data_7I60
# 
_entry.id   7I60 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   7I60         pdb_00007i60 10.2210/pdb7i60/pdb 
WWPDB D_1001408359 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I60 
_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   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                       15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(2-methoxypyridin-3-yl)sulfamoyl]piperidine-3-carboxamide' 314.361   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                          65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                78.133    2   ?         ? ? ? 
5 water       nat water                                                               18.015    342 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[(2-methoxypyridin-3-yl)sulfamoyl]piperidine-3-carboxamide' A1B4N 
3 'ZINC ION'                                                          ZN    
4 'DIMETHYL SULFOXIDE'                                                DMS   
5 water                                                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1B4N non-polymer         . '(3S)-1-[(2-methoxypyridin-3-yl)sulfamoyl]piperidine-3-carboxamide' ? 'C12 H18 N4 O4 S' 314.361 
ALA   'L-peptide linking' y ALANINE                                                             ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                                            ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                          ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                     ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                                            ? 'C3 H7 N O2 S'    121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                ? 'C2 H6 O S'       78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                           ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                     ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                             ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                           ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                               ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                          ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                             ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                              ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                          ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                       ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                             ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                              ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                           ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                          ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                            ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                              ? 'C5 H11 N O2'     117.146 
ZN    non-polymer         . 'ZINC ION'                                                          ? 'Zn 2'            65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 ?   ?   ?   C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B4N 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B4N 
_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 A1B4N 1   201 201 A1B4N LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 2   DMS   DMS A . 
F 2 A1B4N 1   201 201 A1B4N LIG C . 
G 3 ZN    1   202 1   ZN    ZN  C . 
H 4 DMS   1   203 2   DMS   DMS C . 
I 5 HOH   1   301 49  HOH   HOH A . 
I 5 HOH   2   302 95  HOH   HOH A . 
I 5 HOH   3   303 61  HOH   HOH A . 
I 5 HOH   4   304 246 HOH   HOH A . 
I 5 HOH   5   305 157 HOH   HOH A . 
I 5 HOH   6   306 84  HOH   HOH A . 
I 5 HOH   7   307 292 HOH   HOH A . 
I 5 HOH   8   308 301 HOH   HOH A . 
I 5 HOH   9   309 344 HOH   HOH A . 
I 5 HOH   10  310 109 HOH   HOH A . 
I 5 HOH   11  311 6   HOH   HOH A . 
I 5 HOH   12  312 311 HOH   HOH A . 
I 5 HOH   13  313 103 HOH   HOH A . 
I 5 HOH   14  314 142 HOH   HOH A . 
I 5 HOH   15  315 298 HOH   HOH A . 
I 5 HOH   16  316 116 HOH   HOH A . 
I 5 HOH   17  317 250 HOH   HOH A . 
I 5 HOH   18  318 248 HOH   HOH A . 
I 5 HOH   19  319 229 HOH   HOH A . 
I 5 HOH   20  320 63  HOH   HOH A . 
I 5 HOH   21  321 48  HOH   HOH A . 
I 5 HOH   22  322 178 HOH   HOH A . 
I 5 HOH   23  323 56  HOH   HOH A . 
I 5 HOH   24  324 268 HOH   HOH A . 
I 5 HOH   25  325 5   HOH   HOH A . 
I 5 HOH   26  326 85  HOH   HOH A . 
I 5 HOH   27  327 176 HOH   HOH A . 
I 5 HOH   28  328 13  HOH   HOH A . 
I 5 HOH   29  329 93  HOH   HOH A . 
I 5 HOH   30  330 232 HOH   HOH A . 
I 5 HOH   31  331 49  HOH   HOH A . 
I 5 HOH   32  332 140 HOH   HOH A . 
I 5 HOH   33  333 14  HOH   HOH A . 
I 5 HOH   34  334 23  HOH   HOH A . 
I 5 HOH   35  335 128 HOH   HOH A . 
I 5 HOH   36  336 7   HOH   HOH A . 
I 5 HOH   37  337 309 HOH   HOH A . 
I 5 HOH   38  338 60  HOH   HOH A . 
I 5 HOH   39  339 107 HOH   HOH A . 
I 5 HOH   40  340 258 HOH   HOH A . 
I 5 HOH   41  341 21  HOH   HOH A . 
I 5 HOH   42  342 336 HOH   HOH A . 
I 5 HOH   43  343 133 HOH   HOH A . 
I 5 HOH   44  344 114 HOH   HOH A . 
I 5 HOH   45  345 249 HOH   HOH A . 
I 5 HOH   46  346 235 HOH   HOH A . 
I 5 HOH   47  347 59  HOH   HOH A . 
I 5 HOH   48  348 340 HOH   HOH A . 
I 5 HOH   49  349 14  HOH   HOH A . 
I 5 HOH   50  350 324 HOH   HOH A . 
I 5 HOH   51  351 22  HOH   HOH A . 
I 5 HOH   52  352 70  HOH   HOH A . 
I 5 HOH   53  353 63  HOH   HOH A . 
I 5 HOH   54  354 171 HOH   HOH A . 
I 5 HOH   55  355 72  HOH   HOH A . 
I 5 HOH   56  356 66  HOH   HOH A . 
I 5 HOH   57  357 71  HOH   HOH A . 
I 5 HOH   58  358 254 HOH   HOH A . 
I 5 HOH   59  359 27  HOH   HOH A . 
I 5 HOH   60  360 119 HOH   HOH A . 
I 5 HOH   61  361 228 HOH   HOH A . 
I 5 HOH   62  362 302 HOH   HOH A . 
I 5 HOH   63  363 99  HOH   HOH A . 
I 5 HOH   64  364 6   HOH   HOH A . 
I 5 HOH   65  365 19  HOH   HOH A . 
I 5 HOH   66  366 321 HOH   HOH A . 
I 5 HOH   67  367 237 HOH   HOH A . 
I 5 HOH   68  368 245 HOH   HOH A . 
I 5 HOH   69  369 26  HOH   HOH A . 
I 5 HOH   70  370 115 HOH   HOH A . 
I 5 HOH   71  371 102 HOH   HOH A . 
I 5 HOH   72  372 10  HOH   HOH A . 
I 5 HOH   73  373 289 HOH   HOH A . 
I 5 HOH   74  374 53  HOH   HOH A . 
I 5 HOH   75  375 314 HOH   HOH A . 
I 5 HOH   76  376 332 HOH   HOH A . 
I 5 HOH   77  377 29  HOH   HOH A . 
I 5 HOH   78  378 115 HOH   HOH A . 
I 5 HOH   79  379 62  HOH   HOH A . 
I 5 HOH   80  380 300 HOH   HOH A . 
I 5 HOH   81  381 253 HOH   HOH A . 
I 5 HOH   82  382 149 HOH   HOH A . 
I 5 HOH   83  383 303 HOH   HOH A . 
I 5 HOH   84  384 306 HOH   HOH A . 
I 5 HOH   85  385 89  HOH   HOH A . 
I 5 HOH   86  386 257 HOH   HOH A . 
I 5 HOH   87  387 263 HOH   HOH A . 
I 5 HOH   88  388 333 HOH   HOH A . 
I 5 HOH   89  389 227 HOH   HOH A . 
I 5 HOH   90  390 265 HOH   HOH A . 
I 5 HOH   91  391 53  HOH   HOH A . 
I 5 HOH   92  392 316 HOH   HOH A . 
I 5 HOH   93  393 277 HOH   HOH A . 
I 5 HOH   94  394 73  HOH   HOH A . 
I 5 HOH   95  395 38  HOH   HOH A . 
I 5 HOH   96  396 101 HOH   HOH A . 
I 5 HOH   97  397 190 HOH   HOH A . 
I 5 HOH   98  398 19  HOH   HOH A . 
I 5 HOH   99  399 243 HOH   HOH A . 
I 5 HOH   100 400 329 HOH   HOH A . 
I 5 HOH   101 401 308 HOH   HOH A . 
I 5 HOH   102 402 66  HOH   HOH A . 
I 5 HOH   103 403 12  HOH   HOH A . 
I 5 HOH   104 404 149 HOH   HOH A . 
I 5 HOH   105 405 197 HOH   HOH A . 
I 5 HOH   106 406 281 HOH   HOH A . 
I 5 HOH   107 407 156 HOH   HOH A . 
I 5 HOH   108 408 101 HOH   HOH A . 
I 5 HOH   109 409 75  HOH   HOH A . 
I 5 HOH   110 410 12  HOH   HOH A . 
I 5 HOH   111 411 96  HOH   HOH A . 
I 5 HOH   112 412 307 HOH   HOH A . 
I 5 HOH   113 413 91  HOH   HOH A . 
I 5 HOH   114 414 52  HOH   HOH A . 
I 5 HOH   115 415 40  HOH   HOH A . 
I 5 HOH   116 416 47  HOH   HOH A . 
I 5 HOH   117 417 112 HOH   HOH A . 
I 5 HOH   118 418 35  HOH   HOH A . 
I 5 HOH   119 419 113 HOH   HOH A . 
I 5 HOH   120 420 315 HOH   HOH A . 
I 5 HOH   121 421 92  HOH   HOH A . 
I 5 HOH   122 422 242 HOH   HOH A . 
I 5 HOH   123 423 85  HOH   HOH A . 
I 5 HOH   124 424 26  HOH   HOH A . 
I 5 HOH   125 425 285 HOH   HOH A . 
I 5 HOH   126 426 274 HOH   HOH A . 
I 5 HOH   127 427 240 HOH   HOH A . 
I 5 HOH   128 428 102 HOH   HOH A . 
I 5 HOH   129 429 323 HOH   HOH A . 
I 5 HOH   130 430 163 HOH   HOH A . 
I 5 HOH   131 431 202 HOH   HOH A . 
I 5 HOH   132 432 16  HOH   HOH A . 
I 5 HOH   133 433 61  HOH   HOH A . 
I 5 HOH   134 434 100 HOH   HOH A . 
I 5 HOH   135 435 290 HOH   HOH A . 
I 5 HOH   136 436 15  HOH   HOH A . 
I 5 HOH   137 437 154 HOH   HOH A . 
I 5 HOH   138 438 157 HOH   HOH A . 
I 5 HOH   139 439 148 HOH   HOH A . 
I 5 HOH   140 440 144 HOH   HOH A . 
I 5 HOH   141 441 126 HOH   HOH A . 
I 5 HOH   142 442 154 HOH   HOH A . 
I 5 HOH   143 443 160 HOH   HOH A . 
I 5 HOH   144 444 330 HOH   HOH A . 
I 5 HOH   145 445 147 HOH   HOH A . 
I 5 HOH   146 446 136 HOH   HOH A . 
I 5 HOH   147 447 256 HOH   HOH A . 
I 5 HOH   148 448 58  HOH   HOH A . 
I 5 HOH   149 449 138 HOH   HOH A . 
I 5 HOH   150 450 57  HOH   HOH A . 
I 5 HOH   151 451 346 HOH   HOH A . 
I 5 HOH   152 452 141 HOH   HOH A . 
I 5 HOH   153 453 129 HOH   HOH A . 
I 5 HOH   154 454 132 HOH   HOH A . 
I 5 HOH   155 455 158 HOH   HOH A . 
I 5 HOH   156 456 187 HOH   HOH A . 
I 5 HOH   157 457 335 HOH   HOH A . 
I 5 HOH   158 458 287 HOH   HOH A . 
I 5 HOH   159 459 286 HOH   HOH A . 
I 5 HOH   160 460 155 HOH   HOH A . 
I 5 HOH   161 461 181 HOH   HOH A . 
I 5 HOH   162 462 140 HOH   HOH A . 
I 5 HOH   163 463 221 HOH   HOH A . 
I 5 HOH   164 464 226 HOH   HOH A . 
I 5 HOH   165 465 320 HOH   HOH A . 
I 5 HOH   166 466 224 HOH   HOH A . 
J 5 HOH   1   301 120 HOH   HOH C . 
J 5 HOH   2   302 161 HOH   HOH C . 
J 5 HOH   3   303 174 HOH   HOH C . 
J 5 HOH   4   304 69  HOH   HOH C . 
J 5 HOH   5   305 64  HOH   HOH C . 
J 5 HOH   6   306 28  HOH   HOH C . 
J 5 HOH   7   307 310 HOH   HOH C . 
J 5 HOH   8   308 137 HOH   HOH C . 
J 5 HOH   9   309 8   HOH   HOH C . 
J 5 HOH   10  310 155 HOH   HOH C . 
J 5 HOH   11  311 2   HOH   HOH C . 
J 5 HOH   12  312 33  HOH   HOH C . 
J 5 HOH   13  313 252 HOH   HOH C . 
J 5 HOH   14  314 337 HOH   HOH C . 
J 5 HOH   15  315 109 HOH   HOH C . 
J 5 HOH   16  316 278 HOH   HOH C . 
J 5 HOH   17  317 32  HOH   HOH C . 
J 5 HOH   18  318 162 HOH   HOH C . 
J 5 HOH   19  319 264 HOH   HOH C . 
J 5 HOH   20  320 70  HOH   HOH C . 
J 5 HOH   21  321 328 HOH   HOH C . 
J 5 HOH   22  322 98  HOH   HOH C . 
J 5 HOH   23  323 64  HOH   HOH C . 
J 5 HOH   24  324 343 HOH   HOH C . 
J 5 HOH   25  325 293 HOH   HOH C . 
J 5 HOH   26  326 50  HOH   HOH C . 
J 5 HOH   27  327 338 HOH   HOH C . 
J 5 HOH   28  328 210 HOH   HOH C . 
J 5 HOH   29  329 123 HOH   HOH C . 
J 5 HOH   30  330 325 HOH   HOH C . 
J 5 HOH   31  331 20  HOH   HOH C . 
J 5 HOH   32  332 65  HOH   HOH C . 
J 5 HOH   33  333 124 HOH   HOH C . 
J 5 HOH   34  334 43  HOH   HOH C . 
J 5 HOH   35  335 234 HOH   HOH C . 
J 5 HOH   36  336 38  HOH   HOH C . 
J 5 HOH   37  337 30  HOH   HOH C . 
J 5 HOH   38  338 275 HOH   HOH C . 
J 5 HOH   39  339 91  HOH   HOH C . 
J 5 HOH   40  340 296 HOH   HOH C . 
J 5 HOH   41  341 238 HOH   HOH C . 
J 5 HOH   42  342 270 HOH   HOH C . 
J 5 HOH   43  343 271 HOH   HOH C . 
J 5 HOH   44  344 39  HOH   HOH C . 
J 5 HOH   45  345 78  HOH   HOH C . 
J 5 HOH   46  346 118 HOH   HOH C . 
J 5 HOH   47  347 204 HOH   HOH C . 
J 5 HOH   48  348 51  HOH   HOH C . 
J 5 HOH   49  349 54  HOH   HOH C . 
J 5 HOH   50  350 122 HOH   HOH C . 
J 5 HOH   51  351 259 HOH   HOH C . 
J 5 HOH   52  352 135 HOH   HOH C . 
J 5 HOH   53  353 71  HOH   HOH C . 
J 5 HOH   54  354 148 HOH   HOH C . 
J 5 HOH   55  355 294 HOH   HOH C . 
J 5 HOH   56  356 241 HOH   HOH C . 
J 5 HOH   57  357 111 HOH   HOH C . 
J 5 HOH   58  358 283 HOH   HOH C . 
J 5 HOH   59  359 11  HOH   HOH C . 
J 5 HOH   60  360 83  HOH   HOH C . 
J 5 HOH   61  361 31  HOH   HOH C . 
J 5 HOH   62  362 151 HOH   HOH C . 
J 5 HOH   63  363 126 HOH   HOH C . 
J 5 HOH   64  364 67  HOH   HOH C . 
J 5 HOH   65  365 239 HOH   HOH C . 
J 5 HOH   66  366 81  HOH   HOH C . 
J 5 HOH   67  367 272 HOH   HOH C . 
J 5 HOH   68  368 87  HOH   HOH C . 
J 5 HOH   69  369 110 HOH   HOH C . 
J 5 HOH   70  370 299 HOH   HOH C . 
J 5 HOH   71  371 276 HOH   HOH C . 
J 5 HOH   72  372 80  HOH   HOH C . 
J 5 HOH   73  373 79  HOH   HOH C . 
J 5 HOH   74  374 97  HOH   HOH C . 
J 5 HOH   75  375 78  HOH   HOH C . 
J 5 HOH   76  376 4   HOH   HOH C . 
J 5 HOH   77  377 334 HOH   HOH C . 
J 5 HOH   78  378 291 HOH   HOH C . 
J 5 HOH   79  379 230 HOH   HOH C . 
J 5 HOH   80  380 1   HOH   HOH C . 
J 5 HOH   81  381 260 HOH   HOH C . 
J 5 HOH   82  382 279 HOH   HOH C . 
J 5 HOH   83  383 266 HOH   HOH C . 
J 5 HOH   84  384 273 HOH   HOH C . 
J 5 HOH   85  385 205 HOH   HOH C . 
J 5 HOH   86  386 16  HOH   HOH C . 
J 5 HOH   87  387 7   HOH   HOH C . 
J 5 HOH   88  388 233 HOH   HOH C . 
J 5 HOH   89  389 146 HOH   HOH C . 
J 5 HOH   90  390 130 HOH   HOH C . 
J 5 HOH   91  391 288 HOH   HOH C . 
J 5 HOH   92  392 255 HOH   HOH C . 
J 5 HOH   93  393 317 HOH   HOH C . 
J 5 HOH   94  394 269 HOH   HOH C . 
J 5 HOH   95  395 3   HOH   HOH C . 
J 5 HOH   96  396 37  HOH   HOH C . 
J 5 HOH   97  397 13  HOH   HOH C . 
J 5 HOH   98  398 247 HOH   HOH C . 
J 5 HOH   99  399 282 HOH   HOH C . 
J 5 HOH   100 400 29  HOH   HOH C . 
J 5 HOH   101 401 48  HOH   HOH C . 
J 5 HOH   102 402 11  HOH   HOH C . 
J 5 HOH   103 403 54  HOH   HOH C . 
J 5 HOH   104 404 231 HOH   HOH C . 
J 5 HOH   105 405 150 HOH   HOH C . 
J 5 HOH   106 406 45  HOH   HOH C . 
J 5 HOH   107 407 50  HOH   HOH C . 
J 5 HOH   108 408 83  HOH   HOH C . 
J 5 HOH   109 409 146 HOH   HOH C . 
J 5 HOH   110 410 244 HOH   HOH C . 
J 5 HOH   111 411 31  HOH   HOH C . 
J 5 HOH   112 412 108 HOH   HOH C . 
J 5 HOH   113 413 41  HOH   HOH C . 
J 5 HOH   114 414 139 HOH   HOH C . 
J 5 HOH   115 415 62  HOH   HOH C . 
J 5 HOH   116 416 326 HOH   HOH C . 
J 5 HOH   117 417 297 HOH   HOH C . 
J 5 HOH   118 418 305 HOH   HOH C . 
J 5 HOH   119 419 120 HOH   HOH C . 
J 5 HOH   120 420 304 HOH   HOH C . 
J 5 HOH   121 421 261 HOH   HOH C . 
J 5 HOH   122 422 262 HOH   HOH C . 
J 5 HOH   123 423 124 HOH   HOH C . 
J 5 HOH   124 424 68  HOH   HOH C . 
J 5 HOH   125 425 341 HOH   HOH C . 
J 5 HOH   126 426 267 HOH   HOH C . 
J 5 HOH   127 427 236 HOH   HOH C . 
J 5 HOH   128 428 44  HOH   HOH C . 
J 5 HOH   129 429 345 HOH   HOH C . 
J 5 HOH   130 430 312 HOH   HOH C . 
J 5 HOH   131 431 52  HOH   HOH C . 
J 5 HOH   132 432 47  HOH   HOH C . 
J 5 HOH   133 433 117 HOH   HOH C . 
J 5 HOH   134 434 295 HOH   HOH C . 
J 5 HOH   135 435 139 HOH   HOH C . 
J 5 HOH   136 436 90  HOH   HOH C . 
J 5 HOH   137 437 196 HOH   HOH C . 
J 5 HOH   138 438 319 HOH   HOH C . 
J 5 HOH   139 439 318 HOH   HOH C . 
J 5 HOH   140 440 95  HOH   HOH C . 
J 5 HOH   141 441 166 HOH   HOH C . 
J 5 HOH   142 442 41  HOH   HOH C . 
J 5 HOH   143 443 153 HOH   HOH C . 
J 5 HOH   144 444 159 HOH   HOH C . 
J 5 HOH   145 445 43  HOH   HOH C . 
J 5 HOH   146 446 104 HOH   HOH C . 
J 5 HOH   147 447 322 HOH   HOH C . 
J 5 HOH   148 448 331 HOH   HOH C . 
J 5 HOH   149 449 131 HOH   HOH C . 
J 5 HOH   150 450 135 HOH   HOH C . 
J 5 HOH   151 451 118 HOH   HOH C . 
J 5 HOH   152 452 116 HOH   HOH C . 
J 5 HOH   153 453 280 HOH   HOH C . 
J 5 HOH   154 454 143 HOH   HOH C . 
J 5 HOH   155 455 145 HOH   HOH C . 
J 5 HOH   156 456 185 HOH   HOH C . 
J 5 HOH   157 457 17  HOH   HOH C . 
J 5 HOH   158 458 152 HOH   HOH C . 
J 5 HOH   159 459 342 HOH   HOH C . 
J 5 HOH   160 460 198 HOH   HOH C . 
J 5 HOH   161 461 172 HOH   HOH C . 
J 5 HOH   162 462 27  HOH   HOH C . 
J 5 HOH   163 463 165 HOH   HOH C . 
J 5 HOH   164 464 284 HOH   HOH C . 
J 5 HOH   165 465 339 HOH   HOH C . 
J 5 HOH   166 466 93  HOH   HOH C . 
J 5 HOH   167 467 199 HOH   HOH C . 
J 5 HOH   168 468 123 HOH   HOH C . 
J 5 HOH   169 469 82  HOH   HOH C . 
J 5 HOH   170 470 182 HOH   HOH C . 
J 5 HOH   171 471 164 HOH   HOH C . 
J 5 HOH   172 472 222 HOH   HOH C . 
J 5 HOH   173 473 313 HOH   HOH C . 
J 5 HOH   174 474 218 HOH   HOH C . 
J 5 HOH   175 475 141 HOH   HOH C . 
J 5 HOH   176 476 207 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           7I60 
_cell.length_a           72.851 
_cell.length_b           61.874 
_cell.length_c           65.185 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.81 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I60 
_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          7I60 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.31 
_exptl_crystal.density_percent_sol   46.71 
_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   2025-01-24 
_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   0.92204 
_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        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I60 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.14 
_reflns.d_resolution_high            1.43 
_reflns.number_obs                   53636 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.104 
_reflns.pdbx_netI_over_sigmaI        8.5 
_reflns.pdbx_redundancy              5.9 
_reflns.pdbx_Rrim_I_all              0.114 
_reflns.pdbx_Rpim_I_all              0.046 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     318889 
_reflns.pdbx_chi_squared             0.81 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.43 
_reflns_shell.d_res_low                   1.51 
_reflns_shell.number_measured_all         34676 
_reflns_shell.number_unique_obs           7788 
_reflns_shell.Rmerge_I_obs                1.534 
_reflns_shell.pdbx_chi_squared            0.68 
_reflns_shell.pdbx_redundancy             4.5 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.1 
_reflns_shell.pdbx_Rrim_I_all             1.741 
_reflns_shell.pdbx_Rpim_I_all             0.811 
_reflns_shell.pdbx_CC_half                0.403 
_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                                 7I60 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     53408 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             47.14 
_refine.ls_d_res_high                            1.429 
_refine.ls_percent_reflns_obs                    99.6 
_refine.ls_R_factor_obs                          0.1887 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1875 
_refine.ls_R_factor_R_free                       0.2119 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.890 
_refine.ls_number_reflns_R_free                  2609 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.952 
_refine.B_iso_mean                               20.91 
_refine.aniso_B[1][1]                            -0.54240 
_refine.aniso_B[2][2]                            1.34200 
_refine.aniso_B[3][3]                            -0.79960 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.22840 
_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             0.065 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.066 
_refine.pdbx_overall_SU_R_Blow_DPI               0.069 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.069 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I60 
_refine_analyze.Luzzati_coordinate_error_obs    0.19 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_refine_hist.number_atoms_solvent             342 
_refine_hist.number_atoms_total               2542 
_refine_hist.d_res_high                       1.429 
_refine_hist.d_res_low                        47.14 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.011 ? 2.00  2258 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.03  ? 2.00  3074 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  754  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  404  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2258 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.55  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.24 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  276  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1968 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.43 
_refine_ls_shell.d_res_low                        1.44 
_refine_ls_shell.number_reflns_R_work             1026 
_refine_ls_shell.R_factor_R_work                  0.3152 
_refine_ls_shell.percent_reflns_obs               93.27 
_refine_ls_shell.R_factor_R_free                  0.3346 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.02 
_refine_ls_shell.number_reflns_R_free             43 
_refine_ls_shell.number_reflns_all                1069 
_refine_ls_shell.R_factor_all                     0.3159 
# 
_struct.entry_id                  7I60 
_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-0036541-001 (A71EV2A-x4899)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I60 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I60 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I60 C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,I 
2 1 B,F,G,H,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 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 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.352 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.355 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 G ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 111.6 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 105.5 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.0 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 107.4 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.5 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 114.8 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 108.0 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.1 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.6 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 108.4 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.8 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 113.5 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
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 
AA1 3 4 ? 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 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
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 ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
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 VAL B 126 ? O VAL C 132 N ALA B 95  ? N ALA C 101 
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I60 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 315 ? ? O A HOH 367 ? ? 2.11 
2 1 O A HOH 380 ? ? O A HOH 390 ? ? 2.12 
3 1 O A HOH 412 ? ? O A HOH 457 ? ? 2.13 
4 1 O A HOH 383 ? ? O A HOH 389 ? ? 2.13 
5 1 O A HOH 376 ? ? O A HOH 412 ? ? 2.18 
6 1 O A HOH 340 ? ? O A HOH 362 ? ? 2.19 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    C 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -138.55 
_pdbx_validate_torsion.psi             -30.77 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 19.7115 6.7924   18.2970 -0.0234 -0.0322 0.0053 -0.0018 0.0115  -0.0027 1.0149 1.2772 0.5060 
-0.7492 -0.2972 0.2690 -0.0039 -0.0054 0.1205 0.0083  0.0465 0.0188  0.0259 0.0484 -0.0426 
'X-RAY DIFFRACTION' 2 ? refined 15.3425 -24.0036 14.1970 -0.0172 -0.0277 0.0046 -0.0018 -0.0008 -0.0051 0.8278 1.2034 0.2624 
0.6058  0.0592  0.0945 -0.0309 0.0158  0.0796 -0.0113 0.0391 -0.0064 0.0234 0.0014 -0.0082 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 146 ? A GLU 140 
2  1 Y 1 A ALA 147 ? A ALA 141 
3  1 Y 1 A MET 148 ? A MET 142 
4  1 Y 1 A GLU 149 ? A GLU 143 
5  1 Y 1 A GLN 150 ? A GLN 144 
6  1 Y 1 C GLU 146 ? B GLU 140 
7  1 Y 1 C ALA 147 ? B ALA 141 
8  1 Y 1 C MET 148 ? B MET 142 
9  1 Y 1 C GLU 149 ? B GLU 143 
10 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B4N N1   N  N N 1   
A1B4N N3   N  N N 2   
A1B4N C4   C  Y N 3   
A1B4N C5   C  Y N 4   
A1B4N C6   C  N N 5   
A1B4N C7   C  N N 6   
A1B4N C8   C  N N 7   
A1B4N C10  C  N N 8   
A1B4N O3   O  N N 9   
A1B4N C9   C  N S 10  
A1B4N C11  C  N N 11  
A1B4N N2   N  N N 12  
A1B4N S    S  N N 13  
A1B4N O1   O  N N 14  
A1B4N O2   O  N N 15  
A1B4N C1   C  Y N 16  
A1B4N O    O  N N 17  
A1B4N C    C  N N 18  
A1B4N C3   C  Y N 19  
A1B4N C2   C  Y N 20  
A1B4N N    N  Y N 21  
A1B4N H7   H  N N 22  
A1B4N H14  H  N N 23  
A1B4N H15  H  N N 24  
A1B4N H6   H  N N 25  
A1B4N H8   H  N N 26  
A1B4N H9   H  N N 27  
A1B4N H10  H  N N 28  
A1B4N H11  H  N N 29  
A1B4N H12  H  N N 30  
A1B4N H13  H  N N 31  
A1B4N H    H  N N 32  
A1B4N H16  H  N N 33  
A1B4N H17  H  N N 34  
A1B4N H2   H  N N 35  
A1B4N H1   H  N N 36  
A1B4N H3   H  N N 37  
A1B4N H5   H  N N 38  
A1B4N H4   H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
ZN    ZN   ZN N N 440 
# 
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 
A1B4N C   O    sing N N 1   
A1B4N O   C1   sing N N 2   
A1B4N C1  N    doub Y N 3   
A1B4N N   C2   sing Y N 4   
A1B4N C2  C3   doub Y N 5   
A1B4N C3  C4   sing Y N 6   
A1B4N C4  C5   doub Y N 7   
A1B4N C1  C5   sing Y N 8   
A1B4N C5  N1   sing N N 9   
A1B4N N1  S    sing N N 10  
A1B4N O1  S    doub N N 11  
A1B4N O2  S    doub N N 12  
A1B4N S   N2   sing N N 13  
A1B4N N2  C6   sing N N 14  
A1B4N C6  C7   sing N N 15  
A1B4N C7  C8   sing N N 16  
A1B4N C8  C9   sing N N 17  
A1B4N C9  C10  sing N N 18  
A1B4N N3  C10  sing N N 19  
A1B4N C10 O3   doub N N 20  
A1B4N C11 C9   sing N N 21  
A1B4N N2  C11  sing N N 22  
A1B4N N1  H7   sing N N 23  
A1B4N N3  H14  sing N N 24  
A1B4N N3  H15  sing N N 25  
A1B4N C4  H6   sing N N 26  
A1B4N C6  H8   sing N N 27  
A1B4N C6  H9   sing N N 28  
A1B4N C7  H10  sing N N 29  
A1B4N C7  H11  sing N N 30  
A1B4N C8  H12  sing N N 31  
A1B4N C8  H13  sing N N 32  
A1B4N C9  H    sing N N 33  
A1B4N C11 H16  sing N N 34  
A1B4N C11 H17  sing N N 35  
A1B4N C   H2   sing N N 36  
A1B4N C   H1   sing N N 37  
A1B4N C   H3   sing N N 38  
A1B4N C3  H5   sing N N 39  
A1B4N C2  H4   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_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_1002344 
_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                    7I60 
_atom_sites.fract_transf_matrix[1][1]   0.013727 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000674 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016162 
_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]   0.015359 
_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   ? 16.350 6.469   8.172  1.00 20.59 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.107 6.559   8.930  1.00 20.48 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 14.950 5.406   9.909  1.00 19.82 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.606 4.370   9.771  1.00 19.81 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 13.920 6.620   7.973  1.00 23.45 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.777 5.391   7.279  1.00 26.81 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.113 5.605   10.925 1.00 18.59 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.831 4.572   11.906 1.00 17.19 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.504 5.132   13.274 1.00 15.70 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.908 6.255   13.616 1.00 15.01 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.786 4.349   14.067 1.00 14.23 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.396 4.776   15.398 1.00 15.06 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.340 3.575   16.340 1.00 14.69 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.261 2.428   15.879 1.00 15.69 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.997 5.414   15.322 1.00 16.62 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.332 3.851   17.674 1.00 13.20 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 12.101 2.855   18.705 1.00 12.89 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.688 3.071   19.207 1.00 13.58 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.317 4.208   19.492 1.00 13.60 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 13.055 3.036   19.898 1.00 13.52 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.530 3.022   19.396 1.00 13.75 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.823 1.953   20.964 1.00 14.39 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.496 3.521   20.481 1.00 15.30 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.905  2.004   19.313 1.00 14.43 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.535  2.112   19.814 1.00 16.24 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.427  1.360   21.125 1.00 16.06 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.419  0.133   21.089 1.00 17.02 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.544  1.544   18.770 1.00 16.54 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.483  2.377   17.516 1.00 17.22 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.673  3.500   17.446 1.00 18.25 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.271  2.073   16.418 1.00 18.49 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.648  4.299   16.311 1.00 19.93 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.255  2.861   15.279 1.00 19.92 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.445  3.979   15.230 1.00 20.80 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.433  4.772   14.101 1.00 23.49 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.377  2.040   22.279 1.00 16.48 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.342  1.377   23.587 1.00 16.62 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.213  1.963   24.399 1.00 17.93 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 7.118  3.183   24.537 1.00 18.84 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.721  1.490   24.309 1.00 18.89 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.235 2.942   24.322 1.00 18.94 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.671  0.925   25.720 1.00 20.69 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.292  1.117   24.860 1.00 18.87 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 5.137  1.606   25.615 1.00 19.16 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.338  2.591   24.781 1.00 19.54 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 4.102  2.324   23.598 1.00 20.17 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 4.032  3.776   25.337 1.00 19.35 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.342  4.799   24.553 1.00 19.16 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.292  5.886   24.066 1.00 17.97 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.907  7.056   23.939 1.00 17.98 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 2.133  5.381   25.300 1.00 22.54 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 1.022  4.375   25.438 1.00 30.66 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.457  3.894   24.450 1.00 33.66 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.718  3.998   26.657 1.00 31.74 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.535  5.499   23.769 1.00 16.10 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.541  6.462   23.303 1.00 15.89 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 7.141  6.018   21.962 1.00 14.68 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.294  4.811   21.691 1.00 15.50 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.715  6.527   24.314 1.00 16.34 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.315  7.056   25.678 1.00 17.10 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.681  8.284   25.812 1.00 18.50 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.578  6.332   26.834 1.00 19.19 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.331  8.786   27.062 1.00 20.62 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.249  6.831   28.090 1.00 20.61 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.583  8.043   28.195 1.00 22.75 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.254  8.577   29.425 1.00 24.54 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.543  7.013   21.160 1.00 13.00 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.257  6.863   19.892 1.00 13.15 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.572  7.660   20.039 1.00 13.52 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.523  8.862   20.328 1.00 13.06 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.416  7.376   18.699 1.00 15.46 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.197  7.610   17.391 1.00 17.84 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.286  7.975   16.213 1.00 18.54 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.874  8.990   15.320 1.00 19.49 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.385  8.748   14.117 1.00 21.63 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.467  7.496   13.657 1.00 23.66 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.843  9.748   13.372 1.00 20.64 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.742 6.991   19.872 1.00 13.20 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 12.046 7.645   19.988 1.00 13.25 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.617 7.775   18.602 1.00 13.16 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.771 6.749   17.916 1.00 13.02 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 13.034 6.840   20.879 1.00 13.94 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.320 7.644   21.143 1.00 13.10 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.384 6.363   22.189 1.00 14.62 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.935 9.019   18.167 1.00 12.67 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.500 9.239   16.830 1.00 12.83 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.730 10.161  16.930 1.00 12.73 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.942 10.857  17.941 1.00 13.63 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.454 9.888   15.879 1.00 14.68 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.332 8.928   15.558 1.00 18.08 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.922 11.206  16.475 1.00 14.87 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.526 10.245  15.825 1.00 12.41 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.589 11.260  15.780 1.00 12.08 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.897 12.634  15.779 1.00 12.51 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.946 12.842  14.997 1.00 13.38 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.387 11.165  14.490 1.00 12.72 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.177 9.882   14.397 1.00 13.40 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.721 8.873   13.848 1.00 14.51 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.391 9.909   14.925 1.00 14.56 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.341 13.564  16.634 1.00 11.73 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.665 14.869  16.706 1.00 11.64 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.684 15.573  15.308 1.00 13.27 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.684 16.208  14.915 1.00 14.81 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.347 15.728  17.746 1.00 12.76 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.567 17.030  18.074 1.00 13.09 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.471 17.889  18.946 1.00 14.39 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.846 19.128  19.446 1.00 16.29 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.848 20.278  18.784 1.00 16.23 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.334 20.344  17.550 1.00 17.20 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.324 21.372  19.337 1.00 16.78 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.788 15.398  14.546 1.00 12.87 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.877 16.087  13.243 1.00 13.94 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.939 15.509  12.160 1.00 16.48 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.745 16.150  11.106 1.00 18.63 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.343 16.197  12.739 1.00 14.79 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.937 14.917  12.244 1.00 15.77 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.501 13.980  13.117 1.00 15.95 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 19.086 14.478  10.967 1.00 16.97 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.964 12.996  12.337 1.00 16.62 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.718 13.242  11.037 1.00 16.94 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.350 14.332  12.421 1.00 14.50 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.394 13.689  11.521 1.00 15.08 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.945 13.727  12.062 1.00 15.74 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 12.038 13.158  11.430 1.00 16.21 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.830 12.234  11.220 1.00 14.91 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.241 12.115  10.571 1.00 16.07 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.570 10.646  10.313 1.00 15.94 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.304 12.900  9.220  1.00 16.04 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.715 14.387  13.226 1.00 15.67 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.361 14.404  13.800 1.00 15.23 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.384 15.089  12.847 1.00 16.09 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.735 16.082  12.223 1.00 16.83 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.368 15.143  15.132 1.00 15.95 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.168  14.554  12.772 1.00 16.27 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 8.149  15.109  11.875 1.00 17.34 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.307  16.187  12.578 1.00 18.26 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.410  16.382  13.799 1.00 17.65 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.211  13.960  11.426 1.00 20.01 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.498  13.496  12.572 1.00 21.49 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.951  12.818  10.773 1.00 20.97 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.369  16.830  11.830 1.00 19.48 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.443  17.780  12.432 1.00 21.19 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.605  17.074  13.531 1.00 18.87 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.375  17.631  14.599 1.00 18.81 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.480  18.345  11.359 1.00 26.01 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 5.143  19.166  10.299 1.00 34.46 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 6.006  20.197  10.621 1.00 38.32 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 5.014  19.107  8.948  1.00 37.46 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.397  20.715  9.462  1.00 39.43 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.822  20.092  8.426  1.00 39.62 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.183  15.820  13.267 1.00 18.86 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.386  15.076  14.253 1.00 19.27 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.194  14.755  15.509 1.00 17.77 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.650  14.787  16.609 1.00 18.27 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.823  13.788  13.672 1.00 23.23 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.915  13.043  14.615 1.00 34.04 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.777  13.463  14.855 1.00 38.36 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 2.400  11.915  15.171 1.00 37.88 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.510  14.437  15.372 1.00 15.83 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.340  14.204  16.567 1.00 14.87 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.347  15.476  17.444 1.00 14.86 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.221  15.371  18.670 1.00 14.75 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.788  13.877  16.156 1.00 14.76 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.947  12.486  15.619 1.00 17.79 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.322  11.571  16.172 1.00 17.65 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.710  12.320  14.605 1.00 17.62 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.560  16.655  16.813 1.00 14.53 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.616  17.891  17.595 1.00 15.13 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.252  18.244  18.216 1.00 17.26 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.201  18.777  19.332 1.00 18.05 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.164  19.040  16.749 1.00 15.46 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.670  19.034  16.664 1.00 15.66 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.437  18.630  15.606 1.00 17.20 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.585  19.540  17.652 1.00 15.40 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.781 18.805  15.897 1.00 16.95 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.893 19.386  17.138 1.00 16.78 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.424  20.109  18.913 1.00 16.53 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 12.032 19.804  17.845 1.00 16.09 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.555 20.527  19.603 1.00 16.90 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.832 20.357  19.079 1.00 16.09 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.153  17.886  17.538 1.00 17.03 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.802  18.146  18.110 1.00 18.14 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.474  17.223  19.309 1.00 18.89 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.522  17.483  20.074 1.00 19.63 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.747  17.983  17.038 1.00 19.03 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.165  16.079  19.412 1.00 17.58 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 2.949  15.156  20.505 1.00 17.58 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.255  15.029  21.338 1.00 16.30 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.563  13.957  21.845 1.00 16.28 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.541  13.792  19.935 1.00 18.84 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.190  13.829  19.277 1.00 22.26 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.167  13.790  19.962 1.00 22.73 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 1.156  13.918  17.955 1.00 23.75 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 5.014  16.110  21.469 1.00 15.30 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.311  16.103  22.147 1.00 15.25 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.239  15.722  23.624 1.00 16.12 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.404  16.237  24.378 1.00 17.80 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 6.914  17.518  22.027 1.00 15.70 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.276  17.727  22.675 1.00 16.85 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.332  16.884  21.962 1.00 16.83 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.677  19.230  22.632 1.00 17.18 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.133  14.811  24.039 1.00 16.00 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.303  14.419  25.431 1.00 17.30 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.623  15.030  25.960 1.00 18.07 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.664  15.695  27.015 1.00 19.49 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.313  12.871  25.584 1.00 18.79 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.706  12.470  27.005 1.00 18.90 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 5.957  12.287  25.210 1.00 19.59 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.695  14.882  25.169 1.00 16.32 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 11.016 15.350  25.580 1.00 16.42 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 11.918 15.438  24.365 1.00 15.20 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.823 14.606  23.465 1.00 15.22 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.620 14.345  26.606 1.00 17.73 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 13.087 14.507  26.947 1.00 19.21 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.641 15.346  27.874 1.00 20.50 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.177 13.771  26.368 1.00 18.59 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 15.021 15.219  27.865 1.00 20.65 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.370 14.223  26.980 1.00 19.34 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.256 12.762  25.407 1.00 18.42 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.628 13.653  26.693 1.00 18.96 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.502 12.238  25.086 1.00 18.62 