  1 
ATOM   911  C  C   . VAL   A 1 115 ? 13.861 3.049   10.131 1.00 12.34 ? 121 VAL   A C   1 
ATOM   912  O  O   . VAL   A 1 115 ? 13.724 3.965   9.307  1.00 13.30 ? 121 VAL   A O   1 
ATOM   913  C  CB  . VAL   A 1 115 ? 12.298 1.062   9.987  1.00 12.82 ? 121 VAL   A CB  1 
ATOM   914  C  CG1 . VAL   A 1 115 ? 11.219 2.011   9.410  1.00 14.94 ? 121 VAL   A CG1 1 
ATOM   915  C  CG2 . VAL   A 1 115 ? 12.123 -0.346  9.453  1.00 15.78 ? 121 VAL   A CG2 1 
ATOM   916  N  N   . GLY   A 1 116 ? 14.072 3.315   11.426 1.00 12.25 ? 122 GLY   A N   1 
ATOM   917  C  CA  . GLY   A 1 116 ? 14.155 4.695   11.925 1.00 12.88 ? 122 GLY   A CA  1 
ATOM   918  C  C   . GLY   A 1 116 ? 14.343 4.716   13.423 1.00 12.07 ? 122 GLY   A C   1 
ATOM   919  O  O   . GLY   A 1 116 ? 14.672 3.670   14.017 1.00 12.09 ? 122 GLY   A O   1 
ATOM   920  N  N   . ILE   A 1 117 ? 14.192 5.894   14.038 1.00 11.93 ? 123 ILE   A N   1 
ATOM   921  C  CA  . ILE   A 1 117 ? 14.410 6.030   15.480 1.00 11.24 ? 123 ILE   A CA  1 
ATOM   922  C  C   . ILE   A 1 117 ? 13.251 6.805   16.091 1.00 11.47 ? 123 ILE   A C   1 
ATOM   923  O  O   . ILE   A 1 117 ? 12.640 7.668   15.444 1.00 12.68 ? 123 ILE   A O   1 
ATOM   924  C  CB  . ILE   A 1 117 ? 15.730 6.745   15.853 1.00 12.15 ? 123 ILE   A CB  1 
ATOM   925  C  CG1 . ILE   A 1 117 ? 15.890 8.079   15.121 1.00 13.73 ? 123 ILE   A CG1 1 
ATOM   926  C  CG2 . ILE   A 1 117 ? 16.904 5.796   15.655 1.00 13.37 ? 123 ILE   A CG2 1 
ATOM   927  C  CD1 . ILE   A 1 117 ? 17.161 8.893   15.649 1.00 14.59 ? 123 ILE   A CD1 1 
ATOM   928  N  N   . VAL   A 1 118 ? 12.945 6.535   17.362 1.00 11.33 ? 124 VAL   A N   1 
ATOM   929  C  CA  . VAL   A 1 118 ? 11.891 7.282   18.070 1.00 11.87 ? 124 VAL   A CA  1 
ATOM   930  C  C   . VAL   A 1 118 ? 12.234 8.779   18.073 1.00 12.82 ? 124 VAL   A C   1 
ATOM   931  O  O   . VAL   A 1 118 ? 13.393 9.147   18.376 1.00 13.05 ? 124 VAL   A O   1 
ATOM   932  C  CB  . VAL   A 1 118 ? 11.766 6.794   19.535 1.00 12.16 ? 124 VAL   A CB  1 
ATOM   933  C  CG1 . VAL   A 1 118 ? 10.758 7.648   20.311 1.00 13.29 ? 124 VAL   A CG1 1 
ATOM   934  C  CG2 . VAL   A 1 118 ? 11.316 5.322   19.597 1.00 12.59 ? 124 VAL   A CG2 1 
ATOM   935  N  N   . SER   A 1 119 ? 11.240 9.632   17.746 1.00 12.85 ? 125 SER   A N   1 
ATOM   936  C  CA  . SER   A 1 119 ? 11.431 11.089  17.694 1.00 14.15 ? 125 SER   A CA  1 
ATOM   937  C  C   . SER   A 1 119 ? 10.301 11.835  18.387 1.00 16.11 ? 125 SER   A C   1 
ATOM   938  O  O   . SER   A 1 119 ? 10.551 12.964  18.829 1.00 18.18 ? 125 SER   A O   1 
ATOM   939  C  CB  . SER   A 1 119 ? 11.574 11.505  16.240 1.00 14.67 ? 125 SER   A CB  1 
ATOM   940  O  OG  . SER   A 1 119 ? 11.677 12.923  16.051 1.00 15.56 ? 125 SER   A OG  1 
ATOM   941  N  N   . THR   A 1 120 ? 9.067  11.274  18.503 1.00 15.05 ? 126 THR   A N   1 
ATOM   942  C  CA  . THR   A 1 120 ? 7.935  12.029  19.106 1.00 16.83 ? 126 THR   A CA  1 
ATOM   943  C  C   . THR   A 1 120 ? 7.043  11.003  19.885 1.00 19.36 ? 126 THR   A C   1 
ATOM   944  O  O   . THR   A 1 120 ? 7.254  9.785   19.803 1.00 17.41 ? 126 THR   A O   1 
ATOM   945  C  CB  . THR   A 1 120 ? 7.043  12.706  17.995 1.00 18.12 ? 126 THR   A CB  1 
ATOM   946  O  OG1 . THR   A 1 120 ? 6.209  11.740  17.360 1.00 18.48 ? 126 THR   A OG1 1 
ATOM   947  C  CG2 . THR   A 1 120 ? 7.809  13.540  16.977 1.00 19.37 ? 126 THR   A CG2 1 
ATOM   948  N  N   . GLY   A 1 121 ? 5.994  11.473  20.574 1.00 20.37 ? 127 GLY   A N   1 
ATOM   949  C  CA  . GLY   A 1 121 ? 5.033  10.567  21.226 1.00 20.79 ? 127 GLY   A CA  1 
ATOM   950  C  C   . GLY   A 1 121 ? 4.086  11.300  22.163 1.00 22.65 ? 127 GLY   A C   1 
ATOM   951  O  O   . GLY   A 1 121 ? 4.115  12.525  22.228 1.00 24.38 ? 127 GLY   A O   1 
ATOM   952  N  N   . GLY   A 1 122 ? 3.400  10.536  22.992 1.00 22.52 ? 128 GLY   A N   1 
ATOM   953  C  CA  . GLY   A 1 122 ? 2.468  11.087  23.994 1.00 22.82 ? 128 GLY   A CA  1 
ATOM   954  C  C   . GLY   A 1 122 ? 1.152  10.354  23.907 1.00 23.55 ? 128 GLY   A C   1 
ATOM   955  O  O   . GLY   A 1 122 ? 0.733  9.963   22.804 1.00 23.91 ? 128 GLY   A O   1 
ATOM   956  N  N   . ASN   A 1 123 ? 0.445  10.222  25.043 1.00 22.54 ? 129 ASN   A N   1 
ATOM   957  C  CA  . ASN   A 1 123 ? -0.906 9.654   25.130 1.00 23.26 ? 129 ASN   A CA  1 
ATOM   958  C  C   . ASN   A 1 123 ? -1.088 8.372   24.352 1.00 22.20 ? 129 ASN   A C   1 
ATOM   959  O  O   . ASN   A 1 123 ? -2.139 8.161   23.719 1.00 22.85 ? 129 ASN   A O   1 
ATOM   960  C  CB  . ASN   A 1 123 ? -1.877 10.732  24.642 1.00 25.65 ? 129 ASN   A CB  1 
ATOM   961  C  CG  . ASN   A 1 123 ? -1.874 11.929  25.538 1.00 29.97 ? 129 ASN   A CG  1 
ATOM   962  O  OD1 . ASN   A 1 123 ? -2.167 11.796  26.721 1.00 31.61 ? 129 ASN   A OD1 1 
ATOM   963  N  ND2 . ASN   A 1 123 ? -1.531 13.100  24.985 1.00 31.31 ? 129 ASN   A ND2 1 
ATOM   964  N  N   . GLY   A 1 124 ? -0.113 7.467   24.467 1.00 18.49 ? 130 GLY   A N   1 
ATOM   965  C  CA  . GLY   A 1 124 ? -0.226 6.186   23.828 1.00 18.19 ? 130 GLY   A CA  1 
ATOM   966  C  C   . GLY   A 1 124 ? 0.131  6.218   22.368 1.00 15.60 ? 130 GLY   A C   1 
ATOM   967  O  O   . GLY   A 1 124 ? -0.044 5.181   21.754 1.00 18.92 ? 130 GLY   A O   1 
ATOM   968  N  N   . LEU   A 1 125 ? 0.792  7.269   21.902 1.00 16.22 ? 131 LEU   A N   1 
ATOM   969  C  CA  . LEU   A 1 125 ? 1.364  7.277   20.536 1.00 16.22 ? 131 LEU   A CA  1 
ATOM   970  C  C   . LEU   A 1 125 ? 2.882  7.329   20.602 1.00 16.48 ? 131 LEU   A C   1 
ATOM   971  O  O   . LEU   A 1 125 ? 3.469  7.825   21.582 1.00 18.18 ? 131 LEU   A O   1 
ATOM   972  C  CB  . LEU   A 1 125 ? 0.884  8.494   19.732 1.00 17.96 ? 131 LEU   A CB  1 
ATOM   973  C  CG  . LEU   A 1 125 ? -0.613 8.502   19.487 1.00 18.54 ? 131 LEU   A CG  1 
ATOM   974  C  CD1 . LEU   A 1 125 ? -1.095 9.907   19.030 1.00 22.20 ? 131 LEU   A CD1 1 
ATOM   975  C  CD2 . LEU   A 1 125 ? -1.008 7.416   18.430 1.00 18.71 ? 131 LEU   A CD2 1 
ATOM   976  N  N   . VAL   A 1 126 ? 3.537  6.835   19.563 1.00 13.66 ? 132 VAL   A N   1 
ATOM   977  C  CA  . VAL   A 1 126 ? 4.980  6.978   19.412 1.00 14.56 ? 132 VAL   A CA  1 
ATOM   978  C  C   . VAL   A 1 126 ? 5.219  7.342   17.911 1.00 14.16 ? 132 VAL   A C   1 
ATOM   979  O  O   . VAL   A 1 126 ? 4.603  6.739   17.038 1.00 14.68 ? 132 VAL   A O   1 
ATOM   980  C  CB  . VAL   A 1 126 ? 5.709  5.688   19.864 1.00 13.86 ? 132 VAL   A CB  1 
ATOM   981  C  CG1 . VAL   A 1 126 ? 5.201  4.460   19.118 1.00 14.09 ? 132 VAL   A CG1 1 
ATOM   982  C  CG2 . VAL   A 1 126 ? 7.232  5.846   19.676 1.00 13.62 ? 132 VAL   A CG2 1 
ATOM   983  N  N   . GLY   A 1 127 ? 6.138  8.240   17.638 1.00 14.03 ? 133 GLY   A N   1 
ATOM   984  C  CA  . GLY   A 1 127 ? 6.468  8.646   16.265 1.00 14.20 ? 133 GLY   A CA  1 
ATOM   985  C  C   . GLY   A 1 127 ? 7.926  8.379   15.979 1.00 13.80 ? 133 GLY   A C   1 
ATOM   986  O  O   . GLY   A 1 127 ? 8.776  8.561   16.858 1.00 14.49 ? 133 GLY   A O   1 
ATOM   987  N  N   . PHE   A 1 128 ? 8.194  7.931   14.773 1.00 12.54 ? 134 PHE   A N   1 
ATOM   988  C  CA  . PHE   A 1 128 ? 9.560  7.534   14.358 1.00 12.59 ? 134 PHE   A CA  1 
ATOM   989  C  C   . PHE   A 1 128 ? 10.021 8.341   13.175 1.00 13.43 ? 134 PHE   A C   1 
ATOM   990  O  O   . PHE   A 1 128 ? 9.276  8.494   12.197 1.00 13.41 ? 134 PHE   A O   1 
ATOM   991  C  CB  . PHE   A 1 128 ? 9.547  6.038   13.913 1.00 12.64 ? 134 PHE   A CB  1 
ATOM   992  C  CG  . PHE   A 1 128 ? 8.930  5.129   14.970 1.00 12.53 ? 134 PHE   A CG  1 
ATOM   993  C  CD1 . PHE   A 1 128 ? 9.687  4.655   16.046 1.00 11.81 ? 134 PHE   A CD1 1 
ATOM   994  C  CD2 . PHE   A 1 128 ? 7.623  4.691   14.844 1.00 14.12 ? 134 PHE   A CD2 1 
ATOM   995  C  CE1 . PHE   A 1 128 ? 9.114  3.790   16.996 1.00 11.85 ? 134 PHE   A CE1 1 
ATOM   996  C  CE2 . PHE   A 1 128 ? 7.069  3.833   15.785 1.00 13.13 ? 134 PHE   A CE2 1 
ATOM   997  C  CZ  . PHE   A 1 128 ? 7.825  3.387   16.859 1.00 12.11 ? 134 PHE   A CZ  1 
ATOM   998  N  N   . ALA   A 1 129 ? 11.268 8.816   13.246 1.00 13.14 ? 135 ALA   A N   1 
ATOM   999  C  CA  . ALA   A 1 129 ? 11.889 9.492   12.083 1.00 12.57 ? 135 ALA   A CA  1 
ATOM   1000 C  C   . ALA   A 1 129 ? 12.403 8.423   11.135 1.00 12.77 ? 135 ALA   A C   1 
ATOM   1001 O  O   . ALA   A 1 129 ? 13.267 7.625   11.533 1.00 12.92 ? 135 ALA   A O   1 
ATOM   1002 C  CB  . ALA   A 1 129 ? 13.016 10.372  12.582 1.00 13.37 ? 135 ALA   A CB  1 
ATOM   1003 N  N   . ASP   A 1 130 ? 11.838 8.326   9.912  1.00 13.23 ? 136 ASP   A N   1 
ATOM   1004 C  CA  . ASP   A 1 130 ? 12.272 7.342   8.924  1.00 13.68 ? 136 ASP   A CA  1 
ATOM   1005 C  C   . ASP   A 1 130 ? 13.695 7.663   8.450  1.00 13.81 ? 136 ASP   A C   1 
ATOM   1006 O  O   . ASP   A 1 130 ? 14.066 8.835   8.284  1.00 15.25 ? 136 ASP   A O   1 
ATOM   1007 C  CB  . ASP   A 1 130 ? 11.336 7.402   7.694  1.00 15.12 ? 136 ASP   A CB  1 
ATOM   1008 C  CG  . ASP   A 1 130 ? 11.607 6.376   6.641  1.00 23.03 ? 136 ASP   A CG  1 
ATOM   1009 O  OD1 . ASP   A 1 130 ? 11.772 5.191   6.993  1.00 18.06 ? 136 ASP   A OD1 1 
ATOM   1010 O  OD2 . ASP   A 1 130 ? 11.775 6.780   5.433  1.00 31.42 ? 136 ASP   A OD2 1 
ATOM   1011 N  N   . VAL   A 1 131 ? 14.475 6.613   8.168  1.00 12.70 ? 137 VAL   A N   1 
ATOM   1012 C  CA  . VAL   A 1 131 ? 15.796 6.760   7.538  1.00 12.27 ? 137 VAL   A CA  1 
ATOM   1013 C  C   . VAL   A 1 131 ? 15.910 5.939   6.245  1.00 12.98 ? 137 VAL   A C   1 
ATOM   1014 O  O   . VAL   A 1 131 ? 16.996 5.961   5.624  1.00 13.05 ? 137 VAL   A O   1 
ATOM   1015 C  CB  . VAL   A 1 131 ? 16.957 6.435   8.493  1.00 12.14 ? 137 VAL   A CB  1 
ATOM   1016 C  CG1 . VAL   A 1 131 ? 16.989 7.359   9.711  1.00 14.04 ? 137 VAL   A CG1 1 
ATOM   1017 C  CG2 . VAL   A 1 131 ? 16.994 4.961   8.912  1.00 14.21 ? 137 VAL   A CG2 1 
ATOM   1018 N  N   . ARG   A 1 132 ? 14.854 5.214   5.818  1.00 13.29 ? 138 ARG   A N   1 
ATOM   1019 C  CA  . ARG   A 1 132 ? 14.963 4.290   4.682  1.00 13.47 ? 138 ARG   A CA  1 
ATOM   1020 C  C   . ARG   A 1 132 ? 15.253 4.975   3.354  1.00 14.67 ? 138 ARG   A C   1 
ATOM   1021 O  O   . ARG   A 1 132 ? 15.743 4.316   2.397  1.00 15.60 ? 138 ARG   A O   1 
ATOM   1022 C  CB  . ARG   A 1 132 ? 13.732 3.404   4.565  1.00 14.28 ? 138 ARG   A CB  1 
ATOM   1023 C  CG  . ARG   A 1 132 ? 13.600 2.464   5.798  1.00 13.63 ? 138 ARG   A CG  1 
ATOM   1024 C  CD  . ARG   A 1 132 ? 12.311 1.654   5.636  1.00 15.06 ? 138 ARG   A CD  1 
ATOM   1025 N  NE  . ARG   A 1 132 ? 11.155 2.528   5.865  1.00 15.43 ? 138 ARG   A NE  1 
ATOM   1026 C  CZ  . ARG   A 1 132 ? 9.896  2.114   5.953  1.00 16.96 ? 138 ARG   A CZ  1 
ATOM   1027 N  NH1 . ARG   A 1 132 ? 9.587  0.846   5.680  1.00 19.59 ? 138 ARG   A NH1 1 
ATOM   1028 N  NH2 . ARG   A 1 132 ? 8.925  2.994   6.218  1.00 18.06 ? 138 ARG   A NH2 1 
ATOM   1029 N  N   . ASP   A 1 133 ? 14.915 6.287   3.235  1.00 14.58 ? 139 ASP   A N   1 
ATOM   1030 C  CA  . ASP   A 1 133 ? 15.196 6.989   1.975  1.00 15.39 ? 139 ASP   A CA  1 
ATOM   1031 C  C   . ASP   A 1 133 ? 16.632 7.510   1.896  1.00 15.38 ? 139 ASP   A C   1 
ATOM   1032 O  O   . ASP   A 1 133 ? 17.032 8.013   0.837  1.00 16.84 ? 139 ASP   A O   1 
ATOM   1033 C  CB  . ASP   A 1 133 ? 14.191 8.147   1.806  1.00 17.07 ? 139 ASP   A CB  1 
ATOM   1034 C  CG  . ASP   A 1 133 ? 14.390 9.215   2.891  1.00 21.47 ? 139 ASP   A CG  1 
ATOM   1035 O  OD1 . ASP   A 1 133 ? 14.450 8.852   4.096  1.00 20.80 ? 139 ASP   A OD1 1 
ATOM   1036 O  OD2 . ASP   A 1 133 ? 14.484 10.414  2.550  1.00 23.66 ? 139 ASP   A OD2 1 
ATOM   1037 N  N   . LEU   A 1 134 ? 17.406 7.473   3.009  1.00 14.54 ? 140 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 134 ? 18.772 8.041   3.027  1.00 14.63 ? 140 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 134 ? 19.750 7.019   2.496  1.00 14.47 ? 140 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 134 ? 20.443 6.331   3.252  1.00 14.79 ? 140 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 134 ? 19.138 8.474   4.464  1.00 14.59 ? 140 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 134 ? 18.145 9.481   5.097  1.00 16.01 ? 140 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 134 ? 18.530 9.769   6.547  1.00 16.21 ? 140 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 134 ? 18.141 10.798  4.315  1.00 17.82 ? 140 LEU   A CD2 1 
ATOM   1045 N  N   . LEU   A 1 135 ? 19.774 6.878   1.154  1.00 14.88 ? 141 LEU   A N   1 
ATOM   1046 C  CA  . LEU   A 1 135 ? 20.542 5.788   0.556  1.00 15.39 ? 141 LEU   A CA  1 
ATOM   1047 C  C   . LEU   A 1 135 ? 22.024 5.899   0.760  1.00 15.30 ? 141 LEU   A C   1 
ATOM   1048 O  O   . LEU   A 1 135 ? 22.722 4.871   0.811  1.00 16.32 ? 141 LEU   A O   1 
ATOM   1049 C  CB  . LEU   A 1 135 ? 20.206 5.643   -0.966 1.00 16.28 ? 141 LEU   A CB  1 
ATOM   1050 C  CG  . LEU   A 1 135 ? 18.707 5.647   -1.301 1.00 18.39 ? 141 LEU   A CG  1 
ATOM   1051 C  CD1 . LEU   A 1 135 ? 18.534 5.383   -2.810 1.00 20.56 ? 141 LEU   A CD1 1 
ATOM   1052 C  CD2 . LEU   A 1 135 ? 17.902 4.592   -0.506 1.00 19.43 ? 141 LEU   A CD2 1 
ATOM   1053 N  N   . TRP   A 1 136 ? 22.524 7.142   0.921  1.00 14.49 ? 142 TRP   A N   1 
ATOM   1054 C  CA  . TRP   A 1 136 ? 23.945 7.391   1.094  1.00 14.96 ? 142 TRP   A CA  1 
ATOM   1055 C  C   . TRP   A 1 136 ? 24.489 6.800   2.411  1.00 15.76 ? 142 TRP   A C   1 
ATOM   1056 O  O   . TRP   A 1 136 ? 25.697 6.671   2.551  1.00 16.76 ? 142 TRP   A O   1 
ATOM   1057 C  CB  . TRP   A 1 136 ? 24.242 8.909   0.984  1.00 15.55 ? 142 TRP   A CB  1 
ATOM   1058 C  CG  . TRP   A 1 136 ? 23.399 9.726   1.906  1.00 14.85 ? 142 TRP   A CG  1 
ATOM   1059 C  CD1 . TRP   A 1 136 ? 22.269 10.405  1.583  1.00 15.51 ? 142 TRP   A CD1 1 
ATOM   1060 C  CD2 . TRP   A 1 136 ? 23.699 10.057  3.271  1.00 14.96 ? 142 TRP   A CD2 1 
ATOM   1061 N  NE1 . TRP   A 1 136 ? 21.788 11.069  2.692  1.00 17.02 ? 142 TRP   A NE1 1 
ATOM   1062 C  CE2 . TRP   A 1 136 ? 22.679 10.905  3.726  1.00 15.53 ? 142 TRP   A CE2 1 
ATOM   1063 C  CE3 . TRP   A 1 136 ? 24.766 9.757   4.127  1.00 15.73 ? 142 TRP   A CE3 1 
ATOM   1064 C  CZ2 . TRP   A 1 136 ? 22.674 11.418  5.032  1.00 16.69 ? 142 TRP   A CZ2 1 
ATOM   1065 C  CZ3 . TRP   A 1 136 ? 24.767 10.289  5.410  1.00 17.50 ? 142 TRP   A CZ3 1 
ATOM   1066 C  CH2 . TRP   A 1 136 ? 23.730 11.083  5.843  1.00 16.84 ? 142 TRP   A CH2 1 
ATOM   1067 N  N   . LEU   A 1 137 ? 23.613 6.448   3.383  1.00 14.24 ? 143 LEU   A N   1 
ATOM   1068 C  CA  . LEU   A 1 137 ? 24.098 5.804   4.614  1.00 15.62 ? 143 LEU   A CA  1 
ATOM   1069 C  C   . LEU   A 1 137 ? 24.799 4.476   4.313  1.00 18.02 ? 143 LEU   A C   1 
ATOM   1070 O  O   . LEU   A 1 137 ? 25.605 4.012   5.143  1.00 18.39 ? 143 LEU   A O   1 
ATOM   1071 C  CB  . LEU   A 1 137 ? 22.952 5.562   5.605  1.00 14.94 ? 143 LEU   A CB  1 
ATOM   1072 C  CG  . LEU   A 1 137 ? 22.388 6.795   6.257  1.00 14.14 ? 143 LEU   A CG  1 
ATOM   1073 C  CD1 . LEU   A 1 137 ? 21.107 6.426   7.032  1.00 15.93 ? 143 LEU   A CD1 1 
ATOM   1074 C  CD2 . LEU   A 1 137 ? 23.485 7.459   7.214  1.00 14.36 ? 143 LEU   A CD2 1 
ATOM   1075 N  N   . ASP   A 1 138 ? 24.484 3.848   3.162  1.00 19.92 ? 144 ASP   A N   1 
ATOM   1076 C  CA  . ASP   A 1 138 ? 25.061 2.531   2.790  1.00 21.66 ? 144 ASP   A CA  1 
ATOM   1077 C  C   . ASP   A 1 138 ? 26.413 2.589   2.108  1.00 25.94 ? 144 ASP   A C   1 
ATOM   1078 O  O   . ASP   A 1 138 ? 26.949 1.534   1.725  1.00 26.93 ? 144 ASP   A O   1 
ATOM   1079 C  CB  . ASP   A 1 138 ? 24.099 1.777   1.812  1.00 21.52 ? 144 ASP   A CB  1 
ATOM   1080 C  CG  . ASP   A 1 138 ? 22.746 1.430   2.364  1.00 26.71 ? 144 ASP   A CG  1 
ATOM   1081 O  OD1 . ASP   A 1 138 ? 22.573 1.503   3.601  1.00 28.92 ? 144 ASP   A OD1 1 
ATOM   1082 O  OD2 . ASP   A 1 138 ? 21.850 1.070   1.568  1.00 32.33 ? 144 ASP   A OD2 1 
ATOM   1083 N  N   . GLU   A 1 139 ? 26.971 3.799   1.880  1.00 27.29 ? 145 GLU   A N   1 
ATOM   1084 C  CA  . GLU   A 1 139 ? 28.253 3.908   1.163  1.00 31.12 ? 145 GLU   A CA  1 
ATOM   1085 C  C   . GLU   A 1 139 ? 29.174 4.968   1.774  1.00 33.10 ? 145 GLU   A C   1 
ATOM   1086 O  O   . GLU   A 1 139 ? 28.748 5.720   2.637  1.00 32.28 ? 145 GLU   A O   1 
ATOM   1087 C  CB  . GLU   A 1 139 ? 27.926 4.259   -0.293 1.00 36.26 ? 145 GLU   A CB  1 
ATOM   1088 C  CG  . GLU   A 1 139 ? 27.280 5.623   -0.420 1.00 44.55 ? 145 GLU   A CG  1 
ATOM   1089 C  CD  . GLU   A 1 139 ? 26.467 5.879   -1.673 1.00 54.10 ? 145 GLU   A CD  1 
ATOM   1090 O  OE1 . GLU   A 1 139 ? 26.081 7.053   -1.892 1.00 54.83 ? 145 GLU   A OE1 1 
ATOM   1091 O  OE2 . GLU   A 1 139 ? 26.217 4.915   -2.434 1.00 58.14 ? 145 GLU   A OE2 1 
ATOM   1092 N  N   . GLU   A 1 140 ? 30.425 5.057   1.272  1.00 36.06 ? 146 GLU   A N   1 
ATOM   1093 C  CA  . GLU   A 1 140 ? 31.469 6.051   1.577  1.00 39.71 ? 146 GLU   A CA  1 
ATOM   1094 C  C   . GLU   A 1 140 ? 31.316 6.780   2.889  1.00 42.13 ? 146 GLU   A C   1 
ATOM   1095 O  O   . GLU   A 1 140 ? 31.799 7.905   3.050  1.00 42.91 ? 146 GLU   A O   1 
ATOM   1096 C  CB  . GLU   A 1 140 ? 31.586 7.076   0.427  1.00 43.94 ? 146 GLU   A CB  1 
ATOM   1097 C  CG  . GLU   A 1 140 ? 30.536 8.179   0.387  1.00 50.16 ? 146 GLU   A CG  1 
ATOM   1098 C  CD  . GLU   A 1 140 ? 31.079 9.585   0.598  1.00 60.33 ? 146 GLU   A CD  1 
ATOM   1099 O  OE1 . GLU   A 1 140 ? 30.308 10.554  0.404  1.00 62.82 ? 146 GLU   A OE1 1 
ATOM   1100 O  OE2 . GLU   A 1 140 ? 32.270 9.722   0.969  1.00 63.26 ? 146 GLU   A OE2 1 
ATOM   1101 N  N   . SER   B 1 1   ? 21.840 -21.356 7.605  1.00 20.70 ? 7   SER   C N   1 
ATOM   1102 C  CA  . SER   B 1 1   ? 20.718 -21.122 8.515  1.00 20.11 ? 7   SER   C CA  1 
ATOM   1103 C  C   . SER   B 1 1   ? 20.698 -22.221 9.611  1.00 19.87 ? 7   SER   C C   1 
ATOM   1104 O  O   . SER   B 1 1   ? 21.384 -23.266 9.481  1.00 20.75 ? 7   SER   C O   1 
ATOM   1105 C  CB  . SER   B 1 1   ? 19.415 -21.174 7.713  1.00 23.21 ? 7   SER   C CB  1 
ATOM   1106 O  OG  . SER   B 1 1   ? 19.259 -22.476 7.172  1.00 28.60 ? 7   SER   C OG  1 
ATOM   1107 N  N   . GLY   B 1 2   ? 19.914 -21.994 10.672 1.00 19.35 ? 8   GLY   C N   1 
ATOM   1108 C  CA  . GLY   B 1 2   ? 19.757 -23.000 11.723 1.00 18.40 ? 8   GLY   C CA  1 
ATOM   1109 C  C   . GLY   B 1 2   ? 19.486 -22.392 13.082 1.00 17.22 ? 8   GLY   C C   1 
ATOM   1110 O  O   . GLY   B 1 2   ? 19.892 -21.266 13.344 1.00 17.24 ? 8   GLY   C O   1 
ATOM   1111 N  N   . ALA   B 1 3   ? 18.794 -23.131 13.945 1.00 16.37 ? 9   ALA   C N   1 
ATOM   1112 C  CA  . ALA   B 1 3   ? 18.490 -22.641 15.285 1.00 16.35 ? 9   ALA   C CA  1 
ATOM   1113 C  C   . ALA   B 1 3   ? 18.623 -23.759 16.322 1.00 14.89 ? 9   ALA   C C   1 
ATOM   1114 O  O   . ALA   B 1 3   ? 18.695 -24.938 15.957 1.00 16.16 ? 9   ALA   C O   1 
ATOM   1115 C  CB  . ALA   B 1 3   ? 17.065 -22.085 15.313 1.00 19.35 ? 9   ALA   C CB  1 
ATOM   1116 N  N   . ILE   B 1 4   ? 18.666 -23.370 17.601 1.00 14.68 ? 10  ILE   C N   1 
ATOM   1117 C  CA  . ILE   B 1 4   ? 18.579 -24.302 18.739 1.00 14.57 ? 10  ILE   C CA  1 
ATOM   1118 C  C   . ILE   B 1 4   ? 17.187 -24.111 19.352 1.00 14.32 ? 10  ILE   C C   1 
ATOM   1119 O  O   . ILE   B 1 4   ? 16.744 -22.962 19.545 1.00 15.59 ? 10  ILE   C O   1 
ATOM   1120 C  CB  . ILE   B 1 4   ? 19.621 -23.995 19.800 1.00 14.71 ? 10  ILE   C CB  1 
ATOM   1121 C  CG1 . ILE   B 1 4   ? 21.051 -23.872 19.205 1.00 15.68 ? 10  ILE   C CG1 1 
ATOM   1122 C  CG2 . ILE   B 1 4   ? 19.534 -25.063 20.904 1.00 16.44 ? 10  ILE   C CG2 1 
ATOM   1123 C  CD1 . ILE   B 1 4   ? 22.020 -23.259 20.232 1.00 16.51 ? 10  ILE   C CD1 1 
ATOM   1124 N  N   . TYR   B 1 5   ? 16.479 -25.202 19.637 1.00 13.95 ? 11  TYR   C N   1 
ATOM   1125 C  CA  . TYR   B 1 5   ? 15.139 -25.150 20.220 1.00 15.91 ? 11  TYR   C CA  1 
ATOM   1126 C  C   . TYR   B 1 5   ? 15.220 -25.839 21.579 1.00 16.18 ? 11  TYR   C C   1 
ATOM   1127 O  O   . TYR   B 1 5   ? 15.279 -27.070 21.644 1.00 17.64 ? 11  TYR   C O   1 
ATOM   1128 C  CB  . TYR   B 1 5   ? 14.084 -25.853 19.303 1.00 16.41 ? 11  TYR   C CB  1 
ATOM   1129 C  CG  . TYR   B 1 5   ? 13.883 -25.110 17.998 1.00 16.55 ? 11  TYR   C CG  1 
ATOM   1130 C  CD1 . TYR   B 1 5   ? 13.062 -23.984 17.933 1.00 16.82 ? 11  TYR   C CD1 1 
ATOM   1131 C  CD2 . TYR   B 1 5   ? 14.605 -25.453 16.860 1.00 17.81 ? 11  TYR   C CD2 1 
ATOM   1132 C  CE1 . TYR   B 1 5   ? 12.929 -23.267 16.754 1.00 18.67 ? 11  TYR   C CE1 1 
ATOM   1133 C  CE2 . TYR   B 1 5   ? 14.461 -24.756 15.669 1.00 19.47 ? 11  TYR   C CE2 1 
ATOM   1134 C  CZ  . TYR   B 1 5   ? 13.651 -23.640 15.635 1.00 19.26 ? 11  TYR   C CZ  1 
ATOM   1135 O  OH  . TYR   B 1 5   ? 13.570 -22.911 14.465 1.00 22.25 ? 11  TYR   C OH  1 
ATOM   1136 N  N   . VAL   B 1 6   ? 15.241 -25.094 22.680 1.00 16.41 ? 12  VAL   C N   1 
ATOM   1137 C  CA  . VAL   B 1 6   ? 15.327 -25.660 24.040 1.00 17.81 ? 12  VAL   C CA  1 
ATOM   1138 C  C   . VAL   B 1 6   ? 14.193 -25.041 24.856 1.00 18.27 ? 12  VAL   C C   1 
ATOM   1139 O  O   . VAL   B 1 6   ? 13.993 -23.818 24.857 1.00 17.41 ? 12  VAL   C O   1 
ATOM   1140 C  CB  . VAL   B 1 6   ? 16.727 -25.364 24.650 1.00 18.10 ? 12  VAL   C CB  1 
ATOM   1141 C  CG1 . VAL   B 1 6   ? 17.089 -23.868 24.555 1.00 18.00 ? 12  VAL   C CG1 1 
ATOM   1142 C  CG2 . VAL   B 1 6   ? 16.769 -25.860 26.092 1.00 19.76 ? 12  VAL   C CG2 1 
ATOM   1143 N  N   . GLY   B 1 7   ? 13.366 -25.879 25.521 1.00 18.90 ? 13  GLY   C N   1 
ATOM   1144 C  CA  . GLY   B 1 7   ? 12.258 -25.336 26.310 1.00 18.45 ? 13  GLY   C CA  1 
ATOM   1145 C  C   . GLY   B 1 7   ? 11.335 -24.482 25.459 1.00 18.70 ? 13  GLY   C C   1 
ATOM   1146 O  O   . GLY   B 1 7   ? 11.062 -24.874 24.318 1.00 19.88 ? 13  GLY   C O   1 
ATOM   1147 N  N   . ASN   B 1 8   ? 10.996 -23.270 25.902 1.00 18.10 ? 14  ASN   C N   1 
ATOM   1148 C  CA  . ASN   B 1 8   ? 10.221 -22.374 25.063 1.00 18.47 ? 14  ASN   C CA  1 
ATOM   1149 C  C   . ASN   B 1 8   ? 11.094 -21.257 24.519 1.00 18.52 ? 14  ASN   C C   1 
ATOM   1150 O  O   . ASN   B 1 8   ? 10.619 -20.126 24.358 1.00 18.71 ? 14  ASN   C O   1 
ATOM   1151 C  CB  . ASN   B 1 8   ? 8.987  -21.823 25.800 1.00 21.24 ? 14  ASN   C CB  1 
ATOM   1152 C  CG  . ASN   B 1 8   ? 7.883  -22.872 25.941 1.00 28.15 ? 14  ASN   C CG  1 
ATOM   1153 O  OD1 . ASN   B 1 8   ? 7.000  -22.996 25.082 1.00 30.80 ? 14  ASN   C OD1 1 
ATOM   1154 N  ND2 . ASN   B 1 8   ? 7.982  -23.682 26.969 1.00 29.56 ? 14  ASN   C ND2 1 
ATOM   1155 N  N   . TYR   B 1 9   ? 12.297 -21.623 24.092 1.00 16.48 ? 15  TYR   C N   1 
ATOM   1156 C  CA  . TYR   B 1 9   ? 13.248 -20.655 23.490 1.00 15.63 ? 15  TYR   C CA  1 
ATOM   1157 C  C   . TYR   B 1 9   ? 13.717 -21.142 22.130 1.00 15.29 ? 15  TYR   C C   1 
ATOM   1158 O  O   . TYR   B 1 9   ? 13.916 -22.357 21.923 1.00 16.10 ? 15  TYR   C O   1 
ATOM   1159 C  CB  . TYR   B 1 9   ? 14.480 -20.504 24.398 1.00 15.81 ? 15  TYR   C CB  1 
ATOM   1160 C  CG  . TYR   B 1 9   ? 14.161 -20.009 25.806 1.00 18.12 ? 15  TYR   C CG  1 
ATOM   1161 C  CD1 . TYR   B 1 9   ? 13.626 -18.745 26.016 1.00 20.67 ? 15  TYR   C CD1 1 
ATOM   1162 C  CD2 . TYR   B 1 9   ? 14.468 -20.783 26.926 1.00 20.81 ? 15  TYR   C CD2 1 
ATOM   1163 C  CE1 . TYR   B 1 9   ? 13.380 -18.274 27.311 1.00 23.65 ? 15  TYR   C CE1 1 
ATOM   1164 C  CE2 . TYR   B 1 9   ? 14.247 -20.310 28.217 1.00 23.97 ? 15  TYR   C CE2 1 
ATOM   1165 C  CZ  . TYR   B 1 9   ? 13.717 -19.059 28.401 1.00 26.40 ? 15  TYR   C CZ  1 
ATOM   1166 O  OH  . TYR   B 1 9   ? 13.500 -18.618 29.695 1.00 31.36 ? 15  TYR   C OH  1 
ATOM   1167 N  N   . ARG   B 1 10  ? 13.963 -20.195 21.234 1.00 14.26 ? 16  ARG   C N   1 
ATOM   1168 C  CA  . ARG   B 1 10  ? 14.583 -20.413 19.914 1.00 14.40 ? 16  ARG   C CA  1 
ATOM   1169 C  C   . ARG   B 1 10  ? 15.860 -19.532 19.902 1.00 14.94 ? 16  ARG   C C   1 
ATOM   1170 O  O   . ARG   B 1 10  ? 15.759 -18.310 20.110 1.00 15.40 ? 16  ARG   C O   1 
ATOM   1171 C  CB  . ARG   B 1 10  ? 13.609 -19.980 18.780 1.00 16.30 ? 16  ARG   C CB  1 
ATOM   1172 C  CG  . ARG   B 1 10  ? 14.260 -19.803 17.394 1.00 17.03 ? 16  ARG   C CG  1 
ATOM   1173 C  CD  . ARG   B 1 10  ? 13.185 -19.522 16.335 1.00 17.60 ? 16  ARG   C CD  1 
ATOM   1174 N  NE  . ARG   B 1 10  ? 13.630 -18.560 15.318 1.00 17.88 ? 16  ARG   C NE  1 
ATOM   1175 C  CZ  . ARG   B 1 10  ? 14.149 -18.862 14.126 1.00 19.49 ? 16  ARG   C CZ  1 
ATOM   1176 N  NH1 . ARG   B 1 10  ? 14.366 -20.131 13.785 1.00 20.33 ? 16  ARG   C NH1 1 
ATOM   1177 N  NH2 . ARG   B 1 10  ? 14.491 -17.894 13.278 1.00 20.43 ? 16  ARG   C NH2 1 
ATOM   1178 N  N   . VAL   B 1 11  ? 17.035 -20.144 19.694 1.00 14.20 ? 17  VAL   C N   1 
ATOM   1179 C  CA  . VAL   B 1 11  ? 18.326 -19.418 19.654 1.00 13.37 ? 17  VAL   C CA  1 
ATOM   1180 C  C   . VAL   B 1 11  ? 18.790 -19.378 18.224 1.00 14.22 ? 17  VAL   C C   1 
ATOM   1181 O  O   . VAL   B 1 11  ? 18.958 -20.450 17.587 1.00 14.48 ? 17  VAL   C O   1 
ATOM   1182 C  CB  . VAL   B 1 11  ? 19.396 -20.160 20.518 1.00 13.43 ? 17  VAL   C CB  1 
ATOM   1183 C  CG1 . VAL   B 1 11  ? 20.655 -19.301 20.602 1.00 16.22 ? 17  VAL   C CG1 1 
ATOM   1184 C  CG2 . VAL   B 1 11  ? 18.847 -20.511 21.918 1.00 15.07 ? 17  VAL   C CG2 1 
ATOM   1185 N  N   . VAL   B 1 12  ? 19.036 -18.161 17.678 1.00 13.35 ? 18  VAL   C N   1 
ATOM   1186 C  CA  A VAL   B 1 12  ? 19.489 -17.995 16.298 0.50 13.50 ? 18  VAL   C CA  1 
ATOM   1187 C  CA  B VAL   B 1 12  ? 19.430 -18.000 16.287 0.50 15.16 ? 18  VAL   C CA  1 
ATOM   1188 C  C   . VAL   B 1 12  ? 20.618 -17.002 16.228 1.00 14.10 ? 18  VAL   C C   1 
ATOM   1189 O  O   . VAL   B 1 12  ? 20.878 -16.248 17.195 1.00 14.86 ? 18  VAL   C O   1 
ATOM   1190 C  CB  A VAL   B 1 12  ? 18.337 -17.483 15.374 0.50 13.38 ? 18  VAL   C CB  1 
ATOM   1191 C  CB  B VAL   B 1 12  ? 18.173 -17.412 15.528 0.50 18.55 ? 18  VAL   C CB  1 
ATOM   1192 C  CG1 A VAL   B 1 12  ? 17.360 -18.606 15.091 0.50 13.88 ? 18  VAL   C CG1 1 
ATOM   1193 C  CG1 B VAL   B 1 12  ? 18.360 -17.365 14.024 0.50 18.58 ? 18  VAL   C CG1 1 
ATOM   1194 C  CG2 A VAL   B 1 12  ? 17.680 -16.177 15.918 0.50 11.39 ? 18  VAL   C CG2 1 
ATOM   1195 C  CG2 B VAL   B 1 12  ? 16.898 -18.182 15.855 0.50 21.62 ? 18  VAL   C CG2 1 
ATOM   1196 N  N   . ASN   B 1 13  ? 21.318 -16.951 15.073 1.00 12.95 ? 19  ASN   C N   1 
ATOM   1197 C  CA  . ASN   B 1 13  ? 22.315 -15.901 14.873 1.00 13.50 ? 19  ASN   C CA  1 
ATOM   1198 C  C   . ASN   B 1 13  ? 21.497 -14.566 14.824 1.00 14.06 ? 19  ASN   C C   1 
ATOM   1199 O  O   . ASN   B 1 13  ? 20.501 -14.472 14.098 1.00 14.43 ? 19  ASN   C O   1 
ATOM   1200 C  CB  . ASN   B 1 13  ? 23.035 -16.052 13.510 1.00 13.79 ? 19  ASN   C CB  1 
ATOM   1201 C  CG  . ASN   B 1 13  ? 23.865 -17.334 13.420 1.00 14.22 ? 19  ASN   C CG  1 
ATOM   1202 O  OD1 . ASN   B 1 13  ? 23.372 -18.387 12.986 1.00 14.97 ? 19  ASN   C OD1 1 
ATOM   1203 N  ND2 . ASN   B 1 13  ? 25.094 -17.211 13.886 1.00 14.66 ? 19  ASN   C ND2 1 
ATOM   1204 N  N   . ARG   B 1 14  ? 22.019 -13.528 15.509 1.00 13.12 ? 20  ARG   C N   1 
ATOM   1205 C  CA  . ARG   B 1 14  ? 21.265 -12.258 15.532 1.00 12.81 ? 20  ARG   C CA  1 
ATOM   1206 C  C   . ARG   B 1 14  ? 21.119 -11.720 14.101 1.00 14.46 ? 20  ARG   C C   1 
ATOM   1207 O  O   . ARG   B 1 14  ? 20.074 -11.139 13.763 1.00 15.50 ? 20  ARG   C O   1 
ATOM   1208 C  CB  . ARG   B 1 14  ? 22.030 -11.266 16.393 1.00 13.19 ? 20  ARG   C CB  1 
ATOM   1209 C  CG  . ARG   B 1 14  ? 21.226 -9.930  16.646 1.00 14.34 ? 20  ARG   C CG  1 
ATOM   1210 C  CD  . ARG   B 1 14  ? 22.093 -8.980  17.437 1.00 15.21 ? 20  ARG   C CD  1 
ATOM   1211 N  NE  . ARG   B 1 14  ? 21.427 -7.711  17.864 1.00 16.53 ? 20  ARG   C NE  1 
ATOM   1212 C  CZ  . ARG   B 1 14  ? 21.337 -6.608  17.127 1.00 16.65 ? 20  ARG   C CZ  1 
ATOM   1213 N  NH1 . ARG   B 1 14  ? 21.718 -6.616  15.856 1.00 17.56 ? 20  ARG   C NH1 1 
ATOM   1214 N  NH2 . ARG   B 1 14  ? 20.822 -5.498  17.646 1.00 16.41 ? 20  ARG   C NH2 1 
ATOM   1215 N  N   . HIS   B 1 15  ? 22.154 -11.910 13.247 1.00 14.67 ? 21  HIS   C N   1 
ATOM   1216 C  CA  . HIS   B 1 15  ? 22.057 -11.361 11.884 1.00 15.32 ? 21  HIS   C CA  1 
ATOM   1217 C  C   . HIS   B 1 15  ? 21.054 -12.095 10.986 1.00 16.29 ? 21  HIS   C C   1 
ATOM   1218 O  O   . HIS   B 1 15  ? 20.734 -11.569 9.917  1.00 18.24 ? 21  HIS   C O   1 
ATOM   1219 C  CB  . HIS   B 1 15  ? 23.454 -11.278 11.213 1.00 14.87 ? 21  HIS   C CB  1 
ATOM   1220 C  CG  . HIS   B 1 15  ? 24.047 -12.601 10.770 1.00 14.86 ? 21  HIS   C CG  1 
ATOM   1221 N  ND1 . HIS   B 1 15  ? 24.783 -13.409 11.638 1.00 15.53 ? 21  HIS   C ND1 1 
ATOM   1222 C  CD2 . HIS   B 1 15  ? 24.044 -13.171 9.542  1.00 15.63 ? 21  HIS   C CD2 1 
ATOM   1223 C  CE1 . HIS   B 1 15  ? 25.186 -14.458 10.912 1.00 16.83 ? 21  HIS   C CE1 1 
ATOM   1224 N  NE2 . HIS   B 1 15  ? 24.758 -14.351 9.646  1.00 16.12 ? 21  HIS   C NE2 1 
ATOM   1225 N  N   . LEU   B 1 16  ? 20.518 -13.241 11.417 1.00 14.99 ? 22  LEU   C N   1 
ATOM   1226 C  CA  . LEU   B 1 16  ? 19.497 -13.991 10.663 1.00 16.17 ? 22  LEU   C CA  1 
ATOM   1227 C  C   . LEU   B 1 16  ? 18.122 -13.936 11.347 1.00 17.07 ? 22  LEU   C C   1 
ATOM   1228 O  O   . LEU   B 1 16  ? 17.191 -14.649 10.923 1.00 18.24 ? 22  LEU   C O   1 
ATOM   1229 C  CB  . LEU   B 1 16  ? 19.967 -15.433 10.465 1.00 16.35 ? 22  LEU   C CB  1 
ATOM   1230 C  CG  . LEU   B 1 16  ? 21.262 -15.570 9.675  1.00 17.40 ? 22  LEU   C CG  1 
ATOM   1231 C  CD1 . LEU   B 1 16  ? 21.704 -17.045 9.594  1.00 17.85 ? 22  LEU   C CD1 1 
ATOM   1232 C  CD2 . LEU   B 1 16  ? 21.127 -14.974 8.262  1.00 17.33 ? 22  LEU   C CD2 1 
ATOM   1233 N  N   . ALA   B 1 17  ? 17.977 -13.150 12.437 1.00 16.85 ? 23  ALA   C N   1 
ATOM   1234 C  CA  . ALA   B 1 17  ? 16.704 -13.101 13.160 1.00 16.80 ? 23  ALA   C CA  1 
ATOM   1235 C  C   . ALA   B 1 17  ? 15.599 -12.556 12.284 1.00 18.35 ? 23  ALA   C C   1 
ATOM   1236 O  O   . ALA   B 1 17  ? 15.830 -11.603 11.516 1.00 19.13 ? 23  ALA   C O   1 
ATOM   1237 C  CB  . ALA   B 1 17  ? 16.830 -12.245 14.424 1.00 18.48 ? 23  ALA   C CB  1 
ATOM   1238 N  N   . THR   B 1 18  ? 14.397 -13.128 12.430 1.00 18.41 ? 24  THR   C N   1 
ATOM   1239 C  CA  . THR   B 1 18  ? 13.217 -12.703 11.649 1.00 19.42 ? 24  THR   C CA  1 
ATOM   1240 C  C   . THR   B 1 18  ? 12.392 -11.658 12.425 1.00 19.90 ? 24  THR   C C   1 
ATOM   1241 O  O   . THR   B 1 18  ? 12.656 -11.331 13.588 1.00 19.83 ? 24  THR   C O   1 
ATOM   1242 C  CB  . THR   B 1 18  ? 12.314 -13.950 11.390 1.00 21.28 ? 24  THR   C CB  1 
ATOM   1243 O  OG1 . THR   B 1 18  ? 11.763 -14.372 12.623 1.00 21.52 ? 24  THR   C OG1 1 
ATOM   1244 C  CG2 . THR   B 1 18  ? 13.049 -15.110 10.713 1.00 22.53 ? 24  THR   C CG2 1 
ATOM   1245 N  N   . HIS   B 1 19  ? 11.355 -11.067 11.730 1.00 21.32 ? 25  HIS   C N   1 
ATOM   1246 C  CA  . HIS   B 1 19  ? 10.460 -10.151 12.428 1.00 22.75 ? 25  HIS   C CA  1 
ATOM   1247 C  C   . HIS   B 1 19  ? 9.751  -10.874 13.558 1.00 20.53 ? 25  HIS   C C   1 
ATOM   1248 O  O   . HIS   B 1 19  ? 9.669  -10.294 14.631 1.00 21.44 ? 25  HIS   C O   1 
ATOM   1249 C  CB  . HIS   B 1 19  ? 9.380  -9.613  11.473 1.00 24.51 ? 25  HIS   C CB  1 
ATOM   1250 C  CG  . HIS   B 1 19  ? 8.232  -8.912  12.166 1.00 28.14 ? 25  HIS   C CG  1 
ATOM   1251 N  ND1 . HIS   B 1 19  ? 8.398  -7.678  12.770 1.00 30.34 ? 25  HIS   C ND1 1 
ATOM   1252 C  CD2 . HIS   B 1 19  ? 6.986  -9.359  12.429 1.00 30.51 ? 25  HIS   C CD2 1 
ATOM   1253 C  CE1 . HIS   B 1 19  ? 7.204  -7.336  13.242 1.00 30.55 ? 25  HIS   C CE1 1 
ATOM   1254 N  NE2 . HIS   B 1 19  ? 6.322  -8.329  13.094 1.00 30.66 ? 25  HIS   C NE2 1 
ATOM   1255 N  N   . ASN   B 1 20  ? 9.350  -12.141 13.365 1.00 21.04 ? 26  ASN   C N   1 
ATOM   1256 C  CA  . ASN   B 1 20  ? 8.714  -12.874 14.455 1.00 21.21 ? 26  ASN   C CA  1 
ATOM   1257 C  C   . ASN   B 1 20  ? 9.650  -13.043 15.656 1.00 19.80 ? 26  ASN   C C   1 
ATOM   1258 O  O   . ASN   B 1 20  ? 9.223  -12.928 16.789 1.00 19.25 ? 26  ASN   C O   1 
ATOM   1259 C  CB  . ASN   B 1 20  ? 8.201  -14.246 14.014 1.00 22.89 ? 26  ASN   C CB  1 
ATOM   1260 C  CG  . ASN   B 1 20  ? 7.402  -14.943 15.110 1.00 29.37 ? 26  ASN   C CG  1 
ATOM   1261 O  OD1 . ASN   B 1 20  ? 6.280  -14.533 15.434 1.00 32.17 ? 26  ASN   C OD1 1 
ATOM   1262 N  ND2 . ASN   B 1 20  ? 7.985  -15.957 15.766 1.00 30.56 ? 26  ASN   C ND2 1 
ATOM   1263 N  N   . ASP   B 1 21  ? 10.972 -13.244 15.403 1.00 18.60 ? 27  ASP   C N   1 
ATOM   1264 C  CA  . ASP   B 1 21  ? 11.928 -13.320 16.496 1.00 18.43 ? 27  ASP   C CA  1 
ATOM   1265 C  C   . ASP   B 1 21  ? 11.965 -12.007 17.292 1.00 17.98 ? 27  ASP   C C   1 
ATOM   1266 O  O   . ASP   B 1 21  ? 11.923 -12.014 18.516 1.00 19.25 ? 27  ASP   C O   1 
ATOM   1267 C  CB  . ASP   B 1 21  ? 13.336 -13.636 15.975 1.00 17.48 ? 27  ASP   C CB  1 
ATOM   1268 C  CG  . ASP   B 1 21  ? 13.555 -15.052 15.498 1.00 17.25 ? 27  ASP   C CG  1 
ATOM   1269 O  OD1 . ASP   B 1 21  ? 12.965 -15.982 16.111 1.00 18.77 ? 27  ASP   C OD1 1 
ATOM   1270 O  OD2 . ASP   B 1 21  ? 14.249 -15.228 14.483 1.00 17.57 ? 27  ASP   C OD2 1 
ATOM   1271 N  N   . TRP   B 1 22  ? 12.059 -10.855 16.570 1.00 18.05 ? 28  TRP   C N   1 
ATOM   1272 C  CA  . TRP   B 1 22  ? 12.090 -9.565  17.255 1.00 18.85 ? 28  TRP   C CA  1 
ATOM   1273 C  C   . TRP   B 1 22  ? 10.769 -9.230  17.965 1.00 18.85 ? 28  TRP   C C   1 
ATOM   1274 O  O   . TRP   B 1 22  ? 10.791 -8.605  19.033 1.00 19.49 ? 28  TRP   C O   1 
ATOM   1275 C  CB  . TRP   B 1 22  ? 12.458 -8.440  16.284 1.00 18.76 ? 28  TRP   C CB  1 
ATOM   1276 C  CG  . TRP   B 1 22  ? 13.931 -8.385  15.998 1.00 18.79 ? 28  TRP   C CG  1 
ATOM   1277 C  CD1 . TRP   B 1 22  ? 14.567 -8.895  14.908 1.00 19.76 ? 28  TRP   C CD1 1 
ATOM   1278 C  CD2 . TRP   B 1 22  ? 14.965 -7.850  16.859 1.00 17.16 ? 28  TRP   C CD2 1 
ATOM   1279 N  NE1 . TRP   B 1 22  ? 15.923 -8.621  14.981 1.00 19.39 ? 28  TRP   C NE1 1 
ATOM   1280 C  CE2 . TRP   B 1 22  ? 16.193 -7.993  16.173 1.00 18.75 ? 28  TRP   C CE2 1 
ATOM   1281 C  CE3 . TRP   B 1 22  ? 14.957 -7.158  18.076 1.00 19.74 ? 28  TRP   C CE3 1 
ATOM   1282 C  CZ2 . TRP   B 1 22  ? 17.382 -7.458  16.651 1.00 18.88 ? 28  TRP   C CZ2 1 
ATOM   1283 C  CZ3 . TRP   B 1 22  ? 16.165 -6.694  18.589 1.00 20.90 ? 28  TRP   C CZ3 1 
ATOM   1284 C  CH2 . TRP   B 1 22  ? 17.354 -6.836  17.862 1.00 20.25 ? 28  TRP   C CH2 1 
ATOM   1285 N  N   . ALA   B 1 23  ? 9.643  -9.719  17.423 1.00 18.95 ? 29  ALA   C N   1 
ATOM   1286 C  CA  . ALA   B 1 23  ? 8.317  -9.460  18.032 1.00 20.56 ? 29  ALA   C CA  1 
ATOM   1287 C  C   . ALA   B 1 23  ? 8.091  -10.351 19.277 1.00 21.30 ? 29  ALA   C C   1 
ATOM   1288 O  O   . ALA   B 1 23  ? 7.122  -10.176 20.025 1.00 21.60 ? 29  ALA   C O   1 
ATOM   1289 C  CB  . ALA   B 1 23  ? 7.226  -9.737  17.016 1.00 20.99 ? 29  ALA   C CB  1 
ATOM   1290 N  N   . ASN   B 1 24  ? 8.948  -11.406 19.467 1.00 21.07 ? 30  ASN   C N   1 
ATOM   1291 C  CA  . ASN   B 1 24  ? 8.838  -12.304 20.619 1.00 20.35 ? 30  ASN   C CA  1 
ATOM   1292 C  C   . ASN   B 1 24  ? 10.201 -12.360 21.327 1.00 19.69 ? 30  ASN   C C   1 
ATOM   1293 O  O   . ASN   B 1 24  ? 10.658 -13.423 21.744 1.00 19.13 ? 30  ASN   C O   1 
ATOM   1294 C  CB  . ASN   B 1 24  ? 8.377  -13.681 20.128 1.00 22.02 ? 30  ASN   C CB  1 
ATOM   1295 C  CG  . ASN   B 1 24  ? 6.959  -13.634 19.653 1.00 23.70 ? 30  ASN   C CG  1 
ATOM   1296 O  OD1 . ASN   B 1 24  ? 6.006  -13.640 20.472 1.00 24.82 ? 30  ASN   C OD1 1 
ATOM   1297 N  ND2 . ASN   B 1 24  ? 6.776  -13.549 18.353 1.00 23.19 ? 30  ASN   C ND2 1 
ATOM   1298 N  N   . LEU   B 1 25  ? 10.901 -11.227 21.408 1.00 20.36 ? 31  LEU   C N   1 
ATOM   1299 C  CA  . LEU   B 1 25  ? 12.281 -11.200 21.912 1.00 19.81 ? 31  LEU   C CA  1 
ATOM   1300 C  C   . LEU   B 1 25  ? 12.418 -11.512 23.375 1.00 20.88 ? 31  LEU   C C   1 
ATOM   1301 O  O   . LEU   B 1 25  ? 11.641 -10.999 24.196 1.00 21.89 ? 31  LEU   C O   1 
ATOM   1302 C  CB  . LEU   B 1 25  ? 12.871 -9.808  21.622 1.00 20.15 ? 31  LEU   C CB  1 
ATOM   1303 C  CG  . LEU   B 1 25  ? 14.333 -9.648  22.022 1.00 19.63 ? 31  LEU   C CG  1 
ATOM   1304 C  CD1 . LEU   B 1 25  ? 15.241 -10.496 21.115 1.00 18.64 ? 31  LEU   C CD1 1 
ATOM   1305 C  CD2 . LEU   B 1 25  ? 14.752 -8.186  21.924 1.00 21.81 ? 31  LEU   C CD2 1 
ATOM   1306 N  N   . VAL   B 1 26  ? 13.393 -12.360 23.727 1.00 19.24 ? 32  VAL   C N   1 
ATOM   1307 C  CA  . VAL   B 1 26  ? 13.751 -12.640 25.108 1.00 20.06 ? 32  VAL   C CA  1 
ATOM   1308 C  C   . VAL   B 1 26  ? 15.089 -11.931 25.438 1.00 20.50 ? 32  VAL   C C   1 
ATOM   1309 O  O   . VAL   B 1 26  ? 15.215 -11.255 26.463 1.00 20.93 ? 32  VAL   C O   1 
ATOM   1310 C  CB  . VAL   B 1 26  ? 13.889 -14.167 25.330 1.00 21.06 ? 32  VAL   C CB  1 
ATOM   1311 C  CG1 . VAL   B 1 26  ? 14.463 -14.488 26.709 1.00 22.35 ? 32  VAL   C CG1 1 
ATOM   1312 C  CG2 . VAL   B 1 26  ? 12.553 -14.880 25.120 1.00 20.61 ? 32  VAL   C CG2 1 
ATOM   1313 N  N   . TRP   B 1 27  ? 16.106 -12.060 24.557 1.00 18.06 ? 33  TRP   C N   1 
ATOM   1314 C  CA  . TRP   B 1 27  ? 17.432 -11.500 24.832 1.00 17.99 ? 33  TRP   C CA  1 
ATOM   1315 C  C   . TRP   B 1 27  ? 18.245 -11.462 23.534 1.00 17.12 ? 33  TRP   C C   1 
ATOM   1316 O  O   . TRP   B 1 27  ? 18.035 -12.343 22.665 1.00 16.89 ? 33  TRP   C O   1 
ATOM   1317 C  CB  . TRP   B 1 27  ? 18.161 -12.411 25.880 1.00 19.31 ? 33  TRP   C CB  1 
ATOM   1318 C  CG  . TRP   B 1 27  ? 19.631 -12.164 26.095 1.00 19.58 ? 33  TRP   C CG  1 
ATOM   1319 C  CD1 . TRP   B 1 27  ? 20.208 -11.216 26.896 1.00 21.78 ? 33  TRP   C CD1 1 
ATOM   1320 C  CD2 . TRP   B 1 27  ? 20.717 -12.838 25.427 1.00 17.56 ? 33  TRP   C CD2 1 
ATOM   1321 N  NE1 . TRP   B 1 27  ? 21.596 -11.299 26.809 1.00 21.90 ? 33  TRP   C NE1 1 
ATOM   1322 C  CE2 . TRP   B 1 27  ? 21.925 -12.295 25.927 1.00 18.97 ? 33  TRP   C CE2 1 
ATOM   1323 C  CE3 . TRP   B 1 27  ? 20.784 -13.864 24.474 1.00 17.15 ? 33  TRP   C CE3 1 
ATOM   1324 C  CZ2 . TRP   B 1 27  ? 23.183 -12.796 25.553 1.00 18.91 ? 33  TRP   C CZ2 1 
ATOM   1325 C  CZ3 . TRP   B 1 27  ? 22.036 -14.368 24.125 1.00 18.32 ? 33  TRP   C CZ3 1 
ATOM   1326 C  CH2 . TRP   B 1 27  ? 23.207 -13.798 24.625 1.00 18.30 ? 33  TRP   C CH2 1 
ATOM   1327 N  N   . GLU   B 1 28  ? 19.077 -10.452 23.369 1.00 16.52 ? 34  GLU   C N   1 
ATOM   1328 C  CA  . GLU   B 1 28  ? 19.938 -10.379 22.200 1.00 17.14 ? 34  GLU   C CA  1 
ATOM   1329 C  C   . GLU   B 1 28  ? 21.229 -9.698  22.551 1.00 17.35 ? 34  GLU   C C   1 
ATOM   1330 O  O   . GLU   B 1 28  ? 21.276 -8.810  23.440 1.00 17.52 ? 34  GLU   C O   1 
ATOM   1331 C  CB  . GLU   B 1 28  ? 19.256 -9.703  21.001 1.00 17.97 ? 34  GLU   C CB  1 
ATOM   1332 C  CG  . GLU   B 1 28  ? 18.699 -8.320  21.300 1.00 19.08 ? 34  GLU   C CG  1 
ATOM   1333 C  CD  . GLU   B 1 28  ? 19.676 -7.158  21.240 1.00 21.42 ? 34  GLU   C CD  1 
ATOM   1334 O  OE1 . GLU   B 1 28  ? 19.450 -6.139  21.937 1.00 24.48 ? 34  GLU   C OE1 1 
ATOM   1335 O  OE2 . GLU   B 1 28  ? 20.677 -7.257  20.494 1.00 20.55 ? 34  GLU   C OE2 1 
ATOM   1336 N  N   . ASP   B 1 29  ? 22.312 -10.075 21.854 1.00 15.55 ? 35  ASP   C N   1 
ATOM   1337 C  CA  . ASP   B 1 29  ? 23.608 -9.434  22.085 1.00 16.08 ? 35  ASP   C CA  1 
ATOM   1338 C  C   . ASP   B 1 29  ? 24.374 -9.401  20.751 1.00 16.16 ? 35  ASP   C C   1 
ATOM   1339 O  O   . ASP   B 1 29  ? 24.814 -10.445 20.250 1.00 15.51 ? 35  ASP   C O   1 
ATOM   1340 C  CB  . ASP   B 1 29  ? 24.368 -10.235 23.172 1.00 17.12 ? 35  ASP   C CB  1 
ATOM   1341 C  CG  . ASP   B 1 29  ? 25.710 -9.668  23.571 1.00 21.33 ? 35  ASP   C CG  1 
ATOM   1342 O  OD1 . ASP   B 1 29  ? 26.446 -9.195  22.689 1.00 22.06 ? 35  ASP   C OD1 1 
ATOM   1343 O  OD2 . ASP   B 1 29  ? 26.086 -9.808  24.752 1.00 23.58 ? 35  ASP   C OD2 1 
ATOM   1344 N  N   . SER   B 1 30  ? 24.536 -8.194  20.168 1.00 15.95 ? 36  SER   C N   1 
ATOM   1345 C  CA  A SER   B 1 30  ? 25.218 -8.035  18.892 0.50 15.87 ? 36  SER   C CA  1 
ATOM   1346 C  CA  B SER   B 1 30  ? 25.209 -8.068  18.887 0.50 16.23 ? 36  SER   C CA  1 
ATOM   1347 C  C   . SER   B 1 30  ? 26.685 -8.488  18.979 1.00 16.19 ? 36  SER   C C   1 
ATOM   1348 O  O   . SER   B 1 30  ? 27.195 -9.082  18.016 1.00 15.57 ? 36  SER   C O   1 
ATOM   1349 C  CB  A SER   B 1 30  ? 25.114 -6.593  18.387 0.50 17.14 ? 36  SER   C CB  1 
ATOM   1350 C  CB  B SER   B 1 30  ? 25.062 -6.657  18.326 0.50 18.49 ? 36  SER   C CB  1 
ATOM   1351 O  OG  A SER   B 1 30  ? 26.027 -6.323  17.329 0.50 17.01 ? 36  SER   C OG  1 
ATOM   1352 O  OG  B SER   B 1 30  ? 25.497 -5.723  19.296 0.50 20.13 ? 36  SER   C OG  1 
ATOM   1353 N  N   . SER   B 1 31  ? 27.372 -8.200  20.115 1.00 16.58 ? 37  SER   C N   1 
ATOM   1354 C  CA  . SER   B 1 31  ? 28.788 -8.611  20.218 1.00 16.93 ? 37  SER   C CA  1 
ATOM   1355 C  C   . SER   B 1 31  ? 28.952 -10.128 20.163 1.00 15.45 ? 37  SER   C C   1 
ATOM   1356 O  O   . SER   B 1 31  ? 30.044 -10.568 19.809 1.00 16.15 ? 37  SER   C O   1 
ATOM   1357 C  CB  . SER   B 1 31  ? 29.409 -8.075  21.492 1.00 19.87 ? 37  SER   C CB  1 
ATOM   1358 O  OG  . SER   B 1 31  ? 28.993 -8.778  22.644 1.00 25.30 ? 37  SER   C OG  1 
ATOM   1359 N  N   . ARG   B 1 32  ? 27.904 -10.916 20.506 1.00 15.22 ? 38  ARG   C N   1 
ATOM   1360 C  CA  . ARG   B 1 32  ? 27.993 -12.384 20.436 1.00 14.92 ? 38  ARG   C CA  1 
ATOM   1361 C  C   . ARG   B 1 32  ? 27.351 -12.955 19.153 1.00 14.41 ? 38  ARG   C C   1 
ATOM   1362 O  O   . ARG   B 1 32  ? 27.374 -14.169 18.947 1.00 14.08 ? 38  ARG   C O   1 
ATOM   1363 C  CB  . ARG   B 1 32  ? 27.252 -12.987 21.665 1.00 16.39 ? 38  ARG   C CB  1 
ATOM   1364 C  CG  . ARG   B 1 32  ? 27.924 -12.635 22.972 1.00 16.99 ? 38  ARG   C CG  1 
ATOM   1365 C  CD  . ARG   B 1 32  ? 27.177 -13.191 24.201 1.00 15.36 ? 38  ARG   C CD  1 
ATOM   1366 N  NE  . ARG   B 1 32  ? 27.226 -14.674 24.243 1.00 14.89 ? 38  ARG   C NE  1 
ATOM   1367 C  CZ  . ARG   B 1 32  ? 27.202 -15.414 25.350 1.00 15.88 ? 38  ARG   C CZ  1 
ATOM   1368 N  NH1 . ARG   B 1 32  ? 27.103 -14.837 26.546 1.00 16.38 ? 38  ARG   C NH1 1 
ATOM   1369 N  NH2 . ARG   B 1 32  ? 27.363 -16.742 25.275 1.00 15.10 ? 38  ARG   C NH2 1 
ATOM   1370 N  N   . ASP   B 1 33  ? 26.662 -12.109 18.347 1.00 13.29 ? 39  ASP   C N   1 
ATOM   1371 C  CA  . ASP   B 1 33  ? 25.884 -12.554 17.209 1.00 13.15 ? 39  ASP   C CA  1 
ATOM   1372 C  C   . ASP   B 1 33  ? 24.784 -13.526 17.650 1.00 13.63 ? 39  ASP   C C   1 
ATOM   1373 O  O   . ASP   B 1 33  ? 24.448 -14.451 16.892 1.00 13.32 ? 39  ASP   C O   1 
ATOM   1374 C  CB  . ASP   B 1 33  ? 26.716 -13.150 16.086 1.00 13.59 ? 39  ASP   C CB  1 
ATOM   1375 C  CG  . ASP   B 1 33  ? 25.923 -13.491 14.837 1.00 14.31 ? 39  ASP   C CG  1 
ATOM   1376 O  OD1 . ASP   B 1 33  ? 25.037 -12.688 14.441 1.00 15.38 ? 39  ASP   C OD1 1 
ATOM   1377 O  OD2 . ASP   B 1 33  ? 26.245 -14.512 14.191 1.00 14.71 ? 39  ASP   C OD2 1 
ATOM   1378 N  N   . LEU   B 1 34  ? 24.114 -13.282 18.816 1.00 13.59 ? 40  LEU   C N   1 
ATOM   1379 C  CA  . LEU   B 1 34  ? 23.025 -14.174 19.269 1.00 13.65 ? 40  LEU   C CA  1 
ATOM   1380 C  C   . LEU   B 1 34  ? 21.737 -13.410 19.515 1.00 13.71 ? 40  LEU   C C   1 
ATOM   1381 O  O   . LEU   B 1 34  ? 21.775 -12.257 19.991 1.00 15.04 ? 40  LEU   C O   1 
ATOM   1382 C  CB  . LEU   B 1 34  ? 23.407 -14.891 20.572 1.00 14.14 ? 40  LEU   C CB  1 
ATOM   1383 C  CG  . LEU   B 1 34  ? 24.494 -15.995 20.475 1.00 14.06 ? 40  LEU   C CG  1 
ATOM   1384 C  CD1 . LEU   B 1 34  ? 24.727 -16.557 21.899 1.00 15.19 ? 40  LEU   C CD1 1 
ATOM   1385 C  CD2 . LEU   B 1 34  ? 24.094 -17.113 19.501 1.00 15.80 ? 40  LEU   C CD2 1 
ATOM   1386 N  N   . LEU   B 1 35  ? 20.623 -14.098 19.272 1.00 13.77 ? 41  LEU   C N   1 
ATOM   1387 C  CA  . LEU   B 1 35  ? 19.299 -13.579 19.643 1.00 14.22 ? 41  LEU   C CA  1 
ATOM   1388 C  C   . LEU   B 1 35  ? 18.465 -14.796 20.061 1.00 14.86 ? 41  LEU   C C   1 
ATOM   1389 O  O   . LEU   B 1 35  ? 18.548 -15.869 19.432 1.00 15.39 ? 41  LEU   C O   1 
ATOM   1390 C  CB  . LEU   B 1 35  ? 18.678 -12.847 18.436 1.00 14.58 ? 41  LEU   C CB  1 