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.672 12.691  25.721 1.00 18.08 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.810 16.421  24.338 1.00 14.77 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.815 16.493  23.266 1.00 15.05 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 15.120 17.052  23.812 1.00 14.74 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 15.116 17.849  24.758 1.00 15.82 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.303 17.288  22.054 1.00 16.25 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.737 18.674  22.350 1.00 17.43 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.762 19.764  22.612 1.00 21.86 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.474 20.660  23.440 1.00 23.78 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.852 19.728  22.003 1.00 18.12 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.256 16.670  23.187 1.00 14.40 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.543 17.186  23.627 1.00 14.25 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.437 17.307  22.398 1.00 14.86 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.886 16.299  21.836 1.00 14.92 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 18.119 16.272  24.719 1.00 17.39 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.424 16.726  25.346 1.00 24.28 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.184 17.454  24.674 1.00 27.26 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.707 16.308  26.486 1.00 25.72 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.675 18.545  21.964 1.00 15.80 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.499 18.813  20.797 0.50 16.73 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.501 18.796  20.789 0.50 16.40 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.924 18.287  21.009 1.00 16.66 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.562 17.824  20.052 1.00 16.61 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.498 20.312  20.495 0.50 19.72 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.515 20.285  20.450 0.50 18.46 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 20.435 20.651  19.491 0.50 23.96 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 20.193 21.011  21.462 0.50 21.14 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.445 18.381  22.257 1.00 16.95 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.830 17.889  22.494 1.00 17.66 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 22.943 16.371  22.354 1.00 17.25 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 24.040 15.890  22.218 1.00 18.52 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.362 18.297  23.861 1.00 21.69 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.771 17.538  24.901 1.00 27.16 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.827 15.639  22.350 1.00 14.91 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.866 14.173  22.193 1.00 14.06 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.318 13.725  20.813 1.00 14.02 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.355 12.526  20.513 1.00 14.32 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 20.989 13.526  23.291 1.00 13.63 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.594 13.684  24.705 1.00 16.15 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.792 13.013  25.816 1.00 15.21 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.787 11.542  25.676 1.00 14.42 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.602 10.685  26.674 1.00 16.33 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.444 11.127  27.924 1.00 17.77 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.640 9.368   26.446 1.00 15.52 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.750 14.656  20.005 1.00 13.85 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 20.053 14.322  18.764 1.00 13.02 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.880 13.372  19.016 1.00 12.61 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.597 12.542  18.148 1.00 12.99 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 20.986 13.775  17.670 1.00 13.34 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.314 13.543  16.325 1.00 14.14 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.535 14.421  15.882 1.00 14.01 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.598 12.498  15.690 1.00 13.89 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.166 13.523  20.163 1.00 12.36 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.013 12.663  20.434 1.00 12.46 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.730 13.460  20.616 1.00 12.80 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.755 14.562  21.151 1.00 13.90 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.193 11.825  21.720 1.00 13.01 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.217 10.695  21.648 1.00 13.33 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.260 9.994   22.999 1.00 14.92 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.895 9.708   20.523 1.00 12.64 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.608 12.854  20.217 1.00 11.81 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.294 13.406  20.469 1.00 11.89 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.367 12.229  20.753 1.00 12.48 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.470 11.173  20.098 1.00 13.40 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.802 14.254  19.268 1.00 12.33 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.412 14.930  19.488 1.00 12.73 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.317 16.251  18.759 1.00 13.82 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.275 14.042  18.952 1.00 13.31 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.505 12.371  21.763 1.00 11.75 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.515 11.348  22.133 1.00 13.10 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 9.128  11.976  22.035 1.00 13.59 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 8.913  13.085  22.565 1.00 14.15 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.745 10.842  23.574 1.00 14.25 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.658  9.823   23.989 1.00 15.00 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 12.131 10.211  23.690 1.00 14.68 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.230  11.300  21.306 1.00 14.17 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.842  11.745  21.161 1.00 14.64 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.905  10.656  21.724 1.00 16.23 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.306  9.491   21.910 1.00 15.72 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.529  12.060  19.701 1.00 16.47 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.691  10.943  18.832 1.00 17.83 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.647  11.041  22.017 1.00 16.47 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.675  10.077  22.550 1.00 17.03 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 2.899  9.372   21.424 1.00 18.41 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.708  9.930   20.350 1.00 18.62 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.723  10.783  23.513 1.00 18.95 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 2.069  11.818  22.809 1.00 21.55 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.459  8.120   21.665 1.00 19.12 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.722  7.340   20.670 1.00 21.19 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.389  6.875   21.284 1.00 23.55 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.263  6.810   22.512 1.00 24.25 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.520  6.084   20.214 1.00 22.49 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.629  5.208   21.318 1.00 22.88 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.903  6.401   19.700 1.00 22.60 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.577 6.517   20.434 1.00 25.16 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -1.841 5.969   20.918 1.00 27.17 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.750 4.422   21.018 1.00 28.87 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.425 3.819   21.859 1.00 31.14 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -3.006 6.429   20.022 1.00 30.04 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.697 6.077   18.673 1.00 31.27 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.238 7.937   20.090 1.00 31.33 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -0.928 3.787   20.174 1.00 27.79 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.773 2.338   20.172 1.00 27.59 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.428  1.910   21.020 1.00 26.72 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.419  2.640   21.115 1.00 25.55 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.583 1.848   18.743 1.00 28.37 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.369  0.698   21.571 1.00 26.41 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.462  0.140   22.382 1.00 27.38 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.621  -0.315  21.497 1.00 26.46 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.376  -0.976  20.488 1.00 27.53 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.926  -1.049  23.190 1.00 31.03 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.970  -1.725  24.067 1.00 38.59 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 2.216  -0.994  25.370 1.00 46.88 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 1.556  0.007   25.711 1.00 49.61 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 3.177  -1.500  26.140 1.00 48.16 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.854  0.078   21.823 1.00 24.10 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 5.011  -0.242  20.979 1.00 23.47 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.456  -1.692  20.949 1.00 23.97 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 5.059  -2.475  21.799 1.00 26.84 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.316  -2.030  19.976 1.00 20.83 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.838  -3.375  19.746 1.00 19.86 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 8.191  -3.632  20.430 1.00 19.80 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.583  -4.782  20.572 1.00 19.16 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 6.951  -3.607  18.239 1.00 21.08 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 8.054  -2.442  17.372 1.00 23.01 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.914  -2.582  20.830 1.00 19.73 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.289 -2.729  21.351 1.00 18.23 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.398 -2.747  22.885 1.00 18.20 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 9.456  -2.301  23.562 1.00 19.91 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 11.144 -1.558  20.803 1.00 17.59 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.368 -1.603  19.305 1.00 20.55 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 11.790 -2.693  18.795 1.00 21.24 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 11.107 -0.565  18.626 1.00 17.78 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 11.583 -3.187  23.428 1.00 17.20 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 11.990 -3.152  24.832 1.00 19.53 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.453 -2.600  24.934 1.00 18.88 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.237 -2.781  24.003 1.00 19.21 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 11.792 -4.488  25.540 1.00 23.73 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 12.709 -5.440  25.020 1.00 25.18 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 10.369 -5.032  25.393 1.00 24.92 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 13.788 -1.869  26.021 1.00 17.64 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 15.076 -1.178  26.156 1.00 15.64 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 16.046 -1.972  27.033 1.00 16.33 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.654 -2.498  28.087 1.00 17.62 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 14.853 0.229   26.793 1.00 15.21 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.723 1.044   26.081 1.00 16.38 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 16.155 1.044   26.818 1.00 15.28 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 14.038 1.286   24.552 1.00 17.58 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.303 -2.101  26.586 1.00 14.94 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.343 -2.756  27.364 1.00 14.96 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.692 -1.882  28.576 1.00 16.32 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.743 -0.648  28.483 1.00 15.63 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.613 -2.944  26.497 1.00 14.83 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 18.956 -2.533  29.735 1.00 17.28 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.369 -1.806  30.953 1.00 17.54 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.611 -2.583  31.370 1.00 19.99 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.526 -3.592  32.066 1.00 21.34 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.275 -1.853  32.042 1.00 17.33 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.973 -1.243  31.592 1.00 16.81 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.038 0.273   31.288 1.00 20.52 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.716 0.751   30.883 1.00 19.47 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.480 1.914   30.276 1.00 21.76 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.478 2.740   29.990 1.00 20.14 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 14.242 2.261   29.955 1.00 21.24 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 21.733 -2.247  30.738 1.00 19.78 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 22.959 -3.039  30.872 1.00 21.08 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.183 -2.166  30.542 1.00 20.35 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 24.063 -0.999  30.176 1.00 20.96 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 22.876 -4.215  29.905 1.00 20.79 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 22.894 -3.691  28.167 1.00 18.24 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.380 -2.789  30.609 1.00 21.87 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.595 -2.080  30.225 1.00 22.22 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.265 -2.792  29.051 1.00 22.09 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.486 -2.778  28.965 1.00 22.57 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 27.573 -1.962  31.427 1.00 26.65 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 28.061 -3.283  31.996 1.00 34.40 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 27.477 -4.341  31.650 1.00 34.25 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 29.024 -3.265  32.797 1.00 41.46 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.497 -3.445  28.150 1.00 20.81 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 27.103 -4.112  26.984 1.00 18.75 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 27.861 -3.098  26.132 1.00 18.34 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.420 -1.942  26.007 1.00 19.16 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 26.026 -4.791  26.145 1.00 19.05 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.370 -6.340  26.816 1.00 18.72 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 29.013 -3.484  25.595 1.00 17.01 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 29.805 -2.687  24.664 1.00 16.30 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 29.990 -3.427  23.313 1.00 14.64 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 30.856 -3.073  22.515 1.00 15.16 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 31.179 -2.265  25.208 1.00 19.18 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 31.183 -1.131  26.222 1.00 24.56 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.625 -0.673  26.450 1.00 30.69 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 33.180 -0.840  27.541 1.00 32.98 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.281 -0.104  25.429 1.00 29.96 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 29.177 -4.504  23.083 1.00 13.54 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 29.082 -5.178  21.793 1.00 13.78 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.617 -5.379  21.483 1.00 13.12 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.768 -5.480  22.393 1.00 13.66 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 29.814 -6.538  21.756 1.00 15.72 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 29.149 -7.458  22.628 1.00 17.62 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 31.261 -6.420  22.131 1.00 16.92 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.301 -5.418  20.196 1.00 12.52 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 25.918 -5.607  19.779 1.00 12.02 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 25.832 -5.670  18.263 1.00 11.13 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 26.831 -5.922  17.593 1.00 11.74 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.620 -5.536  17.738 1.00 11.57 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.361 -5.657  16.290 1.00 11.41 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.487 -4.462  15.863 1.00 11.95 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.493 -4.169  16.518 1.00 12.32 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.660 -7.004  15.976 1.00 13.40 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.265 -7.089  14.500 1.00 15.00 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.568 -8.176  16.339 1.00 13.96 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 23.851 -3.788  14.738 1.00 10.95 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 23.021 -2.684  14.257 1.00 10.73 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.496 -2.952  12.855 1.00 11.60 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 23.121 -3.678  12.084 1.00 11.26 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.763 -1.307  14.317 1.00 10.63 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.772 -1.032  13.215 1.00 10.56 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 26.040 -1.598  13.253 1.00 11.71 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.493 -0.131  12.187 1.00 11.34 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 26.982 -1.333  12.264 1.00 11.35 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.420 0.119   11.169 1.00 11.68 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.666 -0.478  11.221 1.00 12.79 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.614 -0.236  10.248 1.00 15.00 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.362 -2.302  12.533 1.00 12.03 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.804 -2.422  11.191 1.00 12.31 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.292 -1.234  10.330 1.00 12.44 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.147 -0.055  10.721 1.00 12.76 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.260 -2.456  11.202 1.00 12.88 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.716 -2.575  9.803  1.00 14.38 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 18.965 -3.705  9.037  1.00 14.79 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 18.027 -1.525  9.215  1.00 15.70 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.487 -3.813  7.738  1.00 16.37 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.553 -1.610  7.914  1.00 16.64 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.794 -2.749  7.178  1.00 18.17 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.347 -2.837  5.881  1.00 22.07 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.844 -1.558  9.136  1.00 11.98 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.394 -0.549  8.200  1.00 11.74 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.502 -0.550  6.919  1.00 13.30 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.624 -1.457  6.074  1.00 14.39 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.839 -0.923  7.861  1.00 13.66 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.614 0.129   6.589  1.00 15.11 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.602 0.453   6.797  1.00 13.60 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.707 0.493   5.663  1.00 14.52 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.416 0.653   4.328  1.00 14.30 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.950 0.110   3.313  1.00 15.45 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.636 1.567   5.834  1.00 18.51 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.206 2.862   5.895  1.00 24.84 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.567 1.359   4.300  1.00 13.88 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.308 1.533   3.032  1.00 14.55 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 22.994 0.263   2.509  1.00 14.72 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.589 0.277   1.412  1.00 15.03 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.317 2.666   3.124  1.00 15.99 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.325 2.382   4.081  1.00 15.78 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.930 -0.823  3.299  1.00 13.58 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.430 -2.125  2.889  1.00 12.87 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.335 -3.224  3.006  1.00 14.80 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.630 -4.399  2.712  1.00 15.94 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.645 -2.531  3.751  1.00 13.65 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.893 -1.670  3.518  1.00 15.39 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.572 -1.996  2.181  1.00 15.85 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.754 -1.150  1.939  1.00 16.61 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.706 0.045   1.355  1.00 17.22 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.547 0.538   0.927  1.00 17.46 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.825 0.746   1.165  1.00 18.25 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 21.121 -2.867  3.529  1.00 15.32 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 20.062 -3.839  3.849  1.00 17.27 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.639 -5.025  4.661  1.00 17.42 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.362 -6.202  4.372  1.00 19.06 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.371 -4.361  2.594  1.00 21.24 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 18.573 -3.328  1.896  1.00 26.01 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.551 -4.059  1.033  1.00 29.08 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.882 -3.091  0.190  1.00 30.22 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.130 -2.933  -1.110 1.00 31.45 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 18.020 -3.714  -1.728 1.00 32.41 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.530 -1.967  -1.790 1.00 29.42 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.525 -4.703  5.627  1.00 15.66 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 22.203 -5.766  6.386  1.00 15.67 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.402 -5.364  7.845  1.00 14.84 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.493 -4.178  8.164  1.00 14.25 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.632 -5.969  5.821  1.00 18.68 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.789 -6.960  4.674  1.00 28.17 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 25.279 -7.268  4.499  1.00 35.63 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 25.509 -8.502  3.653  1.00 42.07 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 24.838 -8.411  2.326  1.00 45.29 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.520 -6.363  8.721  1.00 13.98 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 22.902 -6.172  10.116 1.00 13.72 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.399 -6.474  10.264 1.00 14.17 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 24.928 -7.447  9.675  1.00 15.98 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 22.113 -7.110  11.052 1.00 13.14 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.628 -6.897  11.023 1.00 14.02 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 19.967 -6.141  11.993 1.00 17.31 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.702 -7.394  10.167 1.00 14.27 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.682 -6.195  11.680 1.00 16.48 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.479 -6.905  10.575 1.00 18.24 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 25.086 -5.671  11.088 1.00 11.90 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.517 -5.849  11.322 1.00 11.92 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.827 -5.915  12.802 1.00 12.65 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.264 -5.141  13.597 1.00 12.28 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.313 -4.642  10.747 1.00 12.65 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.316 -4.544  9.238  1.00 14.64 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 28.065 -5.427  8.459  1.00 16.83 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.614 -3.543  8.591  1.00 15.15 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 28.082 -5.328  7.058  1.00 16.86 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.636 -3.421  7.205  1.00 15.85 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.379 -4.308  6.436  1.00 16.97 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.397 -4.168  5.054  1.00 18.86 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.716 -6.825  13.207 1.00 12.31 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 28.134 -6.839  14.634 1.00 12.86 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 29.162 -5.702  14.890 1.00 14.52 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 30.027 -5.441  14.026 1.00 16.81 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.809 -8.220  14.797 1.00 13.75 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.324 -8.516  13.415 1.00 13.10 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.414 -7.852  12.400 1.00 12.17 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 29.144 -5.102  16.084 1.00 12.65 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 30.047 -3.988  16.395 1.00 12.77 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.543 -4.042  17.803 1.00 12.89 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 29.855 -4.542  18.700 1.00 13.03 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.352 -2.590  16.182 1.00 14.73 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.307 -2.215  14.685 1.00 16.97 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 27.971 -2.557  16.828 1.00 15.30 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.778 -3.517  18.018 1.00 13.50 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 32.298 -3.206  19.360 1.00 14.42 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 32.199 -1.656  19.439 1.00 13.67 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.642 -1.003  18.499 1.00 14.61 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.768 -3.592  19.482 1.00 18.23 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 33.840 -5.007  19.430 1.00 25.59 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.544 -1.095  20.464 1.00 12.00 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.363 0.349   20.521 1.00 12.70 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.864 0.948   21.828 1.00 14.17 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.890 0.293   22.886 1.00 14.89 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.879 0.730   20.257 1.00 12.81 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.835 -0.024  21.060 1.00 12.07 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.296 -1.228  20.587 1.00 12.31 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.356 0.479   22.256 1.00 13.16 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.330 -1.924  21.331 1.00 12.64 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.400 -0.228  23.002 1.00 12.77 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.901 -1.426  22.537 1.00 13.26 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.240 2.245   21.774 1.00 14.40 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.726 2.916   22.970 1.00 14.91 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.582 3.268   23.951 1.00 15.22 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.410 3.272   23.583 1.00 14.89 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.511 4.161   22.578 1.00 16.27 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.646 5.049   21.881 1.00 18.39 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 31.924 3.514   25.222 1.00 15.26 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 30.936 3.904   26.230 1.00 16.34 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.355 5.280   25.896 1.00 17.58 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 31.042 6.115   25.299 1.00 17.93 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.598 3.916   27.629 1.00 20.77 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 31.867 2.510   28.117 1.00 25.63 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.463 2.536   29.513 1.00 30.70 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.623 1.137   30.043 1.00 36.46 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 33.147 1.145   31.428 1.00 40.23 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 29.103 5.568   26.300 1.00 16.83 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.519 6.876   25.950 1.00 16.57 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.365 8.039   26.432 1.00 17.51 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.758 8.074   27.605 1.00 18.94 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 27.144 6.883   26.645 1.00 18.12 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 26.905 5.494   27.141 1.00 20.08 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 28.168 4.700   27.055 1.00 17.16 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.663 8.985   25.517 1.00 17.12 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 30.535 10.094  25.896 1.00 18.39 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 30.245 11.361  25.086 1.00 17.24 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 29.357 11.358  24.213 1.00 17.27 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 31.993 9.647   25.774 1.00 22.94 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 32.375 9.628   24.422 1.00 28.06 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 30.970 12.471  25.414 1.00 16.93 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 30.786 13.784  24.759 1.00 18.71 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 31.788 13.812  23.613 1.00 19.21 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 33.015 13.828  23.879 1.00 20.05 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 31.238 14.891  25.733 1.00 20.88 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 30.285 15.879  26.318 1.00 25.93 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 31.059 17.044  26.966 1.00 27.77 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 29.270 16.411  25.305 1.00 25.67 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 31.296 13.857  22.365 1.00 19.13 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 32.131 13.771  21.161 1.00 20.29 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 31.884 14.935  20.235 1.00 21.21 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 30.730 15.306  20.015 1.00 21.03 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 31.810 12.414  20.461 1.00 21.30 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 32.226 11.259  21.376 1.00 23.39 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 32.463 12.299  19.084 1.00 22.51 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 31.962 9.872   20.858 1.00 25.84 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 32.965 15.534  19.682 1.00 21.37 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 32.802 16.650  18.765 1.00 22.28 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 32.169 16.201  17.442 1.00 23.32 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 32.621 15.228  16.846 1.00 23.53 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 34.163 17.322  18.484 1.00 23.32 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 34.019 18.544  17.619 1.00 26.13 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 34.432 18.529  16.297 1.00 27.97 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 33.415 19.684  18.106 1.00 28.51 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 34.301 19.659  15.498 1.00 29.64 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 33.277 20.812  17.306 1.00 30.24 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 33.743 20.796  16.013 1.00 30.04 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 31.104 16.913  16.991 1.00 23.43 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 30.443 16.600  15.732 1.00 23.51 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 30.478 17.860  14.867 1.00 24.80 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 29.987 18.939  15.279 1.00 24.93 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 28.976 16.115  15.972 1.00 23.96 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 28.284 15.788  14.652 1.00 25.14 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 28.968 14.885  16.893 1.00 23.53 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 31.019 17.715  13.656 1.00 25.43 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 31.172 18.798  12.684 1.00 26.76 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 29.823 19.391  12.314 1.00 26.96 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 28.811 18.689  12.393 1.00 27.02 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 31.794 18.215  11.398 1.00 31.66 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 32.460 19.258  10.532 1.00 43.48 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 33.690 19.798  11.217 1.00 55.89 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 33.905 21.029  11.191 1.00 59.36 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 34.435 18.986  11.803 1.00 60.59 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 29.796 20.671  11.867 1.00 26.88 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 28.543 21.288  11.433 1.00 26.97 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 27.921 20.519  10.276 1.00 26.81 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 28.638 19.946  9.449  1.00 26.96 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 28.786 22.717  10.990 1.00 27.56 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 26.586 20.472  10.256 1.00 26.26 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 25.804 19.870  9.186  1.00 25.72 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 24.671 20.860  8.863  1.00 27.22 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 24.585 21.925  9.484  1.00 28.61 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 25.201 18.545  9.665  1.00 26.10 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 24.225 18.797  10.665 1.00 26.13 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 23.796 20.505  7.919  1.00 27.24 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 22.625 21.341  7.612  1.00 28.82 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 21.651 21.393  8.831  1.00 27.98 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 20.813 22.293  8.920  1.00 28.62 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 21.942 20.767  6.341  1.00 34.78 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 20.418 20.717  6.300  1.00 45.16 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 19.750 21.898  5.621  1.00 54.96 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 18.979 22.616  6.301  1.00 56.56 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 20.000 22.106  4.410  1.00 58.57 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 21.756 20.414  9.762  1.00 26.49 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 20.830 20.343  10.882 1.00 26.16 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 21.322 20.985  12.158 1.00 25.75 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 20.499 21.334  12.986 1.00 26.55 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 20.480 18.879  11.177 1.00 25.81 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 20.009 18.092  9.975  1.00 26.09 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 20.901 17.364  9.205  1.00 26.97 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 18.670 18.072  9.610  1.00 26.34 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 20.468 16.599  8.128  1.00 28.11 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 18.228 17.331  8.515  1.00 27.05 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 19.129 16.594  7.777  1.00 28.71 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 18.693 15.847  6.700  1.00 31.00 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 22.649 21.064  12.366 1.00 24.64 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 23.191 21.601  13.607 1.00 23.66 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 24.472 22.370  13.365 1.00 25.71 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 25.258 21.989  12.489 1.00 25.69 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 23.596 20.426  14.544 1.00 22.14 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 22.487 19.521  15.043 1.00 20.97 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 21.604 19.944  16.020 1.00 20.71 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 22.355 18.231  14.568 1.00 20.83 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 20.618 19.097  16.523 1.00 19.83 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 21.370 17.368  15.063 1.00 19.55 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 20.505 17.802  16.047 1.00 19.08 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 19.497 16.990  16.533 1.00 16.92 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 24.787 23.337  14.242 1.00 27.39 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 26.123 23.945  14.178 1.00 28.14 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 27.146 22.936  14.690 1.00 27.92 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 26.790 21.923  15.326 1.00 28.61 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 26.016 25.107  15.183 1.00 29.82 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 25.020 24.596  16.211 1.00 30.96 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 23.999 23.850  15.388 1.00 28.73 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 28.456 23.233  14.506 1.00 27.49 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 29.517 22.404  15.071 1.00 28.25 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 29.332 22.416  16.613 1.00 27.25 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 29.009 23.475  17.182 1.00 27.57 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 30.870 22.991  14.700 1.00 29.45 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 29.353 21.226  17.247 1.00 25.66 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 29.064 21.164  18.680 1.00 24.36 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 29.534 19.843  19.290 1.00 23.49 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 29.922 18.950  18.557 1.00 24.40 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 27.524 21.320  18.848 1.00 24.23 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 26.766 19.998  18.484 1.00 24.93 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 25.338 20.172  18.031 1.00 23.46 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 24.458 19.030  18.401 1.00 21.79 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 24.426 17.865  17.763 1.00 22.02 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 23.558 16.928  18.125 1.00 21.37 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 25.285 17.614  16.779 1.00 22.11 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 29.436 19.692  20.611 1.00 22.82 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 29.697 18.400  21.239 1.00 23.33 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 28.359 17.704  21.415 1.00 21.82 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 27.411 18.294  21.956 1.00 22.07 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 30.383 18.547  22.589 1.00 24.40 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 31.814 19.007  22.440 1.00 25.69 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 32.850 18.092  22.344 1.00 26.47 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 32.118 20.357  22.322 1.00 27.52 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 34.168 18.515  22.175 1.00 29.15 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 33.421 20.789  22.117 1.00 29.22 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 34.442 19.866  22.044 1.00 30.62 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? 35.734 20.350  21.885 1.00 34.56 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 28.269 16.462  20.942 1.00 19.66 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 27.064 15.656  21.105 1.00 18.16 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 27.335 14.719  22.278 1.00 16.81 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 28.384 14.045  22.326 1.00 17.97 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 26.709 14.889  19.821 1.00 17.12 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 25.470 13.946  20.014 1.00 16.46 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 24.830 13.489  18.722 1.00 18.05 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 24.741 14.233  17.745 1.00 18.99 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 24.338 12.221  18.679 1.00 14.55 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 26.429 14.708  23.247 1.00 15.61 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 26.585 13.886  24.439 1.00 15.80 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 25.929 12.506  24.276 1.00 16.66 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 25.084 12.324  23.379 1.00 16.42 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 25.975 14.620  25.633 1.00 18.33 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 24.584 14.848  25.442 1.00 19.18 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 26.303 11.550  25.150 1.00 15.30 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 25.698 10.207  25.178 1.00 15.37 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 25.857 9.482   23.838 1.00 15.00 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 24.995 8.670   23.470 1.00 14.68 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 24.211 10.295  25.610 1.00 16.39 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 24.030 10.880  26.988 1.00 18.35 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 23.983 10.069  28.118 1.00 21.60 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 23.951 12.175  27.379 1.00 19.04 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 23.834 10.901  29.153 1.00 22.00 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 23.823 12.171  28.756 1.00 21.33 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 26.998 9.726   23.154 1.00 14.91 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 27.241 9.121   21.833 1.00 14.76 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 28.276 7.993   21.955 1.00 13.98 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 29.248 8.125   22.712 1.00 14.07 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 27.826 10.223  20.903 1.00 15.17 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 27.998 9.844   19.413 1.00 17.47 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 26.627 9.502   18.768 1.00 18.12 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 28.596 11.062  18.653 1.00 19.34 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 28.057 6.900   21.234 1.00 13.78 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 28.940 5.725   21.260 1.00 13.81 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 29.439 5.483   19.859 1.00 14.17 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 28.626 5.452   18.936 1.00 14.31 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 28.140 4.504   21.737 1.00 13.77 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 27.562 4.697   23.139 1.00 15.63 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 26.453 3.368   23.668 1.00 18.38 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 25.156 3.542   22.511 1.00 18.89 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 30.757 5.329   19.665 1.00 13.76 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 31.293 5.117   18.315 1.00 14.51 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 31.717 3.685   18.074 1.00 13.93 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 32.212 3.026   19.006 1.00 13.73 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 32.525 6.025   18.041 1.00 16.03 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 32.258 7.527   18.141 1.00 20.27 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 33.514 8.319   17.748 1.00 22.06 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 31.090 7.963   17.262 1.00 20.85 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 31.663 3.273   16.812 1.00 13.11 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 32.123 1.934   16.404 1.00 12.85 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 32.638 1.986   14.972 1.00 12.52 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 32.324 2.916   14.238 1.00 14.07 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 30.955 0.935   16.451 1.00 13.89 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 33.466 0.996   14.582 1.00 11.84 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 33.894 0.890   13.208 1.00 12.54 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 32.793 0.141   12.451 1.00 13.56 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 32.424 -0.988  12.816 1.00 15.76 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? 35.230 0.150   13.125 1.00 13.42 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? 35.647 -0.056  11.671 1.00 14.83 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? 36.271 0.957   13.883 1.00 14.21 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 32.277 0.784   11.416 1.00 15.13 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 31.197 0.214   10.629 1.00 15.74 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 30.749 1.187   9.559  1.00 15.69 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 31.050 2.388   9.615  1.00 16.76 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 30.080 0.669   8.533  1.00 15.36 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 29.590 1.511   7.462  1.00 14.33 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 28.327 2.284   7.850  1.00 14.55 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 27.419 1.732   8.485  1.00 14.12 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 29.305 0.694   6.196  1.00 15.02 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 28.732 1.532   5.089  1.00 15.40 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 29.511 2.449   4.411  1.00 17.45 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 27.456 1.610   4.631  1.00 16.79 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 28.694 3.027   3.533  1.00 19.20 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 27.438 2.551   3.646  1.00 17.81 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 28.231 3.542   7.405  1.00 15.16 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 27.017 4.328   7.571  1.00 15.23 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 27.022 5.501   6.608  1.00 17.25 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 28.097 5.972   6.198  1.00 19.18 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 26.849 4.815   9.002  1.00 16.54 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 27.825 5.797   9.304  1.00 20.22 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 25.833 5.878   6.184  1.00 14.98 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 25.517 7.032   5.345  1.00 15.35 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 24.400 7.817   6.091  1.00 16.68 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 23.735 7.277   6.995  1.00 16.23 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 25.031 6.540   3.949  1.00 18.19 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 26.152 5.864   3.176  1.00 21.84 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 25.766 5.220   1.850  1.00 25.77 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 24.990 5.839   1.081  1.00 26.82 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 26.244 4.091   1.584  1.00 23.35 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 24.178 9.113   5.780  1.00 17.58 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 23.209 9.903   6.576  1.00 17.38 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 21.797 9.315   6.703  1.00 17.53 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 21.196 9.377   7.783  1.00 18.42 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 23.212 11.274  5.890  1.00 19.24 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 24.604 11.370  5.282  1.00 19.49 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 24.881 9.943   4.782  1.00 17.79 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 21.293 8.694   5.640  1.00 15.93 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 19.956 8.080   5.682  1.00 15.41 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 19.883 6.838   6.565  1.00 15.23 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 18.798 6.284   6.774  1.00 15.59 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 21.039 6.340   7.056  1.00 14.41 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 21.054 5.220   8.003  1.00 13.37 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 20.618 5.638   9.432  1.00 13.16 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 20.322 4.772   10.281 1.00 12.58 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 22.454 4.567   8.084  1.00 14.49 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 22.762 3.776   6.838  1.00 15.41 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 21.833 3.173   6.288  1.00 15.45 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 23.958 3.785   6.390  1.00 16.08 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 20.511 6.946   9.704  1.00 12.88 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 20.069 7.431   11.035 1.00 12.47 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 18.732 6.800   11.396 1.00 13.12 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.855 6.703   10.528 1.00 15.59 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 19.970 8.954   11.049 1.00 14.07 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 21.594 9.769   11.166 1.00 16.14 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 18.611 6.349   12.628 1.00 12.00 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.378 5.701   13.079 1.00 12.45 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.480 4.183   13.128 1.00 13.05 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 16.643 3.522   13.725 1.00 13.63 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 18.495 3.612   12.473 1.00 11.93 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 18.727 2.162   12.518 1.00 11.64 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 19.034 1.760   13.957 1.00 11.36 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 19.783 2.457   14.649 1.00 12.14 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 18.436 0.652   14.420 1.00 10.91 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 18.604 0.246   15.814 1.00 11.61 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 19.882 -0.554  16.070 1.00 11.41 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 20.232 -1.444  15.273 1.00 12.22 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.339 -0.516  16.283 1.00 13.23 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 16.195 0.506   16.553 1.00 13.99 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.590 -1.428  17.504 1.00 14.85 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 14.814 -0.197  16.881 1.00 15.74 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 20.530 -0.272  17.221 1.00 10.75 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 21.657 -1.054  17.778 1.00 10.77 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 21.049 -1.854  18.954 1.00 11.82 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 20.374 -1.255  19.812 1.00 12.71 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 22.743 -0.107  18.315 1.00 11.85 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 23.864 -0.789  19.130 1.00 13.78 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 24.700 -1.739  18.248 1.00 14.35 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 24.792 0.276   19.740 1.00 15.20 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 21.196 -3.199  18.917 1.00 11.80 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 20.660 -4.060  19.968 1.00 13.42 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 21.759 -4.955  20.519 1.00 13.50 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 22.645 -5.416  19.778 1.00 13.99 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 19.650 -5.070  19.365 1.00 17.13 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 18.570 -4.510  18.522 1.00 25.03 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.712 -5.673  18.034 1.00 27.41 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 16.993 -6.207  19.191 1.00 30.31 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 15.834 -5.719  19.608 1.00 28.36 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 15.212 -4.801  18.901 1.00 21.84 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 15.278 -6.171  20.727 1.00 24.27 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 21.619 -5.301  21.786 1.00 13.97 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 22.420 -6.370  22.393 1.00 13.42 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 21.453 -7.480  22.828 1.00 14.20 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 20.253 -7.418  22.544 1.00 15.76 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 23.177 -5.810  23.585 1.00 15.51 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 22.068 -5.280  24.916 1.00 14.94 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 21.959 -8.512  23.517 1.00 15.50 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 21.082 -9.599  23.971 1.00 16.77 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 19.981 -9.154  24.951 1.00 18.20 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 19.037 -9.915  25.179 1.00 19.17 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 21.912 -10.733 24.619 1.00 19.05 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 22.526 -10.312 25.959 1.00 24.45 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 23.547 -11.314 26.460 1.00 36.31 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 24.773 -11.135 26.331 1.00 40.32 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 23.057 -12.383 27.047 1.00 36.20 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 20.083 -7.948  25.519 1.00 16.20 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 19.122 -7.439  26.526 1.00 15.75 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 18.030 -6.561  25.981 1.00 15.89 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.050 -6.299  26.717 1.00 16.48 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 19.840 -6.689  27.691 1.00 16.23 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 20.929 -7.504  28.335 1.00 19.71 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 22.261 -7.213  28.119 1.00 22.02 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 20.847 -8.607  29.137 1.00 21.17 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 22.963 -8.141  28.769 1.00 22.65 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 22.157 -9.016  29.389 1.00 21.99 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 18.208 -6.087  24.733 1.00 14.69 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.220 -5.218  24.125 1.00 14.79 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 17.859 -4.092  23.331 1.00 13.21 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 19.027 -4.162  22.941 1.00 13.75 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.062 -3.058  23.084 1.00 12.85 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.538 -1.894  22.331 1.00 12.93 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 18.534 -1.069  23.140 1.00 12.65 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 18.215 -0.642  24.275 1.00 12.85 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 16.340 -1.013  21.880 1.00 13.46 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 16.835 0.286   21.218 1.00 13.64 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 15.420 -1.819  20.942 1.00 14.23 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 19.666 -0.744  22.523 1.00 11.94 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 20.704 0.069   23.131 1.00 12.67 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 20.630 1.546   22.675 1.00 13.17 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 20.844 2.474   23.453 1.00 13.29 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 22.081 -0.527  22.777 1.00 13.80 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 23.234 0.369   23.264 1.00 14.98 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 22.242 -1.945  23.338 1.00 13.65 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 20.399 1.750   21.378 1.00 11.86 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 20.378 3.109   20.828 1.00 12.26 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 20.106 3.132   19.338 1.00 11.88 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 19.736 2.104   18.767 1.00 11.83 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 20.203 4.320   18.714 1.00 12.07 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 19.931 4.436   17.273 1.00 11.85 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 21.094 5.122   16.561 1.00 11.41 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 21.729 6.002   17.138 1.00 11.78 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 18.619 5.221   16.985 1.00 12.55 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 18.577 6.546   17.750 1.00 13.78 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.394 4.341   17.300 1.00 14.82 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.287 7.442   17.285 1.00 15.00 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 21.329 4.798   15.279 1.00 10.61 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 22.378 5.500   14.487 1.00 10.36 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 22.104 7.002   14.472 1.00 11.15 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 20.950 7.393   14.287 1.00 11.73 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 22.386 4.960   13.033 1.00 11.67 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 23.378 5.768   12.151 1.00 13.39 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 22.754 3.462   12.996 1.00 12.77 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 23.129 7.802   14.705 1.00 11.47 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 22.971 9.270   14.754 1.00 12.26 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 24.117 10.001  14.008 1.00 14.67 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 23.919 11.116  13.550 1.00 15.78 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 22.928 9.714   16.215 1.00 12.73 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 22.860 11.132  16.397 1.00 14.43 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 25.322 9.402   13.948 1.00 13.57 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 26.463 10.081  13.252 1.00 14.49 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 27.222 9.023   12.433 1.00 14.49 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 26.977 7.824   12.581 1.00 14.34 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 27.437 10.777  14.282 1.00 17.10 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 28.234 9.792   14.949 1.00 18.07 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 26.726 11.693  15.283 1.00 17.74 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 28.118 9.456   11.555 1.00 15.76 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 28.949 8.517   10.824 1.00 16.69 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 29.908 9.211   9.886  1.00 17.56 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 29.819 10.422  9.685  1.00 18.26 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 30.776 8.401   9.299  1.00 19.17 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 31.682 8.862   8.258  1.00 20.15 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 32.994 8.140   8.322  1.00 20.72 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 33.403 7.703   9.401  1.00 20.90 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 33.641 7.966   7.170  1.00 20.68 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 34.973 7.369   7.082  1.00 22.08 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 35.127 6.047   7.794  1.00 21.42 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? 36.197 5.753   8.339  1.00 22.19 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? 36.002 8.381   7.565  1.00 25.76 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? 35.970 9.612   6.695  1.00 32.94 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? 36.041 9.498   5.467  1.00 35.19 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? 35.808 10.794  7.301  1.00 34.29 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 34.123 5.205   7.686  1.00 19.19 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 34.179 3.875   8.252  1.00 17.84 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 33.850 3.829   9.725  1.00 16.80 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 34.018 2.778   10.340 1.00 17.55 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 33.307 4.938   10.282 1.00 16.06 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 32.819 4.968   11.661 1.00 15.37 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 31.273 5.102   11.645 1.00 15.98 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 30.683 5.623   10.686 1.00 18.50 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 33.368 6.185   12.407 1.00 16.46 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 34.845 6.134   12.762 1.00 20.56 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? 35.266 7.465   13.304 1.00 23.94 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? 35.136 5.016   13.828 1.00 20.87 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 30.645 4.667   12.723 1.00 12.76 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 29.207 4.836   12.892 1.00 12.55 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 29.010 5.230   14.372 1.00 12.99 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 29.646 4.641   15.235 1.00 13.29 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 28.378 3.611   12.475 1.00 13.58 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 28.868 2.328   13.151 1.00 14.65 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 26.886 3.858   12.747 1.00 14.40 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 28.163 6.233   14.626 1.00 12.39 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 27.912 6.703   15.991 1.00 12.76 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 26.466 6.486   16.372 1.00 12.84 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 25.583 6.701   15.542 1.00 13.04 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 26.213 6.004   17.588 1.00 11.52 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 24.850 5.676   18.067 1.00 11.66 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 24.506 6.546   19.280 1.00 12.05 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 25.295 6.669   20.224 1.00 11.69 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 24.773 4.193   18.515 1.00 11.52 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 25.290 3.200   17.492 1.00 11.39 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 24.459 2.732   16.480 1.00 11.88 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 26.612 2.758   17.531 1.00 13.07 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 24.931 1.835   15.533 1.00 11.98 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 27.089 1.843   16.587 1.00 13.76 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 26.243 1.375   15.596 1.00 12.81 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 23.285 7.103   19.266 1.00 11.60 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 22.763 7.849   20.394 1.00 11.57 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 22.261 6.796   21.418 1.00 11.20 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 21.340 6.021   21.105 1.00 12.12 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 21.604 8.737   19.950 1.00 12.78 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 22.829 6.788   22.636 1.00 11.73 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 22.419 5.836   23.674 1.00 12.95 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 21.051 6.200   24.228 1.00 12.33 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 20.746 7.397   24.386 1.00 12.46 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 23.427 5.878   24.842 1.00 15.29 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 23.188 4.843   25.926 1.00 20.38 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 22.896 3.690   25.587 1.00 18.74 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 23.174 5.226   27.121 1.00 25.93 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 20.225 5.168   24.557 1.00 11.17 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 18.942 5.426   25.226 1.00 12.18 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 18.828 4.651   26.560 1.00 13.14 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.792 4.754   27.219 1.00 14.34 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.702 5.103   24.353 1.00 13.58 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.660 5.975   23.082 1.00 13.75 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.654 3.616   23.993 1.00 13.82 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 19.873 3.901   26.969 1.00 13.69 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 19.789 3.024   28.152 1.00 14.13 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 19.654 3.727   29.459 1.00 16.79 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 19.149 3.133   30.422 1.00 18.17 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 21.008 2.053   28.216 1.00 14.17 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 21.039 1.071   27.048 1.00 14.33 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 22.302 0.237   27.103 1.00 16.12 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 23.458 1.056   26.780 1.00 14.80 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 24.702 0.583   26.690 1.00 16.97 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 24.955 -0.713  26.950 1.00 15.77 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 25.697 1.386   26.311 1.00 17.57 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 20.079 5.006   29.515 1.00 15.76 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 19.950 5.767   30.764 1.00 16.66 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 18.554 6.407   30.928 1.00 17.71 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 18.250 6.925   32.024 1.00 19.14 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 21.014 6.874   30.830 1.00 18.03 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 20.860 7.917   29.742 1.00 22.64 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 20.678 7.525   28.556 1.00 21.89 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 20.931 9.133   30.068 1.00 24.54 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.710 6.361   29.888 1.00 15.60 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 16.370 6.987   29.944 1.00 15.01 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 15.384 6.026   30.586 1.00 15.92 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 14.603 5.334   29.900 1.00 16.19 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 15.919 7.400   28.527 1.00 15.06 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 16.900 8.373   27.780 1.00 16.62 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 16.457 8.580   26.324 1.00 16.56 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.025 9.686   28.492 1.00 17.69 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 15.452 5.924   31.942 1.00 16.26 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 14.663 4.903   32.631 1.00 17.75 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 13.169 5.114   32.526 1.00 18.42 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 12.393 4.140   32.580 1.00 20.07 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 15.079 4.832   34.108 1.00 19.29 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 16.581 4.739   34.377 1.00 21.68 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 16.832 4.527   35.894 1.00 22.48 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.253 3.602   33.545 1.00 22.38 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 12.748 6.393   32.373 1.00 17.74 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 11.333 6.716   32.281 1.00 18.67 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 10.664 6.137   31.019 1.00 19.31 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 9.428  6.095   30.964 1.00 21.07 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 11.143 8.241   32.372 1.00 18.44 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 11.960 9.042   31.387 1.00 18.53 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 13.204 9.574   31.575 1.00 18.67 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 11.580 9.370   30.047 1.00 18.12 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 13.604 10.254  30.441 1.00 18.69 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 12.616 10.155  29.493 1.00 18.01 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 10.426 9.139   29.286 1.00 18.38 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 12.556 10.652  28.191 1.00 18.08 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 10.361 9.654   28.006 1.00 18.93 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 11.403 10.431  27.488 1.00 18.36 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 11.449 5.669   30.008 1.00 18.46 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 10.830 5.098   28.806 1.00 18.89 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 10.010 3.843   29.128 1.00 23.34 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 9.093  3.518   28.371 1.00 23.32 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 11.909 4.733   27.758 1.00 17.54 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 12.518 5.901   26.993 1.00 17.48 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 13.649 5.394   26.087 1.00 17.65 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 11.458 6.607   26.106 1.00 17.48 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 10.362 3.133   30.234 1.00 27.53 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 9.732  1.878   30.685 1.00 32.63 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 8.502  2.053   31.538 1.00 37.59 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 7.957  1.038   31.973 1.00 38.67 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 10.702 1.067   31.565 1.00 35.97 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 11.928 0.554   30.887 1.00 43.36 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 11.876 0.321   29.665 1.00 44.71 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 12.949 0.361   31.582 1.00 47.10 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 8.094  3.286   31.848 1.00 40.14 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 6.898  3.498   32.668 1.00 43.25 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 5.987  4.536   32.031 1.00 45.51 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 4.823  4.658   32.426 1.00 47.06 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 7.273  3.897   34.108 1.00 46.09 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 8.041  5.204   34.194 1.00 52.59 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 9.181  5.185   35.193 1.00 60.82 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 9.321  6.168   35.956 1.00 62.88 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 9.937  4.185   35.211 1.00 63.02 ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 19.595 -24.796 24.041 1.00 21.41 ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 20.755 -24.695 23.133 1.00 22.25 ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 20.765 -25.854 22.116 1.00 21.34 ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 20.113 -26.891 22.313 1.00 22.50 ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 22.064 -24.682 23.930 1.00 24.77 ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 22.225 -25.911 24.626 1.00 27.69 ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 21.507 -25.663 21.036 1.00 19.28 ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 21.644 -26.680 20.006 1.00 18.03 ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 21.887 -26.089 18.636 1.00 16.60 ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 21.523 -24.932 18.372 1.00 16.86 ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 22.503 -26.863 17.770 1.00 15.27 ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 22.826 -26.409 16.409 1.00 15.11 ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 22.765 -27.591 15.426 1.00 14.57 ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 22.807 -28.771 15.840 1.00 15.97 ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 24.246 -25.814 16.388 1.00 15.80 ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 22.694 -27.266 14.130 1.00 14.53 ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 22.800 -28.224 13.036 1.00 13.99 ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 24.162 -28.022 12.386 1.00 15.36 ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 24.569 -26.903 12.119 1.00 14.80 ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 21.712 -27.974 11.981 1.00 13.97 ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 20.329 -28.018 12.634 1.00 14.80 ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 21.814 -29.005 10.821 1.00 14.95 ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 19.255 -27.402 11.671 1.00 16.06 ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 24.899 -29.120 12.163 1.00 16.23 ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 26.212 -29.057 11.545 1.00 16.23 ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 26.160 -29.775 10.195 1.00 17.52 ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 26.035 -31.001 10.170 1.00 19.39 ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 27.248 -29.718 12.487 1.00 16.32 ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 27.441 -28.909 13.762 1.00 15.68 ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 28.297 -27.810 13.796 1.00 16.27 ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 26.716 -29.198 14.910 1.00 17.19 ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 28.437 -27.036 14.952 1.00 18.87 ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 26.853 -28.430 16.072 1.00 18.65 ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 27.708 -27.349 16.085 1.00 20.16 ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 27.822 -26.579 17.226 1.00 23.01 ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 26.262 -29.046 9.081  1.00 17.52 ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 26.160 -29.652 7.751  1.00 19.31 ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 27.235 -29.050 6.873  1.00 20.84 ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 27.332 -27.839 6.770  1.00 20.11 ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 24.705 -29.474 7.173  1.00 21.75 ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 24.221 -28.024 7.274  1.00 22.53 ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 24.594 -30.008 5.741  1.00 22.82 ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 28.116 -29.878 6.293  1.00 21.10 ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 29.196 -29.369 5.449  1.00 21.74 ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 30.093 -28.441 6.245  1.00 22.37 ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 30.410 -28.751 7.402  1.00 24.09 ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 30.387 -27.248 5.720  1.00 21.63 ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 31.167 -26.278 6.495  1.00 21.79 ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 30.275 -25.189 7.102  1.00 19.98 ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 30.706 -24.039 7.240  1.00 20.31 ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 32.312 -25.679 5.692  1.00 25.43 ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 33.389 -26.698 5.418  1.00 34.41 ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 34.010 -27.265 6.339  1.00 36.85 ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 33.607 -26.970 4.148  1.00 36.72 ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 29.048 -25.569 7.479  1.00 18.41 ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 28.101 -24.629 8.060  1.00 17.46 ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 27.607 -25.092 9.440  1.00 15.98 ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 27.438 -26.301 9.695  1.00 15.92 ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 26.848 -24.495 7.161  1.00 18.32 ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 27.122 -23.948 5.778  1.00 20.26 ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 27.816 -22.758 5.607  1.00 22.46 ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 26.714 -24.639 4.640  1.00 22.11 ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 28.076 -22.250 4.338  1.00 23.99 ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 26.971 -24.139 3.360  1.00 23.69 ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 27.654 -22.945 3.219  1.00 25.67 ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 27.907 -22.410 1.970  1.00 27.77 ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 27.323 -24.093 10.308 1.00 14.05 ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 26.703 -24.284 11.629 1.00 13.83 ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 25.412 -23.447 11.637 1.00 13.35 ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 25.483 -22.243 11.367 1.00 14.34 ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 27.638 -23.841 12.761 1.00 15.17 ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 26.983 -23.611 14.135 1.00 16.61 ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 28.012 -23.300 15.248 1.00 17.26 ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 27.571 -22.287 16.213 1.00 18.13 ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 27.112 -22.549 17.435 1.00 19.87 ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 26.949 -23.813 17.838 1.00 19.70 ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 26.774 -21.553 18.251 1.00 18.56 ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 24.231 -24.090 11.875 1.00 13.74 ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 22.942 -23.397 11.886 1.00 13.26 ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 22.487 -23.284 13.338 1.00 13.13 ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 22.351 -24.317 14.011 1.00 13.93 ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 21.855 -24.161 11.073 1.00 14.58 ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 20.582 -23.307 10.928 1.00 14.04 ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 22.381 -24.599 9.718  1.00 14.84 ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 22.267 -22.045 13.818 1.00 12.87 ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 21.833 -21.851 15.204 1.00 12.46 ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 20.607 -20.894 15.246 1.00 12.40 ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 20.351 -20.143 14.287 1.00 12.85 ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 22.977 -21.246 16.080 1.00 15.76 ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 24.085 -22.255 16.276 1.00 19.63 ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 23.506 -19.946 15.470 1.00 15.19 ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 19.904 -20.838 16.402 1.00 11.06 ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 18.880 -19.778 16.597 1.00 10.88 ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 19.648 -18.427 16.564 1.00 11.87 ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 20.692 -18.271 17.259 1.00 12.69 ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 18.238 -19.892 17.956 1.00 12.24 ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.389 -21.132 18.099 1.00 13.34 ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 17.853 -22.188 18.569 1.00 13.91 ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 16.115 -21.037 17.681 1.00 12.97 ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 19.160 -17.477 15.761 1.00 12.89 ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 19.873 -16.181 15.662 1.00 12.46 ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 20.013 -15.519 17.048 1.00 13.11 ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 21.074 -14.950 17.339 1.00 13.95 ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 19.126 -15.254 14.696 1.00 12.82 ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 19.900 -13.966 14.332 1.00 13.89 ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 18.959 -13.078 13.524 1.00 15.02 ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 19.568 -11.836 12.984 1.00 15.15 ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 19.628 -10.686 13.653 1.00 16.63 ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 19.288 -10.638 14.936 1.00 15.28 ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 20.134 -9.594  13.071 1.00 15.76 ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 18.973 -15.653 17.912 1.00 13.03 ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 19.055 -15.000 19.234 1.00 13.02 ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 20.067 -15.639 20.201 1.00 14.16 ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 20.393 -15.032 21.227 1.00 15.61 ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.663 -14.862 19.886 1.00 13.09 ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 17.050 -16.132 20.419 1.00 13.54 ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 16.375 -17.022 19.588 1.00 13.50 ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 17.003 -16.590 21.697 1.00 15.03 ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 15.936 -18.002 20.383 1.00 13.96 ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 16.291 -17.792 21.662 1.00 15.01 ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 20.570 -16.826 19.873 1.00 13.82 ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 21.594 -17.491 20.699 1.00 14.45 ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 22.988 -17.479 20.023 1.00 15.67 ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 23.925 -18.122 20.536 1.00 16.55 ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 21.142 -18.963 20.973 1.00 14.49 ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 19.795 -19.077 21.756 1.00 16.28 ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 19.419 -20.554 22.003 1.00 17.70 ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 19.853 -18.285 23.129 1.00 16.99 ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 23.131 -16.797 18.852 1.00 14.25 ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 24.430 -16.800 18.150 1.00 14.92 ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 25.507 -16.166 19.011 1.00 16.07 ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 25.245 -15.182 19.686 1.00 16.56 ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 24.320 -16.035 16.829 1.00 14.49 ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 26.718 -16.727 18.966 1.00 16.17 ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 27.826 -16.200 19.763 1.00 16.90 ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 28.632 -15.115 19.006 1.00 17.31 ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 28.415 -14.902 17.812 1.00 16.71 ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 28.761 -17.373 20.097 1.00 18.39 ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 29.350 -17.834 18.874 1.00 19.39 ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 28.054 -18.502 20.821 1.00 18.42 ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 29.640 -14.488 19.671 1.00 17.11 ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 30.530 -13.546 18.975 1.00 17.75 ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 31.233 -14.251 17.797 1.00 17.54 ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 31.363 -13.673 16.713 1.00 18.43 ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 31.618 -13.038 19.962 1.00 20.97 ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 31.086 -12.175 21.062 1.00 29.07 ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 30.195 -11.124 20.814 1.00 32.77 ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 31.369 -12.196 22.386 1.00 32.11 ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 29.980 -10.547 21.988 1.00 33.38 ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 30.664 -11.154 22.963 1.00 33.12 ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 31.634 -15.515 17.995 1.00 16.88 ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 32.328 -16.256 16.924 1.00 16.71 ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 31.402 -16.520 15.753 1.00 16.64 ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 31.847 -16.462 14.607 1.00 17.36 ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 32.920 -17.569 17.426 1.00 19.50 ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 33.744 -18.299 16.387 1.00 24.97 ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? 34.856 -17.881 16.044 1.00 26.53 ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 33.215 -19.387 15.856 1.00 26.60 ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 30.105 -16.827 16.019 1.00 16.31 ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 29.160 -17.011 14.906 1.00 16.31 ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 29.059 -15.710 14.067 1.00 16.55 ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 29.086 -15.757 12.841 1.00 17.44 ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 27.765 -17.339 15.457 1.00 15.98 ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 27.613 -18.748 15.989 1.00 17.34 ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 28.190 -19.677 15.373 1.00 17.87 ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 26.913 -18.916 17.042 1.00 16.49 ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 28.938 -14.550 14.735 1.00 16.84 ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 28.824 -13.286 13.995 1.00 17.46 ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 30.140 -12.926 13.261 1.00 18.79 ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 30.089 -12.326 12.185 1.00 19.74 ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 28.386 -12.162 14.940 1.00 16.72 ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 26.900 -12.116 15.158 1.00 15.25 ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 26.202 -12.569 16.241 1.00 16.78 ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 25.932 -11.534 14.264 1.00 14.48 ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 24.850 -12.347 16.060 1.00 17.00 ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 24.661 -11.691 14.862 1.00 15.79 ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 26.019 -10.928 13.005 1.00 15.40 ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 23.492 -11.202 14.272 1.00 15.55 ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 24.850 -10.458 12.414 1.00 15.70 ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 23.610 -10.630 13.031 1.00 15.24 ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 31.283 -13.333 13.800 1.00 17.59 ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 32.570 -13.034 13.138 1.00 18.47 ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 32.794 -13.927 11.895 1.00 19.26 ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 33.701 -13.660 11.080 1.00 19.81 ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 33.724 -13.240 14.117 1.00 17.47 ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 32.068 -15.071 11.815 1.00 18.48 ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 32.197 -15.996 10.691 1.00 18.24 ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 30.820 -16.138 10.008 1.00 18.07 ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 30.447 -17.216 9.577  1.00 17.41 ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 32.671 -17.359 11.208 1.00 19.95 ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 34.094 -17.289 11.725 1.00 24.03 ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? 