ATOM   1391 C  CG  . LEU   B 1 35  ? 17.268 -12.261 18.700 1.00 15.14 ? 41  LEU   C CG  1 
ATOM   1392 C  CD1 . LEU   B 1 35  ? 17.056 -10.946 17.923 1.00 17.86 ? 41  LEU   C CD1 1 
ATOM   1393 C  CD2 . LEU   B 1 35  ? 16.160 -13.278 18.347 1.00 15.69 ? 41  LEU   C CD2 1 
ATOM   1394 N  N   . VAL   B 1 36  ? 17.691 -14.626 21.135 1.00 14.77 ? 42  VAL   C N   1 
ATOM   1395 C  CA  . VAL   B 1 36  ? 16.777 -15.642 21.635 1.00 14.50 ? 42  VAL   C CA  1 
ATOM   1396 C  C   . VAL   B 1 36  ? 15.344 -15.098 21.632 1.00 14.78 ? 42  VAL   C C   1 
ATOM   1397 O  O   . VAL   B 1 36  ? 15.117 -13.969 22.115 1.00 16.28 ? 42  VAL   C O   1 
ATOM   1398 C  CB  . VAL   B 1 36  ? 17.187 -16.086 23.053 1.00 15.35 ? 42  VAL   C CB  1 
ATOM   1399 C  CG1 . VAL   B 1 36  ? 16.221 -17.151 23.593 1.00 16.63 ? 42  VAL   C CG1 1 
ATOM   1400 C  CG2 . VAL   B 1 36  ? 18.642 -16.643 23.029 1.00 16.22 ? 42  VAL   C CG2 1 
ATOM   1401 N  N   . SER   B 1 37  ? 14.428 -15.866 21.055 1.00 15.70 ? 43  SER   C N   1 
ATOM   1402 C  CA  . SER   B 1 37  ? 13.013 -15.492 21.044 1.00 16.43 ? 43  SER   C CA  1 
ATOM   1403 C  C   . SER   B 1 37  ? 12.211 -16.596 21.718 1.00 17.33 ? 43  SER   C C   1 
ATOM   1404 O  O   . SER   B 1 37  ? 12.705 -17.719 21.960 1.00 17.09 ? 43  SER   C O   1 
ATOM   1405 C  CB  . SER   B 1 37  ? 12.529 -15.295 19.614 1.00 17.61 ? 43  SER   C CB  1 
ATOM   1406 O  OG  . SER   B 1 37  ? 12.716 -16.461 18.816 1.00 18.64 ? 43  SER   C OG  1 
ATOM   1407 N  N   . SER   B 1 38  ? 10.958 -16.280 22.103 1.00 17.77 ? 44  SER   C N   1 
ATOM   1408 C  CA  . SER   B 1 38  ? 10.097 -17.254 22.765 1.00 18.62 ? 44  SER   C CA  1 
ATOM   1409 C  C   . SER   B 1 38  ? 9.277  -18.054 21.750 1.00 20.81 ? 44  SER   C C   1 
ATOM   1410 O  O   . SER   B 1 38  ? 8.952  -17.560 20.665 1.00 21.53 ? 44  SER   C O   1 
ATOM   1411 C  CB  . SER   B 1 38  ? 9.196  -16.530 23.763 1.00 20.37 ? 44  SER   C CB  1 
ATOM   1412 O  OG  . SER   B 1 38  ? 8.356  -15.628 23.066 1.00 24.60 ? 44  SER   C OG  1 
ATOM   1413 N  N   . THR   B 1 39  ? 8.908  -19.279 22.112 1.00 20.71 ? 45  THR   C N   1 
ATOM   1414 C  CA  . THR   B 1 39  ? 8.148  -20.158 21.211 1.00 21.75 ? 45  THR   C CA  1 
ATOM   1415 C  C   . THR   B 1 39  ? 6.859  -20.626 21.910 1.00 24.47 ? 45  THR   C C   1 
ATOM   1416 O  O   . THR   B 1 39  ? 6.816  -20.716 23.127 1.00 24.29 ? 45  THR   C O   1 
ATOM   1417 C  CB  . THR   B 1 39  ? 8.988  -21.422 20.822 1.00 22.19 ? 45  THR   C CB  1 
ATOM   1418 O  OG1 . THR   B 1 39  ? 9.276  -22.167 22.003 1.00 22.80 ? 45  THR   C OG1 1 
ATOM   1419 C  CG2 . THR   B 1 39  ? 10.327 -21.070 20.122 1.00 21.86 ? 45  THR   C CG2 1 
ATOM   1420 N  N   . THR   B 1 40  ? 5.869  -21.016 21.122 1.00 26.47 ? 46  THR   C N   1 
ATOM   1421 C  CA  . THR   B 1 40  ? 4.633  -21.579 21.675 1.00 28.23 ? 46  THR   C CA  1 
ATOM   1422 C  C   . THR   B 1 40  ? 4.851  -23.055 21.984 1.00 28.43 ? 46  THR   C C   1 
ATOM   1423 O  O   . THR   B 1 40  ? 4.447  -23.539 23.047 1.00 29.97 ? 46  THR   C O   1 
ATOM   1424 C  CB  . THR   B 1 40  ? 3.490  -21.326 20.710 1.00 32.75 ? 46  THR   C CB  1 
ATOM   1425 O  OG1 . THR   B 1 40  ? 3.808  -21.966 19.481 1.00 36.54 ? 46  THR   C OG1 1 
ATOM   1426 C  CG2 . THR   B 1 40  ? 3.267  -19.845 20.459 1.00 32.36 ? 46  THR   C CG2 1 
ATOM   1427 N  N   . ALA   B 1 41  ? 5.505  -23.785 21.060 1.00 26.38 ? 47  ALA   C N   1 
ATOM   1428 C  CA  . ALA   B 1 41  ? 5.766  -25.208 21.274 1.00 26.64 ? 47  ALA   C CA  1 
ATOM   1429 C  C   . ALA   B 1 41  ? 7.087  -25.445 22.026 1.00 24.92 ? 47  ALA   C C   1 
ATOM   1430 O  O   . ALA   B 1 41  ? 8.014  -24.664 21.894 1.00 23.82 ? 47  ALA   C O   1 
ATOM   1431 C  CB  . ALA   B 1 41  ? 5.823  -25.935 19.933 1.00 27.88 ? 47  ALA   C CB  1 
ATOM   1432 N  N   . GLN   B 1 42  ? 7.175  -26.508 22.798 1.00 24.41 ? 48  GLN   C N   1 
ATOM   1433 C  CA  . GLN   B 1 42  ? 8.390  -26.879 23.518 1.00 24.93 ? 48  GLN   C CA  1 
ATOM   1434 C  C   . GLN   B 1 42  ? 9.392  -27.507 22.549 1.00 24.94 ? 48  GLN   C C   1 
ATOM   1435 O  O   . GLN   B 1 42  ? 9.008  -28.277 21.662 1.00 26.89 ? 48  GLN   C O   1 
ATOM   1436 C  CB  . GLN   B 1 42  ? 8.076  -27.836 24.683 1.00 29.23 ? 48  GLN   C CB  1 
ATOM   1437 C  CG  . GLN   B 1 42  ? 7.530  -27.080 25.906 1.00 37.48 ? 48  GLN   C CG  1 
ATOM   1438 C  CD  . GLN   B 1 42  ? 7.309  -28.036 27.054 1.00 48.05 ? 48  GLN   C CD  1 
ATOM   1439 O  OE1 . GLN   B 1 42  ? 6.419  -28.895 27.023 1.00 52.23 ? 48  GLN   C OE1 1 
ATOM   1440 N  NE2 . GLN   B 1 42  ? 8.115  -27.912 28.097 1.00 50.57 ? 48  GLN   C NE2 1 
ATOM   1441 N  N   . GLY   B 1 43  ? 10.653 -27.127 22.717 1.00 21.59 ? 49  GLY   C N   1 
ATOM   1442 C  CA  . GLY   B 1 43  ? 11.792 -27.633 21.953 1.00 21.98 ? 49  GLY   C CA  1 
ATOM   1443 C  C   . GLY   B 1 43  ? 12.394 -28.823 22.654 1.00 21.89 ? 49  GLY   C C   1 
ATOM   1444 O  O   . GLY   B 1 43  ? 12.105 -29.075 23.844 1.00 23.46 ? 49  GLY   C O   1 
ATOM   1445 N  N   . CYS   B 1 44  ? 13.224 -29.563 21.926 1.00 20.73 ? 50  CYS   C N   1 
ATOM   1446 C  CA  . CYS   B 1 44  ? 13.801 -30.787 22.467 1.00 21.83 ? 50  CYS   C CA  1 
ATOM   1447 C  C   . CYS   B 1 44  ? 15.300 -30.830 22.535 1.00 21.25 ? 50  CYS   C C   1 
ATOM   1448 O  O   . CYS   B 1 44  ? 15.835 -31.879 22.943 1.00 23.58 ? 50  CYS   C O   1 
ATOM   1449 C  CB  . CYS   B 1 44  ? 13.278 -31.979 21.673 1.00 22.80 ? 50  CYS   C CB  1 
ATOM   1450 S  SG  . CYS   B 1 44  ? 11.469 -32.127 21.722 1.00 30.87 ? 50  CYS   C SG  1 
ATOM   1451 N  N   . ASP   B 1 45  ? 16.011 -29.780 22.128 1.00 17.53 ? 51  ASP   C N   1 
ATOM   1452 C  CA  . ASP   B 1 45  ? 17.475 -29.779 22.196 1.00 16.84 ? 51  ASP   C CA  1 
ATOM   1453 C  C   . ASP   B 1 45  ? 17.884 -29.577 23.650 1.00 17.47 ? 51  ASP   C C   1 
ATOM   1454 O  O   . ASP   B 1 45  ? 17.156 -28.936 24.445 1.00 19.53 ? 51  ASP   C O   1 
ATOM   1455 C  CB  . ASP   B 1 45  ? 18.066 -28.624 21.351 1.00 18.38 ? 51  ASP   C CB  1 
ATOM   1456 C  CG  . ASP   B 1 45  ? 17.871 -28.789 19.862 1.00 22.17 ? 51  ASP   C CG  1 
ATOM   1457 O  OD1 . ASP   B 1 45  ? 17.903 -29.941 19.373 1.00 22.96 ? 51  ASP   C OD1 1 
ATOM   1458 O  OD2 . ASP   B 1 45  ? 17.732 -27.751 19.152 1.00 19.26 ? 51  ASP   C OD2 1 
ATOM   1459 N  N   . THR   B 1 46  ? 18.995 -30.203 24.031 1.00 15.90 ? 52  THR   C N   1 
ATOM   1460 C  CA  . THR   B 1 46  ? 19.603 -30.050 25.353 1.00 15.95 ? 52  THR   C CA  1 
ATOM   1461 C  C   . THR   B 1 46  ? 20.863 -29.197 25.175 1.00 15.46 ? 52  THR   C C   1 
ATOM   1462 O  O   . THR   B 1 46  ? 21.671 -29.494 24.278 1.00 16.10 ? 52  THR   C O   1 
ATOM   1463 C  CB  . THR   B 1 46  ? 19.994 -31.416 25.914 1.00 18.10 ? 52  THR   C CB  1 
ATOM   1464 O  OG1 . THR   B 1 46  ? 18.775 -32.193 26.098 1.00 20.24 ? 52  THR   C OG1 1 
ATOM   1465 C  CG2 . THR   B 1 46  ? 20.761 -31.287 27.242 1.00 20.05 ? 52  THR   C CG2 1 
ATOM   1466 N  N   . ILE   B 1 47  ? 21.053 -28.173 26.026 1.00 15.40 ? 53  ILE   C N   1 
ATOM   1467 C  CA  . ILE   B 1 47  ? 22.263 -27.351 25.970 1.00 15.01 ? 53  ILE   C CA  1 
ATOM   1468 C  C   . ILE   B 1 47  ? 23.358 -28.024 26.801 1.00 14.51 ? 53  ILE   C C   1 
ATOM   1469 O  O   . ILE   B 1 47  ? 23.118 -28.499 27.923 1.00 15.98 ? 53  ILE   C O   1 
ATOM   1470 C  CB  . ILE   B 1 47  ? 22.020 -25.965 26.585 1.00 16.09 ? 53  ILE   C CB  1 
ATOM   1471 C  CG1 . ILE   B 1 47  ? 20.835 -25.254 25.940 1.00 16.99 ? 53  ILE   C CG1 1 
ATOM   1472 C  CG2 . ILE   B 1 47  ? 23.289 -25.113 26.491 1.00 16.49 ? 53  ILE   C CG2 1 
ATOM   1473 C  CD1 . ILE   B 1 47  ? 21.006 -25.107 24.387 1.00 19.52 ? 53  ILE   C CD1 1 
ATOM   1474 N  N   . ALA   B 1 48  ? 24.560 -28.110 26.238 1.00 12.97 ? 54  ALA   C N   1 
ATOM   1475 C  CA  . ALA   B 1 48  ? 25.679 -28.686 26.989 1.00 12.62 ? 54  ALA   C CA  1 
ATOM   1476 C  C   . ALA   B 1 48  ? 26.046 -27.762 28.150 1.00 12.83 ? 54  ALA   C C   1 
ATOM   1477 O  O   . ALA   B 1 48  ? 26.059 -26.525 28.016 1.00 13.09 ? 54  ALA   C O   1 
ATOM   1478 C  CB  . ALA   B 1 48  ? 26.880 -28.812 26.071 1.00 12.90 ? 54  ALA   C CB  1 
ATOM   1479 N  N   . ARG   B 1 49  ? 26.408 -28.363 29.295 1.00 12.80 ? 55  ARG   C N   1 
ATOM   1480 C  CA  . ARG   B 1 49  ? 26.870 -27.621 30.468 1.00 13.54 ? 55  ARG   C CA  1 
ATOM   1481 C  C   . ARG   B 1 49  ? 28.190 -28.282 30.843 1.00 13.65 ? 55  ARG   C C   1 
ATOM   1482 O  O   . ARG   B 1 49  ? 28.226 -29.300 31.571 1.00 14.79 ? 55  ARG   C O   1 
ATOM   1483 C  CB  . ARG   B 1 49  ? 25.828 -27.632 31.598 1.00 13.93 ? 55  ARG   C CB  1 
ATOM   1484 C  CG  . ARG   B 1 49  ? 24.452 -27.099 31.177 1.00 12.79 ? 55  ARG   C CG  1 
ATOM   1485 C  CD  . ARG   B 1 49  ? 24.478 -25.611 30.849 1.00 15.16 ? 55  ARG   C CD  1 
ATOM   1486 N  NE  . ARG   B 1 49  ? 23.122 -25.150 30.484 1.00 15.87 ? 55  ARG   C NE  1 
ATOM   1487 C  CZ  . ARG   B 1 49  ? 22.880 -24.040 29.790 1.00 16.54 ? 55  ARG   C CZ  1 
ATOM   1488 N  NH1 . ARG   B 1 49  ? 23.871 -23.225 29.461 1.00 14.69 ? 55  ARG   C NH1 1 
ATOM   1489 N  NH2 . ARG   B 1 49  ? 21.634 -23.721 29.444 1.00 18.06 ? 55  ARG   C NH2 1 
ATOM   1490 N  N   . CYS   B 1 50  ? 29.281 -27.703 30.332 1.00 13.22 ? 56  CYS   C N   1 
ATOM   1491 C  CA  . CYS   B 1 50  ? 30.617 -28.350 30.366 1.00 12.87 ? 56  CYS   C CA  1 
ATOM   1492 C  C   . CYS   B 1 50  ? 31.671 -27.375 29.850 1.00 13.34 ? 56  CYS   C C   1 
ATOM   1493 O  O   . CYS   B 1 50  ? 31.355 -26.278 29.378 1.00 13.90 ? 56  CYS   C O   1 
ATOM   1494 C  CB  . CYS   B 1 50  ? 30.569 -29.571 29.436 1.00 13.00 ? 56  CYS   C CB  1 
ATOM   1495 S  SG  . CYS   B 1 50  ? 30.417 -29.115 27.654 1.00 13.26 ? 56  CYS   C SG  1 
ATOM   1496 N  N   . ASP   B 1 51  ? 32.951 -27.853 29.860 1.00 14.53 ? 57  ASP   C N   1 
ATOM   1497 C  CA  . ASP   B 1 51  ? 34.071 -27.116 29.274 1.00 13.99 ? 57  ASP   C CA  1 
ATOM   1498 C  C   . ASP   B 1 51  ? 34.756 -27.995 28.201 1.00 14.70 ? 57  ASP   C C   1 
ATOM   1499 O  O   . ASP   B 1 51  ? 35.952 -27.816 27.934 1.00 16.09 ? 57  ASP   C O   1 
ATOM   1500 C  CB  . ASP   B 1 51  ? 35.080 -26.696 30.351 1.00 17.18 ? 57  ASP   C CB  1 
ATOM   1501 C  CG  . ASP   B 1 51  ? 35.741 -27.826 31.074 1.00 21.20 ? 57  ASP   C CG  1 
ATOM   1502 O  OD1 . ASP   B 1 51  ? 35.429 -28.979 30.782 1.00 19.93 ? 57  ASP   C OD1 1 
ATOM   1503 O  OD2 . ASP   B 1 51  ? 36.647 -27.547 31.921 1.00 28.32 ? 57  ASP   C OD2 1 
ATOM   1504 N  N   . CYS   B 1 52  ? 33.969 -28.832 27.480 1.00 14.00 ? 58  CYS   C N   1 
ATOM   1505 C  CA  . CYS   B 1 52  ? 34.544 -29.606 26.356 1.00 13.46 ? 58  CYS   C CA  1 
ATOM   1506 C  C   . CYS   B 1 52  ? 35.205 -28.708 25.330 1.00 13.43 ? 58  CYS   C C   1 
ATOM   1507 O  O   . CYS   B 1 52  ? 34.753 -27.575 25.083 1.00 13.85 ? 58  CYS   C O   1 
ATOM   1508 C  CB  . CYS   B 1 52  ? 33.474 -30.419 25.626 1.00 13.23 ? 58  CYS   C CB  1 
ATOM   1509 S  SG  . CYS   B 1 52  ? 32.837 -31.844 26.551 1.00 14.03 ? 58  CYS   C SG  1 
ATOM   1510 N  N   . GLN   B 1 53  ? 36.264 -29.243 24.736 1.00 13.09 ? 59  GLN   C N   1 
ATOM   1511 C  CA  . GLN   B 1 53  ? 36.955 -28.659 23.590 1.00 14.42 ? 59  GLN   C CA  1 
ATOM   1512 C  C   . GLN   B 1 53  ? 36.982 -29.598 22.404 1.00 12.92 ? 59  GLN   C C   1 
ATOM   1513 O  O   . GLN   B 1 53  ? 37.744 -29.366 21.451 1.00 13.31 ? 59  GLN   C O   1 
ATOM   1514 C  CB  . GLN   B 1 53  ? 38.392 -28.230 23.933 1.00 14.23 ? 59  GLN   C CB  1 
ATOM   1515 C  CG  . GLN   B 1 53  ? 38.383 -27.026 24.843 1.00 17.35 ? 59  GLN   C CG  1 
ATOM   1516 C  CD  . GLN   B 1 53  ? 39.752 -26.419 25.019 1.00 20.12 ? 59  GLN   C CD  1 
ATOM   1517 O  OE1 . GLN   B 1 53  ? 40.311 -26.431 26.153 1.00 21.42 ? 59  GLN   C OE1 1 
ATOM   1518 N  NE2 . GLN   B 1 53  ? 40.347 -25.870 23.955 1.00 18.45 ? 59  GLN   C NE2 1 
ATOM   1519 N  N   . THR   B 1 54  ? 36.194 -30.689 22.412 1.00 13.12 ? 60  THR   C N   1 
ATOM   1520 C  CA  . THR   B 1 54  ? 36.061 -31.542 21.226 1.00 14.16 ? 60  THR   C CA  1 
ATOM   1521 C  C   . THR   B 1 54  ? 34.588 -31.803 21.001 1.00 14.05 ? 60  THR   C C   1 
ATOM   1522 O  O   . THR   B 1 54  ? 33.789 -31.878 21.949 1.00 14.12 ? 60  THR   C O   1 
ATOM   1523 C  CB  . THR   B 1 54  ? 36.808 -32.851 21.334 1.00 17.11 ? 60  THR   C CB  1 
ATOM   1524 O  OG1 . THR   B 1 54  ? 36.237 -33.603 22.363 1.00 22.19 ? 60  THR   C OG1 1 
ATOM   1525 C  CG2 . THR   B 1 54  ? 38.283 -32.661 21.648 1.00 17.53 ? 60  THR   C CG2 1 
ATOM   1526 N  N   . GLY   B 1 55  ? 34.195 -31.852 19.727 1.00 12.48 ? 61  GLY   C N   1 
ATOM   1527 C  CA  . GLY   B 1 55  ? 32.791 -32.068 19.385 1.00 12.74 ? 61  GLY   C CA  1 
ATOM   1528 C  C   . GLY   B 1 55  ? 32.642 -32.287 17.892 1.00 11.95 ? 61  GLY   C C   1 
ATOM   1529 O  O   . GLY   B 1 55  ? 33.639 -32.556 17.200 1.00 13.58 ? 61  GLY   C O   1 
ATOM   1530 N  N   . VAL   B 1 56  ? 31.430 -32.131 17.410 1.00 11.30 ? 62  VAL   C N   1 
ATOM   1531 C  CA  . VAL   B 1 56  ? 31.127 -32.351 15.988 1.00 10.66 ? 62  VAL   C CA  1 
ATOM   1532 C  C   . VAL   B 1 56  ? 30.219 -31.216 15.566 1.00 10.76 ? 62  VAL   C C   1 
ATOM   1533 O  O   . VAL   B 1 56  ? 29.262 -30.896 16.266 1.00 11.91 ? 62  VAL   C O   1 
ATOM   1534 C  CB  . VAL   B 1 56  ? 30.372 -33.694 15.839 1.00 11.07 ? 62  VAL   C CB  1 
ATOM   1535 C  CG1 . VAL   B 1 56  ? 29.866 -33.891 14.404 1.00 13.72 ? 62  VAL   C CG1 1 
ATOM   1536 C  CG2 . VAL   B 1 56  ? 31.297 -34.878 16.239 1.00 12.65 ? 62  VAL   C CG2 1 
ATOM   1537 N  N   . TYR   B 1 57  ? 30.482 -30.633 14.384 1.00 11.47 ? 63  TYR   C N   1 
ATOM   1538 C  CA  . TYR   B 1 57  ? 29.588 -29.558 13.870 1.00 10.91 ? 63  TYR   C CA  1 
ATOM   1539 C  C   . TYR   B 1 57  ? 29.018 -29.921 12.508 1.00 11.44 ? 63  TYR   C C   1 
ATOM   1540 O  O   . TYR   B 1 57  ? 29.709 -30.572 11.719 1.00 12.46 ? 63  TYR   C O   1 
ATOM   1541 C  CB  . TYR   B 1 57  ? 30.265 -28.144 13.829 1.00 11.12 ? 63  TYR   C CB  1 
ATOM   1542 C  CG  . TYR   B 1 57  ? 31.143 -27.827 12.636 1.00 11.60 ? 63  TYR   C CG  1 
ATOM   1543 C  CD1 . TYR   B 1 57  ? 32.422 -28.342 12.538 1.00 12.44 ? 63  TYR   C CD1 1 
ATOM   1544 C  CD2 . TYR   B 1 57  ? 30.678 -26.999 11.603 1.00 12.14 ? 63  TYR   C CD2 1 
ATOM   1545 C  CE1 . TYR   B 1 57  ? 33.255 -28.021 11.467 1.00 12.90 ? 63  TYR   C CE1 1 
ATOM   1546 C  CE2 . TYR   B 1 57  ? 31.497 -26.671 10.534 1.00 12.83 ? 63  TYR   C CE2 1 
ATOM   1547 C  CZ  . TYR   B 1 57  ? 32.768 -27.206 10.450 1.00 13.36 ? 63  TYR   C CZ  1 
ATOM   1548 O  OH  . TYR   B 1 57  ? 33.622 -26.906 9.403  1.00 15.47 ? 63  TYR   C OH  1 
ATOM   1549 N  N   . TYR   B 1 58  ? 27.866 -29.324 12.206 1.00 11.44 ? 64  TYR   C N   1 
ATOM   1550 C  CA  . TYR   B 1 58  ? 27.258 -29.513 10.874 1.00 11.75 ? 64  TYR   C CA  1 
ATOM   1551 C  C   . TYR   B 1 58  ? 27.653 -28.370 9.953  1.00 12.35 ? 64  TYR   C C   1 
ATOM   1552 O  O   . TYR   B 1 58  ? 27.387 -27.185 10.258 1.00 12.68 ? 64  TYR   C O   1 
ATOM   1553 C  CB  . TYR   B 1 58  ? 25.744 -29.615 10.961 1.00 12.76 ? 64  TYR   C CB  1 
ATOM   1554 C  CG  . TYR   B 1 58  ? 25.126 -29.922 9.613  1.00 13.75 ? 64  TYR   C CG  1 
ATOM   1555 C  CD1 . TYR   B 1 58  ? 25.465 -31.081 8.923  1.00 14.26 ? 64  TYR   C CD1 1 
ATOM   1556 C  CD2 . TYR   B 1 58  ? 24.279 -29.019 8.998  1.00 14.39 ? 64  TYR   C CD2 1 
ATOM   1557 C  CE1 . TYR   B 1 58  ? 24.979 -31.336 7.647  1.00 14.93 ? 64  TYR   C CE1 1 
ATOM   1558 C  CE2 . TYR   B 1 58  ? 23.758 -29.278 7.731  1.00 15.10 ? 64  TYR   C CE2 1 
ATOM   1559 C  CZ  . TYR   B 1 58  ? 24.099 -30.454 7.088  1.00 14.89 ? 64  TYR   C CZ  1 
ATOM   1560 O  OH  . TYR   B 1 58  ? 23.646 -30.720 5.799  1.00 19.24 ? 64  TYR   C OH  1 
ATOM   1561 N  N   . CYS   B 1 59  ? 28.155 -28.741 8.786  1.00 12.06 ? 65  CYS   C N   1 
ATOM   1562 C  CA  . CYS   B 1 59  ? 28.551 -27.797 7.733  1.00 12.42 ? 65  CYS   C CA  1 
ATOM   1563 C  C   . CYS   B 1 59  ? 27.620 -27.996 6.506  1.00 13.27 ? 65  CYS   C C   1 
ATOM   1564 O  O   . CYS   B 1 59  ? 27.792 -28.939 5.727  1.00 14.46 ? 65  CYS   C O   1 
ATOM   1565 C  CB  . CYS   B 1 59  ? 30.007 -28.047 7.359  1.00 11.50 ? 65  CYS   C CB  1 
ATOM   1566 S  SG  . CYS   B 1 59  ? 30.587 -27.027 5.957  1.00 14.99 ? 65  CYS   C SG  1 
ATOM   1567 N  N   . SER   B 1 60  ? 26.620 -27.096 6.354  1.00 14.74 ? 66  SER   C N   1 
ATOM   1568 C  CA  . SER   B 1 60  ? 25.647 -27.273 5.277  1.00 15.70 ? 66  SER   C CA  1 
ATOM   1569 C  C   . SER   B 1 60  ? 26.267 -27.208 3.887  1.00 15.78 ? 66  SER   C C   1 
ATOM   1570 O  O   . SER   B 1 60  ? 25.824 -27.957 3.001  1.00 18.02 ? 66  SER   C O   1 
ATOM   1571 C  CB  . SER   B 1 60  ? 24.539 -26.257 5.402  1.00 17.76 ? 66  SER   C CB  1 
ATOM   1572 O  OG  . SER   B 1 60  ? 23.589 -26.497 4.377  1.00 21.22 ? 66  SER   C OG  1 
ATOM   1573 N  N   . SER   B 1 61  ? 27.273 -26.346 3.703  1.00 14.85 ? 67  SER   C N   1 
ATOM   1574 C  CA  . SER   B 1 61  ? 27.900 -26.224 2.365  1.00 15.82 ? 67  SER   C CA  1 
ATOM   1575 C  C   . SER   B 1 61  ? 28.672 -27.469 1.905  1.00 17.52 ? 67  SER   C C   1 
ATOM   1576 O  O   . SER   B 1 61  ? 29.022 -27.598 0.712  1.00 18.99 ? 67  SER   C O   1 
ATOM   1577 C  CB  . SER   B 1 61  ? 28.780 -24.992 2.302  1.00 16.88 ? 67  SER   C CB  1 
ATOM   1578 O  OG  . SER   B 1 61  ? 29.864 -25.085 3.198  1.00 16.19 ? 67  SER   C OG  1 
ATOM   1579 N  N   . ARG   B 1 62  ? 28.945 -28.406 2.836  1.00 16.49 ? 68  ARG   C N   1 
ATOM   1580 C  CA  . ARG   B 1 62  ? 29.591 -29.683 2.473  1.00 16.74 ? 68  ARG   C CA  1 
ATOM   1581 C  C   . ARG   B 1 62  ? 28.657 -30.883 2.714  1.00 16.09 ? 68  ARG   C C   1 
ATOM   1582 O  O   . ARG   B 1 62  ? 29.073 -32.029 2.557  1.00 17.52 ? 68  ARG   C O   1 
ATOM   1583 C  CB  . ARG   B 1 62  ? 30.873 -29.869 3.294  1.00 17.53 ? 68  ARG   C CB  1 
ATOM   1584 C  CG  . ARG   B 1 62  ? 31.903 -28.751 3.079  1.00 22.26 ? 68  ARG   C CG  1 
ATOM   1585 C  CD  . ARG   B 1 62  ? 32.571 -28.957 1.773  1.00 20.95 ? 68  ARG   C CD  1 
ATOM   1586 N  NE  . ARG   B 1 62  ? 33.573 -27.892 1.467  1.00 23.12 ? 68  ARG   C NE  1 
ATOM   1587 C  CZ  . ARG   B 1 62  ? 33.315 -26.746 0.848  1.00 26.21 ? 68  ARG   C CZ  1 
ATOM   1588 N  NH1 . ARG   B 1 62  ? 32.097 -26.493 0.389  1.00 29.87 ? 68  ARG   C NH1 1 
ATOM   1589 N  NH2 . ARG   B 1 62  ? 34.313 -25.899 0.542  1.00 25.69 ? 68  ARG   C NH2 1 
ATOM   1590 N  N   . ARG   B 1 63  ? 27.450 -30.631 3.224  1.00 16.52 ? 69  ARG   C N   1 
ATOM   1591 C  CA  . ARG   B 1 63  ? 26.518 -31.692 3.670  1.00 17.76 ? 69  ARG   C CA  1 
ATOM   1592 C  C   . ARG   B 1 63  ? 27.215 -32.712 4.567  1.00 18.14 ? 69  ARG   C C   1 
ATOM   1593 O  O   . ARG   B 1 63  ? 27.099 -33.939 4.363  1.00 20.32 ? 69  ARG   C O   1 
ATOM   1594 C  CB  . ARG   B 1 63  ? 25.863 -32.397 2.471  1.00 18.53 ? 69  ARG   C CB  1 
ATOM   1595 C  CG  . ARG   B 1 63  ? 25.044 -31.479 1.604  1.00 22.00 ? 69  ARG   C CG  1 
ATOM   1596 C  CD  . ARG   B 1 63  ? 23.799 -31.064 2.296  1.00 25.77 ? 69  ARG   C CD  1 
ATOM   1597 N  NE  . ARG   B 1 63  ? 22.792 -30.643 1.325  1.00 27.90 ? 69  ARG   C NE  1 
ATOM   1598 C  CZ  . ARG   B 1 63  ? 22.561 -29.385 0.982  1.00 29.36 ? 69  ARG   C CZ  1 
ATOM   1599 N  NH1 . ARG   B 1 63  ? 21.585 -29.095 0.130  1.00 29.87 ? 69  ARG   C NH1 1 
ATOM   1600 N  NH2 . ARG   B 1 63  ? 23.321 -28.404 1.463  1.00 28.14 ? 69  ARG   C NH2 1 
ATOM   1601 N  N   . LYS   B 1 64  ? 28.007 -32.191 5.546  1.00 15.93 ? 70  LYS   C N   1 
ATOM   1602 C  CA  . LYS   B 1 64  ? 28.800 -33.097 6.355  1.00 16.68 ? 70  LYS   C CA  1 
ATOM   1603 C  C   . LYS   B 1 64  ? 28.896 -32.617 7.775  1.00 15.99 ? 70  LYS   C C   1 
ATOM   1604 O  O   . LYS   B 1 64  ? 28.878 -31.393 8.057  1.00 15.25 ? 70  LYS   C O   1 
ATOM   1605 C  CB  . LYS   B 1 64  ? 30.220 -33.158 5.765  1.00 20.16 ? 70  LYS   C CB  1 
ATOM   1606 C  CG  . LYS   B 1 64  ? 30.373 -34.239 4.683  1.00 30.26 ? 70  LYS   C CG  1 
ATOM   1607 C  CD  . LYS   B 1 64  ? 31.828 -34.489 4.325  1.00 39.48 ? 70  LYS   C CD  1 
ATOM   1608 C  CE  . LYS   B 1 64  ? 31.941 -35.335 3.083  1.00 45.20 ? 70  LYS   C CE  1 
ATOM   1609 N  NZ  . LYS   B 1 64  ? 31.280 -34.680 1.923  1.00 49.87 ? 70  LYS   C NZ  1 
ATOM   1610 N  N   . HIS   B 1 65  ? 28.989 -33.599 8.689  1.00 14.16 ? 71  HIS   C N   1 
ATOM   1611 C  CA  . HIS   B 1 65  ? 29.266 -33.311 10.104 1.00 14.17 ? 71  HIS   C CA  1 
ATOM   1612 C  C   . HIS   B 1 65  ? 30.738 -33.583 10.293 1.00 16.14 ? 71  HIS   C C   1 
ATOM   1613 O  O   . HIS   B 1 65  ? 31.234 -34.676 9.947  1.00 19.41 ? 71  HIS   C O   1 
ATOM   1614 C  CB  . HIS   B 1 65  ? 28.426 -34.235 11.006 1.00 14.20 ? 71  HIS   C CB  1 
ATOM   1615 C  CG  . HIS   B 1 65  ? 26.959 -33.948 10.956 1.00 13.30 ? 71  HIS   C CG  1 
ATOM   1616 N  ND1 . HIS   B 1 65  ? 26.300 -33.189 11.898 1.00 17.11 ? 71  HIS   C ND1 1 
ATOM   1617 C  CD2 . HIS   B 1 65  ? 26.055 -34.342 10.026 1.00 13.84 ? 71  HIS   C CD2 1 
ATOM   1618 C  CE1 . HIS   B 1 65  ? 25.014 -33.201 11.557 1.00 15.21 ? 71  HIS   C CE1 1 
ATOM   1619 N  NE2 . HIS   B 1 65  ? 24.805 -33.896 10.470 1.00 16.41 ? 71  HIS   C NE2 1 
ATOM   1620 N  N   . TYR   B 1 66  ? 31.501 -32.615 10.839 1.00 13.55 ? 72  TYR   C N   1 
ATOM   1621 C  CA  . TYR   B 1 66  ? 32.939 -32.814 10.996 1.00 13.47 ? 72  TYR   C CA  1 
ATOM   1622 C  C   . TYR   B 1 66  ? 33.327 -32.859 12.478 1.00 12.61 ? 72  TYR   C C   1 
ATOM   1623 O  O   . TYR   B 1 66  ? 32.893 -31.985 13.249 1.00 13.05 ? 72  TYR   C O   1 
ATOM   1624 C  CB  . TYR   B 1 66  ? 33.677 -31.580 10.436 1.00 14.71 ? 72  TYR   C CB  1 
ATOM   1625 C  CG  . TYR   B 1 66  ? 33.651 -31.471 8.917  1.00 14.64 ? 72  TYR   C CG  1 
ATOM   1626 C  CD1 . TYR   B 1 66  ? 34.487 -32.241 8.141  1.00 16.52 ? 72  TYR   C CD1 1 
ATOM   1627 C  CD2 . TYR   B 1 66  ? 32.843 -30.534 8.272  1.00 14.83 ? 72  TYR   C CD2 1 
ATOM   1628 C  CE1 . TYR   B 1 66  ? 34.520 -32.098 6.749  1.00 17.03 ? 72  TYR   C CE1 1 
ATOM   1629 C  CE2 . TYR   B 1 66  ? 32.836 -30.409 6.884  1.00 16.13 ? 72  TYR   C CE2 1 
ATOM   1630 C  CZ  . TYR   B 1 66  ? 33.691 -31.180 6.134  1.00 16.33 ? 72  TYR   C CZ  1 
ATOM   1631 O  OH  . TYR   B 1 66  ? 33.671 -31.006 4.748  1.00 18.25 ? 72  TYR   C OH  1 
ATOM   1632 N  N   . PRO   B 1 67  ? 34.108 -33.841 12.890 1.00 12.90 ? 73  PRO   C N   1 
ATOM   1633 C  CA  . PRO   B 1 67  ? 34.664 -33.808 14.247 1.00 12.62 ? 73  PRO   C CA  1 
ATOM   1634 C  C   . PRO   B 1 67  ? 35.757 -32.751 14.344 1.00 13.33 ? 73  PRO   C C   1 
ATOM   1635 O  O   . PRO   B 1 67  ? 36.623 -32.677 13.447 1.00 15.98 ? 73  PRO   C O   1 
ATOM   1636 C  CB  . PRO   B 1 67  ? 35.248 -35.215 14.444 1.00 15.16 ? 73  PRO   C CB  1 
ATOM   1637 C  CG  . PRO   B 1 67  ? 35.437 -35.759 13.057 1.00 17.48 ? 73  PRO   C CG  1 
ATOM   1638 C  CD  . PRO   B 1 67  ? 34.617 -34.989 12.091 1.00 14.53 ? 73  PRO   C CD  1 
ATOM   1639 N  N   . VAL   B 1 68  ? 35.735 -31.935 15.402 1.00 12.42 ? 74  VAL   C N   1 
ATOM   1640 C  CA  . VAL   B 1 68  ? 36.721 -30.849 15.539 1.00 12.70 ? 74  VAL   C CA  1 
ATOM   1641 C  C   . VAL   B 1 68  ? 37.116 -30.692 16.988 1.00 12.33 ? 74  VAL   C C   1 
ATOM   1642 O  O   . VAL   B 1 68  ? 36.361 -30.963 17.916 1.00 12.53 ? 74  VAL   C O   1 
ATOM   1643 C  CB  . VAL   B 1 68  ? 36.105 -29.485 15.060 1.00 14.16 ? 74  VAL   C CB  1 
ATOM   1644 C  CG1 . VAL   B 1 68  ? 35.994 -29.390 13.517 1.00 17.06 ? 74  VAL   C CG1 1 
ATOM   1645 C  CG2 . VAL   B 1 68  ? 34.739 -29.196 15.745 1.00 15.97 ? 74  VAL   C CG2 1 
ATOM   1646 N  N   . SER   B 1 69  ? 38.325 -30.151 17.172 1.00 12.71 ? 75  SER   C N   1 
ATOM   1647 C  CA  . SER   B 1 69  ? 38.791 -29.523 18.404 1.00 13.24 ? 75  SER   C CA  1 
ATOM   1648 C  C   . SER   B 1 69  ? 38.507 -28.022 18.293 1.00 12.65 ? 75  SER   C C   1 
ATOM   1649 O  O   . SER   B 1 69  ? 38.635 -27.421 17.189 1.00 12.40 ? 75  SER   C O   1 
ATOM   1650 C  CB  . SER   B 1 69  ? 40.301 -29.692 18.510 1.00 16.15 ? 75  SER   C CB  1 
ATOM   1651 O  OG  . SER   B 1 69  ? 40.607 -31.064 18.685 1.00 20.17 ? 75  SER   C OG  1 
ATOM   1652 N  N   . PHE   B 1 70  ? 38.025 -27.422 19.364 1.00 11.78 ? 76  PHE   C N   1 
ATOM   1653 C  CA  . PHE   B 1 70  ? 37.675 -25.996 19.325 1.00 12.41 ? 76  PHE   C CA  1 
ATOM   1654 C  C   . PHE   B 1 70  ? 38.191 -25.262 20.566 1.00 12.45 ? 76  PHE   C C   1 
ATOM   1655 O  O   . PHE   B 1 70  ? 38.354 -25.878 21.632 1.00 13.19 ? 76  PHE   C O   1 
ATOM   1656 C  CB  . PHE   B 1 70  ? 36.163 -25.752 19.078 1.00 13.20 ? 76  PHE   C CB  1 
ATOM   1657 C  CG  . PHE   B 1 70  ? 35.255 -26.450 20.081 1.00 11.88 ? 76  PHE   C CG  1 
ATOM   1658 C  CD1 . PHE   B 1 70  ? 34.834 -27.752 19.876 1.00 12.41 ? 76  PHE   C CD1 1 
ATOM   1659 C  CD2 . PHE   B 1 70  ? 34.794 -25.782 21.204 1.00 12.72 ? 76  PHE   C CD2 1 
ATOM   1660 C  CE1 . PHE   B 1 70  ? 34.018 -28.376 20.788 1.00 12.25 ? 76  PHE   C CE1 1 
ATOM   1661 C  CE2 . PHE   B 1 70  ? 33.942 -26.422 22.103 1.00 12.61 ? 76  PHE   C CE2 1 
ATOM   1662 C  CZ  . PHE   B 1 70  ? 33.592 -27.715 21.917 1.00 12.83 ? 76  PHE   C CZ  1 
ATOM   1663 N  N   . SER   B 1 71  ? 38.460 -23.960 20.439 1.00 12.21 ? 77  SER   C N   1 
ATOM   1664 C  CA  . SER   B 1 71  ? 39.059 -23.194 21.514 1.00 13.47 ? 77  SER   C CA  1 
ATOM   1665 C  C   . SER   B 1 71  ? 38.064 -22.810 22.594 1.00 14.71 ? 77  SER   C C   1 
ATOM   1666 O  O   . SER   B 1 71  ? 36.867 -23.077 22.503 1.00 14.61 ? 77  SER   C O   1 
ATOM   1667 C  CB  . SER   B 1 71  ? 39.785 -21.981 20.912 1.00 13.59 ? 77  SER   C CB  1 
ATOM   1668 O  OG  . SER   B 1 71  ? 38.868 -21.080 20.290 1.00 15.49 ? 77  SER   C OG  1 
ATOM   1669 N  N   . LYS   B 1 72  ? 38.564 -22.181 23.655 1.00 15.07 ? 78  LYS   C N   1 
ATOM   1670 C  CA  . LYS   B 1 72  ? 37.689 -21.748 24.775 1.00 14.77 ? 78  LYS   C CA  1 
ATOM   1671 C  C   . LYS   B 1 72  ? 36.992 -20.441 24.390 1.00 14.67 ? 78  LYS   C C   1 
ATOM   1672 O  O   . LYS   B 1 72  ? 37.586 -19.609 23.693 1.00 16.16 ? 78  LYS   C O   1 
ATOM   1673 C  CB  . LYS   B 1 72  ? 38.590 -21.497 25.990 1.00 18.07 ? 78  LYS   C CB  1 
ATOM   1674 C  CG  . LYS   B 1 72  ? 39.250 -22.779 26.477 1.00 21.74 ? 78  LYS   C CG  1 
ATOM   1675 C  CD  . LYS   B 1 72  ? 39.825 -22.581 27.906 1.00 33.47 ? 78  LYS   C CD  1 
ATOM   1676 C  CE  . LYS   B 1 72  ? 40.257 -23.894 28.526 1.00 43.09 ? 78  LYS   C CE  1 
ATOM   1677 N  NZ  . LYS   B 1 72  ? 40.509 -23.733 29.990 1.00 48.00 ? 78  LYS   C NZ  1 
ATOM   1678 N  N   . PRO   B 1 73  ? 35.756 -20.187 24.850 1.00 14.03 ? 79  PRO   C N   1 
ATOM   1679 C  CA  . PRO   B 1 73  ? 35.037 -18.949 24.430 1.00 14.95 ? 79  PRO   C CA  1 
ATOM   1680 C  C   . PRO   B 1 73  ? 35.813 -17.687 24.808 1.00 15.40 ? 79  PRO   C C   1 
ATOM   1681 O  O   . PRO   B 1 73  ? 36.295 -17.561 25.971 1.00 16.47 ? 79  PRO   C O   1 
ATOM   1682 C  CB  . PRO   B 1 73  ? 33.707 -18.989 25.185 1.00 16.21 ? 79  PRO   C CB  1 
ATOM   1683 C  CG  . PRO   B 1 73  ? 33.650 -20.315 25.806 1.00 18.11 ? 79  PRO   C CG  1 
ATOM   1684 C  CD  . PRO   B 1 73  ? 34.964 -21.065 25.738 1.00 14.65 ? 79  PRO   C CD  1 
ATOM   1685 N  N   . SER   B 1 74  ? 36.041 -16.799 23.848 1.00 13.60 ? 80  SER   C N   1 
ATOM   1686 C  CA  . SER   B 1 74  ? 36.907 -15.641 24.070 1.00 15.64 ? 80  SER   C CA  1 
ATOM   1687 C  C   . SER   B 1 74  ? 36.507 -14.484 23.150 1.00 15.10 ? 80  SER   C C   1 
ATOM   1688 O  O   . SER   B 1 74  ? 35.641 -14.611 22.284 1.00 14.97 ? 80  SER   C O   1 
ATOM   1689 C  CB  . SER   B 1 74  ? 38.344 -16.029 23.709 1.00 19.81 ? 80  SER   C CB  1 
ATOM   1690 O  OG  . SER   B 1 74  ? 38.765 -17.133 24.486 1.00 28.39 ? 80  SER   C OG  1 
ATOM   1691 N  N   . LEU   B 1 75  ? 37.180 -13.347 23.346 1.00 16.01 ? 81  LEU   C N   1 
ATOM   1692 C  CA  . LEU   B 1 75  ? 36.999 -12.138 22.530 1.00 18.23 ? 81  LEU   C CA  1 
ATOM   1693 C  C   . LEU   B 1 75  ? 38.019 -12.227 21.365 1.00 18.75 ? 81  LEU   C C   1 
ATOM   1694 O  O   . LEU   B 1 75  ? 39.252 -12.187 21.588 1.00 21.08 ? 81  LEU   C O   1 
ATOM   1695 C  CB  . LEU   B 1 75  ? 37.275 -10.891 23.401 1.00 20.82 ? 81  LEU   C CB  1 
ATOM   1696 C  CG  . LEU   B 1 75  ? 36.970 -9.528  22.784 1.00 23.43 ? 81  LEU   C CG  1 
ATOM   1697 C  CD1 . LEU   B 1 75  ? 35.469 -9.348  22.560 1.00 22.23 ? 81  LEU   C CD1 1 
ATOM   1698 C  CD2 . LEU   B 1 75  ? 37.444 -8.430  23.751 1.00 25.51 ? 81  LEU   C CD2 1 
ATOM   1699 N  N   . ILE   B 1 76  ? 37.529 -12.427 20.143 1.00 18.04 ? 82  ILE   C N   1 
ATOM   1700 C  CA  . ILE   B 1 76  ? 38.363 -12.686 18.955 1.00 19.33 ? 82  ILE   C CA  1 
ATOM   1701 C  C   . ILE   B 1 76  ? 38.100 -11.657 17.875 1.00 20.32 ? 82  ILE   C C   1 
ATOM   1702 O  O   . ILE   B 1 76  ? 36.923 -11.300 17.631 1.00 19.15 ? 82  ILE   C O   1 
ATOM   1703 C  CB  . ILE   B 1 76  ? 38.031 -14.093 18.427 1.00 21.87 ? 82  ILE   C CB  1 
ATOM   1704 C  CG1 . ILE   B 1 76  ? 38.346 -15.151 19.493 1.00 25.40 ? 82  ILE   C CG1 1 
ATOM   1705 C  CG2 . ILE   B 1 76  ? 38.747 -14.399 17.073 1.00 23.29 ? 82  ILE   C CG2 1 
ATOM   1706 C  CD1 . ILE   B 1 76  ? 38.200 -16.456 19.131 1.00 26.65 ? 82  ILE   C CD1 1 
ATOM   1707 N  N   . PHE   B 1 77  ? 39.177 -11.183 17.218 1.00 20.15 ? 83  PHE   C N   1 
ATOM   1708 C  CA  . PHE   B 1 77  ? 38.987 -10.217 16.133 1.00 20.65 ? 83  PHE   C CA  1 
ATOM   1709 C  C   . PHE   B 1 77  ? 38.570 -11.052 14.908 1.00 21.02 ? 83  PHE   C C   1 
ATOM   1710 O  O   . PHE   B 1 77  ? 39.255 -12.012 14.524 1.00 23.83 ? 83  PHE   C O   1 
ATOM   1711 C  CB  . PHE   B 1 77  ? 40.299 -9.451  15.834 1.00 21.50 ? 83  PHE   C CB  1 
ATOM   1712 C  CG  . PHE   B 1 77  ? 40.031 -8.293  14.896 1.00 22.80 ? 83  PHE   C CG  1 
ATOM   1713 C  CD1 . PHE   B 1 77  ? 39.372 -7.165  15.336 1.00 23.82 ? 83  PHE   C CD1 1 
ATOM   1714 C  CD2 . PHE   B 1 77  ? 40.377 -8.365  13.552 1.00 24.17 ? 83  PHE   C CD2 1 
ATOM   1715 C  CE1 . PHE   B 1 77  ? 39.079 -6.112  14.463 1.00 25.38 ? 83  PHE   C CE1 1 
ATOM   1716 C  CE2 . PHE   B 1 77  ? 40.116 -7.297  12.690 1.00 24.77 ? 83  PHE   C CE2 1 
ATOM   1717 C  CZ  . PHE   B 1 77  ? 39.485 -6.175  13.154 1.00 24.95 ? 83  PHE   C CZ  1 
ATOM   1718 N  N   . VAL   B 1 78  ? 37.475 -10.659 14.261 1.00 17.91 ? 84  VAL   C N   1 
ATOM   1719 C  CA  . VAL   B 1 78  ? 36.946 -11.370 13.108 1.00 17.38 ? 84  VAL   C CA  1 
ATOM   1720 C  C   . VAL   B 1 78  ? 37.031 -10.411 11.902 1.00 17.49 ? 84  VAL   C C   1 
ATOM   1721 O  O   . VAL   B 1 78  ? 36.573 -9.282  12.023 1.00 17.47 ? 84  VAL   C O   1 
ATOM   1722 C  CB  . VAL   B 1 78  ? 35.462 -11.765 13.398 1.00 18.29 ? 84  VAL   C CB  1 
ATOM   1723 C  CG1 . VAL   B 1 78  ? 34.882 -12.530 12.221 1.00 19.30 ? 84  VAL   C CG1 1 
ATOM   1724 C  CG2 . VAL   B 1 78  ? 35.326 -12.576 14.694 1.00 19.07 ? 84  VAL   C CG2 1 
ATOM   1725 N  N   . GLU   B 1 79  ? 37.528 -10.874 10.751 1.00 16.91 ? 85  GLU   C N   1 
ATOM   1726 C  CA  . GLU   B 1 79  ? 37.563 -10.051 9.528  1.00 17.61 ? 85  GLU   C CA  1 
ATOM   1727 C  C   . GLU   B 1 79  ? 36.133 -9.800  9.013  1.00 17.45 ? 85  GLU   C C   1 
ATOM   1728 O  O   . GLU   B 1 79  ? 35.169 -10.485 9.380  1.00 16.77 ? 85  GLU   C O   1 
ATOM   1729 C  CB  . GLU   B 1 79  ? 38.379 -10.763 8.435  1.00 20.44 ? 85  GLU   C CB  1 
ATOM   1730 C  CG  . GLU   B 1 79  ? 39.875 -10.792 8.746  1.00 24.67 ? 85  GLU   C CG  1 
ATOM   1731 C  CD  . GLU   B 1 79  ? 40.505 -9.429  8.997  1.00 31.42 ? 85  GLU   C CD  1 
ATOM   1732 O  OE1 . GLU   B 1 79  ? 40.146 -8.443  8.306  1.00 33.97 ? 85  GLU   C OE1 1 
ATOM   1733 O  OE2 . GLU   B 1 79  ? 41.335 -9.331  9.927  1.00 32.11 ? 85  GLU   C OE2 1 
ATOM   1734 N  N   . ALA   B 1 80  ? 35.964 -8.783  8.168  1.00 19.10 ? 86  ALA   C N   1 
ATOM   1735 C  CA  . ALA   B 1 80  ? 34.694 -8.427  7.607  1.00 19.75 ? 86  ALA   C CA  1 
ATOM   1736 C  C   . ALA   B 1 80  ? 34.066 -9.602  6.872  1.00 20.77 ? 86  ALA   C C   1 
ATOM   1737 O  O   . ALA   B 1 80  ? 34.776 -10.400 6.249  1.00 21.84 ? 86  ALA   C O   1 
ATOM   1738 C  CB  . ALA   B 1 80  ? 34.904 -7.258  6.635  1.00 20.65 ? 86  ALA   C CB  1 
ATOM   1739 N  N   . SER   B 1 81  ? 32.773 -9.764  7.071  1.00 19.52 ? 87  SER   C N   1 
ATOM   1740 C  CA  . SER   B 1 81  ? 32.051 -10.785 6.370  1.00 20.36 ? 87  SER   C CA  1 
ATOM   1741 C  C   . SER   B 1 81  ? 30.942 -10.110 5.575  1.00 21.20 ? 87  SER   C C   1 
ATOM   1742 O  O   . SER   B 1 81  ? 30.790 -8.848  5.583  1.00 20.79 ? 87  SER   C O   1 
ATOM   1743 C  CB  . SER   B 1 81  ? 31.476 -11.780 7.379  1.00 19.10 ? 87  SER   C CB  1 
ATOM   1744 O  OG  . SER   B 1 81  ? 30.462 -11.098 8.107  1.00 20.08 ? 87  SER   C OG  1 
ATOM   1745 N  N   . GLU   B 1 82  ? 30.122 -10.927 4.934  1.00 22.95 ? 88  GLU   C N   1 
ATOM   1746 C  CA  . GLU   B 1 82  ? 29.018 -10.309 4.211  1.00 23.67 ? 88  GLU   C CA  1 
ATOM   1747 C  C   . GLU   B 1 82  ? 27.971 -9.664  5.153  1.00 23.74 ? 88  GLU   C C   1 
ATOM   1748 O  O   . GLU   B 1 82  ? 27.167 -8.838  4.707  1.00 25.19 ? 88  GLU   C O   1 
ATOM   1749 C  CB  . GLU   B 1 82  ? 28.402 -11.265 3.197  1.00 28.76 ? 88  GLU   C CB  1 
ATOM   1750 C  CG  . GLU   B 1 82  ? 27.736 -12.506 3.736  1.00 35.34 ? 88  GLU   C CG  1 
ATOM   1751 C  CD  . GLU   B 1 82  ? 27.089 -13.258 2.586  1.00 42.16 ? 88  GLU   C CD  1 
ATOM   1752 O  OE1 . GLU   B 1 82  ? 27.746 -13.386 1.526  1.00 44.02 ? 88  GLU   C OE1 1 
ATOM   1753 O  OE2 . GLU   B 1 82  ? 25.922 -13.688 2.732  1.00 43.44 ? 88  GLU   C OE2 1 
ATOM   1754 N  N   . TYR   B 1 83  ? 28.013 -9.972  6.463  1.00 20.49 ? 89  TYR   C N   1 
ATOM   1755 C  CA  . TYR   B 1 83  ? 26.984 -9.500  7.374  1.00 20.53 ? 89  TYR   C CA  1 
ATOM   1756 C  C   . TYR   B 1 83  ? 27.489 -8.650  8.571  1.00 21.26 ? 89  TYR   C C   1 
ATOM   1757 O  O   . TYR   B 1 83  ? 26.655 -8.049  9.238  1.00 22.12 ? 89  TYR   C O   1 
ATOM   1758 C  CB  . TYR   B 1 83  ? 26.114 -10.701 7.858  1.00 19.75 ? 89  TYR   C CB  1 
ATOM   1759 C  CG  . TYR   B 1 83  ? 26.932 -11.920 8.302  1.00 18.63 ? 89  TYR   C CG  1 
ATOM   1760 C  CD1 . TYR   B 1 83  ? 27.326 -12.907 7.387  1.00 19.45 ? 89  TYR   C CD1 1 
ATOM   1761 C  CD2 . TYR   B 1 83  ? 27.382 -12.043 9.608  1.00 18.61 ? 89  TYR   C CD2 1 
ATOM   1762 C  CE1 . TYR   B 1 83  ? 28.113 -13.998 7.782  1.00 17.94 ? 89  TYR   C CE1 1 
ATOM   1763 C  CE2 . TYR   B 1 83  ? 28.140 -13.130 10.019 1.00 19.65 ? 89  TYR   C CE2 1 
ATOM   1764 C  CZ  . TYR   B 1 83  ? 28.498 -14.121 9.108  1.00 18.59 ? 89  TYR   C CZ  1 
ATOM   1765 O  OH  . TYR   B 1 83  ? 29.311 -15.185 9.488  1.00 19.01 ? 89  TYR   C OH  1 
ATOM   1766 N  N   . TYR   B 1 84  ? 28.801 -8.519  8.813  1.00 18.53 ? 90  TYR   C N   1 
ATOM   1767 C  CA  . TYR   B 1 84  ? 29.348 -7.605  9.833  1.00 18.30 ? 90  TYR   C CA  1 
ATOM   1768 C  C   . TYR   B 1 84  ? 30.656 -7.000  9.290  1.00 17.63 ? 90  TYR   C C   1 
ATOM   1769 O  O   . TYR   B 1 84  ? 31.377 -7.657  8.530  1.00 17.85 ? 90  TYR   C O   1 
ATOM   1770 C  CB  . TYR   B 1 84  ? 29.730 -8.354  11.166 1.00 17.88 ? 90  TYR   C CB  1 
ATOM   1771 C  CG  . TYR   B 1 84  ? 28.547 -8.805  12.008 1.00 15.57 ? 90  TYR   C CG  1 
ATOM   1772 C  CD1 . TYR   B 1 84  ? 27.633 -7.884  12.530 1.00 16.34 ? 90  TYR   C CD1 1 
ATOM   1773 C  CD2 . TYR   B 1 84  ? 28.320 -10.134 12.258 1.00 15.54 ? 90  TYR   C CD2 1 
ATOM   1774 C  CE1 . TYR   B 1 84  ? 26.558 -8.291  13.329 1.00 16.06 ? 90  TYR   C CE1 1 
ATOM   1775 C  CE2 . TYR   B 1 84  ? 27.252 -10.557 13.052 1.00 15.17 ? 90  TYR   C CE2 1 
ATOM   1776 C  CZ  . TYR   B 1 84  ? 26.376 -9.635  13.600 1.00 15.44 ? 90  TYR   C CZ  1 
ATOM   1777 O  OH  . TYR   B 1 84  ? 25.299 -10.062 14.366 1.00 15.78 ? 90  TYR   C OH  1 
ATOM   1778 N  N   . PRO   B 1 85  ? 31.049 -5.804  9.761  1.00 17.63 ? 91  PRO   C N   1 
ATOM   1779 C  CA  . PRO   B 1 85  ? 32.404 -5.308  9.457  1.00 17.06 ? 91  PRO   C CA  1 
ATOM   1780 C  C   . PRO   B 1 85  ? 33.442 -6.099  10.274 1.00 17.63 ? 91  PRO   C C   1 
ATOM   1781 O  O   . PRO   B 1 85  ? 33.082 -6.930  11.159 1.00 17.66 ? 91  PRO   C O   1 
ATOM   1782 C  CB  . PRO   B 1 85  ? 32.330 -3.847  9.943  1.00 18.14 ? 91  PRO   C CB  1 
ATOM   1783 C  CG  . PRO   B 1 85  ? 31.403 -3.909  11.104 1.00 18.75 ? 91  PRO   C CG  1 
ATOM   1784 C  CD  . PRO   B 1 85  ? 30.331 -4.935  10.733 1.00 18.17 ? 91  PRO   C CD  1 
ATOM   1785 N  N   . ALA   B 1 86  ? 34.753 -5.834  10.050 1.00 17.06 ? 92  ALA   C N   1 
ATOM   1786 C  CA  . ALA   B 1 86  ? 35.818 -6.415  10.866 1.00 18.02 ? 92  ALA   C CA  1 
ATOM   1787 C  C   . ALA   B 1 86  ? 35.650 -5.850  12.278 1.00 19.59 ? 92  ALA   C C   1 
ATOM   1788 O  O   . ALA   B 1 86  ? 35.389 -4.642  12.446 1.00 21.18 ? 92  ALA   C O   1 
ATOM   1789 C  CB  . ALA   B 1 86  ? 37.182 -6.021  10.290 1.00 18.33 ? 92  ALA   C CB  1 
ATOM   1790 N  N   . ARG   B 1 87  ? 35.648 -6.733  13.274 1.00 18.88 ? 93  ARG   C N   1 
ATOM   1791 C  CA  . ARG   B 1 87  ? 35.356 -6.327  14.640 1.00 18.90 ? 93  ARG   C CA  1 
ATOM   1792 C  C   . ARG   B 1 87  ? 35.720 -7.426  15.626 1.00 18.24 ? 93  ARG   C C   1 
ATOM   1793 O  O   . ARG   B 1 87  ? 35.971 -8.566  15.224 1.00 17.98 ? 93  ARG   C O   1 
ATOM   1794 C  CB  . ARG   B 1 87  ? 33.841 -6.028  14.805 1.00 19.13 ? 93  ARG   C CB  1 
ATOM   1795 C  CG  . ARG   B 1 87  ? 32.979 -7.304  14.800 1.00 17.44 ? 93  ARG   C CG  1 
ATOM   1796 C  CD  . ARG   B 1 87  ? 31.492 -6.998  14.810 1.00 18.01 ? 93  ARG   C CD  1 
ATOM   1797 N  NE  . ARG   B 1 87  ? 30.786 -8.269  15.050 1.00 17.85 ? 93  ARG   C NE  1 
ATOM   1798 C  CZ  . ARG   B 1 87  ? 29.707 -8.440  15.780 1.00 18.67 ? 93  ARG   C CZ  1 
ATOM   1799 N  NH1 . ARG   B 1 87  ? 29.109 -7.393  16.366 1.00 18.75 ? 93  ARG   C NH1 1 
ATOM   1800 N  NH2 . ARG   B 1 87  ? 29.223 -9.662  15.971 1.00 20.41 ? 93  ARG   C NH2 1 
ATOM   1801 N  N   . TYR   B 1 88  ? 35.673 -7.105  16.931 1.00 19.78 ? 94  TYR   C N   1 
ATOM   1802 C  CA  . TYR   B 1 88  ? 35.802 -8.139  17.961 1.00 21.35 ? 94  TYR   C CA  1 
ATOM   1803 C  C   . TYR   B 1 88  ? 34.436 -8.745  18.225 1.00 19.42 ? 94  TYR   C C   1 
ATOM   1804 O  O   . TYR   B 1 88  ? 33.453 -8.022  18.426 1.00 20.74 ? 94  TYR   C O   1 
ATOM   1805 C  CB  . TYR   B 1 88  ? 36.301 -7.557  19.301 1.00 24.55 ? 94  TYR   C CB  1 
ATOM   1806 C  CG  . TYR   B 1 88  ? 37.760 -7.213  19.223 1.00 28.50 ? 94  TYR   C CG  1 
ATOM   1807 C  CD1 . TYR   B 1 88  ? 38.729 -8.187  19.393 1.00 30.75 ? 94  TYR   C CD1 1 
ATOM   1808 C  CD2 . TYR   B 1 88  ? 38.166 -5.927  18.878 1.00 30.99 ? 94  TYR   C CD2 1 
ATOM   1809 C  CE1 . TYR   B 1 88  ? 40.076 -7.885  19.236 1.00 32.71 ? 94  TYR   C CE1 1 
ATOM   1810 C  CE2 . TYR   B 1 88  ? 39.497 -5.611  18.725 1.00 33.07 ? 94  TYR   C CE2 1 
ATOM   1811 C  CZ  . TYR   B 1 88  ? 40.450 -6.585  18.913 1.00 34.53 ? 94  TYR   C CZ  1 
ATOM   1812 O  OH  . TYR   B 1 88  ? 41.746 -6.164  18.743 1.00 38.93 ? 94  TYR   C OH  1 
ATOM   1813 N  N   . GLN   B 1 89  ? 34.377 -10.063 18.270 1.00 17.99 ? 95  GLN   C N   1 
ATOM   1814 C  CA  . GLN   B 1 89  ? 33.150 -10.772 18.634 1.00 16.56 ? 95  GLN   C CA  1 
ATOM   1815 C  C   . GLN   B 1 89  ? 33.475 -11.503 19.959 1.00 15.82 ? 95  GLN   C C   1 
ATOM   1816 O  O   . GLN   B 1 89  ? 34.562 -12.105 20.099 1.00 16.27 ? 95  GLN   C O   1 
ATOM   1817 C  CB  . GLN   B 1 89  ? 32.788 -11.754 17.528 1.00 17.22 ? 95  GLN   C CB  1 
ATOM   1818 C  CG  . GLN   B 1 89  ? 31.531 -12.524 17.854 1.00 17.56 ? 95  GLN   C CG  1 
ATOM   1819 C  CD  . GLN   B 1 89  ? 30.819 -13.071 16.637 1.00 17.00 ? 95  GLN   C CD  1 
ATOM   1820 O  OE1 . GLN   B 1 89  ? 30.761 -12.459 15.547 1.00 17.31 ? 95  GLN   C OE1 1 
ATOM   1821 N  NE2 . GLN   B 1 89  ? 30.251 -14.235 16.804 1.00 16.92 ? 95  GLN   C NE2 1 
ATOM   1822 N  N   . SER   B 1 90  ? 32.569 -11.467 20.909 1.00 14.36 ? 96  SER   C N   1 
ATOM   1823 C  CA  . SER   B 1 90  ? 32.778 -12.092 22.213 1.00 16.27 ? 96  SER   C CA  1 
ATOM   1824 C  C   . SER   B 1 90  ? 32.163 -13.512 22.263 1.00 14.75 ? 96  SER   C C   1 
ATOM   1825 O  O   . SER   B 1 90  ? 31.310 -13.850 21.441 1.00 15.18 ? 96  SER   C O   1 
ATOM   1826 C  CB  . SER   B 1 90  ? 32.208 -11.211 23.347 1.00 17.23 ? 96  SER   C CB  1 
ATOM   1827 O  OG  . SER   B 1 90  ? 30.808 -11.148 23.206 1.00 17.26 ? 96  SER   C OG  1 
ATOM   1828 N  N   . HIS   B 1 91  ? 32.613 -14.306 23.256 1.00 13.80 ? 97  HIS   C N   1 
ATOM   1829 C  CA  . HIS   B 1 91  ? 32.135 -15.654 23.511 1.00 13.43 ? 97  HIS   C CA  1 
ATOM   1830 C  C   . HIS   B 1 91  ? 32.208 -16.527 22.236 1.00 13.83 ? 97  HIS   C C   1 
ATOM   1831 O  O   . HIS   B 1 91  ? 31.311 -17.349 21.988 1.00 14.29 ? 97  HIS   C O   1 
ATOM   1832 C  CB  . HIS   B 1 91  ? 30.698 -15.646 24.094 1.00 14.45 ? 97  HIS   C CB  1 
ATOM   1833 C  CG  . HIS   B 1 91  ? 30.583 -14.876 25.394 1.00 15.69 ? 97  HIS   C CG  1 
ATOM   1834 N  ND1 . HIS   B 1 91  ? 30.572 -15.536 26.612 1.00 17.64 ? 97  HIS   C ND1 1 
ATOM   1835 C  CD2 . HIS   B 1 91  ? 30.461 -13.533 25.614 1.00 16.90 ? 97  HIS   C CD2 1 
ATOM   1836 C  CE1 . HIS   B 1 91  ? 30.414 -14.587 27.544 1.00 18.27 ? 97  HIS   C CE1 1 
ATOM   1837 N  NE2 . HIS   B 1 91  ? 30.332 -13.364 26.986 1.00 19.40 ? 97  HIS   C NE2 1 
ATOM   1838 N  N   . LEU   B 1 92  ? 33.293 -16.368 21.489 1.00 12.75 ? 98  LEU   C N   1 
ATOM   1839 C  CA  . LEU   B 1 92  ? 33.497 -17.080 20.243 1.00 13.06 ? 98  LEU   C CA  1 
ATOM   1840 C  C   . LEU   B 1 92  ? 34.575 -18.143 20.428 1.00 13.02 ? 98  LEU   C C   1 
ATOM   1841 O  O   . LEU   B 1 92  ? 35.550 -17.947 21.147 1.00 13.80 ? 98  LEU   C O   1 
ATOM   1842 C  CB  . LEU   B 1 92  ? 33.968 -16.061 19.134 1.00 14.22 ? 98  LEU   C CB  1 
ATOM   1843 C  CG  . LEU   B 1 92  ? 34.053 -16.651 17.721 1.00 15.11 ? 98  LEU   C CG  1 
ATOM   1844 C  CD1 . LEU   B 1 92  ? 32.688 -16.952 17.146 1.00 16.77 ? 98  LEU   C CD1 1 
ATOM   1845 C  CD2 . LEU   B 1 92  ? 34.722 -15.630 16.735 1.00 16.50 ? 98  LEU   C CD2 1 
ATOM   1846 N  N   . MET   B 1 93  ? 34.367 -19.294 19.782 1.00 12.23 ? 99  MET   C N   1 
ATOM   1847 C  CA  . MET   B 1 93  ? 35.336 -20.416 19.841 1.00 11.74 ? 99  MET   C CA  1 
ATOM   1848 C  C   . MET   B 1 93  ? 35.730 -20.751 18.392 1.00 12.78 ? 99  MET   C C   1 
ATOM   1849 O  O   . MET   B 1 93  ? 34.846 -20.762 17.513 1.00 13.67 ? 99  MET   C O   1 
ATOM   1850 C  CB  . MET   B 1 93  ? 34.617 -21.655 20.417 1.00 12.55 ? 99  MET   C CB  1 
ATOM   1851 C  CG  . MET   B 1 93  ? 34.151 -21.390 21.841 1.00 13.76 ? 99  MET   C CG  1 
ATOM   1852 S  SD  . MET   B 1 93  ? 33.091 -22.705 22.468 1.00 14.89 ? 99  MET   C SD  1 
ATOM   1853 C  CE  . MET   B 1 93  ? 31.735 -22.612 21.386 1.00 16.37 ? 99  MET   C CE  1 
ATOM   1854 N  N   . LEU   B 1 94  ? 37.005 -21.008 18.097 1.00 12.11 ? 100 LEU   C N   1 
ATOM   1855 C  CA  . LEU   B 1 94  ? 37.439 -21.315 16.742 1.00 12.79 ? 100 LEU   C CA  1 
ATOM   1856 C  C   . LEU   B 1 94  ? 37.881 -22.780 16.612 1.00 12.36 ? 100 LEU   C C   1 
ATOM   1857 O  O   . LEU   B 1 94  ? 38.378 -23.387 17.554 1.00 13.59 ? 100 LEU   C O   1 
ATOM   1858 C  CB  . LEU   B 1 94  ? 38.679 -20.459 16.377 1.00 14.08 ? 100 LEU   C CB  1 
ATOM   1859 C  CG  . LEU   B 1 94  ? 38.515 -18.966 16.340 1.00 15.64 ? 100 LEU   C CG  1 
ATOM   1860 C  CD1 . LEU   B 1 94  ? 39.863 -18.319 15.920 1.00 17.80 ? 100 LEU   C CD1 1 
ATOM   1861 C  CD2 . LEU   B 1 94  ? 37.345 -18.530 15.432 1.00 16.61 ? 100 LEU   C CD2 1 
ATOM   1862 N  N   . ALA   B 1 95  ? 37.711 -23.320 15.400 1.00 12.76 ? 101 ALA   C N   1 
ATOM   1863 C  CA  . ALA   B 1 95  ? 38.249 -24.617 14.998 1.00 12.05 ? 101 ALA   C CA  1 
ATOM   1864 C  C   . ALA   B 1 95  ? 38.796 -24.472 13.556 1.00 12.82 ? 101 ALA   C C   1 
ATOM   1865 O  O   . ALA   B 1 95  ? 38.406 -23.543 12.850 1.00 12.41 ? 101 ALA   C O   1 
ATOM   1866 C  CB  . ALA   B 1 95  ? 37.129 -25.673 15.017 1.00 12.70 ? 101 ALA   C CB  1 
ATOM   1867 N  N   . VAL   B 1 96  ? 39.624 -25.414 13.146 1.00 13.20 ? 102 VAL   C N   1 
ATOM   1868 C  CA  . VAL   B 1 96  ? 40.067 -25.486 11.767 1.00 14.45 ? 102 VAL   C CA  1 
ATOM   1869 C  C   . VAL   B 1 96  ? 39.011 -26.232 10.961 1.00 14.11 ? 102 VAL   C C   1 
ATOM   1870 O  O   . VAL   B 1 96  ? 38.680 -27.411 11.268 1.00 16.32 ? 102 VAL   C O   1 