35.050 -17.298 10.944 1.00 25.62 ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 34.260 -17.188 13.044 1.00 22.51 ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 30.097 -15.042 9.911  1.00 18.21 ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 28.738 -15.011 9.376  1.00 18.29 ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 28.650 -15.396 7.899  1.00 19.22 ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 29.396 -14.873 7.074  1.00 21.41 ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 28.189 -13.596 9.573  1.00 18.56 ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 26.758 -13.367 9.104  1.00 19.56 ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 25.778 -14.206 9.911  1.00 19.46 ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 26.415 -11.882 9.242  1.00 19.75 ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 27.709 -16.285 7.563  1.00 17.42 ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 27.398 -16.662 6.195  1.00 18.35 ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 26.058 -16.008 5.803  1.00 18.81 ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 25.935 -15.373 4.749  1.00 20.42 ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 27.330 -18.203 6.031  1.00 19.10 ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 26.813 -18.581 4.641  1.00 19.58 ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 28.708 -18.826 6.289  1.00 19.86 ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 25.049 -16.151 6.676  1.00 16.51 ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 23.720 -15.626 6.397  1.00 16.09 ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 22.941 -15.543 7.687  1.00 15.73 ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 23.113 -16.380 8.565  1.00 16.63 ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 23.002 -16.589 5.402  1.00 16.92 ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 21.511 -16.377 5.206  1.00 18.07 ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 20.899 -15.499 4.353  1.00 20.30 ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 20.456 -17.100 5.865  1.00 18.10 ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 19.522 -15.610 4.465  1.00 20.30 ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 19.226 -16.597 5.378  1.00 19.01 ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 20.434 -18.115 6.833  1.00 18.03 ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 17.984 -17.137 5.771  1.00 18.73 ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 19.204 -18.622 7.244  1.00 17.94 ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 17.998 -18.127 6.720  1.00 17.54 ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 22.096 -14.526 7.836  1.00 15.42 ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 21.207 -14.464 8.990  1.00 15.84 ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 19.866 -13.854 8.555  1.00 15.69 ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 19.828 -13.044 7.615  1.00 15.53 ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 21.823 -13.691 10.171 1.00 16.70 ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 22.397 -12.321 9.838  1.00 18.09 ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 21.395 -11.195 9.669  1.00 21.33 ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 21.662 -10.288 8.844  1.00 24.06 ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 20.351 -11.199 10.357 1.00 18.31 ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 18.789 -14.213 9.262  1.00 14.86 ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.476 -13.647 8.945  1.00 14.42 ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 16.695 -13.526 10.250 1.00 13.69 ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 16.271 -14.532 10.844 1.00 13.95 ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 16.766 -14.528 7.896  1.00 16.48 ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 15.433 -14.008 7.408  1.00 21.46 ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 14.762 -13.310 8.171  1.00 25.22 ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 15.024 -14.382 6.298  1.00 22.22 ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 16.538 -12.278 10.719 1.00 14.67 ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 15.829 -11.999 11.955 0.50 15.08 ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 15.827 -12.017 11.964 0.50 15.01 ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 14.379 -12.482 11.888 1.00 15.48 ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 13.850 -12.962 12.885 1.00 16.52 ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 15.900 -10.503 12.261 0.50 17.26 ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 15.887 -10.529 12.310 0.50 17.02 ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 15.076 -10.153 13.357 0.50 20.04 ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 15.130 -9.786  11.370 0.50 19.36 ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 13.740 -12.354 10.703 1.00 14.70 ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 12.338 -12.784 10.591 1.00 15.11 ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 12.196 -14.301 10.746 1.00 15.51 ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 11.090 -14.741 11.015 1.00 17.06 ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 11.710 -12.343 9.272  1.00 19.12 ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 12.168 -13.126 8.177  1.00 24.51 ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 13.271 -15.061 10.610 1.00 13.37 ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 13.191 -16.529 10.764 1.00 12.17 ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 13.840 -17.024 12.075 1.00 12.63 ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 13.779 -18.229 12.363 1.00 13.11 ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 13.930 -17.205 9.580  1.00 12.79 ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 13.196 -16.981 8.253  1.00 14.05 ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 13.904 -17.640 7.043  1.00 14.62 ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 13.860 -19.100 7.156  1.00 13.42 ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 13.909 -19.939 6.119  1.00 15.61 ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 13.977 -19.470 4.875  1.00 16.41 ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 13.833 -21.261 6.318  1.00 15.85 ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 14.527 -16.143 12.813 1.00 13.10 ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 15.311 -16.532 13.984 1.00 11.90 ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 16.404 -17.518 13.615 1.00 12.26 ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 16.752 -18.365 14.445 1.00 12.55 ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 14.465 -17.037 15.178 1.00 12.31 ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 15.252 -17.343 16.444 1.00 13.75 ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 16.139 -16.524 16.819 1.00 13.93 ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 14.982 -18.403 17.083 1.00 12.52 ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 17.021 -17.357 12.412 1.00 11.47 ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 18.128 -18.250 12.032 1.00 11.91 ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 19.408 -17.495 11.739 1.00 12.59 ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 19.369 -16.402 11.199 1.00 13.42 ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 17.804 -19.047 10.758 1.00 12.57 ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 16.746 -20.136 10.894 1.00 14.20 ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 16.527 -20.789 9.531  1.00 15.03 ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 17.116 -21.176 11.959 1.00 14.32 ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 20.548 -18.133 12.028 1.00 12.00 ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 21.851 -17.584 11.671 1.00 12.64 ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 22.726 -18.787 11.274 1.00 12.76 ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 22.656 -19.861 11.889 1.00 13.41 ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 22.473 -16.787 12.838 1.00 13.19 ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 23.844 -16.132 12.520 1.00 13.77 ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 24.030 -14.805 13.261 1.00 14.60 ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 25.025 -17.063 12.920 1.00 14.31 ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 23.509 -18.624 10.203 1.00 12.30 ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 24.424 -19.671 9.725  1.00 13.34 ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 25.835 -19.094 9.713  1.00 14.44 ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 26.046 -17.989 9.199  1.00 15.11 ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 24.040 -20.155 8.298  1.00 14.81 ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 25.061 -21.173 7.761  1.00 16.31 ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 22.618 -20.742 8.301  1.00 14.56 ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 26.771 -19.798 10.362 1.00 14.84 ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 28.176 -19.387 10.388 1.00 15.23 ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 29.037 -20.490 9.745  1.00 16.50 ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 28.587 -21.628 9.549  1.00 16.65 ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 28.623 -19.122 11.817 1.00 15.99 ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 28.499 -20.256 12.676 1.00 17.42 ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 30.276 -20.121 9.344  1.00 17.35 ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 31.169 -21.095 8.708  1.00 19.94 ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 32.023 -21.840 9.758  1.00 21.60 ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 32.353 -21.282 10.808 1.00 22.20 ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 32.064 -20.385 7.699  1.00 21.81 ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 32.822 -19.398 8.374  1.00 25.61 ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 32.365 -23.117 9.468  1.00 22.28 ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 33.163 -23.951 10.376 1.00 25.35 ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 34.409 -24.461 9.624  1.00 28.74 ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 34.415 -24.497 8.391  1.00 29.25 ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 32.352 -25.196 10.823 1.00 27.54 ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 32.105 -26.024 9.688  1.00 29.57 ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 31.020 -24.849 11.471 1.00 27.96 ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? 35.437 -24.893 10.358 1.00 30.99 ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? 36.618 -25.496 9.735  1.00 33.46 ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? 36.434 -27.024 9.619  1.00 34.51 ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? 37.001 -27.637 8.709  1.00 36.44 ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? 37.886 -25.119 10.512 1.00 36.63 ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? 37.683 -25.432 11.895 1.00 39.17 ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? 38.222 -23.636 10.381 1.00 37.21 ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? 35.653 -27.641 10.533 1.00 33.58 ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? 35.393 -29.079 10.524 1.00 33.58 ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 34.161 -29.440 9.717  1.00 32.98 ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 33.213 -28.669 9.672  1.00 32.40 ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? 35.240 -29.591 11.944 1.00 34.21 ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 34.157 -30.633 9.116  1.00 32.32 ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 33.041 -31.107 8.304  1.00 32.36 ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 31.888 -31.595 9.184  1.00 30.98 ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 32.095 -32.392 10.101 1.00 31.64 ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 33.522 -32.239 7.378  1.00 35.36 ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 32.425 -32.844 6.498  1.00 40.57 ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 32.102 -32.015 5.271  1.00 47.18 ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 32.761 -31.011 4.964  1.00 48.92 ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 31.084 -32.436 4.529  1.00 48.76 ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 30.683 -31.098 8.892  1.00 28.02 ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 29.467 -31.478 9.598  1.00 26.52 ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 28.805 -32.629 8.882  1.00 25.33 ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 28.811 -32.694 7.644  1.00 26.13 ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 28.220 -33.526 9.649  1.00 23.65 ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 27.635 -34.729 9.078  1.00 22.60 ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 26.114 -34.855 9.233  1.00 21.27 ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 25.604 -35.963 9.031  1.00 22.25 ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 28.347 -35.960 9.616  1.00 24.81 ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 30.116 -36.009 9.222  1.00 31.34 ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 25.377 -33.769 9.584  1.00 18.49 ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 23.917 -33.896 9.654  1.00 18.60 ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 23.374 -33.891 8.213  1.00 20.40 ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 23.960 -33.250 7.321  1.00 22.00 ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 23.298 -32.709 10.447 1.00 18.82 ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 23.609 -32.740 11.951 1.00 24.38 ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 23.796 -33.846 12.499 1.00 25.59 ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 23.624 -31.657 12.595 1.00 22.51 ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 22.276 -34.585 7.972  1.00 19.97 ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 21.616 -34.619 6.660  1.00 19.91 ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 20.371 -33.749 6.778  1.00 18.12 ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 19.613 -33.946 7.726  1.00 19.01 ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 21.146 -36.061 6.336  1.00 23.72 ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 22.311 -36.870 6.089  1.00 26.77 ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 20.228 -36.113 5.098  1.00 24.40 ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 20.151 -32.816 5.854  1.00 17.20 ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 18.965 -31.966 5.883  1.00 16.48 ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 17.858 -32.655 5.080  1.00 16.47 ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 18.085 -33.150 3.960  1.00 16.64 ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 19.234 -30.574 5.265  1.00 17.18 ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 20.481 -29.883 5.884  1.00 19.59 ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 17.995 -29.670 5.386  1.00 17.30 ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 20.334 -29.639 7.439  1.00 21.73 ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 16.646 -32.696 5.653  1.00 15.39 ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 15.503 -33.268 4.950  1.00 14.46 ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 15.079 -32.363 3.795  1.00 13.63 ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 15.120 -31.130 3.931  1.00 13.96 ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 14.340 -33.391 5.929  1.00 13.54 ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 14.655 -32.955 2.656  1.00 13.87 ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 14.182 -32.171 1.486  1.00 13.65 ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 12.823 -32.832 1.186  1.00 13.79 ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 12.734 -33.838 0.468  1.00 14.37 ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 15.155 -32.314 0.307  1.00 14.32 ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 16.562 -31.790 0.624  1.00 15.13 ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 16.620 -30.282 0.967  1.00 16.80 ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 17.995 -29.878 1.277  1.00 17.56 ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 18.339 -28.753 1.901  1.00 19.42 ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.412 -27.904 2.306  1.00 17.44 ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 19.625 -28.470 2.119  1.00 20.77 ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 11.765 -32.301 1.805  1.00 14.16 ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 10.461 -32.941 1.810  1.00 14.89 ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 9.357  -31.984 2.297  1.00 15.33 ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 9.643  -30.874 2.749  1.00 14.90 ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 10.522 -34.151 2.740  1.00 15.90 ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 10.686 -33.673 4.491  1.00 14.18 ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 8.083  -32.518 2.303  1.00 15.10 ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 6.948  -31.816 2.875  1.00 16.01 ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 6.316  -32.614 4.039  1.00 16.24 ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 5.121  -32.500 4.298  1.00 16.29 ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 5.901  -31.425 1.831  1.00 18.59 ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 5.187  -32.571 1.183  1.00 24.00 ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 5.578  -33.742 1.420  1.00 24.29 ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 4.213  -32.311 0.447  1.00 28.90 ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 7.125  -33.412 4.778  1.00 14.43 ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 6.649  -34.148 5.959  1.00 13.19 ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 5.974  -33.215 6.937  1.00 12.34 ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 6.403  -32.051 7.113  1.00 11.80 ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 7.812  -34.855 6.646  1.00 13.22 ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 8.321  -36.358 5.790  1.00 14.91 ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 4.960  -33.767 7.606  1.00 12.23 ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 4.225  -33.169 8.714  1.00 12.48 ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 4.230  -34.072 9.939  1.00 12.76 ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 3.434  -33.846 10.862 1.00 13.04 ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 2.791  -32.741 8.330  1.00 13.57 ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 2.807  -31.441 7.489  1.00 15.54 ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 1.405  -31.028 7.174  1.00 16.39 ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 0.915  -31.212 6.024  1.00 18.32 ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 0.702  -30.508 8.212  1.00 15.56 ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 5.122  -35.107 10.004 1.00 12.60 ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 5.262  -35.931 11.219 1.00 13.82 ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 6.781  -36.112 11.421 1.00 13.21 ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 7.562  -36.219 10.441 1.00 13.01 ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 4.559  -37.310 11.136 1.00 18.23 ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 5.214  -38.122 10.170 1.00 20.61 ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 3.091  -37.213 10.780 1.00 20.06 ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 7.177  -36.109 12.690 1.00 12.07 ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 8.601  -36.250 12.996 1.00 12.55 ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 8.815  -36.374 14.490 1.00 11.41 ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 7.870  -36.643 15.218 1.00 12.81 ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 10.060 -36.248 14.921 1.00 11.41 ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 10.412 -36.397 16.340 1.00 10.65 ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 11.317 -35.214 16.719 1.00 11.47 ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 12.300 -34.956 16.017 1.00 11.31 ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 11.174 -37.734 16.536 1.00 12.18 ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 11.674 -37.898 17.983 1.00 14.49 ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 10.287 -38.919 16.165 1.00 12.66 ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 11.036 -34.564 17.896 1.00 11.47 ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 11.946 -33.499 18.351 1.00 10.63 ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 12.575 -33.795 19.696 1.00 11.98 ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 12.000 -34.539 20.491 1.00 11.27 ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 11.254 -32.101 18.387 1.00 10.90 ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 10.343 -31.845 19.570 1.00 11.08 ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 9.042  -32.344 19.591 1.00 12.99 ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 10.728 -30.985 20.599 1.00 11.77 ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 8.172  -32.075 20.651 1.00 14.13 ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 9.868  -30.708 21.675 1.00 12.96 ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 8.589  -31.263 21.698 1.00 14.23 ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 7.702  -30.993 22.720 1.00 16.34 ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 13.765 -33.234 19.923 1.00 12.19 ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 14.445 -33.388 21.212 1.00 12.04 ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 14.064 -32.223 22.127 1.00 11.81 ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 14.204 -31.046 21.749 1.00 12.41 ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 15.970 -33.481 21.064 1.00 12.86 ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 16.627 -33.663 22.419 1.00 14.18 ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 16.393 -34.803 23.178 1.00 15.33 ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.392 -32.653 22.985 1.00 16.35 ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 16.957 -34.968 24.445 1.00 17.44 ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 17.960 -32.806 24.254 1.00 18.18 ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 17.743 -33.965 24.974 1.00 19.80 ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 18.282 -34.119 26.246 1.00 23.09 ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 13.571 -32.573 23.358 1.00 12.37 ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 13.143 -31.595 24.357 1.00 13.46 ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 14.134 -31.672 25.565 1.00 15.03 ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 14.043 -32.605 26.387 1.00 16.56 ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 11.715 -31.900 24.783 1.00 14.28 ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 11.083 -30.846 26.121 1.00 16.85 ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 15.084 -30.700 25.649 1.00 14.29 ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 16.072 -30.764 26.714 1.00 16.98 ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 15.466 -30.644 28.090 1.00 18.28 ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 15.967 -31.276 29.033 1.00 19.90 ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 17.188 -29.736 26.507 1.00 20.65 ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 16.695 -28.413 26.501 1.00 25.35 ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 14.371 -29.881 28.224 1.00 17.23 ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 13.755 -29.711 29.560 1.00 16.80 ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 13.040 -30.944 30.088 1.00 18.36 ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 12.584 -30.947 31.254 1.00 20.22 ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 12.832 -28.501 29.566 1.00 16.92 ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 11.728 -28.704 28.710 1.00 16.75 ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 12.949 -32.005 29.265 1.00 16.67 ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 12.404 -33.287 29.679 1.00 15.65 ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 13.428 -34.431 29.455 1.00 16.44 ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 13.098 -35.595 29.709 1.00 17.66 ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 11.108 -33.596 28.904 1.00 17.12 ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 9.949  -32.643 29.228 1.00 19.94 ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 9.351  -32.947 30.604 1.00 21.46 ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 8.260  -32.023 30.957 1.00 24.26 ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 8.427  -30.868 31.589 1.00 30.63 ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 9.645  -30.462 31.939 1.00 30.85 ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 7.380  -30.107 31.881 1.00 32.15 ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 14.627 -34.121 28.882 1.00 16.82 ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 15.639 -35.120 28.460 1.00 18.55 ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 14.976 -36.249 27.658 1.00 19.43 ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 15.207 -37.447 27.910 1.00 20.36 ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 16.411 -35.697 29.660 1.00 21.33 ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 17.218 -34.664 30.391 1.00 25.43 ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 18.436 -34.269 29.618 1.00 31.74 ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 19.444 -33.625 30.458 1.00 35.04 ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 19.508 -32.316 30.683 1.00 38.43 ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 18.602 -31.497 30.155 1.00 35.85 ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 20.471 -31.816 31.445 1.00 39.98 ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 14.047 -35.859 26.744 1.00 18.07 ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 13.271 -36.847 26.012 1.00 18.18 ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 13.013 -36.398 24.583 1.00 16.07 ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 12.964 -35.197 24.316 1.00 15.04 ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 11.853 -36.989 26.657 1.00 22.20 ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 11.693 -38.025 27.755 1.00 33.15 ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 10.207 -38.242 28.012 1.00 39.22 ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 9.937  -39.483 28.839 1.00 45.71 ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 10.571 -39.387 30.180 1.00 48.66 ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 12.787 -37.360 23.703 1.00 14.51 ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 12.338 -37.125 22.339 1.00 13.35 ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 10.830 -37.366 22.295 1.00 15.25 ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 10.332 -38.365 22.860 1.00 17.03 ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 13.035 -38.074 21.344 1.00 13.55 ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 14.523 -37.874 21.261 1.00 15.65 ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 15.116 -37.109 20.251 1.00 17.68 ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 15.499 -38.390 22.045 1.00 15.59 ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 16.430 -37.186 20.468 1.00 16.28 ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 16.702 -37.913 21.549 1.00 17.92 ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 10.107 -36.509 21.554 1.00 12.83 ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 8.660  -36.666 21.422 1.00 12.75 ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 8.250  -36.746 19.958 1.00 12.58 ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 8.691  -35.906 19.173 1.00 12.20 ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 7.937  -35.455 22.040 1.00 13.38 ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 8.030  -35.368 23.550 1.00 14.14 ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 7.302  -36.225 24.360 1.00 15.66 ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 8.798  -34.382 24.168 1.00 15.76 ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 7.321  -36.088 25.752 1.00 17.14 ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 8.868  -34.277 25.552 1.00 17.21 ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 8.123  -35.128 26.341 1.00 19.13 ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 8.166  -34.971 27.721 1.00 21.67 ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 7.426  -37.759 19.598 1.00 12.90 ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 6.918  -37.835 18.219 1.00 11.80 ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 5.759  -36.815 18.101 1.00 13.27 ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 4.899  -36.763 19.006 1.00 14.26 ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 6.414  -39.292 18.115 1.00 12.35 ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 6.059  -39.656 19.509 1.00 13.91 ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 6.935  -38.870 20.448 1.00 13.00 ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 5.705  -36.049 17.004 1.00 13.12 ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 4.631  -35.053 16.835 1.00 13.32 ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 4.211  -34.919 15.378 1.00 12.89 ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 5.004  -35.137 14.466 1.00 13.85 ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 5.085  -33.630 17.306 1.00 14.65 ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 5.224  -33.531 18.830 1.00 16.10 ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 6.357  -33.154 16.578 1.00 14.39 ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 2.956  -34.451 15.171 1.00 12.17 ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 2.489  -33.916 13.913 1.00 12.44 ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 2.785  -32.379 13.974 1.00 12.27 ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 2.729  -31.747 15.063 1.00 13.34 ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 0.969  -34.105 13.789 1.00 14.70 ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 0.656  -35.484 13.676 1.00 20.94 ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 3.167  -31.793 12.841 1.00 11.26 ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 3.479  -30.358 12.827 1.00 11.47 ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 2.915  -29.700 11.574 1.00 12.72 ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 2.661  -30.378 10.569 1.00 13.68 ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 4.990  -30.066 13.009 1.00 11.38 ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 5.904  -30.791 12.038 1.00 11.51 ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 6.381  -32.077 12.315 1.00 11.48 ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 6.350  -30.163 10.883 1.00 12.95 ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 7.263  -32.707 11.437 1.00 11.81 ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 7.225  -30.801 10.008 1.00 12.68 ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 7.675  -32.075 10.288 1.00 12.14 ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 2.670  -28.374 11.664 1.00 11.93 ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 2.046  -27.650 10.565 1.00 13.58 ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 2.973  -27.326 9.405  1.00 14.65 ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 4.159  -27.653 9.421  1.00 14.51 ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 1.420  -26.355 11.088 1.00 14.20 ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 2.392  -25.427 11.547 1.00 15.86 ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 2.421  -26.686 8.360  1.00 14.28 ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 3.239  -26.242 7.234  1.00 16.06 ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 3.950  -24.934 7.604  1.00 15.36 ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 3.376  -24.099 8.331  1.00 17.53 ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 2.305  -25.997 6.035  1.00 18.23 ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 1.595  -27.254 5.591  1.00 23.25 ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 0.762  -26.965 4.341  1.00 30.86 ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 0.064  -28.186 3.811  1.00 38.21 ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? -0.869 -27.824 2.710  1.00 42.53 ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 5.150  -24.650 7.050  1.00 14.92 ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 5.850  -23.400 7.414  1.00 15.56 ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 5.020  -22.165 7.091  1.00 17.83 ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 4.418  -22.072 5.999  1.00 19.53 ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 7.147  -23.420 6.584  1.00 16.77 ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 7.288  -24.796 6.074  1.00 18.05 ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 5.958  -25.495 6.145  1.00 14.27 ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 4.920  -21.240 8.069  1.00 17.17 ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 4.038  -20.089 7.868  1.00 19.67 ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 4.450  -18.899 8.714  1.00 18.47 ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 5.425  -18.985 9.472  1.00 17.28 ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 2.593  -20.501 8.155  1.00 25.03 ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 2.342  -20.621 9.550  1.00 29.96 ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 3.754  -17.758 8.528  1.00 18.13 ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 4.024  -16.503 9.230  1.00 19.62 ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 3.166  -16.504 10.482 1.00 20.29 ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 1.916  -16.500 10.361 1.00 21.66 ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 3.490  -15.359 8.351  1.00 22.18 ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 4.438  -14.426 7.626  1.00 26.85 ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 3.661  -13.217 7.089  1.00 28.92 ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 5.585  -13.943 8.509  1.00 27.46 ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 3.791  -16.477 11.661 1.00 18.50 ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 3.119  -16.555 12.956 1.00 19.53 ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 3.529  -15.414 13.906 1.00 19.15 ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 4.702  -15.090 13.995 1.00 17.91 ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 3.434  -17.945 13.568 1.00 22.19 ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 2.857  -19.073 12.646 1.00 24.44 ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 2.968  -18.048 15.020 1.00 23.87 ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 3.131  -20.483 13.069 1.00 26.73 ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 2.566  -14.794 14.593 1.00 19.20 ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 2.868  -13.680 15.494 1.00 19.89 ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 3.633  -14.133 16.729 1.00 19.81 ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 3.217  -15.085 17.380 1.00 20.79 ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 1.559  -12.963 15.934 1.00 21.00 ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 1.838  -11.723 16.756 1.00 22.13 ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 1.570  -11.697 18.113 1.00 23.51 ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 2.444  -10.614 16.185 1.00 22.90 ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 1.828  -10.541 18.865 1.00 24.31 ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 2.711  -9.466  16.943 1.00 24.67 ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 2.412  -9.444  18.282 1.00 24.65 ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 4.737  -13.428 17.070 1.00 19.67 ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 5.525  -13.736 18.263 1.00 19.97 ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 5.641  -12.468 19.118 1.00 20.28 ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 6.073  -11.425 18.620 1.00 20.18 ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 6.923  -14.270 17.880 1.00 20.47 ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 7.693  -14.718 19.133 1.00 20.86 ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 6.816  -15.419 16.882 1.00 20.92 ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 5.252  -12.551 20.399 1.00 21.33 ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 5.294  -11.431 21.339 1.00 21.74 ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 6.714  -10.917 21.562 1.00 21.07 ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 7.673  -11.678 21.383 1.00 19.97 ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 4.744  -11.879 22.705 1.00 24.44 ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 3.427  -12.625 22.652 1.00 33.51 ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 2.202  -11.747 22.772 1.00 41.87 ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 1.096  -12.309 22.945 1.00 44.01 ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 2.333  -10.507 22.655 1.00 42.79 ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 6.861  -9.642  21.978 1.00 20.79 ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 8.202  -9.096  22.238 1.00 20.66 ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 8.923  -9.895  23.323 1.00 21.24 ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 8.297  -10.452 24.231 1.00 21.81 ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 8.105  -7.628  22.682 1.00 20.40 ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 10.245 -9.986  23.195 1.00 19.55 ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 11.096 -10.614 24.186 1.00 18.19 ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 12.324 -9.664  24.310 1.00 19.52 ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 12.397 -8.605  23.631 1.00 19.95 ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 11.533 -12.013 23.700 1.00 17.99 ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 12.333 -11.899 22.534 1.00 17.12 ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 13.283 -10.008 25.168 1.00 18.67 ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 14.532 -9.206  25.239 1.00 19.08 ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 15.287 -9.288  23.895 1.00 18.84 ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 16.078 -8.381  23.570 1.00 19.44 ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 15.438 -9.692  26.383 1.00 22.37 ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 14.937 -9.224  27.742 1.00 27.06 ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 15.798 -9.555  28.948 1.00 36.91 ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 15.281 -9.418  30.084 1.00 40.68 ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 16.978 -9.942  28.767 1.00 35.00 ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 15.057 -10.365 23.117 1.00 17.77 ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 15.804 -10.592 21.893 1.00 17.53 ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 15.216 -9.943  20.640 1.00 18.04 ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 15.973 -9.716  19.683 1.00 20.19 ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 15.885 -12.115 21.616 1.00 17.03 ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 16.421 -12.911 22.778 1.00 18.14 ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 17.786 -12.965 23.044 1.00 19.72 ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 15.570 -13.619 23.606 1.00 18.83 ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 18.290 -13.776 24.061 1.00 20.88 ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 16.057 -14.416 24.634 1.00 20.93 ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 17.418 -14.468 24.880 1.00 22.75 ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 17.905 -15.276 25.905 1.00 26.24 ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 13.897 -9.704  20.614 1.00 17.71 ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 13.237 -9.212  19.409 1.00 18.05 ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 12.070 -8.328  19.774 1.00 19.17 ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 11.377 -8.575  20.774 1.00 19.92 ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 12.593 -10.403 18.625 1.00 17.33 ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 13.577 -11.349 17.979 1.00 16.35 ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 13.759 -12.638 18.471 1.00 16.02 ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 14.296 -10.973 16.854 1.00 15.99 ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 14.611 -13.524 17.860 1.00 16.11 ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 15.151 -11.861 16.227 1.00 15.62 ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 15.300 -13.133 16.737 1.00 15.65 ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 16.201 -13.977 16.169 1.00 15.73 ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 11.717 -7.381  18.884 1.00 19.87 ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 10.446 -6.690  19.071 1.00 19.72 ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 9.284  -7.654  18.776 1.00 19.87 ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 9.477  -8.695  18.129 1.00 19.13 ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 10.473 -5.619  17.961 1.00 20.49 ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 11.311 -6.225  16.897 1.00 21.29 ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 12.368 -7.021  17.599 1.00 20.05 ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 8.046  -7.272  19.122 1.00 19.94 ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 6.846  -8.029  18.730 1.00 19.94 ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 6.821  -8.040  17.170 1.00 20.08 ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 7.157  -7.012  16.557 1.00 20.64 ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 5.582  -7.333  19.255 1.00 20.37 ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 6.606  -9.219  16.552 1.00 19.34 ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 6.733  -9.291  15.097 1.00 19.05 ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 6.119  -10.580 14.562 1.00 18.95 ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 5.815  -11.484 15.344 1.00 20.47 ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 8.252  -9.248  14.734 1.00 18.73 ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 8.956  -10.620 15.061 1.00 16.73 ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 10.457 -10.494 15.285 1.00 17.73 ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 11.220 -11.669 14.858 1.00 16.69 ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 11.261 -12.845 15.481 1.00 18.42 ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 12.041 -13.816 15.024 1.00 16.77 ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 10.525 -13.059 16.575 1.00 17.47 ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 6.056  -10.722 13.230 1.00 18.76 ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 5.668  -12.014 12.652 1.00 19.69 ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 6.964  -12.755 12.303 1.00 17.76 ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 7.860  -12.186 11.656 1.00 17.93 ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 4.850  -11.810 11.379 1.00 20.99 ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 3.455  -11.340 11.698 1.00 24.51 ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 2.431  -12.247 11.921 1.00 26.63 ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 3.180  -9.995  11.868 1.00 26.96 ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 1.149  -11.822 12.243 1.00 28.64 ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 1.898  -9.559  12.200 1.00 28.67 ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 0.895  -10.482 12.414 1.00 30.17 ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? -0.395 -10.099 12.741 1.00 33.01 ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 7.066  -14.009 12.759 1.00 15.95 ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 8.209  -14.846 12.424 1.00 15.29 ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 7.768  -15.748 11.265 1.00 14.90 ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 6.703  -16.362 11.317 1.00 16.35 ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 8.665  -15.655 13.642 1.00 15.75 ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 9.816  -16.649 13.296 1.00 15.88 ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 10.564 -17.161 14.513 1.00 14.48 ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 10.764 -16.448 15.500 1.00 15.18 ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 11.013 -18.448 14.452 1.00 12.49 ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 8.591  -15.800 10.217 1.00 14.33 ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 8.264  -16.565 9.008  1.00 14.11 ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 8.877  -17.969 9.056  1.00 13.89 ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 9.794  -18.231 9.863  1.00 14.77 ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 8.778  -15.824 7.771  1.00 16.45 ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 10.185 -15.623 7.829  1.00 18.68 ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 8.380  -18.863 8.158  1.00 13.74 ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 8.926  -20.233 8.005  1.00 14.11 ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 8.847  -21.018 9.334  1.00 14.36 ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 9.720  -21.857 9.607  1.00 14.48 ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 10.380 -20.178 7.462  1.00 14.91 ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 10.489 -19.538 6.101  1.00 16.24 ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 10.409 -20.298 4.943  1.00 18.47 ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 10.567 -18.228 5.758  1.00 18.02 ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 10.528 -19.437 3.930  1.00 18.81 ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 10.613 -18.180 4.366  1.00 20.09 ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 7.801  -20.750 10.145 1.00 14.04 ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 7.652  -21.383 11.479 1.00 13.78 ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 6.559  -22.472 11.422 1.00 14.60 ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 5.536  -22.282 10.777 1.00 14.93 ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 7.232  -20.295 12.494 1.00 14.94 ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 7.210  -20.684 13.949 1.00 17.45 ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 8.614  -21.073 14.425 1.00 16.40 ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 6.760  -19.505 14.811 1.00 20.54 ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 6.801  -23.628 12.063 1.00 13.80 ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 5.837  -24.743 12.084 1.00 13.92 ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 5.463  -25.026 13.537 1.00 14.83 ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 6.363  -25.029 14.390 1.00 15.40 ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 6.520  -25.990 11.495 1.00 13.47 ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 6.962  -25.727 10.063 1.00 17.95 ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 7.966  -27.057 9.448  1.00 18.97 ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 9.454  -26.932 10.488 1.00 15.82 ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 4.183  -25.299 13.827 1.00 13.61 ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 3.783  -25.553 15.215 1.00 13.07 ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 3.389  -27.010 15.434 1.00 12.60 ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 2.846  -27.642 14.543 1.00 12.07 ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 2.537  -24.709 15.597 1.00 14.22 ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 2.731  -23.200 15.569 1.00 17.44 ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 1.444  -22.484 16.028 1.00 20.69 ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 3.855  -22.775 16.457 1.00 18.45 ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 3.587  -27.475 16.656 1.00 12.87 ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 3.121  -28.801 17.082 1.00 11.81 ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 2.546  -28.664 18.504 1.00 12.38 ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 2.944  -27.771 19.252 1.00 13.51 ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 4.299  -29.798 17.120 1.00 12.72 ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 1.691  -29.608 18.899 1.00 12.86 ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 1.227  -29.687 20.282 1.00 13.63 ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 2.323  -30.393 21.071 1.00 14.66 ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 2.654  -31.559 20.768 1.00 15.89 ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? -0.127 -30.431 20.386 1.00 15.25 ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? -0.549 -30.522 21.853 1.00 15.70 ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? -1.182 -29.664 19.570 1.00 16.94 ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 2.921  -29.693 22.017 1.00 15.58 ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 4.009  -30.272 22.790 1.00 16.61 ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 4.582  -29.328 23.817 1.00 17.12 ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 4.337  -28.110 23.763 1.00 17.57 ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 5.418  -29.879 24.712 1.00 15.95 ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 6.059  -29.084 25.743 1.00 16.45 ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 7.352  -28.433 25.255 1.00 15.78 ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 8.132  -29.062 24.528 1.00 16.11 ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 6.422  -29.976 26.959 1.00 17.86 ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 7.176  -29.222 28.014 1.00 18.86 ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 6.555  -28.236 28.779 1.00 20.86 ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 8.493  -29.278 28.354 1.00 20.23 ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 7.500  -27.758 29.587 1.00 22.33 ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 8.685  -28.351 29.356 1.00 22.69 ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 7.604  -27.208 25.747 1.00 15.89 ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 8.860  -26.516 25.545 1.00 17.03 ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 9.053  -25.435 26.611 1.00 17.53 ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 8.088  -24.931 27.213 1.00 17.81 ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 8.974  -25.936 24.137 1.00 18.69 ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 8.080  -24.845 23.990 1.00 20.79 ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 10.315 -25.127 26.869 1.00 17.17 ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 10.782 -24.021 27.704 1.00 17.67 ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 11.748 -23.225 26.800 1.00 17.69 ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 12.304 -23.773 25.826 1.00 16.89 ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 11.560 -24.531 28.940 1.00 20.35 ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 10.801 -25.566 29.741 1.00 31.01 ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 10.170 -25.082 31.024 1.00 40.94 ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 10.176 -23.853 31.269 1.00 43.20 ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 9.637  -25.935 31.769 1.00 43.15 ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 12.026 -21.943 27.111 1.00 17.92 ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 12.950 -21.177 26.251 1.00 17.76 ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 14.323 -21.837 26.047 1.00 16.92 ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 14.900 -21.735 24.939 1.00 17.66 ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 13.053 -19.826 26.969 1.00 19.49 ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 11.700 -19.712 27.693 1.00 20.76 ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 11.432 -21.107 28.176 1.00 19.28 ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 14.829 -22.501 27.103 1.00 16.52 ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 16.106 -23.209 27.026 1.00 15.99 ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 16.123 -24.394 26.063 1.00 15.60 ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 17.188 -24.948 25.755 1.00 15.16 ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 14.945 -24.806 25.576 1.00 13.93 ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 14.835 -25.905 24.604 1.00 13.77 ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 15.186 -25.443 23.162 1.00 13.13 ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 15.325 -26.293 22.262 1.00 13.13 ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 13.395 -26.490 24.608 1.00 13.62 ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 13.132 -27.305 25.865 1.00 16.45 ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 14.078 -27.928 26.369 1.00 17.67 ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 11.986 -27.284 26.356 1.00 17.52 ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 15.321 -24.114 22.904 1.00 13.23 ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 15.684 -23.618 21.561 1.00 13.11 ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 16.938 -24.294 21.069 1.00 13.36 ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 17.866 -24.493 21.867 1.00 14.33 ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 15.880 -22.108 21.561 1.00 13.96 ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 14.325 -21.174 21.601 1.00 16.29 ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 16.925 -24.706 19.813 1.00 12.81 ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 18.071 -25.386 19.235 1.00 13.26 ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 17.906 -26.902 19.167 1.00 13.79 ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 18.656 -27.585 18.466 1.00 14.43 ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 16.919 -27.446 19.881 1.00 12.10 ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 16.624 -28.877 19.842 1.00 12.45 ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 16.145 -29.228 18.424 1.00 12.54 ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 15.368 -28.473 17.817 1.00 12.57 ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 16.650 -30.351 17.879 1.00 11.86 ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 16.350 -30.707 16.499 1.00 12.05 ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 15.034 -31.443 16.335 1.00 11.62 ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 14.712 -32.340 17.140 1.00 13.06 ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.556 -31.503 15.895 1.00 14.92 ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 18.736 -30.518 15.585 1.00 16.83 ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.173 -32.337 14.649 1.00 16.81 ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 20.023 -31.260 15.112 1.00 19.81 ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 14.299 -31.098 15.245 1.00 10.96 ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 13.095 -31.829 14.777 1.00 11.28 ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 13.578 -32.606 13.544 1.00 12.14 ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 14.176 -32.007 12.641 1.00 12.24 ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 11.994 -30.819 14.376 1.00 11.05 ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 10.779 -31.431 13.636 1.00 12.28 ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 9.980  -32.392 14.549 1.00 12.90 ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 9.843  -30.300 13.155 1.00 12.97 ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 13.367 -33.951 13.541 1.00 12.14 ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 13.805 -34.813 12.430 1.00 13.56 ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 12.641 -35.630 11.918 1.00 14.33 ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 11.798 -36.076 12.703 1.00 15.42 ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 14.814 -35.876 12.917 1.00 16.47 ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 15.976 -35.380 13.688 1.00 25.14 ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 16.853 -36.572 14.075 1.00 31.26 ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 17.424 -37.131 12.859 1.00 35.55 ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 18.565 -36.713 12.317 1.00 37.74 ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 19.333 -35.837 12.958 1.00 39.48 ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 18.958 -37.190 11.150 1.00 36.13 ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 12.645 -35.884 10.630 1.00 12.84 ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 11.670 -36.810 10.010 1.00 13.42 ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 12.481 -37.990 9.442  1.00 16.07 ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 13.706 -38.078 9.618  1.00 15.40 ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 10.854 -36.118 8.927  1.00 13.61 ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 11.872 -35.588 7.533  1.00 13.82 ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 11.789 -38.907 8.717  1.00 17.84 ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 12.480 -40.025 8.108  1.00 19.23 ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 13.549 -39.600 7.078  1.00 19.51 ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 14.387 -40.409 6.697  1.00 21.41 ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 11.465 -40.981 7.452  1.00 22.51 ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 10.792 -40.396 6.212  1.00 26.87 ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 9.765  -41.338 5.626  1.00 35.28 ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 8.562  -41.118 5.773  1.00 36.97 ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 10.221 -42.394 4.944  1.00 37.06 ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 13.530 -38.332 6.615  1.00 16.34 ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 14.478 -37.855 5.588  1.00 16.65 ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 15.683 -37.104 6.131  1.00 17.99 ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 16.604 -36.834 5.373  1.00 20.12 ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 13.774 -36.976 4.535  1.00 17.33 ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 12.575 -37.638 3.915  1.00 18.15 ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 11.292 -37.234 4.225  1.00 18.72 ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 12.509 -38.628 2.993  1.00 18.85 ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 10.470 -38.023 3.549  1.00 20.27 ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 11.153 -38.881 2.776  1.00 20.31 ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 15.664 -36.743 7.418  1.00 16.62 ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 16.767 -35.981 7.998  1.00 15.71 ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 16.282 -34.835 8.871  1.00 14.24 ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 15.153 -34.848 9.359  1.00 13.77 ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 17.140 -33.851 9.072  1.00 13.70 ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 16.813 -32.677 9.888  1.00 13.19 ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 15.797 -31.774 9.220  1.00 12.16 ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 16.027 -31.328 8.083  1.00 13.84 ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 18.098 -31.877 10.245 1.00 14.20 ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 17.749 -30.582 10.993 1.00 14.67 ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 19.056 -32.763 11.060 1.00 14.99 ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 14.708 -31.409 9.942  1.00 11.89 ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 13.662 -30.544 9.422  1.00 12.06 ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 13.845 -29.101 9.906  1.00 12.29 ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 13.640 -28.152 9.150  1.00 12.31 ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 12.285 -31.070 9.881  1.00 12.21 ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 11.158 -30.081 9.515  1.00 13.25 ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 12.011 -32.442 9.273  1.00 12.46 ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 14.203 -28.949 11.183 1.00 11.60 ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 14.355 -27.610 11.749 1.00 12.22 ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 14.736 -27.651 13.208 1.00 11.48 ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 15.106 -28.716 13.720 1.00 12.11 ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 14.703 -26.475 13.863 1.00 11.93 ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 15.109 -26.415 15.267 1.00 11.98 ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 14.057 -25.694 16.088 1.00 11.44 ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 13.403 -24.784 15.589 1.00 11.09 ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 16.473 -25.697 15.450 1.00 12.95 ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 16.497 -24.328 14.730 1.00 13.40 ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.655 -26.605 15.026 1.00 14.71 ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 17.905 -23.520 15.071 1.00 15.22 ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 13.906 -26.053 17.384 1.00 10.48 ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 12.955 -25.333 18.266 1.00 10.68 ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 13.310 -23.834 18.295 1.00 11.25 ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 14.497 -23.493 18.418 1.00 11.94 ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 13.049 -25.900 19.712 1.00 11.83 ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 12.199 -25.068 20.674 1.00 13.27 ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 12.626 -27.383 19.762 1.00 12.39 ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 12.295 -22.978 18.187 1.00 11.33 ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 12.511 -21.526 18.151 1.00 11.92 ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 11.482 -20.756 18.984 1.00 13.09 ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 11.793 -19.675 19.513 1.00 13.20 ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 12.479 -21.054 16.694 1.00 13.07 ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 12.610 -19.636 16.581 1.00 14.08 ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 10.245 -21.264 19.108 1.00 12.38 ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 9.213  -20.563 19.898 1.00 14.46 ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 8.418  -21.588 20.737 1.00 14.74 ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 8.515  -22.797 20.520 1.00 13.52 ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 8.213  -19.787 19.000 1.00 15.74 ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 7.328  -20.697 18.339 1.00 16.89 ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 8.873  -18.896 17.999 1.00 15.08 ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 7.645  -21.095 21.694 1.00 15.35 ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 6.767  -21.960 22.470 1.00 16.73 ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 5.823  -21.172 23.337 1.00 18.08 ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 6.053  -20.005 23.634 1.00 17.93 ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 4.772  -21.836 23.785 1.00 18.55 ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 3.781  -21.224 24.659 1.00 20.30 ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 2.421  -21.873 24.478 1.00 20.43 ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 2.129  -22.430 23.422 1.00 20.12 ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 1.592  -21.815 25.527 1.00 21.43 ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 0.245  -22.392 25.504 1.00 22.35 ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 0.198  -23.856 25.061 1.00 21.78 ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? -0.787 -24.281 24.428 1.00 22.58 ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? -0.655 -21.566 24.620 1.00 25.08 ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? -0.880 -20.193 25.160 1.00 32.25 ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? -0.973 -19.973 26.374 1.00 34.80 ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? -1.059 -19.269 24.254 1.00 34.51 ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 1.228  -24.631 25.407 1.00 20.44 ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 1.244  -26.046 25.040 1.00 18.82 ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 1.527  -26.313 23.568 1.00 16.88 ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 1.263  -27.418 23.073 1.00 16.50 ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 2.083  -25.323 22.867 1.00 15.50 ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 2.458  -25.451 21.471 1.00 15.73 ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 3.963  -25.150 21.360 1.00 16.04 ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 4.464  -24.269 22.048 1.00 17.75 ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 1.640  -24.455 20.635 1.00 17.74 ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 0.111  -24.747 20.673 1.00 20.30 ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? -0.691 -23.486 20.509 1.00 22.78 ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? -0.264 -25.726 19.585 1.00 20.76 ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 4.653  -25.866 20.503 1.00 13.61 ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 6.070  -25.655 20.281 1.00 13.75 ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 6.252  -25.264 18.808 1.00 13.54 ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 5.607  -25.861 17.914 1.00 13.44 ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 6.926  -26.887 20.662 1.00 14.19 ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 6.402  -28.170 20.030 1.00 17.06 ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 8.431  -26.653 20.324 1.00 14.44 ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 7.156  -24.295 18.584 1.00 13.32 ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 7.376  -23.824 17.227 1.00 13.39 ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 8.787  -24.122 16.755 1.00 12.70 ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 9.729  -23.966 17.521 1.00 12.74 ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 8.930  -24.587 15.494 1.00 11.47 ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 10.214 -24.976 14.912 1.00 11.51 ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 10.495 -24.111 13.693 1.00 12.17 ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 9.621  -23.958 12.831 1.00 12.65 ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 10.177 -26.462 14.438 1.00 12.20 ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 9.707  -27.437 15.490 1.00 12.31 ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 10.596 -27.975 16.401 1.00 11.73 ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 8.358  -27.791 15.585 1.00 13.21 ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 10.147 -28.853 17.383 1.00 12.71 ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 7.921  -28.701 16.537 1.00 14.49 ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 8.820  -29.226 17.435 1.00 14.17 ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 11.732 -23.590 13.616 1.00 11.49 ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 12.194 -22.827 12.454 1.00 10.74 ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 12.572 -23.839 11.378 1.00 10.72 ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 13.489 -24.650 11.594 1.00 11.64 ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 13.428 -21.999 12.825 1.00 11.05 ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 11.883 -23.805 10.232 1.00 11.08 ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 12.181 -24.728 9.130  1.00 11.90 ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 13.517 -24.444 8.475  1.00 12.69 ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 13.874 -23.265 8.297  1.00 13.08 ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 11.070 -24.585 8.061  1.00 13.32 ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 11.157 -25.606 6.946  1.00 18.94 ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 11.400 -26.779 7.239  1.00 18.03 ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 11.080 -25.209 5.781  1.00 21.55 ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 14.277 -25.509 8.075  1.00 11.79 ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 15.507 -25.276 7.287  1.00 12.55 ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 15.467 -26.025 5.944  1.00 13.63 ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 16.436 -25.960 5.198  1.00 14.08 ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 16.814 -25.663 8.043  1.00 13.39 ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 16.983 -24.806 9.318  1.00 13.51 ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 16.827 -27.163 8.379  1.00 13.46 ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 14.361 -26.734 5.630  1.00 12.82 ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 14.260 -27.575 4.437  1.00 12.78 ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 14.331 -26.824 3.135  1.00 14.40 ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 14.689 -27.422 2.116  1.00 15.63 ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 12.978 -28.438 4.471  1.00 12.94 ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 12.968 -29.453 5.606  1.00 13.96 ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 11.638 -30.178 5.657  1.00 12.43 ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 10.560 -29.278 6.080  1.00 13.22 ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 9.304  -29.674 6.312  1.00 14.62 ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 8.932  -30.919 6.049  1.00 14.08 ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 8.396  -28.811 6.770  1.00 14.84 ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 13.943 -25.547 3.131  1.00 14.00 ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 13.998 -24.745 1.911  1.00 15.44 ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 15.380 -24.170 1.631  1.00 16.25 ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 15.589 -23.648 0.525  1.00 17.92 ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 12.971 -23.612 1.960  1.00 16.03 ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 13.280 -22.597 3.037  1.00 19.29 ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 13.569 -23.021 4.178  1.00 18.06 ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 13.227 -21.354 2.739  1.00 22.02 ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 16.339 -24.275 2.593  1.00 15.13 ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.683 -23.699 2.418  1.00 15.62 ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 18.569 -24.670 1.673  1.00 16.64 ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 19.407 -25.366 2.260  1.00 17.03 ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 18.287 -23.316 3.790  1.00 15.80 ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.428 -22.352 4.644  1.00 17.19 ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 18.013 -22.215 6.067  1.00 17.53 ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.258 -21.013 3.969  1.00 18.51 ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 18.369 -24.751 0.339  1.00 16.70 ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 19.040 -25.765 -0.463 1.00 18.17 ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 20.536 -25.595 -0.509 1.00 19.37 ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 21.259 -26.577 -0.676 1.00 21.32 ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 18.460 -25.798 -1.889 1.00 18.38 ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 16.945 -25.820 -2.012 1.00 19.10 ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 16.517 -25.949 -3.475 1.00 20.14 ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 16.306 -26.942 -1.144 1.00 18.58 ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 21.009 -24.335 -0.383 1.00 19.15 ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 22.438 -24.044 -0.427 1.00 19.56 ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 23.229 -24.650 0.757  1.00 20.74 ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 24.459 -24.733 0.684  1.00 21.30 ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 22.664 -22.525 -0.514 1.00 19.67 ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 21.984 -21.736 0.567  1.00 19.11 ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 20.750 -21.156 0.518  1.00 19.77 ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 22.521 -21.447 1.882  1.00 19.12 ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 20.491 -20.504 1.716  1.00 20.18 ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 21.575 -20.655 2.555  1.00 19.84 ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 23.750 -21.728 2.515  1.00 20.16 ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 21.772 -20.229 3.876  1.00 20.83 ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 23.973 -21.237 3.799  1.00 21.28 ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 23.008 -20.468 4.446  1.00 21.10 ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 22.538 -25.132 1.824  1.00 20.53 ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 23.259 -25.756 2.945  1.00 20.89 ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 24.017 -27.016 2.494  1.00 24.85 ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 25.020 -27.354 3.131  1.00 25.12 ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 22.273 -26.137 4.079  1.00 18.99 ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 21.778 -24.978 4.948  1.00 18.09 ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 20.731 -25.496 5.932  1.00 17.85 ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 22.944 -24.312 5.736  1.00 18.37 ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 23.511 -27.702 1.434  1.00 27.28 ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 24.034 -28.959 0.871  1.00 31.73 ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 25.177 -28.794 -0.101 1.00 35.50 ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 25.636 -29.809 -0.627 1.00 36.46 ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 22.941 -29.712 0.096  1.00 34.73 ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 21.768 -30.214 0.889  1.00 40.66 ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 21.932 -30.473 2.095  1.00 42.91 ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 20.675 -30.363 0.294  1.00 44.26 ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 25.576 -27.564 -0.435 1.00 37.20 ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 26.686 -27.359 -1.368 1.00 40.53 ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 27.698 -26.364 -0.810 1.00 42.64 ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 28.799 -26.246 -1.355 1.00 44.30 ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 26.172 -26.911 -2.743 1.00 43.93 ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 25.448 -25.579 -2.720 1.00 50.36 ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 24.210 -25.544 -3.593 1.00 60.45 ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 24.015 -24.539 -4.316 1.00 63.01 ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 23.432 -26.524 -3.552 1.00 63.45 ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1B4N C 2 .   ? 26.433 12.292  8.821  1.00 22.38 ? 201 A1B4N A N1  1 
HETATM 2156 N  N3  . A1B4N C 2 .   ? 23.799 13.813  15.042 1.00 18.88 ? 201 A1B4N A N3  1 
HETATM 2157 C  C4  . A1B4N C 2 .   ? 25.074 10.588  9.931  1.00 22.36 ? 201 A1B4N A C4  1 
HETATM 2158 C  C5  . A1B4N C 2 .   ? 26.060 10.944  9.020  1.00 22.37 ? 201 A1B4N A C5  1 
HETATM 2159 C  C6  . A1B4N C 2 .   ? 24.522 14.421  9.823  1.00 21.33 ? 201 A1B4N A C6  1 
HETATM 2160 C  C7  . A1B4N C 2 .   ? 23.110 14.548  10.374 1.00 21.58 ? 201 A1B4N A C7  1 
HETATM 2161 C  C8  . A1B4N C 2 .   ? 23.123 15.088  11.803 1.00 20.82 ? 201 A1B4N A C8  1 
HETATM 2162 C  C10 . A1B4N C 2 .   ? 24.122 14.702  14.107 1.00 20.02 ? 201 A1B4N A C10 1 
HETATM 2163 O  O3  . A1B4N C 2 .   ? 24.595 15.816  14.376 1.00 19.72 ? 201 A1B4N A O3  1 
HETATM 2164 C  C9  . A1B4N C 2 .   ? 24.027 14.210  12.672 1.00 19.86 ? 201 A1B4N A C9  1 
HETATM 2165 C  C11 . A1B4N C 2 .   ? 25.459 14.234  12.145 1.00 20.04 ? 201 A1B4N A C11 1 
HETATM 2166 N  N2  . A1B4N C 2 .   ? 25.527 13.817  10.730 1.00 20.60 ? 201 A1B4N A N2  1 
HETATM 2167 S  S   . A1B4N C 2 .   ? 26.897 13.227  10.107 1.00 21.13 ? 201 A1B4N A S   1 
HETATM 2168 O  O1  . A1B4N C 2 .   ? 27.539 12.487  11.145 1.00 20.69 ? 201 A1B4N A O1  1 
HETATM 2169 O  O2  . A1B4N C 2 .   ? 27.570 14.356  9.542  1.00 23.29 ? 201 A1B4N A O2  1 
HETATM 2170 C  C1  . A1B4N C 2 .   ? 26.714 9.950   8.302  1.00 22.79 ? 201 A1B4N A C1  1 
HETATM 2171 O  O   . A1B4N C 2 .   ? 27.570 10.387  7.342  1.00 24.05 ? 201 A1B4N A O   1 
HETATM 2172 C  C   . A1B4N C 2 .   ? 28.421 9.416   6.713  1.00 24.14 ? 201 A1B4N A C   1 
HETATM 2173 C  C3  . A1B4N C 2 .   ? 24.810 9.242   10.115 1.00 22.42 ? 201 A1B4N A C3  1 
HETATM 2174 C  C2  . A1B4N C 2 .   ? 25.539 8.329   9.399  1.00 22.47 ? 201 A1B4N A C2  1 
HETATM 2175 N  N   . A1B4N C 2 .   ? 26.475 8.661   8.490  1.00 22.21 ? 201 A1B4N A N   1 
HETATM 2176 ZN ZN  . ZN    D 3 .   ? 23.120 -5.671  26.964 1.00 17.82 2 202 ZN    A ZN  1 
HETATM 2177 S  S   . DMS   E 4 .   ? 20.477 20.152  25.251 1.00 63.72 ? 203 DMS   A S   1 
HETATM 2178 O  O   . DMS   E 4 .   ? 20.592 20.806  23.903 1.00 63.47 ? 203 DMS   A O   1 
HETATM 2179 C  C1  . DMS   E 4 .   ? 21.895 20.676  26.264 1.00 63.70 ? 203 DMS   A C1  1 
HETATM 2180 C  C2  . DMS   E 4 .   ? 19.206 21.030  26.215 1.00 63.68 ? 203 DMS   A C2  1 
HETATM 2181 N  N1  . A1B4N F 2 .   ? 9.729  -18.624 24.391 1.00 18.02 ? 201 A1B4N C N1  1 
HETATM 2182 N  N3  . A1B4N F 2 .   ? 11.966 -16.925 18.106 1.00 14.98 ? 201 A1B4N C N3  1 
HETATM 2183 C  C4  . A1B4N F 2 .   ? 10.918 -20.310 23.098 1.00 18.46 ? 201 A1B4N C C4  1 
HETATM 2184 C  C5  . A1B4N F 2 .   ? 10.002 -19.979 24.087 1.00 18.18 ? 201 A1B4N C C5  1 
HETATM 2185 C  C6  . A1B4N F 2 .   ? 11.662 -16.387 23.391 1.00 17.55 ? 201 A1B4N C C6  1 
HETATM 2186 C  C7  . A1B4N F 2 .   ? 13.042 -16.318 22.745 1.00 16.70 ? 201 A1B4N C C7  1 
HETATM 2187 C  C8  . A1B4N F 2 .   ? 12.964 -15.773 21.319 1.00 15.20 ? 201 A1B4N C C8  1 
HETATM 2188 C  C10 . A1B4N F 2 .   ? 11.774 -16.041 19.091 1.00 15.06 ? 201 A1B4N C C10 1 
HETATM 2189 O  O3  . A1B4N F 2 .   ? 11.383 -14.873 18.902 1.00 14.81 ? 201 A1B4N C O3  1 
HETATM 2190 C  C9  . A1B4N F 2 .   ? 11.947 -16.582 20.499 1.00 14.35 ? 201 A1B4N C C9  1 
HETATM 2191 C  C11 . A1B4N F 2 .   ? 10.563 -16.528 21.148 1.00 15.13 ? 201 A1B4N C C11 1 
HETATM 2192 N  N2  . A1B4N F 2 .   ? 10.609 -16.996 22.547 1.00 17.12 ? 201 A1B4N C N2  1 
HETATM 2193 S  S   . A1B4N F 2 .   ? 9.258  -17.595 23.257 1.00 17.20 ? 201 A1B4N C S   1 
HETATM 2194 O  O1  . A1B4N F 2 .   ? 8.492  -18.189 22.210 1.00 15.61 ? 201 A1B4N C O1  1 
HETATM 2195 O  O2  . A1B4N F 2 .   ? 8.708  -16.488 23.974 1.00 19.18 ? 201 A1B4N C O2  1 
HETATM 2196 C  C1  . A1B4N F 2 .   ? 9.346  -21.007 24.781 1.00 18.73 ? 201 A1B4N C C1  1 
HETATM 2197 O  O   . A1B4N F 2 .   ? 8.509  -20.613 25.762 1.00 19.68 ? 201 A1B4N C O   1 
HETATM 2198 C  C   . A1B4N F 2 .   ? 7.698  -21.617 26.389 1.00 20.14 ? 201 A1B4N C C   1 
HETATM 2199 C  C3  . A1B4N F 2 .   ? 11.104 -21.652 22.816 1.00 19.03 ? 201 A1B4N C C3  1 
HETATM 2200 C  C2  . A1B4N F 2 .   ? 10.384 -22.594 23.524 1.00 18.31 ? 201 A1B4N C C2  1 
HETATM 2201 N  N   . A1B4N F 2 .   ? 9.524  -22.291 24.511 1.00 17.84 ? 201 A1B4N C N   1 
HETATM 2202 ZN ZN  . ZN    G 3 .   ? 10.588 -35.760 5.565  1.00 14.77 2 202 ZN    C ZN  1 
HETATM 2203 S  S   . DMS   H 4 .   ? 14.436 -10.863 6.925  1.00 72.53 ? 203 DMS   C S   1 
HETATM 2204 O  O   . DMS   H 4 .   ? 14.481 -10.377 8.356  1.00 72.16 ? 203 DMS   C O   1 
HETATM 2205 C  C1  . DMS   H 4 .   ? 12.849 -10.364 6.198  1.00 72.60 ? 203 DMS   C C1  1 
HETATM 2206 C  C2  . DMS   H 4 .   ? 15.466 -9.746  5.930  1.00 72.51 ? 203 DMS   C C2  1 
HETATM 2207 O  O   . HOH   I 5 .   ? 32.188 22.628  11.557 1.00 35.60 ? 301 HOH   A O   1 
HETATM 2208 O  O   . HOH   I 5 .   ? 14.839 22.294  24.527 1.00 27.86 ? 302 HOH   A O   1 
HETATM 2209 O  O   . HOH   I 5 .   ? 11.581 -1.543  27.990 1.00 23.63 ? 303 HOH   A O   1 
HETATM 2210 O  O   . HOH   I 5 .   ? 23.953 7.375   28.195 1.00 23.95 ? 304 HOH   A O   1 
HETATM 2211 O  O   . HOH   I 5 .   ? 13.050 -4.590  20.270 1.00 33.28 ? 305 HOH   A O   1 
HETATM 2212 O  O   . HOH   I 5 .   ? 11.194 21.397  24.434 1.00 27.42 ? 306 HOH   A O   1 
HETATM 2213 O  O   . HOH   I 5 .   ? 32.137 7.280   23.107 1.00 36.53 ? 307 HOH   A O   1 
HETATM 2214 O  O   . HOH   I 5 .   ? 14.424 -5.347  26.982 1.00 22.17 ? 308 HOH   A O   1 
HETATM 2215 O  O   . HOH   I 5 .   ? 0.387  19.837  20.339 1.00 38.32 ? 309 HOH   A O   1 
HETATM 2216 O  O   . HOH   I 5 .   ? 17.818 -7.536  21.556 1.00 23.61 ? 310 HOH   A O   1 
HETATM 2217 O  O   . HOH   I 5 .   ? 5.130  -5.026  22.498 1.00 49.44 ? 311 HOH   A O   1 
HETATM 2218 O  O   . HOH   I 5 .   ? 31.052 -5.335  11.584 1.00 31.91 ? 312 HOH   A O   1 
HETATM 2219 O  O   . HOH   I 5 .   ? 22.513 6.621   1.609  1.00 24.36 ? 313 HOH   A O   1 
HETATM 2220 O  O   . HOH   I 5 .   ? 37.112 7.603   3.947  1.00 37.75 ? 314 HOH   A O   1 
HETATM 2221 O  O   . HOH   I 5 .   ? 12.335 18.020  13.146 1.00 35.46 ? 315 HOH   A O   1 
HETATM 2222 O  O   . HOH   I 5 .   ? 16.092 -0.732  4.781  1.00 28.35 ? 316 HOH   A O   1 
HETATM 2223 O  O   . HOH   I 5 .   ? 30.706 5.293   8.020  1.00 24.04 ? 317 HOH   A O   1 
HETATM 2224 O  O   . HOH   I 5 .   ? 27.128 19.256  15.119 1.00 21.56 ? 318 HOH   A O   1 
HETATM 2225 O  O   . HOH   I 5 .   ? 15.078 8.681   13.350 1.00 14.54 ? 319 HOH   A O   1 
HETATM 2226 O  O   . HOH   I 5 .   ? 18.458 -11.610 27.207 1.00 27.29 ? 320 HOH   A O   1 
HETATM 2227 O  O   . HOH   I 5 .   ? 11.205 -0.094  15.955 1.00 20.36 ? 321 HOH   A O   1 
HETATM 2228 O  O   . HOH   I 5 .   ? 6.511  2.897   28.932 1.00 36.79 ? 322 HOH   A O   1 
HETATM 2229 O  O   . HOH   I 5 .   ? 32.115 2.925   5.017  1.00 31.49 ? 323 HOH   A O   1 
HETATM 2230 O  O   . HOH   I 5 .   ? -1.820 15.604  20.348 1.00 24.99 ? 324 HOH   A O   1 
HETATM 2231 O  O   . HOH   I 5 .   ? 7.260  7.647   31.775 1.00 38.70 ? 325 HOH   A O   1 
HETATM 2232 O  O   . HOH   I 5 .   ? 8.928  3.961   11.973 1.00 33.94 ? 326 HOH   A O   1 
HETATM 2233 O  O   . HOH   I 5 .   ? 34.863 14.998  25.505 1.00 47.80 ? 327 HOH   A O   1 
HETATM 2234 O  O   . HOH   I 5 .   ? 34.510 -0.890  16.515 1.00 13.52 ? 328 HOH   A O   1 
HETATM 2235 O  O   . HOH   I 5 .   ? 17.198 20.775  22.932 1.00 18.67 ? 329 HOH   A O   1 
HETATM 2236 O  O   . HOH   I 5 .   ? 23.739 1.840   -0.825 1.00 17.01 ? 330 HOH   A O   1 
HETATM 2237 O  O   . HOH   I 5 .   ? 20.111 2.041   9.295  1.00 13.84 ? 331 HOH   A O   1 
HETATM 2238 O  O   . HOH   I 5 .   ? 23.784 16.620  27.372 1.00 36.72 ? 332 HOH   A O   1 
HETATM 2239 O  O   . HOH   I 5 .   ? 25.616 17.911  12.856 1.00 19.26 ? 333 HOH   A O   1 
HETATM 2240 O  O   . HOH   I 5 .   ? 29.749 7.213   4.392  1.00 32.11 ? 334 HOH   A O   1 
HETATM 2241 O  O   . HOH   I 5 .   ? 29.435 26.054  16.337 1.00 51.02 ? 335 HOH   A O   1 
HETATM 2242 O  O   . HOH   I 5 .   ? 24.155 3.836   29.279 1.00 22.24 ? 336 HOH   A O   1 
HETATM 2243 O  O   . HOH   I 5 .   ? 6.800  -1.862  24.133 1.00 27.06 ? 337 HOH   A O   1 
HETATM 2244 O  O   . HOH   I 5 .   ? 28.833 17.367  8.494  1.00 34.14 ? 338 HOH   A O   1 
HETATM 2245 O  O   . HOH   I 5 .   ? 28.906 16.148  11.165 1.00 44.30 ? 339 HOH   A O   1 
HETATM 2246 O  O   . HOH   I 5 .   ? 5.202  11.053  12.428 1.00 29.58 ? 340 HOH   A O   1 
HETATM 2247 O  O   . HOH   I 5 .   ? 23.004 20.833  20.519 1.00 26.90 ? 341 HOH   A O   1 
HETATM 2248 O  O   . HOH   I 5 .   ? 0.244  5.557   28.901 1.00 53.56 ? 342 HOH   A O   1 
HETATM 2249 O  O   . HOH   I 5 .   ? 22.880 -6.190  0.608  1.00 56.01 ? 343 HOH   A O   1 
HETATM 2250 O  O   . HOH   I 5 .   ? 11.561 13.200  8.696  1.00 58.25 ? 344 HOH   A O   1 
HETATM 2251 O  O   . HOH   I 5 .   ? 25.123 4.236   -1.182 1.00 21.93 ? 345 HOH   A O   1 
HETATM 2252 O  O   . HOH   I 5 .   ? 23.541 10.982  21.501 1.00 11.91 ? 346 HOH   A O   1 
HETATM 2253 O  O   . HOH   I 5 .   ? 28.554 -6.141  3.477  1.00 27.24 ? 347 HOH   A O   1 
HETATM 2254 O  O   . HOH   I 5 .   ? 13.874 -1.902  30.143 1.00 33.20 ? 348 HOH   A O   1 
HETATM 2255 O  O   . HOH   I 5 .   ? 17.980 20.346  13.645 1.00 27.51 ? 349 HOH   A O   1 
HETATM 2256 O  O   . HOH   I 5 .   ? 31.832 13.114  15.211 1.00 39.28 ? 350 HOH   A O   1 
HETATM 2257 O  O   . HOH   I 5 .   ? 6.873  15.714  29.151 1.00 38.48 ? 351 HOH   A O   1 
HETATM 2258 O  O   . HOH   I 5 .   ? 28.071 3.126   -0.300 1.00 23.72 ? 352 HOH   A O   1 
HETATM 2259 O  O   . HOH   I 5 .   ? 11.169 10.631  10.605 1.00 40.92 ? 353 HOH   A O   1 
HETATM 2260 O  O   . HOH   I 5 .   ? 16.557 18.744  26.982 1.00 36.92 ? 354 HOH   A O   1 
HETATM 2261 O  O   . HOH   I 5 .   ? 4.210  10.012  17.926 1.00 33.10 ? 355 HOH   A O   1 
HETATM 2262 O  O   . HOH   I 5 .   ? 17.215 2.117   9.349  1.00 20.51 ? 356 HOH   A O   1 
HETATM 2263 O  O   . HOH   I 5 .   ? 5.162  3.110   21.054 1.00 19.39 ? 357 HOH   A O   1 
HETATM 2264 O  O   . HOH   I 5 .   ? 4.077  20.034  21.575 1.00 24.59 ? 358 HOH   A O   1 
HETATM 2265 O  O   . HOH   I 5 .   ? 22.015 8.885   2.917  1.00 24.72 ? 359 HOH   A O   1 
HETATM 2266 O  O   . HOH   I 5 .   ? 16.797 4.485   5.908  1.00 26.77 ? 360 HOH   A O   1 
HETATM 2267 O  O   . HOH   I 5 .   ? 21.640 9.880   23.372 1.00 12.91 ? 361 HOH   A O   1 
HETATM 2268 O  O   . HOH   I 5 .   ? 4.821  10.600  14.534 1.00 36.12 ? 362 HOH   A O   1 
HETATM 2269 O  O   . HOH   I 5 .   ? 34.887 -6.543  21.567 1.00 39.34 ? 363 HOH   A O   1 
HETATM 2270 O  O   . HOH   I 5 .   ? 12.668 -6.114  22.268 1.00 22.06 ? 364 HOH   A O   1 
HETATM 2271 O  O   . HOH   I 5 .   ? 20.178 11.901  8.580  1.00 21.09 ? 365 HOH   A O   1 
HETATM 2272 O  O   . HOH   I 5 .   ? 20.554 -12.663 28.368 1.00 41.86 ? 366 HOH   A O   1 
HETATM 2273 O  O   . HOH   I 5 .   ? 13.538 18.803  14.688 1.00 28.49 ? 367 HOH   A O   1 
HETATM 2274 O  O   . HOH   I 5 .   ? 30.422 -5.826  26.389 1.00 30.44 ? 368 HOH   A O   1 
HETATM 2275 O  O   . HOH   I 5 .   ? 4.432  4.223   28.127 1.00 31.43 ? 369 HOH   A O   1 
HETATM 2276 O  O   . HOH   I 5 .   ? 3.475  18.222  23.661 1.00 26.32 ? 370 HOH   A O   1 
HETATM 2277 O  O   . HOH   I 5 .   ? 4.241  20.405  15.286 1.00 35.18 ? 371 HOH   A O   1 
HETATM 2278 O  O   . HOH   I 5 .   ? 25.515 1.447   29.861 1.00 25.77 ? 372 HOH   A O   1 
HETATM 2279 O  O   . HOH   I 5 .   ? 19.564 -6.230  32.633 1.00 41.86 ? 373 HOH   A O   1 
HETATM 2280 O  O   . HOH   I 5 .   ? 17.299 18.538  15.537 1.00 16.05 ? 374 HOH   A O   1 
HETATM 2281 O  O   . HOH   I 5 .   ? 27.202 -8.758  8.509  1.00 31.52 ? 375 HOH   A O   1 
HETATM 2282 O  O   . HOH   I 5 .   ? 20.023 -5.029  15.329 1.00 27.77 ? 376 HOH   A O   1 
HETATM 2283 O  O   . HOH   I 5 .   ? 29.732 -2.184  8.340  1.00 20.42 ? 377 HOH   A O   1 
HETATM 2284 O  O   . HOH   I 5 .   ? 16.435 8.970   6.741  1.00 24.72 ? 378 HOH   A O   1 
HETATM 2285 O  O   . HOH   I 5 .   ? 30.279 12.426  7.661  1.00 31.74 ? 379 HOH   A O   1 
HETATM 2286 O  O   . HOH   I 5 .   ? 24.786 -8.785  24.654 1.00 26.50 ? 380 HOH   A O   1 
HETATM 2287 O  O   . HOH   I 5 .   ? 17.175 0.288   2.534  1.00 33.76 ? 381 HOH   A O   1 
HETATM 2288 O  O   . HOH   I 5 .   ? 34.628 3.240   26.221 1.00 31.50 ? 382 HOH   A O   1 
HETATM 2289 O  O   . HOH   I 5 .   ? 29.676 0.917   25.106 1.00 43.56 ? 383 HOH   A O   1 
HETATM 2290 O  O   . HOH   I 5 .   ? 27.963 13.131  6.493  1.00 41.91 ? 384 HOH   A O   1 
HETATM 2291 O  O   . HOH   I 5 .   ? 34.163 0.507   8.537  1.00 19.21 ? 385 HOH   A O   1 
HETATM 2292 O  O   . HOH   I 5 .   ? 2.796  8.642   26.108 1.00 31.52 ? 386 HOH   A O   1 
HETATM 2293 O  O   . HOH   I 5 .   ? 30.662 -3.105  11.868 1.00 26.27 ? 387 HOH   A O   1 
HETATM 2294 O  O   . HOH   I 5 .   ? 14.848 -4.052  16.103 1.00 26.42 ? 388 HOH   A O   1 
HETATM 2295 O  O   . HOH   I 5 .   ? 28.483 0.703   26.859 1.00 20.88 ? 389 HOH   A O   1 
HETATM 2296 O  O   . HOH   I 5 .   ? 26.610 -7.866  24.071 1.00 34.56 ? 390 HOH   A O   1 
HETATM 2297 O  O   . HOH   I 5 .   ? 21.640 -11.496 30.846 1.00 47.47 ? 391 HOH   A O   1 
HETATM 2298 O  O   . HOH   I 5 .   ? 20.550 13.603  6.461  1.00 32.91 ? 392 HOH   A O   1 
HETATM 2299 O  O   . HOH   I 5 .   ? 24.116 18.059  6.346  1.00 48.22 ? 393 HOH   A O   1 
HETATM 2300 O  O   . HOH   I 5 .   ? 29.858 6.316   29.959 1.00 32.86 ? 394 HOH   A O   1 
HETATM 2301 O  O   . HOH   I 5 .   ? 12.164 -2.654  15.879 1.00 28.62 ? 395 HOH   A O   1 
HETATM 2302 O  O   . HOH   I 5 .   ? 22.533 -8.329  19.370 1.00 27.88 ? 396 HOH   A O   1 
HETATM 2303 O  O   . HOH   I 5 .   ? 35.255 13.974  16.355 1.00 31.19 ? 397 HOH   A O   1 
HETATM 2304 O  O   . HOH   I 5 .   ? 32.110 8.780   4.758  1.00 33.15 ? 398 HOH   A O   1 
HETATM 2305 O  O   . HOH   I 5 .   ? 31.015 10.721  14.469 1.00 34.53 ? 399 HOH   A O   1 
HETATM 2306 O  O   . HOH   I 5 .   ? 2.588  1.426   28.117 1.00 45.12 ? 400 HOH   A O   1 