ATOM   1871 C  CB  . VAL   B 1 96  ? 41.432 -26.232 11.712 1.00 15.79 ? 102 VAL   C CB  1 
ATOM   1872 C  CG1 . VAL   B 1 96  ? 41.894 -26.349 10.263 1.00 17.82 ? 102 VAL   C CG1 1 
ATOM   1873 C  CG2 . VAL   B 1 96  ? 42.456 -25.486 12.554 1.00 16.30 ? 102 VAL   C CG2 1 
ATOM   1874 N  N   . GLY   B 1 97  ? 38.416 -25.524 10.010 1.00 14.85 ? 103 GLY   C N   1 
ATOM   1875 C  CA  . GLY   B 1 97  ? 37.362 -26.136 9.226  1.00 16.26 ? 103 GLY   C CA  1 
ATOM   1876 C  C   . GLY   B 1 97  ? 36.698 -25.168 8.312  1.00 15.92 ? 103 GLY   C C   1 
ATOM   1877 O  O   . GLY   B 1 97  ? 36.950 -23.950 8.355  1.00 18.02 ? 103 GLY   C O   1 
ATOM   1878 N  N   . HIS   B 1 98  ? 35.827 -25.706 7.470  1.00 15.74 ? 104 HIS   C N   1 
ATOM   1879 C  CA  . HIS   B 1 98  ? 35.118 -24.914 6.511  1.00 15.98 ? 104 HIS   C CA  1 
ATOM   1880 C  C   . HIS   B 1 98  ? 33.878 -24.208 7.060  1.00 14.73 ? 104 HIS   C C   1 
ATOM   1881 O  O   . HIS   B 1 98  ? 33.074 -24.807 7.801  1.00 15.39 ? 104 HIS   C O   1 
ATOM   1882 C  CB  . HIS   B 1 98  ? 34.744 -25.809 5.336  1.00 19.49 ? 104 HIS   C CB  1 
ATOM   1883 C  CG  . HIS   B 1 98  ? 34.260 -25.005 4.218  1.00 23.70 ? 104 HIS   C CG  1 
ATOM   1884 N  ND1 . HIS   B 1 98  ? 35.082 -24.081 3.591  1.00 25.37 ? 104 HIS   C ND1 1 
ATOM   1885 C  CD2 . HIS   B 1 98  ? 33.012 -24.921 3.722  1.00 26.70 ? 104 HIS   C CD2 1 
ATOM   1886 C  CE1 . HIS   B 1 98  ? 34.313 -23.475 2.703  1.00 27.76 ? 104 HIS   C CE1 1 
ATOM   1887 N  NE2 . HIS   B 1 98  ? 33.051 -23.950 2.747  1.00 28.37 ? 104 HIS   C NE2 1 
ATOM   1888 N  N   . SER   B 1 99  ? 33.637 -22.938 6.615  1.00 15.35 ? 105 SER   C N   1 
ATOM   1889 C  CA  . SER   B 1 99  ? 32.436 -22.181 7.048  1.00 15.58 ? 105 SER   C CA  1 
ATOM   1890 C  C   . SER   B 1 99  ? 32.192 -21.050 6.048  1.00 17.55 ? 105 SER   C C   1 
ATOM   1891 O  O   . SER   B 1 99  ? 33.019 -20.126 5.960  1.00 19.76 ? 105 SER   C O   1 
ATOM   1892 C  CB  . SER   B 1 99  ? 32.715 -21.577 8.431  1.00 16.76 ? 105 SER   C CB  1 
ATOM   1893 O  OG  . SER   B 1 99  ? 31.654 -20.713 8.830  1.00 17.67 ? 105 SER   C OG  1 
ATOM   1894 N  N   . GLU   B 1 100 ? 31.095 -21.125 5.307  1.00 17.28 ? 106 GLU   C N   1 
ATOM   1895 C  CA  . GLU   B 1 100 ? 30.630 -20.069 4.380  1.00 17.97 ? 106 GLU   C CA  1 
ATOM   1896 C  C   . GLU   B 1 100 ? 29.522 -19.340 5.098  1.00 16.68 ? 106 GLU   C C   1 
ATOM   1897 O  O   . GLU   B 1 100 ? 28.949 -19.835 6.078  1.00 16.39 ? 106 GLU   C O   1 
ATOM   1898 C  CB  . GLU   B 1 100 ? 30.105 -20.746 3.113  1.00 22.28 ? 106 GLU   C CB  1 
ATOM   1899 C  CG  . GLU   B 1 100 ? 31.321 -21.059 2.279  1.00 35.14 ? 106 GLU   C CG  1 
ATOM   1900 C  CD  . GLU   B 1 100 ? 31.065 -21.898 1.069  1.00 37.86 ? 106 GLU   C CD  1 
ATOM   1901 O  OE1 . GLU   B 1 100 ? 29.889 -22.106 0.688  1.00 44.17 ? 106 GLU   C OE1 1 
ATOM   1902 O  OE2 . GLU   B 1 100 ? 32.074 -22.437 0.570  1.00 33.33 ? 106 GLU   C OE2 1 
ATOM   1903 N  N   . PRO   B 1 101 ? 29.097 -18.166 4.584  1.00 16.88 ? 107 PRO   C N   1 
ATOM   1904 C  CA  . PRO   B 1 101 ? 28.017 -17.429 5.278  1.00 16.95 ? 107 PRO   C CA  1 
ATOM   1905 C  C   . PRO   B 1 101 ? 26.755 -18.276 5.482  1.00 17.36 ? 107 PRO   C C   1 
ATOM   1906 O  O   . PRO   B 1 101 ? 26.145 -18.204 6.547  1.00 17.30 ? 107 PRO   C O   1 
ATOM   1907 C  CB  . PRO   B 1 101 ? 27.752 -16.214 4.337  1.00 18.72 ? 107 PRO   C CB  1 
ATOM   1908 C  CG  . PRO   B 1 101 ? 28.929 -16.153 3.415  1.00 21.90 ? 107 PRO   C CG  1 
ATOM   1909 C  CD  . PRO   B 1 101 ? 29.728 -17.387 3.484  1.00 19.67 ? 107 PRO   C CD  1 
ATOM   1910 N  N   . GLY   B 1 102 ? 26.392 -19.115 4.510  1.00 15.90 ? 108 GLY   C N   1 
ATOM   1911 C  CA  . GLY   B 1 102 ? 25.171 -19.921 4.614  1.00 16.25 ? 108 GLY   C CA  1 
ATOM   1912 C  C   . GLY   B 1 102 ? 25.274 -21.037 5.644  1.00 15.69 ? 108 GLY   C C   1 
ATOM   1913 O  O   . GLY   B 1 102 ? 24.274 -21.686 5.968  1.00 16.76 ? 108 GLY   C O   1 
ATOM   1914 N  N   . ASP   B 1 103 ? 26.487 -21.314 6.161  1.00 14.44 ? 109 ASP   C N   1 
ATOM   1915 C  CA  . ASP   B 1 103 ? 26.646 -22.340 7.187  1.00 13.81 ? 109 ASP   C CA  1 
ATOM   1916 C  C   . ASP   B 1 103 ? 26.283 -21.826 8.581  1.00 14.31 ? 109 ASP   C C   1 
ATOM   1917 O  O   . ASP   B 1 103 ? 26.174 -22.625 9.522  1.00 14.16 ? 109 ASP   C O   1 
ATOM   1918 C  CB  . ASP   B 1 103 ? 28.105 -22.831 7.192  1.00 15.50 ? 109 ASP   C CB  1 
ATOM   1919 C  CG  . ASP   B 1 103 ? 28.416 -23.635 5.971  1.00 16.00 ? 109 ASP   C CG  1 
ATOM   1920 O  OD1 . ASP   B 1 103 ? 27.574 -24.385 5.540  1.00 16.74 ? 109 ASP   C OD1 1 
ATOM   1921 O  OD2 . ASP   B 1 103 ? 29.543 -23.498 5.431  1.00 16.77 ? 109 ASP   C OD2 1 
ATOM   1922 N  N   . CYS   B 1 104 ? 26.106 -20.492 8.783  1.00 13.48 ? 110 CYS   C N   1 
ATOM   1923 C  CA  . CYS   B 1 104 ? 25.700 -19.941 10.089 1.00 13.36 ? 110 CYS   C CA  1 
ATOM   1924 C  C   . CYS   B 1 104 ? 24.440 -20.623 10.576 1.00 13.62 ? 110 CYS   C C   1 
ATOM   1925 O  O   . CYS   B 1 104 ? 23.514 -20.866 9.791  1.00 15.36 ? 110 CYS   C O   1 
ATOM   1926 C  CB  . CYS   B 1 104 ? 25.477 -18.429 10.014 1.00 14.40 ? 110 CYS   C CB  1 
ATOM   1927 S  SG  . CYS   B 1 104 ? 26.995 -17.463 9.911  1.00 15.82 ? 110 CYS   C SG  1 
ATOM   1928 N  N   . GLY   B 1 105 ? 24.458 -20.997 11.843 1.00 11.73 ? 111 GLY   C N   1 
ATOM   1929 C  CA  . GLY   B 1 105 ? 23.301 -21.665 12.450 1.00 13.02 ? 111 GLY   C CA  1 
ATOM   1930 C  C   . GLY   B 1 105 ? 23.501 -23.167 12.611 1.00 13.04 ? 111 GLY   C C   1 
ATOM   1931 O  O   . GLY   B 1 105 ? 22.730 -23.818 13.335 1.00 14.25 ? 111 GLY   C O   1 
ATOM   1932 N  N   . GLY   B 1 106 ? 24.523 -23.732 11.959 1.00 13.13 ? 112 GLY   C N   1 
ATOM   1933 C  CA  . GLY   B 1 106 ? 24.833 -25.164 12.131 1.00 13.34 ? 112 GLY   C CA  1 
ATOM   1934 C  C   . GLY   B 1 106 ? 25.233 -25.462 13.570 1.00 12.16 ? 112 GLY   C C   1 
ATOM   1935 O  O   . GLY   B 1 106 ? 25.968 -24.682 14.197 1.00 12.88 ? 112 GLY   C O   1 
ATOM   1936 N  N   . ILE   B 1 107 ? 24.743 -26.573 14.099 1.00 12.30 ? 113 ILE   C N   1 
ATOM   1937 C  CA  . ILE   B 1 107 ? 25.033 -26.898 15.499 1.00 12.15 ? 113 ILE   C CA  1 
ATOM   1938 C  C   . ILE   B 1 107 ? 26.398 -27.541 15.693 1.00 11.46 ? 113 ILE   C C   1 
ATOM   1939 O  O   . ILE   B 1 107 ? 26.823 -28.424 14.938 1.00 11.90 ? 113 ILE   C O   1 
ATOM   1940 C  CB  . ILE   B 1 107 ? 23.883 -27.834 16.037 1.00 15.05 ? 113 ILE   C CB  1 
ATOM   1941 C  CG1 . ILE   B 1 107 ? 22.675 -26.880 16.461 1.00 18.20 ? 113 ILE   C CG1 1 
ATOM   1942 C  CG2 . ILE   B 1 107 ? 24.332 -28.703 17.240 1.00 15.48 ? 113 ILE   C CG2 1 
ATOM   1943 C  CD1 . ILE   B 1 107 ? 21.352 -27.602 16.839 1.00 22.13 ? 113 ILE   C CD1 1 
ATOM   1944 N  N   . LEU   B 1 108 ? 27.086 -27.104 16.783 1.00 11.29 ? 114 LEU   C N   1 
ATOM   1945 C  CA  . LEU   B 1 108 ? 28.260 -27.781 17.336 1.00 10.59 ? 114 LEU   C CA  1 
ATOM   1946 C  C   . LEU   B 1 108 ? 27.764 -28.528 18.594 1.00 11.25 ? 114 LEU   C C   1 
ATOM   1947 O  O   . LEU   B 1 108 ? 27.127 -27.927 19.457 1.00 11.01 ? 114 LEU   C O   1 
ATOM   1948 C  CB  . LEU   B 1 108 ? 29.322 -26.733 17.734 1.00 10.59 ? 114 LEU   C CB  1 
ATOM   1949 C  CG  . LEU   B 1 108 ? 30.503 -27.251 18.538 1.00 10.99 ? 114 LEU   C CG  1 
ATOM   1950 C  CD1 . LEU   B 1 108 ? 31.377 -28.191 17.701 1.00 12.68 ? 114 LEU   C CD1 1 
ATOM   1951 C  CD2 . LEU   B 1 108 ? 31.352 -26.093 19.039 1.00 12.21 ? 114 LEU   C CD2 1 
ATOM   1952 N  N   . ARG   B 1 109 ? 28.062 -29.832 18.677 1.00 11.40 ? 115 ARG   C N   1 
ATOM   1953 C  CA  . ARG   B 1 109 ? 27.589 -30.658 19.811 1.00 11.84 ? 115 ARG   C CA  1 
ATOM   1954 C  C   . ARG   B 1 109 ? 28.698 -31.505 20.369 1.00 12.32 ? 115 ARG   C C   1 
ATOM   1955 O  O   . ARG   B 1 109 ? 29.625 -31.924 19.651 1.00 12.35 ? 115 ARG   C O   1 
ATOM   1956 C  CB  . ARG   B 1 109 ? 26.408 -31.544 19.328 1.00 15.04 ? 115 ARG   C CB  1 
ATOM   1957 C  CG  . ARG   B 1 109 ? 26.812 -32.572 18.341 1.00 19.38 ? 115 ARG   C CG  1 
ATOM   1958 C  CD  . ARG   B 1 109 ? 25.626 -33.445 17.891 1.00 24.34 ? 115 ARG   C CD  1 
ATOM   1959 N  NE  . ARG   B 1 109 ? 24.728 -32.738 16.975 1.00 30.03 ? 115 ARG   C NE  1 
ATOM   1960 C  CZ  . ARG   B 1 109 ? 23.457 -32.437 17.252 1.00 39.15 ? 115 ARG   C CZ  1 
ATOM   1961 N  NH1 . ARG   B 1 109 ? 22.937 -32.738 18.442 1.00 41.98 ? 115 ARG   C NH1 1 
ATOM   1962 N  NH2 . ARG   B 1 109 ? 22.714 -31.790 16.363 1.00 40.42 ? 115 ARG   C NH2 1 
ATOM   1963 N  N   . CYS   B 1 110 ? 28.601 -31.738 21.671 1.00 12.91 ? 116 CYS   C N   1 
ATOM   1964 C  CA  . CYS   B 1 110 ? 29.537 -32.628 22.372 1.00 13.17 ? 116 CYS   C CA  1 
ATOM   1965 C  C   . CYS   B 1 110 ? 28.714 -33.725 23.050 1.00 14.65 ? 116 CYS   C C   1 
ATOM   1966 O  O   . CYS   B 1 110 ? 27.485 -33.811 22.877 1.00 14.84 ? 116 CYS   C O   1 
ATOM   1967 C  CB  . CYS   B 1 110 ? 30.376 -31.838 23.378 1.00 11.97 ? 116 CYS   C CB  1 
ATOM   1968 S  SG  . CYS   B 1 110 ? 29.377 -31.164 24.752 1.00 12.61 ? 116 CYS   C SG  1 
ATOM   1969 N  N   . GLN   B 1 111 ? 29.374 -34.580 23.908 1.00 15.67 ? 117 GLN   C N   1 
ATOM   1970 C  CA  . GLN   B 1 111 ? 28.610 -35.633 24.612 1.00 16.85 ? 117 GLN   C CA  1 
ATOM   1971 C  C   . GLN   B 1 111 ? 27.532 -35.059 25.550 1.00 17.20 ? 117 GLN   C C   1 
ATOM   1972 O  O   . GLN   B 1 111 ? 26.558 -35.761 25.925 1.00 18.18 ? 117 GLN   C O   1 
ATOM   1973 C  CB  . GLN   B 1 111 ? 29.545 -36.593 25.420 1.00 17.56 ? 117 GLN   C CB  1 
ATOM   1974 C  CG  . GLN   B 1 111 ? 30.258 -35.870 26.526 1.00 21.40 ? 117 GLN   C CG  1 
ATOM   1975 C  CD  . GLN   B 1 111 ? 31.207 -36.715 27.301 1.00 31.88 ? 117 GLN   C CD  1 
ATOM   1976 O  OE1 . GLN   B 1 111 ? 32.434 -36.643 27.101 1.00 37.09 ? 117 GLN   C OE1 1 
ATOM   1977 N  NE2 . GLN   B 1 111 ? 30.647 -37.407 28.268 1.00 30.68 ? 117 GLN   C NE2 1 
ATOM   1978 N  N   . HIS   B 1 112 ? 27.640 -33.763 25.937 1.00 14.97 ? 118 HIS   C N   1 
ATOM   1979 C  CA  . HIS   B 1 112 ? 26.675 -33.168 26.879 1.00 14.66 ? 118 HIS   C CA  1 
ATOM   1980 C  C   . HIS   B 1 112 ? 25.503 -32.473 26.214 1.00 14.71 ? 118 HIS   C C   1 
ATOM   1981 O  O   . HIS   B 1 112 ? 24.554 -32.066 26.913 1.00 16.33 ? 118 HIS   C O   1 
ATOM   1982 C  CB  . HIS   B 1 112 ? 27.406 -32.183 27.813 1.00 15.72 ? 118 HIS   C CB  1 
ATOM   1983 C  CG  . HIS   B 1 112 ? 28.576 -32.815 28.500 1.00 14.07 ? 118 HIS   C CG  1 
ATOM   1984 N  ND1 . HIS   B 1 112 ? 29.894 -32.548 28.124 1.00 12.62 ? 118 HIS   C ND1 1 
ATOM   1985 C  CD2 . HIS   B 1 112 ? 28.590 -33.660 29.559 1.00 17.30 ? 118 HIS   C CD2 1 
ATOM   1986 C  CE1 . HIS   B 1 112 ? 30.649 -33.265 28.938 1.00 14.44 ? 118 HIS   C CE1 1 
ATOM   1987 N  NE2 . HIS   B 1 112 ? 29.898 -33.906 29.839 1.00 17.25 ? 118 HIS   C NE2 1 
ATOM   1988 N  N   . GLY   B 1 113 ? 25.572 -32.244 24.894 1.00 14.01 ? 119 GLY   C N   1 
ATOM   1989 C  CA  . GLY   B 1 113 ? 24.499 -31.536 24.202 1.00 13.82 ? 119 GLY   C CA  1 
ATOM   1990 C  C   . GLY   B 1 113 ? 25.030 -30.481 23.245 1.00 12.80 ? 119 GLY   C C   1 
ATOM   1991 O  O   . GLY   B 1 113 ? 26.145 -30.591 22.733 1.00 12.84 ? 119 GLY   C O   1 
ATOM   1992 N  N   . VAL   B 1 114 ? 24.185 -29.483 22.974 1.00 12.72 ? 120 VAL   C N   1 
ATOM   1993 C  CA  . VAL   B 1 114 ? 24.519 -28.424 22.018 1.00 12.84 ? 120 VAL   C CA  1 
ATOM   1994 C  C   . VAL   B 1 114 ? 25.449 -27.407 22.700 1.00 11.96 ? 120 VAL   C C   1 
ATOM   1995 O  O   . VAL   B 1 114 ? 25.143 -26.862 23.764 1.00 13.12 ? 120 VAL   C O   1 
ATOM   1996 C  CB  . VAL   B 1 114 ? 23.204 -27.721 21.559 1.00 13.92 ? 120 VAL   C CB  1 
ATOM   1997 C  CG1 . VAL   B 1 114 ? 23.568 -26.491 20.691 1.00 15.17 ? 120 VAL   C CG1 1 
ATOM   1998 C  CG2 . VAL   B 1 114 ? 22.291 -28.695 20.790 1.00 16.33 ? 120 VAL   C CG2 1 
ATOM   1999 N  N   . VAL   B 1 115 ? 26.608 -27.177 22.091 1.00 11.41 ? 121 VAL   C N   1 
ATOM   2000 C  CA  . VAL   B 1 115 ? 27.633 -26.236 22.584 1.00 11.58 ? 121 VAL   C CA  1 
ATOM   2001 C  C   . VAL   B 1 115 ? 27.402 -24.816 22.059 1.00 12.75 ? 121 VAL   C C   1 
ATOM   2002 O  O   . VAL   B 1 115 ? 27.622 -23.840 22.782 1.00 12.90 ? 121 VAL   C O   1 
ATOM   2003 C  CB  . VAL   B 1 115 ? 29.022 -26.762 22.177 1.00 11.67 ? 121 VAL   C CB  1 
ATOM   2004 C  CG1 . VAL   B 1 115 ? 30.097 -25.766 22.558 1.00 13.32 ? 121 VAL   C CG1 1 
ATOM   2005 C  CG2 . VAL   B 1 115 ? 29.276 -28.141 22.800 1.00 13.82 ? 121 VAL   C CG2 1 
ATOM   2006 N  N   . GLY   B 1 116 ? 27.041 -24.715 20.790 1.00 12.05 ? 122 GLY   C N   1 
ATOM   2007 C  CA  . GLY   B 1 116 ? 26.824 -23.411 20.173 1.00 13.52 ? 122 GLY   C CA  1 
ATOM   2008 C  C   . GLY   B 1 116 ? 26.485 -23.585 18.709 1.00 12.67 ? 122 GLY   C C   1 
ATOM   2009 O  O   . GLY   B 1 116 ? 26.184 -24.703 18.268 1.00 12.64 ? 122 GLY   C O   1 
ATOM   2010 N  N   . ILE   B 1 117 ? 26.496 -22.440 17.971 1.00 12.07 ? 123 ILE   C N   1 
ATOM   2011 C  CA  . ILE   B 1 117 ? 26.139 -22.478 16.564 1.00 11.64 ? 123 ILE   C CA  1 
ATOM   2012 C  C   . ILE   B 1 117 ? 27.182 -21.737 15.744 1.00 11.44 ? 123 ILE   C C   1 
ATOM   2013 O  O   . ILE   B 1 117 ? 27.838 -20.780 16.213 1.00 12.70 ? 123 ILE   C O   1 
ATOM   2014 C  CB  . ILE   B 1 117 ? 24.752 -21.826 16.285 1.00 12.93 ? 123 ILE   C CB  1 
ATOM   2015 C  CG1 . ILE   B 1 117 ? 24.627 -20.423 16.914 1.00 14.92 ? 123 ILE   C CG1 1 
ATOM   2016 C  CG2 . ILE   B 1 117 ? 23.617 -22.756 16.706 1.00 14.31 ? 123 ILE   C CG2 1 
ATOM   2017 C  CD1 . ILE   B 1 117 ? 23.287 -19.645 16.461 1.00 15.04 ? 123 ILE   C CD1 1 
ATOM   2018 N  N   . VAL   B 1 118 ? 27.344 -22.161 14.466 1.00 11.56 ? 124 VAL   C N   1 
ATOM   2019 C  CA  . VAL   B 1 118 ? 28.282 -21.473 13.568 1.00 11.23 ? 124 VAL   C CA  1 
ATOM   2020 C  C   . VAL   B 1 118 ? 27.917 -19.998 13.442 1.00 12.60 ? 124 VAL   C C   1 
ATOM   2021 O  O   . VAL   B 1 118 ? 26.730 -19.660 13.245 1.00 12.18 ? 124 VAL   C O   1 
ATOM   2022 C  CB  . VAL   B 1 118 ? 28.273 -22.133 12.172 1.00 11.87 ? 124 VAL   C CB  1 
ATOM   2023 C  CG1 . VAL   B 1 118 ? 29.151 -21.382 11.172 1.00 12.97 ? 124 VAL   C CG1 1 
ATOM   2024 C  CG2 . VAL   B 1 118 ? 28.735 -23.589 12.225 1.00 12.82 ? 124 VAL   C CG2 1 
ATOM   2025 N  N   . SER   B 1 119 ? 28.952 -19.113 13.554 1.00 11.94 ? 125 SER   C N   1 
ATOM   2026 C  CA  . SER   B 1 119 ? 28.743 -17.665 13.430 1.00 12.67 ? 125 SER   C CA  1 
ATOM   2027 C  C   . SER   B 1 119 ? 29.754 -16.990 12.515 1.00 13.34 ? 125 SER   C C   1 
ATOM   2028 O  O   . SER   B 1 119 ? 29.414 -15.930 11.979 1.00 13.82 ? 125 SER   C O   1 
ATOM   2029 C  CB  . SER   B 1 119 ? 28.788 -17.070 14.834 1.00 13.29 ? 125 SER   C CB  1 
ATOM   2030 O  OG  . SER   B 1 119 ? 28.661 -15.639 14.785 1.00 14.67 ? 125 SER   C OG  1 
ATOM   2031 N  N   . THR   B 1 120 ? 30.988 -17.534 12.387 1.00 12.78 ? 126 THR   C N   1 
ATOM   2032 C  CA  . THR   B 1 120 ? 32.022 -16.874 11.568 1.00 13.08 ? 126 THR   C CA  1 
ATOM   2033 C  C   . THR   B 1 120 ? 32.715 -17.891 10.677 1.00 13.36 ? 126 THR   C C   1 
ATOM   2034 O  O   . THR   B 1 120 ? 32.642 -19.129 10.905 1.00 13.20 ? 126 THR   C O   1 
ATOM   2035 C  CB  . THR   B 1 120 ? 33.075 -16.125 12.450 1.00 13.23 ? 126 THR   C CB  1 
ATOM   2036 O  OG1 . THR   B 1 120 ? 33.948 -17.078 13.106 1.00 14.24 ? 126 THR   C OG1 1 
ATOM   2037 C  CG2 . THR   B 1 120 ? 32.473 -15.223 13.455 1.00 15.17 ? 126 THR   C CG2 1 
ATOM   2038 N  N   . GLY   B 1 121 ? 33.410 -17.372 9.681  1.00 13.94 ? 127 GLY   C N   1 
ATOM   2039 C  CA  . GLY   B 1 121 ? 34.171 -18.208 8.759  1.00 15.35 ? 127 GLY   C CA  1 
ATOM   2040 C  C   . GLY   B 1 121 ? 35.227 -17.368 8.074  1.00 18.32 ? 127 GLY   C C   1 
ATOM   2041 O  O   . GLY   B 1 121 ? 34.966 -16.232 7.714  1.00 20.44 ? 127 GLY   C O   1 
ATOM   2042 N  N   . GLY   B 1 122 ? 36.363 -17.963 7.797  1.00 21.35 ? 128 GLY   C N   1 
ATOM   2043 C  CA  . GLY   B 1 122 ? 37.447 -17.229 7.151  1.00 23.54 ? 128 GLY   C CA  1 
ATOM   2044 C  C   . GLY   B 1 122 ? 38.788 -17.831 7.405  1.00 23.01 ? 128 GLY   C C   1 
ATOM   2045 O  O   . GLY   B 1 122 ? 39.042 -18.342 8.487  1.00 23.42 ? 128 GLY   C O   1 
ATOM   2046 N  N   . ASN   B 1 123 ? 39.694 -17.693 6.429  1.00 22.46 ? 129 ASN   C N   1 
ATOM   2047 C  CA  . ASN   B 1 123 ? 41.081 -18.150 6.541  1.00 23.05 ? 129 ASN   C CA  1 
ATOM   2048 C  C   . ASN   B 1 123 ? 41.177 -19.629 6.970  1.00 21.24 ? 129 ASN   C C   1 
ATOM   2049 O  O   . ASN   B 1 123 ? 42.103 -19.981 7.719  1.00 24.01 ? 129 ASN   C O   1 
ATOM   2050 C  CB  . ASN   B 1 123 ? 41.887 -17.254 7.525  1.00 27.68 ? 129 ASN   C CB  1 
ATOM   2051 C  CG  . ASN   B 1 123 ? 42.647 -16.123 6.875  1.00 36.13 ? 129 ASN   C CG  1 
ATOM   2052 O  OD1 . ASN   B 1 123 ? 42.797 -16.054 5.648  1.00 38.09 ? 129 ASN   C OD1 1 
ATOM   2053 N  ND2 . ASN   B 1 123 ? 43.155 -15.195 7.681  1.00 39.22 ? 129 ASN   C ND2 1 
ATOM   2054 N  N   . GLY   B 1 124 ? 40.225 -20.488 6.546  1.00 19.03 ? 130 GLY   C N   1 
ATOM   2055 C  CA  . GLY   B 1 124 ? 40.268 -21.906 6.946  1.00 18.83 ? 130 GLY   C CA  1 
ATOM   2056 C  C   . GLY   B 1 124 ? 39.820 -22.209 8.372  1.00 17.31 ? 130 GLY   C C   1 
ATOM   2057 O  O   . GLY   B 1 124 ? 40.046 -23.318 8.877  1.00 17.31 ? 130 GLY   C O   1 
ATOM   2058 N  N   . LEU   B 1 125 ? 39.193 -21.216 9.010  1.00 15.07 ? 131 LEU   C N   1 
ATOM   2059 C  CA  . LEU   B 1 125 ? 38.705 -21.344 10.368 1.00 14.67 ? 131 LEU   C CA  1 
ATOM   2060 C  C   . LEU   B 1 125 ? 37.194 -21.245 10.399 1.00 14.88 ? 131 LEU   C C   1 
ATOM   2061 O  O   . LEU   B 1 125 ? 36.582 -20.556 9.537  1.00 16.50 ? 131 LEU   C O   1 
ATOM   2062 C  CB  . LEU   B 1 125 ? 39.310 -20.267 11.292 1.00 16.80 ? 131 LEU   C CB  1 
ATOM   2063 C  CG  . LEU   B 1 125 ? 40.840 -20.298 11.407 1.00 20.47 ? 131 LEU   C CG  1 
ATOM   2064 C  CD1 . LEU   B 1 125 ? 41.405 -18.988 11.985 1.00 25.67 ? 131 LEU   C CD1 1 
ATOM   2065 C  CD2 . LEU   B 1 125 ? 41.336 -21.457 12.218 1.00 22.75 ? 131 LEU   C CD2 1 
ATOM   2066 N  N   . VAL   B 1 126 ? 36.570 -21.892 11.359 1.00 12.50 ? 132 VAL   C N   1 
ATOM   2067 C  CA  . VAL   B 1 126 ? 35.128 -21.763 11.602 1.00 12.59 ? 132 VAL   C CA  1 
ATOM   2068 C  C   . VAL   B 1 126 ? 34.985 -21.300 13.053 1.00 11.85 ? 132 VAL   C C   1 
ATOM   2069 O  O   . VAL   B 1 126 ? 35.676 -21.813 13.953 1.00 12.11 ? 132 VAL   C O   1 
ATOM   2070 C  CB  . VAL   B 1 126 ? 34.368 -23.093 11.363 1.00 12.96 ? 132 VAL   C CB  1 
ATOM   2071 C  CG1 . VAL   B 1 126 ? 34.992 -24.279 12.066 1.00 14.89 ? 132 VAL   C CG1 1 
ATOM   2072 C  CG2 . VAL   B 1 126 ? 32.868 -22.974 11.708 1.00 13.65 ? 132 VAL   C CG2 1 
ATOM   2073 N  N   . GLY   B 1 127 ? 34.113 -20.310 13.265 1.00 11.44 ? 133 GLY   C N   1 
ATOM   2074 C  CA  . GLY   B 1 127 ? 33.880 -19.798 14.611 1.00 11.31 ? 133 GLY   C CA  1 
ATOM   2075 C  C   . GLY   B 1 127 ? 32.448 -20.116 15.062 1.00 11.84 ? 133 GLY   C C   1 
ATOM   2076 O  O   . GLY   B 1 127 ? 31.514 -19.954 14.272 1.00 12.29 ? 133 GLY   C O   1 
ATOM   2077 N  N   . PHE   B 1 128 ? 32.322 -20.490 16.331 1.00 10.60 ? 134 PHE   C N   1 
ATOM   2078 C  CA  . PHE   B 1 128 ? 31.028 -20.848 16.932 1.00 11.58 ? 134 PHE   C CA  1 
ATOM   2079 C  C   . PHE   B 1 128 ? 30.710 -19.919 18.074 1.00 11.84 ? 134 PHE   C C   1 
ATOM   2080 O  O   . PHE   B 1 128 ? 31.564 -19.668 18.942 1.00 11.70 ? 134 PHE   C O   1 
ATOM   2081 C  CB  . PHE   B 1 128 ? 31.096 -22.291 17.524 1.00 11.23 ? 134 PHE   C CB  1 
ATOM   2082 C  CG  . PHE   B 1 128 ? 31.625 -23.304 16.520 1.00 11.47 ? 134 PHE   C CG  1 
ATOM   2083 C  CD1 . PHE   B 1 128 ? 30.774 -23.905 15.598 1.00 11.53 ? 134 PHE   C CD1 1 
ATOM   2084 C  CD2 . PHE   B 1 128 ? 32.959 -23.706 16.547 1.00 12.64 ? 134 PHE   C CD2 1 
ATOM   2085 C  CE1 . PHE   B 1 128 ? 31.254 -24.865 14.736 1.00 12.81 ? 134 PHE   C CE1 1 
ATOM   2086 C  CE2 . PHE   B 1 128 ? 33.451 -24.659 15.636 1.00 12.63 ? 134 PHE   C CE2 1 
ATOM   2087 C  CZ  . PHE   B 1 128 ? 32.598 -25.231 14.753 1.00 13.02 ? 134 PHE   C CZ  1 
ATOM   2088 N  N   . ALA   B 1 129 ? 29.458 -19.416 18.109 1.00 12.01 ? 135 ALA   C N   1 
ATOM   2089 C  CA  . ALA   B 1 129 ? 28.969 -18.621 19.235 1.00 11.71 ? 135 ALA   C CA  1 
ATOM   2090 C  C   . ALA   B 1 129 ? 28.575 -19.605 20.368 1.00 12.41 ? 135 ALA   C C   1 
ATOM   2091 O  O   . ALA   B 1 129 ? 27.676 -20.448 20.192 1.00 12.62 ? 135 ALA   C O   1 
ATOM   2092 C  CB  . ALA   B 1 129 ? 27.743 -17.816 18.779 1.00 12.84 ? 135 ALA   C CB  1 
ATOM   2093 N  N   . ASP   B 1 130 ? 29.257 -19.524 21.491 1.00 12.23 ? 136 ASP   C N   1 
ATOM   2094 C  CA  . ASP   B 1 130 ? 28.979 -20.409 22.636 1.00 12.05 ? 136 ASP   C CA  1 
ATOM   2095 C  C   . ASP   B 1 130 ? 27.637 -20.054 23.250 1.00 12.53 ? 136 ASP   C C   1 
ATOM   2096 O  O   . ASP   B 1 130 ? 27.256 -18.868 23.322 1.00 13.22 ? 136 ASP   C O   1 
ATOM   2097 C  CB  . ASP   B 1 130 ? 30.053 -20.166 23.733 1.00 13.41 ? 136 ASP   C CB  1 
ATOM   2098 C  CG  . ASP   B 1 130 ? 29.971 -21.104 24.915 1.00 16.38 ? 136 ASP   C CG  1 
ATOM   2099 O  OD1 . ASP   B 1 130 ? 29.817 -22.313 24.701 1.00 16.09 ? 136 ASP   C OD1 1 
ATOM   2100 O  OD2 . ASP   B 1 130 ? 29.922 -20.599 26.068 1.00 18.30 ? 136 ASP   C OD2 1 
ATOM   2101 N  N   . VAL   B 1 131 ? 26.919 -21.062 23.734 1.00 12.19 ? 137 VAL   C N   1 
ATOM   2102 C  CA  . VAL   B 1 131 ? 25.681 -20.871 24.515 1.00 12.66 ? 137 VAL   C CA  1 
ATOM   2103 C  C   . VAL   B 1 131 ? 25.771 -21.543 25.886 1.00 12.76 ? 137 VAL   C C   1 
ATOM   2104 O  O   . VAL   B 1 131 ? 24.777 -21.475 26.658 1.00 13.40 ? 137 VAL   C O   1 
ATOM   2105 C  CB  . VAL   B 1 131 ? 24.411 -21.307 23.775 1.00 13.89 ? 137 VAL   C CB  1 
ATOM   2106 C  CG1 . VAL   B 1 131 ? 24.246 -20.474 22.490 1.00 13.61 ? 137 VAL   C CG1 1 
ATOM   2107 C  CG2 . VAL   B 1 131 ? 24.446 -22.800 23.444 1.00 13.44 ? 137 VAL   C CG2 1 
ATOM   2108 N  N   . ARG   B 1 132 ? 26.874 -22.224 26.228 1.00 12.52 ? 138 ARG   C N   1 
ATOM   2109 C  CA  . ARG   B 1 132 ? 26.939 -23.008 27.480 1.00 12.87 ? 138 ARG   C CA  1 
ATOM   2110 C  C   . ARG   B 1 132 ? 26.866 -22.174 28.748 1.00 13.88 ? 138 ARG   C C   1 
ATOM   2111 O  O   . ARG   B 1 132 ? 26.571 -22.735 29.827 1.00 14.77 ? 138 ARG   C O   1 
ATOM   2112 C  CB  . ARG   B 1 132 ? 28.197 -23.868 27.482 1.00 12.94 ? 138 ARG   C CB  1 
ATOM   2113 C  CG  . ARG   B 1 132 ? 28.204 -24.911 26.333 1.00 12.86 ? 138 ARG   C CG  1 
ATOM   2114 C  CD  . ARG   B 1 132 ? 29.503 -25.679 26.369 1.00 13.62 ? 138 ARG   C CD  1 
ATOM   2115 N  NE  . ARG   B 1 132 ? 30.602 -24.792 25.960 1.00 12.63 ? 138 ARG   C NE  1 
ATOM   2116 C  CZ  . ARG   B 1 132 ? 31.856 -25.188 25.780 1.00 13.24 ? 138 ARG   C CZ  1 
ATOM   2117 N  NH1 . ARG   B 1 132 ? 32.230 -26.417 26.112 1.00 13.53 ? 138 ARG   C NH1 1 
ATOM   2118 N  NH2 . ARG   B 1 132 ? 32.769 -24.333 25.322 1.00 13.55 ? 138 ARG   C NH2 1 
ATOM   2119 N  N   . ASP   B 1 133 ? 27.198 -20.881 28.665 1.00 13.73 ? 139 ASP   C N   1 
ATOM   2120 C  CA  . ASP   B 1 133 ? 27.137 -20.014 29.851 1.00 14.69 ? 139 ASP   C CA  1 
ATOM   2121 C  C   . ASP   B 1 133 ? 25.733 -19.471 30.095 1.00 15.56 ? 139 ASP   C C   1 
ATOM   2122 O  O   . ASP   B 1 133 ? 25.523 -18.858 31.156 1.00 16.89 ? 139 ASP   C O   1 
ATOM   2123 C  CB  . ASP   B 1 133 ? 28.126 -18.839 29.715 1.00 15.86 ? 139 ASP   C CB  1 
ATOM   2124 C  CG  . ASP   B 1 133 ? 27.767 -17.897 28.569 1.00 17.66 ? 139 ASP   C CG  1 
ATOM   2125 O  OD1 . ASP   B 1 133 ? 27.402 -18.388 27.479 1.00 16.08 ? 139 ASP   C OD1 1 
ATOM   2126 O  OD2 . ASP   B 1 133 ? 27.795 -16.640 28.781 1.00 19.39 ? 139 ASP   C OD2 1 
ATOM   2127 N  N   . LEU   B 1 134 ? 24.792 -19.644 29.132 1.00 14.76 ? 140 LEU   C N   1 
ATOM   2128 C  CA  . LEU   B 1 134 ? 23.439 -19.054 29.244 1.00 14.69 ? 140 LEU   C CA  1 
ATOM   2129 C  C   . LEU   B 1 134 ? 22.569 -20.003 30.038 1.00 14.78 ? 140 LEU   C C   1 
ATOM   2130 O  O   . LEU   B 1 134 ? 21.746 -20.741 29.479 1.00 14.82 ? 140 LEU   C O   1 
ATOM   2131 C  CB  . LEU   B 1 134 ? 22.856 -18.814 27.849 1.00 14.28 ? 140 LEU   C CB  1 
ATOM   2132 C  CG  . LEU   B 1 134 ? 23.737 -17.870 26.980 1.00 15.06 ? 140 LEU   C CG  1 
ATOM   2133 C  CD1 . LEU   B 1 134 ? 23.139 -17.743 25.531 1.00 16.43 ? 140 LEU   C CD1 1 
ATOM   2134 C  CD2 . LEU   B 1 134 ? 23.877 -16.444 27.624 1.00 17.93 ? 140 LEU   C CD2 1 
ATOM   2135 N  N   . LEU   B 1 135 ? 22.766 -20.023 31.391 1.00 16.12 ? 141 LEU   C N   1 
ATOM   2136 C  CA  . LEU   B 1 135 ? 22.119 -21.073 32.203 1.00 16.49 ? 141 LEU   C CA  1 
ATOM   2137 C  C   . LEU   B 1 135 ? 20.611 -20.976 32.240 1.00 16.31 ? 141 LEU   C C   1 
ATOM   2138 O  O   . LEU   B 1 135 ? 19.924 -21.995 32.426 1.00 17.69 ? 141 LEU   C O   1 
ATOM   2139 C  CB  . LEU   B 1 135 ? 22.707 -21.131 33.629 1.00 16.51 ? 141 LEU   C CB  1 
ATOM   2140 C  CG  . LEU   B 1 135 ? 24.249 -21.084 33.708 1.00 16.54 ? 141 LEU   C CG  1 
ATOM   2141 C  CD1 . LEU   B 1 135 ? 24.764 -21.089 35.179 1.00 17.61 ? 141 LEU   C CD1 1 
ATOM   2142 C  CD2 . LEU   B 1 135 ? 24.904 -22.249 32.948 1.00 16.94 ? 141 LEU   C CD2 1 
ATOM   2143 N  N   . TRP   B 1 136 ? 20.103 -19.749 32.028 1.00 16.52 ? 142 TRP   C N   1 
ATOM   2144 C  CA  . TRP   B 1 136 ? 18.653 -19.487 32.062 1.00 17.69 ? 142 TRP   C CA  1 
ATOM   2145 C  C   . TRP   B 1 136 ? 17.909 -20.184 30.907 1.00 18.23 ? 142 TRP   C C   1 
ATOM   2146 O  O   . TRP   B 1 136 ? 16.693 -20.339 30.977 1.00 20.15 ? 142 TRP   C O   1 
ATOM   2147 C  CB  . TRP   B 1 136 ? 18.395 -17.979 32.051 1.00 18.02 ? 142 TRP   C CB  1 
ATOM   2148 C  CG  . TRP   B 1 136 ? 19.088 -17.248 30.939 1.00 17.34 ? 142 TRP   C CG  1 
ATOM   2149 C  CD1 . TRP   B 1 136 ? 20.258 -16.562 31.025 1.00 19.18 ? 142 TRP   C CD1 1 
ATOM   2150 C  CD2 . TRP   B 1 136 ? 18.578 -17.015 29.605 1.00 17.58 ? 142 TRP   C CD2 1 
ATOM   2151 N  NE1 . TRP   B 1 136 ? 20.555 -15.971 29.801 1.00 19.06 ? 142 TRP   C NE1 1 
ATOM   2152 C  CE2 . TRP   B 1 136 ? 19.539 -16.250 28.914 1.00 18.67 ? 142 TRP   C CE2 1 
ATOM   2153 C  CE3 . TRP   B 1 136 ? 17.424 -17.421 28.934 1.00 18.30 ? 142 TRP   C CE3 1 
ATOM   2154 C  CZ2 . TRP   B 1 136 ? 19.355 -15.852 27.577 1.00 18.06 ? 142 TRP   C CZ2 1 
ATOM   2155 C  CZ3 . TRP   B 1 136 ? 17.227 -16.996 27.627 1.00 18.67 ? 142 TRP   C CZ3 1 
ATOM   2156 C  CH2 . TRP   B 1 136 ? 18.197 -16.255 26.961 1.00 18.28 ? 142 TRP   C CH2 1 
ATOM   2157 N  N   . LEU   B 1 137 ? 18.617 -20.666 29.868 1.00 17.45 ? 143 LEU   C N   1 
ATOM   2158 C  CA  . LEU   B 1 137 ? 17.940 -21.418 28.798 1.00 17.19 ? 143 LEU   C CA  1 
ATOM   2159 C  C   . LEU   B 1 137 ? 17.319 -22.724 29.365 1.00 19.77 ? 143 LEU   C C   1 
ATOM   2160 O  O   . LEU   B 1 137 ? 16.425 -23.279 28.739 1.00 21.83 ? 143 LEU   C O   1 
ATOM   2161 C  CB  . LEU   B 1 137 ? 18.895 -21.775 27.651 1.00 16.97 ? 143 LEU   C CB  1 
ATOM   2162 C  CG  . LEU   B 1 137 ? 19.336 -20.597 26.783 1.00 16.24 ? 143 LEU   C CG  1 
ATOM   2163 C  CD1 . LEU   B 1 137 ? 20.493 -21.041 25.865 1.00 16.88 ? 143 LEU   C CD1 1 
ATOM   2164 C  CD2 . LEU   B 1 137 ? 18.182 -20.031 25.937 1.00 17.51 ? 143 LEU   C CD2 1 
ATOM   2165 N  N   . ASP   B 1 138 ? 17.841 -23.230 30.505 1.00 18.39 ? 144 ASP   C N   1 
ATOM   2166 C  CA  . ASP   B 1 138 ? 17.374 -24.502 31.091 1.00 20.16 ? 144 ASP   C CA  1 
ATOM   2167 C  C   . ASP   B 1 138 ? 16.116 -24.361 31.958 1.00 23.23 ? 144 ASP   C C   1 
ATOM   2168 O  O   . ASP   B 1 138 ? 15.649 -25.384 32.497 1.00 24.90 ? 144 ASP   C O   1 
ATOM   2169 C  CB  . ASP   B 1 138 ? 18.474 -25.154 31.960 1.00 19.12 ? 144 ASP   C CB  1 
ATOM   2170 C  CG  . ASP   B 1 138 ? 19.724 -25.593 31.190 1.00 20.20 ? 144 ASP   C CG  1 
ATOM   2171 O  OD1 . ASP   B 1 138 ? 19.681 -25.638 29.946 1.00 21.19 ? 144 ASP   C OD1 1 
ATOM   2172 O  OD2 . ASP   B 1 138 ? 20.739 -25.923 31.846 1.00 22.32 ? 144 ASP   C OD2 1 
ATOM   2173 N  N   . GLU   B 1 139 ? 15.575 -23.149 32.112 1.00 23.90 ? 145 GLU   C N   1 
ATOM   2174 C  CA  . GLU   B 1 139 ? 14.417 -22.943 32.996 1.00 27.85 ? 145 GLU   C CA  1 
ATOM   2175 C  C   . GLU   B 1 139 ? 13.409 -21.929 32.437 1.00 32.39 ? 145 GLU   C C   1 
ATOM   2176 O  O   . GLU   B 1 139 ? 13.697 -21.237 31.473 1.00 33.23 ? 145 GLU   C O   1 
ATOM   2177 C  CB  . GLU   B 1 139 ? 14.983 -22.453 34.346 1.00 32.02 ? 145 GLU   C CB  1 
ATOM   2178 C  CG  . GLU   B 1 139 ? 15.608 -21.076 34.247 1.00 39.40 ? 145 GLU   C CG  1 
ATOM   2179 C  CD  . GLU   B 1 139 ? 16.599 -20.691 35.330 1.00 48.43 ? 145 GLU   C CD  1 
ATOM   2180 O  OE1 . GLU   B 1 139 ? 17.014 -19.506 35.360 1.00 49.78 ? 145 GLU   C OE1 1 
ATOM   2181 O  OE2 . GLU   B 1 139 ? 16.953 -21.568 36.150 1.00 50.16 ? 145 GLU   C OE2 1 
ATOM   2182 N  N   . GLU   B 1 140 ? 12.253 -21.772 33.118 1.00 35.25 ? 146 GLU   C N   1 
ATOM   2183 C  CA  . GLU   B 1 140 ? 11.190 -20.778 32.874 1.00 38.31 ? 146 GLU   C CA  1 
ATOM   2184 C  C   . GLU   B 1 140 ? 11.128 -20.185 31.482 1.00 40.75 ? 146 GLU   C C   1 
ATOM   2185 O  O   . GLU   B 1 140 ? 10.627 -19.077 31.305 1.00 41.73 ? 146 GLU   C O   1 
ATOM   2186 C  CB  . GLU   B 1 140 ? 11.272 -19.643 33.919 1.00 41.83 ? 146 GLU   C CB  1 
ATOM   2187 C  CG  . GLU   B 1 140 ? 12.306 -18.554 33.667 1.00 49.19 ? 146 GLU   C CG  1 
ATOM   2188 C  CD  . GLU   B 1 140 ? 11.718 -17.169 33.420 1.00 57.99 ? 146 GLU   C CD  1 
ATOM   2189 O  OE1 . GLU   B 1 140 ? 12.499 -16.190 33.373 1.00 60.41 ? 146 GLU   C OE1 1 
ATOM   2190 O  OE2 . GLU   B 1 140 ? 10.477 -17.064 33.260 1.00 59.17 ? 146 GLU   C OE2 1 
HETATM 2191 N  N1  . A1BP2 C 2 .   ? 10.597 15.590  17.380 1.00 22.70 ? 201 A1BP2 A N1  1 
HETATM 2192 C  C4  . A1BP2 C 2 .   ? 5.485  12.580  25.444 1.00 26.78 ? 201 A1BP2 A C4  1 
HETATM 2193 C  C5  . A1BP2 C 2 .   ? 6.198  13.571  24.791 1.00 27.02 ? 201 A1BP2 A C5  1 
HETATM 2194 C  C6  . A1BP2 C 2 .   ? 7.227  13.247  23.909 1.00 27.28 ? 201 A1BP2 A C6  1 
HETATM 2195 C  C7  . A1BP2 C 2 .   ? 8.117  14.308  23.308 1.00 27.76 ? 201 A1BP2 A C7  1 
HETATM 2196 C  C8  . A1BP2 C 2 .   ? 7.800  14.563  21.847 1.00 26.88 ? 201 A1BP2 A C8  1 
HETATM 2197 C  C10 . A1BP2 C 2 .   ? 9.724  16.478  19.456 1.00 24.96 ? 201 A1BP2 A C10 1 
HETATM 2198 C  C13 . A1BP2 C 2 .   ? 11.908 17.052  20.676 1.00 26.70 ? 201 A1BP2 A C13 1 
HETATM 2199 O  O2  . A1BP2 C 2 .   ? 9.609  17.625  17.382 1.00 26.75 ? 201 A1BP2 A O2  1 
HETATM 2200 C  C11 . A1BP2 C 2 .   ? 9.976  16.609  17.978 1.00 25.39 ? 201 A1BP2 A C11 1 
HETATM 2201 C  C9  . A1BP2 C 2 .   ? 8.522  15.596  19.767 1.00 26.30 ? 201 A1BP2 A C9  1 
HETATM 2202 C  C12 . A1BP2 C 2 .   ? 10.845 15.990  20.401 1.00 26.68 ? 201 A1BP2 A C12 1 
HETATM 2203 C  C14 . A1BP2 C 2 .   ? 10.081 15.570  21.652 1.00 27.25 ? 201 A1BP2 A C14 1 
HETATM 2204 N  N   . A1BP2 C 2 .   ? 8.762  15.178  21.145 1.00 27.11 ? 201 A1BP2 A N   1 
HETATM 2205 O  O1  . A1BP2 C 2 .   ? 6.726  14.270  21.356 1.00 27.41 ? 201 A1BP2 A O1  1 
HETATM 2206 C  C1  . A1BP2 C 2 .   ? 7.488  11.906  23.655 1.00 26.82 ? 201 A1BP2 A C1  1 
HETATM 2207 O  O   . A1BP2 C 2 .   ? 8.421  11.688  22.676 1.00 27.10 ? 201 A1BP2 A O   1 
HETATM 2208 C  C   . A1BP2 C 2 .   ? 9.385  10.652  22.865 1.00 28.04 ? 201 A1BP2 A C   1 
HETATM 2209 C  C3  . A1BP2 C 2 .   ? 5.775  11.259  25.209 1.00 26.01 ? 201 A1BP2 A C3  1 
HETATM 2210 C  C2  . A1BP2 C 2 .   ? 6.770  10.908  24.303 1.00 26.10 ? 201 A1BP2 A C2  1 
HETATM 2211 C  C1  . GOL   D 3 .   ? 14.481 -6.927  26.989 1.00 46.10 ? 202 GOL   A C1  1 
HETATM 2212 O  O1  . GOL   D 3 .   ? 15.268 -5.815  27.420 1.00 46.94 ? 202 GOL   A O1  1 
HETATM 2213 C  C2  . GOL   D 3 .   ? 13.381 -6.446  26.079 1.00 44.75 ? 202 GOL   A C2  1 
HETATM 2214 O  O2  . GOL   D 3 .   ? 13.967 -5.713  25.016 1.00 45.03 ? 202 GOL   A O2  1 
HETATM 2215 C  C3  . GOL   D 3 .   ? 12.532 -7.559  25.517 1.00 43.10 ? 202 GOL   A C3  1 
HETATM 2216 O  O3  . GOL   D 3 .   ? 11.382 -7.015  24.871 1.00 40.90 ? 202 GOL   A O3  1 
HETATM 2217 ZN ZN  . ZN    E 4 .   ? 11.345 -4.227  5.974  1.00 20.54 2 203 ZN    A ZN  1 
HETATM 2218 ZN ZN  . ZN    F 4 .   ? 30.589 -31.228 26.690 1.00 13.45 2 201 ZN    C ZN  1 
HETATM 2219 S  S   . DMS   G 5 .   ? 20.833 -32.435 9.673  1.00 70.74 ? 202 DMS   C S   1 
HETATM 2220 O  O   . DMS   G 5 .   ? 21.634 -32.406 8.409  1.00 70.86 ? 202 DMS   C O   1 
HETATM 2221 C  C1  . DMS   G 5 .   ? 21.927 -32.756 11.070 1.00 70.74 ? 202 DMS   C C1  1 
HETATM 2222 C  C2  . DMS   G 5 .   ? 20.500 -30.707 10.113 1.00 70.57 ? 202 DMS   C C2  1 
HETATM 2223 O  O   . HOH   H 6 .   ? 11.232 8.661   4.223  1.00 23.47 ? 301 HOH   A O   1 
HETATM 2224 O  O   . HOH   H 6 .   ? 8.490  -2.903  31.742 1.00 24.51 ? 302 HOH   A O   1 
HETATM 2225 O  O   . HOH   H 6 .   ? 7.339  20.562  17.114 1.00 31.10 ? 303 HOH   A O   1 
HETATM 2226 O  O   . HOH   H 6 .   ? 2.023  23.159  21.190 1.00 38.49 ? 304 HOH   A O   1 
HETATM 2227 O  O   . HOH   H 6 .   ? 37.351 14.984  13.596 1.00 67.85 ? 305 HOH   A O   1 
HETATM 2228 O  O   . HOH   H 6 .   ? 8.287  8.429   22.303 1.00 29.79 ? 306 HOH   A O   1 
HETATM 2229 O  O   . HOH   H 6 .   ? 35.329 -3.882  7.897  1.00 22.93 ? 307 HOH   A O   1 
HETATM 2230 O  O   . HOH   H 6 .   ? 14.040 2.925   1.194  1.00 27.57 ? 308 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 6 .   ? 35.465 7.958   9.826  1.00 46.60 ? 309 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 6 .   ? 0.381  -0.916  19.433 1.00 27.06 ? 310 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 6 .   ? 14.071 17.301  4.210  1.00 38.57 ? 311 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 6 .   ? 23.073 13.335  23.757 1.00 42.76 ? 312 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 6 .   ? 4.540  14.923  20.180 1.00 57.36 ? 313 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 6 .   ? 9.918  -8.824  23.787 1.00 31.70 ? 314 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 6 .   ? 8.639  -6.419  9.857  1.00 33.20 ? 315 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 6 .   ? 2.596  -2.843  20.648 1.00 31.38 ? 316 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 6 .   ? 29.345 22.348  19.377 1.00 27.92 ? 317 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 6 .   ? 9.170  2.459   2.647  1.00 29.53 ? 318 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 6 .   ? 6.474  2.412   2.923  1.00 31.66 ? 319 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 6 .   ? 2.958  9.498   8.819  1.00 30.16 ? 320 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 6 .   ? 9.560  21.911  9.775  1.00 41.60 ? 321 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 6 .   ? 27.710 8.104   1.580  1.00 37.48 ? 322 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 6 .   ? 30.376 10.576  15.687 1.00 29.39 ? 323 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 6 .   ? 19.224 10.143  19.641 1.00 14.59 ? 324 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 6 .   ? 12.278 22.268  12.178 1.00 40.69 ? 325 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 6 .   ? 33.807 14.147  9.710  1.00 31.45 ? 326 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 6 .   ? 17.331 1.063   28.301 1.00 24.24 ? 327 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 6 .   ? 22.594 0.910   17.470 1.00 17.70 ? 328 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 6 .   ? 12.804 -5.728  30.563 1.00 35.69 ? 329 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 6 .   ? 28.100 3.015   5.085  1.00 32.13 ? 330 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 6 .   ? 4.746  -3.751  28.930 1.00 26.59 ? 331 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 6 .   ? 8.435  24.908  23.902 1.00 32.11 ? 332 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 6 .   ? 23.459 21.651  7.182  1.00 26.15 ? 333 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 6 .   ? 24.820 5.240   21.554 1.00 31.08 ? 334 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 6 .   ? 21.554 5.172   24.779 1.00 42.22 ? 335 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 6 .   ? 18.987 16.865  26.390 1.00 47.66 ? 336 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 6 .   ? 21.820 2.387   -0.808 1.00 32.64 ? 337 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 6 .   ? 31.875 6.974   5.610  1.00 30.14 ? 338 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 6 .   ? 33.547 11.126  15.665 1.00 34.47 ? 339 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 6 .   ? 15.080 11.299  0.036  1.00 29.27 ? 340 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 6 .   ? 5.774  17.292  21.245 1.00 59.87 ? 341 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 6 .   ? 11.263 12.652  11.005 1.00 17.33 ? 342 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 6 .   ? -0.174 1.270   15.772 1.00 14.31 ? 343 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 6 .   ? 16.529 3.924   23.678 1.00 18.14 ? 344 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 6 .   ? 17.044 -3.369  27.765 1.00 34.24 ? 345 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 6 .   ? 3.761  9.294   27.935 1.00 31.58 ? 346 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 6 .   ? 13.619 4.082   23.503 1.00 13.39 ? 347 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 6 .   ? 20.982 -4.137  14.249 1.00 17.54 ? 348 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 6 .   ? 5.297  5.319   32.665 1.00 21.79 ? 349 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 6 .   ? 13.778 13.861  23.916 1.00 20.35 ? 350 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 6 .   ? 18.372 21.854  9.399  1.00 19.88 ? 351 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 6 .   ? 3.761  12.847  18.027 1.00 38.04 ? 352 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 6 .   ? 20.704 -0.941  3.125  1.00 32.30 ? 353 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 6 .   ? 31.528 19.986  11.724 1.00 23.25 ? 354 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 6 .   ? 1.235  5.092   27.066 1.00 29.77 ? 355 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 6 .   ? 29.733 11.696  18.608 1.00 29.63 ? 356 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 6 .   ? 29.263 12.033  21.348 1.00 36.37 ? 357 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 6 .   ? 35.291 10.943  12.221 1.00 48.47 ? 358 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 6 .   ? 20.822 -2.564  16.942 1.00 16.06 ? 359 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 6 .   ? 10.242 10.129  31.378 1.00 23.53 ? 360 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 6 .   ? 32.683 16.639  9.246  1.00 32.80 ? 361 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 6 .   ? 0.724  -0.910  9.172  1.00 33.40 ? 362 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 6 .   ? 6.638  -6.953  23.822 1.00 24.34 ? 363 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 6 .   ? 26.994 -1.235  9.018  1.00 26.12 ? 364 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 6 .   ? 3.593  -8.137  10.235 1.00 44.69 ? 365 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 6 .   ? 17.502 20.030  16.887 1.00 17.49 ? 366 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 6 .   ? 23.317 -6.450  12.043 1.00 32.88 ? 367 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 6 .   ? 28.898 3.424   12.836 1.00 17.55 ? 368 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 6 .   ? 11.886 11.135  29.659 1.00 23.49 ? 369 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 6 .   ? 13.191 11.381  9.147  1.00 15.20 ? 370 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 6 .   ? 4.028  0.073   24.057 1.00 20.77 ? 371 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 6 .   ? 9.445  4.033   33.488 1.00 14.23 ? 372 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 6 .   ? 11.535 17.955  4.728  1.00 35.47 ? 373 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 6 .   ? 27.281 -1.253  15.977 1.00 28.50 ? 374 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 6 .   ? 30.506 3.111   14.988 1.00 23.26 ? 375 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 6 .   ? 19.674 20.313  5.671  1.00 50.50 ? 376 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 6 .   ? 30.339 4.548   5.907  1.00 21.81 ? 377 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 6 .   ? 22.918 -0.633  5.447  1.00 22.59 ? 378 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 6 .   ? 2.513  16.289  19.116 1.00 38.09 ? 379 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 6 .   ? 28.941 15.855  4.387  1.00 27.90 ? 380 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 6 .   ? 18.013 17.673  4.167  1.00 34.07 ? 381 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 6 .   ? 19.333 3.050   19.418 1.00 19.93 ? 382 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 6 .   ? 30.067 -1.386  8.785  1.00 31.43 ? 383 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 6 .   ? 1.807  11.262  27.338 1.00 39.08 ? 384 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 6 .   ? 0.172  5.955   6.071  1.00 28.99 ? 385 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 6 .   ? 16.821 6.440   27.125 1.00 27.76 ? 386 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 6 .   ? 23.416 11.726  21.966 1.00 33.83 ? 387 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 6 .   ? 17.671 24.309  10.262 1.00 38.92 ? 388 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 6 .   ? 36.439 18.128  14.587 1.00 30.63 ? 389 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 6 .   ? 30.714 15.768  22.839 1.00 28.66 ? 390 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 6 .   ? 4.042  -4.123  6.008  1.00 29.07 ? 391 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 6 .   ? 35.865 15.279  11.084 1.00 41.13 ? 392 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 6 .   ? 14.456 -2.400  17.986 1.00 18.33 ? 393 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 6 .   ? 36.226 -0.315  12.847 1.00 31.95 ? 394 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 6 .   ? 8.086  6.555   33.802 1.00 18.69 ? 395 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 6 .   ? 3.045  7.667   24.463 1.00 23.54 ? 396 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 6 .   ? 15.091 14.992  3.250  1.00 31.42 ? 397 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 6 .   ? 27.858 17.682  24.167 1.00 24.27 ? 398 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 6 .   ? 17.434 10.863  26.100 1.00 22.94 ? 399 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 6 .   ? 16.313 9.402   -1.631 1.00 21.97 ? 400 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 6 .   ? 8.500  19.493  19.339 1.00 29.79 ? 401 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 6 .   ? 31.972 8.802   7.700  1.00 23.79 ? 402 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 6 .   ? 16.493 21.312  19.054 1.00 27.72 ? 403 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 6 .   ? 33.929 18.692  10.781 1.00 28.76 ? 404 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 6 .   ? 25.166 17.958  4.660  1.00 32.50 ? 405 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 6 .   ? 35.575 12.055  17.532 1.00 44.82 ? 406 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 6 .   ? 25.418 19.742  21.678 1.00 27.24 ? 407 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 6 .   ? 17.479 0.930   20.287 1.00 21.03 ? 408 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 6 .   ? 19.805 13.216  2.131  1.00 31.19 ? 409 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 6 .   ? 7.247  13.642  4.633  1.00 23.97 ? 410 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 6 .   ? 22.457 19.653  19.709 1.00 31.40 ? 411 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 6 .   ? 36.365 16.157  16.915 1.00 37.02 ? 412 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 6 .   ? 5.989  -3.723  31.519 1.00 26.50 ? 413 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 6 .   ? 16.999 -4.036  3.024  1.00 25.59 ? 414 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 6 .   ? 17.154 -2.487  19.653 1.00 23.47 ? 415 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 6 .   ? 32.175 2.029   6.024  1.00 38.14 ? 416 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 6 .   ? 0.577  -1.108  16.744 1.00 21.57 ? 417 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 6 .   ? 19.193 -0.387  32.953 1.00 37.95 ? 418 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 6 .   ? 23.224 19.114  6.299  1.00 20.62 ? 419 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 6 .   ? 22.620 3.531   20.929 1.00 21.99 ? 420 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 6 .   ? 20.894 10.011  21.918 1.00 17.88 ? 421 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 6 .   ? 16.956 -5.581  12.242 1.00 29.43 ? 422 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 6 .   ? 3.342  -0.344  21.371 1.00 29.93 ? 423 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 6 .   ? 23.243 8.430   21.733 1.00 24.80 ? 424 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 6 .   ? 10.447 4.913   3.292  1.00 27.98 ? 425 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 6 .   ? 33.854 5.338   16.887 1.00 31.22 ? 426 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 6 .   ? -1.381 -2.978  15.558 1.00 32.63 ? 427 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 6 .   ? 21.054 -4.801  11.577 1.00 35.85 ? 428 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 6 .   ? 2.086  14.510  16.769 1.00 39.01 ? 429 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 6 .   ? 0.926  7.685   27.460 1.00 34.97 ? 430 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 6 .   ? 33.980 7.912   16.784 1.00 35.62 ? 431 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 6 .   ? 1.189  -5.022  17.405 1.00 38.98 ? 432 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 6 .   ? 11.927 15.779  24.839 1.00 42.65 ? 433 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 6 .   ? 31.618 9.302   17.668 1.00 42.33 ? 434 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 6 .   ? 2.104  -5.370  14.594 1.00 46.30 ? 435 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 6 .   ? 19.030 -3.324  33.892 1.00 39.60 ? 436 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 6 .   ? 11.880 10.645  0.047  1.00 36.05 ? 437 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 6 .   ? 33.363 -4.101  5.958  1.00 45.28 ? 438 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 6 .   ? 21.579 19.637  4.178  1.00 37.30 ? 439 HOH   A O   1 