HETATM 2307 O  O   . HOH   I 5 .   ? 17.567 22.346  15.710 1.00 32.63 ? 401 HOH   A O   1 
HETATM 2308 O  O   . HOH   I 5 .   ? 18.829 10.577  31.635 1.00 49.41 ? 402 HOH   A O   1 
HETATM 2309 O  O   . HOH   I 5 .   ? 17.931 -5.266  30.409 1.00 30.25 ? 403 HOH   A O   1 
HETATM 2310 O  O   . HOH   I 5 .   ? 16.222 -0.627  12.851 1.00 21.13 ? 404 HOH   A O   1 
HETATM 2311 O  O   . HOH   I 5 .   ? 29.423 25.933  13.616 1.00 30.11 ? 405 HOH   A O   1 
HETATM 2312 O  O   . HOH   I 5 .   ? 26.798 -6.525  29.702 1.00 39.82 ? 406 HOH   A O   1 
HETATM 2313 O  O   . HOH   I 5 .   ? 14.447 1.458   13.596 1.00 29.97 ? 407 HOH   A O   1 
HETATM 2314 O  O   . HOH   I 5 .   ? 20.486 23.586  15.001 1.00 47.68 ? 408 HOH   A O   1 
HETATM 2315 O  O   . HOH   I 5 .   ? 35.661 14.385  20.424 1.00 29.33 ? 409 HOH   A O   1 
HETATM 2316 O  O   . HOH   I 5 .   ? 12.306 18.536  26.440 1.00 25.10 ? 410 HOH   A O   1 
HETATM 2317 O  O   . HOH   I 5 .   ? 20.080 13.931  29.004 1.00 31.91 ? 411 HOH   A O   1 
HETATM 2318 O  O   . HOH   I 5 .   ? 18.337 -3.763  14.788 1.00 32.17 ? 412 HOH   A O   1 
HETATM 2319 O  O   . HOH   I 5 .   ? 32.004 14.943  12.880 1.00 31.53 ? 413 HOH   A O   1 
HETATM 2320 O  O   . HOH   I 5 .   ? 30.210 -2.167  3.432  1.00 41.33 ? 414 HOH   A O   1 
HETATM 2321 O  O   . HOH   I 5 .   ? 3.536  2.503   18.920 1.00 30.57 ? 415 HOH   A O   1 
HETATM 2322 O  O   . HOH   I 5 .   ? 15.829 12.331  30.701 1.00 36.51 ? 416 HOH   A O   1 
HETATM 2323 O  O   . HOH   I 5 .   ? 6.861  16.367  8.846  1.00 32.84 ? 417 HOH   A O   1 
HETATM 2324 O  O   . HOH   I 5 .   ? 3.958  14.824  10.380 1.00 24.21 ? 418 HOH   A O   1 
HETATM 2325 O  O   . HOH   I 5 .   ? 17.540 16.802  28.620 1.00 44.24 ? 419 HOH   A O   1 
HETATM 2326 O  O   . HOH   I 5 .   ? 27.867 25.002  19.602 1.00 52.76 ? 420 HOH   A O   1 
HETATM 2327 O  O   . HOH   I 5 .   ? 28.653 22.109  22.364 1.00 30.42 ? 421 HOH   A O   1 
HETATM 2328 O  O   . HOH   I 5 .   ? 28.058 11.963  27.671 1.00 22.14 ? 422 HOH   A O   1 
HETATM 2329 O  O   . HOH   I 5 .   ? 32.800 12.097  27.888 1.00 32.91 ? 423 HOH   A O   1 
HETATM 2330 O  O   . HOH   I 5 .   ? 33.137 -2.843  15.310 1.00 25.70 ? 424 HOH   A O   1 
HETATM 2331 O  O   . HOH   I 5 .   ? 25.719 8.860   1.059  1.00 32.42 ? 425 HOH   A O   1 
HETATM 2332 O  O   . HOH   I 5 .   ? -1.382 11.140  19.461 1.00 38.83 ? 426 HOH   A O   1 
HETATM 2333 O  O   . HOH   I 5 .   ? 13.279 8.603   11.118 1.00 20.70 ? 427 HOH   A O   1 
HETATM 2334 O  O   . HOH   I 5 .   ? 11.189 2.213   12.449 1.00 25.61 ? 428 HOH   A O   1 
HETATM 2335 O  O   . HOH   I 5 .   ? 25.268 20.602  22.112 1.00 37.49 ? 429 HOH   A O   1 
HETATM 2336 O  O   . HOH   I 5 .   ? 32.759 5.453   4.835  1.00 50.87 ? 430 HOH   A O   1 
HETATM 2337 O  O   . HOH   I 5 .   ? 2.274  13.993  25.108 1.00 50.36 ? 431 HOH   A O   1 
HETATM 2338 O  O   . HOH   I 5 .   ? 15.224 23.319  16.834 1.00 22.06 ? 432 HOH   A O   1 
HETATM 2339 O  O   . HOH   I 5 .   ? 20.191 23.907  22.842 1.00 64.01 ? 433 HOH   A O   1 
HETATM 2340 O  O   . HOH   I 5 .   ? 31.947 -7.067  17.814 1.00 35.33 ? 434 HOH   A O   1 
HETATM 2341 O  O   . HOH   I 5 .   ? 10.907 6.994   11.417 1.00 39.14 ? 435 HOH   A O   1 
HETATM 2342 O  O   . HOH   I 5 .   ? 15.818 8.469   34.109 1.00 31.08 ? 436 HOH   A O   1 
HETATM 2343 O  O   . HOH   I 5 .   ? 16.215 -5.123  12.350 1.00 31.99 ? 437 HOH   A O   1 
HETATM 2344 O  O   . HOH   I 5 .   ? 24.556 -5.425  33.028 1.00 41.14 ? 438 HOH   A O   1 
HETATM 2345 O  O   . HOH   I 5 .   ? 27.305 16.474  6.698  1.00 53.93 ? 439 HOH   A O   1 
HETATM 2346 O  O   . HOH   I 5 .   ? 16.152 7.111   4.516  1.00 40.48 ? 440 HOH   A O   1 
HETATM 2347 O  O   . HOH   I 5 .   ? 18.012 10.947  6.597  1.00 30.81 ? 441 HOH   A O   1 
HETATM 2348 O  O   . HOH   I 5 .   ? 9.007  18.098  8.706  1.00 41.16 ? 442 HOH   A O   1 
HETATM 2349 O  O   . HOH   I 5 .   ? 33.045 0.719   6.121  1.00 34.88 ? 443 HOH   A O   1 
HETATM 2350 O  O   . HOH   I 5 .   ? 23.402 23.023  18.982 1.00 37.22 ? 444 HOH   A O   1 
HETATM 2351 O  O   . HOH   I 5 .   ? 27.836 12.059  3.893  1.00 45.94 ? 445 HOH   A O   1 
HETATM 2352 O  O   . HOH   I 5 .   ? 13.935 21.682  14.835 1.00 23.63 ? 446 HOH   A O   1 
HETATM 2353 O  O   . HOH   I 5 .   ? 28.166 1.550   29.321 1.00 34.44 ? 447 HOH   A O   1 
HETATM 2354 O  O   . HOH   I 5 .   ? 5.391  7.225   35.367 1.00 60.82 ? 448 HOH   A O   1 
HETATM 2355 O  O   . HOH   I 5 .   ? 33.766 -2.166  9.161  1.00 26.13 ? 449 HOH   A O   1 
HETATM 2356 O  O   . HOH   I 5 .   ? 18.240 13.192  30.595 1.00 49.73 ? 450 HOH   A O   1 
HETATM 2357 O  O   . HOH   I 5 .   ? 2.111  21.633  20.318 1.00 34.20 ? 451 HOH   A O   1 
HETATM 2358 O  O   . HOH   I 5 .   ? 31.866 11.494  5.598  1.00 37.13 ? 452 HOH   A O   1 
HETATM 2359 O  O   . HOH   I 5 .   ? 8.878  -2.127  27.832 1.00 53.48 ? 453 HOH   A O   1 
HETATM 2360 O  O   . HOH   I 5 .   ? 9.462  22.144  12.244 1.00 29.24 ? 454 HOH   A O   1 
HETATM 2361 O  O   . HOH   I 5 .   ? 31.397 -3.855  9.690  1.00 28.58 ? 455 HOH   A O   1 
HETATM 2362 O  O   . HOH   I 5 .   ? 2.933  4.109   17.008 1.00 37.83 ? 456 HOH   A O   1 
HETATM 2363 O  O   . HOH   I 5 .   ? 16.414 -3.352  13.972 1.00 30.41 ? 457 HOH   A O   1 
HETATM 2364 O  O   . HOH   I 5 .   ? 32.892 -5.736  25.826 1.00 51.19 ? 458 HOH   A O   1 
HETATM 2365 O  O   . HOH   I 5 .   ? 28.584 4.017   30.489 1.00 45.21 ? 459 HOH   A O   1 
HETATM 2366 O  O   . HOH   I 5 .   ? 15.078 -3.984  10.133 1.00 57.19 ? 460 HOH   A O   1 
HETATM 2367 O  O   . HOH   I 5 .   ? 4.681  18.055  28.447 1.00 67.70 ? 461 HOH   A O   1 
HETATM 2368 O  O   . HOH   I 5 .   ? 27.768 9.289   2.920  1.00 32.45 ? 462 HOH   A O   1 
HETATM 2369 O  O   . HOH   I 5 .   ? 35.218 11.545  15.628 1.00 44.28 ? 463 HOH   A O   1 
HETATM 2370 O  O   . HOH   I 5 .   ? 4.650  1.063   14.672 1.00 46.14 ? 464 HOH   A O   1 
HETATM 2371 O  O   . HOH   I 5 .   ? 25.011 24.773  19.988 1.00 43.94 ? 465 HOH   A O   1 
HETATM 2372 O  O   . HOH   I 5 .   ? 1.973  17.725  27.834 1.00 57.47 ? 466 HOH   A O   1 
HETATM 2373 O  O   . HOH   J 5 .   ? 20.474 -8.508  7.775  1.00 26.19 ? 301 HOH   C O   1 
HETATM 2374 O  O   . HOH   J 5 .   ? 13.031 -14.312 4.889  1.00 41.19 ? 302 HOH   C O   1 
HETATM 2375 O  O   . HOH   J 5 .   ? 35.785 -15.532 15.927 1.00 28.63 ? 303 HOH   C O   1 
HETATM 2376 O  O   . HOH   J 5 .   ? 22.867 -36.229 12.343 1.00 39.73 ? 304 HOH   C O   1 
HETATM 2377 O  O   . HOH   J 5 .   ? 23.623 -37.579 9.222  1.00 47.00 ? 305 HOH   C O   1 
HETATM 2378 O  O   . HOH   J 5 .   ? 12.372 -29.605 33.429 1.00 22.13 ? 306 HOH   C O   1 
HETATM 2379 O  O   . HOH   J 5 .   ? 2.776  -23.058 10.597 1.00 26.11 ? 307 HOH   C O   1 
HETATM 2380 O  O   . HOH   J 5 .   ? 30.958 -10.585 10.460 1.00 30.53 ? 308 HOH   C O   1 
HETATM 2381 O  O   . HOH   J 5 .   ? 10.168 -22.933 4.899  1.00 21.07 ? 309 HOH   C O   1 
HETATM 2382 O  O   . HOH   J 5 .   ? 14.167 -19.851 0.820  1.00 31.86 ? 310 HOH   C O   1 
HETATM 2383 O  O   . HOH   J 5 .   ? 23.533 -31.437 15.199 1.00 23.32 ? 311 HOH   C O   1 
HETATM 2384 O  O   . HOH   J 5 .   ? 17.234 -38.075 3.142  1.00 35.34 ? 312 HOH   C O   1 
HETATM 2385 O  O   . HOH   J 5 .   ? 23.970 -9.334  7.989  1.00 25.08 ? 313 HOH   C O   1 
HETATM 2386 O  O   . HOH   J 5 .   ? 7.196  -39.178 6.954  1.00 44.41 ? 314 HOH   C O   1 
HETATM 2387 O  O   . HOH   J 5 .   ? 24.824 -20.625 20.683 1.00 36.18 ? 315 HOH   C O   1 
HETATM 2388 O  O   . HOH   J 5 .   ? 37.659 -17.395 11.486 1.00 34.12 ? 316 HOH   C O   1 
HETATM 2389 O  O   . HOH   J 5 .   ? 20.520 -22.492 18.777 1.00 14.25 ? 317 HOH   C O   1 
HETATM 2390 O  O   . HOH   J 5 .   ? 10.568 -27.728 33.519 1.00 33.08 ? 318 HOH   C O   1 
HETATM 2391 O  O   . HOH   J 5 .   ? 4.240  -36.093 21.511 1.00 26.69 ? 319 HOH   C O   1 
HETATM 2392 O  O   . HOH   J 5 .   ? 5.883  -18.328 25.719 1.00 24.58 ? 320 HOH   C O   1 
HETATM 2393 O  O   . HOH   J 5 .   ? 30.249 -25.564 17.771 1.00 38.01 ? 321 HOH   C O   1 
HETATM 2394 O  O   . HOH   J 5 .   ? 27.688 -15.319 2.712  1.00 34.82 ? 322 HOH   C O   1 
HETATM 2395 O  O   . HOH   J 5 .   ? 26.341 -33.113 6.076  1.00 40.70 ? 323 HOH   C O   1 
HETATM 2396 O  O   . HOH   J 5 .   ? 19.487 -36.453 26.828 1.00 43.02 ? 324 HOH   C O   1 
HETATM 2397 O  O   . HOH   J 5 .   ? 20.558 -15.708 26.090 1.00 33.72 ? 325 HOH   C O   1 
HETATM 2398 O  O   . HOH   J 5 .   ? 9.975  -26.287 3.572  1.00 19.12 ? 326 HOH   C O   1 
HETATM 2399 O  O   . HOH   J 5 .   ? -2.780 -24.740 26.194 1.00 32.99 ? 327 HOH   C O   1 
HETATM 2400 O  O   . HOH   J 5 .   ? 16.756 -14.114 4.229  1.00 44.17 ? 328 HOH   C O   1 
HETATM 2401 O  O   . HOH   J 5 .   ? 22.160 -32.582 3.797  1.00 27.22 ? 329 HOH   C O   1 
HETATM 2402 O  O   . HOH   J 5 .   ? 27.592 -27.781 2.338  1.00 45.02 ? 330 HOH   C O   1 
HETATM 2403 O  O   . HOH   J 5 .   ? 8.443  -28.436 2.972  1.00 20.17 ? 331 HOH   C O   1 
HETATM 2404 O  O   . HOH   J 5 .   ? 30.933 -21.512 13.131 1.00 31.86 ? 332 HOH   C O   1 
HETATM 2405 O  O   . HOH   J 5 .   ? 3.681  -23.523 3.804  1.00 25.89 ? 333 HOH   C O   1 
HETATM 2406 O  O   . HOH   J 5 .   ? 10.670 -12.785 20.553 1.00 17.80 ? 334 HOH   C O   1 
HETATM 2407 O  O   . HOH   J 5 .   ? 15.443 -29.044 23.149 1.00 15.32 ? 335 HOH   C O   1 
HETATM 2408 O  O   . HOH   J 5 .   ? 30.507 -20.304 19.191 1.00 25.42 ? 336 HOH   C O   1 
HETATM 2409 O  O   . HOH   J 5 .   ? 9.098  -11.388 18.539 1.00 17.57 ? 337 HOH   C O   1 
HETATM 2410 O  O   . HOH   J 5 .   ? 7.998  -13.917 22.947 1.00 31.32 ? 338 HOH   C O   1 
HETATM 2411 O  O   . HOH   J 5 .   ? 16.207 -39.001 10.312 1.00 43.78 ? 339 HOH   C O   1 
HETATM 2412 O  O   . HOH   J 5 .   ? 0.806  -31.722 17.040 1.00 14.05 ? 340 HOH   C O   1 
HETATM 2413 O  O   . HOH   J 5 .   ? 29.501 -28.115 10.045 1.00 22.55 ? 341 HOH   C O   1 
HETATM 2414 O  O   . HOH   J 5 .   ? 11.186 -36.494 31.501 1.00 31.67 ? 342 HOH   C O   1 
HETATM 2415 O  O   . HOH   J 5 .   ? 2.706  -31.067 3.911  1.00 31.43 ? 343 HOH   C O   1 
HETATM 2416 O  O   . HOH   J 5 .   ? 11.427 -19.689 11.568 1.00 13.57 ? 344 HOH   C O   1 
HETATM 2417 O  O   . HOH   J 5 .   ? 6.813  -23.531 29.244 1.00 33.54 ? 345 HOH   C O   1 
HETATM 2418 O  O   . HOH   J 5 .   ? -0.203 -19.180 21.610 1.00 35.87 ? 346 HOH   C O   1 
HETATM 2419 O  O   . HOH   J 5 .   ? 21.414 -36.683 9.941  1.00 32.29 ? 347 HOH   C O   1 
HETATM 2420 O  O   . HOH   J 5 .   ? 26.363 -22.865 -0.302 1.00 39.77 ? 348 HOH   C O   1 
HETATM 2421 O  O   . HOH   J 5 .   ? 5.960  -32.800 29.590 1.00 44.89 ? 349 HOH   C O   1 
HETATM 2422 O  O   . HOH   J 5 .   ? 17.950 -10.135 9.409  1.00 18.17 ? 350 HOH   C O   1 
HETATM 2423 O  O   . HOH   J 5 .   ? 23.673 -12.904 19.314 1.00 38.45 ? 351 HOH   C O   1 
HETATM 2424 O  O   . HOH   J 5 .   ? 28.913 -9.826  18.695 1.00 50.14 ? 352 HOH   C O   1 
HETATM 2425 O  O   . HOH   J 5 .   ? 19.931 -31.978 26.992 1.00 29.24 ? 353 HOH   C O   1 
HETATM 2426 O  O   . HOH   J 5 .   ? 8.329  -39.656 24.339 1.00 34.55 ? 354 HOH   C O   1 
HETATM 2427 O  O   . HOH   J 5 .   ? 26.419 -27.372 19.524 1.00 35.32 ? 355 HOH   C O   1 
HETATM 2428 O  O   . HOH   J 5 .   ? 18.403 -29.026 22.957 1.00 20.27 ? 356 HOH   C O   1 
HETATM 2429 O  O   . HOH   J 5 .   ? 34.876 -11.108 11.012 1.00 39.30 ? 357 HOH   C O   1 
HETATM 2430 O  O   . HOH   J 5 .   ? 30.643 -20.524 16.453 1.00 29.33 ? 358 HOH   C O   1 
HETATM 2431 O  O   . HOH   J 5 .   ? 11.143 -35.905 -0.581 1.00 35.84 ? 359 HOH   C O   1 
HETATM 2432 O  O   . HOH   J 5 .   ? 8.246  -5.457  14.482 1.00 29.77 ? 360 HOH   C O   1 
HETATM 2433 O  O   . HOH   J 5 .   ? 10.034 -40.883 1.136  1.00 48.73 ? 361 HOH   C O   1 
HETATM 2434 O  O   . HOH   J 5 .   ? 20.691 -29.520 18.170 1.00 28.76 ? 362 HOH   C O   1 
HETATM 2435 O  O   . HOH   J 5 .   ? 18.305 -11.951 5.501  1.00 36.57 ? 363 HOH   C O   1 
HETATM 2436 O  O   . HOH   J 5 .   ? 16.026 -19.088 24.163 1.00 19.59 ? 364 HOH   C O   1 
HETATM 2437 O  O   . HOH   J 5 .   ? 22.284 -12.392 17.323 1.00 21.68 ? 365 HOH   C O   1 
HETATM 2438 O  O   . HOH   J 5 .   ? 8.451  -12.992 25.472 1.00 45.97 ? 366 HOH   C O   1 
HETATM 2439 O  O   . HOH   J 5 .   ? 4.916  -30.938 -1.929 1.00 33.88 ? 367 HOH   C O   1 
HETATM 2440 O  O   . HOH   J 5 .   ? 8.674  -38.662 9.519  1.00 25.51 ? 368 HOH   C O   1 
HETATM 2441 O  O   . HOH   J 5 .   ? 31.398 -10.844 16.487 1.00 22.76 ? 369 HOH   C O   1 
HETATM 2442 O  O   . HOH   J 5 .   ? 8.711  -17.767 26.902 1.00 25.83 ? 370 HOH   C O   1 
HETATM 2443 O  O   . HOH   J 5 .   ? 10.717 -13.850 5.662  1.00 47.57 ? 371 HOH   C O   1 
HETATM 2444 O  O   . HOH   J 5 .   ? 6.975  -37.098 29.208 1.00 39.67 ? 372 HOH   C O   1 
HETATM 2445 O  O   . HOH   J 5 .   ? 19.759 -22.386 25.572 1.00 25.70 ? 373 HOH   C O   1 
HETATM 2446 O  O   . HOH   J 5 .   ? 5.338  -25.417 24.572 1.00 25.59 ? 374 HOH   C O   1 
HETATM 2447 O  O   . HOH   J 5 .   ? 1.077  -33.929 20.445 1.00 33.38 ? 375 HOH   C O   1 
HETATM 2448 O  O   . HOH   J 5 .   ? 13.141 -20.748 9.458  1.00 14.15 ? 376 HOH   C O   1 
HETATM 2449 O  O   . HOH   J 5 .   ? 29.683 -26.504 3.039  1.00 38.14 ? 377 HOH   C O   1 
HETATM 2450 O  O   . HOH   J 5 .   ? 19.428 -27.268 25.491 1.00 38.58 ? 378 HOH   C O   1 
HETATM 2451 O  O   . HOH   J 5 .   ? 18.548 -12.483 17.008 1.00 15.93 ? 379 HOH   C O   1 
HETATM 2452 O  O   . HOH   J 5 .   ? 7.967  -35.076 0.546  1.00 18.68 ? 380 HOH   C O   1 
HETATM 2453 O  O   . HOH   J 5 .   ? 18.465 -11.094 19.269 1.00 26.69 ? 381 HOH   C O   1 
HETATM 2454 O  O   . HOH   J 5 .   ? 16.098 -17.485 26.296 1.00 29.96 ? 382 HOH   C O   1 
HETATM 2455 O  O   . HOH   J 5 .   ? 16.632 -8.524  17.140 1.00 35.79 ? 383 HOH   C O   1 
HETATM 2456 O  O   . HOH   J 5 .   ? 22.033 -14.912 23.604 1.00 31.71 ? 384 HOH   C O   1 
HETATM 2457 O  O   . HOH   J 5 .   ? 4.657  -30.545 31.014 1.00 59.46 ? 385 HOH   C O   1 
HETATM 2458 O  O   . HOH   J 5 .   ? 9.923  -10.178 11.379 1.00 33.56 ? 386 HOH   C O   1 
HETATM 2459 O  O   . HOH   J 5 .   ? 3.685  -36.256 6.821  1.00 22.91 ? 387 HOH   C O   1 
HETATM 2460 O  O   . HOH   J 5 .   ? 5.588  -29.275 7.375  1.00 15.60 ? 388 HOH   C O   1 
HETATM 2461 O  O   . HOH   J 5 .   ? 13.137 -12.190 27.084 1.00 28.76 ? 389 HOH   C O   1 
HETATM 2462 O  O   . HOH   J 5 .   ? 0.833  -16.589 18.102 1.00 37.09 ? 390 HOH   C O   1 
HETATM 2463 O  O   . HOH   J 5 .   ? 2.310  -37.756 14.447 1.00 37.18 ? 391 HOH   C O   1 
HETATM 2464 O  O   . HOH   J 5 .   ? 14.438 -22.519 29.992 1.00 27.20 ? 392 HOH   C O   1 
HETATM 2465 O  O   . HOH   J 5 .   ? 3.966  -27.056 28.134 1.00 48.07 ? 393 HOH   C O   1 
HETATM 2466 O  O   . HOH   J 5 .   ? 3.934  -24.268 26.469 1.00 30.21 ? 394 HOH   C O   1 
HETATM 2467 O  O   . HOH   J 5 .   ? 12.294 -9.884  12.475 1.00 27.28 ? 395 HOH   C O   1 
HETATM 2468 O  O   . HOH   J 5 .   ? -0.206 -15.729 14.415 1.00 29.48 ? 396 HOH   C O   1 
HETATM 2469 O  O   . HOH   J 5 .   ? 4.428  -8.167  22.683 1.00 29.89 ? 397 HOH   C O   1 
HETATM 2470 O  O   . HOH   J 5 .   ? 14.854 -35.912 17.095 1.00 21.46 ? 398 HOH   C O   1 
HETATM 2471 O  O   . HOH   J 5 .   ? 4.235  -33.548 22.237 1.00 29.33 ? 399 HOH   C O   1 
HETATM 2472 O  O   . HOH   J 5 .   ? 0.914  -29.508 25.108 1.00 32.89 ? 400 HOH   C O   1 
HETATM 2473 O  O   . HOH   J 5 .   ? 36.686 -32.134 9.097  1.00 47.22 ? 401 HOH   C O   1 
HETATM 2474 O  O   . HOH   J 5 .   ? 5.695  -32.806 24.486 1.00 20.07 ? 402 HOH   C O   1 
HETATM 2475 O  O   . HOH   J 5 .   ? 6.467  -8.280  11.623 1.00 27.63 ? 403 HOH   C O   1 
HETATM 2476 O  O   . HOH   J 5 .   ? 4.509  -20.256 19.116 1.00 30.42 ? 404 HOH   C O   1 
HETATM 2477 O  O   . HOH   J 5 .   ? 18.950 -31.664 19.197 1.00 19.53 ? 405 HOH   C O   1 
HETATM 2478 O  O   . HOH   J 5 .   ? 31.469 -22.319 4.952  1.00 36.80 ? 406 HOH   C O   1 
HETATM 2479 O  O   . HOH   J 5 .   ? 1.776  -17.747 6.311  1.00 32.92 ? 407 HOH   C O   1 
HETATM 2480 O  O   . HOH   J 5 .   ? 14.191 -16.747 3.699  1.00 28.62 ? 408 HOH   C O   1 
HETATM 2481 O  O   . HOH   J 5 .   ? 20.935 -12.107 21.238 1.00 35.81 ? 409 HOH   C O   1 
HETATM 2482 O  O   . HOH   J 5 .   ? 15.241 -35.707 1.690  1.00 22.86 ? 410 HOH   C O   1 
HETATM 2483 O  O   . HOH   J 5 .   ? 19.584 -7.491  15.115 1.00 22.08 ? 411 HOH   C O   1 
HETATM 2484 O  O   . HOH   J 5 .   ? 28.733 -33.400 12.592 1.00 30.83 ? 412 HOH   C O   1 
HETATM 2485 O  O   . HOH   J 5 .   ? 22.587 -12.361 5.832  1.00 25.97 ? 413 HOH   C O   1 
HETATM 2486 O  O   . HOH   J 5 .   ? 35.640 -29.307 4.870  1.00 52.29 ? 414 HOH   C O   1 
HETATM 2487 O  O   . HOH   J 5 .   ? 6.592  -18.418 5.784  1.00 23.89 ? 415 HOH   C O   1 
HETATM 2488 O  O   . HOH   J 5 .   ? 4.510  -5.698  15.949 1.00 41.16 ? 416 HOH   C O   1 
HETATM 2489 O  O   . HOH   J 5 .   ? 26.372 -33.274 13.969 1.00 29.86 ? 417 HOH   C O   1 
HETATM 2490 O  O   . HOH   J 5 .   ? 16.896 -8.117  14.685 1.00 33.53 ? 418 HOH   C O   1 
HETATM 2491 O  O   . HOH   J 5 .   ? 10.819 -15.256 3.510  1.00 39.78 ? 419 HOH   C O   1 
HETATM 2492 O  O   . HOH   J 5 .   ? 2.520  -20.683 20.940 1.00 44.29 ? 420 HOH   C O   1 
HETATM 2493 O  O   . HOH   J 5 .   ? 24.876 -24.006 20.083 1.00 28.72 ? 421 HOH   C O   1 
HETATM 2494 O  O   . HOH   J 5 .   ? 32.278 -16.742 20.728 1.00 24.02 ? 422 HOH   C O   1 
HETATM 2495 O  O   . HOH   J 5 .   ? 18.176 -18.483 1.687  1.00 39.22 ? 423 HOH   C O   1 
HETATM 2496 O  O   . HOH   J 5 .   ? 29.562 -15.113 22.706 1.00 36.60 ? 424 HOH   C O   1 
HETATM 2497 O  O   . HOH   J 5 .   ? 8.455  -21.591 30.021 1.00 33.02 ? 425 HOH   C O   1 
HETATM 2498 O  O   . HOH   J 5 .   ? 32.675 -16.784 6.696  1.00 51.86 ? 426 HOH   C O   1 
HETATM 2499 O  O   . HOH   J 5 .   ? 1.258  -34.406 17.784 1.00 20.09 ? 427 HOH   C O   1 
HETATM 2500 O  O   . HOH   J 5 .   ? 24.147 -29.138 19.128 1.00 26.32 ? 428 HOH   C O   1 
HETATM 2501 O  O   . HOH   J 5 .   ? 35.513 -20.723 9.242  1.00 46.84 ? 429 HOH   C O   1 
HETATM 2502 O  O   . HOH   J 5 .   ? 17.236 -22.157 -1.677 1.00 33.13 ? 430 HOH   C O   1 
HETATM 2503 O  O   . HOH   J 5 .   ? 31.179 -28.969 12.037 1.00 31.89 ? 431 HOH   C O   1 
HETATM 2504 O  O   . HOH   J 5 .   ? 12.212 -39.204 12.880 1.00 30.77 ? 432 HOH   C O   1 
HETATM 2505 O  O   . HOH   J 5 .   ? 13.767 -42.462 4.332  1.00 52.15 ? 433 HOH   C O   1 
HETATM 2506 O  O   . HOH   J 5 .   ? 22.521 -22.617 20.831 1.00 19.68 ? 434 HOH   C O   1 
HETATM 2507 O  O   . HOH   J 5 .   ? 0.402  -34.613 10.091 1.00 43.56 ? 435 HOH   C O   1 
HETATM 2508 O  O   . HOH   J 5 .   ? -0.641 -35.893 16.621 1.00 31.90 ? 436 HOH   C O   1 
HETATM 2509 O  O   . HOH   J 5 .   ? 3.600  -18.045 18.687 1.00 34.59 ? 437 HOH   C O   1 
HETATM 2510 O  O   . HOH   J 5 .   ? 6.801  -20.613 4.268  1.00 47.41 ? 438 HOH   C O   1 
HETATM 2511 O  O   . HOH   J 5 .   ? 9.814  -14.983 26.703 1.00 43.62 ? 439 HOH   C O   1 
HETATM 2512 O  O   . HOH   J 5 .   ? 20.587 -9.187  17.609 1.00 36.39 ? 440 HOH   C O   1 
HETATM 2513 O  O   . HOH   J 5 .   ? 19.638 -24.410 28.002 1.00 37.33 ? 441 HOH   C O   1 
HETATM 2514 O  O   . HOH   J 5 .   ? 5.143  -15.560 21.925 1.00 48.42 ? 442 HOH   C O   1 
HETATM 2515 O  O   . HOH   J 5 .   ? 12.797 -7.750  14.053 1.00 31.94 ? 443 HOH   C O   1 
HETATM 2516 O  O   . HOH   J 5 .   ? 6.915  -36.549 2.889  1.00 26.26 ? 444 HOH   C O   1 
HETATM 2517 O  O   . HOH   J 5 .   ? 31.867 -26.149 -3.008 1.00 60.66 ? 445 HOH   C O   1 
HETATM 2518 O  O   . HOH   J 5 .   ? 32.617 -9.067  19.379 1.00 50.41 ? 446 HOH   C O   1 
HETATM 2519 O  O   . HOH   J 5 .   ? 1.957  -29.838 1.457  1.00 43.87 ? 447 HOH   C O   1 
HETATM 2520 O  O   . HOH   J 5 .   ? 16.808 -20.374 0.191  1.00 43.39 ? 448 HOH   C O   1 
HETATM 2521 O  O   . HOH   J 5 .   ? 12.515 -17.079 1.563  1.00 48.51 ? 449 HOH   C O   1 
HETATM 2522 O  O   . HOH   J 5 .   ? 15.693 -13.384 27.991 1.00 55.20 ? 450 HOH   C O   1 
HETATM 2523 O  O   . HOH   J 5 .   ? 17.210 -34.810 17.855 1.00 38.47 ? 451 HOH   C O   1 
HETATM 2524 O  O   . HOH   J 5 .   ? 4.558  -28.995 4.802  1.00 37.75 ? 452 HOH   C O   1 
HETATM 2525 O  O   . HOH   J 5 .   ? 9.010  -12.240 6.694  1.00 39.77 ? 453 HOH   C O   1 
HETATM 2526 O  O   . HOH   J 5 .   ? 19.508 -22.014 -2.719 1.00 32.09 ? 454 HOH   C O   1 
HETATM 2527 O  O   . HOH   J 5 .   ? 18.141 -20.260 25.781 1.00 27.43 ? 455 HOH   C O   1 
HETATM 2528 O  O   . HOH   J 5 .   ? 30.550 -31.495 13.301 1.00 33.16 ? 456 HOH   C O   1 
HETATM 2529 O  O   . HOH   J 5 .   ? 24.588 -15.783 23.361 1.00 47.19 ? 457 HOH   C O   1 
HETATM 2530 O  O   . HOH   J 5 .   ? 29.308 -22.200 21.010 1.00 33.37 ? 458 HOH   C O   1 
HETATM 2531 O  O   . HOH   J 5 .   ? 8.515  -19.130 29.306 1.00 33.24 ? 459 HOH   C O   1 
HETATM 2532 O  O   . HOH   J 5 .   ? 2.546  -29.076 27.274 1.00 38.87 ? 460 HOH   C O   1 
HETATM 2533 O  O   . HOH   J 5 .   ? 2.195  -40.121 8.594  1.00 58.02 ? 461 HOH   C O   1 
HETATM 2534 O  O   . HOH   J 5 .   ? 10.164 -10.707 27.712 1.00 60.64 ? 462 HOH   C O   1 
HETATM 2535 O  O   . HOH   J 5 .   ? 4.577  -22.421 28.075 1.00 34.80 ? 463 HOH   C O   1 
HETATM 2536 O  O   . HOH   J 5 .   ? 32.559 -19.449 20.752 1.00 28.79 ? 464 HOH   C O   1 
HETATM 2537 O  O   . HOH   J 5 .   ? -1.420 -25.286 28.440 1.00 47.17 ? 465 HOH   C O   1 
HETATM 2538 O  O   . HOH   J 5 .   ? 8.560  -24.008 2.779  1.00 31.99 ? 466 HOH   C O   1 
HETATM 2539 O  O   . HOH   J 5 .   ? 33.045 -9.341  11.869 1.00 34.88 ? 467 HOH   C O   1 
HETATM 2540 O  O   . HOH   J 5 .   ? 32.120 -27.305 13.911 1.00 34.84 ? 468 HOH   C O   1 
HETATM 2541 O  O   . HOH   J 5 .   ? 38.314 -14.787 9.333  1.00 37.58 ? 469 HOH   C O   1 
HETATM 2542 O  O   . HOH   J 5 .   ? 13.024 -20.250 -1.582 1.00 38.54 ? 470 HOH   C O   1 
HETATM 2543 O  O   . HOH   J 5 .   ? 4.647  -19.316 27.870 1.00 34.89 ? 471 HOH   C O   1 
HETATM 2544 O  O   . HOH   J 5 .   ? 31.875 -36.236 12.491 1.00 31.02 ? 472 HOH   C O   1 
HETATM 2545 O  O   . HOH   J 5 .   ? 12.271 -14.562 26.237 1.00 35.63 ? 473 HOH   C O   1 
HETATM 2546 O  O   . HOH   J 5 .   ? 5.457  -39.939 23.288 1.00 28.83 ? 474 HOH   C O   1 
HETATM 2547 O  O   . HOH   J 5 .   ? 29.753 -8.673  9.103  1.00 31.39 ? 475 HOH   C O   1 
HETATM 2548 O  O   . HOH   J 5 .   ? 35.920 -10.072 8.623  1.00 49.28 ? 476 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   ? 0.2660 0.2525 0.2637 0.0137  -0.0055 0.0140  7   SER   A N   
2    C CA  . SER   A 1   ? 0.2605 0.2491 0.2687 0.0112  -0.0083 0.0118  7   SER   A CA  
3    C C   . SER   A 1   ? 0.2499 0.2394 0.2638 0.0071  -0.0090 0.0073  7   SER   A C   
4    O O   . SER   A 1   ? 0.2519 0.2405 0.2605 0.0069  -0.0093 0.0051  7   SER   A O   
5    C CB  . SER   A 1   ? 0.2980 0.2881 0.3049 0.0155  -0.0148 0.0110  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3420 0.3328 0.3437 0.0174  -0.0203 0.0065  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2305 0.2211 0.2547 0.0041  -0.0083 0.0063  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2110 0.2014 0.2407 0.0009  -0.0076 0.0031  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1896 0.1798 0.2270 -0.0017 -0.0033 0.0038  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1809 0.1710 0.2185 -0.0016 -0.0004 0.0062  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1689 0.1587 0.2129 -0.0037 -0.0024 0.0018  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1777 0.1668 0.2276 -0.0051 0.0022  0.0026  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1738 0.1600 0.2246 -0.0063 0.0056  0.0013  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1867 0.1718 0.2376 -0.0068 0.0038  -0.0005 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1930 0.1846 0.2538 -0.0053 0.0010  0.0027  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1553 0.1397 0.2066 -0.0063 0.0107  0.0023  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1525 0.1330 0.2042 -0.0063 0.0155  0.0024  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1572 0.1380 0.2208 -0.0073 0.0185  0.0029  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1557 0.1385 0.2224 -0.0069 0.0191  0.0037  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1644 0.1424 0.2067 -0.0039 0.0193  0.0030  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1702 0.1493 0.2031 -0.0029 0.0161  0.0020  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1780 0.1506 0.2182 -0.0024 0.0250  0.0041  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1922 0.1710 0.2181 -0.0002 0.0179  0.0011  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1660 0.1448 0.2376 -0.0087 0.0209  0.0025  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1840 0.1634 0.2695 -0.0099 0.0249  0.0030  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1843 0.1574 0.2683 -0.0087 0.0340  0.0054  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1971 0.1664 0.2831 -0.0096 0.0362  0.0053  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1817 0.1647 0.2820 -0.0125 0.0204  -0.0002 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1883 0.1772 0.2889 -0.0120 0.0117  -0.0021 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1973 0.1905 0.3056 -0.0115 0.0104  -0.0016 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2070 0.1967 0.2988 -0.0112 0.0054  -0.0038 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2176 0.2153 0.3243 -0.0098 0.0030  -0.0024 11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2245 0.2185 0.3140 -0.0095 -0.0016 -0.0046 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2320 0.2297 0.3285 -0.0086 -0.0027 -0.0037 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2662 0.2672 0.3590 -0.0057 -0.0091 -0.0036 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1918 0.1629 0.2713 -0.0061 0.0396  0.0077  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1976 0.1618 0.2719 -0.0032 0.0488  0.0107  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2114 0.1754 0.2945 -0.0024 0.0555  0.0126  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2220 0.1894 0.3043 -0.0015 0.0535  0.0118  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2341 0.1951 0.2886 0.0015  0.0489  0.0112  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2349 0.2005 0.2843 0.0025  0.0441  0.0092  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2622 0.2156 0.3082 0.0064  0.0583  0.0147  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2211 0.1812 0.3147 -0.0031 0.0637  0.0148  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2213 0.1813 0.3252 -0.0023 0.0713  0.0169  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2183 0.1870 0.3371 -0.0056 0.0649  0.0139  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2211 0.1948 0.3506 -0.0094 0.0576  0.0107  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2159 0.1862 0.3333 -0.0033 0.0665  0.0145  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2066 0.1847 0.3365 -0.0054 0.0603  0.0121  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1947 0.1754 0.3124 -0.0043 0.0520  0.0104  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1923 0.1766 0.3143 -0.0038 0.0498  0.0097  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2451 0.2241 0.3872 -0.0042 0.0678  0.0136  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3417 0.3203 0.5029 -0.0066 0.0751  0.0146  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3723 0.3562 0.5504 -0.0107 0.0699  0.0117  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3584 0.3303 0.5174 -0.0038 0.0873  0.0186  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1764 0.1551 0.2802 -0.0040 0.0479  0.0097  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1765 0.1572 0.2702 -0.0033 0.0412  0.0082  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1608 0.1441 0.2530 -0.0056 0.0334  0.0067  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1717 0.1533 0.2637 -0.0068 0.0333  0.0065  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1894 0.1654 0.2659 0.0003  0.0437  0.0082  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2012 0.1740 0.2747 0.0041  0.0508  0.0090  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2158 0.1911 0.2959 0.0045  0.0510  0.0083  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2332 0.2001 0.2959 0.0082  0.0574  0.0105  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2451 0.2171 0.3213 0.0086  0.0574  0.0086  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2542 0.2176 0.3113 0.0130  0.0639  0.0111  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2779 0.2441 0.3425 0.0130  0.0640  0.0099  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3037 0.2664 0.3622 0.0183  0.0703  0.0100  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1390 0.1256 0.2293 -0.0056 0.0275  0.0060  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1418 0.1303 0.2276 -0.0065 0.0207  0.0052  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1507 0.1379 0.2251 -0.0052 0.0200  0.0052  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1443 0.1319 0.2202 -0.0043 0.0208  0.0055  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1663 0.1596 0.2615 -0.0068 0.0151  0.0048  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1985 0.1932 0.2862 -0.0060 0.0088  0.0048  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2034 0.2024 0.2984 -0.0047 0.0028  0.0044  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2180 0.2170 0.3054 -0.0022 -0.0002 0.0066  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2476 0.2469 0.3272 -0.0003 -0.0050 0.0067  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2738 0.2737 0.3515 -0.0009 -0.0081 0.0039  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2376 0.2359 0.3108 0.0026  -0.0059 0.0098  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1503 0.1361 0.2151 -0.0050 0.0187  0.0046  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1537 0.1392 0.2104 -0.0041 0.0180  0.0038  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1526 0.1400 0.2075 -0.0047 0.0136  0.0045  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1518 0.1392 0.2038 -0.0051 0.0113  0.0043  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1664 0.1494 0.2137 -0.0025 0.0200  0.0025  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1572 0.1411 0.1995 -0.0014 0.0189  0.0004  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1765 0.1561 0.2229 -0.0006 0.0253  0.0029  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1457 0.1339 0.2019 -0.0045 0.0129  0.0054  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1484 0.1374 0.2017 -0.0041 0.0101  0.0070  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1478 0.1361 0.1996 -0.0042 0.0121  0.0069  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1583 0.1462 0.2133 -0.0045 0.0144  0.0050  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1698 0.1599 0.2280 -0.0029 0.0077  0.0094  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2110 0.2030 0.2729 -0.0030 0.0046  0.0083  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1700 0.1596 0.2352 -0.0027 0.0102  0.0102  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1450 0.1334 0.1931 -0.0036 0.0114  0.0088  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1403 0.1280 0.1908 -0.0040 0.0143  0.0091  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1438 0.1299 0.2015 -0.0037 0.0160  0.0111  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1551 0.1406 0.2127 -0.0020 0.0146  0.0144  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1502 0.1374 0.1959 -0.0028 0.0148  0.0121  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1605 0.1491 0.1994 -0.0028 0.0134  0.0102  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1765 0.1651 0.2095 -0.0017 0.0104  0.0104  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1742 0.1641 0.2150 -0.0038 0.0153  0.0076  19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1320 0.1174 0.1962 -0.0049 0.0187  0.0087  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1292 0.1124 0.2008 -0.0046 0.0207  0.0103  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1508 0.1312 0.2222 -0.0029 0.0224  0.0162  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1702 0.1490 0.2436 -0.0009 0.0223  0.0195  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1412 0.1238 0.2200 -0.0061 0.0230  0.0057  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1435 0.1233 0.2305 -0.0057 0.0251  0.0061  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1575 0.1366 0.2527 -0.0073 0.0270  0.0005  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1799 0.1559 0.2833 -0.0070 0.0291  -0.0006 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1779 0.1497 0.2891 -0.0072 0.0327  0.0029  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1910 0.1610 0.3015 -0.0072 0.0351  0.0086  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1833 0.1519 0.3024 -0.0069 0.0346  0.0011  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1470 0.1269 0.2152 -0.0028 0.0242  0.0179  21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1625 0.1386 0.2288 -0.0001 0.0273  0.0244  21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1978 0.1741 0.2542 0.0041  0.0233  0.0283  21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2275 0.2001 0.2803 0.0081  0.0252  0.0340  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1732 0.1482 0.2405 -0.0009 0.0321  0.0256  21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1879 0.1656 0.2457 -0.0002 0.0300  0.0251  21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.1888 0.1707 0.2467 -0.0027 0.0273  0.0192  21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2071 0.1832 0.2546 0.0034  0.0304  0.0297  21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2000 0.1827 0.2488 -0.0011 0.0263  0.0204  21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2074 0.1869 0.2494 0.0026  0.0279  0.0264  21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1729 0.1529 0.2252 0.0037  0.0179  0.0249  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1821 0.1635 0.2276 0.0073  0.0126  0.0264  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1875 0.1712 0.2395 0.0072  0.0091  0.0245  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.1934 0.1795 0.2430 0.0098  0.0038  0.0241  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1818 0.1654 0.2194 0.0070  0.0094  0.0237  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.1992 0.1809 0.2303 0.0077  0.0130  0.0257  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.1994 0.1833 0.2230 0.0077  0.0095  0.0226  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2024 0.1803 0.2268 0.0130  0.0154  0.0321  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1837 0.1671 0.2447 0.0046  0.0118  0.0227  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1750 0.1608 0.2430 0.0046  0.0096  0.0210  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1856 0.1713 0.2546 0.0091  0.0071  0.0247  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.1969 0.1787 0.2637 0.0118  0.0097  0.0291  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1819 0.1666 0.2576 0.0021  0.0136  0.0188  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1850 0.1749 0.2582 0.0102  0.0023  0.0228  24  THR   A N   
135  C CA  . THR   A 18  ? 0.1976 0.1888 0.2723 0.0154  -0.0017 0.0253  24  THR   A CA  
136  C C   . THR   A 18  ? 0.2059 0.1968 0.2912 0.0157  0.0008  0.0260  24  THR   A C   
137  O O   . THR   A 18  ? 0.1964 0.1864 0.2878 0.0118  0.0052  0.0239  24  THR   A O   
138  C CB  . THR   A 18  ? 0.2287 0.2258 0.3056 0.0165  -0.0090 0.0214  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2425 0.2428 0.3312 0.0123  -0.0078 0.0175  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2441 0.2414 0.3111 0.0163  -0.0118 0.0197  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2202 0.2122 0.3077 0.0211  -0.0025 0.0286  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2383 0.2305 0.3366 0.0220  -0.0007 0.0291  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2032 0.2007 0.3131 0.0179  -0.0009 0.0239  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2005 0.1967 0.3176 0.0159  0.0039  0.0231  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2987 0.2926 0.3972 0.0294  -0.0059 0.0320  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4117 0.3992 0.4984 0.0350  -0.0043 0.0385  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4636 0.4433 0.5492 0.0336  0.0038  0.0425  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4533 0.4407 0.5293 0.0424  -0.0094 0.0415  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4829 0.4574 0.5579 0.0398  0.0046  0.0487  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4864 0.4651 0.5537 0.0458  -0.0033 0.0486  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2006 0.2036 0.3123 0.0170  -0.0060 0.0203  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2004 0.2076 0.3240 0.0133  -0.0048 0.0161  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1837 0.1871 0.3045 0.0084  0.0020  0.0149  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1871 0.1909 0.3160 0.0066  0.0064  0.0135  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2473 0.2604 0.3751 0.0130  -0.0112 0.0121  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3778 0.3948 0.5206 0.0093  -0.0088 0.0084  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4267 0.4478 0.5832 0.0106  -0.0089 0.0076  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4276 0.4432 0.5685 0.0051  -0.0060 0.0063  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1643 0.1640 0.2732 0.0068  0.0031  0.0155  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1544 0.1508 0.2598 0.0034  0.0086  0.0140  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1542 0.1475 0.2630 0.0037  0.0136  0.0146  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1522 0.1447 0.2634 0.0023  0.0177  0.0124  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1578 0.1515 0.2514 0.0024  0.0084  0.0145  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.1970 0.1927 0.2863 0.0016  0.0048  0.0129  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.1927 0.1904 0.2874 -0.0001 0.0051  0.0105  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.1979 0.1928 0.2786 0.0029  0.0022  0.0142  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1511 0.1418 0.2592 0.0060  0.0135  0.0175  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1586 0.1456 0.2708 0.0062  0.0181  0.0175  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1813 0.1705 0.3039 0.0076  0.0193  0.0167  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1911 0.1781 0.3167 0.0071  0.0238  0.0146  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1649 0.1475 0.2751 0.0083  0.0188  0.0213  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1707 0.1500 0.2743 0.0061  0.0208  0.0210  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.1930 0.1716 0.2889 0.0067  0.0193  0.0237  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1678 0.1441 0.2731 0.0035  0.0248  0.0175  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.1913 0.1672 0.2854 0.0041  0.0226  0.0223  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1875 0.1622 0.2879 0.0021  0.0255  0.0181  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1808 0.1557 0.2914 0.0028  0.0276  0.0133  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1786 0.1513 0.2815 -0.0004 0.0284  0.0142  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.1861 0.1587 0.2974 0.0007  0.0298  0.0092  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1771 0.1490 0.2854 -0.0010 0.0299  0.0093  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1748 0.1689 0.3035 0.0096  0.0153  0.0177  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1837 0.1810 0.3247 0.0108  0.0167  0.0168  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.1913 0.1903 0.3360 0.0080  0.0208  0.0136  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.1971 0.1974 0.3514 0.0088  0.0246  0.0128  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1905 0.1937 0.3388 0.0140  0.0105  0.0177  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1772 0.1760 0.3149 0.0053  0.0205  0.0123  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1767 0.1754 0.3158 0.0035  0.0253  0.0103  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1667 0.1602 0.2926 0.0025  0.0285  0.0091  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1682 0.1609 0.2894 0.0013  0.0305  0.0081  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1898 0.1926 0.3333 0.0017  0.0221  0.0094  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2259 0.2351 0.3848 0.0029  0.0185  0.0090  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2269 0.2384 0.3983 0.0029  0.0228  0.0084  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2439 0.2562 0.4023 0.0046  0.0107  0.0092  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1569 0.1469 0.2778 0.0034  0.0290  0.0088  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1609 0.1472 0.2713 0.0028  0.0305  0.0064  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1740 0.1582 0.2804 0.0041  0.0356  0.0039  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.1939 0.1773 0.3053 0.0060  0.0397  0.0034  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1675 0.1508 0.2784 0.0034  0.0304  0.0058  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1854 0.1657 0.2889 0.0028  0.0311  0.0020  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1871 0.1685 0.2838 0.0009  0.0280  0.0026  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1892 0.1661 0.2976 0.0031  0.0320  0.0008  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1762 0.1591 0.2726 0.0037  0.0357  0.0024  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1962 0.1763 0.2848 0.0064  0.0403  0.0002  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2095 0.1874 0.2895 0.0077  0.0385  -0.0043 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2294 0.2049 0.3063 0.0109  0.0408  -0.0079 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2169 0.1966 0.3004 0.0062  0.0420  0.0018  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2237 0.1992 0.2953 0.0104  0.0466  0.0000  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2223 0.2043 0.3176 0.0047  0.0443  0.0049  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1877 0.1669 0.2653 0.0054  0.0340  -0.0047 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1910 0.1694 0.2634 0.0062  0.0318  -0.0096 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1741 0.1543 0.2491 0.0028  0.0281  -0.0085 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1741 0.1558 0.2482 0.0011  0.0267  -0.0048 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2120 0.1895 0.2721 0.0094  0.0325  -0.0122 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2323 0.2106 0.2870 0.0105  0.0287  -0.0179 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2493 0.2270 0.3026 0.0134  0.0276  -0.0246 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2249 0.2054 0.2763 0.0089  0.0254  -0.0180 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2511 0.2313 0.3023 0.0134  0.0232  -0.0293 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2345 0.2163 0.2839 0.0108  0.0223  -0.0249 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2227 0.2044 0.2729 0.0064  0.0246  -0.0135 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2296 0.2143 0.2763 0.0104  0.0188  -0.0270 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2258 0.2095 0.2723 0.0060  0.0215  -0.0153 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2188 0.2042 0.2640 0.0079  0.0188  -0.0217 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1676 0.1473 0.2461 0.0021  0.0268  -0.0120 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1699 0.1509 0.2509 -0.0006 0.0247  -0.0108 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1652 0.1466 0.2482 -0.0007 0.0235  -0.0173 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1784 0.1586 0.2641 0.0009  0.0239  -0.0227 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1830 0.1628 0.2717 -0.0022 0.0255  -0.0056 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1959 0.1729 0.2932 -0.0016 0.0278  -0.0065 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2504 0.2254 0.3546 -0.0027 0.0286  -0.0111 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2739 0.2467 0.3829 -0.0016 0.0300  -0.0152 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2023 0.1780 0.3082 -0.0047 0.0282  -0.0112 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1603 0.1438 0.2431 -0.0025 0.0218  -0.0175 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1561 0.1413 0.2441 -0.0029 0.0203  -0.0244 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1614 0.1476 0.2557 -0.0061 0.0212  -0.0214 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1636 0.1518 0.2517 -0.0063 0.0202  -0.0189 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1982 0.1860 0.2765 0.0005  0.0172  -0.0300 35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2826 0.2736 0.3664 0.0011  0.0140  -0.0390 35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3158 0.3078 0.4122 -0.0024 0.0147  -0.0401 35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3031 0.2955 0.3787 0.0056  0.0110  -0.0449 35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1701 0.1539 0.2765 -0.0083 0.0239  -0.0214 36  SER   A N   
241  C CA  A SER   A 30  ? 0.1796 0.1631 0.2929 -0.0108 0.0267  -0.0177 36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1754 0.1590 0.2886 -0.0108 0.0266  -0.0177 36  SER   A CA  
243  C C   . SER   A 30  ? 0.1764 0.1648 0.2919 -0.0116 0.0247  -0.0232 36  SER   A C   
244  O O   . SER   A 30  ? 0.1756 0.1650 0.2905 -0.0127 0.0262  -0.0192 36  SER   A O   
245  C CB  A SER   A 30  ? 0.2143 0.1934 0.3416 -0.0126 0.0311  -0.0171 36  SER   A CB  
246  C CB  B SER   A 30  ? 0.1984 0.1775 0.3256 -0.0126 0.0311  -0.0169 36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2657 0.2437 0.4011 -0.0148 0.0352  -0.0140 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2282 0.2085 0.3664 -0.0136 0.0301  -0.0264 36  SER   A OG  
249  N N   . SER   A 31  ? 0.1782 0.1696 0.2964 -0.0105 0.0210  -0.0327 37  SER   A N   
250  C CA  . SER   A 31  ? 0.1841 0.1813 0.3057 -0.0106 0.0182  -0.0388 37  SER   A CA  
251  C C   . SER   A 31  ? 0.1830 0.1828 0.2897 -0.0084 0.0157  -0.0359 37  SER   A C   
252  O O   . SER   A 31  ? 0.1968 0.2010 0.3060 -0.0085 0.0143  -0.0386 37  SER   A O   
253  C CB  . SER   A 31  ? 0.2322 0.2328 0.3590 -0.0086 0.0135  -0.0505 37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3067 0.3076 0.4177 -0.0036 0.0095  -0.0527 37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1587 0.1558 0.2520 -0.0065 0.0156  -0.0305 38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1519 0.1503 0.2321 -0.0046 0.0138  -0.0276 38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1534 0.1494 0.2297 -0.0063 0.0165  -0.0187 38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1602 0.1568 0.2271 -0.0052 0.0153  -0.0163 38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1509 0.1478 0.2192 -0.0007 0.0121  -0.0286 38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1825 0.1818 0.2493 0.0032  0.0085  -0.0377 38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1761 0.1728 0.2289 0.0083  0.0082  -0.0378 38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1703 0.1664 0.2113 0.0102  0.0083  -0.0336 38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1995 0.1937 0.2273 0.0158  0.0080  -0.0343 38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2196 0.2129 0.2426 0.0208  0.0071  -0.0394 38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1926 0.1855 0.2116 0.0171  0.0088  -0.0301 38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1503 0.1431 0.2328 -0.0082 0.0197  -0.0141 39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1424 0.1328 0.2197 -0.0083 0.0211  -0.0063 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1406 0.1303 0.2083 -0.0067 0.0189  -0.0045 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1476 0.1371 0.2090 -0.0062 0.0181  -0.0005 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1468 0.1383 0.2219 -0.0087 0.0223  -0.0035 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1599 0.1488 0.2287 -0.0076 0.0233  0.0038  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1583 0.1440 0.2300 -0.0072 0.0251  0.0076  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1591 0.1489 0.2197 -0.0066 0.0220  0.0054  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1377 0.1269 0.2052 -0.0056 0.0184  -0.0074 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1414 0.1296 0.2025 -0.0043 0.0177  -0.0053 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1447 0.1310 0.2108 -0.0041 0.0192  -0.0036 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1569 0.1422 0.2289 -0.0040 0.0205  -0.0061 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1506 0.1392 0.2046 -0.0019 0.0170  -0.0092 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1564 0.1466 0.2034 -0.0010 0.0153  -0.0104 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1795 0.1689 0.2183 0.0028  0.0152  -0.0135 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1491 0.1388 0.1926 -0.0021 0.0149  -0.0057 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1327 0.1188 0.1974 -0.0038 0.0189  -0.0001 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1322 0.1174 0.2022 -0.0032 0.0202  0.0013  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1402 0.1259 0.2080 -0.0027 0.0204  0.0022  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1528 0.1394 0.2171 -0.0034 0.0185  0.0034  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1360 0.1208 0.2116 -0.0035 0.0196  0.0053  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1388 0.1233 0.2214 -0.0024 0.0207  0.0066  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1515 0.1341 0.2396 -0.0016 0.0213  0.0094  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1450 0.1320 0.2289 -0.0019 0.0184  0.0087  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1306 0.1152 0.2008 -0.0015 0.0233  0.0013  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1474 0.1319 0.2184 -0.0011 0.0253  0.0026  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1497 0.1354 0.2312 -0.0011 0.0266  0.0042  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1561 0.1408 0.2406 0.0001  0.0285  0.0033  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1653 0.1471 0.2290 0.0015  0.0293  0.0006  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1744 0.1549 0.2406 0.0019  0.0335  0.0028  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1742 0.1555 0.2279 0.0022  0.0273  -0.0014 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1541 0.1421 0.2420 -0.0022 0.0251  0.0059  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1554 0.1458 0.2553 -0.0019 0.0257  0.0070  43  SER   A CA  
299  C C   . SER   A 37  ? 0.1732 0.1640 0.2795 -0.0025 0.0296  0.0071  43  SER   A C   
300  O O   . SER   A 37  ? 0.1690 0.1580 0.2703 -0.0033 0.0307  0.0068  43  SER   A O   
301  C CB  . SER   A 37  ? 0.1758 0.1696 0.2803 -0.0020 0.0197  0.0083  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1932 0.1887 0.2957 -0.0031 0.0157  0.0079  43  SER   A OG  
303  N N   . SER   A 38  ? 0.1715 0.1643 0.2898 -0.0020 0.0323  0.0076  44  SER   A N   
304  C CA  . SER   A 38  ? 0.1755 0.1686 0.3032 -0.0027 0.0374  0.0079  44  SER   A CA  
305  C C   . SER   A 38  ? 0.1868 0.1852 0.3275 -0.0050 0.0323  0.0069  44  SER   A C   
306  O O   . SER   A 38  ? 0.1868 0.1894 0.3312 -0.0046 0.0254  0.0062  44  SER   A O   
307  C CB  . SER   A 38  ? 0.1973 0.1901 0.3326 -0.0008 0.0440  0.0086  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2256 0.2228 0.3705 -0.0003 0.0397  0.0084  44  SER   A OG  
309  N N   . THR   A 39  ? 0.1936 0.1914 0.3413 -0.0068 0.0358  0.0064  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2134 0.2163 0.3755 -0.0092 0.0308  0.0039  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2360 0.2408 0.4180 -0.0105 0.0376  0.0037  45  THR   A C   
312  O O   . THR   A 39  ? 0.2470 0.2471 0.4275 -0.0095 0.0475  0.0064  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2331 0.2335 0.3879 -0.0109 0.0283  0.0026  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2407 0.2351 0.3936 -0.0114 0.0375  0.0045  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2415 0.2398 0.3774 -0.0097 0.0232  0.0031  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2478 0.2595 0.4487 -0.0122 0.0324  0.0002  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2647 0.2789 0.4885 -0.0142 0.0389  -0.0008 46  THR   A CA  
318  C C   . THR   A 40  ? 0.2858 0.2963 0.5150 -0.0175 0.0427  -0.0019 46  THR   A C   
319  O O   . THR   A 40  ? 0.3111 0.3189 0.5533 -0.0189 0.0532  -0.0003 46  THR   A O   
320  C CB  . THR   A 40  ? 0.2908 0.3153 0.5354 -0.0140 0.0312  -0.0049 46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3058 0.3342 0.5481 -0.0141 0.0191  -0.0092 46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3074 0.3343 0.5487 -0.0104 0.0297  -0.0030 46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2757 0.2852 0.4952 -0.0184 0.0353  -0.0043 47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2729 0.2784 0.4970 -0.0213 0.0382  -0.0057 47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.2727 0.2680 0.4746 -0.0200 0.0452  -0.0009 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.2655 0.2588 0.4467 -0.0172 0.0427  0.0012  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2805 0.2907 0.5066 -0.0224 0.0257  -0.0118 47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.2691 0.2582 0.4761 -0.0217 0.0535  0.0003  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.2916 0.2708 0.4779 -0.0194 0.0601  0.0048  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.2851 0.2635 0.4570 -0.0196 0.0512  0.0024  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.2938 0.2755 0.4766 -0.0224 0.0446  -0.0025 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3363 0.3083 0.5342 -0.0207 0.0727  0.0075  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4429 0.4039 0.6196 -0.0172 0.0802  0.0126  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.5549 0.5112 0.7152 -0.0116 0.0885  0.0182  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.5863 0.5467 0.7518 -0.0107 0.0900  0.0186  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.5808 0.5283 0.7208 -0.0072 0.0937  0.0222  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.2642 0.2390 0.4126 -0.0162 0.0504  0.0050  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.2608 0.2355 0.3955 -0.0160 0.0423  0.0029  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.2699 0.2382 0.4028 -0.0169 0.0450  0.0026  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3064 0.2684 0.4450 -0.0169 0.0548  0.0054  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.2326 0.2020 0.3568 -0.0170 0.0369  -0.0003 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.2231 0.1869 0.3448 -0.0177 0.0377  -0.0014 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.2315 0.1889 0.3318 -0.0138 0.0411  0.0024  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.2265 0.1774 0.3241 -0.0135 0.0446  0.0030  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.2358 0.2047 0.3605 -0.0193 0.0265  -0.0075 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.2648 0.2391 0.3705 -0.0164 0.0170  -0.0078 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.2348 0.1941 0.3207 -0.0108 0.0398  0.0045  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.2236 0.1790 0.2901 -0.0068 0.0408  0.0065  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2282 0.1773 0.2860 -0.0024 0.0500  0.0111  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.2475 0.1963 0.3127 -0.0023 0.0556  0.0131  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.2165 0.1782 0.2736 -0.0059 0.0332  0.0050  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.2517 0.2180 0.3109 -0.0081 0.0247  0.0014  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.2621 0.2256 0.3192 -0.0084 0.0233  -0.0002 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.2137 0.1859 0.2760 -0.0090 0.0196  0.0002  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2226 0.1674 0.2637 0.0021  0.0512  0.0126  52  THR   A N   
356  C CA  . THR   A 46  ? 0.2585 0.1977 0.2858 0.0085  0.0577  0.0162  52  THR   A CA  
357  C C   . THR   A 46  ? 0.2545 0.1971 0.2658 0.0123  0.0514  0.0141  52  THR   A C   
358  O O   . THR   A 46  ? 0.2580 0.2040 0.2679 0.0105  0.0449  0.0115  52  THR   A O   
359  C CB  . THR   A 46  ? 0.3158 0.2449 0.3411 0.0114  0.0672  0.0205  52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3370 0.2635 0.3561 0.0119  0.0641  0.0196  52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3252 0.2514 0.3703 0.0068  0.0738  0.0219  52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2423 0.1848 0.2430 0.0176  0.0531  0.0146  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2192 0.1663 0.2087 0.0208  0.0466  0.0113  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2350 0.1770 0.2084 0.0284  0.0485  0.0124  53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2564 0.1908 0.2222 0.0338  0.0561  0.0163  53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2126 0.1635 0.2017 0.0222  0.0458  0.0094  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2208 0.1757 0.2257 0.0159  0.0452  0.0092  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2138 0.1705 0.1961 0.0243  0.0385  0.0046  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2312 0.1923 0.2443 0.0101  0.0376  0.0067  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2180 0.1638 0.1859 0.0293  0.0420  0.0093  54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2243 0.1670 0.1772 0.0371  0.0421  0.0095  54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2444 0.1887 0.1869 0.0440  0.0411  0.0071  54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2317 0.1827 0.1796 0.0416  0.0367  0.0030  54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2209 0.1691 0.1734 0.0359  0.0348  0.0059  54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2641 0.2017 0.1909 0.0535  0.0452  0.0095  55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.2712 0.2100 0.1852 0.0620  0.0433  0.0063  55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3072 0.2451 0.2071 0.0703  0.0399  0.0052  55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3316 0.2604 0.2187 0.0778  0.0462  0.0104  55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.2739 0.2041 0.1805 0.0672  0.0529  0.0114  55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.2619 0.1928 0.1842 0.0590  0.0570  0.0130  55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3027 0.2431 0.2339 0.0545  0.0498  0.0067  55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.2846 0.2250 0.2303 0.0477  0.0543  0.0091  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3072 0.2545 0.2650 0.0416  0.0496  0.0054  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2841 0.2386 0.2425 0.0408  0.0411  -0.0007 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.2965 0.2436 0.2668 0.0365  0.0538  0.0079  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2999 0.2469 0.2048 0.0680  0.0309  -0.0009 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3192 0.2670 0.2147 0.0745  0.0269  -0.0024 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3037 0.2638 0.2058 0.0733  0.0165  -0.0112 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3052 0.2721 0.2191 0.0672  0.0132  -0.0154 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3154 0.2586 0.2158 0.0698  0.0304  0.0024  56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2734 0.2251 0.1945 0.0564  0.0258  -0.0004 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3240 0.2869 0.2201 0.0790  0.0118  -0.0137 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3213 0.2963 0.2268 0.0774  0.0027  -0.0221 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.3162 0.2937 0.2295 0.0726  0.0017  -0.0210 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3188 0.3040 0.2347 0.0754  -0.0045 -0.0264 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3799 0.3590 0.2736 0.0894  -0.0039 -0.0286 57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.4857 0.4588 0.3624 0.1001  -0.0028 -0.0251 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.4886 0.4519 0.3610 0.0988  0.0049  -0.0167 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5764 0.5544 0.4446 0.1102  -0.0097 -0.0311 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3007 0.2719 0.2180 0.0660  0.0076  -0.0146 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2719 0.2450 0.1955 0.0618  0.0067  -0.0140 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2581 0.2425 0.1964 0.0557  0.0013  -0.0197 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2643 0.2522 0.2112 0.0506  0.0007  -0.0216 58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2771 0.2423 0.2043 0.0553  0.0129  -0.0078 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2821 0.2331 0.1963 0.0614  0.0209  -0.0005 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2383 0.2281 0.1798 0.0567  -0.0020 -0.0223 59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2213 0.2207 0.1774 0.0510  -0.0052 -0.0266 59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.1996 0.1976 0.1591 0.0466  -0.0028 -0.0234 59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2006 0.2057 0.1698 0.0438  -0.0044 -0.0261 59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2528 0.2624 0.2134 0.0561  -0.0117 -0.0344 59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3185 0.3329 0.2816 0.0585  -0.0158 -0.0404 59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3888 0.4152 0.3622 0.0616  -0.0227 -0.0494 59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4192 0.4485 0.3853 0.0708  -0.0281 -0.0546 59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3712 0.4049 0.3622 0.0548  -0.0226 -0.0517 59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1916 0.1797 0.1430 0.0465  0.0016  -0.0177 60  THR   A N   
416  C CA  . THR   A 54  ? 0.1947 0.1801 0.1487 0.0421  0.0038  -0.0151 60  THR   A CA  
417  C C   . THR   A 54  ? 0.1892 0.1666 0.1427 0.0375  0.0077  -0.0108 60  THR   A C   
418  O O   . THR   A 54  ? 0.1995 0.1713 0.1482 0.0394  0.0103  -0.0085 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2229 0.2049 0.1694 0.0475  0.0041  -0.0144 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2538 0.2259 0.1897 0.0522  0.0075  -0.0105 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2349 0.2254 0.1827 0.0530  -0.0002 -0.0191 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1799 0.1571 0.1387 0.0319  0.0083  -0.0098 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1749 0.1460 0.1356 0.0275  0.0109  -0.0069 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1620 0.1341 0.1269 0.0231  0.0100  -0.0073 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1690 0.1442 0.1330 0.0243  0.0088  -0.0087 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1670 0.1364 0.1361 0.0188  0.0106  -0.0060 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1642 0.1338 0.1354 0.0158  0.0090  -0.0067 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1680 0.1407 0.1454 0.0119  0.0078  -0.0061 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1721 0.1430 0.1532 0.0103  0.0089  -0.0051 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1923 0.1542 0.1625 0.0155  0.0099  -0.0068 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2118 0.1742 0.1837 0.0131  0.0070  -0.0088 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2029 0.1609 0.1666 0.0199  0.0114  -0.0070 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1537 0.1306 0.1319 0.0108  0.0063  -0.0064 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1485 0.1275 0.1316 0.0081  0.0053  -0.0053 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1605 0.1383 0.1417 0.0077  0.0029  -0.0058 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1585 0.1352 0.1341 0.0098  0.0023  -0.0070 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1442 0.1289 0.1307 0.0078  0.0063  -0.0046 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1430 0.1306 0.1278 0.0089  0.0070  -0.0041 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1577 0.1469 0.1401 0.0112  0.0080  -0.0055 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1522 0.1407 0.1378 0.0082  0.0074  -0.0020 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1525 0.1444 0.1344 0.0124  0.0100  -0.0047 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1568 0.1469 0.1400 0.0099  0.0097  -0.0006 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1707 0.1626 0.1527 0.0117  0.0113  -0.0020 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.1986 0.1921 0.1792 0.0136  0.0147  -0.0005 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1644 0.1427 0.1500 0.0059  0.0012  -0.0052 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1690 0.1468 0.1521 0.0067  -0.0023 -0.0063 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1706 0.1516 0.1505 0.0083  -0.0017 -0.0036 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1723 0.1556 0.1571 0.0069  0.0000  -0.0012 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1741 0.1511 0.1643 0.0047  -0.0052 -0.0077 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.1939 0.1712 0.1811 0.0067  -0.0102 -0.0099 64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2018 0.1766 0.1835 0.0087  -0.0128 -0.0135 64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2093 0.1894 0.1978 0.0075  -0.0127 -0.0086 64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2231 0.1984 0.2004 0.0116  -0.0183 -0.0165 64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2227 0.2033 0.2063 0.0109  -0.0180 -0.0109 64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2448 0.2231 0.2224 0.0131  -0.0211 -0.0151 64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.2961 0.2750 0.2673 0.0175  -0.0272 -0.0182 64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1677 0.1482 0.1394 0.0115  -0.0025 -0.0040 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1657 0.1477 0.1327 0.0141  -0.0003 -0.0005 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.1882 0.1687 0.1484 0.0175  -0.0048 -0.0012 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2053 0.1839 0.1573 0.0207  -0.0074 -0.0039 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.1916 0.1740 0.1533 0.0163  0.0034  -0.0001 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2119 0.1949 0.1675 0.0202  0.0083  0.0049  65  CYS   A SG  
463  N N   . SER   A 60  ? 0.1905 0.1721 0.1541 0.0174  -0.0062 0.0009  66  SER   A N   
464  C CA  . SER   A 60  ? 0.2044 0.1854 0.1617 0.0216  -0.0115 -0.0002 66  SER   A CA  
465  C C   . SER   A 60  ? 0.2070 0.1862 0.1501 0.0280  -0.0100 0.0022  66  SER   A C   
466  O O   . SER   A 60  ? 0.2250 0.2030 0.1590 0.0329  -0.0155 -0.0010 66  SER   A O   
467  C CB  . SER   A 60  ? 0.2523 0.2349 0.2161 0.0209  -0.0131 0.0018  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3324 0.3149 0.2965 0.0212  -0.0072 0.0078  66  SER   A OG  
469  N N   . SER   A 61  ? 0.2023 0.1812 0.1437 0.0285  -0.0025 0.0074  67  SER   A N   
470  C CA  . SER   A 61  ? 0.2162 0.1927 0.1439 0.0351  0.0010  0.0107  67  SER   A CA  
471  C C   . SER   A 61  ? 0.2218 0.1969 0.1405 0.0379  0.0002  0.0070  67  SER   A C   
472  O O   . SER   A 61  ? 0.2308 0.2035 0.1366 0.0442  0.0031  0.0093  67  SER   A O   
473  C CB  . SER   A 61  ? 0.2334 0.2098 0.1646 0.0346  0.0105  0.0174  67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2266 0.2055 0.1675 0.0297  0.0145  0.0161  67  SER   A OG  
475  N N   . ARG   A 62  ? 0.2050 0.1810 0.1301 0.0337  -0.0031 0.0016  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.1990 0.1730 0.1169 0.0360  -0.0047 -0.0028 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2230 0.1959 0.1436 0.0346  -0.0131 -0.0101 68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2397 0.2103 0.1558 0.0362  -0.0151 -0.0147 68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2065 0.1818 0.1304 0.0327  0.0008  -0.0023 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.2282 0.2050 0.1515 0.0342  0.0092  0.0033  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.2397 0.2140 0.1487 0.0412  0.0120  0.0044  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.2483 0.2239 0.1589 0.0425  0.0216  0.0102  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.2572 0.2317 0.1655 0.0449  0.0265  0.0163  68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.2630 0.2352 0.1654 0.0471  0.0220  0.0173  68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.2686 0.2439 0.1810 0.0456  0.0364  0.0215  68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2258 0.2003 0.1561 0.0312  -0.0172 -0.0112 69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2481 0.2219 0.1863 0.0285  -0.0236 -0.0179 69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2492 0.2206 0.1920 0.0250  -0.0212 -0.0204 69  ARG   A C   
489  O O   . ARG   A 63  ? 0.2710 0.2395 0.2136 0.0256  -0.0251 -0.0264 69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3012 0.2742 0.2316 0.0339  -0.0316 -0.0239 69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.3621 0.3374 0.2888 0.0379  -0.0355 -0.0223 69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4014 0.3771 0.3266 0.0416  -0.0459 -0.0310 69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.4174 0.3953 0.3356 0.0478  -0.0504 -0.0295 69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.4397 0.4160 0.3391 0.0572  -0.0530 -0.0296 69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.4573 0.4301 0.3440 0.0611  -0.0517 -0.0316 69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.4159 0.3937 0.3082 0.0635  -0.0564 -0.0271 69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2255 0.1977 0.1717 0.0223  -0.0147 -0.0160 70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2258 0.1956 0.1741 0.0206  -0.0121 -0.0175 70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2119 0.1831 0.1689 0.0166  -0.0079 -0.0143 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2023 0.1769 0.1621 0.0155  -0.0057 -0.0105 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.2672 0.2368 0.2057 0.0245  -0.0085 -0.0162 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.3919 0.3582 0.3203 0.0291  -0.0115 -0.0207 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.4885 0.4548 0.4105 0.0321  -0.0063 -0.0190 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5744 0.5364 0.4876 0.0362  -0.0087 -0.0241 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6189 0.5797 0.5222 0.0408  -0.0138 -0.0271 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2009 0.1689 0.1613 0.0151  -0.0066 -0.0158 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.1957 0.1644 0.1610 0.0132  -0.0026 -0.0132 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2028 0.1725 0.1629 0.0160  0.0004  -0.0124 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2286 0.1956 0.1829 0.0186  0.0000  -0.0146 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.1881 0.1518 0.1594 0.0112  -0.0021 -0.0145 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.1966 0.1598 0.1762 0.0082  -0.0045 -0.0158 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2355 0.2002 0.2222 0.0057  -0.0025 -0.0132 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.1992 0.1610 0.1822 0.0076  -0.0089 -0.0200 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2224 0.1868 0.2171 0.0035  -0.0052 -0.0154 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2455 0.2087 0.2388 0.0046  -0.0096 -0.0198 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1719 0.1457 0.1347 0.0156  0.0031  -0.0100 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1719 0.1483 0.1326 0.0183  0.0054  -0.0099 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.1798 0.1570 0.1437 0.0186  0.0066  -0.0097 72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1732 0.1517 0.1418 0.0165  0.0066  -0.0087 72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.1786 0.1610 0.1411 0.0185  0.0075  -0.0081 72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2061 0.1877 0.1625 0.0203  0.0077  -0.0074 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2366 0.2167 0.1860 0.0238  0.0085  -0.0088 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2124 0.1945 0.1689 0.0194  0.0073  -0.0053 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2401 0.2190 0.1816 0.0267  0.0089  -0.0082 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2243 0.2052 0.1728 0.0226  0.0076  -0.0042 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2417 0.2210 0.1821 0.0264  0.0085  -0.0057 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.2696 0.2472 0.1999 0.0307  0.0091  -0.0047 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.1770 0.1532 0.1376 0.0219  0.0073  -0.0107 73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.1833 0.1606 0.1449 0.0239  0.0079  -0.0107 73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.1994 0.1856 0.1666 0.0243  0.0078  -0.0115 73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2264 0.2168 0.1955 0.0247  0.0088  -0.0120 73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.1978 0.1710 0.1535 0.0283  0.0085  -0.0115 73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.1900 0.1641 0.1437 0.0286  0.0085  -0.0126 73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.1777 0.1517 0.1328 0.0248  0.0076  -0.0121 73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1740 0.1626 0.1441 0.0248  0.0071  -0.0121 74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1700 0.1672 0.1481 0.0248  0.0064  -0.0143 74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1709 0.1705 0.1483 0.0290  0.0043  -0.0169 74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1768 0.1709 0.1475 0.0312  0.0042  -0.0158 74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.1917 0.1909 0.1768 0.0201  0.0070  -0.0133 74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2196 0.2189 0.2062 0.0174  0.0091  -0.0111 74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2018 0.1956 0.1840 0.0186  0.0067  -0.0117 74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1732 0.1814 0.1582 0.0307  0.0028  -0.0207 75  SER   A N   
543  C CA  . SER   A 69  ? 0.1828 0.1957 0.1694 0.0349  -0.0008 -0.0250 75  SER   A CA  
544  C C   . SER   A 69  ? 0.1674 0.1859 0.1660 0.0305  -0.0012 -0.0273 75  SER   A C   
545  O O   . SER   A 69  ? 0.1747 0.1973 0.1833 0.0266  0.0010  -0.0272 75  SER   A O   
546  C CB  . SER   A 69  ? 0.2274 0.2475 0.2179 0.0396  -0.0030 -0.0291 75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3263 0.3405 0.3056 0.0440  -0.0024 -0.0268 75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1472 0.1645 0.1441 0.0312  -0.0029 -0.0285 76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1510 0.1723 0.1593 0.0269  -0.0030 -0.0307 76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1665 0.1935 0.1785 0.0309  -0.0078 -0.0376 76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1797 0.2051 0.1810 0.0375  -0.0108 -0.0392 76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1558 0.1702 0.1607 0.0227  -0.0002 -0.0259 76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1532 0.1599 0.1455 0.0256  0.0001  -0.0232 76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1615 0.1613 0.1451 0.0259  0.0023  -0.0188 76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1681 0.1741 0.1579 0.0279  -0.0012 -0.0252 76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1712 0.1635 0.1457 0.0282  0.0040  -0.0160 76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1695 0.1678 0.1479 0.0310  0.0007  -0.0219 76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1803 0.1717 0.1520 0.0309  0.0036  -0.0171 76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1622 0.1955 0.1895 0.0272  -0.0084 -0.0419 77  SER   A N   
560  C CA  . SER   A 71  ? 0.1648 0.2041 0.1976 0.0308  -0.0138 -0.0500 77  SER   A CA  
561  C C   . SER   A 71  ? 0.1738 0.2075 0.1971 0.0325  -0.0146 -0.0497 77  SER   A C   
562  O O   . SER   A 71  ? 0.1739 0.2002 0.1915 0.0291  -0.0104 -0.0433 77  SER   A O   
563  C CB  . SER   A 71  ? 0.1721 0.2195 0.2267 0.0260  -0.0137 -0.0553 77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1987 0.2415 0.2583 0.0194  -0.0086 -0.0505 77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1738 0.2111 0.1948 0.0386  -0.0203 -0.0569 78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.1923 0.2246 0.2039 0.0414  -0.0208 -0.0572 78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2037 0.2360 0.2283 0.0342  -0.0186 -0.0579 78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2001 0.2385 0.2426 0.0293  -0.0187 -0.0615 78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2488 0.2858 0.2547 0.0508  -0.0282 -0.0661 78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.3173 0.3511 0.3055 0.0595  -0.0294 -0.0635 78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3828 0.4209 0.3628 0.0705  -0.0371 -0.0720 78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4641 0.4972 0.4241 0.0802  -0.0373 -0.0681 78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.5144 0.5509 0.4632 0.0927  -0.0451 -0.0761 78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.1991 0.2245 0.2159 0.0339  -0.0159 -0.0544 79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.1919 0.2169 0.2209 0.0275  -0.0135 -0.0545 79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.1962 0.2287 0.2405 0.0274  -0.0182 -0.0648 79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2148 0.2505 0.2544 0.0342  -0.0240 -0.0725 79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2181 0.2354 0.2348 0.0296  -0.0111 -0.0509 79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2506 0.2630 0.2492 0.0358  -0.0103 -0.0468 79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2123 0.2297 0.2099 0.0394  -0.0140 -0.0496 79  PRO   A CD  
581  N N   . SER   A 74  ? 0.1841 0.2194 0.2470 0.0201  -0.0155 -0.0650 80  SER   A N   
582  C CA  . SER   A 74  ? 0.1916 0.2341 0.2731 0.0191  -0.0192 -0.0752 80  SER   A CA  
583  C C   . SER   A 74  ? 0.1719 0.2126 0.2706 0.0112  -0.0138 -0.0732 80  SER   A C   
584  O O   . SER   A 74  ? 0.1759 0.2100 0.2703 0.0073  -0.0078 -0.0636 80  SER   A O   
585  C CB  . SER   A 74  ? 0.2432 0.2946 0.3340 0.0208  -0.0229 -0.0809 80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3043 0.3562 0.4057 0.0147  -0.0169 -0.0750 80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1594 0.2056 0.2781 0.0093  -0.0162 -0.0827 81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.1766 0.2206 0.3138 0.0023  -0.0107 -0.0816 81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.1763 0.2241 0.3296 -0.0024 -0.0059 -0.0792 81  LEU   A C   
590  O O   . LEU   A 75  ? 0.1792 0.2357 0.3471 -0.0017 -0.0096 -0.0879 81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.1971 0.2457 0.3504 0.0029  -0.0158 -0.0946 81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2631 0.3062 0.4160 0.0026  -0.0156 -0.0967 81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2768 0.3256 0.4526 0.0015  -0.0200 -0.1106 81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2625 0.2969 0.4158 -0.0030 -0.0067 -0.0852 81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.1778 0.2195 0.3294 -0.0066 0.0022  -0.0680 82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.1883 0.2318 0.3508 -0.0100 0.0084  -0.0635 82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.1972 0.2353 0.3733 -0.0154 0.0172  -0.0579 82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2006 0.2310 0.3676 -0.0161 0.0198  -0.0516 82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2090 0.2495 0.3509 -0.0076 0.0097  -0.0545 82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2375 0.2831 0.3680 -0.0018 0.0020  -0.0600 82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2220 0.2624 0.3707 -0.0103 0.0172  -0.0480 82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2760 0.3185 0.3875 0.0009  0.0026  -0.0528 82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.1905 0.2323 0.3891 -0.0190 0.0224  -0.0599 83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.1998 0.2352 0.4114 -0.0236 0.0323  -0.0536 83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2211 0.2489 0.4160 -0.0230 0.0394  -0.0396 83  PHE   A C   
606  O O   . PHE   A 77  ? 0.2259 0.2558 0.4124 -0.0211 0.0403  -0.0360 83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2013 0.2423 0.4425 -0.0274 0.0376  -0.0587 83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2346 0.2678 0.4905 -0.0318 0.0490  -0.0520 83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.2582 0.2877 0.5169 -0.0329 0.0601  -0.0420 83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.2634 0.2918 0.5281 -0.0339 0.0492  -0.0549 83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.2780 0.2991 0.5490 -0.0358 0.0716  -0.0348 83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.2837 0.3038 0.5616 -0.0374 0.0604  -0.0480 83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.2813 0.2977 0.5624 -0.0382 0.0718  -0.0378 83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.2273 0.2462 0.4168 -0.0238 0.0438  -0.0322 84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.2360 0.2477 0.4096 -0.0222 0.0495  -0.0198 84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.2502 0.2550 0.4371 -0.0246 0.0602  -0.0134 84  VAL   A C   
617  O O   . VAL   A 78  ? 0.2500 0.2509 0.4462 -0.0265 0.0612  -0.0150 84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.2504 0.2579 0.4020 -0.0195 0.0440  -0.0163 84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.2729 0.2738 0.4087 -0.0172 0.0484  -0.0050 84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.2471 0.2602 0.3867 -0.0169 0.0349  -0.0223 84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.2592 0.2616 0.4456 -0.0239 0.0686  -0.0056 85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.2749 0.2697 0.4720 -0.0249 0.0808  0.0024  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.2848 0.2702 0.4692 -0.0228 0.0821  0.0102  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.2927 0.2775 0.4564 -0.0197 0.0749  0.0118  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.3400 0.3332 0.5297 -0.0222 0.0887  0.0109  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.4860 0.4733 0.6928 -0.0235 0.1032  0.0174  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.6301 0.6244 0.8688 -0.0291 0.1057  0.0078  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.6686 0.6582 0.9285 -0.0324 0.1141  0.0084  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.6848 0.6894 0.9280 -0.0299 0.0988  -0.0010 85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.2820 0.2597 0.4794 -0.0240 0.0918  0.0152  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.2903 0.2587 0.4759 -0.0211 0.0936  0.0232  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.2983 0.2627 0.4578 -0.0149 0.0940  0.0334  86  ALA   A C   
633  O O   . ALA   A 80  ? 0.3016 0.2666 0.4561 -0.0129 0.0988  0.0376  86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.2945 0.2544 0.4982 -0.0226 0.1057  0.0283  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.2977 0.2589 0.4412 -0.0117 0.0884  0.0364  87  SER   A N   
636  C CA  . SER   A 81  ? 0.3001 0.2575 0.4197 -0.0052 0.0872  0.0450  87  SER   A CA  
637  C C   . SER   A 81  ? 0.3231 0.2722 0.4388 -0.0020 0.0893  0.0515  87  SER   A C   
638  O O   . SER   A 81  ? 0.3363 0.2828 0.4680 -0.0052 0.0920  0.0492  87  SER   A O   
639  C CB  . SER   A 81  ? 0.3077 0.2718 0.4123 -0.0045 0.0752  0.0397  87  SER   A CB  
640  O OG  . SER   A 81  ? 0.3069 0.2723 0.4135 -0.0062 0.0682  0.0348  87  SER   A OG  
641  N N   . GLU   A 82  ? 0.3315 0.2770 0.4265 0.0047  0.0873  0.0587  88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.3555 0.2943 0.4452 0.0089  0.0876  0.0645  88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.3418 0.2850 0.4365 0.0055  0.0783  0.0568  88  GLU   A C   
644  O O   . GLU   A 82  ? 0.3506 0.2890 0.4479 0.0071  0.0791  0.0595  88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.4401 0.3759 0.5056 0.0176  0.0854  0.0721  88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.5753 0.5112 0.6295 0.0219  0.0766  0.0727  88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.7034 0.6301 0.7547 0.0281  0.0821  0.0817  88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.7210 0.6469 0.7811 0.0265  0.0800  0.0798  88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.7554 0.6752 0.7947 0.0354  0.0889  0.0908  88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.3198 0.2716 0.4149 0.0015  0.0700  0.0478  89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.3137 0.2692 0.4110 -0.0007 0.0621  0.0413  89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.3017 0.2593 0.4174 -0.0063 0.0627  0.0332  89  TYR   A C   
653  O O   . TYR   A 83  ? 0.3107 0.2687 0.4294 -0.0071 0.0588  0.0296  89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.3110 0.2735 0.3963 -0.0005 0.0530  0.0369  89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.3206 0.2823 0.3883 0.0050  0.0506  0.0426  89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.3340 0.2963 0.3943 0.0065  0.0528  0.0445  89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.3271 0.2877 0.3860 0.0092  0.0458  0.0453  89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.3543 0.3160 0.3975 0.0121  0.0497  0.0484  89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.3414 0.3019 0.3846 0.0148  0.0423  0.0489  89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.3652 0.3259 0.3998 0.0163  0.0441  0.0503  89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.3996 0.3601 0.4180 0.0224  0.0400  0.0529  89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.2828 0.2425 0.4107 -0.0100 0.0667  0.0295  90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.2634 0.2263 0.4091 -0.0149 0.0657  0.0199  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.2837 0.2448 0.4485 -0.0180 0.0744  0.0193  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.2841 0.2451 0.4471 -0.0172 0.0795  0.0239  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.2425 0.2144 0.3844 -0.0164 0.0574  0.0109  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.2319 0.2066 0.3581 -0.0142 0.0491  0.0096  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.2281 0.2024 0.3561 -0.0144 0.0455  0.0055  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.2344 0.2118 0.3453 -0.0120 0.0455  0.0120  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.2203 0.1970 0.3359 -0.0125 0.0393  0.0045  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.2213 0.2009 0.3206 -0.0105 0.0388  0.0105  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.2145 0.1939 0.3166 -0.0109 0.0361  0.0069  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.1898 0.1709 0.2823 -0.0094 0.0310  0.0060  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.2984 0.2593 0.4829 -0.0219 0.0756  0.0121  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.3004 0.2616 0.5073 -0.0259 0.0828  0.0089  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.2932 0.2648 0.5026 -0.0277 0.0773  0.0005  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.3048 0.2824 0.5000 -0.0262 0.0676  -0.0040 91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.3158 0.2753 0.5419 -0.0292 0.0824  0.0007  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.3335 0.2970 0.5457 -0.0274 0.0713  -0.0052 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.3142 0.2753 0.5023 -0.0227 0.0699  0.0052  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.2804 0.2543 0.5099 -0.0311 0.0835  -0.0023 92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.2843 0.2689 0.5200 -0.0327 0.0780  -0.0116 92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2682 0.2591 0.5080 -0.0336 0.0668  -0.0250 92  ALA   A C   
684  O O   . ALA   A 86  ? 0.2692 0.2567 0.5214 -0.0355 0.0672  -0.0294 92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.2902 0.2761 0.5524 -0.0366 0.0871  -0.0134 92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2503 0.2488 0.4758 -0.0313 0.0572  -0.0301 93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2328 0.2359 0.4569 -0.0303 0.0470  -0.0413 93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2226 0.2345 0.4354 -0.0275 0.0384  -0.0470 93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2363 0.2499 0.4409 -0.0265 0.0401  -0.0417 93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.2390 0.2354 0.4461 -0.0279 0.0453  -0.0361 93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.2567 0.2531 0.4375 -0.0241 0.0418  -0.0289 93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.2450 0.2342 0.4122 -0.0222 0.0434  -0.0202 93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.2301 0.2210 0.3769 -0.0190 0.0369  -0.0191 93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.2371 0.2294 0.3699 -0.0172 0.0358  -0.0141 93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2340 0.2269 0.3512 -0.0147 0.0309  -0.0134 93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.2374 0.2302 0.3723 -0.0178 0.0401  -0.0102 93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2135 0.2300 0.4237 -0.0253 0.0293  -0.0574 94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2227 0.2458 0.4181 -0.0211 0.0213  -0.0615 94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2135 0.2317 0.3838 -0.0176 0.0189  -0.0551 94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2192 0.2331 0.3863 -0.0170 0.0180  -0.0558 94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2306 0.2614 0.4352 -0.0191 0.0127  -0.0762 94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2358 0.2736 0.4669 -0.0224 0.0139  -0.0839 94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2424 0.2883 0.4749 -0.0208 0.0112  -0.0866 94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2510 0.2870 0.5075 -0.0272 0.0187  -0.0879 94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2649 0.3182 0.5245 -0.0240 0.0127  -0.0938 94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2612 0.3036 0.5455 -0.0309 0.0211  -0.0947 94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2753 0.3268 0.5615 -0.0293 0.0180  -0.0977 94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3124 0.3712 0.6294 -0.0331 0.0205  -0.1054 94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1914 0.2102 0.3454 -0.0154 0.0182  -0.0491 95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1809 0.1957 0.3133 -0.0123 0.0160  -0.0437 95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1657 0.1852 0.2877 -0.0077 0.0087  -0.0506 95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1780 0.2033 0.3015 -0.0063 0.0061  -0.0542 95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1726 0.1840 0.2938 -0.0126 0.0200  -0.0330 95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1720 0.1800 0.2735 -0.0098 0.0174  -0.0285 95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.1964 0.2002 0.2891 -0.0101 0.0208  -0.0189 95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2075 0.2082 0.3058 -0.0119 0.0257  -0.0137 95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1572 0.1605 0.2351 -0.0079 0.0182  -0.0163 95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1548 0.1718 0.2666 -0.0046 0.0056  -0.0526 96  SER   A N   