HETATM 2362 O  O   . HOH   H 6 .   ? 16.653 -4.974  34.294 1.00 31.04 ? 440 HOH   A O   1 
HETATM 2363 O  O   . HOH   H 6 .   ? 15.622 13.356  26.027 1.00 33.53 ? 441 HOH   A O   1 
HETATM 2364 O  O   . HOH   H 6 .   ? 2.603  -0.405  26.475 1.00 34.07 ? 442 HOH   A O   1 
HETATM 2365 O  O   . HOH   H 6 .   ? 18.442 2.258   22.824 1.00 38.44 ? 443 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 6 .   ? 29.675 0.862   16.743 1.00 37.10 ? 444 HOH   A O   1 
HETATM 2367 O  O   . HOH   H 6 .   ? 23.659 1.129   19.969 1.00 32.84 ? 445 HOH   A O   1 
HETATM 2368 O  O   . HOH   H 6 .   ? 0.095  -0.023  23.055 1.00 29.57 ? 446 HOH   A O   1 
HETATM 2369 O  O   . HOH   H 6 .   ? 13.507 25.020  15.457 1.00 44.61 ? 447 HOH   A O   1 
HETATM 2370 O  O   . HOH   H 6 .   ? 30.179 7.146   17.901 1.00 34.27 ? 448 HOH   A O   1 
HETATM 2371 O  O   . HOH   H 6 .   ? 21.177 11.499  24.426 1.00 34.25 ? 449 HOH   A O   1 
HETATM 2372 O  O   . HOH   H 6 .   ? 21.166 3.063   23.253 1.00 33.22 ? 450 HOH   A O   1 
HETATM 2373 O  O   . HOH   H 6 .   ? 12.219 -4.960  33.136 1.00 30.04 ? 451 HOH   A O   1 
HETATM 2374 O  O   . HOH   H 6 .   ? 21.165 -0.954  19.060 1.00 32.70 ? 452 HOH   A O   1 
HETATM 2375 O  O   . HOH   H 6 .   ? 37.700 -4.579  6.722  1.00 32.17 ? 453 HOH   A O   1 
HETATM 2376 O  O   . HOH   H 6 .   ? 31.206 4.690   17.211 1.00 26.44 ? 454 HOH   A O   1 
HETATM 2377 O  O   . HOH   H 6 .   ? 2.470  -1.747  22.676 1.00 27.73 ? 455 HOH   A O   1 
HETATM 2378 O  O   . HOH   H 6 .   ? 39.277 -2.637  10.768 1.00 38.19 ? 456 HOH   A O   1 
HETATM 2379 O  O   . HOH   H 6 .   ? 3.963  -6.683  23.365 1.00 39.22 ? 457 HOH   A O   1 
HETATM 2380 O  O   . HOH   H 6 .   ? 28.774 1.399   19.185 1.00 53.20 ? 458 HOH   A O   1 
HETATM 2381 O  O   . HOH   H 6 .   ? 26.331 0.425   20.014 1.00 50.70 ? 459 HOH   A O   1 
HETATM 2382 O  O   . HOH   I 6 .   ? 17.529 -33.390 23.918 1.00 40.60 ? 301 HOH   C O   1 
HETATM 2383 O  O   . HOH   I 6 .   ? 38.245 -7.403  7.004  1.00 21.91 ? 302 HOH   C O   1 
HETATM 2384 O  O   . HOH   I 6 .   ? 38.768 -18.775 21.595 1.00 28.15 ? 303 HOH   C O   1 
HETATM 2385 O  O   . HOH   I 6 .   ? 18.902 -32.281 19.751 1.00 40.99 ? 304 HOH   C O   1 
HETATM 2386 O  O   . HOH   I 6 .   ? 19.745 -4.187  20.206 1.00 23.61 ? 305 HOH   C O   1 
HETATM 2387 O  O   . HOH   I 6 .   ? 22.917 -6.008  21.059 1.00 21.58 ? 306 HOH   C O   1 
HETATM 2388 O  O   . HOH   I 6 .   ? 30.781 -18.237 26.876 1.00 18.70 ? 307 HOH   C O   1 
HETATM 2389 O  O   . HOH   I 6 .   ? 16.840 -9.505  27.596 1.00 41.13 ? 308 HOH   C O   1 
HETATM 2390 O  O   . HOH   I 6 .   ? 36.133 -26.372 34.233 1.00 29.60 ? 309 HOH   C O   1 
HETATM 2391 O  O   . HOH   I 6 .   ? 31.019 -23.930 -1.352 1.00 22.36 ? 310 HOH   C O   1 
HETATM 2392 O  O   . HOH   I 6 .   ? 20.726 -18.803 12.815 1.00 16.22 ? 311 HOH   C O   1 
HETATM 2393 O  O   . HOH   I 6 .   ? 21.653 -26.156 34.328 1.00 27.25 ? 312 HOH   C O   1 
HETATM 2394 O  O   . HOH   I 6 .   ? 16.418 -17.193 11.009 1.00 43.05 ? 313 HOH   C O   1 
HETATM 2395 O  O   . HOH   I 6 .   ? 17.850 -6.099  24.066 1.00 25.92 ? 314 HOH   C O   1 
HETATM 2396 O  O   . HOH   I 6 .   ? 36.263 -2.469  11.173 1.00 29.89 ? 315 HOH   C O   1 
HETATM 2397 O  O   . HOH   I 6 .   ? 28.221 -5.348  18.494 1.00 39.35 ? 316 HOH   C O   1 
HETATM 2398 O  O   . HOH   I 6 .   ? 17.866 -27.564 16.487 1.00 18.81 ? 317 HOH   C O   1 
HETATM 2399 O  O   . HOH   I 6 .   ? 18.645 -8.877  13.825 1.00 28.50 ? 318 HOH   C O   1 
HETATM 2400 O  O   . HOH   I 6 .   ? 36.130 -17.590 11.620 1.00 30.88 ? 319 HOH   C O   1 
HETATM 2401 O  O   . HOH   I 6 .   ? 10.246 -17.613 18.308 1.00 28.35 ? 320 HOH   C O   1 
HETATM 2402 O  O   . HOH   I 6 .   ? 14.755 -23.900 12.260 1.00 36.06 ? 321 HOH   C O   1 
HETATM 2403 O  O   . HOH   I 6 .   ? 10.430 -16.946 15.204 1.00 34.04 ? 322 HOH   C O   1 
HETATM 2404 O  O   . HOH   I 6 .   ? 42.589 -11.438 11.050 1.00 31.20 ? 323 HOH   C O   1 
HETATM 2405 O  O   . HOH   I 6 .   ? 37.320 -31.972 10.936 1.00 22.79 ? 324 HOH   C O   1 
HETATM 2406 O  O   . HOH   I 6 .   ? 34.987 -32.836 3.262  1.00 37.26 ? 325 HOH   C O   1 
HETATM 2407 O  O   . HOH   I 6 .   ? 5.807  -16.437 22.691 1.00 58.16 ? 326 HOH   C O   1 
HETATM 2408 O  O   . HOH   I 6 .   ? 37.308 -18.834 28.132 1.00 24.66 ? 327 HOH   C O   1 
HETATM 2409 O  O   . HOH   I 6 .   ? 26.495 -15.299 30.744 1.00 31.10 ? 328 HOH   C O   1 
HETATM 2410 O  O   . HOH   I 6 .   ? 39.993 -29.699 11.909 1.00 26.20 ? 329 HOH   C O   1 
HETATM 2411 O  O   . HOH   I 6 .   ? 23.954 -8.098  9.549  1.00 24.38 ? 330 HOH   C O   1 
HETATM 2412 O  O   . HOH   I 6 .   ? 30.991 -21.582 28.380 1.00 17.13 ? 331 HOH   C O   1 
HETATM 2413 O  O   . HOH   I 6 .   ? 24.862 -15.763 7.309  1.00 20.85 ? 332 HOH   C O   1 
HETATM 2414 O  O   . HOH   I 6 .   ? 26.584 -5.464  10.132 1.00 23.69 ? 333 HOH   C O   1 
HETATM 2415 O  O   . HOH   I 6 .   ? 40.459 -27.391 15.138 1.00 13.96 ? 334 HOH   C O   1 
HETATM 2416 O  O   . HOH   I 6 .   ? 25.997 -25.345 8.758  1.00 14.37 ? 335 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 6 .   ? 40.390 -25.378 7.084  1.00 39.07 ? 336 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 6 .   ? 6.957  -9.328  22.651 1.00 33.12 ? 337 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 6 .   ? 31.144 -6.110  5.765  1.00 39.04 ? 338 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 6 .   ? 32.477 -23.763 29.094 1.00 16.83 ? 339 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 6 .   ? 13.266 -11.211 28.431 1.00 39.41 ? 340 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 6 .   ? 10.664 -16.914 12.543 1.00 37.20 ? 341 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 6 .   ? 17.527 -24.158 8.538  1.00 42.44 ? 342 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 6 .   ? 21.989 -28.747 4.771  1.00 28.45 ? 343 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 6 .   ? 35.164 -13.182 8.727  1.00 20.49 ? 344 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 6 .   ? 29.889 -15.314 19.550 1.00 16.72 ? 345 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 6 .   ? 20.750 -25.713 13.814 1.00 24.59 ? 346 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 6 .   ? 37.194 -10.411 4.871  1.00 41.43 ? 347 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 6 .   ? 11.919 -24.283 21.697 1.00 18.13 ? 348 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 6 .   ? 9.086  -7.840  21.098 1.00 30.17 ? 349 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 6 .   ? 25.747 -37.870 24.287 1.00 31.64 ? 350 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 6 .   ? 14.564 -28.796 25.487 1.00 37.70 ? 351 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 6 .   ? 13.900 -24.400 29.293 1.00 33.37 ? 352 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 6 .   ? 30.173 -10.654 27.744 1.00 39.21 ? 353 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 6 .   ? 19.130 -27.726 28.128 1.00 19.74 ? 354 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 6 .   ? 31.991 -10.487 13.784 1.00 21.01 ? 355 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 6 .   ? 11.140 -21.783 13.572 1.00 47.49 ? 356 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 6 .   ? 4.328  -10.378 19.633 1.00 31.50 ? 357 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 6 .   ? 27.022 -35.651 20.778 1.00 26.85 ? 358 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 6 .   ? 36.287 -21.385 6.840  1.00 25.57 ? 359 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 6 .   ? 22.909 -8.560  14.044 1.00 17.30 ? 360 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 6 .   ? 23.509 -33.668 29.015 1.00 29.95 ? 361 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 6 .   ? 30.017 -15.961 30.419 1.00 33.29 ? 362 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 6 .   ? 37.623 -31.556 25.722 1.00 27.33 ? 363 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 6 .   ? 29.745 -13.118 12.955 1.00 17.23 ? 364 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 6 .   ? 23.792 -3.433  19.073 1.00 35.99 ? 365 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 6 .   ? 6.924  -17.108 18.692 1.00 41.64 ? 366 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 6 .   ? 34.713 -35.072 18.102 1.00 27.23 ? 367 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 6 .   ? 22.940 -28.244 12.593 1.00 21.94 ? 368 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 6 .   ? 22.299 -23.785 6.094  1.00 39.39 ? 369 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 6 .   ? 28.881 -36.362 7.859  1.00 20.82 ? 370 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 6 .   ? 13.089 -29.621 19.040 1.00 42.08 ? 371 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 6 .   ? 23.140 -25.498 8.935  1.00 20.56 ? 372 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 6 .   ? 32.965 -9.846  11.142 1.00 16.46 ? 373 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 6 .   ? 26.755 -12.144 27.547 1.00 27.05 ? 374 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 6 .   ? 8.809  -13.346 10.785 1.00 28.07 ? 375 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 6 .   ? 10.038 -24.872 19.813 1.00 22.92 ? 376 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 6 .   ? 22.480 -13.791 29.682 1.00 36.80 ? 377 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 6 .   ? 26.673 -6.114  22.027 1.00 29.56 ? 378 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 6 .   ? 34.370 -13.562 25.460 1.00 21.20 ? 379 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 6 .   ? 30.246 -18.199 8.386  1.00 25.44 ? 380 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 6 .   ? 31.252 -12.205 10.687 1.00 16.64 ? 381 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 6 .   ? 28.152 -16.412 22.028 1.00 15.00 ? 382 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 6 .   ? 35.582 -24.809 24.666 1.00 18.79 ? 383 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 6 .   ? 36.855 -29.358 10.078 1.00 21.18 ? 384 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 6 .   ? 33.657 -33.897 24.059 1.00 41.32 ? 385 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 6 .   ? 26.286 -31.296 14.827 1.00 21.18 ? 386 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 6 .   ? 21.658 -18.963 5.933  1.00 30.76 ? 387 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 6 .   ? 11.596 -22.605 28.692 1.00 28.33 ? 388 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 6 .   ? 22.853 -33.525 5.466  1.00 33.12 ? 389 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 6 .   ? 43.255 -25.902 23.564 1.00 23.41 ? 390 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 6 .   ? 10.290 -31.011 25.103 1.00 36.26 ? 391 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 6 .   ? 3.871  -8.332  14.721 1.00 29.42 ? 392 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 6 .   ? 33.002 -30.437 31.627 1.00 19.38 ? 393 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 6 .   ? 31.561 -13.439 4.334  1.00 33.60 ? 394 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 6 .   ? 26.001 -31.108 30.826 1.00 18.39 ? 395 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 6 .   ? 38.861 -13.119 25.776 1.00 25.84 ? 396 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 6 .   ? 35.122 -4.276  17.676 1.00 31.80 ? 397 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 6 .   ? 38.747 -14.762 13.492 1.00 32.85 ? 398 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 6 .   ? 20.373 -23.683 34.846 1.00 27.73 ? 399 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 6 .   ? 41.718 -12.578 17.955 1.00 26.16 ? 400 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 6 .   ? 35.204 -13.702 6.136  1.00 37.20 ? 401 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 6 .   ? 35.700 -28.686 7.730  1.00 18.92 ? 402 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 6 .   ? 17.186 -25.348 12.724 1.00 26.57 ? 403 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 6 .   ? 42.202 -12.158 13.849 1.00 37.36 ? 404 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 6 .   ? 15.187 -29.955 18.023 1.00 38.13 ? 405 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 6 .   ? 33.621 -36.134 8.771  1.00 38.97 ? 406 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 6 .   ? 32.154 -34.698 31.709 1.00 36.26 ? 407 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 6 .   ? 16.427 -20.538 11.583 1.00 26.23 ? 408 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 6 .   ? 6.474  -18.748 25.426 1.00 46.98 ? 409 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 6 .   ? 39.968 -30.076 14.598 1.00 17.47 ? 410 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 6 .   ? 18.635 -8.365  25.558 1.00 21.32 ? 411 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 6 .   ? 20.354 -32.272 22.234 1.00 32.52 ? 412 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 6 .   ? 32.771 -14.390 9.401  1.00 16.62 ? 413 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 6 .   ? 18.749 -19.148 10.845 1.00 20.83 ? 414 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 6 .   ? 34.650 -23.204 -0.939 1.00 37.48 ? 415 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 6 .   ? 23.403 -17.616 33.220 1.00 24.27 ? 416 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 6 .   ? 36.525 -24.868 27.196 1.00 30.80 ? 417 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 6 .   ? 34.073 -15.700 27.136 1.00 33.50 ? 418 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 6 .   ? 6.440  -20.027 18.207 1.00 34.51 ? 419 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 6 .   ? 6.594  -23.057 18.215 1.00 36.01 ? 420 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 6 .   ? 23.337 -30.968 13.366 1.00 33.79 ? 421 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 6 .   ? 43.441 -25.668 26.062 1.00 35.97 ? 422 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 6 .   ? 31.513 -15.746 7.119  1.00 32.43 ? 423 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 6 .   ? 37.547 -14.063 9.871  1.00 31.98 ? 424 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 6 .   ? 34.239 -31.932 29.510 1.00 24.05 ? 425 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 6 .   ? 20.389 -19.605 36.001 1.00 36.88 ? 426 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 6 .   ? 26.189 -35.474 7.421  1.00 27.00 ? 427 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 6 .   ? 23.830 -15.757 31.479 1.00 32.10 ? 428 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 6 .   ? 21.228 -17.464 34.517 1.00 27.99 ? 429 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 6 .   ? 21.455 -26.934 10.277 1.00 35.06 ? 430 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 6 .   ? 22.786 -16.857 5.447  1.00 42.26 ? 431 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 6 .   ? 28.526 -12.798 30.372 1.00 45.68 ? 432 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 6 .   ? 16.462 -27.611 14.142 1.00 35.21 ? 433 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 6 .   ? 18.643 -26.104 10.399 1.00 42.10 ? 434 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 6 .   ? 32.537 -19.415 28.990 1.00 27.69 ? 435 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 6 .   ? 40.358 -28.220 7.431  1.00 43.70 ? 436 HOH   C O   1 
HETATM 2518 O  O   . HOH   I 6 .   ? 5.485  -10.291 9.469  1.00 50.65 ? 437 HOH   C O   1 
HETATM 2519 O  O   . HOH   I 6 .   ? 18.408 -2.325  23.435 1.00 41.59 ? 438 HOH   C O   1 
HETATM 2520 O  O   . HOH   I 6 .   ? 10.126 -21.309 16.380 1.00 34.91 ? 439 HOH   C O   1 
HETATM 2521 O  O   . HOH   I 6 .   ? 18.105 -17.977 8.396  1.00 36.82 ? 440 HOH   C O   1 
HETATM 2522 O  O   . HOH   I 6 .   ? 18.105 -16.505 38.219 1.00 31.64 ? 441 HOH   C O   1 
HETATM 2523 O  O   . HOH   I 6 .   ? 16.855 -28.876 28.750 1.00 38.41 ? 442 HOH   C O   1 
HETATM 2524 O  O   . HOH   I 6 .   ? 9.103  -23.418 17.715 1.00 35.02 ? 443 HOH   C O   1 
HETATM 2525 O  O   . HOH   I 6 .   ? 35.191 -23.163 28.937 1.00 25.39 ? 444 HOH   C O   1 
HETATM 2526 O  O   . HOH   I 6 .   ? 35.443 -20.510 29.444 1.00 37.32 ? 445 HOH   C O   1 
HETATM 2527 O  O   . HOH   I 6 .   ? 11.282 -28.008 17.578 1.00 53.28 ? 446 HOH   C O   1 
HETATM 2528 O  O   . HOH   I 6 .   ? 3.093  -8.619  21.876 1.00 49.58 ? 447 HOH   C O   1 
HETATM 2529 O  O   . HOH   I 6 .   ? 19.244 -17.587 5.877  1.00 40.50 ? 448 HOH   C O   1 
HETATM 2530 O  O   . HOH   I 6 .   ? 3.279  -9.568  17.031 1.00 38.76 ? 449 HOH   C O   1 
HETATM 2531 O  O   . HOH   I 6 .   ? 19.798 -15.180 34.654 1.00 35.91 ? 450 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   ? 0.2386 0.2157 0.2074 -0.0155 -0.0012 -0.0139 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2408 0.2203 0.2149 -0.0144 -0.0049 -0.0112 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2252 0.2077 0.2070 -0.0083 -0.0085 -0.0055 7   SER   A C   
4    O O   . SER   A 1   ? 0.2310 0.2146 0.2128 -0.0065 -0.0092 -0.0032 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2745 0.2605 0.2431 -0.0222 -0.0089 -0.0104 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3166 0.3103 0.2840 -0.0238 -0.0138 -0.0046 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2107 0.1943 0.1988 -0.0060 -0.0102 -0.0037 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1915 0.1773 0.1871 -0.0014 -0.0122 0.0006  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1810 0.1652 0.1825 0.0019  -0.0108 -0.0002 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2032 0.1838 0.2038 0.0020  -0.0080 -0.0031 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1642 0.1509 0.1724 0.0042  -0.0122 0.0027  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1756 0.1619 0.1888 0.0062  -0.0108 0.0019  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1708 0.1575 0.1896 0.0088  -0.0095 0.0031  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1754 0.1624 0.1960 0.0094  -0.0098 0.0053  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1939 0.1833 0.2097 0.0042  -0.0129 0.0029  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1506 0.1370 0.1717 0.0097  -0.0072 0.0014  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1408 0.1276 0.1671 0.0106  -0.0046 0.0010  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1516 0.1405 0.1846 0.0109  -0.0046 0.0018  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1530 0.1433 0.1852 0.0100  -0.0056 0.0013  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1503 0.1376 0.1739 0.0096  -0.0019 -0.0015 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1673 0.1542 0.1852 0.0093  -0.0021 -0.0014 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1697 0.1567 0.1970 0.0087  0.0020  -0.0036 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1800 0.1708 0.1963 0.0077  -0.0006 -0.0016 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1500 0.1393 0.1911 0.0123  -0.0030 0.0036  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1588 0.1510 0.2085 0.0131  -0.0022 0.0051  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1683 0.1582 0.2231 0.0134  0.0041  0.0017  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1677 0.1547 0.2289 0.0148  0.0078  0.0022  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1703 0.1661 0.2280 0.0146  -0.0049 0.0115  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1677 0.1674 0.2191 0.0121  -0.0108 0.0140  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1666 0.1702 0.2171 0.0098  -0.0134 0.0141  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1839 0.1829 0.2291 0.0110  -0.0131 0.0154  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1829 0.1891 0.2259 0.0058  -0.0176 0.0148  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1967 0.1990 0.2346 0.0071  -0.0174 0.0163  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1989 0.2042 0.2351 0.0043  -0.0192 0.0153  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2278 0.2356 0.2557 -0.0011 -0.0222 0.0148  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1647 0.1556 0.2165 0.0113  0.0061  -0.0021 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1689 0.1586 0.2229 0.0094  0.0126  -0.0067 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1779 0.1709 0.2373 0.0091  0.0139  -0.0070 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1717 0.1681 0.2275 0.0083  0.0101  -0.0059 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1842 0.1745 0.2276 0.0053  0.0135  -0.0104 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2004 0.1945 0.2374 0.0045  0.0086  -0.0084 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2065 0.1971 0.2502 0.0010  0.0204  -0.0159 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1867 0.1786 0.2564 0.0100  0.0199  -0.0083 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1853 0.1808 0.2614 0.0098  0.0221  -0.0087 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1792 0.1796 0.2586 0.0120  0.0153  -0.0027 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1744 0.1755 0.2578 0.0147  0.0116  0.0025  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1682 0.1724 0.2440 0.0098  0.0132  -0.0034 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1671 0.1755 0.2437 0.0103  0.0070  0.0012  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1648 0.1716 0.2292 0.0081  0.0023  0.0006  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1703 0.1794 0.2330 0.0065  -0.0008 0.0017  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1832 0.1967 0.2671 0.0097  0.0083  0.0018  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2148 0.2312 0.3145 0.0129  0.0120  0.0050  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2429 0.2648 0.3507 0.0147  0.0082  0.0116  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2176 0.2311 0.3227 0.0134  0.0201  0.0009  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1562 0.1590 0.2138 0.0083  0.0020  -0.0006 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1531 0.1540 0.2015 0.0071  -0.0012 -0.0007 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1543 0.1528 0.1998 0.0082  -0.0039 0.0009  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1613 0.1586 0.2094 0.0098  -0.0027 0.0015  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1637 0.1639 0.2065 0.0055  0.0014  -0.0031 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1794 0.1832 0.2231 0.0029  0.0040  -0.0044 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1933 0.1991 0.2373 0.0019  0.0023  -0.0029 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1988 0.2043 0.2423 0.0005  0.0086  -0.0077 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1972 0.2072 0.2417 -0.0010 0.0045  -0.0036 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2038 0.2138 0.2466 -0.0032 0.0112  -0.0091 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2136 0.2262 0.2571 -0.0037 0.0088  -0.0066 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2680 0.2860 0.3108 -0.0078 0.0112  -0.0075 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1451 0.1421 0.1848 0.0069  -0.0067 0.0013  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1510 0.1456 0.1856 0.0068  -0.0087 0.0017  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1541 0.1449 0.1827 0.0066  -0.0073 -0.0001 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1570 0.1466 0.1848 0.0054  -0.0068 -0.0005 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1511 0.1481 0.1848 0.0041  -0.0122 0.0033  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1736 0.1680 0.1997 0.0019  -0.0134 0.0024  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1754 0.1744 0.1997 -0.0029 -0.0169 0.0039  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1941 0.1887 0.2093 -0.0073 -0.0159 -0.0001 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2241 0.2181 0.2328 -0.0098 -0.0163 -0.0009 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2222 0.2198 0.2324 -0.0080 -0.0185 0.0028  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2164 0.2055 0.2175 -0.0143 -0.0137 -0.0057 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1460 0.1352 0.1718 0.0078  -0.0063 -0.0004 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1397 0.1270 0.1622 0.0081  -0.0047 -0.0005 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1573 0.1411 0.1755 0.0079  -0.0051 -0.0012 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1618 0.1459 0.1783 0.0081  -0.0061 -0.0011 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1452 0.1350 0.1673 0.0085  -0.0031 -0.0002 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1565 0.1472 0.1776 0.0089  -0.0020 0.0018  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1634 0.1567 0.1884 0.0072  -0.0018 -0.0010 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1477 0.1280 0.1645 0.0071  -0.0035 -0.0021 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1543 0.1306 0.1666 0.0059  -0.0023 -0.0040 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1798 0.1562 0.1921 0.0058  -0.0024 -0.0041 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1647 0.1372 0.1786 0.0075  0.0019  -0.0038 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1754 0.1489 0.1944 0.0093  0.0034  -0.0012 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1447 0.1194 0.1536 0.0015  -0.0032 -0.0065 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2243 0.1994 0.2339 0.0015  -0.0034 -0.0063 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1469 0.1273 0.1554 -0.0001 -0.0077 -0.0048 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2388 0.2111 0.2416 -0.0022 -0.0023 -0.0094 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.1118 0.0843 0.1235 0.0002  -0.0016 -0.0073 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2458 0.2267 0.2575 0.0004  -0.0076 -0.0044 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1628 0.1316 0.1735 0.0069  0.0045  -0.0059 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1718 0.1361 0.1865 0.0089  0.0101  -0.0055 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1782 0.1369 0.1949 0.0068  0.0131  -0.0076 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1855 0.1419 0.1965 0.0021  0.0124  -0.0119 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1763 0.1366 0.1869 0.0077  0.0136  -0.0089 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1846 0.1498 0.1931 0.0092  0.0111  -0.0070 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1953 0.1630 0.1981 0.0069  0.0072  -0.0081 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.2047 0.1723 0.2191 0.0130  0.0133  -0.0031 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1640 0.1209 0.1887 0.0097  0.0167  -0.0041 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1867 0.1373 0.2142 0.0076  0.0203  -0.0059 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.2110 0.1523 0.2338 0.0035  0.0260  -0.0129 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.2179 0.1553 0.2367 -0.0017 0.0268  -0.0174 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1879 0.1382 0.2267 0.0120  0.0240  0.0007  20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1907 0.1344 0.2340 0.0103  0.0278  0.0003  20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.2022 0.1465 0.2589 0.0151  0.0319  0.0088  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.2137 0.1523 0.2764 0.0140  0.0354  0.0101  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2483 0.1742 0.3153 0.0129  0.0440  0.0064  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2439 0.1617 0.3082 0.0117  0.0499  -0.0001 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2622 0.1831 0.3359 0.0121  0.0474  0.0087  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1990 0.1375 0.2216 0.0047  0.0303  -0.0144 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2189 0.1480 0.2368 -0.0003 0.0375  -0.0222 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2283 0.1599 0.2326 -0.0082 0.0331  -0.0283 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2588 0.1839 0.2568 -0.0150 0.0387  -0.0357 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2417 0.1671 0.2645 0.0032  0.0446  -0.0223 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.2254 0.1575 0.2420 0.0036  0.0403  -0.0219 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2152 0.1561 0.2364 0.0091  0.0351  -0.0145 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2409 0.1720 0.2475 -0.0015 0.0413  -0.0278 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2199 0.1641 0.2342 0.0078  0.0330  -0.0162 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2422 0.1812 0.2478 0.0017  0.0363  -0.0237 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2166 0.1580 0.2170 -0.0080 0.0241  -0.0249 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2116 0.1584 0.2018 -0.0148 0.0188  -0.0274 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2340 0.1860 0.2245 -0.0171 0.0131  -0.0255 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2401 0.1993 0.2250 -0.0219 0.0076  -0.0251 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.2152 0.1691 0.2027 -0.0127 0.0137  -0.0241 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2310 0.1808 0.2172 -0.0115 0.0191  -0.0264 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2351 0.1921 0.2188 -0.0097 0.0138  -0.0227 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2609 0.2051 0.2385 -0.0198 0.0253  -0.0344 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.2254 0.1751 0.2236 -0.0136 0.0143  -0.0232 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.2168 0.1718 0.2160 -0.0155 0.0093  -0.0213 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2271 0.1814 0.2190 -0.0250 0.0099  -0.0265 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2457 0.1912 0.2341 -0.0296 0.0169  -0.0326 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.2129 0.1654 0.2209 -0.0109 0.0112  -0.0182 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2191 0.1831 0.2096 -0.0282 0.0031  -0.0238 24  THR   A N   
139  C CA  . THR   A 18  ? 0.2238 0.1911 0.2071 -0.0385 0.0019  -0.0273 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2267 0.1918 0.2140 -0.0403 0.0032  -0.0280 24  THR   A C   
141  O O   . THR   A 18  ? 0.2156 0.1779 0.2113 -0.0332 0.0041  -0.0249 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2453 0.2269 0.2273 -0.0411 -0.0067 -0.0218 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2416 0.2290 0.2334 -0.0350 -0.0108 -0.0156 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2542 0.2392 0.2336 -0.0390 -0.0087 -0.0194 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2397 0.2066 0.2202 -0.0509 0.0034  -0.0322 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2442 0.2103 0.2283 -0.0534 0.0039  -0.0325 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2285 0.2053 0.2211 -0.0476 -0.0032 -0.0246 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2245 0.1981 0.2239 -0.0436 -0.0017 -0.0231 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2690 0.2384 0.2432 -0.0674 0.0041  -0.0379 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3543 0.3267 0.3321 -0.0709 0.0026  -0.0368 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.4144 0.3744 0.3965 -0.0695 0.0095  -0.0401 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.4041 0.3914 0.3842 -0.0739 -0.0052 -0.0313 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.4276 0.3943 0.4117 -0.0737 0.0061  -0.0382 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.4389 0.4225 0.4225 -0.0760 -0.0029 -0.0327 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.2194 0.2086 0.2128 -0.0467 -0.0101 -0.0191 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.2132 0.2115 0.2164 -0.0410 -0.0151 -0.0121 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.2009 0.1930 0.2112 -0.0307 -0.0125 -0.0106 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.2057 0.1999 0.2230 -0.0274 -0.0129 -0.0081 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2273 0.2389 0.2328 -0.0410 -0.0216 -0.0057 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.3168 0.3371 0.3342 -0.0357 -0.0250 0.0010  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3538 0.3807 0.3746 -0.0396 -0.0269 0.0027  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3429 0.3625 0.3672 -0.0271 -0.0248 0.0043  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1898 0.1749 0.1979 -0.0266 -0.0095 -0.0121 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1858 0.1667 0.1997 -0.0185 -0.0072 -0.0103 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1791 0.1536 0.1962 -0.0182 -0.0030 -0.0114 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1795 0.1565 0.2026 -0.0143 -0.0034 -0.0082 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1827 0.1581 0.1937 -0.0153 -0.0045 -0.0116 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1979 0.1790 0.2074 -0.0139 -0.0082 -0.0093 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1859 0.1742 0.2005 -0.0115 -0.0118 -0.0053 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.1992 0.1774 0.2031 -0.0154 -0.0068 -0.0115 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1820 0.1480 0.1953 -0.0227 0.0017  -0.0160 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1868 0.1457 0.2044 -0.0225 0.0065  -0.0163 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1950 0.1595 0.2152 -0.0255 0.0036  -0.0148 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1962 0.1590 0.2222 -0.0229 0.0053  -0.0121 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.2018 0.1488 0.2156 -0.0275 0.0138  -0.0224 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.2045 0.1442 0.2202 -0.0226 0.0190  -0.0226 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2377 0.1750 0.2475 -0.0243 0.0209  -0.0264 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.2105 0.1460 0.2356 -0.0154 0.0229  -0.0176 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2272 0.1581 0.2426 -0.0183 0.0264  -0.0249 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.2153 0.1460 0.2407 -0.0126 0.0272  -0.0187 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2309 0.1682 0.2646 -0.0115 0.0227  -0.0115 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2338 0.1615 0.2692 -0.0058 0.0315  -0.0132 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2350 0.1703 0.2773 -0.0054 0.0262  -0.0057 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2372 0.1676 0.2810 -0.0025 0.0308  -0.0063 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1805 0.1530 0.1971 -0.0311 -0.0009 -0.0157 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1867 0.1659 0.2067 -0.0342 -0.0037 -0.0138 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1957 0.1839 0.2232 -0.0279 -0.0074 -0.0083 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.2098 0.2036 0.2418 -0.0292 -0.0089 -0.0064 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.2085 0.1951 0.2228 -0.0432 -0.0072 -0.0156 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1843 0.1739 0.2133 -0.0219 -0.0083 -0.0063 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1859 0.1825 0.2217 -0.0166 -0.0101 -0.0024 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1769 0.1689 0.2131 -0.0113 -0.0073 -0.0019 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1750 0.1702 0.2131 -0.0075 -0.0080 -0.0005 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1962 0.2008 0.2339 -0.0157 -0.0140 0.0000  30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.2159 0.2289 0.2554 -0.0213 -0.0174 0.0017  30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2438 0.2631 0.2904 -0.0209 -0.0181 0.0040  30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2296 0.2437 0.2624 -0.0274 -0.0194 0.0004  30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1716 0.1565 0.2070 -0.0114 -0.0039 -0.0024 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1689 0.1509 0.2051 -0.0071 -0.0015 -0.0005 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1845 0.1729 0.2245 -0.0050 -0.0019 0.0027  31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1993 0.1906 0.2422 -0.0067 -0.0017 0.0039  31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1771 0.1504 0.2142 -0.0078 0.0029  -0.0003 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1905 0.1623 0.2308 -0.0035 0.0055  0.0036  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1909 0.1610 0.2275 -0.0014 0.0054  0.0018  31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.2272 0.1906 0.2722 -0.0035 0.0108  0.0055  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1690 0.1599 0.2084 -0.0022 -0.0019 0.0038  32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1708 0.1680 0.2118 -0.0018 -0.0014 0.0063  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1812 0.1782 0.2231 -0.0008 0.0002  0.0107  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1926 0.1942 0.2369 -0.0022 0.0008  0.0147  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1598 0.1609 0.1998 -0.0008 -0.0018 0.0042  32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1887 0.1963 0.2284 -0.0023 -0.0003 0.0055  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1841 0.1869 0.2269 -0.0011 -0.0029 0.0020  32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1717 0.1647 0.2125 0.0015  0.0009  0.0111  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1700 0.1645 0.2137 0.0031  0.0025  0.0167  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1722 0.1596 0.2158 0.0058  0.0044  0.0158  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1734 0.1581 0.2124 0.0059  0.0033  0.0109  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1832 0.1876 0.2249 0.0020  0.0011  0.0189  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1935 0.2031 0.2379 0.0029  0.0016  0.0256  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.2149 0.2314 0.2647 0.0021  0.0019  0.0339  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1904 0.2002 0.2336 0.0049  0.0016  0.0258  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2333 0.2554 0.2860 0.0034  0.0019  0.0399  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.2140 0.2319 0.2622 0.0050  0.0018  0.0345  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1959 0.2010 0.2345 0.0062  0.0013  0.0202  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2271 0.2490 0.2759 0.0063  0.0017  0.0373  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.2067 0.2147 0.2450 0.0073  0.0014  0.0224  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2186 0.2348 0.2620 0.0074  0.0017  0.0306  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1822 0.1667 0.2319 0.0077  0.0076  0.0206  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1789 0.1569 0.2297 0.0103  0.0107  0.0196  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1923 0.1740 0.2522 0.0134  0.0133  0.0285  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.2008 0.1861 0.2677 0.0134  0.0140  0.0354  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.2034 0.1696 0.2531 0.0090  0.0145  0.0138  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2169 0.1779 0.2727 0.0079  0.0179  0.0158  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2247 0.1808 0.2918 0.0113  0.0243  0.0221  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2472 0.2025 0.3216 0.0112  0.0262  0.0274  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.2257 0.1785 0.2956 0.0142  0.0278  0.0225  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1874 0.1687 0.2485 0.0160  0.0149  0.0293  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1825 0.1688 0.2543 0.0193  0.0174  0.0389  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1838 0.1622 0.2586 0.0225  0.0225  0.0367  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1874 0.1676 0.2558 0.0224  0.0208  0.0331  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1976 0.1996 0.2678 0.0178  0.0123  0.0451  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2440 0.2561 0.3258 0.0202  0.0134  0.0575  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2928 0.2993 0.3833 0.0246  0.0184  0.0601  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2866 0.3131 0.3686 0.0170  0.0094  0.0646  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1950 0.1638 0.2796 0.0251  0.0298  0.0384  36  SER   A N   
245  C CA  A SER   A 30  ? 0.2091 0.1690 0.2975 0.0277  0.0367  0.0353  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.2204 0.1804 0.3086 0.0276  0.0366  0.0351  36  SER   A CA  
247  C C   . SER   A 30  ? 0.2173 0.1873 0.3128 0.0315  0.0364  0.0433  36  SER   A C   
248  O O   . SER   A 30  ? 0.2175 0.1847 0.3096 0.0322  0.0384  0.0387  36  SER   A O   
249  C CB  A SER   A 30  ? 0.2183 0.1653 0.3178 0.0293  0.0462  0.0357  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2650 0.2115 0.3636 0.0291  0.0462  0.0349  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.2279 0.1668 0.3346 0.0324  0.0549  0.0343  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.3231 0.2753 0.4363 0.0323  0.0473  0.0473  36  SER   A OG  
253  N N   . SER   A 31  ? 0.2051 0.1885 0.3099 0.0331  0.0335  0.0558  37  SER   A N   
254  C CA  . SER   A 31  ? 0.2090 0.2047 0.3210 0.0357  0.0326  0.0647  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1978 0.2002 0.2960 0.0326  0.0265  0.0591  37  SER   A C   
256  O O   . SER   A 31  ? 0.2067 0.2152 0.3086 0.0344  0.0271  0.0628  37  SER   A O   
257  C CB  . SER   A 31  ? 0.2242 0.2359 0.3475 0.0362  0.0295  0.0801  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2960 0.3196 0.4082 0.0304  0.0212  0.0802  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1762 0.1772 0.2599 0.0280  0.0213  0.0506  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1750 0.1803 0.2464 0.0250  0.0165  0.0448  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1817 0.1744 0.2435 0.0245  0.0179  0.0332  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1679 0.1628 0.2209 0.0225  0.0146  0.0288  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1842 0.1974 0.2476 0.0201  0.0105  0.0440  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1908 0.2202 0.2602 0.0182  0.0079  0.0552  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1837 0.2205 0.2446 0.0122  0.0034  0.0532  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1664 0.2047 0.2163 0.0086  0.0012  0.0459  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1809 0.2290 0.2240 0.0024  -0.0015 0.0450  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.2068 0.2656 0.2514 -0.0017 -0.0030 0.0510  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1771 0.2245 0.2117 -0.0005 -0.0021 0.0381  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1727 0.1528 0.2358 0.0252  0.0228  0.0282  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1645 0.1349 0.2176 0.0227  0.0235  0.0179  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1714 0.1445 0.2140 0.0190  0.0169  0.0135  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1820 0.1531 0.2163 0.0171  0.0151  0.0079  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1849 0.1531 0.2355 0.0235  0.0261  0.0149  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1960 0.1556 0.2363 0.0198  0.0271  0.0052  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.2054 0.1568 0.2442 0.0173  0.0302  0.0005  39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.2046 0.1661 0.2378 0.0186  0.0250  0.0024  39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1604 0.1380 0.2044 0.0180  0.0140  0.0163  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1510 0.1312 0.1875 0.0150  0.0091  0.0124  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1556 0.1320 0.1922 0.0130  0.0089  0.0103  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1696 0.1447 0.2127 0.0137  0.0115  0.0140  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1595 0.1504 0.1959 0.0140  0.0057  0.0164  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1757 0.1720 0.2094 0.0141  0.0045  0.0172  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1882 0.1951 0.2208 0.0110  0.0021  0.0200  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1919 0.1830 0.2187 0.0136  0.0035  0.0108  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1528 0.1283 0.1834 0.0105  0.0060  0.0054  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1497 0.1242 0.1804 0.0082  0.0050  0.0038  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1545 0.1342 0.1821 0.0069  0.0009  0.0022  41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1584 0.1386 0.1825 0.0071  -0.0007 0.0005  41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1642 0.1304 0.1924 0.0055  0.0075  -0.0008 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1783 0.1439 0.2062 0.0020  0.0064  -0.0026 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1917 0.1479 0.2196 -0.0010 0.0116  -0.0059 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1848 0.1547 0.2078 -0.0009 0.0018  -0.0051 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1500 0.1334 0.1800 0.0058  -0.0002 0.0031  42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1454 0.1333 0.1751 0.0050  -0.0026 0.0018  42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1460 0.1340 0.1774 0.0028  -0.0036 0.0008  42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1581 0.1453 0.1916 0.0017  -0.0024 0.0019  42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1418 0.1359 0.1730 0.0049  -0.0020 0.0035  42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1596 0.1566 0.1923 0.0042  -0.0024 0.0012  42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1639 0.1595 0.1929 0.0059  -0.0014 0.0048  42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1518 0.1412 0.1829 0.0019  -0.0058 -0.0005 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1441 0.1362 0.1776 -0.0006 -0.0074 -0.0005 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1567 0.1550 0.1958 0.0006  -0.0084 0.0008  43  SER   A C   
304  O O   . SER   A 37  ? 0.1602 0.1592 0.2006 0.0030  -0.0075 0.0009  43  SER   A O   
305  C CB  . SER   A 37  ? 0.1695 0.1601 0.1991 -0.0041 -0.0092 -0.0019 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1773 0.1697 0.2052 -0.0033 -0.0111 -0.0012 43  SER   A OG  
307  N N   . SER   A 38  ? 0.1652 0.1677 0.2088 -0.0011 -0.0092 0.0016  44  SER   A N   
308  C CA  . SER   A 38  ? 0.1692 0.1775 0.2207 0.0005  -0.0088 0.0032  44  SER   A CA  
309  C C   . SER   A 38  ? 0.1977 0.2106 0.2532 0.0004  -0.0119 0.0064  44  SER   A C   
310  O O   . SER   A 38  ? 0.2191 0.2331 0.2706 -0.0030 -0.0152 0.0071  44  SER   A O   
311  C CB  . SER   A 38  ? 0.2065 0.2186 0.2624 -0.0012 -0.0079 0.0033  44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2305 0.2439 0.2851 -0.0048 -0.0107 0.0041  44  SER   A OG  
313  N N   . THR   A 39  ? 0.1944 0.2105 0.2585 0.0036  -0.0104 0.0086  45  THR   A N   
314  C CA  . THR   A 39  ? 0.2100 0.2320 0.2807 0.0042  -0.0133 0.0140  45  THR   A CA  
315  C C   . THR   A 39  ? 0.2335 0.2627 0.3184 0.0062  -0.0117 0.0179  45  THR   A C   
316  O O   . THR   A 39  ? 0.2209 0.2484 0.3104 0.0079  -0.0066 0.0151  45  THR   A O   
317  C CB  . THR   A 39  ? 0.2237 0.2423 0.2947 0.0073  -0.0122 0.0148  45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.2303 0.2455 0.3071 0.0106  -0.0063 0.0126  45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.2385 0.2504 0.2968 0.0060  -0.0131 0.0113  45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2451 0.2835 0.3375 0.0053  -0.0157 0.0249  46  THR   A N   
321  C CA  . THR   A 40  ? 0.2620 0.3086 0.3709 0.0079  -0.0139 0.0304  46  THR   A CA  
322  C C   . THR   A 40  ? 0.2629 0.3069 0.3835 0.0138  -0.0089 0.0330  46  THR   A C   
323  O O   . THR   A 40  ? 0.2879 0.3308 0.4197 0.0171  -0.0022 0.0319  46  THR   A O   
324  C CB  . THR   A 40  ? 0.3051 0.3649 0.4186 0.0041  -0.0205 0.0384  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3507 0.4133 0.4622 0.0032  -0.0246 0.0434  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.3150 0.3755 0.4163 -0.0028 -0.0242 0.0345  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2541 0.2960 0.3715 0.0145  -0.0110 0.0355  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2623 0.3004 0.3906 0.0197  -0.0058 0.0380  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2600 0.2854 0.3794 0.0205  0.0002  0.0285  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2523 0.2731 0.3560 0.0175  -0.0022 0.0229  47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2871 0.3299 0.4165 0.0195  -0.0111 0.0461  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.2372 0.2574 0.3671 0.0241  0.0082  0.0272  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2443 0.2540 0.3661 0.0235  0.0143  0.0184  48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2345 0.2399 0.3503 0.0238  0.0121  0.0198  48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2488 0.2574 0.3739 0.0264  0.0100  0.0279  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.2795 0.2846 0.4143 0.0257  0.0252  0.0152  48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3434 0.3503 0.4783 0.0235  0.0293  0.0096  48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.4205 0.4221 0.5672 0.0245  0.0416  0.0048  48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.4095 0.4120 0.5756 0.0292  0.0467  0.0102  48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.4650 0.4617 0.6011 0.0197  0.0472  -0.0052 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.1980 0.1975 0.2987 0.0210  0.0120  0.0130  49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.1954 0.1909 0.2897 0.0210  0.0103  0.0135  49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.1918 0.1794 0.2895 0.0216  0.0183  0.0096  49  GLY   A C   
344  O O   . GLY   A 43  ? 0.2050 0.1893 0.3072 0.0209  0.0260  0.0042  49  GLY   A O   
345  N N   . CYS   A 44  ? 0.1809 0.1654 0.2749 0.0219  0.0168  0.0113  50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.2009 0.1772 0.2986 0.0220  0.0246  0.0080  50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.2008 0.1729 0.2838 0.0178  0.0253  0.0010  50  CYS   A C   
348  O O   . CYS   A 44  ? 0.2153 0.1806 0.2997 0.0164  0.0322  -0.0029 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.2110 0.1865 0.3206 0.0258  0.0245  0.0165  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.2509 0.2323 0.3838 0.0311  0.0262  0.0266  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1761 0.1521 0.2459 0.0156  0.0188  -0.0001 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.1776 0.1518 0.2352 0.0118  0.0193  -0.0052 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.1911 0.1652 0.2450 0.0074  0.0248  -0.0123 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.2070 0.1840 0.2640 0.0072  0.0257  -0.0133 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1717 0.1502 0.2189 0.0114  0.0117  -0.0032 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.1904 0.1697 0.2381 0.0137  0.0066  0.0025  51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.1968 0.1729 0.2478 0.0146  0.0083  0.0045  51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.1946 0.1777 0.2384 0.0138  0.0013  0.0047  51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.2020 0.1741 0.2491 0.0029  0.0282  -0.0170 52  THR   A N   
360  C CA  A THR   A 46  ? 0.2201 0.1946 0.2607 -0.0036 0.0327  -0.0236 52  THR   A CA  
361  C CA  B THR   A 46  ? 0.2080 0.1825 0.2488 -0.0036 0.0328  -0.0236 52  THR   A CA  
362  C C   . THR   A 46  ? 0.1998 0.1804 0.2282 -0.0072 0.0278  -0.0231 52  THR   A C   
363  O O   . THR   A 46  ? 0.2158 0.1956 0.2412 -0.0060 0.0247  -0.0206 52  THR   A O   
364  C CB  A THR   A 46  ? 0.2723 0.2399 0.3167 -0.0073 0.0429  -0.0299 52  THR   A CB  
365  C CB  B THR   A 46  ? 0.2279 0.1956 0.2715 -0.0078 0.0429  -0.0302 52  THR   A CB  
366  O OG1 A THR   A 46  ? 0.2877 0.2518 0.3447 -0.0042 0.0483  -0.0303 52  THR   A OG1 
367  O OG1 B THR   A 46  ? 0.2407 0.2055 0.2799 -0.0091 0.0425  -0.0301 52  THR   A OG1 
368  C CG2 A THR   A 46  ? 0.3001 0.2711 0.3337 -0.0170 0.0473  -0.0373 52  THR   A CG2 
369  C CG2 B THR   A 46  ? 0.2235 0.1838 0.2831 -0.0029 0.0493  -0.0293 52  THR   A CG2 
370  N N   . ILE   A 47  ? 0.1947 0.1826 0.2172 -0.0117 0.0270  -0.0244 53  ILE   A N   
371  C CA  . ILE   A 47  ? 0.1799 0.1755 0.1937 -0.0147 0.0223  -0.0219 53  ILE   A CA  
372  C C   . ILE   A 47  ? 0.1952 0.1942 0.2016 -0.0233 0.0265  -0.0265 53  ILE   A C   
373  O O   . ILE   A 47  ? 0.2075 0.2068 0.2123 -0.0298 0.0329  -0.0326 53  ILE   A O   
374  C CB  . ILE   A 47  ? 0.1799 0.1831 0.1922 -0.0152 0.0188  -0.0189 53  ILE   A CB  
375  C CG1 . ILE   A 47  ? 0.1919 0.1918 0.2107 -0.0084 0.0155  -0.0155 53  ILE   A CG1 
376  C CG2 . ILE   A 47  ? 0.1820 0.1938 0.1886 -0.0171 0.0142  -0.0139 53  ILE   A CG2 
377  C CD1 . ILE   A 47  ? 0.2005 0.1966 0.2205 -0.0027 0.0109  -0.0114 53  ILE   A CD1 
378  N N   . ALA   A 48  ? 0.1787 0.1808 0.1804 -0.0243 0.0235  -0.0240 54  ALA   A N   
379  C CA  . ALA   A 48  ? 0.1840 0.1918 0.1779 -0.0335 0.0263  -0.0273 54  ALA   A CA  
380  C C   . ALA   A 48  ? 0.1974 0.2187 0.1856 -0.0405 0.0246  -0.0256 54  ALA   A C   
381  O O   . ALA   A 48  ? 0.1891 0.2173 0.1790 -0.0369 0.0188  -0.0185 54  ALA   A O   
382  C CB  . ALA   A 48  ? 0.1841 0.1939 0.1757 -0.0320 0.0223  -0.0232 54  ALA   A CB  
383  N N   . ARG   A 49  ? 0.2159 0.2418 0.1972 -0.0516 0.0300  -0.0318 55  ARG   A N   
384  C CA  . ARG   A 49  ? 0.2273 0.2687 0.2017 -0.0607 0.0284  -0.0298 55  ARG   A CA  
385  C C   . ARG   A 49  ? 0.2557 0.3056 0.2211 -0.0717 0.0299  -0.0320 55  ARG   A C   
386  O O   . ARG   A 49  ? 0.2772 0.3267 0.2358 -0.0826 0.0371  -0.0409 55  ARG   A O   
387  C CB  . ARG   A 49  ? 0.2376 0.2779 0.2112 -0.0656 0.0343  -0.0362 55  ARG   A CB  
388  C CG  . ARG   A 49  ? 0.2391 0.2708 0.2225 -0.0550 0.0333  -0.0346 55  ARG   A CG  
389  C CD  . ARG   A 49  ? 0.2160 0.2551 0.2024 -0.0490 0.0248  -0.0244 55  ARG   A CD  
390  N NE  . ARG   A 49  ? 0.2046 0.2356 0.1992 -0.0406 0.0246  -0.0240 55  ARG   A NE  
391  C CZ  . ARG   A 49  ? 0.2198 0.2510 0.2193 -0.0331 0.0187  -0.0169 55  ARG   A CZ  
392  N NH1 . ARG   A 49  ? 0.2038 0.2423 0.2022 -0.0320 0.0132  -0.0093 55  ARG   A NH1 
393  N NH2 . ARG   A 49  ? 0.2442 0.2683 0.2503 -0.0269 0.0187  -0.0172 55  ARG   A NH2 
394  N N   . CYS   A 50  ? 0.2491 0.3062 0.2149 -0.0691 0.0236  -0.0241 56  CYS   A N   
395  C CA  . CYS   A 50  ? 0.2705 0.3349 0.2293 -0.0777 0.0241  -0.0249 56  CYS   A CA  
396  C C   . CYS   A 50  ? 0.2722 0.3515 0.2331 -0.0756 0.0159  -0.0127 56  CYS   A C   
397  O O   . CYS   A 50  ? 0.2796 0.3622 0.2475 -0.0674 0.0108  -0.0042 56  CYS   A O   
398  C CB  . CYS   A 50  ? 0.2830 0.3309 0.2442 -0.0733 0.0283  -0.0308 56  CYS   A CB  
399  S SG  . CYS   A 50  ? 0.2486 0.2883 0.2198 -0.0571 0.0221  -0.0229 56  CYS   A SG  
400  N N   . ASP   A 51  ? 0.2986 0.3862 0.2540 -0.0833 0.0157  -0.0124 57  ASP   A N   
401  C CA  . ASP   A 51  ? 0.3244 0.4269 0.2832 -0.0816 0.0089  -0.0007 57  ASP   A CA  
402  C C   . ASP   A 51  ? 0.3108 0.4053 0.2716 -0.0765 0.0090  -0.0013 57  ASP   A C   
403  O O   . ASP   A 51  ? 0.3156 0.4231 0.2761 -0.0801 0.0059  0.0050  57  ASP   A O   
404  C CB  . ASP   A 51  ? 0.4095 0.5359 0.3607 -0.0966 0.0068  0.0038  57  ASP   A CB  
405  C CG  . ASP   A 51  ? 0.5667 0.6940 0.5057 -0.1114 0.0125  -0.0068 57  ASP   A CG  
406  O OD1 . ASP   A 51  ? 0.6084 0.7168 0.5461 -0.1091 0.0185  -0.0170 57  ASP   A OD1 
407  O OD2 . ASP   A 51  ? 0.6245 0.7718 0.5551 -0.1261 0.0114  -0.0046 57  ASP   A OD2 
408  N N   . CYS   A 52  ? 0.2842 0.3587 0.2478 -0.0686 0.0125  -0.0079 58  CYS   A N   
409  C CA  . CYS   A 52  ? 0.2559 0.3228 0.2214 -0.0638 0.0125  -0.0080 58  CYS   A CA  
410  C C   . CYS   A 52  ? 0.2460 0.3196 0.2191 -0.0549 0.0066  0.0026  58  CYS   A C   
411  O O   . CYS   A 52  ? 0.2581 0.3317 0.2376 -0.0474 0.0040  0.0078  58  CYS   A O   
412  C CB  . CYS   A 52  ? 0.2656 0.3115 0.2341 -0.0567 0.0167  -0.0150 58  CYS   A CB  
413  S SG  . CYS   A 52  ? 0.2705 0.3044 0.2337 -0.0657 0.0264  -0.0280 58  CYS   A SG  
414  N N   . GLN   A 53  ? 0.2106 0.2887 0.1834 -0.0560 0.0056  0.0053  59  GLN   A N   
415  C CA  A GLN   A 53  ? 0.1987 0.2816 0.1794 -0.0477 0.0018  0.0143  59  GLN   A CA  
416  C CA  B GLN   A 53  ? 0.2003 0.2821 0.1811 -0.0473 0.0019  0.0140  59  GLN   A CA  
417  C C   . GLN   A 53  ? 0.1814 0.2512 0.1621 -0.0426 0.0035  0.0107  59  GLN   A C   
418  O O   . GLN   A 53  ? 0.1851 0.2587 0.1706 -0.0379 0.0018  0.0162  59  GLN   A O   
419  C CB  A GLN   A 53  ? 0.2129 0.3181 0.1961 -0.0530 -0.0017 0.0245  59  GLN   A CB  
420  C CB  B GLN   A 53  ? 0.2166 0.3207 0.2004 -0.0520 -0.0018 0.0244  59  GLN   A CB  
421  C CG  A GLN   A 53  ? 0.1859 0.3067 0.1761 -0.0523 -0.0053 0.0350  59  GLN   A CG  
422  C CG  B GLN   A 53  ? 0.1928 0.3078 0.1774 -0.0557 -0.0036 0.0287  59  GLN   A CG  
423  C CD  A GLN   A 53  ? 0.2420 0.3848 0.2390 -0.0547 -0.0088 0.0477  59  GLN   A CD  
424  C CD  B GLN   A 53  ? 0.1891 0.2949 0.1820 -0.0446 -0.0042 0.0313  59  GLN   A CD  
425  O OE1 A GLN   A 53  ? 0.2590 0.4213 0.2522 -0.0660 -0.0111 0.0523  59  GLN   A OE1 
426  O OE1 B GLN   A 53  ? 0.1866 0.2915 0.1786 -0.0456 -0.0041 0.0300  59  GLN   A OE1 
427  N NE2 A GLN   A 53  ? 0.1798 0.3215 0.1877 -0.0449 -0.0091 0.0543  59  GLN   A NE2 
428  N NE2 B GLN   A 53  ? 0.1972 0.2956 0.1979 -0.0342 -0.0043 0.0343  59  GLN   A NE2 
429  N N   . THR   A 54  ? 0.1691 0.2245 0.1452 -0.0441 0.0074  0.0018  60  THR   A N   
430  C CA  . THR   A 54  ? 0.1784 0.2209 0.1550 -0.0394 0.0089  -0.0010 60  THR   A CA  
431  C C   . THR   A 54  ? 0.1798 0.2065 0.1583 -0.0343 0.0112  -0.0060 60  THR   A C   
432  O O   . THR   A 54  ? 0.1971 0.2216 0.1745 -0.0376 0.0137  -0.0102 60  THR   A O   
433  C CB  . THR   A 54  ? 0.2223 0.2645 0.1935 -0.0469 0.0117  -0.0048 60  THR   A CB  
434  O OG1 . THR   A 54  ? 0.3059 0.3425 0.2722 -0.0547 0.0166  -0.0126 60  THR   A OG1 
435  C CG2 . THR   A 54  ? 0.2227 0.2823 0.1922 -0.0530 0.0092  0.0005  60  THR   A CG2 
436  N N   . GLY   A 55  ? 0.1753 0.1930 0.1572 -0.0266 0.0103  -0.0048 61  GLY   A N   
437  C CA  . GLY   A 55  ? 0.1719 0.1771 0.1569 -0.0218 0.0116  -0.0075 61  GLY   A CA  
438  C C   . GLY   A 55  ? 0.1571 0.1555 0.1441 -0.0157 0.0100  -0.0052 61  GLY   A C   
439  O O   . GLY   A 55  ? 0.1669 0.1680 0.1520 -0.0162 0.0093  -0.0033 61  GLY   A O   
440  N N   . VAL   A 56  ? 0.1584 0.1499 0.1491 -0.0105 0.0092  -0.0049 62  VAL   A N   
441  C CA  . VAL   A 56  ? 0.1442 0.1305 0.1360 -0.0062 0.0074  -0.0024 62  VAL   A CA  
442  C C   . VAL   A 56  ? 0.1451 0.1313 0.1389 -0.0016 0.0047  -0.0007 62  VAL   A C   
443  O O   . VAL   A 56  ? 0.1592 0.1445 0.1557 -0.0009 0.0050  -0.0018 62  VAL   A O   
444  C CB  . VAL   A 56  ? 0.1772 0.1549 0.1723 -0.0065 0.0100  -0.0032 62  VAL   A CB  
445  C CG1 . VAL   A 56  ? 0.2138 0.1885 0.2106 -0.0028 0.0073  0.0010  62  VAL   A CG1 
446  C CG2 . VAL   A 56  ? 0.1895 0.1657 0.1822 -0.0118 0.0137  -0.0056 62  VAL   A CG2 
447  N N   . TYR   A 57  ? 0.1400 0.1271 0.1322 0.0008  0.0027  0.0014  63  TYR   A N   
448  C CA  . TYR   A 57  ? 0.1451 0.1311 0.1383 0.0038  0.0009  0.0021  63  TYR   A CA  
449  C C   . TYR   A 57  ? 0.1507 0.1338 0.1425 0.0044  -0.0009 0.0037  63  TYR   A C   
450  O O   . TYR   A 57  ? 0.1575 0.1404 0.1466 0.0031  -0.0008 0.0048  63  TYR   A O   
451  C CB  . TYR   A 57  ? 0.1405 0.1309 0.1337 0.0052  0.0012  0.0025  63  TYR   A CB  
452  C CG  . TYR   A 57  ? 0.1482 0.1395 0.1390 0.0057  0.0021  0.0032  63  TYR   A CG  
453  C CD1 . TYR   A 57  ? 0.1597 0.1548 0.1495 0.0042  0.0032  0.0042  63  TYR   A CD1 
454  C CD2 . TYR   A 57  ? 0.1600 0.1485 0.1493 0.0067  0.0025  0.0022  63  TYR   A CD2 
455  C CE1 . TYR   A 57  ? 0.1741 0.1704 0.1625 0.0046  0.0048  0.0047  63  TYR   A CE1 
456  C CE2 . TYR   A 57  ? 0.1729 0.1619 0.1599 0.0064  0.0047  0.0018  63  TYR   A CE2 
457  C CZ  . TYR   A 57  ? 0.1769 0.1697 0.1638 0.0058  0.0058  0.0032  63  TYR   A CZ  
458  O OH  . TYR   A 57  ? 0.2175 0.2112 0.2026 0.0054  0.0086  0.0027  63  TYR   A OH  
459  N N   . TYR   A 58  ? 0.1501 0.1321 0.1429 0.0055  -0.0026 0.0041  64  TYR   A N   
460  C CA  . TYR   A 58  ? 0.1445 0.1263 0.1348 0.0045  -0.0049 0.0062  64  TYR   A CA  
461  C C   . TYR   A 58  ? 0.1542 0.1372 0.1392 0.0034  -0.0043 0.0041  64  TYR   A C   
462  O O   . TYR   A 58  ? 0.1553 0.1377 0.1409 0.0043  -0.0032 0.0018  64  TYR   A O   
463  C CB  . TYR   A 58  ? 0.1558 0.1377 0.1506 0.0050  -0.0073 0.0084  64  TYR   A CB  
464  C CG  . TYR   A 58  ? 0.1659 0.1506 0.1581 0.0025  -0.0105 0.0122  64  TYR   A CG  
465  C CD1 . TYR   A 58  ? 0.1689 0.1545 0.1613 0.0013  -0.0113 0.0164  64  TYR   A CD1 
466  C CD2 . TYR   A 58  ? 0.1683 0.1557 0.1573 0.0002  -0.0124 0.0117  64  TYR   A CD2 
467  C CE1 . TYR   A 58  ? 0.1873 0.1778 0.1766 -0.0021 -0.0147 0.0209  64  TYR   A CE1 
468  C CE2 . TYR   A 58  ? 0.1773 0.1695 0.1620 -0.0041 -0.0155 0.0151  64  TYR   A CE2 
469  C CZ  . TYR   A 58  ? 0.1974 0.1919 0.1827 -0.0052 -0.0170 0.0203  64  TYR   A CZ  
470  O OH  . TYR   A 58  ? 0.2203 0.2217 0.2014 -0.0103 -0.0207 0.0252  64  TYR   A OH  
471  N N   . CYS   A 59  ? 0.1520 0.1360 0.1321 0.0010  -0.0045 0.0048  65  CYS   A N   
472  C CA  . CYS   A 59  ? 0.1628 0.1471 0.1370 -0.0012 -0.0023 0.0018  65  CYS   A CA  
473  C C   . CYS   A 59  ? 0.1655 0.1520 0.1342 -0.0059 -0.0050 0.0030  65  CYS   A C   
474  O O   . CYS   A 59  ? 0.1767 0.1660 0.1425 -0.0085 -0.0070 0.0063  65  CYS   A O   
475  C CB  . CYS   A 59  ? 0.1615 0.1469 0.1338 -0.0013 0.0003  0.0014  65  CYS   A CB  
476  S SG  . CYS   A 59  ? 0.1869 0.1720 0.1529 -0.0043 0.0050  -0.0029 65  CYS   A SG  
477  N N   . SER   A 60  ? 0.1669 0.1533 0.1342 -0.0078 -0.0053 0.0008  66  SER   A N   
478  C CA  . SER   A 60  ? 0.1802 0.1712 0.1416 -0.0139 -0.0086 0.0025  66  SER   A CA  
479  C C   . SER   A 60  ? 0.1840 0.1768 0.1356 -0.0199 -0.0063 -0.0001 66  SER   A C   
480  O O   . SER   A 60  ? 0.2023 0.2014 0.1491 -0.0253 -0.0101 0.0039  66  SER   A O   
481  C CB  . SER   A 60  ? 0.2117 0.2025 0.1728 -0.0159 -0.0090 0.0002  66  SER   A CB  
482  O OG  . SER   A 60  ? 0.2369 0.2228 0.1944 -0.0172 -0.0034 -0.0070 66  SER   A OG  
483  N N   . SER   A 61  ? 0.1797 0.1680 0.1296 -0.0189 -0.0001 -0.0059 67  SER   A N   
484  C CA  . SER   A 61  ? 0.1768 0.1661 0.1179 -0.0244 0.0036  -0.0094 67  SER   A CA  
485  C C   . SER   A 61  ? 0.1821 0.1753 0.1217 -0.0248 0.0016  -0.0049 67  SER   A C   
486  O O   . SER   A 61  ? 0.1920 0.1870 0.1240 -0.0299 0.0043  -0.0073 67  SER   A O   
487  C CB  . SER   A 61  ? 0.1926 0.1757 0.1350 -0.0226 0.0122  -0.0165 67  SER   A CB  
488  O OG  . SER   A 61  ? 0.2037 0.1850 0.1548 -0.0152 0.0140  -0.0146 67  SER   A OG  
489  N N   . ARG   A 62  ? 0.1857 0.1794 0.1326 -0.0198 -0.0024 0.0011  68  ARG   A N   
490  C CA  . ARG   A 62  ? 0.1909 0.1875 0.1373 -0.0204 -0.0046 0.0062  68  ARG   A CA  
491  C C   . ARG   A 62  ? 0.1969 0.1966 0.1485 -0.0200 -0.0106 0.0144  68  ARG   A C   
492  O O   . ARG   A 62  ? 0.1992 0.2005 0.1524 -0.0201 -0.0123 0.0198  68  ARG   A O   
493  C CB  . ARG   A 62  ? 0.1975 0.1908 0.1495 -0.0150 -0.0016 0.0054  68  ARG   A CB  
494  C CG  . ARG   A 62  ? 0.1942 0.1862 0.1439 -0.0149 0.0047  -0.0004 68  ARG   A CG  
495  C CD  . ARG   A 62  ? 0.2065 0.2017 0.1487 -0.0200 0.0062  -0.0007 68  ARG   A CD  
496  N NE  . ARG   A 62  ? 0.2429 0.2368 0.1847 -0.0195 0.0135  -0.0062 68  ARG   A NE  
497  C CZ  . ARG   A 62  ? 0.2229 0.2146 0.1605 -0.0227 0.0189  -0.0124 68  ARG   A CZ  
498  N NH1 . ARG   A 62  ? 0.2340 0.2257 0.1655 -0.0278 0.0172  -0.0143 68  ARG   A NH1 
499  N NH2 . ARG   A 62  ? 0.2396 0.2297 0.1794 -0.0215 0.0268  -0.0167 68  ARG   A NH2 
500  N N   . ARG   A 63  ? 0.2069 0.2069 0.1630 -0.0187 -0.0131 0.0158  69  ARG   A N   
501  C CA  . ARG   A 63  ? 0.2139 0.2162 0.1787 -0.0166 -0.0176 0.0240  69  ARG   A CA  
502  C C   . ARG   A 63  ? 0.2408 0.2379 0.2133 -0.0115 -0.0158 0.0259  69  ARG   A C   
503  O O   . ARG   A 63  ? 0.2683 0.2668 0.2465 -0.0112 -0.0177 0.0333  69  ARG   A O   
504  C CB  . ARG   A 63  ? 0.2686 0.2799 0.2308 -0.0225 -0.0223 0.0321  69  ARG   A CB  
505  C CG  . ARG   A 63  ? 0.2918 0.3096 0.2518 -0.0268 -0.0257 0.0335  69  ARG   A CG  
506  C CD  . ARG   A 63  ? 0.2887 0.3180 0.2495 -0.0321 -0.0315 0.0448  69  ARG   A CD  
507  N NE  . ARG   A 63  ? 0.3010 0.3386 0.2529 -0.0404 -0.0340 0.0433  69  ARG   A NE  
508  C CZ  . ARG   A 63  ? 0.2554 0.2995 0.1938 -0.0501 -0.0343 0.0411  69  ARG   A CZ  
509  N NH1 . ARG   A 63  ? 0.2799 0.3243 0.2129 -0.0522 -0.0329 0.0415  69  ARG   A NH1 
510  N NH2 . ARG   A 63  ? 0.2719 0.3230 0.2018 -0.0587 -0.0358 0.0385  69  ARG   A NH2 
511  N N   . LYS   A 64  ? 0.2068 0.1986 0.1801 -0.0081 -0.0119 0.0200  70  LYS   A N   
512  C CA  . LYS   A 64  ? 0.2074 0.1951 0.1856 -0.0054 -0.0097 0.0203  70  LYS   A CA  
513  C C   . LYS   A 64  ? 0.2043 0.1884 0.1865 -0.0020 -0.0071 0.0157  70  LYS   A C   
514  O O   . LYS   A 64  ? 0.1929 0.1775 0.1729 -0.0013 -0.0061 0.0116  70  LYS   A O   
515  C CB  . LYS   A 64  ? 0.2356 0.2242 0.2077 -0.0075 -0.0076 0.0186  70  LYS   A CB  
516  C CG  . LYS   A 64  ? 0.3557 0.3471 0.3258 -0.0108 -0.0097 0.0247  70  LYS   A CG  
517  C CD  . LYS   A 64  ? 0.4664 0.4580 0.4319 -0.0125 -0.0072 0.0231  70  LYS   A CD  
518  C CE  . LYS   A 64  ? 0.5338 0.5295 0.4957 -0.0168 -0.0095 0.0292  70  LYS   A CE  
519  N NZ  . LYS   A 64  ? 0.5837 0.5857 0.5382 -0.0214 -0.0120 0.0298  70  LYS   A NZ  
520  N N   . HIS   A 65  ? 0.1852 0.1658 0.1733 -0.0006 -0.0052 0.0164  71  HIS   A N   
521  C CA  . HIS   A 65  ? 0.1839 0.1624 0.1743 0.0007  -0.0024 0.0120  71  HIS   A CA  
522  C C   . HIS   A 65  ? 0.1975 0.1770 0.1843 -0.0012 -0.0001 0.0099  71  HIS   A C   
523  O O   . HIS   A 65  ? 0.2409 0.2190 0.2271 -0.0029 0.0006  0.0120  71  HIS   A O   
524  C CB  . HIS   A 65  ? 0.1670 0.1409 0.1655 0.0018  -0.0005 0.0130  71  HIS   A CB  
525  C CG  . HIS   A 65  ? 0.1764 0.1507 0.1802 0.0040  -0.0024 0.0152  71  HIS   A CG  
526  N ND1 . HIS   A 65  ? 0.2017 0.1778 0.2095 0.0044  -0.0053 0.0217  71  HIS   A ND1 
527  C CD2 . HIS   A 65  ? 0.1916 0.1657 0.1980 0.0054  -0.0017 0.0123  71  HIS   A CD2 
528  C CE1 . HIS   A 65  ? 0.2057 0.1828 0.2188 0.0062  -0.0063 0.0224  71  HIS   A CE1 
529  N NE2 . HIS   A 65  ? 0.2163 0.1915 0.2287 0.0069  -0.0040 0.0166  71  HIS   A NE2 
530  N N   . TYR   A 66  ? 0.1722 0.1550 0.1572 -0.0010 0.0011  0.0068  72  TYR   A N   
531  C CA  . TYR   A 66  ? 0.1792 0.1657 0.1619 -0.0031 0.0029  0.0060  72  TYR   A CA  
532  C C   . TYR   A 66  ? 0.1657 0.1547 0.1501 -0.0048 0.0045  0.0039  72  TYR   A C   
533  O O   . TYR   A 66  ? 0.1683 0.1590 0.1546 -0.0034 0.0042  0.0030  72  TYR   A O   
534  C CB  . TYR   A 66  ? 0.1829 0.1743 0.1634 -0.0018 0.0031  0.0058  72  TYR   A CB  
535  C CG  . TYR   A 66  ? 0.1837 0.1741 0.1602 -0.0022 0.0025  0.0067  72  TYR   A CG  
536  C CD1 . TYR   A 66  ? 0.2001 0.1913 0.1734 -0.0046 0.0029  0.0081  72  TYR   A CD1 
537  C CD2 . TYR   A 66  ? 0.1825 0.1718 0.1575 -0.0013 0.0019  0.0057  72  TYR   A CD2 
538  C CE1 . TYR   A 66  ? 0.2195 0.2111 0.1880 -0.0062 0.0025  0.0089  72  TYR   A CE1 
539  C CE2 . TYR   A 66  ? 0.1998 0.1894 0.1694 -0.0035 0.0019  0.0057  72  TYR   A CE2 
540  C CZ  . TYR   A 66  ? 0.2146 0.2058 0.1808 -0.0060 0.0021  0.0074  72  TYR   A CZ  
541  O OH  . TYR   A 66  ? 0.2514 0.2441 0.2112 -0.0095 0.0022  0.0073  72  TYR   A OH  
542  N N   . PRO   A 67  ? 0.1708 0.1609 0.1538 -0.0088 0.0065  0.0030  73  PRO   A N   
543  C CA  . PRO   A 67  ? 0.1664 0.1618 0.1491 -0.0126 0.0079  0.0010  73  PRO   A CA  
544  C C   . PRO   A 67  ? 0.1804 0.1864 0.1634 -0.0120 0.0066  0.0035  73  PRO   A C   
545  O O   . PRO   A 67  ? 0.2185 0.2275 0.2010 -0.0107 0.0064  0.0057  73  PRO   A O   
546  C CB  . PRO   A 67  ? 0.2021 0.1960 0.1824 -0.0183 0.0107  -0.0007 73  PRO   A CB  
547  C CG  . PRO   A 67  ? 0.2303 0.2210 0.2098 -0.0166 0.0100  0.0018  73  PRO   A CG  
548  C CD  . PRO   A 67  ? 0.1942 0.1817 0.1752 -0.0111 0.0074  0.0041  73  PRO   A CD  
549  N N   . VAL   A 68  ? 0.1568 0.1688 0.1414 -0.0130 0.0063  0.0038  74  VAL   A N   
550  C CA  . VAL   A 68  ? 0.1776 0.2008 0.1653 -0.0119 0.0053  0.0082  74  VAL   A CA  
551  C C   . VAL   A 68  ? 0.1638 0.1975 0.1513 -0.0176 0.0050  0.0093  74  VAL   A C   
552  O O   . VAL   A 68  ? 0.1725 0.2038 0.1578 -0.0210 0.0057  0.0060  74  VAL   A O   
553  C CB  . VAL   A 68  ? 0.2304 0.2516 0.2226 -0.0056 0.0047  0.0099  74  VAL   A CB  
554  C CG1 . VAL   A 68  ? 0.2564 0.2716 0.2480 -0.0018 0.0054  0.0095  74  VAL   A CG1 
555  C CG2 . VAL   A 68  ? 0.2373 0.2528 0.2295 -0.0049 0.0041  0.0073  74  VAL   A CG2 
556  N N   . SER   A 69  ? 0.1663 0.2134 0.1572 -0.0187 0.0041  0.0151  75  SER   A N   
557  C CA  . SER   A 69  ? 0.1639 0.2256 0.1564 -0.0237 0.0026  0.0194  75  SER   A CA  
558  C C   . SER   A 69  ? 0.1568 0.2221 0.1580 -0.0170 0.0017  0.0253  75  SER   A C   
559  O O   . SER   A 69  ? 0.1657 0.2289 0.1728 -0.0104 0.0029  0.0281  75  SER   A O   
560  C CB  . SER   A 69  ? 0.2133 0.2896 0.2070 -0.0284 0.0019  0.0245  75  SER   A CB  
561  O OG  . SER   A 69  ? 0.3135 0.3861 0.2991 -0.0354 0.0034  0.0189  75  SER   A OG  
562  N N   . PHE   A 70  ? 0.1594 0.2293 0.1616 -0.0187 0.0005  0.0269  76  PHE   A N   
563  C CA  . PHE   A 70  ? 0.1635 0.2351 0.1745 -0.0123 0.0002  0.0325  76  PHE   A CA  
564  C C   . PHE   A 70  ? 0.1630 0.2521 0.1786 -0.0165 -0.0020 0.0408  76  PHE   A C   
565  O O   . PHE   A 70  ? 0.1828 0.2807 0.1918 -0.0256 -0.0035 0.0397  76  PHE   A O   
566  C CB  . PHE   A 70  ? 0.1714 0.2279 0.1804 -0.0081 0.0010  0.0265  76  PHE   A CB  
567  C CG  . PHE   A 70  ? 0.1617 0.2142 0.1634 -0.0135 0.0007  0.0203  76  PHE   A CG  
568  C CD1 . PHE   A 70  ? 0.1635 0.2059 0.1588 -0.0157 0.0022  0.0130  76  PHE   A CD1 
569  C CD2 . PHE   A 70  ? 0.1584 0.2170 0.1610 -0.0162 -0.0002 0.0221  76  PHE   A CD2 
570  C CE1 . PHE   A 70  ? 0.1711 0.2090 0.1620 -0.0201 0.0037  0.0073  76  PHE   A CE1 
571  C CE2 . PHE   A 70  ? 0.1771 0.2317 0.1733 -0.0214 0.0009  0.0156  76  PHE   A CE2 
572  C CZ  . PHE   A 70  ? 0.1683 0.2124 0.1593 -0.0233 0.0033  0.0080  76  PHE   A CZ  
573  N N   . SER   A 71  ? 0.1599 0.2549 0.1872 -0.0107 -0.0019 0.0495  77  SER   A N   
574  C CA  . SER   A 71  ? 0.1592 0.2728 0.1935 -0.0139 -0.0043 0.0604  77  SER   A CA  
575  C C   . SER   A 71  ? 0.1588 0.2714 0.1890 -0.0170 -0.0058 0.0584  77  SER   A C   
576  O O   . SER   A 71  ? 0.1698 0.2662 0.1951 -0.0142 -0.0043 0.0497  77  SER   A O   
577  C CB  . SER   A 71  ? 0.1822 0.3012 0.2334 -0.0055 -0.0025 0.0714  77  SER   A CB  
578  O OG  . SER   A 71  ? 0.2000 0.3030 0.2558 0.0028  0.0009  0.0683  77  SER   A OG  
579  N N   . LYS   A 72  ? 0.1592 0.2899 0.1919 -0.0230 -0.0086 0.0670  78  LYS   A N   
580  C CA  . LYS   A 72  ? 0.1659 0.2974 0.1951 -0.0266 -0.0098 0.0660  78  LYS   A CA  
581  C C   . LYS   A 72  ? 0.1749 0.2986 0.2151 -0.0168 -0.0084 0.0703  78  LYS   A C   
582  O O   . LYS   A 72  ? 0.1814 0.3064 0.2346 -0.0093 -0.0069 0.0783  78  LYS   A O   
583  C CB  . LYS   A 72  ? 0.1837 0.3400 0.2118 -0.0375 -0.0136 0.0751  78  LYS   A CB  
584  C CG  . LYS   A 72  ? 0.2398 0.4020 0.2541 -0.0496 -0.0140 0.0679  78  LYS   A CG  
585  C CD  . LYS   A 72  ? 0.3199 0.5075 0.3302 -0.0631 -0.0176 0.0755  78  LYS   A CD  
586  C CE  . LYS   A 72  ? 0.4112 0.6020 0.4052 -0.0772 -0.0164 0.0654  78  LYS   A CE  
587  N NZ  . LYS   A 72  ? 0.4630 0.6760 0.4500 -0.0921 -0.0191 0.0698  78  LYS   A NZ  
588  N N   . PRO   A 73  ? 0.1686 0.2835 0.2047 -0.0169 -0.0081 0.0651  79  PRO   A N   
589  C CA  . PRO   A 73  ? 0.1739 0.2801 0.2199 -0.0083 -0.0064 0.0684  79  PRO   A CA  
590  C C   . PRO   A 73  ? 0.1824 0.3039 0.2437 -0.0059 -0.0072 0.0843  79  PRO   A C   
591  O O   . PRO   A 73  ? 0.1998 0.3409 0.2615 -0.0132 -0.0108 0.0929  79  PRO   A O   
592  C CB  . PRO   A 73  ? 0.2080 0.3076 0.2459 -0.0117 -0.0068 0.0612  79  PRO   A CB  
593  C CG  . PRO   A 73  ? 0.2565 0.3599 0.2812 -0.0213 -0.0078 0.0537  79  PRO   A CG  
594  C CD  . PRO   A 73  ? 0.1965 0.3087 0.2192 -0.0250 -0.0085 0.0555  79  PRO   A CD  
595  N N   . SER   A 74  ? 0.1673 0.2809 0.2416 0.0036  -0.0033 0.0883  80  SER   A N   
596  C CA  . SER   A 74  ? 0.1972 0.3239 0.2899 0.0077  -0.0024 0.1044  80  SER   A CA  
597  C C   . SER   A 74  ? 0.1718 0.2829 0.2770 0.0176  0.0036  0.1051  80  SER   A C   
598  O O   . SER   A 74  ? 0.1765 0.2676 0.2750 0.0208  0.0068  0.0929  80  SER   A O   
599  C CB  . SER   A 74  ? 0.2863 0.4248 0.3856 0.0080  -0.0023 0.1110  80  SER   A CB  
600  O OG  . SER   A 74  ? 0.4253 0.5779 0.5120 -0.0025 -0.0074 0.1094  80  SER   A OG  
601  N N   . LEU   A 75  ? 0.1890 0.3102 0.3140 0.0223  0.0058  0.1206  81  LEU   A N   
602  C CA  . LEU   A 75  ? 0.2168 0.3240 0.3570 0.0315  0.0132  0.1229  81  LEU   A CA  
603  C C   . LEU   A 75  ? 0.2254 0.3283 0.3760 0.0379  0.0195  0.1236  81  LEU   A C   
604  O O   . LEU   A 75  ? 0.2465 0.3671 0.4100 0.0388  0.0190  0.1367  81  LEU   A O   
605  C CB  . LEU   A 75  ? 0.2301 0.3521 0.3880 0.0328  0.0126  0.1409  81  LEU   A CB  
606  C CG  . LEU   A 75  ? 0.2708 0.3788 0.4454 0.0412  0.0206  0.1446  81  LEU   A CG  
607  C CD1 . LEU   A 75  ? 0.2811 0.3695 0.4428 0.0401  0.0215  0.1307  81  LEU   A CD1 
608  C CD2 . LEU   A 75  ? 0.2763 0.4025 0.4708 0.0423  0.0193  0.1657  81  LEU   A CD2 
609  N N   . ILE   A 76  ? 0.2156 0.2972 0.3601 0.0413  0.0252  0.1098  82  ILE   A N   
610  C CA  . ILE   A 76  ? 0.2356 0.3107 0.3859 0.0461  0.0318  0.1069  82  ILE   A CA  
611  C C   . ILE   A 76  ? 0.2600 0.3154 0.4205 0.0529  0.0426  0.1024  82  ILE   A C   
612  O O   . ILE   A 76  ? 0.2494 0.2897 0.4026 0.0522  0.0441  0.0935  82  ILE   A O   
613  C CB  . ILE   A 76  ? 0.2600 0.3283 0.3891 0.0412  0.0284  0.0923  82  ILE   A CB  
614  C CG1 . ILE   A 76  ? 0.2960 0.3824 0.4146 0.0334  0.0192  0.0954  82  ILE   A CG1 
615  C CG2 . ILE   A 76  ? 0.2864 0.3457 0.4182 0.0451  0.0355  0.0867  82  ILE   A CG2 
616  C CD1 . ILE   A 76  ? 0.3148 0.3968 0.4165 0.0288  0.0163  0.0842  82  ILE   A CD1 
617  N N   . PHE   A 77  ? 0.2759 0.3315 0.4542 0.0591  0.0509  0.1086  83  PHE   A N   
618  C CA  . PHE   A 77  ? 0.2798 0.3159 0.4686 0.0648  0.0632  0.1033  83  PHE   A CA  
619  C C   . PHE   A 77  ? 0.3015 0.3207 0.4719 0.0618  0.0661  0.0848  83  PHE   A C   
620  O O   . PHE   A 77  ? 0.3298 0.3537 0.4927 0.0600  0.0640  0.0814  83  PHE   A O   
621  C CB  . PHE   A 77  ? 0.2809 0.3229 0.4968 0.0726  0.0727  0.1163  83  PHE   A CB  
622  C CG  . PHE   A 77  ? 0.3197 0.3415 0.5496 0.0782  0.0869  0.1124  83  PHE   A CG  
623  C CD1 . PHE   A 77  ? 0.3406 0.3572 0.5810 0.0804  0.0894  0.1182  83  PHE   A CD1 
624  C CD2 . PHE   A 77  ? 0.3544 0.3610 0.5852 0.0802  0.0982  0.1016  83  PHE   A CD2 
625  C CE1 . PHE   A 77  ? 0.3712 0.3674 0.6239 0.0847  0.1036  0.1136  83  PHE   A CE1 
626  C CE2 . PHE   A 77  ? 0.3634 0.3503 0.6065 0.0841  0.1128  0.0966  83  PHE   A CE2 
627  C CZ  . PHE   A 77  ? 0.3706 0.3520 0.6250 0.0864  0.1157  0.1026  83  PHE   A CZ  
628  N N   . VAL   A 78  ? 0.2902 0.2907 0.4523 0.0603  0.0702  0.0731  84  VAL   A N   
629  C CA  . VAL   A 78  ? 0.2904 0.2764 0.4348 0.0563  0.0726  0.0564  84  VAL   A CA  
630  C C   . VAL   A 78  ? 0.3157 0.2838 0.4694 0.0590  0.0872  0.0499  84  VAL   A C   
631  O O   . VAL   A 78  ? 0.3180 0.2784 0.4820 0.0611  0.0927  0.0522  84  VAL   A O   
632  C CB  . VAL   A 78  ? 0.2722 0.2533 0.3963 0.0500  0.0642  0.0473  84  VAL   A CB  
633  C CG1 . VAL   A 78  ? 0.2872 0.2562 0.3935 0.0451  0.0656  0.0320  84  VAL   A CG1 
634  C CG2 . VAL   A 78  ? 0.2727 0.2704 0.3891 0.0471  0.0517  0.0533  84  VAL   A CG2 
635  N N   . GLU   A 79  ? 0.3412 0.3023 0.4896 0.0576  0.0936  0.0406  85  GLU   A N   
636  C CA  . GLU   A 79  ? 0.3816 0.3252 0.5370 0.0586  0.1090  0.0323  85  GLU   A CA  
637  C C   . GLU   A 79  ? 0.4123 0.3399 0.5537 0.0524  0.1110  0.0193  85  GLU   A C   
638  O O   . GLU   A 79  ? 0.4197 0.3495 0.5424 0.0467  0.1002  0.0144  85  GLU   A O   
639  C CB  . GLU   A 79  ? 0.4328 0.3746 0.5821 0.0567  0.1142  0.0245  85  GLU   A CB  
640  C CG  . GLU   A 79  ? 0.5436 0.4994 0.7104 0.0632  0.1158  0.0367  85  GLU   A CG  
641  C CD  . GLU   A 79  ? 0.6761 0.6328 0.8729 0.0719  0.1261  0.0496  85  GLU   A CD  
642  O OE1 . GLU   A 79  ? 0.7136 0.6534 0.9201 0.0735  0.1400  0.0440  85  GLU   A OE1 
643  O OE2 . GLU   A 79  ? 0.7193 0.6944 0.9305 0.0768  0.1203  0.0658  85  GLU   A OE2 
644  N N   . ALA   A 80  ? 0.4234 0.3344 0.5741 0.0528  0.1260  0.0132  86  ALA   A N   
645  C CA  . ALA   A 80  ? 0.4447 0.3398 0.5832 0.0458  0.1301  0.0002  86  ALA   A CA  
646  C C   . ALA   A 80  ? 0.4586 0.3519 0.5709 0.0362  0.1248  -0.0135 86  ALA   A C   
647  O O   . ALA   A 80  ? 0.4719 0.3688 0.5780 0.0348  0.1253  -0.0170 86  ALA   A O   
648  C CB  . ALA   A 80  ? 0.4560 0.3333 0.6094 0.0470  0.1494  -0.0052 86  ALA   A CB  
649  N N   . SER   A 81  ? 0.4597 0.3499 0.5568 0.0296  0.1181  -0.0196 87  SER   A N   
650  C CA  . SER   A 81  ? 0.4633 0.3530 0.5364 0.0198  0.1125  -0.0312 87  SER   A CA  
651  C C   . SER   A 81  ? 0.4648 0.3406 0.5295 0.0114  0.1189  -0.0426 87  SER   A C   
652  O O   . SER   A 81  ? 0.4598 0.3257 0.5377 0.0139  0.1278  -0.0415 87  SER   A O   
653  C CB  . SER   A 81  ? 0.4811 0.3849 0.5434 0.0194  0.0954  -0.0256 87  SER   A CB  
654  O OG  . SER   A 81  ? 0.4895 0.3927 0.5541 0.0198  0.0909  -0.0222 87  SER   A OG  
655  N N   . GLU   A 82  ? 0.4724 0.3493 0.5155 0.0011  0.1129  -0.0519 88  GLU   A N   
656  C CA  . GLU   A 82  ? 0.4732 0.3402 0.5065 -0.0084 0.1167  -0.0619 88  GLU   A CA  
657  C C   . GLU   A 82  ? 0.4307 0.2999 0.4695 -0.0053 0.1094  -0.0549 88  GLU   A C   
658  O O   . GLU   A 82  ? 0.4217 0.2812 0.4593 -0.0106 0.1148  -0.0607 88  GLU   A O   
659  C CB  . GLU   A 82  ? 0.5252 0.3986 0.5349 -0.0200 0.1084  -0.0697 88  GLU   A CB  
660  C CG  . GLU   A 82  ? 0.6299 0.5078 0.6313 -0.0227 0.1093  -0.0731 88  GLU   A CG  
661  C CD  . GLU   A 82  ? 0.7286 0.6182 0.7109 -0.0306 0.0964  -0.0742 88  GLU   A CD  
662  O OE1 . GLU   A 82  ? 0.7462 0.6469 0.7278 -0.0259 0.0869  -0.0668 88  GLU   A OE1 
663  O OE2 . GLU   A 82  ? 0.7516 0.6400 0.7205 -0.0417 0.0957  -0.0816 88  GLU   A OE2 
664  N N   . TYR   A 83  ? 0.4016 0.2834 0.4459 0.0024  0.0977  -0.0429 89  TYR   A N   
665  C CA  . TYR   A 83  ? 0.3682 0.2538 0.4152 0.0041  0.0900  -0.0369 89  TYR   A CA  
666  C C   . TYR   A 83  ? 0.3438 0.2298 0.4107 0.0134  0.0925  -0.0256 89  TYR   A C   
667  O O   . TYR   A 83  ? 0.3450 0.2306 0.4151 0.0136  0.0897  -0.0223 89  TYR   A O   
668  C CB  . TYR   A 83  ? 0.3605 0.2603 0.3967 0.0036  0.0748  -0.0329 89  TYR   A CB  
669  C CG  . TYR   A 83  ? 0.3749 0.2765 0.3925 -0.0059 0.0708  -0.0417 89  TYR   A CG  
670  C CD1 . TYR   A 83  ? 0.4107 0.3099 0.4181 -0.0144 0.0689  -0.0478 89  TYR   A CD1 
671  C CD2 . TYR   A 83  ? 0.4078 0.3139 0.4186 -0.0069 0.0694  -0.0433 89  TYR   A CD2 
672  C CE1 . TYR   A 83  ? 0.4336 0.3374 0.4247 -0.0236 0.0643  -0.0539 89  TYR   A CE1 
673  C CE2 . TYR   A 83  ? 0.4323 0.3419 0.4266 -0.0159 0.0652  -0.0496 89  TYR   A CE2 
674  C CZ  . TYR   A 83  ? 0.4579 0.3665 0.4427 -0.0245 0.0630  -0.0547 89  TYR   A CZ  
675  O OH  . TYR   A 83  ? 0.5060 0.4211 0.4756 -0.0338 0.0578  -0.0587 89  TYR   A OH  
676  N N   . TYR   A 84  ? 0.3444 0.2332 0.4255 0.0210  0.0972  -0.0183 90  TYR   A N   
677  C CA  . TYR   A 84  ? 0.3216 0.2138 0.4234 0.0297  0.0990  -0.0051 90  TYR   A CA  
678  C C   . TYR   A 84  ? 0.3486 0.2346 0.4684 0.0354  0.1127  -0.0023 90  TYR   A C   
679  O O   . TYR   A 84  ? 0.3645 0.2516 0.4798 0.0348  0.1151  -0.0067 90  TYR   A O   
680  C CB  . TYR   A 84  ? 0.3095 0.2204 0.4124 0.0342  0.0859  0.0068  90  TYR   A CB  
681  C CG  . TYR   A 84  ? 0.2764 0.1953 0.3654 0.0301  0.0730  0.0063  90  TYR   A CG  
682  C CD1 . TYR   A 84  ? 0.2665 0.1845 0.3585 0.0297  0.0708  0.0094  90  TYR   A CD1 
683  C CD2 . TYR   A 84  ? 0.2576 0.1842 0.3316 0.0269  0.0638  0.0027  90  TYR   A CD2 
684  C CE1 . TYR   A 84  ? 0.2518 0.1771 0.3322 0.0261  0.0599  0.0087  90  TYR   A CE1 
685  C CE2 . TYR   A 84  ? 0.2450 0.1784 0.3088 0.0239  0.0534  0.0026  90  TYR   A CE2 
686  C CZ  . TYR   A 84  ? 0.2400 0.1724 0.3067 0.0233  0.0518  0.0050  90  TYR   A CZ  
687  O OH  . TYR   A 84  ? 0.2147 0.1537 0.2722 0.0204  0.0425  0.0045  90  TYR   A OH  
688  N N   . PRO   A 85  ? 0.3645 0.2474 0.5058 0.0419  0.1199  0.0073  91  PRO   A N   
689  C CA  . PRO   A 85  ? 0.3851 0.2656 0.5481 0.0494  0.1321  0.0138  91  PRO   A CA  
690  C C   . PRO   A 85  ? 0.4015 0.3023 0.5701 0.0551  0.1225  0.0268  91  PRO   A C   
691  O O   . PRO   A 85  ? 0.3979 0.3127 0.5546 0.0532  0.1077  0.0307  91  PRO   A O   
692  C CB  . PRO   A 85  ? 0.4023 0.2760 0.5877 0.0547  0.1403  0.0232  91  PRO   A CB  
693  C CG  . PRO   A 85  ? 0.3986 0.2820 0.5764 0.0529  0.1266  0.0290  91  PRO   A CG  
694  C CD  . PRO   A 85  ? 0.3617 0.2450 0.5109 0.0435  0.1171  0.0150  91  PRO   A CD  
695  N N   . ALA   A 86  ? 0.4066 0.3100 0.5943 0.0620  0.1311  0.0343  92  ALA   A N   
696  C CA  . ALA   A 86  ? 0.3925 0.3168 0.5876 0.0669  0.1225  0.0481  92  ALA   A CA  
697  C C   . ALA   A 86  ? 0.3692 0.3064 0.5761 0.0705  0.1146  0.0645  92  ALA   A C   
698  O O   . ALA   A 86  ? 0.3820 0.3117 0.6046 0.0737  0.1219  0.0699  92  ALA   A O   
699  C CB  . ALA   A 86  ? 0.3899 0.3141 0.6063 0.0737  0.1349  0.0538  92  ALA   A CB  
700  N N   . ARG   A 87  ? 0.3479 0.3031 0.5435 0.0680  0.0994  0.0701  93  ARG   A N   
701  C CA  . ARG   A 87  ? 0.3175 0.2859 0.5198 0.0689  0.0911  0.0837  93  ARG   A CA  
702  C C   . ARG   A 87  ? 0.2926 0.2826 0.4843 0.0659  0.0769  0.0897  93  ARG   A C   
703  O O   . ARG   A 87  ? 0.3224 0.3142 0.5008 0.0631  0.0737  0.0819  93  ARG   A O   
704  C CB  . ARG   A 87  ? 0.3362 0.2938 0.5243 0.0636  0.0880  0.0745  93  ARG   A CB  
705  C CG  . ARG   A 87  ? 0.3393 0.2993 0.4996 0.0561  0.0766  0.0625  93  ARG   A CG  
706  C CD  . ARG   A 87  ? 0.3227 0.2714 0.4701 0.0509  0.0750  0.0525  93  ARG   A CD  
707  N NE  . ARG   A 87  ? 0.3091 0.2646 0.4362 0.0450  0.0627  0.0471  93  ARG   A NE  
708  C CZ  . ARG   A 87  ? 0.3063 0.2652 0.4179 0.0416  0.0569  0.0398  93  ARG   A CZ  
709  N NH1 . ARG   A 87  ? 0.3282 0.2862 0.4399 0.0429  0.0607  0.0371  93  ARG   A NH1 
710  N NH2 . ARG   A 87  ? 0.2415 0.2047 0.3381 0.0369  0.0476  0.0355  93  ARG   A NH2 
711  N N   . TYR   A 88  ? 0.2761 0.2817 0.4728 0.0654  0.0690  0.1026  94  TYR   A N   
712  C CA  . TYR   A 88  ? 0.2805 0.3056 0.4653 0.0604  0.0561  0.1068  94  TYR   A CA  
713  C C   . TYR   A 88  ? 0.2553 0.2748 0.4170 0.0536  0.0487  0.0944  94  TYR   A C   
714  O O   . TYR   A 88  ? 0.2685 0.2810 0.4295 0.0526  0.0490  0.0930  94  TYR   A O   
715  C CB  . TYR   A 88  ? 0.2808 0.3273 0.4809 0.0613  0.0513  0.1266  94  TYR   A CB  
716  C CG  . TYR   A 88  ? 0.2825 0.3415 0.5051 0.0671  0.0558  0.1414  94  TYR   A CG  
717  C CD1 . TYR   A 88  ? 0.2899 0.3646 0.5084 0.0649  0.0506  0.1443  94  TYR   A CD1 
718  C CD2 . TYR   A 88  ? 0.2896 0.3432 0.5385 0.0752  0.0666  0.1518  94  TYR   A CD2 
719  C CE1 . TYR   A 88  ? 0.3008 0.3874 0.5406 0.0703  0.0551  0.1577  94  TYR   A CE1 
720  C CE2 . TYR   A 88  ? 0.3004 0.3650 0.5722 0.0814  0.0720  0.1655  94  TYR   A CE2 
721  C CZ  . TYR   A 88  ? 0.3085 0.3905 0.5756 0.0789  0.0657  0.1687  94  TYR   A CZ  
722  O OH  . TYR   A 88  ? 0.3435 0.4387 0.6335 0.0846  0.0704  0.1830  94  TYR   A OH  
723  N N   . GLN   A 89  ? 0.2247 0.2476 0.3684 0.0489  0.0422  0.0859  95  GLN   A N   
724  C CA  . GLN   A 89  ? 0.2031 0.2229 0.3264 0.0427  0.0350  0.0752  95  GLN   A CA  
725  C C   . GLN   A 89  ? 0.1871 0.2264 0.3053 0.0379  0.0258  0.0823  95  GLN   A C   
726  O O   . GLN   A 89  ? 0.1865 0.2382 0.3067 0.0373  0.0237  0.0876  95  GLN   A O   
727  C CB  . GLN   A 89  ? 0.2094 0.2172 0.3175 0.0406  0.0358  0.0606  95  GLN   A CB  
728  C CG  . GLN   A 89  ? 0.1974 0.2032 0.2878 0.0351  0.0288  0.0517  95  GLN   A CG  
729  C CD  . GLN   A 89  ? 0.1999 0.1924 0.2775 0.0331  0.0302  0.0384  95  GLN   A CD  
730  O OE1 . GLN   A 89  ? 0.2199 0.2003 0.2996 0.0345  0.0371  0.0332  95  GLN   A OE1 
731  N NE2 . GLN   A 89  ? 0.1859 0.1809 0.2500 0.0291  0.0238  0.0329  95  GLN   A NE2 
732  N N   . SER   A 90  ? 0.1602 0.2025 0.2711 0.0337  0.0207  0.0816  96  SER   A N   
733  C CA  . SER   A 90  ? 0.1682 0.2285 0.2730 0.0275  0.0131  0.0869  96  SER   A CA  
734  C C   . SER   A 90  ? 0.1648 0.2219 0.2505 0.0219  0.0089  0.0743  96  SER   A C   
735  O O   . SER   A 90  ? 0.1790 0.2204 0.2566 0.0230  0.0106  0.0627  96  SER   A O   
736  C CB  . SER   A 90  ? 0.2096 0.2764 0.3186 0.0254  0.0110  0.0943  96  SER   A CB  
737  O OG  . SER   A 90  ? 0.2540 0.3063 0.3542 0.0246  0.0116  0.0837  96  SER   A OG  
738  N N   . HIS   A 91  ? 0.1697 0.2423 0.2491 0.0155  0.0037  0.0772  97  HIS   A N   
739  C CA  . HIS   A 91  ? 0.1630 0.2339 0.2262 0.0095  0.0005  0.0666  97  HIS   A CA  
740  C C   . HIS   A 91  ? 0.1660 0.2249 0.2239 0.0123  0.0027  0.0576  97  HIS   A C   
741  O O   . HIS   A 91  ? 0.1736 0.2230 0.2205 0.0104  0.0020  0.0471  97  HIS   A O   
742  C CB  . HIS   A 91  ? 0.1864 0.2501 0.2418 0.0070  -0.0005 0.0595  97  HIS   A CB  
743  C CG  . HIS   A 91  ? 0.1934 0.2698 0.2522 0.0029  -0.0028 0.0678  97  HIS   A CG  
744  N ND1 . HIS   A 91  ? 0.2314 0.3200 0.2813 -0.0059 -0.0060 0.0672  97  HIS   A ND1 
745  C CD2 . HIS   A 91  ? 0.2204 0.2988 0.2904 0.0060  -0.0017 0.0767  97  HIS   A CD2 
746  C CE1 . HIS   A 91  ? 0.2246 0.3232 0.2794 -0.0083 -0.0075 0.0757  97  HIS   A CE1 
747  N NE2 . HIS   A 91  ? 0.2352 0.3281 0.3027 -0.0009 -0.0052 0.0823  97  HIS   A NE2 
748  N N   . LEU   A 92  ? 0.1467 0.2072 0.2128 0.0164  0.0054  0.0622  98  LEU   A N   
749  C CA  . LEU   A 92  ? 0.1599 0.2102 0.2217 0.0188  0.0078  0.0547  98  LEU   A CA  
750  C C   . LEU   A 92  ? 0.1543 0.2161 0.2123 0.0147  0.0054  0.0565  98  LEU   A C   
751  O O   . LEU   A 92  ? 0.1613 0.2392 0.2263 0.0129  0.0037  0.0667  98  LEU   A O   
752  C CB  . LEU   A 92  ? 0.1740 0.2172 0.2482 0.0258  0.0143  0.0577  98  LEU   A CB  
753  C CG  . LEU   A 92  ? 0.2212 0.2532 0.2903 0.0276  0.0177  0.0492  98  LEU   A CG  
754  C CD1 . LEU   A 92  ? 0.2286 0.2466 0.2859 0.0260  0.0172  0.0379  98  LEU   A CD1 
755  C CD2 . LEU   A 92  ? 0.2575 0.2833 0.3400 0.0337  0.0259  0.0521  98  LEU   A CD2 
756  N N   . MET   A 93  ? 0.1548 0.2089 0.2019 0.0129  0.0049  0.0472  99  MET   A N   
757  C CA  . MET   A 93  ? 0.1447 0.2072 0.1870 0.0086  0.0032  0.0473  99  MET   A CA  
758  C C   . MET   A 93  ? 0.1649 0.2188 0.2076 0.0126  0.0064  0.0437  99  MET   A C   
759  O O   . MET   A 93  ? 0.1783 0.2179 0.2160 0.0148  0.0081  0.0359  99  MET   A O   
760  C CB  . MET   A 93  ? 0.1571 0.2167 0.1864 0.0022  0.0007  0.0391  99  MET   A CB  
761  C CG  . MET   A 93  ? 0.1750 0.2428 0.2027 -0.0030 -0.0016 0.0413  99  MET   A CG  
762  S SD  . MET   A 93  ? 0.2073 0.2692 0.2218 -0.0101 -0.0021 0.0305  99  MET   A SD  
763  C CE  . MET   A 93  ? 0.2558 0.2983 0.2698 -0.0031 -0.0004 0.0231  99  MET   A CE  
764  N N   . LEU   A 94  ? 0.1544 0.2177 0.2021 0.0127  0.0072  0.0491  100 LEU   A N   
765  C CA  . LEU   A 94  ? 0.1670 0.2231 0.2150 0.0160  0.0108  0.0456  100 LEU   A CA  
766  C C   . LEU   A 94  ? 0.1594 0.2178 0.1977 0.0110  0.0086  0.0416  100 LEU   A C   
767  O O   . LEU   A 94  ? 0.1666 0.2371 0.2022 0.0052  0.0053  0.0448  100 LEU   A O   
768  C CB  . LEU   A 94  ? 0.1918 0.2553 0.2552 0.0210  0.0152  0.0547  100 LEU   A CB  
769  C CG  . LEU   A 94  ? 0.2487 0.3081 0.3248 0.0270  0.0196  0.0592  100 LEU   A CG  
770  C CD1 . LEU   A 94  ? 0.2581 0.3232 0.3515 0.0327  0.0258  0.0677  100 LEU   A CD1 
771  C CD2 . LEU   A 94  ? 0.2842 0.3245 0.3544 0.0292  0.0232  0.0489  100 LEU   A CD2 
772  N N   . ALA   A 95  ? 0.1602 0.2079 0.1933 0.0125  0.0108  0.0351  101 ALA   A N   
773  C CA  . ALA   A 95  ? 0.1567 0.2052 0.1817 0.0083  0.0094  0.0317  101 ALA   A CA  
774  C C   . ALA   A 95  ? 0.1596 0.2023 0.1858 0.0117  0.0135  0.0297  101 ALA   A C   
775  O O   . ALA   A 95  ? 0.1693 0.2042 0.1995 0.0162  0.0175  0.0281  101 ALA   A O   
776  C CB  . ALA   A 95  ? 0.1711 0.2093 0.1846 0.0050  0.0071  0.0238  101 ALA   A CB  
777  N N   . VAL   A 96  ? 0.1536 0.1995 0.1755 0.0087  0.0131  0.0290  102 VAL   A N   
778  C CA  . VAL   A 96  ? 0.1556 0.1962 0.1760 0.0103  0.0166  0.0261  102 VAL   A CA  
779  C C   . VAL   A 96  ? 0.1874 0.2156 0.1959 0.0081  0.0148  0.0184  102 VAL   A C   
780  O O   . VAL   A 96  ? 0.2238 0.2512 0.2258 0.0041  0.0114  0.0167  102 VAL   A O   
781  C CB  . VAL   A 96  ? 0.1539 0.2051 0.1755 0.0075  0.0165  0.0297  102 VAL   A CB  
782  C CG1 . VAL   A 96  ? 0.1817 0.2272 0.2000 0.0082  0.0200  0.0260  102 VAL   A CG1 
783  C CG2 . VAL   A 96  ? 0.1608 0.2267 0.1960 0.0097  0.0178  0.0392  102 VAL   A CG2 
784  N N   . GLY   A 97  ? 0.2025 0.2218 0.2096 0.0104  0.0176  0.0146  103 GLY   A N   
785  C CA  . GLY   A 97  ? 0.2193 0.2293 0.2166 0.0081  0.0155  0.0093  103 GLY   A CA  
786  C C   . GLY   A 97  ? 0.2139 0.2169 0.2099 0.0093  0.0193  0.0055  103 GLY   A C   
787  O O   . GLY   A 97  ? 0.2268 0.2291 0.2298 0.0124  0.0238  0.0058  103 GLY   A O   
788  N N   . HIS   A 98  ? 0.2352 0.2331 0.2221 0.0061  0.0180  0.0019  104 HIS   A N   
789  C CA  . HIS   A 98  ? 0.2594 0.2516 0.2426 0.0048  0.0215  -0.0026 104 HIS   A CA  
790  C C   . HIS   A 98  ? 0.2497 0.2371 0.2334 0.0055  0.0205  -0.0044 104 HIS   A C   
791  O O   . HIS   A 98  ? 0.2367 0.2240 0.2191 0.0052  0.0152  -0.0030 104 HIS   A O   
792  C CB  . HIS   A 98  ? 0.2597 0.2505 0.2325 -0.0002 0.0197  -0.0047 104 HIS   A CB  
793  C CG  . HIS   A 98  ? 0.2641 0.2507 0.2313 -0.0037 0.0237  -0.0100 104 HIS   A CG  
794  N ND1 . HIS   A 98  ? 0.2639 0.2491 0.2331 -0.0036 0.0319  -0.0136 104 HIS   A ND1 
795  C CD2 . HIS   A 98  ? 0.2832 0.2670 0.2437 -0.0077 0.0215  -0.0125 104 HIS   A CD2 
796  C CE1 . HIS   A 98  ? 0.2841 0.2645 0.2464 -0.0083 0.0348  -0.0193 104 HIS   A CE1 
797  N NE2 . HIS   A 98  ? 0.2869 0.2674 0.2433 -0.0113 0.0281  -0.0184 104 HIS   A NE2 
798  N N   . SER   A 99  ? 0.2610 0.2444 0.2472 0.0062  0.0260  -0.0075 105 SER   A N   
799  C CA  . SER   A 99  ? 0.2309 0.2092 0.2162 0.0055  0.0260  -0.0102 105 SER   A CA  
800  C C   . SER   A 99  ? 0.2571 0.2292 0.2400 0.0027  0.0334  -0.0164 105 SER   A C   
801  O O   . SER   A 99  ? 0.2848 0.2562 0.2722 0.0041  0.0406  -0.0176 105 SER   A O   
802  C CB  . SER   A 99  ? 0.2595 0.2389 0.2537 0.0099  0.0245  -0.0065 105 SER   A CB  
803  O OG  . SER   A 99  ? 0.2614 0.2424 0.2664 0.0141  0.0303  -0.0038 105 SER   A OG  
804  N N   . GLU   A 100 ? 0.2392 0.2070 0.2160 -0.0014 0.0324  -0.0204 106 GLU   A N   
805  C CA  . GLU   A 100 ? 0.2528 0.2137 0.2253 -0.0062 0.0392  -0.0277 106 GLU   A CA  
806  C C   . GLU   A 100 ? 0.2762 0.2334 0.2515 -0.0058 0.0380  -0.0283 106 GLU   A C   
807  O O   . GLU   A 100 ? 0.2641 0.2248 0.2421 -0.0029 0.0308  -0.0234 106 GLU   A O   
808  C CB  . GLU   A 100 ? 0.2586 0.2213 0.2169 -0.0153 0.0377  -0.0320 106 GLU   A CB  
809  C CG  . GLU   A 100 ? 0.2789 0.2450 0.2347 -0.0159 0.0397  -0.0316 106 GLU   A CG  
810  C CD  . GLU   A 100 ? 0.2944 0.2646 0.2362 -0.0251 0.0372  -0.0339 106 GLU   A CD  
811  O OE1 . GLU   A 100 ? 0.3709 0.3395 0.3039 -0.0330 0.0390  -0.0393 106 GLU   A OE1 
812  O OE2 . GLU   A 100 ? 0.2894 0.2650 0.2287 -0.0252 0.0338  -0.0300 106 GLU   A OE2 
813  N N   . PRO   A 101 ? 0.2875 0.2369 0.2634 -0.0083 0.0460  -0.0344 107 PRO   A N   
814  C CA  . PRO   A 101 ? 0.2897 0.2351 0.2700 -0.0072 0.0456  -0.0344 107 PRO   A CA  
815  C C   . PRO   A 101 ? 0.2845 0.2349 0.2582 -0.0104 0.0355  -0.0322 107 PRO   A C   
816  O O   . PRO   A 101 ? 0.2842 0.2361 0.2644 -0.0059 0.0312  -0.0276 107 PRO   A O   
817  C CB  . PRO   A 101 ? 0.3095 0.2446 0.2886 -0.0121 0.0570  -0.0432 107 PRO   A CB  
818  C CG  . PRO   A 101 ? 0.3285 0.2619 0.3113 -0.0102 0.0653  -0.0449 107 PRO   A CG  
819  C CD  . PRO   A 101 ? 0.3016 0.2445 0.2766 -0.0115 0.0574  -0.0416 107 PRO   A CD  
820  N N   . GLY   A 102 ? 0.2707 0.2252 0.2327 -0.0178 0.0314  -0.0342 108 GLY   A N   
821  C CA  . GLY   A 102 ? 0.2526 0.2133 0.2102 -0.0208 0.0223  -0.0308 108 GLY   A CA  
822  C C   . GLY   A 102 ? 0.2229 0.1900 0.1853 -0.0151 0.0145  -0.0230 108 GLY   A C   
823  O O   . GLY   A 102 ? 0.2226 0.1946 0.1844 -0.0162 0.0077  -0.0192 108 GLY   A O   
824  N N   . ASP   A 103 ? 0.2114 0.1787 0.1793 -0.0093 0.0159  -0.0204 109 ASP   A N   
825  C CA  . ASP   A 103 ? 0.2076 0.1794 0.1804 -0.0045 0.0102  -0.0142 109 ASP   A CA  
826  C C   . ASP   A 103 ? 0.1903 0.1614 0.1710 0.0000  0.0090  -0.0120 109 ASP   A C   
827  O O   . ASP   A 103 ? 0.1824 0.1569 0.1665 0.0026  0.0048  -0.0081 109 ASP   A O   
828  C CB  . ASP   A 103 ? 0.1909 0.1642 0.1658 -0.0015 0.0121  -0.0124 109 ASP   A CB  
829  C CG  . ASP   A 103 ? 0.2009 0.1766 0.1679 -0.0060 0.0113  -0.0130 109 ASP   A CG  
830  O OD1 . ASP   A 103 ? 0.1973 0.1761 0.1595 -0.0097 0.0064  -0.0112 109 ASP   A OD1 
831  O OD2 . ASP   A 103 ? 0.2109 0.1863 0.1774 -0.0057 0.0158  -0.0144 109 ASP   A OD2 
832  N N   . CYS   A 104 ? 0.1868 0.1533 0.1709 0.0007  0.0134  -0.0145 110 CYS   A N   
833  C CA  . CYS   A 104 ? 0.1908 0.1575 0.1821 0.0042  0.0120  -0.0119 110 CYS   A CA  
834  C C   . CYS   A 104 ? 0.1858 0.1558 0.1753 0.0026  0.0058  -0.0103 110 CYS   A C   
835  O O   . CYS   A 104 ? 0.1954 0.1664 0.1793 -0.0020 0.0035  -0.0118 110 CYS   A O   
836  C CB  . CYS   A 104 ? 0.2091 0.1697 0.2038 0.0040  0.0178  -0.0148 110 CYS   A CB  
837  S SG  . CYS   A 104 ? 0.2272 0.1848 0.2312 0.0088  0.0261  -0.0135 110 CYS   A SG  
838  N N   . GLY   A 105 ? 0.1705 0.1437 0.1652 0.0060  0.0032  -0.0068 111 GLY   A N   
839  C CA  . GLY   A 105 ? 0.1704 0.1463 0.1661 0.0054  -0.0013 -0.0051 111 GLY   A CA  
840  C C   . GLY   A 105 ? 0.1654 0.1444 0.1616 0.0063  -0.0040 -0.0024 111 GLY   A C   
841  O O   . GLY   A 105 ? 0.1778 0.1586 0.1776 0.0070  -0.0061 -0.0006 111 GLY   A O   
842  N N   . GLY   A 106 ? 0.1716 0.1508 0.1648 0.0061  -0.0030 -0.0023 112 GLY   A N   
843  C CA  . GLY   A 106 ? 0.1619 0.1428 0.1559 0.0066  -0.0047 0.0001  112 GLY   A CA  
844  C C   . GLY   A 106 ? 0.1466 0.1285 0.1451 0.0086  -0.0037 0.0006  112 GLY   A C   
845  O O   . GLY   A 106 ? 0.1534 0.1366 0.1530 0.0096  -0.0017 0.0002  112 GLY   A O   
846  N N   . ILE   A 107 ? 0.1513 0.1333 0.1528 0.0086  -0.0044 0.0017  113 ILE   A N   
847  C CA  . ILE   A 107 ? 0.1516 0.1345 0.1558 0.0086  -0.0025 0.0007  113 ILE   A CA  
848  C C   . ILE   A 107 ? 0.1430 0.1273 0.1449 0.0073  -0.0008 0.0004  113 ILE   A C   
849  O O   . ILE   A 107 ? 0.1474 0.1303 0.1477 0.0068  -0.0009 0.0012  113 ILE   A O   
850  C CB  . ILE   A 107 ? 0.1530 0.1341 0.1626 0.0089  -0.0021 0.0011  113 ILE   A CB  
851  C CG1 . ILE   A 107 ? 0.1690 0.1510 0.1818 0.0097  -0.0033 0.0012  113 ILE   A CG1 
852  C CG2 . ILE   A 107 ? 0.1674 0.1480 0.1786 0.0072  0.0016  -0.0013 113 ILE   A CG2 
853  C CD1 . ILE   A 107 ? 0.1994 0.1805 0.2194 0.0106  -0.0028 0.0028  113 ILE   A CD1 
854  N N   . LEU   A 108 ? 0.1342 0.1226 0.1362 0.0061  0.0005  -0.0001 114 LEU   A N   
855  C CA  . LEU   A 108 ? 0.1338 0.1259 0.1339 0.0031  0.0021  -0.0005 114 LEU   A CA  
856  C C   . LEU   A 108 ? 0.1345 0.1259 0.1356 -0.0001 0.0044  -0.0033 114 LEU   A C   
857  O O   . LEU   A 108 ? 0.1457 0.1386 0.1486 -0.0003 0.0046  -0.0040 114 LEU   A O   
858  C CB  . LEU   A 108 ? 0.1379 0.1377 0.1381 0.0027  0.0019  0.0021  114 LEU   A CB  
859  C CG  . LEU   A 108 ? 0.1434 0.1506 0.1416 -0.0021 0.0028  0.0027  114 LEU   A CG  
860  C CD1 . LEU   A 108 ? 0.1628 0.1691 0.1585 -0.0029 0.0033  0.0026  114 LEU   A CD1 
861  C CD2 . LEU   A 108 ? 0.1684 0.1862 0.1695 -0.0025 0.0020  0.0077  114 LEU   A CD2 
862  N N   . ARG   A 109 ? 0.1470 0.1359 0.1471 -0.0030 0.0069  -0.0054 115 ARG   A N   
863  C CA  . ARG   A 109 ? 0.1471 0.1334 0.1485 -0.0067 0.0113  -0.0096 115 ARG   A CA  
864  C C   . ARG   A 109 ? 0.1618 0.1499 0.1588 -0.0130 0.0144  -0.0124 115 ARG   A C   
865  O O   . ARG   A 109 ? 0.1628 0.1523 0.1572 -0.0135 0.0133  -0.0107 115 ARG   A O   
866  C CB  . ARG   A 109 ? 0.1645 0.1420 0.1724 -0.0034 0.0131  -0.0097 115 ARG   A CB  
867  C CG  . ARG   A 109 ? 0.1765 0.1494 0.1853 -0.0026 0.0135  -0.0079 115 ARG   A CG  
868  C CD  . ARG   A 109 ? 0.1943 0.1605 0.2123 0.0008  0.0153  -0.0058 115 ARG   A CD  
869  N NE  . ARG   A 109 ? 0.2049 0.1735 0.2250 0.0051  0.0101  -0.0012 115 ARG   A NE  
870  C CZ  . ARG   A 109 ? 0.2001 0.1685 0.2271 0.0075  0.0100  0.0001  115 ARG   A CZ  
871  N NH1 . ARG   A 109 ? 0.2040 0.1696 0.2363 0.0066  0.0153  -0.0033 115 ARG   A NH1 
872  N NH2 . ARG   A 109 ? 0.2101 0.1817 0.2381 0.0100  0.0051  0.0045  115 ARG   A NH2 
873  N N   . CYS   A 110 ? 0.1812 0.1694 0.1771 -0.0187 0.0190  -0.0173 116 CYS   A N   
874  C CA  . CYS   A 110 ? 0.2248 0.2137 0.2158 -0.0268 0.0236  -0.0218 116 CYS   A CA  
875  C C   . CYS   A 110 ? 0.2647 0.2429 0.2599 -0.0290 0.0314  -0.0280 116 CYS   A C   
876  O O   . CYS   A 110 ? 0.2618 0.2335 0.2647 -0.0232 0.0323  -0.0271 116 CYS   A O   
877  C CB  . CYS   A 110 ? 0.2308 0.2328 0.2152 -0.0341 0.0223  -0.0219 116 CYS   A CB  
878  S SG  . CYS   A 110 ? 0.2299 0.2350 0.2142 -0.0377 0.0249  -0.0254 116 CYS   A SG  
879  N N   . GLN   A 111 ? 0.3157 0.2920 0.3066 -0.0379 0.0381  -0.0345 117 GLN   A N   
880  C CA  . GLN   A 111 ? 0.3413 0.3058 0.3377 -0.0402 0.0478  -0.0413 117 GLN   A CA  
881  C C   . GLN   A 111 ? 0.3364 0.3015 0.3355 -0.0407 0.0507  -0.0445 117 GLN   A C   
882  O O   . GLN   A 111 ? 0.3782 0.3330 0.3859 -0.0388 0.0580  -0.0480 117 GLN   A O   
883  C CB  . GLN   A 111 ? 0.3791 0.3408 0.3692 -0.0516 0.0559  -0.0494 117 GLN   A CB  
884  C CG  . GLN   A 111 ? 0.4614 0.4372 0.4394 -0.0627 0.0548  -0.0527 117 GLN   A CG  
885  C CD  . GLN   A 111 ? 0.5376 0.5230 0.5077 -0.0676 0.0502  -0.0498 117 GLN   A CD  
886  O OE1 . GLN   A 111 ? 0.5511 0.5407 0.5127 -0.0798 0.0545  -0.0555 117 GLN   A OE1 
887  N NE2 . GLN   A 111 ? 0.5298 0.5188 0.5027 -0.0589 0.0419  -0.0411 117 GLN   A NE2 
888  N N   . HIS   A 112 ? 0.2845 0.2619 0.2776 -0.0425 0.0451  -0.0424 118 HIS   A N   
889  C CA  . HIS   A 112 ? 0.2690 0.2487 0.2633 -0.0439 0.0474  -0.0452 118 HIS   A CA  
890  C C   . HIS   A 112 ? 0.2623 0.2399 0.2654 -0.0334 0.0429  -0.0395 118 HIS   A C   
891  O O   . HIS   A 112 ? 0.2842 0.2618 0.2905 -0.0333 0.0453  -0.0415 118 HIS   A O   
892  C CB  . HIS   A 112 ? 0.2531 0.2482 0.2370 -0.0524 0.0440  -0.0449 118 HIS   A CB  
893  C CG  . HIS   A 112 ? 0.2707 0.2705 0.2448 -0.0647 0.0480  -0.0502 118 HIS   A CG  
894  N ND1 . HIS   A 112 ? 0.2841 0.2946 0.2522 -0.0675 0.0421  -0.0452 118 HIS   A ND1 
895  C CD2 . HIS   A 112 ? 0.3158 0.3108 0.2858 -0.0752 0.0582  -0.0605 118 HIS   A CD2 
896  C CE1 . HIS   A 112 ? 0.3250 0.3379 0.2849 -0.0800 0.0478  -0.0520 118 HIS   A CE1 
897  N NE2 . HIS   A 112 ? 0.3482 0.3513 0.3083 -0.0853 0.0579  -0.0619 118 HIS   A NE2 
898  N N   . GLY   A 113 ? 0.2378 0.2150 0.2437 -0.0255 0.0359  -0.0324 119 GLY   A N   
899  C CA  . GLY   A 113 ? 0.2180 0.1943 0.2307 -0.0172 0.0313  -0.0272 119 GLY   A CA  
900  C C   . GLY   A 113 ? 0.1874 0.1700 0.1966 -0.0132 0.0228  -0.0208 119 GLY   A C   
901  O O   . GLY   A 113 ? 0.1957 0.1814 0.1999 -0.0147 0.0206  -0.0192 119 GLY   A O   
902  N N   . VAL   A 114 ? 0.1642 0.1483 0.1768 -0.0084 0.0189  -0.0174 120 VAL   A N   
903  C CA  . VAL   A 114 ? 0.1629 0.1510 0.1734 -0.0046 0.0125  -0.0122 120 VAL   A CA  
904  C C   . VAL   A 114 ? 0.1458 0.1432 0.1511 -0.0081 0.0107  -0.0108 120 VAL   A C   
905  O O   . VAL   A 114 ? 0.1551 0.1572 0.1598 -0.0115 0.0119  -0.0121 120 VAL   A O   
906  C CB  . VAL   A 114 ? 0.1618 0.1479 0.1776 0.0005  0.0098  -0.0097 120 VAL   A CB  
907  C CG1 . VAL   A 114 ? 0.1743 0.1632 0.1876 0.0031  0.0049  -0.0059 120 VAL   A CG1 
908  C CG2 . VAL   A 114 ? 0.1782 0.1580 0.2004 0.0039  0.0105  -0.0084 120 VAL   A CG2 
909  N N   . VAL   A 115 ? 0.1393 0.1404 0.1422 -0.0073 0.0079  -0.0074 121 VAL   A N   
910  C CA  . VAL   A 115 ? 0.1510 0.1623 0.1515 -0.0100 0.0061  -0.0038 121 VAL   A CA  
911  C C   . VAL   A 115 ? 0.1507 0.1630 0.1550 -0.0048 0.0031  0.0010  121 VAL   A C   
912  O O   . VAL   A 115 ? 0.1600 0.1797 0.1657 -0.0059 0.0021  0.0047  121 VAL   A O   
913  C CB  . VAL   A 115 ? 0.1581 0.1735 0.1554 -0.0124 0.0058  -0.0024 121 VAL   A CB  
914  C CG1 . VAL   A 115 ? 0.1806 0.2086 0.1785 -0.0140 0.0034  0.0040  121 VAL   A CG1 
915  C CG2 . VAL   A 115 ? 0.1974 0.2117 0.1905 -0.0191 0.0097  -0.0078 121 VAL   A CG2 
916  N N   . GLY   A 116 ? 0.1514 0.1566 0.1574 0.0004  0.0020  0.0013  122 GLY   A N   
917  C CA  . GLY   A 116 ? 0.1587 0.1630 0.1678 0.0044  0.0007  0.0044  122 GLY   A CA  
918  C C   . GLY   A 116 ? 0.1511 0.1480 0.1596 0.0076  0.0002  0.0031  122 GLY   A C   
919  O O   . GLY   A 116 ? 0.1532 0.1462 0.1600 0.0072  0.0001  0.0008  122 GLY   A O   
920  N N   . ILE   A 117 ? 0.1494 0.1444 0.1597 0.0101  0.0005  0.0045  123 ILE   A N   
921  C CA  . ILE   A 117 ? 0.1434 0.1322 0.1515 0.0113  0.0004  0.0026  123 ILE   A CA  
922  C C   . ILE   A 117 ? 0.1461 0.1346 0.1550 0.0129  0.0028  0.0038  123 ILE   A C   
923  O O   . ILE   A 117 ? 0.1587 0.1505 0.1727 0.0143  0.0047  0.0071  123 ILE   A O   
924  C CB  . ILE   A 117 ? 0.1562 0.1409 0.1647 0.0114  -0.0003 0.0009  123 ILE   A CB  
925  C CG1 . ILE   A 117 ? 0.1746 0.1598 0.1872 0.0124  0.0011  0.0024  123 ILE   A CG1 
926  C CG2 . ILE   A 117 ? 0.1715 0.1563 0.1803 0.0105  -0.0024 0.0000  123 ILE   A CG2 
927  C CD1 . ILE   A 117 ? 0.1872 0.1677 0.1995 0.0115  0.0009  0.0002  123 ILE   A CD1 
928  N N   . VAL   A 118 ? 0.1468 0.1319 0.1519 0.0125  0.0034  0.0018  124 VAL   A N   
929  C CA  . VAL   A 118 ? 0.1537 0.1374 0.1599 0.0137  0.0071  0.0018  124 VAL   A CA  
930  C C   . VAL   A 118 ? 0.1658 0.1453 0.1761 0.0149  0.0106  0.0012  124 VAL   A C   
931  O O   . VAL   A 118 ? 0.1709 0.1463 0.1787 0.0132  0.0097  -0.0017 124 VAL   A O   
932  C CB  . VAL   A 118 ? 0.1607 0.1411 0.1603 0.0116  0.0073  -0.0014 124 VAL   A CB  
933  C CG1 . VAL   A 118 ? 0.1755 0.1534 0.1762 0.0122  0.0127  -0.0027 124 VAL   A CG1 
934  C CG2 . VAL   A 118 ? 0.1660 0.1496 0.1626 0.0105  0.0047  -0.0001 124 VAL   A CG2 
935  N N   . SER   A 119 ? 0.1631 0.1441 0.1809 0.0177  0.0148  0.0045  125 SER   A N   
936  C CA  . SER   A 119 ? 0.1792 0.1551 0.2035 0.0194  0.0196  0.0046  125 SER   A CA  
937  C C   . SER   A 119 ? 0.2033 0.1758 0.2332 0.0216  0.0269  0.0047  125 SER   A C   
938  O O   . SER   A 119 ? 0.2311 0.1956 0.2641 0.0217  0.0327  0.0017  125 SER   A O   
939  C CB  . SER   A 119 ? 0.1813 0.1631 0.2132 0.0213  0.0181  0.0109  125 SER   A CB  
940  O OG  . SER   A 119 ? 0.1912 0.1684 0.2317 0.0235  0.0231  0.0128  125 SER   A OG  
941  N N   . THR   A 120 ? 0.1872 0.1654 0.2192 0.0230  0.0275  0.0075  126 THR   A N   
942  C CA  . THR   A 120 ? 0.2080 0.1836 0.2479 0.0257  0.0356  0.0082  126 THR   A CA  
943  C C   . THR   A 120 ? 0.2409 0.2198 0.2749 0.0243  0.0350  0.0065  126 THR   A C   
944  O O   . THR   A 120 ? 0.2175 0.2008 0.2432 0.0217  0.0284  0.0061  126 THR   A O   
945  C CB  . THR   A 120 ? 0.2163 0.1997 0.2723 0.0308  0.0380  0.0185  126 THR   A CB  
946  O OG1 . THR   A 120 ? 0.2165 0.2126 0.2731 0.0308  0.0330  0.0245  126 THR   A OG1 
947  C CG2 . THR   A 120 ? 0.2300 0.2134 0.2926 0.0322  0.0372  0.0227  126 THR   A CG2 
948  N N   . GLY   A 121 ? 0.2524 0.2295 0.2922 0.0261  0.0424  0.0061  127 GLY   A N   
949  C CA  . GLY   A 121 ? 0.2577 0.2391 0.2933 0.0249  0.0421  0.0056  127 GLY   A CA  
950  C C   . GLY   A 121 ? 0.2806 0.2574 0.3224 0.0264  0.0524  0.0030  127 GLY   A C   
951  O O   . GLY   A 121 ? 0.3020 0.2718 0.3527 0.0288  0.0603  0.0021  127 GLY   A O   
952  N N   . GLY   A 122 ? 0.2805 0.2594 0.3160 0.0241  0.0527  0.0005  128 GLY   A N   
953  C CA  . GLY   A 122 ? 0.2842 0.2590 0.3240 0.0246  0.0630  -0.0031 128 GLY   A CA  
954  C C   . GLY   A 122 ? 0.2883 0.2735 0.3329 0.0265  0.0624  0.0025  128 GLY   A C   
955  O O   . GLY   A 122 ? 0.2869 0.2829 0.3386 0.0294  0.0569  0.0114  128 GLY   A O   
956  N N   . ASN   A 123 ? 0.2774 0.2605 0.3186 0.0244  0.0684  -0.0024 129 ASN   A N   
957  C CA  . ASN   A 123 ? 0.2814 0.2739 0.3283 0.0261  0.0697  0.0024  129 ASN   A CA  
958  C C   . ASN   A 123 ? 0.2657 0.2696 0.3083 0.0250  0.0587  0.0087  129 ASN   A C   
959  O O   . ASN   A 123 ? 0.2666 0.2819 0.3196 0.0278  0.0582  0.0168  129 ASN   A O   
960  C CB  . ASN   A 123 ? 0.3034 0.2991 0.3722 0.0332  0.0786  0.0093  129 ASN   A CB  
961  C CG  . ASN   A 123 ? 0.3606 0.3435 0.4345 0.0338  0.0921  0.0019  129 ASN   A CG  
962  O OD1 . ASN   A 123 ? 0.3857 0.3635 0.4517 0.0297  0.0981  -0.0064 129 ASN   A OD1 
963  N ND2 . ASN   A 123 ? 0.3752 0.3525 0.4621 0.0383  0.0976  0.0044  129 ASN   A ND2 
964  N N   . GLY   A 124 ? 0.2246 0.2259 0.2522 0.0202  0.0507  0.0049  130 GLY   A N   
965  C CA  . GLY   A 124 ? 0.2196 0.2292 0.2424 0.0182  0.0420  0.0091  130 GLY   A CA  
966  C C   . GLY   A 124 ? 0.1829 0.1983 0.2114 0.0201  0.0367  0.0152  130 GLY   A C   
967  O O   . GLY   A 124 ? 0.2238 0.2462 0.2488 0.0177  0.0307  0.0181  130 GLY   A O   
968  N N   . LEU   A 125 ? 0.1901 0.2014 0.2247 0.0230  0.0386  0.0157  131 LEU   A N   
969  C CA  . LEU   A 125 ? 0.1874 0.2038 0.2251 0.0236  0.0330  0.0207  131 LEU   A CA  
970  C C   . LEU   A 125 ? 0.1968 0.2036 0.2257 0.0217  0.0300  0.0150  131 LEU   A C   
971  O O   . LEU   A 125 ? 0.2232 0.2201 0.2475 0.0209  0.0335  0.0086  131 LEU   A O   
972  C CB  . LEU   A 125 ? 0.2020 0.2238 0.2564 0.0287  0.0371  0.0286  131 LEU   A CB  
973  C CG  . LEU   A 125 ? 0.2011 0.2356 0.2676 0.0310  0.0396  0.0370  131 LEU   A CG  
974  C CD1 . LEU   A 125 ? 0.2397 0.2777 0.3262 0.0373  0.0460  0.0454  131 LEU   A CD1 
975  C CD2 . LEU   A 125 ? 0.1996 0.2487 0.2628 0.0269  0.0314  0.0429  131 LEU   A CD2 
976  N N   . VAL   A 126 ? 0.1607 0.1712 0.1873 0.0203  0.0238  0.0171  132 VAL   A N   
977  C CA  . VAL   A 126 ? 0.1762 0.1797 0.1975 0.0192  0.0211  0.0132  132 VAL   A CA  
978  C C   . VAL   A 126 ? 0.1666 0.1769 0.1945 0.0202  0.0186  0.0191  132 VAL   A C   
979  O O   . VAL   A 126 ? 0.1692 0.1898 0.1987 0.0186  0.0157  0.0238  132 VAL   A O   
980  C CB  . VAL   A 126 ? 0.1724 0.1724 0.1818 0.0152  0.0163  0.0088  132 VAL   A CB  
981  C CG1 . VAL   A 126 ? 0.1733 0.1810 0.1810 0.0128  0.0125  0.0115  132 VAL   A CG1 
982  C CG2 . VAL   A 126 ? 0.1725 0.1668 0.1785 0.0144  0.0136  0.0059  132 VAL   A CG2 
983  N N   . GLY   A 127 ? 0.1657 0.1710 0.1962 0.0217  0.0194  0.0183  133 GLY   A N   
984  C CA  . GLY   A 127 ? 0.1639 0.1757 0.2001 0.0221  0.0170  0.0239  133 GLY   A CA  
985  C C   . GLY   A 127 ? 0.1629 0.1694 0.1919 0.0198  0.0134  0.0194  133 GLY   A C   
986  O O   . GLY   A 127 ? 0.1765 0.1733 0.2007 0.0195  0.0143  0.0135  133 GLY   A O   
987  N N   . PHE   A 128 ? 0.1447 0.1585 0.1731 0.0174  0.0096  0.0222  134 PHE   A N   
988  C CA  . PHE   A 128 ? 0.1486 0.1586 0.1713 0.0151  0.0066  0.0181  134 PHE   A CA  
989  C C   . PHE   A 128 ? 0.1559 0.1707 0.1838 0.0151  0.0060  0.0224  134 PHE   A C   
990  O O   . PHE   A 128 ? 0.1502 0.1762 0.1830 0.0140  0.0053  0.0291  134 PHE   A O   
991  C CB  . PHE   A 128 ? 0.1502 0.1640 0.1661 0.0107  0.0038  0.0160  134 PHE   A CB  
992  C CG  . PHE   A 128 ? 0.1513 0.1620 0.1627 0.0102  0.0042  0.0132  134 PHE   A CG  
993  C CD1 . PHE   A 128 ? 0.1469 0.1487 0.1533 0.0105  0.0038  0.0084  134 PHE   A CD1 
994  C CD2 . PHE   A 128 ? 0.1687 0.1870 0.1809 0.0088  0.0045  0.0163  134 PHE   A CD2 
995  C CE1 . PHE   A 128 ? 0.1493 0.1492 0.1516 0.0095  0.0040  0.0069  134 PHE   A CE1 
996  C CE2 . PHE   A 128 ? 0.1584 0.1741 0.1663 0.0080  0.0050  0.0139  134 PHE   A CE2 
997  C CZ  . PHE   A 128 ? 0.1504 0.1565 0.1532 0.0084  0.0047  0.0092  134 PHE   A CZ  
998  N N   . ALA   A 129 ? 0.1549 0.1626 0.1818 0.0156  0.0059  0.0191  135 ALA   A N   
999  C CA  . ALA   A 129 ? 0.1450 0.1569 0.1758 0.0149  0.0050  0.0227  135 ALA   A CA  
1000 C C   . ALA   A 129 ? 0.1477 0.1650 0.1727 0.0102  0.0020  0.0208  135 ALA   A C   
1001 O O   . ALA   A 129 ? 0.1535 0.1646 0.1729 0.0091  0.0012  0.0147  135 ALA   A O   
1002 C CB  . ALA   A 129 ? 0.1581 0.1604 0.1897 0.0166  0.0064  0.0193  135 ALA   A CB  
1003 N N   . ASP   A 130 ? 0.1490 0.1783 0.1753 0.0068  0.0007  0.0261  136 ASP   A N   
1004 C CA  . ASP   A 130 ? 0.1551 0.1897 0.1752 0.0007  -0.0007 0.0231  136 ASP   A CA  
1005 C C   . ASP   A 130 ? 0.1581 0.1887 0.1777 0.0002  -0.0007 0.0203  136 ASP   A C   
1006 O O   . ASP   A 130 ? 0.1748 0.2050 0.1998 0.0027  -0.0007 0.0241  136 ASP   A O   
1007 C CB  . ASP   A 130 ? 0.1675 0.2183 0.1889 -0.0045 -0.0021 0.0304  136 ASP   A CB  
1008 C CG  . ASP   A 130 ? 0.2682 0.3253 0.2817 -0.0129 -0.0024 0.0264  136 ASP   A CG  
1009 O OD1 . ASP   A 130 ? 0.2094 0.2602 0.2168 -0.0150 -0.0009 0.0189  136 ASP   A OD1 
1010 O OD2 . ASP   A 130 ? 0.3707 0.4387 0.3843 -0.0178 -0.0034 0.0306  136 ASP   A OD2 
1011 N N   . VAL   A 131 ? 0.1468 0.1747 0.1610 -0.0033 -0.0002 0.0139  137 VAL   A N   
1012 C CA  . VAL   A 131 ? 0.1420 0.1681 0.1560 -0.0047 0.0004  0.0112  137 VAL   A CA  
1013 C C   . VAL   A 131 ? 0.1501 0.1838 0.1593 -0.0124 0.0018  0.0086  137 VAL   A C   
1014 O O   . VAL   A 131 ? 0.1513 0.1842 0.1603 -0.0143 0.0031  0.0057  137 VAL   A O   
1015 C CB  . VAL   A 131 ? 0.1440 0.1587 0.1585 -0.0011 0.0010  0.0058  137 VAL   A CB  
1016 C CG1 . VAL   A 131 ? 0.1693 0.1774 0.1868 0.0042  0.0000  0.0074  137 VAL   A CG1 
1017 C CG2 . VAL   A 131 ? 0.1727 0.1829 0.1842 -0.0023 0.0026  0.0006  137 VAL   A CG2 
1018 N N   . ARG   A 132 ? 0.1529 0.1941 0.1579 -0.0177 0.0021  0.0089  138 ARG   A N   
1019 C CA  . ARG   A 132 ? 0.1554 0.2024 0.1540 -0.0268 0.0048  0.0043  138 ARG   A CA  
1020 C C   . ARG   A 132 ? 0.1671 0.2257 0.1645 -0.0326 0.0041  0.0078  138 ARG   A C   
1021 O O   . ARG   A 132 ? 0.1798 0.2414 0.1716 -0.0405 0.0075  0.0020  138 ARG   A O   
1022 C CB  . ARG   A 132 ? 0.1654 0.2184 0.1588 -0.0325 0.0053  0.0037  138 ARG   A CB  
1023 C CG  . ARG   A 132 ? 0.1612 0.2018 0.1549 -0.0281 0.0070  -0.0011 138 ARG   A CG  
1024 C CD  . ARG   A 132 ? 0.1788 0.2261 0.1673 -0.0343 0.0075  -0.0012 138 ARG   A CD  
1025 N NE  . ARG   A 132 ? 0.1790 0.2362 0.1709 -0.0319 0.0032  0.0080  138 ARG   A NE  
1026 C CZ  . ARG   A 132 ? 0.1966 0.2613 0.1865 -0.0353 0.0023  0.0106  138 ARG   A CZ  
1027 N NH1 . ARG   A 132 ? 0.2324 0.2968 0.2151 -0.0430 0.0053  0.0043  138 ARG   A NH1 
1028 N NH2 . ARG   A 132 ? 0.2057 0.2792 0.2015 -0.0317 -0.0009 0.0199  138 ARG   A NH2 
1029 N N   . ASP   A 133 ? 0.1617 0.2274 0.1647 -0.0294 0.0004  0.0173  139 ASP   A N   
1030 C CA  . ASP   A 133 ? 0.1680 0.2459 0.1707 -0.0350 -0.0007 0.0224  139 ASP   A CA  
1031 C C   . ASP   A 133 ? 0.1697 0.2398 0.1749 -0.0320 0.0005  0.0194  139 ASP   A C   
1032 O O   . ASP   A 133 ? 0.1855 0.2647 0.1898 -0.0371 0.0001  0.0224  139 ASP   A O   
1033 C CB  . ASP   A 133 ? 0.1829 0.2728 0.1929 -0.0331 -0.0046 0.0356  139 ASP   A CB  
1034 C CG  . ASP   A 133 ? 0.2392 0.3177 0.2590 -0.0219 -0.0050 0.0391  139 ASP   A CG  
1035 O OD1 . ASP   A 133 ? 0.2350 0.3003 0.2550 -0.0161 -0.0036 0.0334  139 ASP   A OD1 
1036 O OD2 . ASP   A 133 ? 0.2630 0.3457 0.2902 -0.0196 -0.0061 0.0475  139 ASP   A OD2 
1037 N N   . LEU   A 134 ? 0.1629 0.2179 0.1716 -0.0242 0.0016  0.0145  140 LEU   A N   
1038 C CA  . LEU   A 134 ? 0.1651 0.2137 0.1771 -0.0213 0.0023  0.0125  140 LEU   A CA  
1039 C C   . LEU   A 134 ? 0.1652 0.2112 0.1732 -0.0259 0.0064  0.0038  140 LEU   A C   
1040 O O   . LEU   A 134 ? 0.1722 0.2076 0.1821 -0.0221 0.0086  -0.0021 140 LEU   A O   
1041 C CB  . LEU   A 134 ? 0.1671 0.2030 0.1842 -0.0125 0.0014  0.0119  140 LEU   A CB  
1042 C CG  . LEU   A 134 ? 0.1834 0.2196 0.2053 -0.0078 -0.0006 0.0191  140 LEU   A CG  
1043 C CD1 . LEU   A 134 ? 0.1893 0.2129 0.2138 -0.0013 -0.0005 0.0163  140 LEU   A CD1 
1044 C CD2 . LEU   A 134 ? 0.2022 0.2455 0.2292 -0.0082 -0.0017 0.0273  140 LEU   A CD2 
1045 N N   . LEU   A 135 ? 0.1685 0.2252 0.1715 -0.0347 0.0081  0.0033  141 LEU   A N   
1046 C CA  . LEU   A 135 ? 0.1772 0.2315 0.1761 -0.0405 0.0140  -0.0062 141 LEU   A CA  
1047 C C   . LEU   A 135 ? 0.1770 0.2230 0.1814 -0.0362 0.0164  -0.0101 141 LEU   A C   
1048 O O   . LEU   A 135 ? 0.1919 0.2307 0.1975 -0.0368 0.0220  -0.0180 141 LEU   A O   
1049 C CB  . LEU   A 135 ? 0.1864 0.2554 0.1770 -0.0530 0.0158  -0.0066 141 LEU   A CB  
1050 C CG  . LEU   A 135 ? 0.2104 0.2922 0.1959 -0.0588 0.0124  -0.0006 141 LEU   A CG  
1051 C CD1 . LEU   A 135 ? 0.2360 0.3335 0.2118 -0.0734 0.0146  -0.0020 141 LEU   A CD1 
1052 C CD2 . LEU   A 135 ? 0.2264 0.3015 0.2102 -0.0575 0.0139  -0.0049 141 LEU   A CD2 
1053 N N   . TRP   A 136 ? 0.1650 0.2115 0.1742 -0.0317 0.0126  -0.0042 142 TRP   A N   
1054 C CA  . TRP   A 136 ? 0.1711 0.2117 0.1857 -0.0283 0.0141  -0.0068 142 TRP   A CA  
1055 C C   . TRP   A 136 ? 0.1832 0.2118 0.2036 -0.0209 0.0148  -0.0101 142 TRP   A C   
1056 O O   . TRP   A 136 ? 0.1954 0.2202 0.2212 -0.0187 0.0169  -0.0127 142 TRP   A O   
1057 C CB  . TRP   A 136 ? 0.1763 0.2201 0.1942 -0.0261 0.0100  0.0005  142 TRP   A CB  
1058 C CG  . TRP   A 136 ? 0.1676 0.2085 0.1883 -0.0203 0.0056  0.0070  142 TRP   A CG  
1059 C CD1 . TRP   A 136 ? 0.1735 0.2220 0.1938 -0.0215 0.0029  0.0146  142 TRP   A CD1 
1060 C CD2 . TRP   A 136 ? 0.1708 0.2014 0.1961 -0.0130 0.0040  0.0067  142 TRP   A CD2 
1061 N NE1 . TRP   A 136 ? 0.1934 0.2349 0.2183 -0.0147 0.0009  0.0182  142 TRP   A NE1 
1062 C CE2 . TRP   A 136 ? 0.1775 0.2081 0.2044 -0.0102 0.0015  0.0129  142 TRP   A CE2 
1063 C CE3 . TRP   A 136 ? 0.1822 0.2047 0.2108 -0.0094 0.0046  0.0025  142 TRP   A CE3 
1064 C CZ2 . TRP   A 136 ? 0.1943 0.2155 0.2242 -0.0045 0.0005  0.0131  142 TRP   A CZ2 
1065 C CZ3 . TRP   A 136 ? 0.2062 0.2215 0.2372 -0.0044 0.0023  0.0038  142 TRP   A CZ3 
1066 C CH2 . TRP   A 136 ? 0.1982 0.2124 0.2290 -0.0024 0.0007  0.0081  142 TRP   A CH2 
1067 N N   . LEU   A 137 ? 0.1657 0.1898 0.1856 -0.0173 0.0128  -0.0090 143 LEU   A N   
1068 C CA  . LEU   A 137 ? 0.1846 0.1994 0.2096 -0.0114 0.0131  -0.0111 143 LEU   A CA  
1069 C C   . LEU   A 137 ? 0.2151 0.2264 0.2433 -0.0130 0.0195  -0.0174 143 LEU   A C   
1070 O O   . LEU   A 137 ? 0.2191 0.2246 0.2548 -0.0082 0.0203  -0.0177 143 LEU   A O   
1071 C CB  . LEU   A 137 ? 0.1777 0.1894 0.2006 -0.0086 0.0105  -0.0092 143 LEU   A CB  
1072 C CG  . LEU   A 137 ? 0.1676 0.1796 0.1903 -0.0052 0.0057  -0.0036 143 LEU   A CG  
1073 C CD1 . LEU   A 137 ? 0.1916 0.2019 0.2116 -0.0037 0.0045  -0.0025 143 LEU   A CD1 
1074 C CD2 . LEU   A 137 ? 0.1706 0.1771 0.1980 -0.0008 0.0037  -0.0028 143 LEU   A CD2 
1075 N N   . ASP   A 138 ? 0.2395 0.2547 0.2628 -0.0203 0.0246  -0.0221 144 ASP   A N   
1076 C CA  . ASP   A 138 ? 0.2620 0.2723 0.2887 -0.0227 0.0331  -0.0295 144 ASP   A CA  
1077 C C   . ASP   A 138 ? 0.3141 0.3250 0.3464 -0.0237 0.0380  -0.0325 144 ASP   A C   
1078 O O   . ASP   A 138 ? 0.3267 0.3331 0.3636 -0.0258 0.0467  -0.0390 144 ASP   A O   
1079 C CB  . ASP   A 138 ? 0.2622 0.2761 0.2795 -0.0323 0.0380  -0.0350 144 ASP   A CB  
1080 C CG  . ASP   A 138 ? 0.3297 0.3432 0.3419 -0.0325 0.0350  -0.0332 144 ASP   A CG  
1081 O OD1 . ASP   A 138 ? 0.3580 0.3661 0.3746 -0.0248 0.0307  -0.0290 144 ASP   A OD1 
1082 O OD2 . ASP   A 138 ? 0.4019 0.4214 0.4053 -0.0412 0.0370  -0.0360 144 ASP   A OD2 
1083 N N   . GLU   A 139 ? 0.3293 0.3456 0.3621 -0.0229 0.0336  -0.0284 145 GLU   A N   
1084 C CA  . GLU   A 139 ? 0.3755 0.3936 0.4133 -0.0245 0.0382  -0.0311 145 GLU   A CA  
1085 C C   . GLU   A 139 ? 0.3981 0.4170 0.4424 -0.0186 0.0326  -0.0253 145 GLU   A C   
1086 O O   . GLU   A 139 ? 0.3885 0.4065 0.4316 -0.0146 0.0255  -0.0198 145 GLU   A O   
1087 C CB  . GLU   A 139 ? 0.4408 0.4682 0.4689 -0.0344 0.0404  -0.0336 145 GLU   A CB  
1088 C CG  . GLU   A 139 ? 0.5451 0.5804 0.5673 -0.0351 0.0320  -0.0257 145 GLU   A CG  
1089 C CD  . GLU   A 139 ? 0.6658 0.7126 0.6773 -0.0452 0.0320  -0.0251 145 GLU   A CD  
1090 O OE1 . GLU   A 139 ? 0.6731 0.7274 0.6826 -0.0456 0.0258  -0.0172 145 GLU   A OE1 
1091 O OE2 . GLU   A 139 ? 0.7181 0.7670 0.7239 -0.0534 0.0385  -0.0322 145 GLU   A OE2 
1092 N N   . GLU   A 140 ? 0.4329 0.4536 0.4836 -0.0191 0.0364  -0.0271 146 GLU   A N   
1093 C CA  . GLU   A 140 ? 0.4765 0.4995 0.5329 -0.0157 0.0324  -0.0226 146 GLU   A CA  
1094 C C   . GLU   A 140 ? 0.5074 0.5279 0.5652 -0.0100 0.0243  -0.0164 146 GLU   A C   
1095 O O   . GLU   A 140 ? 0.5163 0.5393 0.5746 -0.0094 0.0199  -0.0126 146 GLU   A O   
1096 C CB  . GLU   A 140 ? 0.5296 0.5603 0.5797 -0.0217 0.0315  -0.0218 146 GLU   A CB  
1097 C CG  . GLU   A 140 ? 0.6100 0.6441 0.6518 -0.0231 0.0246  -0.0161 146 GLU   A CG  
1098 C CD  . GLU   A 140 ? 0.7375 0.7732 0.7816 -0.0211 0.0195  -0.0105 146 GLU   A CD  
1099 O OE1 . GLU   A 140 ? 0.7697 0.8079 0.8091 -0.0222 0.0153  -0.0053 146 GLU   A OE1 
1100 O OE2 . GLU   A 140 ? 0.7725 0.8070 0.8239 -0.0186 0.0201  -0.0108 146 GLU   A OE2 
1101 N N   . SER   B 1   ? 0.2449 0.2687 0.2730 0.0026  -0.0153 0.0513  7   SER   C N   
1102 C CA  . SER   B 1   ? 0.2337 0.2587 0.2715 0.0018  -0.0154 0.0524  7   SER   C CA  
1103 C C   . SER   B 1   ? 0.2328 0.2541 0.2680 0.0016  -0.0148 0.0477  7   SER   C C   
1104 O O   . SER   B 1   ? 0.2482 0.2662 0.2740 0.0017  -0.0154 0.0441  7   SER   C O   
1105 C CB  . SER   B 1   ? 0.2712 0.2991 0.3115 -0.0001 -0.0200 0.0567  7   SER   C CB  
1106 O OG  . SER   B 1   ? 0.3436 0.3691 0.3741 -0.0018 -0.0239 0.0544  7   SER   C OG  
1107 N N   . GLY   B 2   ? 0.2235 0.2449 0.2669 0.0015  -0.0132 0.0479  8   GLY   C N   
1108 C CA  . GLY   B 2   ? 0.2134 0.2313 0.2545 0.0013  -0.0124 0.0443  8   GLY   C CA  
1109 C C   . GLY   B 2   ? 0.1962 0.2134 0.2446 0.0023  -0.0085 0.0437  8   GLY   C C   
1110 O O   . GLY   B 2   ? 0.1944 0.2129 0.2476 0.0035  -0.0057 0.0441  8   GLY   C O   
1111 N N   . ALA   B 3   ? 0.1859 0.2008 0.2351 0.0018  -0.0078 0.0426  9   ALA   C N   
1112 C CA  . ALA   B 3   ? 0.1844 0.1979 0.2389 0.0028  -0.0036 0.0417  9   ALA   C CA  
1113 C C   . ALA   B 3   ? 0.1694 0.1785 0.2178 0.0032  -0.0024 0.0385  9   ALA   C C   
1114 O O   . ALA   B 3   ? 0.1881 0.1956 0.2305 0.0024  -0.0049 0.0375  9   ALA   C O   
1115 C CB  . ALA   B 3   ? 0.2177 0.2339 0.2836 0.0019  -0.0029 0.0459  9   ALA   C CB  
1116 N N   . ILE   B 4   ? 0.1671 0.1740 0.2167 0.0045  0.0017  0.0368  10  ILE   C N   
1117 C CA  . ILE   B 4   ? 0.1687 0.1713 0.2133 0.0051  0.0035  0.0346  10  ILE   C CA  
1118 C C   . ILE   B 4   ? 0.1629 0.1653 0.2157 0.0046  0.0066  0.0371  10  ILE   C C   
1119 O O   . ILE   B 4   ? 0.1760 0.1800 0.2364 0.0049  0.0093  0.0385  10  ILE   C O   
1120 C CB  . ILE   B 4   ? 0.1734 0.1732 0.2122 0.0069  0.0059  0.0309  10  ILE   C CB  
1121 C CG1 . ILE   B 4   ? 0.1870 0.1879 0.2209 0.0076  0.0035  0.0289  10  ILE   C CG1 
1122 C CG2 . ILE   B 4   ? 0.1990 0.1943 0.2314 0.0076  0.0074  0.0294  10  ILE   C CG2 
1123 C CD1 . ILE   B 4   ? 0.1990 0.1982 0.2301 0.0091  0.0054  0.0255  10  ILE   C CD1 
1124 N N   . TYR   B 5   ? 0.1591 0.1595 0.2113 0.0038  0.0065  0.0379  11  TYR   C N   
1125 C CA  . TYR   B 5   ? 0.1812 0.1814 0.2419 0.0033  0.0099  0.0405  11  TYR   C CA  
1126 C C   . TYR   B 5   ? 0.1884 0.1834 0.2427 0.0046  0.0138  0.0386  11  TYR   C C   
1127 O O   . TYR   B 5   ? 0.2094 0.2020 0.2587 0.0042  0.0124  0.0381  11  TYR   C O   
1128 C CB  . TYR   B 5   ? 0.1844 0.1873 0.2519 0.0009  0.0062  0.0439  11  TYR   C CB  
1129 C CG  . TYR   B 5   ? 0.1824 0.1906 0.2559 -0.0004 0.0022  0.0465  11  TYR   C CG  
1130 C CD1 . TYR   B 5   ? 0.1807 0.1923 0.2660 -0.0003 0.0041  0.0500  11  TYR   C CD1 
1131 C CD2 . TYR   B 5   ? 0.2002 0.2096 0.2671 -0.0012 -0.0029 0.0456  11  TYR   C CD2 
1132 C CE1 . TYR   B 5   ? 0.2008 0.2173 0.2913 -0.0012 0.0004  0.0529  11  TYR   C CE1 
1133 C CE2 . TYR   B 5   ? 0.2182 0.2322 0.2892 -0.0021 -0.0064 0.0483  11  TYR   C CE2 
1134 C CZ  . TYR   B 5   ? 0.2105 0.2282 0.2931 -0.0021 -0.0049 0.0521  11  TYR   C CZ  
1135 O OH  . TYR   B 5   ? 0.2457 0.2679 0.3319 -0.0027 -0.0084 0.0553  11  TYR   C OH  
1136 N N   . VAL   B 6   ? 0.1924 0.1851 0.2462 0.0062  0.0188  0.0373  12  VAL   C N   
1137 C CA  . VAL   B 6   ? 0.2145 0.2017 0.2606 0.0077  0.0228  0.0356  12  VAL   C CA  
1138 C C   . VAL   B 6   ? 0.2182 0.2041 0.2717 0.0082  0.0291  0.0375  12  VAL   C C   
1139 O O   . VAL   B 6   ? 0.2047 0.1922 0.2644 0.0086  0.0314  0.0376  12  VAL   C O   
1140 C CB  . VAL   B 6   ? 0.2225 0.2074 0.2576 0.0094  0.0224  0.0313  12  VAL   C CB  
1141 C CG1 . VAL   B 6   ? 0.2194 0.2062 0.2583 0.0098  0.0234  0.0299  12  VAL   C CG1 
1142 C CG2 . VAL   B 6   ? 0.2483 0.2276 0.2747 0.0111  0.0264  0.0299  12  VAL   C CG2 
1143 N N   . GLY   B 7   ? 0.2269 0.2100 0.2812 0.0083  0.0325  0.0393  13  GLY   C N   
1144 C CA  . GLY   B 7   ? 0.2193 0.2009 0.2810 0.0089  0.0394  0.0413  13  GLY   C CA  
1145 C C   . GLY   B 7   ? 0.2155 0.2023 0.2928 0.0076  0.0391  0.0447  13  GLY   C C   
1146 O O   . GLY   B 7   ? 0.2268 0.2181 0.3104 0.0057  0.0337  0.0471  13  GLY   C O   
1147 N N   . ASN   B 8   ? 0.2061 0.1926 0.2890 0.0087  0.0442  0.0446  14  ASN   C N   
1148 C CA  . ASN   B 8   ? 0.2039 0.1957 0.3022 0.0078  0.0437  0.0482  14  ASN   C CA  
1149 C C   . ASN   B 8   ? 0.2042 0.1981 0.3015 0.0082  0.0412  0.0461  14  ASN   C C   
1150 O O   . ASN   B 8   ? 0.2024 0.1983 0.3102 0.0085  0.0438  0.0479  14  ASN   C O   
1151 C CB  . ASN   B 8   ? 0.2357 0.2262 0.3451 0.0088  0.0517  0.0508  14  ASN   C CB  
1152 C CG  . ASN   B 8   ? 0.3209 0.3115 0.4371 0.0078  0.0532  0.0546  14  ASN   C CG  
1153 O OD1 . ASN   B 8   ? 0.3482 0.3440 0.4782 0.0061  0.0503  0.0590  14  ASN   C OD1 
1154 N ND2 . ASN   B 8   ? 0.3439 0.3289 0.4502 0.0088  0.0570  0.0530  14  ASN   C ND2 
1155 N N   . TYR   B 9   ? 0.1819 0.1759 0.2685 0.0079  0.0358  0.0432  15  TYR   C N   
1156 C CA  . TYR   B 9   ? 0.1707 0.1669 0.2562 0.0081  0.0331  0.0414  15  TYR   C CA  
1157 C C   . TYR   B 9   ? 0.1653 0.1659 0.2498 0.0066  0.0257  0.0428  15  TYR   C C   
1158 O O   . TYR   B 9   ? 0.1781 0.1779 0.2558 0.0058  0.0224  0.0423  15  TYR   C O   
1159 C CB  . TYR   B 9   ? 0.1788 0.1704 0.2513 0.0095  0.0343  0.0359  15  TYR   C CB  
1160 C CG  . TYR   B 9   ? 0.2106 0.1968 0.2808 0.0110  0.0414  0.0336  15  TYR   C CG  
1161 C CD1 . TYR   B 9   ? 0.2400 0.2260 0.3195 0.0116  0.0463  0.0340  15  TYR   C CD1 
1162 C CD2 . TYR   B 9   ? 0.2507 0.2315 0.3085 0.0120  0.0434  0.0308  15  TYR   C CD2 
1163 C CE1 . TYR   B 9   ? 0.2808 0.2609 0.3568 0.0130  0.0533  0.0312  15  TYR   C CE1 
1164 C CE2 . TYR   B 9   ? 0.2940 0.2693 0.3475 0.0135  0.0500  0.0283  15  TYR   C CE2 
1165 C CZ  . TYR   B 9   ? 0.3220 0.2968 0.3843 0.0139  0.0550  0.0282  15  TYR   C CZ  
1166 O OH  . TYR   B 9   ? 0.3888 0.3573 0.4455 0.0153  0.0619  0.0252  15  TYR   C OH  
1167 N N   . ARG   B 10  ? 0.1491 0.1536 0.2392 0.0063  0.0236  0.0441  16  ARG   C N   
1168 C CA  . ARG   B 10  ? 0.1505 0.1587 0.2381 0.0052  0.0172  0.0451  16  ARG   C CA  
1169 C C   . ARG   B 10  ? 0.1589 0.1667 0.2421 0.0063  0.0174  0.0420  16  ARG   C C   
1170 O O   . ARG   B 10  ? 0.1622 0.1703 0.2524 0.0070  0.0207  0.0424  16  ARG   C O   
1171 C CB  . ARG   B 10  ? 0.1686 0.1823 0.2683 0.0039  0.0146  0.0506  16  ARG   C CB  
1172 C CG  . ARG   B 10  ? 0.1773 0.1949 0.2748 0.0032  0.0091  0.0520  16  ARG   C CG  
1173 C CD  . ARG   B 10  ? 0.1792 0.2021 0.2876 0.0018  0.0058  0.0579  16  ARG   C CD  
1174 N NE  . ARG   B 10  ? 0.1807 0.2072 0.2915 0.0021  0.0037  0.0604  16  ARG   C NE  
1175 C CZ  . ARG   B 10  ? 0.2024 0.2311 0.3069 0.0012  -0.0016 0.0613  16  ARG   C CZ  
1176 N NH1 . ARG   B 10  ? 0.2168 0.2441 0.3115 -0.0001 -0.0055 0.0592  16  ARG   C NH1 
1177 N NH2 . ARG   B 10  ? 0.2124 0.2441 0.3197 0.0017  -0.0026 0.0641  16  ARG   C NH2 
1178 N N   . VAL   B 11  ? 0.1535 0.1602 0.2260 0.0064  0.0143  0.0390  17  VAL   C N   
1179 C CA  . VAL   B 11  ? 0.1441 0.1507 0.2131 0.0073  0.0141  0.0361  17  VAL   C CA  
1180 C C   . VAL   B 11  ? 0.1535 0.1641 0.2229 0.0066  0.0098  0.0383  17  VAL   C C   
1181 O O   . VAL   B 11  ? 0.1586 0.1696 0.2218 0.0059  0.0062  0.0385  17  VAL   C O   
1182 C CB  . VAL   B 11  ? 0.1502 0.1529 0.2074 0.0082  0.0138  0.0312  17  VAL   C CB  
1183 C CG1 . VAL   B 11  ? 0.1859 0.1887 0.2417 0.0089  0.0137  0.0282  17  VAL   C CG1 
1184 C CG2 . VAL   B 11  ? 0.1735 0.1717 0.2276 0.0089  0.0176  0.0295  17  VAL   C CG2 
1185 N N   . VAL   B 12  ? 0.1393 0.1525 0.2154 0.0068  0.0105  0.0399  18  VAL   C N   
1186 C CA  A VAL   B 12  ? 0.1400 0.1568 0.2161 0.0064  0.0072  0.0426  18  VAL   C CA  
1187 C CA  B VAL   B 12  ? 0.1609 0.1778 0.2373 0.0064  0.0072  0.0427  18  VAL   C CA  
1188 C C   . VAL   B 12  ? 0.1471 0.1642 0.2244 0.0073  0.0086  0.0410  18  VAL   C C   
1189 O O   . VAL   B 12  ? 0.1564 0.1713 0.2368 0.0080  0.0121  0.0383  18  VAL   C O   
1190 C CB  A VAL   B 12  ? 0.1339 0.1548 0.2196 0.0056  0.0060  0.0486  18  VAL   C CB  
1191 C CB  B VAL   B 12  ? 0.1990 0.2198 0.2861 0.0056  0.0066  0.0487  18  VAL   C CB  
1192 C CG1 A VAL   B 12  ? 0.1406 0.1621 0.2248 0.0042  0.0029  0.0503  18  VAL   C CG1 
1193 C CG1 B VAL   B 12  ? 0.1985 0.2230 0.2846 0.0050  0.0025  0.0524  18  VAL   C CG1 
1194 C CG2 A VAL   B 12  ? 0.1045 0.1259 0.2025 0.0063  0.0105  0.0504  18  VAL   C CG2 
1195 C CG2 B VAL   B 12  ? 0.2371 0.2576 0.3268 0.0047  0.0062  0.0502  18  VAL   C CG2 
1196 N N   . ASN   B 13  ? 0.1324 0.1520 0.2076 0.0072  0.0062  0.0427  19  ASN   C N   
1197 C CA  . ASN   B 13  ? 0.1379 0.1584 0.2167 0.0080  0.0080  0.0423  19  ASN   C CA  
1198 C C   . ASN   B 13  ? 0.1402 0.1624 0.2316 0.0081  0.0107  0.0460  19  ASN   C C   
1199 O O   . ASN   B 13  ? 0.1424 0.1673 0.2385 0.0076  0.0094  0.0510  19  ASN   C O   
1200 C CB  . ASN   B 13  ? 0.1420 0.1650 0.2170 0.0080  0.0056  0.0447  19  ASN   C CB  
1201 C CG  . ASN   B 13  ? 0.1518 0.1730 0.2154 0.0081  0.0034  0.0414  19  ASN   C CG  
1202 O OD1 . ASN   B 13  ? 0.1635 0.1843 0.2209 0.0074  0.0006  0.0420  19  ASN   C OD1 
1203 N ND2 . ASN   B 13  ? 0.1583 0.1783 0.2204 0.0090  0.0046  0.0378  19  ASN   C ND2 
1204 N N   . ARG   B 14  ? 0.1270 0.1476 0.2239 0.0087  0.0142  0.0436  20  ARG   C N   
1205 C CA  . ARG   B 14  ? 0.1185 0.1401 0.2280 0.0089  0.0175  0.0467  20  ARG   C CA  
1206 C C   . ARG   B 14  ? 0.1361 0.1621 0.2511 0.0089  0.0161  0.0533  20  ARG   C C   
1207 O O   . ARG   B 14  ? 0.1455 0.1736 0.2697 0.0090  0.0168  0.0582  20  ARG   C O   
1208 C CB  . ARG   B 14  ? 0.1229 0.1416 0.2367 0.0093  0.0211  0.0424  20  ARG   C CB  
1209 C CG  . ARG   B 14  ? 0.1331 0.1514 0.2603 0.0097  0.0256  0.0447  20  ARG   C CG  
1210 C CD  . ARG   B 14  ? 0.1441 0.1591 0.2748 0.0098  0.0288  0.0397  20  ARG   C CD  
1211 N NE  . ARG   B 14  ? 0.1573 0.1705 0.3004 0.0101  0.0339  0.0404  20  ARG   C NE  
1212 C CZ  . ARG   B 14  ? 0.1541 0.1693 0.3091 0.0105  0.0358  0.0450  20  ARG   C CZ  
1213 N NH1 . ARG   B 14  ? 0.1639 0.1836 0.3198 0.0106  0.0331  0.0501  20  ARG   C NH1 
1214 N NH2 . ARG   B 14  ? 0.1483 0.1610 0.3143 0.0109  0.0408  0.0447  20  ARG   C NH2 
1215 N N   . HIS   B 15  ? 0.1402 0.1676 0.2497 0.0090  0.0141  0.0537  21  HIS   C N   
1216 C CA  . HIS   B 15  ? 0.1458 0.1770 0.2591 0.0092  0.0131  0.0601  21  HIS   C CA  
1217 C C   . HIS   B 15  ? 0.1585 0.1924 0.2681 0.0085  0.0089  0.0648  21  HIS   C C   
1218 O O   . HIS   B 15  ? 0.1808 0.2180 0.2941 0.0087  0.0078  0.0708  21  HIS   C O   
1219 C CB  . HIS   B 15  ? 0.1415 0.1731 0.2504 0.0097  0.0132  0.0596  21  HIS   C CB  
1220 C CG  . HIS   B 15  ? 0.1460 0.1771 0.2414 0.0095  0.0100  0.0574  21  HIS   C CG  
1221 N ND1 . HIS   B 15  ? 0.1577 0.1860 0.2463 0.0095  0.0097  0.0512  21  HIS   C ND1 
1222 C CD2 . HIS   B 15  ? 0.1577 0.1906 0.2457 0.0093  0.0072  0.0608  21  HIS   C CD2 
1223 C CE1 . HIS   B 15  ? 0.1776 0.2060 0.2559 0.0094  0.0071  0.0511  21  HIS   C CE1 
1224 N NE2 . HIS   B 15  ? 0.1682 0.1991 0.2453 0.0093  0.0056  0.0564  21  HIS   C NE2 
1225 N N   . LEU   B 16  ? 0.1447 0.1772 0.2478 0.0077  0.0066  0.0623  22  LEU   C N   
1226 C CA  . LEU   B 16  ? 0.1597 0.1946 0.2602 0.0066  0.0021  0.0660  22  LEU   C CA  
1227 C C   . LEU   B 16  ? 0.1680 0.2033 0.2773 0.0061  0.0028  0.0675  22  LEU   C C   
1228 O O   . LEU   B 16  ? 0.1825 0.2196 0.2910 0.0049  -0.0010 0.0700  22  LEU   C O   
1229 C CB  . LEU   B 16  ? 0.1671 0.2002 0.2538 0.0058  -0.0012 0.0624  22  LEU   C CB  
1230 C CG  . LEU   B 16  ? 0.1834 0.2161 0.2615 0.0064  -0.0016 0.0614  22  LEU   C CG  
1231 C CD1 . LEU   B 16  ? 0.1942 0.2244 0.2595 0.0058  -0.0041 0.0573  22  LEU   C CD1 
1232 C CD2 . LEU   B 16  ? 0.1812 0.2173 0.2602 0.0065  -0.0033 0.0676  22  LEU   C CD2 
1233 N N   . ALA   B 17  ? 0.1631 0.1964 0.2808 0.0069  0.0077  0.0656  23  ALA   C N   
1234 C CA  . ALA   B 17  ? 0.1596 0.1928 0.2860 0.0068  0.0095  0.0668  23  ALA   C CA  
1235 C C   . ALA   B 17  ? 0.1740 0.2120 0.3112 0.0065  0.0076  0.0744  23  ALA   C C   
1236 O O   . ALA   B 17  ? 0.1812 0.2218 0.3238 0.0072  0.0077  0.0785  23  ALA   C O   
1237 C CB  . ALA   B 17  ? 0.1801 0.2096 0.3126 0.0078  0.0157  0.0632  23  ALA   C CB  
1238 N N   . THR   B 18  ? 0.1729 0.2123 0.3144 0.0056  0.0060  0.0764  24  THR   C N   
1239 C CA  . THR   B 18  ? 0.1800 0.2246 0.3333 0.0052  0.0034  0.0840  24  THR   C CA  
1240 C C   . THR   B 18  ? 0.1807 0.2252 0.3502 0.0065  0.0092  0.0862  24  THR   C C   
1241 O O   . THR   B 18  ? 0.1810 0.2210 0.3516 0.0075  0.0152  0.0815  24  THR   C O   
1242 C CB  . THR   B 18  ? 0.2039 0.2503 0.3546 0.0033  -0.0019 0.0850  24  THR   C CB  
1243 O OG1 . THR   B 18  ? 0.2068 0.2501 0.3608 0.0033  0.0020  0.0818  24  THR   C OG1 
1244 C CG2 . THR   B 18  ? 0.2255 0.2709 0.3598 0.0020  -0.0072 0.0820  24  THR   C CG2 
1245 N N   . HIS   B 19  ? 0.1925 0.2422 0.3754 0.0066  0.0074  0.0939  25  HIS   C N   
1246 C CA  . HIS   B 19  ? 0.2050 0.2547 0.4047 0.0079  0.0131  0.0964  25  HIS   C CA  
1247 C C   . HIS   B 19  ? 0.1773 0.2242 0.3784 0.0075  0.0162  0.0930  25  HIS   C C   
1248 O O   . HIS   B 19  ? 0.1885 0.2313 0.3950 0.0088  0.0234  0.0901  25  HIS   C O   
1249 C CB  . HIS   B 19  ? 0.2203 0.2766 0.4344 0.0079  0.0097  0.1058  25  HIS   C CB  
1250 C CG  . HIS   B 19  ? 0.2597 0.3168 0.4927 0.0091  0.0151  0.1090  25  HIS   C CG  
1251 N ND1 . HIS   B 19  ? 0.2854 0.3395 0.5280 0.0111  0.0227  0.1086  25  HIS   C ND1 
1252 C CD2 . HIS   B 19  ? 0.2856 0.3450 0.5286 0.0085  0.0147  0.1118  25  HIS   C CD2 
1253 C CE1 . HIS   B 19  ? 0.2821 0.3375 0.5410 0.0119  0.0264  0.1121  25  HIS   C CE1 
1254 N NE2 . HIS   B 19  ? 0.2821 0.3408 0.5421 0.0104  0.0220  0.1142  25  HIS   C NE2 
1255 N N   . ASN   B 20  ? 0.1855 0.2336 0.3803 0.0057  0.0112  0.0926  26  ASN   C N   
1256 C CA  . ASN   B 20  ? 0.1884 0.2335 0.3842 0.0054  0.0146  0.0895  26  ASN   C CA  
1257 C C   . ASN   B 20  ? 0.1767 0.2146 0.3611 0.0063  0.0201  0.0814  26  ASN   C C   
1258 O O   . ASN   B 20  ? 0.1695 0.2038 0.3580 0.0072  0.0264  0.0792  26  ASN   C O   
1259 C CB  . ASN   B 20  ? 0.2105 0.2577 0.4015 0.0031  0.0081  0.0902  26  ASN   C CB  
1260 C CG  . ASN   B 20  ? 0.2921 0.3367 0.4871 0.0028  0.0122  0.0883  26  ASN   C CG  
1261 O OD1 . ASN   B 20  ? 0.3217 0.3683 0.5324 0.0033  0.0155  0.0924  26  ASN   C OD1 
1262 N ND2 . ASN   B 20  ? 0.3134 0.3531 0.4947 0.0024  0.0130  0.0823  26  ASN   C ND2 
1263 N N   . ASP   B 21  ? 0.1669 0.2028 0.3371 0.0062  0.0179  0.0772  27  ASP   C N   
1264 C CA  . ASP   B 21  ? 0.1701 0.1998 0.3301 0.0070  0.0222  0.0699  27  ASP   C CA  
1265 C C   . ASP   B 21  ? 0.1627 0.1895 0.3311 0.0087  0.0295  0.0686  27  ASP   C C   
1266 O O   . ASP   B 21  ? 0.1812 0.2028 0.3474 0.0095  0.0349  0.0642  27  ASP   C O   
1267 C CB  . ASP   B 21  ? 0.1630 0.1920 0.3093 0.0067  0.0184  0.0666  27  ASP   C CB  
1268 C CG  . ASP   B 21  ? 0.1637 0.1932 0.2983 0.0052  0.0127  0.0654  27  ASP   C CG  
1269 O OD1 . ASP   B 21  ? 0.1842 0.2120 0.3169 0.0046  0.0131  0.0640  27  ASP   C OD1 
1270 O OD2 . ASP   B 21  ? 0.1693 0.2008 0.2974 0.0047  0.0082  0.0661  27  ASP   C OD2 
1271 N N   . TRP   B 22  ? 0.1595 0.1891 0.3371 0.0094  0.0296  0.0726  28  TRP   C N   
1272 C CA  . TRP   B 22  ? 0.1676 0.1942 0.3544 0.0109  0.0366  0.0713  28  TRP   C CA  
1273 C C   . TRP   B 22  ? 0.1635 0.1891 0.3634 0.0117  0.0423  0.0736  28  TRP   C C   
1274 O O   . TRP   B 22  ? 0.1727 0.1930 0.3747 0.0129  0.0493  0.0695  28  TRP   C O   
1275 C CB  . TRP   B 22  ? 0.1627 0.1925 0.3574 0.0114  0.0357  0.0757  28  TRP   C CB  
1276 C CG  . TRP   B 22  ? 0.1674 0.1958 0.3510 0.0112  0.0336  0.0718  28  TRP   C CG  
1277 C CD1 . TRP   B 22  ? 0.1811 0.2129 0.3567 0.0104  0.0276  0.0737  28  TRP   C CD1 
1278 C CD2 . TRP   B 22  ? 0.1499 0.1730 0.3291 0.0116  0.0377  0.0650  28  TRP   C CD2 
1279 N NE1 . TRP   B 22  ? 0.1797 0.2091 0.3480 0.0105  0.0282  0.0693  28  TRP   C NE1 
1280 C CE2 . TRP   B 22  ? 0.1725 0.1967 0.3432 0.0111  0.0339  0.0638  28  TRP   C CE2 
1281 C CE3 . TRP   B 22  ? 0.1833 0.2007 0.3659 0.0124  0.0443  0.0601  28  TRP   C CE3 
1282 C CZ2 . TRP   B 22  ? 0.1764 0.1971 0.3437 0.0113  0.0360  0.0584  28  TRP   C CZ2 
1283 C CZ3 . TRP   B 22  ? 0.2012 0.2146 0.3783 0.0123  0.0459  0.0539  28  TRP   C CZ3 
1284 C CH2 . TRP   B 22  ? 0.1945 0.2099 0.3649 0.0117  0.0416  0.0533  28  TRP   C CH2 
1285 N N   . ALA   B 23  ? 0.1604 0.1910 0.3685 0.0111  0.0393  0.0796  29  ALA   C N   
1286 C CA  . ALA   B 23  ? 0.1760 0.2065 0.3986 0.0120  0.0447  0.0826  29  ALA   C CA  
1287 C C   . ALA   B 23  ? 0.1898 0.2149 0.4044 0.0119  0.0488  0.0773  29  ALA   C C   
1288 O O   . ALA   B 23  ? 0.1909 0.2143 0.4154 0.0129  0.0551  0.0784  29  ALA   C O   
1289 C CB  . ALA   B 23  ? 0.1749 0.2130 0.4094 0.0111  0.0393  0.0909  29  ALA   C CB  
1290 N N   . ASN   B 24  ? 0.1936 0.2163 0.3905 0.0108  0.0452  0.0721  30  ASN   C N   
1291 C CA  . ASN   B 24  ? 0.1893 0.2068 0.3771 0.0109  0.0487  0.0675  30  ASN   C CA  
1292 C C   . ASN   B 24  ? 0.1884 0.2001 0.3595 0.0112  0.0496  0.0597  30  ASN   C C   
1293 O O   . ASN   B 24  ? 0.1867 0.1958 0.3443 0.0107  0.0477  0.0561  30  ASN   C O   
1294 C CB  . ASN   B 24  ? 0.2103 0.2312 0.3950 0.0091  0.0427  0.0699  30  ASN   C CB  
1295 C CG  . ASN   B 24  ? 0.2241 0.2503 0.4263 0.0087  0.0423  0.0771  30  ASN   C CG  
1296 O OD1 . ASN   B 24  ? 0.2359 0.2603 0.4468 0.0094  0.0485  0.0781  30  ASN   C OD1 
1297 N ND2 . ASN   B 24  ? 0.2134 0.2462 0.4215 0.0075  0.0353  0.0823  30  ASN   C ND2 
1298 N N   . LEU   B 25  ? 0.1972 0.2070 0.3694 0.0121  0.0520  0.0574  31  LEU   C N   
1299 C CA  . LEU   B 25  ? 0.1965 0.2019 0.3544 0.0121  0.0515  0.0504  31  LEU   C CA  
1300 C C   . LEU   B 25  ? 0.2157 0.2140 0.3635 0.0128  0.0566  0.0442  31  LEU   C C   
1301 O O   . LEU   B 25  ? 0.2278 0.2223 0.3817 0.0139  0.0637  0.0438  31  LEU   C O   
1302 C CB  . LEU   B 25  ? 0.1985 0.2038 0.3632 0.0127  0.0532  0.0499  31  LEU   C CB  
1303 C CG  . LEU   B 25  ? 0.1972 0.1988 0.3499 0.0125  0.0521  0.0432  31  LEU   C CG  
1304 C CD1 . LEU   B 25  ? 0.1865 0.1920 0.3298 0.0114  0.0444  0.0437  31  LEU   C CD1 
1305 C CD2 . LEU   B 25  ? 0.2222 0.2227 0.3838 0.0130  0.0553  0.0424  31  LEU   C CD2 
1306 N N   . VAL   B 26  ? 0.2011 0.1970 0.3330 0.0123  0.0532  0.0395  32  VAL   C N   
1307 C CA  . VAL   B 26  ? 0.2179 0.2068 0.3375 0.0130  0.0570  0.0333  32  VAL   C CA  
1308 C C   . VAL   B 26  ? 0.2269 0.2128 0.3393 0.0130  0.0562  0.0273  32  VAL   C C   
1309 O O   . VAL   B 26  ? 0.2351 0.2153 0.3448 0.0137  0.0613  0.0225  32  VAL   C O   
1310 C CB  . VAL   B 26  ? 0.2348 0.2233 0.3421 0.0126  0.0534  0.0327  32  VAL   C CB  
1311 C CG1 . VAL   B 26  ? 0.2584 0.2400 0.3509 0.0134  0.0562  0.0265  32  VAL   C CG1 
1312 C CG2 . VAL   B 26  ? 0.2257 0.2166 0.3407 0.0124  0.0546  0.0382  32  VAL   C CG2 
1313 N N   . TRP   B 27  ? 0.1955 0.1853 0.3052 0.0122  0.0498  0.0274  33  TRP   C N   
1314 C CA  . TRP   B 27  ? 0.1974 0.1850 0.3011 0.0120  0.0484  0.0220  33  TRP   C CA  
1315 C C   . TRP   B 27  ? 0.1837 0.1769 0.2900 0.0112  0.0426  0.0246  33  TRP   C C   
1316 O O   . TRP   B 27  ? 0.1795 0.1771 0.2849 0.0108  0.0385  0.0288  33  TRP   C O   
1317 C CB  . TRP   B 27  ? 0.2211 0.2044 0.3081 0.0121  0.0469  0.0164  33  TRP   C CB  
1318 C CG  . TRP   B 27  ? 0.2274 0.2095 0.3071 0.0116  0.0434  0.0112  33  TRP   C CG  
1319 C CD1 . TRP   B 27  ? 0.2572 0.2349 0.3354 0.0115  0.0457  0.0055  33  TRP   C CD1 
1320 C CD2 . TRP   B 27  ? 0.2023 0.1881 0.2767 0.0111  0.0370  0.0113  33  TRP   C CD2 
1321 N NE1 . TRP   B 27  ? 0.2602 0.2390 0.3329 0.0109  0.0406  0.0022  33  TRP   C NE1 
1322 C CE2 . TRP   B 27  ? 0.2222 0.2059 0.2926 0.0108  0.0355  0.0058  33  TRP   C CE2 
1323 C CE3 . TRP   B 27  ? 0.1962 0.1864 0.2688 0.0109  0.0325  0.0152  33  TRP   C CE3 
1324 C CZ2 . TRP   B 27  ? 0.2223 0.2086 0.2875 0.0104  0.0299  0.0045  33  TRP   C CZ2 
1325 C CZ3 . TRP   B 27  ? 0.2126 0.2047 0.2790 0.0106  0.0274  0.0136  33  TRP   C CZ3 
1326 C CH2 . TRP   B 27  ? 0.2136 0.2041 0.2774 0.0105  0.0264  0.0087  33  TRP   C CH2 
1327 N N   . GLU   B 28  ? 0.1748 0.1680 0.2851 0.0110  0.0427  0.0225  34  GLU   C N   
1328 C CA  . GLU   B 28  ? 0.1803 0.1783 0.2926 0.0104  0.0381  0.0248  34  GLU   C CA  
1329 C C   . GLU   B 28  ? 0.1843 0.1802 0.2948 0.0101  0.0376  0.0196  34  GLU   C C   
1330 O O   . GLU   B 28  ? 0.1871 0.1785 0.3000 0.0101  0.0416  0.0153  34  GLU   C O   
1331 C CB  . GLU   B 28  ? 0.1848 0.1875 0.3106 0.0105  0.0385  0.0318  34  GLU   C CB  
1332 C CG  . GLU   B 28  ? 0.1951 0.1959 0.3338 0.0111  0.0443  0.0323  34  GLU   C CG  
1333 C CD  . GLU   B 28  ? 0.2235 0.2231 0.3673 0.0108  0.0455  0.0297  34  GLU   C CD  
1334 O OE1 . GLU   B 28  ? 0.2614 0.2568 0.4119 0.0111  0.0507  0.0270  34  GLU   C OE1 
1335 O OE2 . GLU   B 28  ? 0.2122 0.2149 0.3539 0.0104  0.0415  0.0303  34  GLU   C OE2 
1336 N N   . ASP   B 29  ? 0.1616 0.1607 0.2684 0.0097  0.0330  0.0198  35  ASP   C N   
1337 C CA  . ASP   B 29  ? 0.1686 0.1667 0.2757 0.0092  0.0321  0.0153  35  ASP   C CA  
1338 C C   . ASP   B 29  ? 0.1665 0.1699 0.2776 0.0090  0.0290  0.0192  35  ASP   C C   
1339 O O   . ASP   B 29  ? 0.1599 0.1657 0.2636 0.0091  0.0251  0.0203  35  ASP   C O   
1340 C CB  . ASP   B 29  ? 0.1873 0.1821 0.2812 0.0090  0.0296  0.0091  35  ASP   C CB  
1341 C CG  . ASP   B 29  ? 0.2410 0.2347 0.3348 0.0083  0.0279  0.0039  35  ASP   C CG  
1342 O OD1 . ASP   B 29  ? 0.2467 0.2439 0.3477 0.0079  0.0266  0.0058  35  ASP   C OD1 
1343 O OD2 . ASP   B 29  ? 0.2736 0.2631 0.3592 0.0080  0.0273  -0.0020 35  ASP   C OD2 
1344 N N   . SER   B 30  ? 0.1595 0.1642 0.2824 0.0088  0.0312  0.0214  36  SER   C N   
1345 C CA  A SER   B 30  ? 0.1554 0.1648 0.2826 0.0088  0.0293  0.0256  36  SER   C CA  
1346 C CA  B SER   B 30  ? 0.1601 0.1695 0.2870 0.0088  0.0292  0.0257  36  SER   C CA  
1347 C C   . SER   B 30  ? 0.1614 0.1712 0.2824 0.0085  0.0260  0.0217  36  SER   C C   
1348 O O   . SER   B 30  ? 0.1533 0.1667 0.2715 0.0088  0.0235  0.0248  36  SER   C O   
1349 C CB  A SER   B 30  ? 0.1665 0.1766 0.3081 0.0089  0.0329  0.0288  36  SER   C CB  
1350 C CB  B SER   B 30  ? 0.1836 0.1939 0.3249 0.0089  0.0327  0.0291  36  SER   C CB  
1351 O OG  A SER   B 30  ? 0.1624 0.1761 0.3078 0.0089  0.0317  0.0319  36  SER   C OG  
1352 O OG  B SER   B 30  ? 0.2042 0.2103 0.3503 0.0083  0.0355  0.0234  36  SER   C OG  
1353 N N   . SER   B 31  ? 0.1681 0.1743 0.2874 0.0078  0.0260  0.0150  37  SER   C N   
1354 C CA  . SER   B 31  ? 0.1736 0.1809 0.2888 0.0074  0.0225  0.0116  37  SER   C CA  
1355 C C   . SER   B 31  ? 0.1585 0.1670 0.2614 0.0081  0.0187  0.0118  37  SER   C C   
1356 O O   . SER   B 31  ? 0.1672 0.1780 0.2683 0.0082  0.0160  0.0114  37  SER   C O   
1357 C CB  . SER   B 31  ? 0.2123 0.2156 0.3272 0.0065  0.0223  0.0043  37  SER   C CB  
1358 O OG  . SER   B 31  ? 0.2861 0.2856 0.3896 0.0066  0.0214  0.0003  37  SER   C OG  
1359 N N   . ARG   B 32  ? 0.1587 0.1656 0.2542 0.0086  0.0188  0.0126  38  ARG   C N   
1360 C CA  . ARG   B 32  ? 0.1583 0.1658 0.2428 0.0091  0.0155  0.0130  38  ARG   C CA  
1361 C C   . ARG   B 32  ? 0.1508 0.1616 0.2351 0.0095  0.0150  0.0191  38  ARG   C C   
1362 O O   . ARG   B 32  ? 0.1493 0.1605 0.2253 0.0098  0.0125  0.0197  38  ARG   C O   
1363 C CB  . ARG   B 32  ? 0.1811 0.1844 0.2571 0.0093  0.0159  0.0100  38  ARG   C CB  
1364 C CG  . ARG   B 32  ? 0.1912 0.1908 0.2637 0.0090  0.0155  0.0037  38  ARG   C CG  
1365 C CD  . ARG   B 32  ? 0.1752 0.1702 0.2382 0.0094  0.0166  0.0010  38  ARG   C CD  
1366 N NE  . ARG   B 32  ? 0.1725 0.1678 0.2253 0.0102  0.0137  0.0021  38  ARG   C NE  
1367 C CZ  . ARG   B 32  ? 0.1898 0.1816 0.2320 0.0107  0.0128  -0.0007 38  ARG   C CZ  
1368 N NH1 . ARG   B 32  ? 0.1989 0.1861 0.2375 0.0105  0.0146  -0.0051 38  ARG   C NH1 
1369 N NH2 . ARG   B 32  ? 0.1823 0.1746 0.2167 0.0114  0.0101  0.0007  38  ARG   C NH2 
1370 N N   . ASP   B 33  ? 0.1330 0.1457 0.2262 0.0094  0.0172  0.0237  39  ASP   C N   
1371 C CA  . ASP   B 33  ? 0.1304 0.1460 0.2234 0.0095  0.0163  0.0294  39  ASP   C CA  
1372 C C   . ASP   B 33  ? 0.1390 0.1531 0.2259 0.0094  0.0156  0.0296  39  ASP   C C   
1373 O O   . ASP   B 33  ? 0.1361 0.1519 0.2180 0.0093  0.0131  0.0324  39  ASP   C O   
1374 C CB  . ASP   B 33  ? 0.1363 0.1548 0.2252 0.0098  0.0139  0.0315  39  ASP   C CB  
1375 C CG  . ASP   B 33  ? 0.1449 0.1661 0.2328 0.0097  0.0126  0.0373  39  ASP   C CG  
1376 O OD1 . ASP   B 33  ? 0.1553 0.1779 0.2510 0.0095  0.0141  0.0415  39  ASP   C OD1 
1377 O OD2 . ASP   B 33  ? 0.1524 0.1742 0.2321 0.0098  0.0101  0.0378  39  ASP   C OD2 
1378 N N   . LEU   B 34  ? 0.1393 0.1500 0.2270 0.0094  0.0181  0.0270  40  LEU   C N   
1379 C CA  . LEU   B 34  ? 0.1422 0.1513 0.2253 0.0094  0.0181  0.0277  40  LEU   C CA  
1380 C C   . LEU   B 34  ? 0.1400 0.1486 0.2322 0.0094  0.0219  0.0301  40  LEU   C C   
1381 O O   . LEU   B 34  ? 0.1552 0.1621 0.2542 0.0096  0.0254  0.0286  40  LEU   C O   
1382 C CB  . LEU   B 34  ? 0.1530 0.1579 0.2263 0.0097  0.0179  0.0223  40  LEU   C CB  
1383 C CG  . LEU   B 34  ? 0.1551 0.1603 0.2187 0.0099  0.0140  0.0203  40  LEU   C CG  
1384 C CD1 . LEU   B 34  ? 0.1739 0.1747 0.2287 0.0104  0.0141  0.0156  40  LEU   C CD1 
1385 C CD2 . LEU   B 34  ? 0.1777 0.1850 0.2377 0.0097  0.0113  0.0239  40  LEU   C CD2 
1386 N N   . LEU   B 35  ? 0.1405 0.1501 0.2328 0.0091  0.0213  0.0335  41  LEU   C N   
1387 C CA  . LEU   B 35  ? 0.1434 0.1524 0.2444 0.0093  0.0251  0.0360  41  LEU   C CA  
1388 C C   . LEU   B 35  ? 0.1536 0.1614 0.2494 0.0090  0.0246  0.0364  41  LEU   C C   
1389 O O   . LEU   B 35  ? 0.1618 0.1713 0.2516 0.0084  0.0204  0.0377  41  LEU   C O   
1390 C CB  . LEU   B 35  ? 0.1426 0.1564 0.2551 0.0091  0.0246  0.0424  41  LEU   C CB  
1391 C CG  . LEU   B 35  ? 0.1457 0.1597 0.2699 0.0094  0.0285  0.0459  41  LEU   C CG  
1392 C CD1 . LEU   B 35  ? 0.1747 0.1918 0.3122 0.0097  0.0299  0.0505  41  LEU   C CD1 
1393 C CD2 . LEU   B 35  ? 0.1518 0.1681 0.2763 0.0087  0.0260  0.0498  41  LEU   C CD2 
1394 N N   . VAL   B 36  ? 0.1530 0.1573 0.2508 0.0095  0.0292  0.0351  42  VAL   C N   
1395 C CA  . VAL   B 36  ? 0.1511 0.1539 0.2461 0.0094  0.0300  0.0359  42  VAL   C CA  
1396 C C   . VAL   B 36  ? 0.1498 0.1538 0.2579 0.0095  0.0339  0.0403  42  VAL   C C   
1397 O O   . VAL   B 36  ? 0.1671 0.1692 0.2823 0.0103  0.0389  0.0396  42  VAL   C O   
1398 C CB  . VAL   B 36  ? 0.1674 0.1643 0.2514 0.0102  0.0326  0.0305  42  VAL   C CB  
1399 C CG1 . VAL   B 36  ? 0.1851 0.1802 0.2666 0.0102  0.0342  0.0319  42  VAL   C CG1 
1400 C CG2 . VAL   B 36  ? 0.1826 0.1789 0.2550 0.0102  0.0282  0.0267  42  VAL   C CG2 
1401 N N   . SER   B 37  ? 0.1591 0.1662 0.2710 0.0087  0.0316  0.0447  43  SER   C N   
1402 C CA  . SER   B 37  ? 0.1633 0.1722 0.2889 0.0087  0.0348  0.0494  43  SER   C CA  
1403 C C   . SER   B 37  ? 0.1761 0.1829 0.2993 0.0085  0.0364  0.0496  43  SER   C C   
1404 O O   . SER   B 37  ? 0.1777 0.1825 0.2892 0.0080  0.0339  0.0470  43  SER   C O   
1405 C CB  . SER   B 37  ? 0.1727 0.1883 0.3079 0.0077  0.0300  0.0555  43  SER   C CB  
1406 O OG  . SER   B 37  ? 0.1875 0.2054 0.3154 0.0062  0.0235  0.0564  43  SER   C OG  
1407 N N   . SER   B 38  ? 0.1777 0.1847 0.3128 0.0089  0.0412  0.0528  44  SER   C N   
1408 C CA  . SER   B 38  ? 0.1892 0.1941 0.3242 0.0087  0.0437  0.0537  44  SER   C CA  
1409 C C   . SER   B 38  ? 0.2125 0.2230 0.3551 0.0068  0.0382  0.0589  44  SER   C C   
1410 O O   . SER   B 38  ? 0.2165 0.2326 0.3688 0.0059  0.0343  0.0632  44  SER   C O   
1411 C CB  . SER   B 38  ? 0.2094 0.2112 0.3534 0.0102  0.0526  0.0542  44  SER   C CB  
1412 O OG  . SER   B 38  ? 0.2556 0.2622 0.4169 0.0102  0.0532  0.0595  44  SER   C OG  
1413 N N   . THR   B 39  ? 0.2131 0.2220 0.3517 0.0060  0.0379  0.0588  45  THR   C N   
1414 C CA  . THR   B 39  ? 0.2226 0.2361 0.3678 0.0038  0.0322  0.0630  45  THR   C CA  
1415 C C   . THR   B 39  ? 0.2539 0.2666 0.4092 0.0037  0.0372  0.0658  45  THR   C C   
1416 O O   . THR   B 39  ? 0.2550 0.2622 0.4059 0.0053  0.0442  0.0635  45  THR   C O   
1417 C CB  . THR   B 39  ? 0.2333 0.2456 0.3642 0.0025  0.0262  0.0600  45  THR   C CB  
1418 O OG1 . THR   B 39  ? 0.2464 0.2526 0.3674 0.0035  0.0304  0.0565  45  THR   C OG1 
1419 C CG2 . THR   B 39  ? 0.2322 0.2452 0.3530 0.0027  0.0217  0.0572  45  THR   C CG2 
1420 N N   . THR   B 40  ? 0.2735 0.2913 0.4410 0.0017  0.0332  0.0708  46  THR   C N   
1421 C CA  . THR   B 40  ? 0.2921 0.3098 0.4708 0.0013  0.0372  0.0739  46  THR   C CA  
1422 C C   . THR   B 40  ? 0.2993 0.3135 0.4676 0.0001  0.0355  0.0716  46  THR   C C   
1423 O O   . THR   B 40  ? 0.3204 0.3302 0.4882 0.0010  0.0420  0.0712  46  THR   C O   
1424 C CB  . THR   B 40  ? 0.3405 0.3656 0.5382 -0.0005 0.0332  0.0804  46  THR   C CB  
1425 O OG1 . THR   B 40  ? 0.3887 0.4177 0.5821 -0.0030 0.0230  0.0807  46  THR   C OG1 
1426 C CG2 . THR   B 40  ? 0.3308 0.3592 0.5396 0.0010  0.0354  0.0832  46  THR   C CG2 
1427 N N   . ALA   B 41  ? 0.2756 0.2913 0.4354 -0.0018 0.0272  0.0701  47  ALA   C N   
1428 C CA  . ALA   B 41  ? 0.2832 0.2953 0.4335 -0.0029 0.0253  0.0678  47  ALA   C CA  
1429 C C   . ALA   B 41  ? 0.2698 0.2758 0.4014 -0.0009 0.0276  0.0623  47  ALA   C C   
1430 O O   . ALA   B 41  ? 0.2583 0.2642 0.3827 0.0003  0.0270  0.0597  47  ALA   C O   
1431 C CB  . ALA   B 41  ? 0.2978 0.3138 0.4476 -0.0059 0.0156  0.0684  47  ALA   C CB  
1432 N N   . GLN   B 42  ? 0.2673 0.2683 0.3918 -0.0007 0.0302  0.0607  48  GLN   C N   
1433 C CA  . GLN   B 42  ? 0.2816 0.2770 0.3888 0.0011  0.0316  0.0561  48  GLN   C CA  
1434 C C   . GLN   B 42  ? 0.2846 0.2810 0.3822 -0.0001 0.0238  0.0535  48  GLN   C C   
1435 O O   . GLN   B 42  ? 0.3071 0.3058 0.4088 -0.0025 0.0185  0.0549  48  GLN   C O   
1436 C CB  . GLN   B 42  ? 0.3391 0.3290 0.4425 0.0020  0.0371  0.0562  48  GLN   C CB  
1437 C CG  . GLN   B 42  ? 0.4442 0.4306 0.5490 0.0045  0.0465  0.0567  48  GLN   C CG  
1438 C CD  . GLN   B 42  ? 0.5829 0.5630 0.6798 0.0057  0.0518  0.0565  48  GLN   C CD  
1439 O OE1 . GLN   B 42  ? 0.6332 0.6131 0.7382 0.0046  0.0536  0.0597  48  GLN   C OE1 
1440 N NE2 . GLN   B 42  ? 0.6217 0.5968 0.7030 0.0080  0.0542  0.0528  48  GLN   C NE2 
1441 N N   . GLY   B 43  ? 0.2467 0.2412 0.3323 0.0016  0.0233  0.0497  49  GLY   C N   
1442 C CA  . GLY   B 43  ? 0.2550 0.2496 0.3303 0.0011  0.0174  0.0469  49  GLY   C CA  
1443 C C   . GLY   B 43  ? 0.2593 0.2486 0.3237 0.0019  0.0182  0.0446  49  GLY   C C   
1444 O O   . GLY   B 43  ? 0.2812 0.2665 0.3437 0.0033  0.0237  0.0449  49  GLY   C O   
1445 N N   . CYS   B 44  ? 0.2473 0.2362 0.3043 0.0013  0.0132  0.0425  50  CYS   C N   
1446 C CA  . CYS   B 44  ? 0.2658 0.2500 0.3136 0.0020  0.0135  0.0408  50  CYS   C CA  
1447 C C   . CYS   B 44  ? 0.2630 0.2454 0.2988 0.0038  0.0118  0.0372  50  CYS   C C   
1448 O O   . CYS   B 44  ? 0.2963 0.2748 0.3248 0.0046  0.0117  0.0361  50  CYS   C O   
1449 C CB  . CYS   B 44  ? 0.2770 0.2611 0.3282 -0.0005 0.0097  0.0418  50  CYS   C CB  
1450 S SG  . CYS   B 44  ? 0.3734 0.3593 0.4403 -0.0028 0.0117  0.0463  50  CYS   C SG  
1451 N N   . ASP   B 45  ? 0.2154 0.2007 0.2499 0.0044  0.0103  0.0357  51  ASP   C N   
1452 C CA  . ASP   B 45  ? 0.2103 0.1945 0.2350 0.0061  0.0087  0.0325  51  ASP   C CA  
1453 C C   . ASP   B 45  ? 0.2216 0.2023 0.2401 0.0084  0.0127  0.0311  51  ASP   C C   
1454 O O   . ASP   B 45  ? 0.2467 0.2266 0.2686 0.0089  0.0170  0.0321  51  ASP   C O   
1455 C CB  . ASP   B 45  ? 0.2277 0.2161 0.2543 0.0060  0.0065  0.0317  51  ASP   C CB  
1456 C CG  . ASP   B 45  ? 0.2736 0.2652 0.3034 0.0039  0.0021  0.0328  51  ASP   C CG  
1457 O OD1 . ASP   B 45  ? 0.2852 0.2752 0.3119 0.0030  -0.0004 0.0324  51  ASP   C OD1 
1458 O OD2 . ASP   B 45  ? 0.2337 0.2293 0.2688 0.0034  0.0011  0.0340  51  ASP   C OD2 
1459 N N   . THR   B 46  ? 0.2055 0.1837 0.2149 0.0099  0.0114  0.0290  52  THR   C N   
1460 C CA  . THR   B 46  ? 0.2099 0.1849 0.2114 0.0122  0.0138  0.0274  52  THR   C CA  
1461 C C   . THR   B 46  ? 0.2039 0.1812 0.2024 0.0130  0.0113  0.0245  52  THR   C C   
1462 O O   . THR   B 46  ? 0.2116 0.1908 0.2095 0.0128  0.0076  0.0236  52  THR   C O   
1463 C CB  . THR   B 46  ? 0.2408 0.2118 0.2350 0.0133  0.0135  0.0277  52  THR   C CB  
1464 O OG1 . THR   B 46  ? 0.2673 0.2360 0.2656 0.0124  0.0162  0.0307  52  THR   C OG1 
1465 C CG2 . THR   B 46  ? 0.2697 0.2377 0.2544 0.0158  0.0148  0.0262  52  THR   C CG2 
1466 N N   . ILE   B 47  ? 0.2040 0.1806 0.2006 0.0140  0.0134  0.0228  53  ILE   C N   
1467 C CA  . ILE   B 47  ? 0.1991 0.1776 0.1937 0.0146  0.0111  0.0198  53  ILE   C CA  
1468 C C   . ILE   B 47  ? 0.1968 0.1728 0.1817 0.0164  0.0093  0.0180  53  ILE   C C   
1469 O O   . ILE   B 47  ? 0.2190 0.1910 0.1972 0.0176  0.0113  0.0183  53  ILE   C O   
1470 C CB  . ILE   B 47  ? 0.2121 0.1905 0.2089 0.0147  0.0141  0.0182  53  ILE   C CB  
1471 C CG1 . ILE   B 47  ? 0.2191 0.1998 0.2264 0.0132  0.0165  0.0206  53  ILE   C CG1 
1472 C CG2 . ILE   B 47  ? 0.2167 0.1971 0.2127 0.0150  0.0114  0.0150  53  ILE   C CG2 
1473 C CD1 . ILE   B 47  ? 0.2473 0.2329 0.2615 0.0119  0.0130  0.0220  53  ILE   C CD1 
1474 N N   . ALA   B 48  ? 0.1768 0.1551 0.1610 0.0168  0.0054  0.0166  54  ALA   C N   
1475 C CA  . ALA   B 48  ? 0.1754 0.1521 0.1519 0.0186  0.0031  0.0152  54  ALA   C CA  
1476 C C   . ALA   B 48  ? 0.1800 0.1555 0.1520 0.0193  0.0035  0.0126  54  ALA   C C   
1477 O O   . ALA   B 48  ? 0.1812 0.1585 0.1576 0.0184  0.0042  0.0107  54  ALA   C O   
1478 C CB  . ALA   B 48  ? 0.1770 0.1571 0.1560 0.0188  -0.0006 0.0143  54  ALA   C CB  
1479 N N   . ARG   B 49  ? 0.1838 0.1559 0.1465 0.0209  0.0030  0.0123  55  ARG   C N   
1480 C CA  . ARG   B 49  ? 0.1960 0.1663 0.1521 0.0216  0.0025  0.0093  55  ARG   C CA  
1481 C C   . ARG   B 49  ? 0.1990 0.1699 0.1497 0.0232  -0.0024 0.0088  55  ARG   C C   
1482 O O   . ARG   B 49  ? 0.2171 0.1849 0.1601 0.0248  -0.0027 0.0107  55  ARG   C O   
1483 C CB  . ARG   B 49  ? 0.2050 0.1702 0.1541 0.0221  0.0072  0.0099  55  ARG   C CB  
1484 C CG  . ARG   B 49  ? 0.1881 0.1531 0.1447 0.0207  0.0124  0.0112  55  ARG   C CG  
1485 C CD  . ARG   B 49  ? 0.2152 0.1825 0.1783 0.0195  0.0130  0.0084  55  ARG   C CD  
1486 N NE  . ARG   B 49  ? 0.2216 0.1888 0.1926 0.0184  0.0180  0.0103  55  ARG   C NE  
1487 C CZ  . ARG   B 49  ? 0.2259 0.1960 0.2064 0.0172  0.0189  0.0097  55  ARG   C CZ  
1488 N NH1 . ARG   B 49  ? 0.2009 0.1736 0.1838 0.0167  0.0158  0.0069  55  ARG   C NH1 
1489 N NH2 . ARG   B 49  ? 0.2424 0.2128 0.2309 0.0164  0.0230  0.0121  55  ARG   C NH2 
1490 N N   . CYS   B 50  ? 0.1906 0.1655 0.1462 0.0228  -0.0061 0.0067  56  CYS   C N   
1491 C CA  . CYS   B 50  ? 0.1859 0.1628 0.1403 0.0242  -0.0111 0.0067  56  CYS   C CA  
1492 C C   . CYS   B 50  ? 0.1879 0.1694 0.1496 0.0234  -0.0142 0.0040  56  CYS   C C   
1493 O O   . CYS   B 50  ? 0.1925 0.1755 0.1602 0.0218  -0.0124 0.0024  56  CYS   C O   
1494 C CB  . CYS   B 50  ? 0.1863 0.1637 0.1440 0.0248  -0.0108 0.0100  56  CYS   C CB  
1495 S SG  . CYS   B 50  ? 0.1843 0.1659 0.1536 0.0230  -0.0096 0.0101  56  CYS   C SG  
1496 N N   . ASP   B 51  ? 0.2018 0.1858 0.1644 0.0246  -0.0187 0.0040  57  ASP   C N   
1497 C CA  . ASP   B 51  ? 0.1905 0.1793 0.1618 0.0240  -0.0215 0.0021  57  ASP   C CA  
1498 C C   . ASP   B 51  ? 0.1965 0.1880 0.1739 0.0251  -0.0223 0.0045  57  ASP   C C   
1499 O O   . ASP   B 51  ? 0.2109 0.2062 0.1943 0.0255  -0.0253 0.0038  57  ASP   C O   
1500 C CB  . ASP   B 51  ? 0.2317 0.2213 0.1998 0.0244  -0.0265 -0.0006 57  ASP   C CB  
1501 C CG  . ASP   B 51  ? 0.2849 0.2737 0.2467 0.0266  -0.0303 0.0013  57  ASP   C CG  
1502 O OD1 . ASP   B 51  ? 0.2700 0.2573 0.2300 0.0280  -0.0286 0.0047  57  ASP   C OD1 
1503 O OD2 . ASP   B 51  ? 0.3755 0.3655 0.3349 0.0269  -0.0354 -0.0006 57  ASP   C OD2 
1504 N N   . CYS   B 52  ? 0.1884 0.1782 0.1654 0.0252  -0.0191 0.0071  58  CYS   C N   
1505 C CA  . CYS   B 52  ? 0.1792 0.1708 0.1614 0.0260  -0.0190 0.0088  58  CYS   C CA  
1506 C C   . CYS   B 52  ? 0.1743 0.1703 0.1657 0.0251  -0.0189 0.0076  58  CYS   C C   
1507 O O   . CYS   B 52  ? 0.1782 0.1753 0.1727 0.0234  -0.0175 0.0064  58  CYS   C O   
1508 C CB  . CYS   B 52  ? 0.1778 0.1666 0.1584 0.0256  -0.0156 0.0109  58  CYS   C CB  
1509 S SG  . CYS   B 52  ? 0.1926 0.1761 0.1645 0.0270  -0.0150 0.0133  58  CYS   C SG  
1510 N N   . GLN   B 53  ? 0.1677 0.1659 0.1637 0.0264  -0.0201 0.0084  59  GLN   C N   
1511 C CA  . GLN   B 53  ? 0.1803 0.1824 0.1851 0.0260  -0.0190 0.0081  59  GLN   C CA  
1512 C C   . GLN   B 53  ? 0.1614 0.1625 0.1669 0.0267  -0.0165 0.0099  59  GLN   C C   
1513 O O   . GLN   B 53  ? 0.1633 0.1672 0.1753 0.0270  -0.0154 0.0101  59  GLN   C O   
1514 C CB  . GLN   B 53  ? 0.1743 0.1804 0.1859 0.0268  -0.0224 0.0071  59  GLN   C CB  
1515 C CG  . GLN   B 53  ? 0.2134 0.2205 0.2254 0.0254  -0.0246 0.0045  59  GLN   C CG  
1516 C CD  . GLN   B 53  ? 0.2440 0.2557 0.2648 0.0255  -0.0280 0.0031  59  GLN   C CD  
1517 O OE1 . GLN   B 53  ? 0.2610 0.2731 0.2797 0.0259  -0.0327 0.0018  59  GLN   C OE1 
1518 N NE2 . GLN   B 53  ? 0.2183 0.2335 0.2491 0.0251  -0.0261 0.0035  59  GLN   C NE2 
1519 N N   . THR   B 54  ? 0.1674 0.1644 0.1666 0.0271  -0.0153 0.0112  60  THR   C N   
1520 C CA  . THR   B 54  ? 0.1812 0.1765 0.1802 0.0273  -0.0128 0.0121  60  THR   C CA  
1521 C C   . THR   B 54  ? 0.1827 0.1746 0.1765 0.0256  -0.0110 0.0127  60  THR   C C   
1522 O O   . THR   B 54  ? 0.1856 0.1754 0.1753 0.0252  -0.0115 0.0130  60  THR   C O   
1523 C CB  . THR   B 54  ? 0.2194 0.2129 0.2179 0.0297  -0.0132 0.0131  60  THR   C CB  
1524 O OG1 . THR   B 54  ? 0.2869 0.2769 0.2793 0.0303  -0.0143 0.0140  60  THR   C OG1 
1525 C CG2 . THR   B 54  ? 0.2213 0.2186 0.2262 0.0316  -0.0154 0.0130  60  THR   C CG2 
1526 N N   . GLY   B 55  ? 0.1628 0.1544 0.1572 0.0245  -0.0090 0.0129  61  GLY   C N   
1527 C CA  . GLY   B 55  ? 0.1681 0.1571 0.1589 0.0226  -0.0079 0.0135  61  GLY   C CA  
1528 C C   . GLY   B 55  ? 0.1583 0.1469 0.1489 0.0216  -0.0064 0.0135  61  GLY   C C   
1529 O O   . GLY   B 55  ? 0.1784 0.1675 0.1702 0.0229  -0.0056 0.0130  61  GLY   C O   
1530 N N   . VAL   B 56  ? 0.1508 0.1386 0.1399 0.0195  -0.0062 0.0141  62  VAL   C N   
1531 C CA  . VAL   B 56  ? 0.1435 0.1306 0.1308 0.0182  -0.0054 0.0141  62  VAL   C CA  
1532 C C   . VAL   B 56  ? 0.1431 0.1331 0.1327 0.0162  -0.0057 0.0153  62  VAL   C C   
1533 O O   . VAL   B 56  ? 0.1572 0.1473 0.1480 0.0151  -0.0062 0.0162  62  VAL   C O   
1534 C CB  . VAL   B 56  ? 0.1519 0.1341 0.1346 0.0174  -0.0057 0.0137  62  VAL   C CB  
1535 C CG1 . VAL   B 56  ? 0.1869 0.1680 0.1666 0.0155  -0.0057 0.0133  62  VAL   C CG1 
1536 C CG2 . VAL   B 56  ? 0.1735 0.1524 0.1546 0.0197  -0.0050 0.0128  62  VAL   C CG2 
1537 N N   . TYR   B 57  ? 0.1513 0.1432 0.1412 0.0157  -0.0051 0.0158  63  TYR   C N   
1538 C CA  . TYR   B 57  ? 0.1424 0.1373 0.1350 0.0138  -0.0055 0.0177  63  TYR   C CA  
1539 C C   . TYR   B 57  ? 0.1510 0.1447 0.1390 0.0123  -0.0062 0.0183  63  TYR   C C   
1540 O O   . TYR   B 57  ? 0.1662 0.1578 0.1495 0.0130  -0.0053 0.0171  63  TYR   C O   
1541 C CB  . TYR   B 57  ? 0.1417 0.1408 0.1401 0.0145  -0.0043 0.0186  63  TYR   C CB  
1542 C CG  . TYR   B 57  ? 0.1473 0.1479 0.1454 0.0152  -0.0028 0.0191  63  TYR   C CG  
1543 C CD1 . TYR   B 57  ? 0.1585 0.1582 0.1560 0.0171  -0.0013 0.0177  63  TYR   C CD1 
1544 C CD2 . TYR   B 57  ? 0.1533 0.1560 0.1521 0.0140  -0.0025 0.0214  63  TYR   C CD2 
1545 C CE1 . TYR   B 57  ? 0.1639 0.1648 0.1616 0.0179  0.0010  0.0184  63  TYR   C CE1 
1546 C CE2 . TYR   B 57  ? 0.1619 0.1656 0.1598 0.0148  -0.0004 0.0223  63  TYR   C CE2 
1547 C CZ  . TYR   B 57  ? 0.1693 0.1719 0.1664 0.0167  0.0016  0.0207  63  TYR   C CZ  
1548 O OH  . TYR   B 57  ? 0.1959 0.1994 0.1926 0.0178  0.0044  0.0217  63  TYR   C OH  
1549 N N   . TYR   B 58  ? 0.1497 0.1452 0.1396 0.0103  -0.0075 0.0204  64  TYR   C N   
1550 C CA  . TYR   B 58  ? 0.1552 0.1503 0.1408 0.0085  -0.0091 0.0213  64  TYR   C CA  
1551 C C   . TYR   B 58  ? 0.1613 0.1598 0.1480 0.0088  -0.0082 0.0234  64  TYR   C C   
1552 O O   . TYR   B 58  ? 0.1620 0.1642 0.1555 0.0087  -0.0078 0.0257  64  TYR   C O   
1553 C CB  . TYR   B 58  ? 0.1674 0.1627 0.1549 0.0061  -0.0117 0.0228  64  TYR   C CB  
1554 C CG  . TYR   B 58  ? 0.1818 0.1765 0.1641 0.0041  -0.0143 0.0235  64  TYR   C CG  
1555 C CD1 . TYR   B 58  ? 0.1926 0.1829 0.1666 0.0038  -0.0148 0.0207  64  TYR   C CD1 
1556 C CD2 . TYR   B 58  ? 0.1877 0.1861 0.1731 0.0026  -0.0163 0.0268  64  TYR   C CD2 
1557 C CE1 . TYR   B 58  ? 0.2035 0.1928 0.1711 0.0018  -0.0175 0.0208  64  TYR   C CE1 
1558 C CE2 . TYR   B 58  ? 0.1987 0.1968 0.1784 0.0006  -0.0194 0.0275  64  TYR   C CE2 
1559 C CZ  . TYR   B 58  ? 0.2007 0.1940 0.1710 0.0001  -0.0201 0.0242  64  TYR   C CZ  
1560 O OH  . TYR   B 58  ? 0.2586 0.2509 0.2214 -0.0019 -0.0234 0.0243  64  TYR   C OH  
1561 N N   . CYS   B 59  ? 0.1605 0.1574 0.1404 0.0090  -0.0077 0.0229  65  CYS   C N   
1562 C CA  . CYS   B 59  ? 0.1644 0.1640 0.1436 0.0093  -0.0064 0.0253  65  CYS   C CA  
1563 C C   . CYS   B 59  ? 0.1777 0.1765 0.1499 0.0072  -0.0093 0.0267  65  CYS   C C   
1564 O O   . CYS   B 59  ? 0.1972 0.1921 0.1601 0.0068  -0.0096 0.0245  65  CYS   C O   
1565 C CB  . CYS   B 59  ? 0.1542 0.1523 0.1305 0.0116  -0.0028 0.0237  65  CYS   C CB  
1566 S SG  . CYS   B 59  ? 0.1983 0.1987 0.1724 0.0123  -0.0002 0.0268  65  CYS   C SG  
1567 N N   . SER   B 60  ? 0.1936 0.1962 0.1705 0.0058  -0.0116 0.0303  66  SER   C N   
1568 C CA  . SER   B 60  ? 0.2076 0.2101 0.1787 0.0035  -0.0154 0.0320  66  SER   C CA  
1569 C C   . SER   B 60  ? 0.2124 0.2137 0.1736 0.0040  -0.0144 0.0326  66  SER   C C   
1570 O O   . SER   B 60  ? 0.2450 0.2434 0.1965 0.0024  -0.0173 0.0314  66  SER   C O   
1571 C CB  . SER   B 60  ? 0.2293 0.2365 0.2088 0.0023  -0.0178 0.0363  66  SER   C CB  
1572 O OG  . SER   B 60  ? 0.2748 0.2823 0.2490 0.0000  -0.0224 0.0381  66  SER   C OG  
1573 N N   . SER   B 61  ? 0.1991 0.2023 0.1626 0.0062  -0.0103 0.0343  67  SER   C N   
1574 C CA  . SER   B 61  ? 0.2150 0.2169 0.1690 0.0069  -0.0084 0.0354  67  SER   C CA  
1575 C C   . SER   B 61  ? 0.2422 0.2383 0.1853 0.0076  -0.0064 0.0308  67  SER   C C   
1576 O O   . SER   B 61  ? 0.2653 0.2589 0.1976 0.0079  -0.0051 0.0310  67  SER   C O   
1577 C CB  . SER   B 61  ? 0.2252 0.2305 0.1857 0.0091  -0.0040 0.0386  67  SER   C CB  
1578 O OG  . SER   B 61  ? 0.2144 0.2194 0.1812 0.0110  -0.0002 0.0360  67  SER   C OG  
1579 N N   . ARG   B 62  ? 0.2294 0.2226 0.1746 0.0080  -0.0059 0.0268  68  ARG   C N   
1580 C CA  . ARG   B 62  ? 0.2376 0.2248 0.1736 0.0087  -0.0039 0.0223  68  ARG   C CA  
1581 C C   . ARG   B 62  ? 0.2320 0.2153 0.1642 0.0063  -0.0081 0.0190  68  ARG   C C   
1582 O O   . ARG   B 62  ? 0.2540 0.2318 0.1799 0.0067  -0.0067 0.0150  68  ARG   C O   
1583 C CB  . ARG   B 62  ? 0.2456 0.2324 0.1879 0.0115  0.0007  0.0205  68  ARG   C CB  
1584 C CG  . ARG   B 62  ? 0.3026 0.2931 0.2501 0.0137  0.0051  0.0234  68  ARG   C CG  
1585 C CD  . ARG   B 62  ? 0.2905 0.2777 0.2277 0.0148  0.0088  0.0231  68  ARG   C CD  
1586 N NE  . ARG   B 62  ? 0.3151 0.3057 0.2577 0.0169  0.0136  0.0263  68  ARG   C NE  
1587 C CZ  . ARG   B 62  ? 0.3529 0.3469 0.2962 0.0166  0.0138  0.0308  68  ARG   C CZ  
1588 N NH1 . ARG   B 62  ? 0.4005 0.3954 0.3390 0.0143  0.0091  0.0329  68  ARG   C NH1 
1589 N NH2 . ARG   B 62  ? 0.3438 0.3402 0.2922 0.0187  0.0189  0.0336  68  ARG   C NH2 
1590 N N   . ARG   B 63  ? 0.2345 0.2207 0.1726 0.0042  -0.0125 0.0208  69  ARG   C N   
1591 C CA  . ARG   B 63  ? 0.2513 0.2345 0.1891 0.0019  -0.0162 0.0182  69  ARG   C CA  
1592 C C   . ARG   B 63  ? 0.2569 0.2361 0.1963 0.0035  -0.0134 0.0146  69  ARG   C C   
1593 O O   . ARG   B 63  ? 0.2883 0.2620 0.2217 0.0025  -0.0141 0.0109  69  ARG   C O   
1594 C CB  . ARG   B 63  ? 0.2661 0.2456 0.1926 -0.0007 -0.0200 0.0165  69  ARG   C CB  
1595 C CG  . ARG   B 63  ? 0.3092 0.2927 0.2339 -0.0025 -0.0239 0.0205  69  ARG   C CG  
1596 C CD  . ARG   B 63  ? 0.3519 0.3400 0.2874 -0.0044 -0.0280 0.0235  69  ARG   C CD  
1597 N NE  . ARG   B 63  ? 0.3790 0.3697 0.3114 -0.0069 -0.0335 0.0265  69  ARG   C NE  
1598 C CZ  . ARG   B 63  ? 0.3944 0.3905 0.3306 -0.0065 -0.0342 0.0318  69  ARG   C CZ  
1599 N NH1 . ARG   B 63  ? 0.4009 0.3995 0.3347 -0.0088 -0.0399 0.0348  69  ARG   C NH1 
1600 N NH2 . ARG   B 63  ? 0.3757 0.3748 0.3186 -0.0037 -0.0294 0.0342  69  ARG   C NH2 
1601 N N   . LYS   B 64  ? 0.2254 0.2073 0.1728 0.0060  -0.0102 0.0155  70  LYS   C N   
1602 C CA  . LYS   B 64  ? 0.2354 0.2140 0.1843 0.0079  -0.0076 0.0127  70  LYS   C CA  
1603 C C   . LYS   B 64  ? 0.2223 0.2043 0.1812 0.0091  -0.0072 0.0141  70  LYS   C C   
1604 O O   . LYS   B 64  ? 0.2092 0.1961 0.1741 0.0094  -0.0070 0.0168  70  LYS   C O   
1605 C CB  . LYS   B 64  ? 0.2812 0.2582 0.2264 0.0105  -0.0030 0.0115  70  LYS   C CB  
1606 C CG  . LYS   B 64  ? 0.4151 0.3856 0.3489 0.0100  -0.0021 0.0081  70  LYS   C CG  
1607 C CD  . LYS   B 64  ? 0.5333 0.5016 0.4651 0.0131  0.0035  0.0067  70  LYS   C CD  
1608 C CE  . LYS   B 64  ? 0.6121 0.5738 0.5314 0.0126  0.0050  0.0034  70  LYS   C CE  
1609 N NZ  . LYS   B 64  ? 0.6737 0.6364 0.5847 0.0105  0.0028  0.0049  70  LYS   C NZ  
1610 N N   . HIS   B 65  ? 0.1996 0.1784 0.1599 0.0097  -0.0069 0.0121  71  HIS   C N   
1611 C CA  . HIS   B 65  ? 0.1966 0.1776 0.1643 0.0113  -0.0062 0.0130  71  HIS   C CA  
1612 C C   . HIS   B 65  ? 0.2215 0.2018 0.1898 0.0142  -0.0032 0.0117  71  HIS   C C   
1613 O O   . HIS   B 65  ? 0.2659 0.2416 0.2299 0.0151  -0.0017 0.0095  71  HIS   C O   
1614 C CB  . HIS   B 65  ? 0.1976 0.1757 0.1663 0.0103  -0.0078 0.0123  71  HIS   C CB  
1615 C CG  . HIS   B 65  ? 0.1851 0.1646 0.1556 0.0074  -0.0107 0.0139  71  HIS   C CG  
1616 N ND1 . HIS   B 65  ? 0.2301 0.2129 0.2072 0.0071  -0.0111 0.0162  71  HIS   C ND1 
1617 C CD2 . HIS   B 65  ? 0.1937 0.1716 0.1606 0.0048  -0.0132 0.0136  71  HIS   C CD2 
1618 C CE1 . HIS   B 65  ? 0.2054 0.1887 0.1837 0.0045  -0.0136 0.0174  71  HIS   C CE1 
1619 N NE2 . HIS   B 65  ? 0.2235 0.2041 0.1960 0.0029  -0.0154 0.0159  71  HIS   C NE2 
1620 N N   . TYR   B 66  ? 0.1853 0.1698 0.1598 0.0159  -0.0020 0.0130  72  TYR   C N   
1621 C CA  . TYR   B 66  ? 0.1835 0.1681 0.1602 0.0186  0.0006  0.0121  72  TYR   C CA  
1622 C C   . TYR   B 66  ? 0.1703 0.1561 0.1526 0.0201  -0.0003 0.0122  72  TYR   C C   
1623 O O   . TYR   B 66  ? 0.1735 0.1625 0.1598 0.0194  -0.0018 0.0133  72  TYR   C O   
1624 C CB  . TYR   B 66  ? 0.1965 0.1855 0.1771 0.0194  0.0025  0.0136  72  TYR   C CB  
1625 C CG  . TYR   B 66  ? 0.1980 0.1857 0.1723 0.0188  0.0042  0.0140  72  TYR   C CG  
1626 C CD1 . TYR   B 66  ? 0.2246 0.2088 0.1943 0.0203  0.0074  0.0123  72  TYR   C CD1 
1627 C CD2 . TYR   B 66  ? 0.2000 0.1902 0.1732 0.0169  0.0030  0.0161  72  TYR   C CD2 
1628 C CE1 . TYR   B 66  ? 0.2339 0.2167 0.1966 0.0198  0.0095  0.0126  72  TYR   C CE1 
1629 C CE2 . TYR   B 66  ? 0.2191 0.2082 0.1855 0.0164  0.0044  0.0168  72  TYR   C CE2 
1630 C CZ  . TYR   B 66  ? 0.2249 0.2101 0.1854 0.0179  0.0077  0.0149  72  TYR   C CZ  
1631 O OH  . TYR   B 66  ? 0.2524 0.2362 0.2047 0.0175  0.0093  0.0156  72  TYR   C OH  
1632 N N   . PRO   B 67  ? 0.1748 0.1580 0.1572 0.0221  0.0006  0.0111  73  PRO   C N   
1633 C CA  . PRO   B 67  ? 0.1691 0.1541 0.1564 0.0238  -0.0006 0.0115  73  PRO   C CA  
1634 C C   . PRO   B 67  ? 0.1741 0.1641 0.1682 0.0250  -0.0001 0.0121  73  PRO   C C   
1635 O O   . PRO   B 67  ? 0.2070 0.1976 0.2026 0.0261  0.0025  0.0120  73  PRO   C O   
1636 C CB  . PRO   B 67  ? 0.2030 0.1839 0.1889 0.0257  0.0003  0.0107  73  PRO   C CB  
1637 C CG  . PRO   B 67  ? 0.2350 0.2125 0.2167 0.0257  0.0031  0.0093  73  PRO   C CG  
1638 C CD  . PRO   B 67  ? 0.1984 0.1770 0.1765 0.0232  0.0029  0.0094  73  PRO   C CD  
1639 N N   . VAL   B 68  ? 0.1601 0.1534 0.1584 0.0249  -0.0022 0.0126  74  VAL   C N   
1640 C CA  . VAL   B 68  ? 0.1595 0.1576 0.1653 0.0256  -0.0021 0.0129  74  VAL   C CA  
1641 C C   . VAL   B 68  ? 0.1533 0.1530 0.1623 0.0265  -0.0050 0.0125  74  VAL   C C   
1642 O O   . VAL   B 68  ? 0.1577 0.1555 0.1628 0.0259  -0.0068 0.0124  74  VAL   C O   
1643 C CB  . VAL   B 68  ? 0.1765 0.1774 0.1843 0.0236  -0.0016 0.0137  74  VAL   C CB  
1644 C CG1 . VAL   B 68  ? 0.2143 0.2146 0.2195 0.0230  0.0012  0.0146  74  VAL   C CG1 
1645 C CG2 . VAL   B 68  ? 0.2006 0.2006 0.2055 0.0217  -0.0035 0.0139  74  VAL   C CG2 
1646 N N   . SER   B 69  ? 0.1543 0.1577 0.1708 0.0276  -0.0053 0.0124  75  SER   C N   
1647 C CA  . SER   B 69  ? 0.1587 0.1649 0.1794 0.0278  -0.0086 0.0117  75  SER   C CA  
1648 C C   . SER   B 69  ? 0.1488 0.1580 0.1737 0.0259  -0.0084 0.0113  75  SER   C C   
1649 O O   . SER   B 69  ? 0.1440 0.1549 0.1724 0.0254  -0.0056 0.0122  75  SER   C O   
1650 C CB  . SER   B 69  ? 0.1920 0.2012 0.2205 0.0299  -0.0093 0.0119  75  SER   C CB  
1651 O OG  . SER   B 69  ? 0.2447 0.2512 0.2704 0.0319  -0.0094 0.0125  75  SER   C OG  
1652 N N   . PHE   B 70  ? 0.1382 0.1475 0.1620 0.0248  -0.0108 0.0102  76  PHE   C N   
1653 C CA  . PHE   B 70  ? 0.1440 0.1554 0.1721 0.0230  -0.0102 0.0097  76  PHE   C CA  
1654 C C   . PHE   B 70  ? 0.1428 0.1559 0.1744 0.0227  -0.0135 0.0075  76  PHE   C C   
1655 O O   . PHE   B 70  ? 0.1541 0.1659 0.1814 0.0236  -0.0164 0.0066  76  PHE   C O   
1656 C CB  . PHE   B 70  ? 0.1564 0.1655 0.1795 0.0213  -0.0086 0.0104  76  PHE   C CB  
1657 C CG  . PHE   B 70  ? 0.1435 0.1490 0.1589 0.0213  -0.0100 0.0099  76  PHE   C CG  
1658 C CD1 . PHE   B 70  ? 0.1533 0.1556 0.1625 0.0219  -0.0096 0.0109  76  PHE   C CD1 
1659 C CD2 . PHE   B 70  ? 0.1547 0.1595 0.1690 0.0205  -0.0111 0.0085  76  PHE   C CD2 
1660 C CE1 . PHE   B 70  ? 0.1545 0.1535 0.1576 0.0219  -0.0103 0.0109  76  PHE   C CE1 
1661 C CE2 . PHE   B 70  ? 0.1570 0.1582 0.1640 0.0206  -0.0115 0.0085  76  PHE   C CE2 
1662 C CZ  . PHE   B 70  ? 0.1624 0.1609 0.1642 0.0214  -0.0111 0.0099  76  PHE   C CZ  
1663 N N   . SER   B 71  ? 0.1363 0.1522 0.1754 0.0215  -0.0130 0.0067  77  SER   C N   
1664 C CA  . SER   B 71  ? 0.1504 0.1679 0.1936 0.0208  -0.0163 0.0041  77  SER   C CA  
1665 C C   . SER   B 71  ? 0.1694 0.1837 0.2059 0.0197  -0.0173 0.0021  77  SER   C C   
1666 O O   . SER   B 71  ? 0.1712 0.1825 0.2013 0.0193  -0.0152 0.0031  77  SER   C O   
1667 C CB  . SER   B 71  ? 0.1467 0.1680 0.2017 0.0199  -0.0150 0.0039  77  SER   C CB  
1668 O OG  . SER   B 71  ? 0.1706 0.1913 0.2268 0.0184  -0.0116 0.0048  77  SER   C OG  
1669 N N   . LYS   B 72  ? 0.1732 0.1881 0.2113 0.0190  -0.0206 -0.0009 78  LYS   C N   
1670 C CA  . LYS   B 72  ? 0.1731 0.1843 0.2040 0.0180  -0.0212 -0.0034 78  LYS   C CA  
1671 C C   . LYS   B 72  ? 0.1701 0.1811 0.2061 0.0161  -0.0178 -0.0041 78  LYS   C C   
1672 O O   . LYS   B 72  ? 0.1845 0.1986 0.2308 0.0154  -0.0169 -0.0039 78  LYS   C O   
1673 C CB  . LYS   B 72  ? 0.2148 0.2266 0.2452 0.0178  -0.0264 -0.0068 78  LYS   C CB  
1674 C CG  . LYS   B 72  ? 0.2629 0.2750 0.2882 0.0198  -0.0301 -0.0056 78  LYS   C CG  
1675 C CD  . LYS   B 72  ? 0.4141 0.4248 0.4330 0.0197  -0.0355 -0.0088 78  LYS   C CD  
1676 C CE  . LYS   B 72  ? 0.5391 0.5485 0.5496 0.0219  -0.0384 -0.0066 78  LYS   C CE  
1677 N NZ  . LYS   B 72  ? 0.6058 0.6123 0.6057 0.0219  -0.0425 -0.0090 78  LYS   C NZ  
1678 N N   . PRO   B 73  ? 0.1651 0.1725 0.1953 0.0155  -0.0156 -0.0046 79  PRO   C N   
1679 C CA  . PRO   B 73  ? 0.1749 0.1820 0.2112 0.0139  -0.0120 -0.0047 79  PRO   C CA  
1680 C C   . PRO   B 73  ? 0.1774 0.1858 0.2218 0.0126  -0.0132 -0.0082 79  PRO   C C   
1681 O O   . PRO   B 73  ? 0.1928 0.1996 0.2334 0.0122  -0.0167 -0.0121 79  PRO   C O   
1682 C CB  . PRO   B 73  ? 0.1949 0.1975 0.2233 0.0137  -0.0098 -0.0053 79  PRO   C CB  
1683 C CG  . PRO   B 73  ? 0.2232 0.2237 0.2412 0.0151  -0.0118 -0.0048 79  PRO   C CG  
1684 C CD  . PRO   B 73  ? 0.1783 0.1815 0.1968 0.0162  -0.0159 -0.0047 79  PRO   C CD  
1685 N N   . SER   B 74  ? 0.1501 0.1613 0.2054 0.0118  -0.0109 -0.0068 80  SER   C N   
1686 C CA  . SER   B 74  ? 0.1721 0.1849 0.2372 0.0104  -0.0121 -0.0098 80  SER   C CA  
1687 C C   . SER   B 74  ? 0.1615 0.1753 0.2369 0.0094  -0.0076 -0.0078 80  SER   C C   
1688 O O   . SER   B 74  ? 0.1601 0.1740 0.2349 0.0099  -0.0042 -0.0038 80  SER   C O   
1689 C CB  . SER   B 74  ? 0.2215 0.2386 0.2926 0.0110  -0.0151 -0.0093 80  SER   C CB  
1690 O OG  . SER   B 74  ? 0.3331 0.3497 0.3958 0.0121  -0.0194 -0.0103 80  SER   C OG  
1691 N N   . LEU   B 75  ? 0.1695 0.1841 0.2547 0.0079  -0.0080 -0.0105 81  LEU   C N   
1692 C CA  . LEU   B 75  ? 0.1933 0.2090 0.2903 0.0069  -0.0039 -0.0086 81  LEU   C CA  
1693 C C   . LEU   B 75  ? 0.1953 0.2159 0.3013 0.0076  -0.0033 -0.0050 81  LEU   C C   
1694 O O   . LEU   B 75  ? 0.2220 0.2451 0.3340 0.0072  -0.0063 -0.0069 81  LEU   C O   
1695 C CB  . LEU   B 75  ? 0.2247 0.2382 0.3282 0.0049  -0.0044 -0.0139 81  LEU   C CB  
1696 C CG  . LEU   B 75  ? 0.2536 0.2670 0.3695 0.0038  0.0002  -0.0125 81  LEU   C CG  
1697 C CD1 . LEU   B 75  ? 0.2406 0.2512 0.3528 0.0044  0.0046  -0.0098 81  LEU   C CD1 
1698 C CD2 . LEU   B 75  ? 0.2788 0.2897 0.4009 0.0016  -0.0012 -0.0188 81  LEU   C CD2 
1699 N N   . ILE   B 76  ? 0.1857 0.2077 0.2920 0.0086  0.0002  0.0004  82  ILE   C N   
1700 C CA  . ILE   B 76  ? 0.1989 0.2249 0.3108 0.0096  0.0016  0.0044  82  ILE   C CA  
1701 C C   . ILE   B 76  ? 0.2079 0.2352 0.3291 0.0093  0.0063  0.0085  82  ILE   C C   
1702 O O   . ILE   B 76  ? 0.1944 0.2199 0.3133 0.0091  0.0086  0.0106  82  ILE   C O   
1703 C CB  . ILE   B 76  ? 0.2347 0.2606 0.3355 0.0114  0.0012  0.0071  82  ILE   C CB  
1704 C CG1 . ILE   B 76  ? 0.2826 0.3073 0.3750 0.0119  -0.0032 0.0036  82  ILE   C CG1 
1705 C CG2 . ILE   B 76  ? 0.2504 0.2794 0.3550 0.0126  0.0037  0.0114  82  ILE   C CG2 
1706 C CD1 . ILE   B 76  ? 0.3016 0.3259 0.3851 0.0135  -0.0037 0.0055  82  ILE   C CD1 
1707 N N   . PHE   B 77  ? 0.2010 0.2314 0.3330 0.0093  0.0078  0.0102  83  PHE   C N   
1708 C CA  . PHE   B 77  ? 0.2041 0.2358 0.3448 0.0093  0.0126  0.0149  83  PHE   C CA  
1709 C C   . PHE   B 77  ? 0.2113 0.2438 0.3437 0.0110  0.0147  0.0203  83  PHE   C C   
1710 O O   . PHE   B 77  ? 0.2478 0.2817 0.3761 0.0123  0.0141  0.0209  83  PHE   C O   
1711 C CB  . PHE   B 77  ? 0.2089 0.2436 0.3644 0.0087  0.0140  0.0152  83  PHE   C CB  
1712 C CG  . PHE   B 77  ? 0.2219 0.2572 0.3872 0.0085  0.0192  0.0199  83  PHE   C CG  
1713 C CD1 . PHE   B 77  ? 0.2336 0.2666 0.4050 0.0071  0.0204  0.0187  83  PHE   C CD1 
1714 C CD2 . PHE   B 77  ? 0.2377 0.2754 0.4051 0.0100  0.0232  0.0259  83  PHE   C CD2 
1715 C CE1 . PHE   B 77  ? 0.2500 0.2835 0.4307 0.0071  0.0253  0.0237  83  PHE   C CE1 
1716 C CE2 . PHE   B 77  ? 0.2424 0.2805 0.4183 0.0099  0.0280  0.0310  83  PHE   C CE2 
1717 C CZ  . PHE   B 77  ? 0.2430 0.2791 0.4260 0.0085  0.0289  0.0300  83  PHE   C CZ  
1718 N N   . VAL   B 78  ? 0.1728 0.2044 0.3033 0.0111  0.0172  0.0242  84  VAL   C N   
1719 C CA  . VAL   B 78  ? 0.1688 0.2009 0.2906 0.0124  0.0186  0.0290  84  VAL   C CA  
1720 C C   . VAL   B 78  ? 0.1670 0.2009 0.2967 0.0128  0.0231  0.0349  84  VAL   C C   
1721 O O   . VAL   B 78  ? 0.1640 0.1977 0.3021 0.0119  0.0248  0.0360  84  VAL   C O   
1722 C CB  . VAL   B 78  ? 0.1842 0.2139 0.2967 0.0121  0.0170  0.0292  84  VAL   C CB  
1723 C CG1 . VAL   B 78  ? 0.2000 0.2301 0.3033 0.0131  0.0175  0.0337  84  VAL   C CG1 
1724 C CG2 . VAL   B 78  ? 0.1973 0.2248 0.3026 0.0118  0.0132  0.0237  84  VAL   C CG2 
1725 N N   . GLU   B 79  ? 0.1603 0.1957 0.2867 0.0141  0.0253  0.0387  85  GLU   C N   
1726 C CA  . GLU   B 79  ? 0.1668 0.2037 0.2985 0.0147  0.0298  0.0450  85  GLU   C CA  
1727 C C   . GLU   B 79  ? 0.1669 0.2030 0.2933 0.0146  0.0297  0.0492  85  GLU   C C   
1728 O O   . GLU   B 79  ? 0.1617 0.1963 0.2791 0.0143  0.0265  0.0476  85  GLU   C O   
1729 C CB  . GLU   B 79  ? 0.2041 0.2419 0.3305 0.0164  0.0322  0.0478  85  GLU   C CB  
1730 C CG  . GLU   B 79  ? 0.2541 0.2936 0.3895 0.0167  0.0334  0.0453  85  GLU   C CG  
1731 C CD  . GLU   B 79  ? 0.3332 0.3744 0.4860 0.0157  0.0359  0.0457  85  GLU   C CD  
1732 O OE1 . GLU   B 79  ? 0.3636 0.4052 0.5219 0.0157  0.0394  0.0507  85  GLU   C OE1 
1733 O OE2 . GLU   B 79  ? 0.3388 0.3809 0.5001 0.0149  0.0339  0.0411  85  GLU   C OE2 
1734 N N   . ALA   B 80  ? 0.1851 0.2223 0.3183 0.0149  0.0333  0.0549  86  ALA   C N   
1735 C CA  . ALA   B 80  ? 0.1942 0.2314 0.3246 0.0150  0.0332  0.0598  86  ALA   C CA  
1736 C C   . ALA   B 80  ? 0.2127 0.2494 0.3272 0.0156  0.0307  0.0615  86  ALA   C C   
1737 O O   . ALA   B 80  ? 0.2288 0.2655 0.3356 0.0165  0.0314  0.0615  86  ALA   C O   
1738 C CB  . ALA   B 80  ? 0.2021 0.2408 0.3417 0.0157  0.0378  0.0666  86  ALA   C CB  
1739 N N   . SER   B 81  ? 0.1984 0.2345 0.3087 0.0149  0.0278  0.0621  87  SER   C N   
1740 C CA  . SER   B 81  ? 0.2137 0.2495 0.3103 0.0151  0.0250  0.0638  87  SER   C CA  
1741 C C   . SER   B 81  ? 0.2234 0.2607 0.3213 0.0151  0.0248  0.0706  87  SER   C C   
1742 O O   . SER   B 81  ? 0.2138 0.2522 0.3238 0.0152  0.0274  0.0740  87  SER   C O   
1743 C CB  . SER   B 81  ? 0.2004 0.2344 0.2907 0.0142  0.0210  0.0583  87  SER   C CB  
1744 O OG  . SER   B 81  ? 0.2105 0.2444 0.3080 0.0133  0.0203  0.0585  87  SER   C OG  
1745 N N   . GLU   B 82  ? 0.2495 0.2867 0.3358 0.0149  0.0215  0.0724  88  GLU   C N   
1746 C CA  . GLU   B 82  ? 0.2574 0.2965 0.3454 0.0148  0.0204  0.0791  88  GLU   C CA  
1747 C C   . GLU   B 82  ? 0.2546 0.2942 0.3533 0.0140  0.0194  0.0789  88  GLU   C C   
1748 O O   . GLU   B 82  ? 0.2701 0.3117 0.3752 0.0142  0.0195  0.0848  88  GLU   C O   
1749 C CB  . GLU   B 82  ? 0.3267 0.3658 0.4001 0.0146  0.0166  0.0815  88  GLU   C CB  
1750 C CG  . GLU   B 82  ? 0.4134 0.4509 0.4785 0.0133  0.0120  0.0767  88  GLU   C CG  
1751 C CD  . GLU   B 82  ? 0.5041 0.5416 0.5560 0.0128  0.0080  0.0797  88  GLU   C CD  
1752 O OE1 . GLU   B 82  ? 0.5307 0.5677 0.5741 0.0136  0.0095  0.0819  88  GLU   C OE1 
1753 O OE2 . GLU   B 82  ? 0.5206 0.5587 0.5710 0.0114  0.0036  0.0799  88  GLU   C OE2 
1754 N N   . TYR   B 83  ? 0.2132 0.2509 0.3144 0.0133  0.0189  0.0723  89  TYR   C N   
1755 C CA  . TYR   B 83  ? 0.2110 0.2486 0.3206 0.0126  0.0185  0.0716  89  TYR   C CA  
1756 C C   . TYR   B 83  ? 0.2171 0.2529 0.3379 0.0124  0.0217  0.0672  89  TYR   C C   
1757 O O   . TYR   B 83  ? 0.2254 0.2607 0.3543 0.0121  0.0225  0.0671  89  TYR   C O   
1758 C CB  . TYR   B 83  ? 0.2044 0.2408 0.3053 0.0116  0.0144  0.0685  89  TYR   C CB  
1759 C CG  . TYR   B 83  ? 0.1945 0.2286 0.2850 0.0115  0.0130  0.0622  89  TYR   C CG  
1760 C CD1 . TYR   B 83  ? 0.2088 0.2428 0.2873 0.0117  0.0112  0.0627  89  TYR   C CD1 
1761 C CD2 . TYR   B 83  ? 0.1943 0.2261 0.2869 0.0113  0.0139  0.0560  89  TYR   C CD2 
1762 C CE1 . TYR   B 83  ? 0.1931 0.2248 0.2635 0.0118  0.0104  0.0573  89  TYR   C CE1 
1763 C CE2 . TYR   B 83  ? 0.2108 0.2408 0.2949 0.0113  0.0125  0.0510  89  TYR   C CE2 
1764 C CZ  . TYR   B 83  ? 0.2009 0.2309 0.2744 0.0117  0.0109  0.0517  89  TYR   C CZ  
1765 O OH  . TYR   B 83  ? 0.2093 0.2374 0.2755 0.0120  0.0100  0.0471  89  TYR   C OH  
1766 N N   . TYR   B 84  ? 0.1822 0.2172 0.3047 0.0126  0.0237  0.0637  90  TYR   C N   
1767 C CA  . TYR   B 84  ? 0.1760 0.2095 0.3098 0.0122  0.0265  0.0597  90  TYR   C CA  
1768 C C   . TYR   B 84  ? 0.1652 0.1997 0.3049 0.0127  0.0295  0.0609  90  TYR   C C   
1769 O O   . TYR   B 84  ? 0.1700 0.2056 0.3025 0.0134  0.0292  0.0621  90  TYR   C O   
1770 C CB  . TYR   B 84  ? 0.1733 0.2041 0.3020 0.0115  0.0245  0.0514  90  TYR   C CB  
1771 C CG  . TYR   B 84  ? 0.1459 0.1749 0.2709 0.0109  0.0226  0.0492  90  TYR   C CG  
1772 C CD1 . TYR   B 84  ? 0.1530 0.1809 0.2870 0.0107  0.0247  0.0500  90  TYR   C CD1 
1773 C CD2 . TYR   B 84  ? 0.1497 0.1778 0.2628 0.0108  0.0194  0.0467  90  TYR   C CD2 
1774 C CE1 . TYR   B 84  ? 0.1510 0.1771 0.2822 0.0103  0.0238  0.0481  90  TYR   C CE1 
1775 C CE2 . TYR   B 84  ? 0.1466 0.1729 0.2569 0.0104  0.0182  0.0449  90  TYR   C CE2 
1776 C CZ  . TYR   B 84  ? 0.1473 0.1727 0.2666 0.0102  0.0206  0.0456  90  TYR   C CZ  
1777 O OH  . TYR   B 84  ? 0.1531 0.1766 0.2701 0.0099  0.0202  0.0441  90  TYR   C OH  
1778 N N   . PRO   B 85  ? 0.1610 0.1948 0.3142 0.0123  0.0326  0.0600  91  PRO   C N   
1779 C CA  . PRO   B 85  ? 0.1511 0.1858 0.3113 0.0125  0.0354  0.0600  91  PRO   C CA  
1780 C C   . PRO   B 85  ? 0.1601 0.1939 0.3160 0.0119  0.0332  0.0528  91  PRO   C C   
1781 O O   . PRO   B 85  ? 0.1637 0.1959 0.3115 0.0114  0.0298  0.0477  91  PRO   C O   
1782 C CB  . PRO   B 85  ? 0.1598 0.1933 0.3361 0.0118  0.0388  0.0600  91  PRO   C CB  
1783 C CG  . PRO   B 85  ? 0.1688 0.1996 0.3439 0.0109  0.0370  0.0553  91  PRO   C CG  
1784 C CD  . PRO   B 85  ? 0.1653 0.1970 0.3279 0.0115  0.0339  0.0578  91  PRO   C CD  
1785 N N   . ALA   B 86  ? 0.1504 0.1853 0.3126 0.0120  0.0352  0.0523  92  ALA   C N   
1786 C CA  . ALA   B 86  ? 0.1629 0.1975 0.3242 0.0114  0.0330  0.0458  92  ALA   C CA  
1787 C C   . ALA   B 86  ? 0.1816 0.2138 0.3491 0.0098  0.0315  0.0395  92  ALA   C C   
1788 O O   . ALA   B 86  ? 0.1982 0.2294 0.3770 0.0090  0.0341  0.0402  92  ALA   C O   
1789 C CB  . ALA   B 86  ? 0.1630 0.1998 0.3335 0.0118  0.0361  0.0475  92  ALA   C CB  
1790 N N   . ARG   B 87  ? 0.1759 0.2066 0.3347 0.0093  0.0275  0.0336  93  ARG   C N   
1791 C CA  . ARG   B 87  ? 0.1765 0.2042 0.3376 0.0079  0.0260  0.0275  93  ARG   C CA  
1792 C C   . ARG   B 87  ? 0.1718 0.1984 0.3227 0.0077  0.0214  0.0216  93  ARG   C C   
1793 O O   . ARG   B 87  ? 0.1711 0.1992 0.3130 0.0088  0.0196  0.0227  93  ARG   C O   
1794 C CB  . ARG   B 87  ? 0.1809 0.2063 0.3397 0.0080  0.0271  0.0291  93  ARG   C CB  
1795 C CG  . ARG   B 87  ? 0.1644 0.1895 0.3087 0.0088  0.0245  0.0297  93  ARG   C CG  
1796 C CD  . ARG   B 87  ? 0.1722 0.1959 0.3163 0.0089  0.0258  0.0324  93  ARG   C CD  
1797 N NE  . ARG   B 87  ? 0.1747 0.1977 0.3058 0.0093  0.0229  0.0316  93  ARG   C NE  
1798 C CZ  . ARG   B 87  ? 0.1870 0.2076 0.3148 0.0091  0.0227  0.0301  93  ARG   C CZ  
1799 N NH1 . ARG   B 87  ? 0.1860 0.2043 0.3221 0.0086  0.0256  0.0292  93  ARG   C NH1 
1800 N NH2 . ARG   B 87  ? 0.2130 0.2331 0.3296 0.0094  0.0201  0.0294  93  ARG   C NH2 
1801 N N   . TYR   B 88  ? 0.1921 0.2157 0.3437 0.0064  0.0196  0.0154  94  TYR   C N   
1802 C CA  . TYR   B 88  ? 0.2163 0.2383 0.3567 0.0064  0.0153  0.0102  94  TYR   C CA  
1803 C C   . TYR   B 88  ? 0.1962 0.2158 0.3258 0.0070  0.0152  0.0109  94  TYR   C C   
1804 O O   . TYR   B 88  ? 0.2127 0.2300 0.3452 0.0066  0.0178  0.0114  94  TYR   C O   
1805 C CB  . TYR   B 88  ? 0.2565 0.2759 0.4004 0.0046  0.0131  0.0030  94  TYR   C CB  
1806 C CG  . TYR   B 88  ? 0.3022 0.3244 0.4561 0.0038  0.0116  0.0014  94  TYR   C CG  
1807 C CD1 . TYR   B 88  ? 0.3314 0.3559 0.4810 0.0044  0.0077  0.0000  94  TYR   C CD1 
1808 C CD2 . TYR   B 88  ? 0.3286 0.3514 0.4975 0.0026  0.0146  0.0021  94  TYR   C CD2 
1809 C CE1 . TYR   B 88  ? 0.3514 0.3792 0.5121 0.0037  0.0066  -0.0007 94  TYR   C CE1 
1810 C CE2 . TYR   B 88  ? 0.3504 0.3761 0.5301 0.0018  0.0136  0.0013  94  TYR   C CE2 
1811 C CZ  . TYR   B 88  ? 0.3693 0.3977 0.5452 0.0023  0.0095  -0.0002 94  TYR   C CZ  
1812 O OH  . TYR   B 88  ? 0.4195 0.4511 0.6086 0.0015  0.0089  -0.0007 94  TYR   C OH  
1813 N N   . GLN   B 89  ? 0.1818 0.2017 0.2999 0.0079  0.0125  0.0109  95  GLN   C N   
1814 C CA  . GLN   B 89  ? 0.1679 0.1854 0.2758 0.0084  0.0121  0.0112  95  GLN   C CA  
1815 C C   . GLN   B 89  ? 0.1623 0.1773 0.2615 0.0082  0.0086  0.0055  95  GLN   C C   
1816 O O   . GLN   B 89  ? 0.1682 0.1846 0.2653 0.0085  0.0055  0.0037  95  GLN   C O   
1817 C CB  . GLN   B 89  ? 0.1777 0.1973 0.2792 0.0095  0.0119  0.0162  95  GLN   C CB  
1818 C CG  . GLN   B 89  ? 0.1858 0.2032 0.2783 0.0098  0.0114  0.0167  95  GLN   C CG  
1819 C CD  . GLN   B 89  ? 0.1791 0.1984 0.2683 0.0103  0.0117  0.0222  95  GLN   C CD  
1820 O OE1 . GLN   B 89  ? 0.1803 0.2019 0.2753 0.0105  0.0136  0.0268  95  GLN   C OE1 
1821 N NE2 . GLN   B 89  ? 0.1817 0.1997 0.2613 0.0106  0.0099  0.0221  95  GLN   C NE2 
1822 N N   . SER   B 90  ? 0.1469 0.1580 0.2408 0.0079  0.0091  0.0030  96  SER   C N   
1823 C CA  . SER   B 90  ? 0.1752 0.1834 0.2597 0.0079  0.0060  -0.0021 96  SER   C CA  
1824 C C   . SER   B 90  ? 0.1601 0.1675 0.2328 0.0091  0.0048  -0.0003 96  SER   C C   
1825 O O   . SER   B 90  ? 0.1653 0.1738 0.2375 0.0096  0.0066  0.0042  96  SER   C O   
1826 C CB  . SER   B 90  ? 0.1888 0.1923 0.2734 0.0069  0.0078  -0.0065 96  SER   C CB  
1827 O OG  . SER   B 90  ? 0.1902 0.1919 0.2737 0.0073  0.0115  -0.0037 96  SER   C OG  
1828 N N   . HIS   B 91  ? 0.1516 0.1573 0.2154 0.0095  0.0015  -0.0037 97  HIS   C N   
1829 C CA  . HIS   B 91  ? 0.1511 0.1554 0.2039 0.0106  0.0002  -0.0026 97  HIS   C CA  
1830 C C   . HIS   B 91  ? 0.1551 0.1626 0.2079 0.0114  0.0000  0.0020  97  HIS   C C   
1831 O O   . HIS   B 91  ? 0.1631 0.1696 0.2103 0.0119  0.0007  0.0045  97  HIS   C O   
1832 C CB  . HIS   B 91  ? 0.1669 0.1674 0.2148 0.0105  0.0033  -0.0024 97  HIS   C CB  
1833 C CG  . HIS   B 91  ? 0.1848 0.1810 0.2305 0.0099  0.0041  -0.0074 97  HIS   C CG  
1834 N ND1 . HIS   B 91  ? 0.2145 0.2070 0.2488 0.0104  0.0025  -0.0104 97  HIS   C ND1 
1835 C CD2 . HIS   B 91  ? 0.1981 0.1928 0.2511 0.0088  0.0067  -0.0097 97  HIS   C CD2 
1836 C CE1 . HIS   B 91  ? 0.2239 0.2126 0.2577 0.0096  0.0041  -0.0148 97  HIS   C CE1 
1837 N NE2 . HIS   B 91  ? 0.2340 0.2237 0.2793 0.0085  0.0067  -0.0147 97  HIS   C NE2 
1838 N N   . LEU   B 92  ? 0.1381 0.1491 0.1970 0.0116  -0.0010 0.0028  98  LEU   C N   
1839 C CA  . LEU   B 92  ? 0.1413 0.1548 0.2000 0.0124  -0.0007 0.0067  98  LEU   C CA  
1840 C C   . LEU   B 92  ? 0.1419 0.1563 0.1966 0.0136  -0.0038 0.0056  98  LEU   C C   
1841 O O   . LEU   B 92  ? 0.1507 0.1657 0.2077 0.0135  -0.0062 0.0026  98  LEU   C O   
1842 C CB  . LEU   B 92  ? 0.1512 0.1681 0.2208 0.0120  0.0016  0.0092  98  LEU   C CB  
1843 C CG  . LEU   B 92  ? 0.1622 0.1812 0.2307 0.0128  0.0027  0.0135  98  LEU   C CG  
1844 C CD1 . LEU   B 92  ? 0.1852 0.2031 0.2489 0.0126  0.0039  0.0167  98  LEU   C CD1 
1845 C CD2 . LEU   B 92  ? 0.1754 0.1975 0.2541 0.0127  0.0052  0.0160  98  LEU   C CD2 
1846 N N   . MET   B 93  ? 0.1339 0.1481 0.1826 0.0145  -0.0038 0.0080  99  MET   C N   
1847 C CA  . MET   B 93  ? 0.1288 0.1434 0.1741 0.0160  -0.0061 0.0075  99  MET   C CA  
1848 C C   . MET   B 93  ? 0.1405 0.1572 0.1879 0.0166  -0.0041 0.0106  99  MET   C C   
1849 O O   . MET   B 93  ? 0.1526 0.1688 0.1980 0.0162  -0.0021 0.0132  99  MET   C O   
1850 C CB  . MET   B 93  ? 0.1435 0.1548 0.1784 0.0166  -0.0072 0.0074  99  MET   C CB  
1851 C CG  . MET   B 93  ? 0.1611 0.1697 0.1921 0.0161  -0.0085 0.0047  99  MET   C CG  
1852 S SD  . MET   B 93  ? 0.1805 0.1849 0.2002 0.0168  -0.0086 0.0055  99  MET   C SD  
1853 C CE  . MET   B 93  ? 0.1990 0.2031 0.2200 0.0158  -0.0054 0.0087  99  MET   C CE  
1854 N N   . LEU   B 94  ? 0.1299 0.1488 0.1815 0.0177  -0.0046 0.0104  100 LEU   C N   
1855 C CA  . LEU   B 94  ? 0.1377 0.1579 0.1905 0.0186  -0.0020 0.0131  100 LEU   C CA  
1856 C C   . LEU   B 94  ? 0.1346 0.1534 0.1815 0.0203  -0.0027 0.0131  100 LEU   C C   
1857 O O   . LEU   B 94  ? 0.1508 0.1691 0.1965 0.0211  -0.0054 0.0113  100 LEU   C O   
1858 C CB  . LEU   B 94  ? 0.1490 0.1729 0.2132 0.0188  -0.0007 0.0134  100 LEU   C CB  
1859 C CG  . LEU   B 94  ? 0.1654 0.1909 0.2379 0.0173  0.0007  0.0137  100 LEU   C CG  
1860 C CD1 . LEU   B 94  ? 0.1876 0.2168 0.2720 0.0176  0.0021  0.0143  100 LEU   C CD1 
1861 C CD2 . LEU   B 94  ? 0.1789 0.2035 0.2488 0.0166  0.0035  0.0169  100 LEU   C CD2 
1862 N N   . ALA   B 95  ? 0.1413 0.1591 0.1844 0.0208  -0.0001 0.0152  101 ALA   C N   
1863 C CA  . ALA   B 95  ? 0.1343 0.1505 0.1730 0.0225  0.0005  0.0153  101 ALA   C CA  
1864 C C   . ALA   B 95  ? 0.1432 0.1603 0.1837 0.0232  0.0045  0.0174  101 ALA   C C   
1865 O O   . ALA   B 95  ? 0.1369 0.1553 0.1793 0.0221  0.0064  0.0192  101 ALA   C O   
1866 C CB  . ALA   B 95  ? 0.1474 0.1594 0.1756 0.0221  -0.0004 0.0151  101 ALA   C CB  
1867 N N   . VAL   B 96  ? 0.1487 0.1649 0.1882 0.0250  0.0060  0.0173  102 VAL   C N   
1868 C CA  . VAL   B 96  ? 0.1648 0.1807 0.2035 0.0259  0.0105  0.0190  102 VAL   C CA  
1869 C C   . VAL   B 96  ? 0.1660 0.1776 0.1926 0.0252  0.0111  0.0193  102 VAL   C C   
1870 O O   . VAL   B 96  ? 0.1973 0.2054 0.2173 0.0255  0.0097  0.0177  102 VAL   C O   
1871 C CB  . VAL   B 96  ? 0.1802 0.1964 0.2234 0.0283  0.0124  0.0186  102 VAL   C CB  
1872 C CG1 . VAL   B 96  ? 0.2069 0.2220 0.2482 0.0295  0.0180  0.0203  102 VAL   C CG1 
1873 C CG2 . VAL   B 96  ? 0.1807 0.2017 0.2369 0.0287  0.0108  0.0183  102 VAL   C CG2 
1874 N N   . GLY   B 97  ? 0.1761 0.1881 0.2002 0.0240  0.0128  0.0214  103 GLY   C N   
1875 C CA  . GLY   B 97  ? 0.1989 0.2072 0.2117 0.0230  0.0125  0.0217  103 GLY   C CA  
1876 C C   . GLY   B 97  ? 0.1946 0.2044 0.2060 0.0217  0.0134  0.0246  103 GLY   C C   
1877 O O   . GLY   B 97  ? 0.2172 0.2306 0.2369 0.0215  0.0145  0.0266  103 GLY   C O   
1878 N N   . HIS   B 98  ? 0.1966 0.2034 0.1978 0.0207  0.0128  0.0250  104 HIS   C N   
1879 C CA  . HIS   B 98  ? 0.2004 0.2083 0.1986 0.0195  0.0131  0.0282  104 HIS   C CA  
1880 C C   . HIS   B 98  ? 0.1827 0.1927 0.1842 0.0175  0.0095  0.0296  104 HIS   C C   
1881 O O   . HIS   B 98  ? 0.1922 0.2007 0.1919 0.0164  0.0063  0.0278  104 HIS   C O   
1882 C CB  . HIS   B 98  ? 0.2506 0.2543 0.2358 0.0191  0.0134  0.0279  104 HIS   C CB  
1883 C CG  . HIS   B 98  ? 0.3046 0.3096 0.2861 0.0183  0.0140  0.0316  104 HIS   C CG  
1884 N ND1 . HIS   B 98  ? 0.3237 0.3310 0.3093 0.0197  0.0182  0.0346  104 HIS   C ND1 
1885 C CD2 . HIS   B 98  ? 0.3447 0.3494 0.3203 0.0163  0.0105  0.0333  104 HIS   C CD2 
1886 C CE1 . HIS   B 98  ? 0.3553 0.3634 0.3362 0.0186  0.0173  0.0382  104 HIS   C CE1 
1887 N NE2 . HIS   B 98  ? 0.3654 0.3722 0.3403 0.0165  0.0124  0.0375  104 HIS   C NE2 
1888 N N   . SER   B 99  ? 0.1879 0.2011 0.1943 0.0170  0.0104  0.0333  105 SER   C N   
1889 C CA  . SER   B 99  ? 0.1886 0.2038 0.1993 0.0154  0.0077  0.0352  105 SER   C CA  
1890 C C   . SER   B 99  ? 0.2121 0.2299 0.2248 0.0151  0.0091  0.0400  105 SER   C C   
1891 O O   . SER   B 99  ? 0.2369 0.2569 0.2572 0.0162  0.0124  0.0417  105 SER   C O   
1892 C CB  . SER   B 99  ? 0.1995 0.2165 0.2206 0.0155  0.0075  0.0334  105 SER   C CB  
1893 O OG  . SER   B 99  ? 0.2088 0.2275 0.2351 0.0142  0.0060  0.0353  105 SER   C OG  
1894 N N   . GLU   B 100 ? 0.2108 0.2283 0.2174 0.0138  0.0067  0.0425  106 GLU   C N   
1895 C CA  . GLU   B 100 ? 0.2182 0.2383 0.2263 0.0135  0.0071  0.0480  106 GLU   C CA  
1896 C C   . GLU   B 100 ? 0.1981 0.2206 0.2148 0.0123  0.0047  0.0497  106 GLU   C C   
1897 O O   . GLU   B 100 ? 0.1943 0.2159 0.2124 0.0114  0.0023  0.0467  106 GLU   C O   
1898 C CB  . GLU   B 100 ? 0.2780 0.2960 0.2727 0.0128  0.0051  0.0494  106 GLU   C CB  
1899 C CG  . GLU   B 100 ? 0.4437 0.4597 0.4317 0.0145  0.0094  0.0489  106 GLU   C CG  
1900 C CD  . GLU   B 100 ? 0.4845 0.4970 0.4571 0.0140  0.0083  0.0488  106 GLU   C CD  
1901 O OE1 . GLU   B 100 ? 0.5663 0.5787 0.5333 0.0121  0.0035  0.0500  106 GLU   C OE1 
1902 O OE2 . GLU   B 100 ? 0.4301 0.4397 0.3964 0.0156  0.0122  0.0470  106 GLU   C OE2 
1903 N N   . PRO   B 101 ? 0.1979 0.2233 0.2203 0.0122  0.0053  0.0548  107 PRO   C N   
1904 C CA  . PRO   B 101 ? 0.1948 0.2224 0.2267 0.0112  0.0036  0.0566  107 PRO   C CA  
1905 C C   . PRO   B 101 ? 0.2018 0.2285 0.2293 0.0095  -0.0011 0.0557  107 PRO   C C   
1906 O O   . PRO   B 101 ? 0.1988 0.2257 0.2328 0.0089  -0.0018 0.0541  107 PRO   C O   
1907 C CB  . PRO   B 101 ? 0.2147 0.2454 0.2513 0.0115  0.0048  0.0633  107 PRO   C CB  
1908 C CG  . PRO   B 101 ? 0.2568 0.2868 0.2884 0.0129  0.0083  0.0644  107 PRO   C CG  
1909 C CD  . PRO   B 101 ? 0.2328 0.2596 0.2550 0.0133  0.0086  0.0593  107 PRO   C CD  
1910 N N   . GLY   B 102 ? 0.1874 0.2129 0.2037 0.0086  -0.0040 0.0563  108 GLY   C N   
1911 C CA  . GLY   B 102 ? 0.1932 0.2180 0.2062 0.0067  -0.0087 0.0557  108 GLY   C CA  
1912 C C   . GLY   B 102 ? 0.1878 0.2095 0.1988 0.0064  -0.0091 0.0499  108 GLY   C C   
1913 O O   . GLY   B 102 ? 0.2018 0.2228 0.2123 0.0048  -0.0124 0.0491  108 GLY   C O   
1914 N N   . ASP   B 103 ? 0.1731 0.1927 0.1830 0.0079  -0.0059 0.0462  109 ASP   C N   
1915 C CA  . ASP   B 103 ? 0.1666 0.1833 0.1748 0.0079  -0.0062 0.0413  109 ASP   C CA  
1916 C C   . ASP   B 103 ? 0.1694 0.1870 0.1872 0.0079  -0.0055 0.0404  109 ASP   C C   
1917 O O   . ASP   B 103 ? 0.1688 0.1840 0.1854 0.0078  -0.0060 0.0371  109 ASP   C O   
1918 C CB  . ASP   B 103 ? 0.1902 0.2046 0.1942 0.0097  -0.0034 0.0381  109 ASP   C CB  
1919 C CG  . ASP   B 103 ? 0.2011 0.2130 0.1938 0.0096  -0.0036 0.0377  109 ASP   C CG  
1920 O OD1 . ASP   B 103 ? 0.2132 0.2234 0.1995 0.0081  -0.0068 0.0374  109 ASP   C OD1 
1921 O OD2 . ASP   B 103 ? 0.2117 0.2233 0.2023 0.0112  -0.0003 0.0377  109 ASP   C OD2 
1922 N N   . CYS   B 104 ? 0.1547 0.1753 0.1821 0.0082  -0.0039 0.0432  110 CYS   C N   
1923 C CA  . CYS   B 104 ? 0.1502 0.1711 0.1862 0.0082  -0.0027 0.0421  110 CYS   C CA  
1924 C C   . CYS   B 104 ? 0.1541 0.1739 0.1896 0.0069  -0.0050 0.0419  110 CYS   C C   
1925 O O   . CYS   B 104 ? 0.1762 0.1971 0.2102 0.0056  -0.0078 0.0448  110 CYS   C O   
1926 C CB  . CYS   B 104 ? 0.1589 0.1828 0.2053 0.0084  -0.0007 0.0456  110 CYS   C CB  
1927 S SG  . CYS   B 104 ? 0.1751 0.2000 0.2260 0.0099  0.0029  0.0452  110 CYS   C SG  
1928 N N   . GLY   B 105 ? 0.1307 0.1482 0.1668 0.0072  -0.0041 0.0385  111 GLY   C N   
1929 C CA  . GLY   B 105 ? 0.1474 0.1636 0.1838 0.0061  -0.0054 0.0383  111 GLY   C CA  
1930 C C   . GLY   B 105 ? 0.1517 0.1645 0.1793 0.0059  -0.0070 0.0352  111 GLY   C C   
1931 O O   . GLY   B 105 ? 0.1675 0.1784 0.1953 0.0052  -0.0074 0.0345  111 GLY   C O   
1932 N N   . GLY   B 106 ? 0.1556 0.1672 0.1762 0.0065  -0.0074 0.0336  112 GLY   C N   
1933 C CA  . GLY   B 106 ? 0.1620 0.1699 0.1748 0.0066  -0.0084 0.0306  112 GLY   C CA  
1934 C C   . GLY   B 106 ? 0.1476 0.1533 0.1610 0.0078  -0.0068 0.0278  112 GLY   C C   
1935 O O   . GLY   B 106 ? 0.1553 0.1620 0.1720 0.0091  -0.0050 0.0268  112 GLY   C O   
1936 N N   . ILE   B 107 ? 0.1516 0.1542 0.1616 0.0074  -0.0076 0.0265  113 ILE   C N   
1937 C CA  . ILE   B 107 ? 0.1506 0.1510 0.1602 0.0086  -0.0062 0.0244  113 ILE   C CA  
1938 C C   . ILE   B 107 ? 0.1441 0.1427 0.1488 0.0104  -0.0060 0.0218  113 ILE   C C   
1939 O O   . ILE   B 107 ? 0.1518 0.1488 0.1516 0.0105  -0.0069 0.0211  113 ILE   C O   
1940 C CB  . ILE   B 107 ? 0.1884 0.1861 0.1973 0.0075  -0.0067 0.0248  113 ILE   C CB  
1941 C CG1 . ILE   B 107 ? 0.2251 0.2248 0.2416 0.0065  -0.0055 0.0273  113 ILE   C CG1 
1942 C CG2 . ILE   B 107 ? 0.1965 0.1905 0.2012 0.0089  -0.0056 0.0227  113 ILE   C CG2 
1943 C CD1 . ILE   B 107 ? 0.2748 0.2728 0.2934 0.0052  -0.0055 0.0286  113 ILE   C CD1 
1944 N N   . LEU   B 108 ? 0.1415 0.1401 0.1475 0.0118  -0.0050 0.0203  114 LEU   C N   
1945 C CA  . LEU   B 108 ? 0.1343 0.1313 0.1367 0.0136  -0.0052 0.0181  114 LEU   C CA  
1946 C C   . LEU   B 108 ? 0.1447 0.1384 0.1441 0.0140  -0.0051 0.0176  114 LEU   C C   
1947 O O   . LEU   B 108 ? 0.1411 0.1348 0.1423 0.0137  -0.0041 0.0178  114 LEU   C O   
1948 C CB  . LEU   B 108 ? 0.1322 0.1318 0.1386 0.0147  -0.0047 0.0170  114 LEU   C CB  
1949 C CG  . LEU   B 108 ? 0.1382 0.1369 0.1426 0.0166  -0.0056 0.0150  114 LEU   C CG  
1950 C CD1 . LEU   B 108 ? 0.1606 0.1587 0.1627 0.0176  -0.0058 0.0148  114 LEU   C CD1 
1951 C CD2 . LEU   B 108 ? 0.1510 0.1525 0.1605 0.0170  -0.0057 0.0137  114 LEU   C CD2 
1952 N N   . ARG   B 109 ? 0.1493 0.1400 0.1440 0.0148  -0.0057 0.0170  115 ARG   C N   
1953 C CA  . ARG   B 109 ? 0.1571 0.1443 0.1485 0.0153  -0.0054 0.0171  115 ARG   C CA  
1954 C C   . ARG   B 109 ? 0.1650 0.1503 0.1528 0.0175  -0.0061 0.0161  115 ARG   C C   
1955 O O   . ARG   B 109 ? 0.1653 0.1510 0.1528 0.0184  -0.0067 0.0154  115 ARG   C O   
1956 C CB  . ARG   B 109 ? 0.1987 0.1834 0.1895 0.0137  -0.0053 0.0185  115 ARG   C CB  
1957 C CG  . ARG   B 109 ? 0.2552 0.2381 0.2432 0.0136  -0.0062 0.0178  115 ARG   C CG  
1958 C CD  . ARG   B 109 ? 0.3190 0.2992 0.3067 0.0115  -0.0066 0.0186  115 ARG   C CD  
1959 N NE  . ARG   B 109 ? 0.3890 0.3720 0.3801 0.0092  -0.0076 0.0197  115 ARG   C NE  
1960 C CZ  . ARG   B 109 ? 0.5027 0.4866 0.4982 0.0076  -0.0075 0.0216  115 ARG   C CZ  
1961 N NH1 . ARG   B 109 ? 0.5390 0.5208 0.5353 0.0080  -0.0057 0.0224  115 ARG   C NH1 
1962 N NH2 . ARG   B 109 ? 0.5166 0.5035 0.5158 0.0056  -0.0089 0.0230  115 ARG   C NH2 
1963 N N   . CYS   B 110 ? 0.1741 0.1574 0.1591 0.0185  -0.0059 0.0162  116 CYS   C N   
1964 C CA  . CYS   B 110 ? 0.1793 0.1606 0.1606 0.0208  -0.0069 0.0160  116 CYS   C CA  
1965 C C   . CYS   B 110 ? 0.2008 0.1776 0.1782 0.0210  -0.0058 0.0176  116 CYS   C C   
1966 O O   . CYS   B 110 ? 0.2033 0.1788 0.1817 0.0192  -0.0042 0.0187  116 CYS   C O   
1967 C CB  . CYS   B 110 ? 0.1637 0.1469 0.1444 0.0221  -0.0082 0.0149  116 CYS   C CB  
1968 S SG  . CYS   B 110 ? 0.1734 0.1548 0.1507 0.0216  -0.0068 0.0149  116 CYS   C SG  
1969 N N   . GLN   B 111 ? 0.2158 0.1903 0.1894 0.0232  -0.0065 0.0182  117 GLN   C N   
1970 C CA  . GLN   B 111 ? 0.2335 0.2034 0.2035 0.0235  -0.0049 0.0203  117 GLN   C CA  
1971 C C   . GLN   B 111 ? 0.2389 0.2076 0.2069 0.0228  -0.0029 0.0212  117 GLN   C C   
1972 O O   . GLN   B 111 ? 0.2528 0.2181 0.2198 0.0224  -0.0007 0.0232  117 GLN   C O   
1973 C CB  . GLN   B 111 ? 0.2444 0.2121 0.2106 0.0264  -0.0061 0.0215  117 GLN   C CB  
1974 C CG  . GLN   B 111 ? 0.2936 0.2631 0.2564 0.0279  -0.0080 0.0210  117 GLN   C CG  
1975 C CD  . GLN   B 111 ? 0.4279 0.3960 0.3874 0.0307  -0.0100 0.0226  117 GLN   C CD  
1976 O OE1 . GLN   B 111 ? 0.4921 0.4631 0.4541 0.0320  -0.0127 0.0218  117 GLN   C OE1 
1977 N NE2 . GLN   B 111 ? 0.4159 0.3800 0.3700 0.0316  -0.0086 0.0251  117 GLN   C NE2 
1978 N N   . HIS   B 112 ? 0.2097 0.1812 0.1779 0.0225  -0.0032 0.0197  118 HIS   C N   
1979 C CA  . HIS   B 112 ? 0.2070 0.1769 0.1730 0.0220  -0.0006 0.0202  118 HIS   C CA  
1980 C C   . HIS   B 112 ? 0.2051 0.1765 0.1772 0.0197  0.0016  0.0205  118 HIS   C C   
1981 O O   . HIS   B 112 ? 0.2263 0.1961 0.1980 0.0193  0.0046  0.0213  118 HIS   C O   
1982 C CB  . HIS   B 112 ? 0.2213 0.1924 0.1835 0.0231  -0.0018 0.0182  118 HIS   C CB  
1983 C CG  . HIS   B 112 ? 0.2025 0.1728 0.1592 0.0254  -0.0048 0.0182  118 HIS   C CG  
1984 N ND1 . HIS   B 112 ? 0.1822 0.1560 0.1414 0.0261  -0.0084 0.0165  118 HIS   C ND1 
1985 C CD2 . HIS   B 112 ? 0.2471 0.2137 0.1965 0.0272  -0.0046 0.0201  118 HIS   C CD2 
1986 C CE1 . HIS   B 112 ? 0.2073 0.1798 0.1614 0.0282  -0.0107 0.0175  118 HIS   C CE1 
1987 N NE2 . HIS   B 112 ? 0.2467 0.2147 0.1941 0.0290  -0.0085 0.0197  118 HIS   C NE2 
1988 N N   . GLY   B 113 ? 0.1933 0.1678 0.1711 0.0182  0.0002  0.0200  119 GLY   C N   
1989 C CA  . GLY   B 113 ? 0.1882 0.1647 0.1723 0.0161  0.0016  0.0207  119 GLY   C CA  
1990 C C   . GLY   B 113 ? 0.1724 0.1533 0.1609 0.0153  -0.0001 0.0194  119 GLY   C C   
1991 O O   . GLY   B 113 ? 0.1726 0.1549 0.1602 0.0161  -0.0022 0.0181  119 GLY   C O   
1992 N N   . VAL   B 114 ? 0.1688 0.1518 0.1628 0.0139  0.0013  0.0201  120 VAL   C N   
1993 C CA  . VAL   B 114 ? 0.1673 0.1544 0.1663 0.0131  0.0003  0.0197  120 VAL   C CA  
1994 C C   . VAL   B 114 ? 0.1560 0.1442 0.1545 0.0143  0.0004  0.0174  120 VAL   C C   
1995 O O   . VAL   B 114 ? 0.1715 0.1581 0.1689 0.0146  0.0023  0.0166  120 VAL   C O   
1996 C CB  . VAL   B 114 ? 0.1780 0.1669 0.1841 0.0113  0.0018  0.0219  120 VAL   C CB  
1997 C CG1 . VAL   B 114 ? 0.1907 0.1837 0.2021 0.0108  0.0011  0.0219  120 VAL   C CG1 
1998 C CG2 . VAL   B 114 ? 0.2082 0.1966 0.2158 0.0098  0.0007  0.0240  120 VAL   C CG2 
1999 N N   . VAL   B 115 ? 0.1479 0.1385 0.1471 0.0148  -0.0016 0.0162  121 VAL   C N   
2000 C CA  . VAL   B 115 ? 0.1492 0.1413 0.1494 0.0155  -0.0023 0.0139  121 VAL   C CA  
2001 C C   . VAL   B 115 ? 0.1606 0.1556 0.1681 0.0144  -0.0011 0.0140  121 VAL   C C   
2002 O O   . VAL   B 115 ? 0.1620 0.1571 0.1712 0.0145  -0.0003 0.0121  121 VAL   C O   
2003 C CB  . VAL   B 115 ? 0.1504 0.1438 0.1494 0.0167  -0.0047 0.0129  121 VAL   C CB  
2004 C CG1 . VAL   B 115 ? 0.1695 0.1652 0.1715 0.0172  -0.0058 0.0107  121 VAL   C CG1 
2005 C CG2 . VAL   B 115 ? 0.1808 0.1711 0.1732 0.0181  -0.0058 0.0130  121 VAL   C CG2 
2006 N N   . GLY   B 116 ? 0.1497 0.1470 0.1613 0.0134  -0.0011 0.0162  122 GLY   C N   
2007 C CA  . GLY   B 116 ? 0.1648 0.1652 0.1839 0.0125  0.0001  0.0173  122 GLY   C CA  
2008 C C   . GLY   B 116 ? 0.1525 0.1551 0.1737 0.0116  -0.0007 0.0201  122 GLY   C C   
2009 O O   . GLY   B 116 ? 0.1541 0.1554 0.1709 0.0113  -0.0019 0.0209  122 GLY   C O   
2010 N N   . ILE   B 117 ? 0.1417 0.1474 0.1694 0.0111  0.0001  0.0217  123 ILE   C N   
2011 C CA  . ILE   B 117 ? 0.1352 0.1430 0.1640 0.0103  -0.0008 0.0248  123 ILE   C CA  
2012 C C   . ILE   B 117 ? 0.1309 0.1414 0.1626 0.0108  -0.0005 0.0252  123 ILE   C C   
2013 O O   . ILE   B 117 ? 0.1448 0.1563 0.1814 0.0113  0.0009  0.0240  123 ILE   C O   
2014 C CB  . ILE   B 117 ? 0.1490 0.1583 0.1839 0.0090  -0.0001 0.0281  123 ILE   C CB  
2015 C CG1 . ILE   B 117 ? 0.1712 0.1815 0.2140 0.0092  0.0026  0.0280  123 ILE   C CG1 
2016 C CG2 . ILE   B 117 ? 0.1679 0.1751 0.2006 0.0082  -0.0006 0.0286  123 ILE   C CG2 
2017 C CD1 . ILE   B 117 ? 0.1694 0.1818 0.2204 0.0082  0.0035  0.0322  123 ILE   C CD1 
2018 N N   . VAL   B 118 ? 0.1330 0.1445 0.1617 0.0106  -0.0015 0.0271  124 VAL   C N   
2019 C CA  . VAL   B 118 ? 0.1273 0.1411 0.1584 0.0112  -0.0004 0.0282  124 VAL   C CA  
2020 C C   . VAL   B 118 ? 0.1407 0.1572 0.1808 0.0107  0.0012  0.0308  124 VAL   C C   
2021 O O   . VAL   B 118 ? 0.1342 0.1515 0.1771 0.0098  0.0009  0.0335  124 VAL   C O   
2022 C CB  . VAL   B 118 ? 0.1373 0.1512 0.1624 0.0109  -0.0014 0.0301  124 VAL   C CB  
2023 C CG1 . VAL   B 118 ? 0.1498 0.1660 0.1770 0.0116  0.0004  0.0321  124 VAL   C CG1 
2024 C CG2 . VAL   B 118 ? 0.1532 0.1640 0.1700 0.0114  -0.0024 0.0274  124 VAL   C CG2 
2025 N N   . SER   B 119 ? 0.1301 0.1480 0.1757 0.0115  0.0030  0.0300  125 SER   C N   
2026 C CA  . SER   B 119 ? 0.1355 0.1555 0.1906 0.0112  0.0050  0.0323  125 SER   C CA  
2027 C C   . SER   B 119 ? 0.1418 0.1641 0.2009 0.0118  0.0068  0.0342  125 SER   C C   
2028 O O   . SER   B 119 ? 0.1450 0.1692 0.2109 0.0116  0.0084  0.0377  125 SER   C O   
2029 C CB  . SER   B 119 ? 0.1422 0.1608 0.2021 0.0111  0.0060  0.0288  125 SER   C CB  
2030 O OG  . SER   B 119 ? 0.1558 0.1759 0.2258 0.0108  0.0083  0.0304  125 SER   C OG  
2031 N N   . THR   B 120 ? 0.1358 0.1580 0.1920 0.0127  0.0069  0.0322  126 THR   C N   
2032 C CA  . THR   B 120 ? 0.1372 0.1615 0.1983 0.0135  0.0093  0.0341  126 THR   C CA  
2033 C C   . THR   B 120 ? 0.1436 0.1673 0.1968 0.0144  0.0095  0.0344  126 THR   C C   
2034 O O   . THR   B 120 ? 0.1451 0.1666 0.1901 0.0146  0.0075  0.0320  126 THR   C O   
2035 C CB  . THR   B 120 ? 0.1359 0.1609 0.2060 0.0137  0.0103  0.0311  126 THR   C CB  
2036 O OG1 . THR   B 120 ? 0.1503 0.1743 0.2165 0.0144  0.0086  0.0271  126 THR   C OG1 
2037 C CG2 . THR   B 120 ? 0.1585 0.1829 0.2349 0.0127  0.0103  0.0295  126 THR   C CG2 
2038 N N   . GLY   B 121 ? 0.1495 0.1749 0.2054 0.0152  0.0122  0.0372  127 GLY   C N   
2039 C CA  . GLY   B 121 ? 0.1698 0.1945 0.2188 0.0163  0.0136  0.0376  127 GLY   C CA  
2040 C C   . GLY   B 121 ? 0.2044 0.2312 0.2605 0.0173  0.0176  0.0401  127 GLY   C C   
2041 O O   . GLY   B 121 ? 0.2285 0.2571 0.2911 0.0170  0.0193  0.0436  127 GLY   C O   
2042 N N   . GLY   B 122 ? 0.2433 0.2697 0.2982 0.0187  0.0196  0.0389  128 GLY   C N   
2043 C CA  . GLY   B 122 ? 0.2677 0.2962 0.3304 0.0198  0.0241  0.0414  128 GLY   C CA  
2044 C C   . GLY   B 122 ? 0.2600 0.2886 0.3257 0.0212  0.0256  0.0388  128 GLY   C C   
2045 O O   . GLY   B 122 ? 0.2647 0.2931 0.3322 0.0210  0.0226  0.0348  128 GLY   C O   
2046 N N   . ASN   B 123 ? 0.2522 0.2814 0.3196 0.0226  0.0304  0.0415  129 ASN   C N   
2047 C CA  . ASN   B 123 ? 0.2576 0.2876 0.3306 0.0242  0.0329  0.0399  129 ASN   C CA  
2048 C C   . ASN   B 123 ? 0.2383 0.2657 0.3030 0.0249  0.0304  0.0360  129 ASN   C C   
2049 O O   . ASN   B 123 ? 0.2706 0.2993 0.3425 0.0257  0.0296  0.0335  129 ASN   C O   
2050 C CB  . ASN   B 123 ? 0.3094 0.3431 0.3991 0.0236  0.0321  0.0385  129 ASN   C CB  
2051 C CG  . ASN   B 123 ? 0.4117 0.4480 0.5131 0.0240  0.0372  0.0423  129 ASN   C CG  
2052 O OD1 . ASN   B 123 ? 0.4380 0.4736 0.5355 0.0252  0.0422  0.0463  129 ASN   C OD1 
2053 N ND2 . ASN   B 123 ? 0.4450 0.4842 0.5611 0.0229  0.0362  0.0411  129 ASN   C ND2 
2054 N N   . GLY   B 124 ? 0.2162 0.2400 0.2668 0.0246  0.0288  0.0356  130 GLY   C N   
2055 C CA  . GLY   B 124 ? 0.2172 0.2380 0.2604 0.0253  0.0268  0.0320  130 GLY   C CA  
2056 C C   . GLY   B 124 ? 0.1972 0.2182 0.2422 0.0243  0.0214  0.0287  130 GLY   C C   
2057 O O   . GLY   B 124 ? 0.1992 0.2181 0.2405 0.0251  0.0198  0.0260  130 GLY   C O   
2058 N N   . LEU   B 125 ? 0.1665 0.1894 0.2167 0.0227  0.0190  0.0291  131 LEU   C N   
2059 C CA  . LEU   B 125 ? 0.1612 0.1839 0.2124 0.0217  0.0145  0.0261  131 LEU   C CA  
2060 C C   . LEU   B 125 ? 0.1666 0.1877 0.2111 0.0200  0.0123  0.0268  131 LEU   C C   
2061 O O   . LEU   B 125 ? 0.1871 0.2089 0.2309 0.0193  0.0137  0.0300  131 LEU   C O   
2062 C CB  . LEU   B 125 ? 0.1829 0.2089 0.2467 0.0211  0.0135  0.0251  131 LEU   C CB  
2063 C CG  . LEU   B 125 ? 0.2253 0.2538 0.2985 0.0225  0.0149  0.0244  131 LEU   C CG  
2064 C CD1 . LEU   B 125 ? 0.2857 0.3175 0.3722 0.0214  0.0142  0.0238  131 LEU   C CD1 
2065 C CD2 . LEU   B 125 ? 0.2554 0.2829 0.3260 0.0236  0.0121  0.0216  131 LEU   C CD2 
2066 N N   . VAL   B 126 ? 0.1384 0.1577 0.1788 0.0194  0.0089  0.0243  132 VAL   C N   
2067 C CA  . VAL   B 126 ? 0.1412 0.1593 0.1776 0.0178  0.0068  0.0248  132 VAL   C CA  
2068 C C   . VAL   B 126 ? 0.1301 0.1487 0.1716 0.0172  0.0047  0.0224  132 VAL   C C   
2069 O O   . VAL   B 126 ? 0.1333 0.1514 0.1753 0.0180  0.0031  0.0197  132 VAL   C O   
2070 C CB  . VAL   B 126 ? 0.1507 0.1653 0.1763 0.0176  0.0052  0.0242  132 VAL   C CB  
2071 C CG1 . VAL   B 126 ? 0.1769 0.1893 0.1994 0.0188  0.0041  0.0212  132 VAL   C CG1 
2072 C CG2 . VAL   B 126 ? 0.1605 0.1743 0.1839 0.0159  0.0030  0.0249  132 VAL   C CG2 
2073 N N   . GLY   B 127 ? 0.1234 0.1427 0.1686 0.0159  0.0047  0.0236  133 GLY   C N   
2074 C CA  . GLY   B 127 ? 0.1206 0.1396 0.1696 0.0153  0.0033  0.0210  133 GLY   C CA  
2075 C C   . GLY   B 127 ? 0.1297 0.1464 0.1736 0.0143  0.0021  0.0211  133 GLY   C C   
2076 O O   . GLY   B 127 ? 0.1357 0.1527 0.1786 0.0136  0.0027  0.0241  133 GLY   C O   
2077 N N   . PHE   B 128 ? 0.1155 0.1303 0.1569 0.0144  0.0005  0.0182  134 PHE   C N   
2078 C CA  . PHE   B 128 ? 0.1303 0.1426 0.1673 0.0137  0.0000  0.0182  134 PHE   C CA  
2079 C C   . PHE   B 128 ? 0.1325 0.1440 0.1734 0.0131  0.0005  0.0162  134 PHE   C C   
2080 O O   . PHE   B 128 ? 0.1305 0.1417 0.1725 0.0135  -0.0004 0.0131  134 PHE   C O   
2081 C CB  . PHE   B 128 ? 0.1296 0.1390 0.1583 0.0144  -0.0019 0.0165  134 PHE   C CB  
2082 C CG  . PHE   B 128 ? 0.1340 0.1434 0.1586 0.0152  -0.0022 0.0174  134 PHE   C CG  
2083 C CD1 . PHE   B 128 ? 0.1365 0.1449 0.1568 0.0144  -0.0022 0.0195  134 PHE   C CD1 
2084 C CD2 . PHE   B 128 ? 0.1484 0.1584 0.1733 0.0166  -0.0027 0.0160  134 PHE   C CD2 
2085 C CE1 . PHE   B 128 ? 0.1547 0.1620 0.1702 0.0151  -0.0023 0.0196  134 PHE   C CE1 
2086 C CE2 . PHE   B 128 ? 0.1498 0.1591 0.1710 0.0175  -0.0022 0.0166  134 PHE   C CE2 
2087 C CZ  . PHE   B 128 ? 0.1571 0.1647 0.1729 0.0167  -0.0019 0.0182  134 PHE   C CZ  
2088 N N   . ALA   B 129 ? 0.1342 0.1451 0.1771 0.0122  0.0020  0.0179  135 ALA   C N   
2089 C CA  . ALA   B 129 ? 0.1301 0.1392 0.1757 0.0118  0.0034  0.0158  135 ALA   C CA  
2090 C C   . ALA   B 129 ? 0.1430 0.1486 0.1802 0.0122  0.0025  0.0137  135 ALA   C C   
2091 O O   . ALA   B 129 ? 0.1472 0.1517 0.1805 0.0121  0.0025  0.0156  135 ALA   C O   
2092 C CB  . ALA   B 129 ? 0.1421 0.1520 0.1938 0.0110  0.0057  0.0190  135 ALA   C CB  
2093 N N   . ASP   B 130 ? 0.1422 0.1460 0.1767 0.0127  0.0016  0.0100  136 ASP   C N   
2094 C CA  . ASP   B 130 ? 0.1439 0.1441 0.1696 0.0133  0.0009  0.0082  136 ASP   C CA  
2095 C C   . ASP   B 130 ? 0.1510 0.1485 0.1765 0.0128  0.0040  0.0086  136 ASP   C C   
2096 O O   . ASP   B 130 ? 0.1576 0.1552 0.1895 0.0121  0.0064  0.0082  136 ASP   C O   
2097 C CB  . ASP   B 130 ? 0.1624 0.1616 0.1854 0.0138  -0.0012 0.0040  136 ASP   C CB  
2098 C CG  . ASP   B 130 ? 0.2047 0.2002 0.2175 0.0147  -0.0024 0.0025  136 ASP   C CG  
2099 O OD1 . ASP   B 130 ? 0.2027 0.1977 0.2108 0.0155  -0.0032 0.0046  136 ASP   C OD1 
2100 O OD2 . ASP   B 130 ? 0.2311 0.2239 0.2404 0.0146  -0.0021 -0.0005 136 ASP   C OD2 
2101 N N   . VAL   B 131 ? 0.1498 0.1446 0.1688 0.0132  0.0044  0.0095  137 VAL   C N   
2102 C CA  . VAL   B 131 ? 0.1571 0.1488 0.1752 0.0130  0.0079  0.0098  137 VAL   C CA  
2103 C C   . VAL   B 131 ? 0.1632 0.1505 0.1711 0.0141  0.0080  0.0075  137 VAL   C C   
2104 O O   . VAL   B 131 ? 0.1731 0.1571 0.1790 0.0142  0.0116  0.0076  137 VAL   C O   
2105 C CB  . VAL   B 131 ? 0.1711 0.1636 0.1929 0.0124  0.0094  0.0139  137 VAL   C CB  
2106 C CG1 . VAL   B 131 ? 0.1630 0.1598 0.1944 0.0114  0.0094  0.0165  137 VAL   C CG1 
2107 C CG2 . VAL   B 131 ? 0.1674 0.1596 0.1836 0.0127  0.0071  0.0154  137 VAL   C CG2 
2108 N N   . ARG   B 132 ? 0.1624 0.1495 0.1640 0.0150  0.0045  0.0058  138 ARG   C N   
2109 C CA  . ARG   B 132 ? 0.1716 0.1546 0.1627 0.0161  0.0041  0.0046  138 ARG   C CA  
2110 C C   . ARG   B 132 ? 0.1871 0.1666 0.1736 0.0162  0.0059  0.0011  138 ARG   C C   
2111 O O   . ARG   B 132 ? 0.2031 0.1783 0.1800 0.0172  0.0070  0.0006  138 ARG   C O   
2112 C CB  . ARG   B 132 ? 0.1736 0.1578 0.1603 0.0172  -0.0004 0.0041  138 ARG   C CB  
2113 C CG  . ARG   B 132 ? 0.1710 0.1573 0.1602 0.0173  -0.0015 0.0073  138 ARG   C CG  
2114 C CD  . ARG   B 132 ? 0.1813 0.1686 0.1675 0.0186  -0.0054 0.0067  138 ARG   C CD  
2115 N NE  . ARG   B 132 ? 0.1656 0.1566 0.1577 0.0183  -0.0075 0.0047  138 ARG   C NE  
2116 C CZ  . ARG   B 132 ? 0.1723 0.1655 0.1654 0.0193  -0.0108 0.0043  138 ARG   C CZ  
2117 N NH1 . ARG   B 132 ? 0.1781 0.1699 0.1658 0.0208  -0.0125 0.0054  138 ARG   C NH1 
2118 N NH2 . ARG   B 132 ? 0.1726 0.1694 0.1729 0.0188  -0.0121 0.0029  138 ARG   C NH2 
2119 N N   . ASP   B 133 ? 0.1830 0.1636 0.1752 0.0153  0.0062  -0.0016 139 ASP   C N   
2120 C CA  . ASP   B 133 ? 0.1980 0.1745 0.1857 0.0152  0.0080  -0.0058 139 ASP   C CA  
2121 C C   . ASP   B 133 ? 0.2093 0.1827 0.1993 0.0149  0.0142  -0.0049 139 ASP   C C   
2122 O O   . ASP   B 133 ? 0.2294 0.1983 0.2141 0.0150  0.0168  -0.0084 139 ASP   C O   
2123 C CB  . ASP   B 133 ? 0.2101 0.1886 0.2038 0.0141  0.0057  -0.0095 139 ASP   C CB  
2124 C CG  . ASP   B 133 ? 0.2273 0.2091 0.2344 0.0130  0.0081  -0.0077 139 ASP   C CG  
2125 O OD1 . ASP   B 133 ? 0.2046 0.1897 0.2167 0.0131  0.0083  -0.0033 139 ASP   C OD1 
2126 O OD2 . ASP   B 133 ? 0.2479 0.2287 0.2602 0.0120  0.0099  -0.0106 139 ASP   C OD2 
2127 N N   . LEU   B 134 ? 0.1956 0.1715 0.1938 0.0146  0.0166  -0.0005 140 LEU   C N   
2128 C CA  . LEU   B 134 ? 0.1936 0.1674 0.1971 0.0143  0.0226  0.0009  140 LEU   C CA  
2129 C C   . LEU   B 134 ? 0.1986 0.1685 0.1944 0.0153  0.0256  0.0026  140 LEU   C C   
2130 O O   . LEU   B 134 ? 0.1973 0.1687 0.1970 0.0152  0.0266  0.0069  140 LEU   C O   
2131 C CB  . LEU   B 134 ? 0.1826 0.1613 0.1988 0.0134  0.0229  0.0053  140 LEU   C CB  
2132 C CG  . LEU   B 134 ? 0.1884 0.1712 0.2126 0.0126  0.0203  0.0044  140 LEU   C CG  
2133 C CD1 . LEU   B 134 ? 0.2006 0.1882 0.2357 0.0119  0.0203  0.0094  140 LEU   C CD1 
2134 C CD2 . LEU   B 134 ? 0.2246 0.2047 0.2520 0.0122  0.0232  0.0003  140 LEU   C CD2 
2135 N N   . LEU   B 135 ? 0.2212 0.1857 0.2055 0.0162  0.0270  -0.0009 141 LEU   C N   
2136 C CA  . LEU   B 135 ? 0.2303 0.1908 0.2054 0.0175  0.0296  0.0011  141 LEU   C CA  
2137 C C   . LEU   B 135 ? 0.2267 0.1854 0.2078 0.0175  0.0364  0.0041  141 LEU   C C   
2138 O O   . LEU   B 135 ? 0.2454 0.2028 0.2241 0.0181  0.0384  0.0076  141 LEU   C O   
2139 C CB  . LEU   B 135 ? 0.2375 0.1925 0.1974 0.0185  0.0293  -0.0030 141 LEU   C CB  
2140 C CG  . LEU   B 135 ? 0.2389 0.1958 0.1938 0.0184  0.0222  -0.0064 141 LEU   C CG  
2141 C CD1 . LEU   B 135 ? 0.2595 0.2109 0.1986 0.0193  0.0213  -0.0105 141 LEU   C CD1 
2142 C CD2 . LEU   B 135 ? 0.2421 0.2034 0.1982 0.0187  0.0169  -0.0032 141 LEU   C CD2 
2143 N N   . TRP   B 136 ? 0.2261 0.1851 0.2164 0.0169  0.0401  0.0032  142 TRP   C N   
2144 C CA  . TRP   B 136 ? 0.2386 0.1963 0.2370 0.0170  0.0470  0.0062  142 TRP   C CA  
2145 C C   . TRP   B 136 ? 0.2401 0.2031 0.2495 0.0162  0.0457  0.0121  142 TRP   C C   
2146 O O   . TRP   B 136 ? 0.2625 0.2248 0.2781 0.0164  0.0506  0.0155  142 TRP   C O   
2147 C CB  . TRP   B 136 ? 0.2402 0.1973 0.2470 0.0166  0.0508  0.0039  142 TRP   C CB  
2148 C CG  . TRP   B 136 ? 0.2267 0.1891 0.2430 0.0154  0.0463  0.0037  142 TRP   C CG  
2149 C CD1 . TRP   B 136 ? 0.2509 0.2133 0.2645 0.0149  0.0428  -0.0009 142 TRP   C CD1 
2150 C CD2 . TRP   B 136 ? 0.2228 0.1912 0.2539 0.0145  0.0453  0.0084  142 TRP   C CD2 
2151 N NE1 . TRP   B 136 ? 0.2435 0.2115 0.2690 0.0138  0.0401  0.0009  142 TRP   C NE1 
2152 C CE2 . TRP   B 136 ? 0.2340 0.2057 0.2695 0.0137  0.0414  0.0067  142 TRP   C CE2 
2153 C CE3 . TRP   B 136 ? 0.2277 0.1992 0.2683 0.0142  0.0469  0.0140  142 TRP   C CE3 
2154 C CZ2 . TRP   B 136 ? 0.2202 0.1977 0.2683 0.0128  0.0396  0.0107  142 TRP   C CZ2 
2155 C CZ3 . TRP   B 136 ? 0.2263 0.2036 0.2795 0.0132  0.0445  0.0177  142 TRP   C CZ3 
2156 C CH2 . TRP   B 136 ? 0.2195 0.1996 0.2755 0.0127  0.0409  0.0161  142 TRP   C CH2 
2157 N N   . LEU   B 137 ? 0.2278 0.1957 0.2393 0.0154  0.0392  0.0133  143 LEU   C N   
2158 C CA  . LEU   B 137 ? 0.2204 0.1925 0.2401 0.0144  0.0375  0.0183  143 LEU   C CA  
2159 C C   . LEU   B 137 ? 0.2559 0.2251 0.2703 0.0150  0.0393  0.0207  143 LEU   C C   
2160 O O   . LEU   B 137 ? 0.2785 0.2500 0.3008 0.0141  0.0396  0.0247  143 LEU   C O   
2161 C CB  . LEU   B 137 ? 0.2158 0.1926 0.2363 0.0136  0.0306  0.0186  143 LEU   C CB  
2162 C CG  . LEU   B 137 ? 0.2024 0.1832 0.2312 0.0128  0.0289  0.0180  143 LEU   C CG  
2163 C CD1 . LEU   B 137 ? 0.2103 0.1946 0.2366 0.0124  0.0227  0.0176  143 LEU   C CD1 
2164 C CD2 . LEU   B 137 ? 0.2129 0.1971 0.2553 0.0119  0.0308  0.0222  143 LEU   C CD2 
2165 N N   . ASP   B 138 ? 0.2445 0.2088 0.2455 0.0164  0.0401  0.0183  144 ASP   C N   
2166 C CA  . ASP   B 138 ? 0.2699 0.2310 0.2649 0.0172  0.0420  0.0207  144 ASP   C CA  
2167 C C   . ASP   B 138 ? 0.3097 0.2666 0.3063 0.0179  0.0500  0.0225  144 ASP   C C   
2168 O O   . ASP   B 138 ? 0.3332 0.2872 0.3256 0.0186  0.0525  0.0250  144 ASP   C O   
2169 C CB  . ASP   B 138 ? 0.2631 0.2207 0.2428 0.0186  0.0393  0.0182  144 ASP   C CB  
2170 C CG  . ASP   B 138 ? 0.2761 0.2374 0.2540 0.0182  0.0318  0.0172  144 ASP   C CG  
2171 O OD1 . ASP   B 138 ? 0.2839 0.2499 0.2711 0.0169  0.0289  0.0188  144 ASP   C OD1 
2172 O OD2 . ASP   B 138 ? 0.3072 0.2665 0.2743 0.0194  0.0290  0.0150  144 ASP   C OD2 
2173 N N   . GLU   B 139 ? 0.3162 0.2727 0.3193 0.0179  0.0545  0.0214  145 GLU   C N   
2174 C CA  . GLU   B 139 ? 0.3672 0.3193 0.3718 0.0189  0.0632  0.0228  145 GLU   C CA  
2175 C C   . GLU   B 139 ? 0.4182 0.3731 0.4393 0.0181  0.0671  0.0248  145 GLU   C C   
2176 O O   . GLU   B 139 ? 0.4244 0.3841 0.4540 0.0170  0.0632  0.0245  145 GLU   C O   
2177 C CB  . GLU   B 139 ? 0.4273 0.3726 0.4166 0.0205  0.0664  0.0179  145 GLU   C CB  
2178 C CG  . GLU   B 139 ? 0.5202 0.4660 0.5108 0.0201  0.0653  0.0132  145 GLU   C CG  
2179 C CD  . GLU   B 139 ? 0.6418 0.5822 0.6161 0.0210  0.0645  0.0073  145 GLU   C CD  
2180 O OE1 . GLU   B 139 ? 0.6585 0.5985 0.6344 0.0205  0.0644  0.0030  145 GLU   C OE1 
2181 O OE2 . GLU   B 139 ? 0.6697 0.6064 0.6299 0.0221  0.0638  0.0070  145 GLU   C OE2 
2182 N N   . GLU   B 140 ? 0.4542 0.4056 0.4795 0.0191  0.0755  0.0268  146 GLU   C N   
2183 C CA  . GLU   B 140 ? 0.4873 0.4402 0.5282 0.0190  0.0811  0.0288  146 GLU   C CA  
2184 C C   . GLU   B 140 ? 0.5106 0.4710 0.5667 0.0173  0.0760  0.0310  146 GLU   C C   
2185 O O   . GLU   B 140 ? 0.5190 0.4805 0.5862 0.0174  0.0796  0.0314  146 GLU   C O   
2186 C CB  . GLU   B 140 ? 0.5360 0.4826 0.5708 0.0205  0.0879  0.0241  146 GLU   C CB  
2187 C CG  . GLU   B 140 ? 0.6296 0.5770 0.6625 0.0200  0.0840  0.0192  146 GLU   C CG  
2188 C CD  . GLU   B 140 ? 0.7360 0.6841 0.7830 0.0200  0.0889  0.0192  146 GLU   C CD  
2189 O OE1 . GLU   B 140 ? 0.7673 0.7150 0.8132 0.0197  0.0870  0.0149  146 GLU   C OE1 
2190 O OE2 . GLU   B 140 ? 0.7462 0.6953 0.8065 0.0204  0.0946  0.0236  146 GLU   C OE2 
2191 N N1  . A1BP2 C .   ? 0.2816 0.2409 0.3400 0.0284  0.0427  0.0110  201 A1BP2 A N1  
2192 C C4  . A1BP2 C .   ? 0.3502 0.2994 0.3678 0.0124  0.0675  -0.0237 201 A1BP2 A C4  
2193 C C5  . A1BP2 C .   ? 0.3529 0.2965 0.3773 0.0143  0.0696  -0.0231 201 A1BP2 A C5  
2194 C C6  . A1BP2 C .   ? 0.3559 0.3030 0.3778 0.0146  0.0602  -0.0194 201 A1BP2 A C6  
2195 C C7  . A1BP2 C .   ? 0.3621 0.3030 0.3895 0.0155  0.0623  -0.0196 201 A1BP2 A C7  
2196 C C8  . A1BP2 C .   ? 0.3440 0.2911 0.3860 0.0227  0.0601  -0.0091 201 A1BP2 A C8  
2197 C C10 . A1BP2 C .   ? 0.3156 0.2586 0.3743 0.0271  0.0580  0.0001  201 A1BP2 A C10 
2198 C C13 . A1BP2 C .   ? 0.3492 0.2770 0.3884 0.0157  0.0587  -0.0161 201 A1BP2 A C13 
2199 O O2  . A1BP2 C .   ? 0.3281 0.2781 0.4103 0.0349  0.0582  0.0165  201 A1BP2 A O2  
2200 C C11 . A1BP2 C .   ? 0.3155 0.2665 0.3827 0.0306  0.0527  0.0098  201 A1BP2 A C11 
2201 C C9  . A1BP2 C .   ? 0.3301 0.2804 0.3887 0.0288  0.0571  0.0024  201 A1BP2 A C9  
2202 C C12 . A1BP2 C .   ? 0.3448 0.2831 0.3859 0.0196  0.0542  -0.0100 201 A1BP2 A C12 
2203 C C14 . A1BP2 C .   ? 0.3549 0.2912 0.3895 0.0170  0.0582  -0.0157 201 A1BP2 A C14 
2204 N N   . A1BP2 C .   ? 0.3471 0.2913 0.3916 0.0229  0.0584  -0.0079 201 A1BP2 A N   
2205 O O1  . A1BP2 C .   ? 0.3452 0.3001 0.3961 0.0273  0.0600  -0.0019 201 A1BP2 A O1  
2206 C C1  . A1BP2 C .   ? 0.3499 0.3054 0.3638 0.0134  0.0496  -0.0163 201 A1BP2 A C1  
2207 O O   . A1BP2 C .   ? 0.3524 0.3109 0.3664 0.0144  0.0423  -0.0126 201 A1BP2 A O   
2208 C C   . A1BP2 C .   ? 0.3670 0.3284 0.3699 0.0104  0.0338  -0.0139 201 A1BP2 A C   
2209 C C3  . A1BP2 C .   ? 0.3406 0.2980 0.3498 0.0110  0.0564  -0.0202 201 A1BP2 A C3  
2210 C C2  . A1BP2 C .   ? 0.3412 0.3014 0.3490 0.0117  0.0478  -0.0166 201 A1BP2 A C2  
2211 C C1  . GOL   D .   ? 0.5837 0.5744 0.5937 -0.0019 -0.0158 0.0476  202 GOL   A C1  
2212 O O1  . GOL   D .   ? 0.5933 0.5910 0.5992 -0.0039 -0.0199 0.0476  202 GOL   A O1  
2213 C C2  . GOL   D .   ? 0.5708 0.5555 0.5740 -0.0012 -0.0118 0.0371  202 GOL   A C2  
2214 O O2  . GOL   D .   ? 0.5742 0.5567 0.5800 0.0013  -0.0105 0.0322  202 GOL   A O2  
2215 C C3  . GOL   D .   ? 0.5511 0.5290 0.5575 -0.0005 -0.0073 0.0358  202 GOL   A C3  
2216 O O3  . GOL   D .   ? 0.5264 0.5027 0.5249 -0.0014 -0.0049 0.0277  202 GOL   A O3  
# 