719  C CA  . SER   A 90  ? 0.1602 0.1801 0.2598 0.0013  -0.0005 -0.0584 96  SER   A CA  
720  C C   . SER   A 90  ? 0.1787 0.1954 0.2588 0.0040  0.0000  -0.0509 96  SER   A C   
721  O O   . SER   A 90  ? 0.1786 0.1906 0.2547 0.0014  0.0043  -0.0423 96  SER   A O   
722  C CB  . SER   A 90  ? 0.1934 0.2116 0.2915 0.0041  -0.0032 -0.0645 96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2087 0.2200 0.3001 0.0031  0.0010  -0.0573 96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1647 0.1836 0.2332 0.0098  -0.0044 -0.0546 97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1728 0.1877 0.2235 0.0129  -0.0035 -0.0483 97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1683 0.1826 0.2190 0.0094  -0.0004 -0.0412 97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1693 0.1788 0.2098 0.0094  0.0020  -0.0344 97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1908 0.1991 0.2327 0.0138  -0.0007 -0.0440 97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2168 0.2250 0.2553 0.0187  -0.0033 -0.0508 97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2638 0.2705 0.2865 0.0263  -0.0053 -0.0526 97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2220 0.2310 0.2706 0.0175  -0.0042 -0.0564 97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2690 0.2758 0.2913 0.0300  -0.0075 -0.0593 97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2546 0.2630 0.2929 0.0247  -0.0072 -0.0622 97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1616 0.1810 0.2240 0.0069  -0.0005 -0.0433 98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1601 0.1788 0.2221 0.0043  0.0028  -0.0370 98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1504 0.1732 0.2076 0.0079  0.0000  -0.0393 98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1476 0.1765 0.2105 0.0106  -0.0041 -0.0470 98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1588 0.1796 0.2379 -0.0006 0.0066  -0.0367 98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1888 0.2079 0.2671 -0.0029 0.0112  -0.0293 98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2033 0.2156 0.2697 -0.0033 0.0131  -0.0215 98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2064 0.2266 0.3020 -0.0068 0.0164  -0.0288 98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1523 0.1719 0.1994 0.0082  0.0018  -0.0334 99  MET   A N   
743  C CA  . MET   A 93  ? 0.1537 0.1759 0.1949 0.0119  -0.0002 -0.0346 99  MET   A CA  
744  C C   . MET   A 93  ? 0.1568 0.1796 0.2019 0.0090  0.0034  -0.0305 99  MET   A C   
745  O O   . MET   A 93  ? 0.1616 0.1794 0.2028 0.0063  0.0067  -0.0243 99  MET   A O   
746  C CB  . MET   A 93  ? 0.1609 0.1771 0.1852 0.0157  -0.0007 -0.0311 99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1873 0.2015 0.2051 0.0196  -0.0029 -0.0340 99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2310 0.2364 0.2310 0.0236  -0.0008 -0.0284 99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2380 0.2384 0.2412 0.0170  0.0036  -0.0216 99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1470 0.1761 0.1999 0.0099  0.0028  -0.0340 100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1551 0.1846 0.2114 0.0078  0.0073  -0.0299 100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1516 0.1806 0.1973 0.0115  0.0063  -0.0287 100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1493 0.1812 0.1913 0.0159  0.0019  -0.0331 100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1654 0.2023 0.2414 0.0056  0.0095  -0.0339 100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2145 0.2514 0.3043 0.0015  0.0117  -0.0353 100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2278 0.2712 0.3392 -0.0011 0.0154  -0.0387 100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2266 0.2555 0.3102 -0.0013 0.0163  -0.0271 100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1435 0.1695 0.1852 0.0103  0.0103  -0.0233 101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1435 0.1686 0.1760 0.0135  0.0100  -0.0222 101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1384 0.1636 0.1736 0.0123  0.0153  -0.0186 101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1570 0.1807 0.1970 0.0092  0.0194  -0.0152 101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1647 0.1817 0.1815 0.0148  0.0086  -0.0188 101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1304 0.1571 0.1622 0.0153  0.0158  -0.0190 102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1399 0.1656 0.1710 0.0152  0.0213  -0.0152 102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1611 0.1784 0.1758 0.0159  0.0209  -0.0109 102 VAL   A C   
766  O O   . VAL   A 96  ? 0.1935 0.2072 0.1981 0.0182  0.0173  -0.0118 102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1480 0.1792 0.1828 0.0185  0.0220  -0.0181 102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1675 0.1968 0.1993 0.0194  0.0284  -0.0138 102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1484 0.1892 0.2023 0.0177  0.0214  -0.0237 102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1828 0.1966 0.1955 0.0145  0.0246  -0.0064 103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.1976 0.2043 0.1963 0.0154  0.0233  -0.0033 103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.1981 0.2022 0.1958 0.0148  0.0274  0.0015  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2073 0.2137 0.2157 0.0127  0.0313  0.0029  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2000 0.1988 0.1848 0.0172  0.0266  0.0038  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.1894 0.1850 0.1700 0.0184  0.0298  0.0086  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.1922 0.1859 0.1748 0.0159  0.0267  0.0097  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.1878 0.1804 0.1684 0.0146  0.0209  0.0070  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2050 0.1960 0.1698 0.0232  0.0289  0.0098  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2134 0.2006 0.1710 0.0261  0.0314  0.0148  104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2388 0.2257 0.1986 0.0280  0.0400  0.0200  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2350 0.2186 0.1843 0.0277  0.0265  0.0154  104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.2656 0.2480 0.2159 0.0315  0.0402  0.0242  104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2507 0.2315 0.1946 0.0315  0.0315  0.0212  104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.1989 0.1917 0.1855 0.0157  0.0312  0.0140  105 SER   A N   
785  C CA  . SER   A 99  ? 0.2002 0.1908 0.1877 0.0143  0.0288  0.0157  105 SER   A CA  
786  C C   . SER   A 99  ? 0.2270 0.2147 0.2138 0.0165  0.0349  0.0219  105 SER   A C   
787  O O   . SER   A 99  ? 0.2497 0.2379 0.2413 0.0172  0.0425  0.0247  105 SER   A O   
788  C CB  . SER   A 99  ? 0.2116 0.2054 0.2116 0.0097  0.0269  0.0125  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.2528 0.2495 0.2658 0.0077  0.0325  0.0129  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.2015 0.1858 0.1820 0.0183  0.0319  0.0242  106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.2083 0.1885 0.1862 0.0214  0.0366  0.0307  106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.2228 0.2029 0.2081 0.0184  0.0331  0.0302  106 GLU   A C   
793  O O   . GLU   A 100 ? 0.2152 0.1979 0.2037 0.0152  0.0266  0.0253  106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.2520 0.2280 0.2110 0.0288  0.0346  0.0333  106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.3012 0.2766 0.2522 0.0324  0.0392  0.0342  106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.3589 0.3304 0.2897 0.0404  0.0364  0.0352  106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.3766 0.3443 0.2980 0.0457  0.0357  0.0392  106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.3303 0.3026 0.2542 0.0421  0.0346  0.0316  106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.2340 0.2110 0.2229 0.0194  0.0380  0.0356  107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.2286 0.2057 0.2261 0.0164  0.0353  0.0348  107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.2322 0.2101 0.2237 0.0173  0.0262  0.0319  107 PRO   A C   
802  O O   . PRO   A 101 ? 0.2398 0.2200 0.2399 0.0132  0.0228  0.0283  107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.2533 0.2253 0.2523 0.0192  0.0426  0.0422  107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.2567 0.2272 0.2565 0.0204  0.0517  0.0456  107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.2389 0.2114 0.2255 0.0232  0.0476  0.0428  107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.2171 0.1935 0.1948 0.0228  0.0222  0.0328  108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2110 0.1889 0.1857 0.0236  0.0133  0.0290  108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.2062 0.1875 0.1848 0.0192  0.0085  0.0223  108 GLY   A C   
809  O O   . GLY   A 102 ? 0.2100 0.1927 0.1899 0.0186  0.0021  0.0186  108 GLY   A O   
810  N N   . ASP   A 103 ? 0.1947 0.1772 0.1756 0.0165  0.0119  0.0206  109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.1797 0.1643 0.1640 0.0129  0.0086  0.0152  109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1726 0.1590 0.1685 0.0083  0.0085  0.0133  109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1642 0.1515 0.1624 0.0061  0.0059  0.0095  109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.1942 0.1797 0.1767 0.0127  0.0119  0.0140  109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.2107 0.1943 0.1807 0.0174  0.0110  0.0143  109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.2136 0.1960 0.1772 0.0197  0.0053  0.0123  109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.2200 0.2036 0.1873 0.0191  0.0162  0.0161  109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1668 0.1530 0.1696 0.0072  0.0116  0.0160  110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1578 0.1455 0.1706 0.0036  0.0116  0.0139  110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1659 0.1537 0.1791 0.0031  0.0067  0.0117  110 CYS   A C   
821  O O   . CYS   A 104 ? 0.1984 0.1856 0.2082 0.0054  0.0034  0.0127  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1762 0.1627 0.1959 0.0032  0.0153  0.0171  110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.1998 0.1868 0.2265 0.0018  0.0222  0.0179  110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1500 0.1386 0.1674 0.0006  0.0065  0.0086  111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1549 0.1433 0.1749 -0.0003 0.0036  0.0067  111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.1641 0.1516 0.1799 -0.0003 0.0019  0.0041  111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1706 0.1573 0.1902 -0.0015 0.0011  0.0024  111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1525 0.1396 0.1612 0.0012  0.0018  0.0039  112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1507 0.1363 0.1553 0.0015  0.0006  0.0013  112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1467 0.1315 0.1533 0.0003  0.0032  0.0001  112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1557 0.1421 0.1635 0.0003  0.0055  0.0004  112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1417 0.1236 0.1491 -0.0002 0.0029  -0.0014 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1513 0.1312 0.1587 0.0000  0.0061  -0.0016 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1514 0.1304 0.1517 0.0023  0.0070  -0.0025 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1634 0.1410 0.1598 0.0030  0.0056  -0.0034 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1712 0.1476 0.1839 -0.0012 0.0073  -0.0018 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.1774 0.1557 0.1985 -0.0029 0.0077  -0.0008 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.1943 0.1662 0.2037 0.0004  0.0114  -0.0013 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.1975 0.1732 0.2275 -0.0046 0.0093  -0.0012 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1433 0.1231 0.1419 0.0039  0.0089  -0.0028 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1461 0.1251 0.1382 0.0072  0.0095  -0.0039 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1621 0.1356 0.1515 0.0091  0.0124  -0.0029 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1728 0.1458 0.1644 0.0091  0.0143  -0.0022 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1578 0.1419 0.1506 0.0086  0.0090  -0.0057 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1840 0.1686 0.1709 0.0130  0.0087  -0.0076 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1924 0.1769 0.1759 0.0141  0.0081  -0.0078 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1986 0.1894 0.1895 0.0142  0.0072  -0.0109 114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1649 0.1336 0.1498 0.0108  0.0136  -0.0025 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1887 0.1506 0.1707 0.0132  0.0179  -0.0006 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.1936 0.1530 0.1662 0.0185  0.0187  -0.0006 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2001 0.1611 0.1704 0.0191  0.0163  -0.0021 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2357 0.1921 0.2232 0.0104  0.0195  0.0001  115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3315 0.2906 0.3289 0.0056  0.0174  -0.0008 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3611 0.3150 0.3651 0.0035  0.0184  -0.0016 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.3991 0.3466 0.4060 0.0043  0.0252  0.0012  115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.3713 0.3190 0.3872 0.0021  0.0279  0.0023  115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.2841 0.2379 0.3076 -0.0011 0.0236  0.0005  115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.3212 0.2625 0.3384 0.0037  0.0355  0.0057  115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2032 0.1577 0.1698 0.0230  0.0226  0.0014  116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2012 0.1509 0.1578 0.0292  0.0243  0.0024  116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2148 0.1539 0.1710 0.0300  0.0312  0.0066  116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2322 0.1691 0.1977 0.0251  0.0337  0.0076  116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2295 0.1822 0.1776 0.0357  0.0231  0.0013  116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2248 0.1730 0.1700 0.0381  0.0282  0.0041  116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.2368 0.1690 0.1832 0.0364  0.0346  0.0090  117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.2566 0.1772 0.2034 0.0375  0.0428  0.0136  117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.2755 0.1924 0.2236 0.0381  0.0490  0.0171  117 GLN   A C   
868  O O   . GLN   A 111 ? 0.2892 0.1971 0.2423 0.0371  0.0568  0.0210  117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.2922 0.2053 0.2264 0.0457  0.0459  0.0164  117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.3653 0.2789 0.2847 0.0550  0.0461  0.0177  117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.5217 0.4301 0.4277 0.0642  0.0469  0.0195  117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.5717 0.4875 0.4729 0.0677  0.0400  0.0155  117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.5265 0.4219 0.4273 0.0685  0.0558  0.0255  117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.2492 0.1724 0.1938 0.0397  0.0463  0.0157  118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.2448 0.1647 0.1887 0.0415  0.0523  0.0187  118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.2402 0.1648 0.1988 0.0337  0.0516  0.0174  118 HIS   A C   
877  O O   . HIS   A 112 ? 0.2482 0.1692 0.2089 0.0344  0.0580  0.0204  118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.2549 0.1776 0.1842 0.0498  0.0502  0.0176  118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.3055 0.2242 0.2191 0.0593  0.0500  0.0186  118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.3335 0.2604 0.2427 0.0618  0.0413  0.0135  118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.3315 0.2388 0.2339 0.0668  0.0578  0.0244  118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.3479 0.2691 0.2434 0.0709  0.0430  0.0157  118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.3456 0.2543 0.2356 0.0745  0.0530  0.0226  118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2193 0.1519 0.1871 0.0272  0.0444  0.0132  119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2144 0.1519 0.1955 0.0206  0.0428  0.0117  119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.1905 0.1379 0.1735 0.0178  0.0345  0.0075  119 GLY   A C   
887  O O   . GLY   A 113 ? 0.1982 0.1488 0.1755 0.0193  0.0300  0.0053  119 GLY   A O   
888  N N   . VAL   A 114 ? 0.1817 0.1333 0.1734 0.0139  0.0334  0.0068  120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1790 0.1388 0.1737 0.0113  0.0270  0.0037  120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1768 0.1400 0.1637 0.0154  0.0252  0.0018  120 VAL   A C   
891  O O   . VAL   A 114 ? 0.1812 0.1426 0.1645 0.0187  0.0282  0.0023  120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.1808 0.1434 0.1871 0.0068  0.0266  0.0038  120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.1800 0.1496 0.1884 0.0050  0.0214  0.0016  120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.1879 0.1489 0.2038 0.0028  0.0265  0.0040  120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1665 0.1350 0.1523 0.0151  0.0203  -0.0010 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1753 0.1485 0.1575 0.0182  0.0175  -0.0043 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1768 0.1557 0.1680 0.0144  0.0150  -0.0063 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1773 0.1586 0.1689 0.0162  0.0142  -0.0090 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1903 0.1660 0.1681 0.0204  0.0144  -0.0063 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2029 0.1853 0.1811 0.0230  0.0106  -0.0112 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.1938 0.1631 0.1619 0.0253  0.0171  -0.0043 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1573 0.1381 0.1553 0.0097  0.0137  -0.0052 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1583 0.1433 0.1641 0.0066  0.0122  -0.0061 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1519 0.1377 0.1618 0.0032  0.0111  -0.0040 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1529 0.1361 0.1604 0.0028  0.0109  -0.0026 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1514 0.1401 0.1673 0.0012  0.0105  -0.0038 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1479 0.1369 0.1654 -0.0006 0.0095  -0.0014 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1408 0.1326 0.1600 -0.0008 0.0099  -0.0014 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1430 0.1372 0.1673 -0.0010 0.0109  -0.0033 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1552 0.1435 0.1783 -0.0021 0.0095  0.0007  123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1684 0.1578 0.1973 -0.0026 0.0110  -0.0001 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1845 0.1704 0.2082 -0.0024 0.0094  0.0010  123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.1820 0.1709 0.2171 -0.0036 0.0110  0.0024  123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1319 0.1235 0.1479 -0.0005 0.0095  0.0006  124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1273 0.1209 0.1454 -0.0003 0.0117  0.0018  124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1347 0.1284 0.1607 -0.0017 0.0138  0.0034  124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1425 0.1343 0.1689 -0.0020 0.0130  0.0054  124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1468 0.1388 0.1578 0.0013  0.0113  0.0044  124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1676 0.1605 0.1805 0.0021  0.0154  0.0070  124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1633 0.1547 0.1672 0.0027  0.0095  0.0024  124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1354 0.1315 0.1688 -0.0026 0.0165  0.0021  125 SER   A N   
922  C CA  . SER   A 119 ? 0.1425 0.1380 0.1852 -0.0041 0.0192  0.0032  125 SER   A CA  
923  C C   . SER   A 119 ? 0.1706 0.1668 0.2202 -0.0046 0.0242  0.0048  125 SER   A C   
924  O O   . SER   A 119 ? 0.1834 0.1772 0.2388 -0.0052 0.0279  0.0081  125 SER   A O   
925  C CB  . SER   A 119 ? 0.1458 0.1430 0.1949 -0.0051 0.0178  -0.0019 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1640 0.1605 0.2236 -0.0068 0.0204  -0.0022 125 SER   A OG  
927  N N   . THR   A 120 ? 0.1552 0.1547 0.2056 -0.0043 0.0249  0.0026  126 THR   A N   
928  C CA  . THR   A 120 ? 0.1635 0.1640 0.2230 -0.0049 0.0309  0.0042  126 THR   A CA  
929  C C   . THR   A 120 ? 0.1657 0.1673 0.2174 -0.0027 0.0319  0.0057  126 THR   A C   
930  O O   . THR   A 120 ? 0.1672 0.1690 0.2085 -0.0010 0.0275  0.0042  126 THR   A O   
931  C CB  . THR   A 120 ? 0.1895 0.1949 0.2655 -0.0074 0.0314  -0.0023 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.2003 0.2111 0.2751 -0.0063 0.0275  -0.0079 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.1956 0.2003 0.2782 -0.0091 0.0294  -0.0055 126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.1801 0.1816 0.2371 -0.0023 0.0385  0.0088  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.1935 0.1963 0.2443 0.0001  0.0402  0.0098  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.2022 0.2043 0.2608 0.0005  0.0494  0.0140  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.2090 0.2083 0.2767 -0.0010 0.0548  0.0172  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.2234 0.2272 0.2779 0.0028  0.0517  0.0144  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.2346 0.2371 0.2941 0.0042  0.0618  0.0194  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.2376 0.2462 0.3035 0.0045  0.0634  0.0158  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.2351 0.2502 0.3087 0.0026  0.0575  0.0084  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.2391 0.2456 0.3008 0.0079  0.0714  0.0209  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.2523 0.2647 0.3219 0.0086  0.0748  0.0182  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.2443 0.2616 0.3079 0.0095  0.0656  0.0115  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.2471 0.2720 0.3238 0.0086  0.0653  0.0062  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.2878 0.3059 0.3849 0.0042  0.0809  0.0154  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.3789 0.3906 0.4821 0.0040  0.0925  0.0234  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.4135 0.4192 0.5044 0.0087  0.1004  0.0313  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.3903 0.4020 0.5107 -0.0005 0.0938  0.0218  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.2241 0.2370 0.2681 0.0118  0.0588  0.0121  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.2088 0.2242 0.2451 0.0133  0.0513  0.0069  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.1923 0.2113 0.2346 0.0105  0.0433  0.0008  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2027 0.2239 0.2404 0.0121  0.0378  -0.0033 130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1801 0.1989 0.2312 0.0071  0.0429  0.0006  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1697 0.1907 0.2237 0.0053  0.0356  -0.0048 131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1834 0.1978 0.2259 0.0047  0.0325  -0.0017 131 LEU   A C   
957  O O   . LEU   A 125 ? 0.2185 0.2280 0.2563 0.0049  0.0361  0.0039  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1750 0.2013 0.2493 0.0019  0.0370  -0.0088 131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.2186 0.2536 0.3089 0.0020  0.0380  -0.0145 131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2528 0.2920 0.3649 -0.0018 0.0399  -0.0185 131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.2228 0.2623 0.3077 0.0051  0.0296  -0.0209 131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1438 0.1583 0.1826 0.0046  0.0261  -0.0053 132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1452 0.1546 0.1768 0.0037  0.0234  -0.0032 132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1478 0.1598 0.1860 0.0024  0.0196  -0.0081 132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1501 0.1657 0.1890 0.0041  0.0166  -0.0128 132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1649 0.1697 0.1814 0.0058  0.0202  -0.0015 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1795 0.1856 0.1914 0.0079  0.0170  -0.0053 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1777 0.1786 0.1908 0.0045  0.0175  -0.0002 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1396 0.1495 0.1817 0.0003  0.0199  -0.0071 133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1420 0.1537 0.1893 -0.0003 0.0167  -0.0118 133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1474 0.1544 0.1861 -0.0002 0.0144  -0.0099 133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1523 0.1554 0.1877 -0.0011 0.0159  -0.0052 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1320 0.1391 0.1667 0.0016  0.0111  -0.0134 134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1376 0.1402 0.1652 0.0020  0.0099  -0.0116 134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1409 0.1442 0.1729 0.0022  0.0091  -0.0150 134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1344 0.1412 0.1687 0.0043  0.0070  -0.0203 134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1401 0.1406 0.1571 0.0050  0.0083  -0.0118 134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1403 0.1401 0.1524 0.0056  0.0086  -0.0100 134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1492 0.1452 0.1570 0.0045  0.0090  -0.0063 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1602 0.1638 0.1726 0.0077  0.0080  -0.0126 134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1524 0.1476 0.1550 0.0056  0.0091  -0.0054 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1708 0.1736 0.1784 0.0087  0.0087  -0.0110 134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1621 0.1604 0.1642 0.0076  0.0093  -0.0075 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1360 0.1360 0.1689 0.0007  0.0102  -0.0124 135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1349 0.1345 0.1703 0.0013  0.0098  -0.0152 135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1346 0.1315 0.1595 0.0049  0.0090  -0.0156 135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1491 0.1423 0.1692 0.0046  0.0103  -0.0116 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1495 0.1464 0.1896 -0.0012 0.0117  -0.0117 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1418 0.1402 0.1636 0.0088  0.0072  -0.0206 136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1623 0.1571 0.1725 0.0136  0.0076  -0.0203 136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1563 0.1469 0.1655 0.0136  0.0105  -0.0180 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1551 0.1469 0.1714 0.0120  0.0105  -0.0199 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.1923 0.1903 0.1983 0.0192  0.0042  -0.0267 136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2631 0.2567 0.2545 0.0259  0.0050  -0.0258 136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2458 0.2352 0.2310 0.0262  0.0075  -0.0210 136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3353 0.3286 0.3212 0.0312  0.0038  -0.0297 136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1459 0.1313 0.1474 0.0155  0.0136  -0.0141 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1601 0.1416 0.1611 0.0163  0.0174  -0.0120 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.1781 0.1548 0.1665 0.0231  0.0203  -0.0116 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.1951 0.1678 0.1820 0.0247  0.0248  -0.0094 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1766 0.1557 0.1839 0.0118  0.0202  -0.0069 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1740 0.1569 0.1915 0.0066  0.0177  -0.0066 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1821 0.1579 0.1849 0.0120  0.0216  -0.0039 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.1880 0.1649 0.1671 0.0279  0.0182  -0.0135 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.2004 0.1715 0.1652 0.0357  0.0216  -0.0119 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.2368 0.2069 0.1941 0.0420  0.0220  -0.0151 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2605 0.2240 0.2060 0.0483  0.0272  -0.0120 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.2035 0.1752 0.1597 0.0402  0.0186  -0.0132 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2046 0.1750 0.1649 0.0354  0.0195  -0.0093 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2293 0.2009 0.1821 0.0400  0.0164  -0.0110 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2074 0.1881 0.1667 0.0389  0.0098  -0.0173 138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2345 0.2190 0.1913 0.0420  0.0059  -0.0202 138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2245 0.2040 0.1706 0.0472  0.0075  -0.0173 138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2361 0.2292 0.2025 0.0400  0.0008  -0.0259 138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2196 0.1956 0.1837 0.0407  0.0171  -0.0214 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2335 0.2088 0.1908 0.0470  0.0167  -0.0259 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2465 0.2181 0.2082 0.0447  0.0224  -0.0228 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2679 0.2373 0.2220 0.0507  0.0236  -0.0255 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2459 0.2290 0.2103 0.0468  0.0089  -0.0353 139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.2968 0.2839 0.2797 0.0374  0.0080  -0.0359 139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2849 0.2721 0.2748 0.0310  0.0097  -0.0306 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3177 0.3073 0.3075 0.0370  0.0056  -0.0418 139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2161 0.1872 0.1895 0.0369  0.0255  -0.0175 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.2071 0.1759 0.1873 0.0344  0.0305  -0.0147 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.2235 0.1851 0.1962 0.0381  0.0388  -0.0086 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.2253 0.1848 0.2052 0.0335  0.0427  -0.0031 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.2013 0.1734 0.1975 0.0254  0.0293  -0.0124 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2162 0.1944 0.2210 0.0216  0.0229  -0.0173 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2107 0.1908 0.2276 0.0144  0.0225  -0.0135 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2284 0.2081 0.2357 0.0235  0.0212  -0.0230 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2343 0.1915 0.1919 0.0472  0.0417  -0.0096 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.2589 0.2079 0.2076 0.0520  0.0510  -0.0029 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.2646 0.2111 0.2243 0.0482  0.0588  0.0018  141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.2869 0.2277 0.2479 0.0481  0.0670  0.0083  141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.2869 0.2313 0.2148 0.0641  0.0527  -0.0049 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.3195 0.2676 0.2365 0.0695  0.0438  -0.0112 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.3392 0.2818 0.2331 0.0834  0.0459  -0.0124 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.3276 0.2763 0.2463 0.0663  0.0419  -0.0083 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.2514 0.2020 0.2207 0.0450  0.0565  -0.0016 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.2596 0.2090 0.2407 0.0418  0.0631  0.0021  142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.2615 0.2130 0.2594 0.0332  0.0637  0.0062  142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.2804 0.2307 0.2892 0.0309  0.0700  0.0098  142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.2534 0.2067 0.2406 0.0408  0.0597  -0.0028 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2493 0.2094 0.2452 0.0351  0.0502  -0.0077 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2521 0.2151 0.2423 0.0372  0.0430  -0.0143 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2373 0.2017 0.2496 0.0268  0.0474  -0.0061 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2463 0.2146 0.2494 0.0302  0.0373  -0.0163 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2334 0.2023 0.2485 0.0243  0.0398  -0.0110 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2359 0.2010 0.2612 0.0219  0.0505  -0.0014 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2287 0.2016 0.2568 0.0177  0.0363  -0.0101 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2372 0.2070 0.2748 0.0157  0.0455  -0.0015 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2289 0.2019 0.2667 0.0141  0.0389  -0.0053 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.2488 0.2035 0.2492 0.0288  0.0573  0.0053  143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.2488 0.2055 0.2637 0.0217  0.0569  0.0081  143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.3065 0.2571 0.3235 0.0224  0.0657  0.0134  143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.3004 0.2526 0.3329 0.0170  0.0671  0.0151  143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2307 0.1910 0.2449 0.0184  0.0492  0.0061  143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2262 0.1928 0.2451 0.0152  0.0415  0.0021  143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2284 0.1975 0.2448 0.0131  0.0357  0.0008  143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2201 0.1901 0.2542 0.0100  0.0406  0.0031  143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.3670 0.3105 0.3687 0.0296  0.0717  0.0158  144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.4341 0.3698 0.4359 0.0315  0.0819  0.0216  144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.4969 0.4284 0.5031 0.0341  0.0927  0.0255  144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.5126 0.4367 0.5198 0.0360  0.1028  0.0309  144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.4857 0.4144 0.4665 0.0399  0.0843  0.0234  144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.5802 0.5114 0.5557 0.0387  0.0760  0.0207  144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.5915 0.5270 0.5802 0.0311  0.0713  0.0196  144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.6342 0.5632 0.5921 0.0461  0.0742  0.0196  144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.5273 0.4623 0.5356 0.0348  0.0918  0.0230  145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.5664 0.4976 0.5792 0.0376  0.1027  0.0267  145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.5862 0.5248 0.6182 0.0316  0.0999  0.0243  145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.6029 0.5401 0.6452 0.0318  0.1086  0.0272  145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.6117 0.5372 0.6024 0.0484  0.1072  0.0267  145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.6947 0.6259 0.6777 0.0501  0.0970  0.0194  145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.8084 0.7359 0.7666 0.0600  0.0945  0.0166  145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.8374 0.7653 0.7865 0.0657  0.0928  0.0122  145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.8407 0.7650 0.7888 0.0627  0.0938  0.0184  145 GLU   A OE2 
1078 N N   . SER   B 1   ? 0.2806 0.2565 0.2764 -0.0045 -0.0177 -0.0134 7   SER   C N   
1079 C CA  . SER   B 1   ? 0.2866 0.2655 0.2932 -0.0018 -0.0195 -0.0126 7   SER   C CA  
1080 C C   . SER   B 1   ? 0.2735 0.2530 0.2842 0.0004  -0.0187 -0.0105 7   SER   C C   
1081 O O   . SER   B 1   ? 0.2910 0.2680 0.2960 -0.0002 -0.0187 -0.0090 7   SER   C O   
1082 C CB  . SER   B 1   ? 0.3185 0.2963 0.3264 -0.0025 -0.0257 -0.0120 7   SER   C CB  
1083 O OG  . SER   B 1   ? 0.3586 0.3325 0.3610 -0.0035 -0.0303 -0.0092 7   SER   C OG  
1084 N N   . GLY   B 2   ? 0.2432 0.2259 0.2635 0.0023  -0.0176 -0.0108 8   GLY   C N   
1085 C CA  . GLY   B 2   ? 0.2258 0.2090 0.2504 0.0039  -0.0161 -0.0099 8   GLY   C CA  
1086 C C   . GLY   B 2   ? 0.2043 0.1910 0.2355 0.0045  -0.0120 -0.0111 8   GLY   C C   
1087 O O   . GLY   B 2   ? 0.2071 0.1954 0.2383 0.0038  -0.0101 -0.0118 8   GLY   C O   
1088 N N   . ALA   B 3   ? 0.1852 0.1727 0.2222 0.0054  -0.0107 -0.0114 9   ALA   C N   
1089 C CA  . ALA   B 3   ? 0.1807 0.1708 0.2225 0.0050  -0.0063 -0.0126 9   ALA   C CA  
1090 C C   . ALA   B 3   ? 0.1739 0.1632 0.2164 0.0049  -0.0032 -0.0132 9   ALA   C C   
1091 O O   . ALA   B 3   ? 0.1922 0.1794 0.2353 0.0060  -0.0050 -0.0129 9   ALA   C O   
1092 C CB  . ALA   B 3   ? 0.1853 0.1781 0.2371 0.0055  -0.0070 -0.0140 9   ALA   C CB  
1093 N N   . ILE   B 4   ? 0.1731 0.1638 0.2153 0.0031  0.0012  -0.0142 10  ILE   C N   
1094 C CA  . ILE   B 4   ? 0.1663 0.1564 0.2090 0.0021  0.0053  -0.0159 10  ILE   C CA  
1095 C C   . ILE   B 4   ? 0.1796 0.1721 0.2318 0.0016  0.0086  -0.0187 10  ILE   C C   
1096 O O   . ILE   B 4   ? 0.1713 0.1659 0.2252 0.0004  0.0096  -0.0187 10  ILE   C O   
1097 C CB  . ILE   B 4   ? 0.1692 0.1586 0.2029 -0.0009 0.0080  -0.0149 10  ILE   C CB  
1098 C CG1 . ILE   B 4   ? 0.1827 0.1705 0.2093 -0.0005 0.0051  -0.0123 10  ILE   C CG1 
1099 C CG2 . ILE   B 4   ? 0.1825 0.1706 0.2149 -0.0030 0.0125  -0.0173 10  ILE   C CG2 
1100 C CD1 . ILE   B 4   ? 0.2008 0.1885 0.2209 -0.0034 0.0062  -0.0105 10  ILE   C CD1 
1101 N N   . TYR   B 5   ? 0.1882 0.1804 0.2481 0.0025  0.0105  -0.0213 11  TYR   C N   
1102 C CA  . TYR   B 5   ? 0.1836 0.1783 0.2548 0.0021  0.0146  -0.0249 11  TYR   C CA  
1103 C C   . TYR   B 5   ? 0.2009 0.1947 0.2700 -0.0009 0.0218  -0.0284 11  TYR   C C   
1104 O O   . TYR   B 5   ? 0.2247 0.2162 0.2958 0.0001  0.0224  -0.0300 11  TYR   C O   
1105 C CB  . TYR   B 5   ? 0.1797 0.1751 0.2651 0.0056  0.0107  -0.0257 11  TYR   C CB  
1106 C CG  . TYR   B 5   ? 0.1710 0.1672 0.2574 0.0074  0.0037  -0.0227 11  TYR   C CG  
1107 C CD1 . TYR   B 5   ? 0.1751 0.1748 0.2682 0.0069  0.0038  -0.0234 11  TYR   C CD1 
1108 C CD2 . TYR   B 5   ? 0.1935 0.1868 0.2729 0.0087  -0.0025 -0.0193 11  TYR   C CD2 
1109 C CE1 . TYR   B 5   ? 0.2080 0.2080 0.3009 0.0079  -0.0025 -0.0211 11  TYR   C CE1 
1110 C CE2 . TYR   B 5   ? 0.2123 0.2059 0.2905 0.0092  -0.0083 -0.0171 11  TYR   C CE2 
1111 C CZ  . TYR   B 5   ? 0.2281 0.2249 0.3129 0.0089  -0.0084 -0.0181 11  TYR   C CZ  
1112 O OH  . TYR   B 5   ? 0.2650 0.2616 0.3478 0.0089  -0.0140 -0.0165 11  TYR   C OH  
1113 N N   . VAL   B 6   ? 0.2022 0.1969 0.2666 -0.0050 0.0271  -0.0297 12  VAL   C N   
1114 C CA  . VAL   B 6   ? 0.2272 0.2203 0.2863 -0.0092 0.0342  -0.0332 12  VAL   C CA  
1115 C C   . VAL   B 6   ? 0.2440 0.2395 0.3082 -0.0127 0.0409  -0.0367 12  VAL   C C   
1116 O O   . VAL   B 6   ? 0.2353 0.2322 0.2966 -0.0144 0.0402  -0.0344 12  VAL   C O   
1117 C CB  . VAL   B 6   ? 0.2648 0.2550 0.3066 -0.0126 0.0332  -0.0299 12  VAL   C CB  
1118 C CG1 . VAL   B 6   ? 0.2765 0.2676 0.3120 -0.0138 0.0296  -0.0252 12  VAL   C CG1 
1119 C CG2 . VAL   B 6   ? 0.2818 0.2697 0.3155 -0.0183 0.0401  -0.0334 12  VAL   C CG2 
1120 N N   . GLY   B 7   ? 0.2441 0.2401 0.3177 -0.0137 0.0477  -0.0427 13  GLY   C N   
1121 C CA  . GLY   B 7   ? 0.2493 0.2478 0.3288 -0.0175 0.0554  -0.0470 13  GLY   C CA  
1122 C C   . GLY   B 7   ? 0.2517 0.2544 0.3438 -0.0146 0.0520  -0.0455 13  GLY   C C   
1123 O O   . GLY   B 7   ? 0.2691 0.2732 0.3730 -0.0090 0.0458  -0.0443 13  GLY   C O   
1124 N N   . ASN   B 8   ? 0.2432 0.2474 0.3314 -0.0185 0.0546  -0.0445 14  ASN   C N   
1125 C CA  . ASN   B 8   ? 0.2403 0.2481 0.3396 -0.0160 0.0509  -0.0429 14  ASN   C CA  
1126 C C   . ASN   B 8   ? 0.2213 0.2279 0.3099 -0.0151 0.0432  -0.0363 14  ASN   C C   
1127 O O   . ASN   B 8   ? 0.2239 0.2324 0.3152 -0.0160 0.0422  -0.0348 14  ASN   C O   
1128 C CB  . ASN   B 8   ? 0.2827 0.2936 0.3897 -0.0202 0.0588  -0.0468 14  ASN   C CB  
1129 C CG  . ASN   B 8   ? 0.3899 0.4032 0.5142 -0.0196 0.0657  -0.0540 14  ASN   C CG  
1130 O OD1 . ASN   B 8   ? 0.4142 0.4299 0.5561 -0.0140 0.0617  -0.0552 14  ASN   C OD1 
1131 N ND2 . ASN   B 8   ? 0.4211 0.4334 0.5406 -0.0256 0.0762  -0.0590 14  ASN   C ND2 
1132 N N   . TYR   B 9   ? 0.2061 0.2096 0.2839 -0.0134 0.0383  -0.0330 15  TYR   C N   
1133 C CA  . TYR   B 9   ? 0.1974 0.1997 0.2664 -0.0125 0.0318  -0.0276 15  TYR   C CA  
1134 C C   . TYR   B 9   ? 0.1782 0.1799 0.2492 -0.0072 0.0245  -0.0256 15  TYR   C C   
1135 O O   . TYR   B 9   ? 0.1773 0.1778 0.2497 -0.0052 0.0239  -0.0269 15  TYR   C O   
1136 C CB  . TYR   B 9   ? 0.2149 0.2137 0.2674 -0.0166 0.0326  -0.0247 15  TYR   C CB  
1137 C CG  . TYR   B 9   ? 0.2419 0.2399 0.2878 -0.0232 0.0387  -0.0253 15  TYR   C CG  
1138 C CD1 . TYR   B 9   ? 0.2680 0.2676 0.3176 -0.0253 0.0398  -0.0244 15  TYR   C CD1 
1139 C CD2 . TYR   B 9   ? 0.2699 0.2650 0.3052 -0.0281 0.0435  -0.0269 15  TYR   C CD2 
1140 C CE1 . TYR   B 9   ? 0.2904 0.2886 0.3325 -0.0323 0.0455  -0.0245 15  TYR   C CE1 
1141 C CE2 . TYR   B 9   ? 0.2932 0.2868 0.3200 -0.0354 0.0491  -0.0273 15  TYR   C CE2 
1142 C CZ  . TYR   B 9   ? 0.3167 0.3119 0.3468 -0.0376 0.0501  -0.0259 15  TYR   C CZ  
1143 O OH  . TYR   B 9   ? 0.3472 0.3403 0.3677 -0.0456 0.0556  -0.0257 15  TYR   C OH  
1144 N N   . ARG   B 10  ? 0.1539 0.1560 0.2240 -0.0057 0.0191  -0.0225 16  ARG   C N   
1145 C CA  . ARG   B 10  ? 0.1521 0.1530 0.2205 -0.0021 0.0125  -0.0204 16  ARG   C CA  
1146 C C   . ARG   B 10  ? 0.1501 0.1492 0.2078 -0.0032 0.0106  -0.0170 16  ARG   C C   
1147 O O   . ARG   B 10  ? 0.1625 0.1622 0.2202 -0.0050 0.0108  -0.0158 16  ARG   C O   
1148 C CB  . ARG   B 10  ? 0.1650 0.1679 0.2435 0.0004  0.0082  -0.0208 16  ARG   C CB  
1149 C CG  . ARG   B 10  ? 0.1853 0.1866 0.2591 0.0025  0.0017  -0.0185 16  ARG   C CG  
1150 C CD  . ARG   B 10  ? 0.1900 0.1928 0.2729 0.0041  -0.0032 -0.0191 16  ARG   C CD  
1151 N NE  . ARG   B 10  ? 0.2031 0.2048 0.2809 0.0040  -0.0072 -0.0178 16  ARG   C NE  
1152 C CZ  . ARG   B 10  ? 0.2278 0.2272 0.3000 0.0048  -0.0121 -0.0168 16  ARG   C CZ  
1153 N NH1 . ARG   B 10  ? 0.2269 0.2244 0.2972 0.0060  -0.0143 -0.0159 16  ARG   C NH1 
1154 N NH2 . ARG   B 10  ? 0.2130 0.2114 0.2809 0.0040  -0.0145 -0.0167 16  ARG   C NH2 
1155 N N   . VAL   B 11  ? 0.1585 0.1552 0.2084 -0.0025 0.0088  -0.0154 17  VAL   C N   
1156 C CA  . VAL   B 11  ? 0.1554 0.1506 0.1976 -0.0034 0.0070  -0.0125 17  VAL   C CA  
1157 C C   . VAL   B 11  ? 0.1539 0.1487 0.1962 -0.0007 0.0027  -0.0120 17  VAL   C C   
1158 O O   . VAL   B 11  ? 0.1648 0.1584 0.2058 0.0010  0.0011  -0.0125 17  VAL   C O   
1159 C CB  . VAL   B 11  ? 0.1757 0.1689 0.2095 -0.0052 0.0084  -0.0113 17  VAL   C CB  
1160 C CG1 . VAL   B 11  ? 0.1708 0.1631 0.1997 -0.0064 0.0062  -0.0080 17  VAL   C CG1 
1161 C CG2 . VAL   B 11  ? 0.1796 0.1726 0.2117 -0.0086 0.0132  -0.0129 17  VAL   C CG2 
1162 N N   . VAL   B 12  ? 0.1501 0.1452 0.1935 -0.0007 0.0009  -0.0112 18  VAL   C N   
1163 C CA  . VAL   B 12  ? 0.1457 0.1399 0.1879 0.0010  -0.0022 -0.0116 18  VAL   C CA  
1164 C C   . VAL   B 12  ? 0.1459 0.1393 0.1860 0.0003  -0.0023 -0.0104 18  VAL   C C   
1165 O O   . VAL   B 12  ? 0.1510 0.1447 0.1925 -0.0012 -0.0012 -0.0087 18  VAL   C O   
1166 C CB  . VAL   B 12  ? 0.1852 0.1804 0.2332 0.0017  -0.0045 -0.0133 18  VAL   C CB  
1167 C CG1 . VAL   B 12  ? 0.2325 0.2284 0.2849 0.0029  -0.0057 -0.0143 18  VAL   C CG1 
1168 C CG2 . VAL   B 12  ? 0.1757 0.1725 0.2292 0.0005  -0.0032 -0.0132 18  VAL   C CG2 
1169 N N   . ASN   B 13  ? 0.1301 0.1224 0.1678 0.0011  -0.0036 -0.0113 19  ASN   C N   
1170 C CA  . ASN   B 13  ? 0.1274 0.1193 0.1668 0.0007  -0.0032 -0.0113 19  ASN   C CA  
1171 C C   . ASN   B 13  ? 0.1375 0.1301 0.1832 0.0003  -0.0036 -0.0120 19  ASN   C C   
1172 O O   . ASN   B 13  ? 0.1473 0.1403 0.1945 0.0006  -0.0049 -0.0139 19  ASN   C O   
1173 C CB  . ASN   B 13  ? 0.1461 0.1367 0.1821 0.0009  -0.0034 -0.0135 19  ASN   C CB  
1174 C CG  . ASN   B 13  ? 0.1625 0.1521 0.1924 0.0009  -0.0029 -0.0128 19  ASN   C CG  
1175 O OD1 . ASN   B 13  ? 0.1716 0.1601 0.1968 0.0011  -0.0040 -0.0129 19  ASN   C OD1 
1176 N ND2 . ASN   B 13  ? 0.1573 0.1472 0.1884 0.0006  -0.0014 -0.0119 19  ASN   C ND2 
1177 N N   . ARG   B 14  ? 0.1491 0.1417 0.1990 -0.0006 -0.0032 -0.0101 20  ARG   C N   
1178 C CA  . ARG   B 14  ? 0.1415 0.1343 0.1978 -0.0012 -0.0036 -0.0104 20  ARG   C CA  
1179 C C   . ARG   B 14  ? 0.1491 0.1413 0.2078 -0.0004 -0.0042 -0.0142 20  ARG   C C   
1180 O O   . ARG   B 14  ? 0.1585 0.1511 0.2204 -0.0008 -0.0050 -0.0156 20  ARG   C O   
1181 C CB  . ARG   B 14  ? 0.1448 0.1368 0.2055 -0.0024 -0.0039 -0.0071 20  ARG   C CB  
1182 C CG  . ARG   B 14  ? 0.1564 0.1480 0.2235 -0.0036 -0.0044 -0.0063 20  ARG   C CG  
1183 C CD  . ARG   B 14  ? 0.1696 0.1595 0.2414 -0.0048 -0.0059 -0.0025 20  ARG   C CD  
1184 N NE  . ARG   B 14  ? 0.1698 0.1584 0.2475 -0.0066 -0.0067 -0.0004 20  ARG   C NE  
1185 C CZ  . ARG   B 14  ? 0.1860 0.1736 0.2722 -0.0058 -0.0073 -0.0024 20  ARG   C CZ  
1186 N NH1 . ARG   B 14  ? 0.1681 0.1560 0.2565 -0.0036 -0.0064 -0.0072 20  ARG   C NH1 
1187 N NH2 . ARG   B 14  ? 0.1738 0.1598 0.2653 -0.0077 -0.0083 0.0001  20  ARG   C NH2 
1188 N N   . HIS   B 15  ? 0.1491 0.1402 0.2056 0.0000  -0.0035 -0.0162 21  HIS   C N   
1189 C CA  . HIS   B 15  ? 0.1492 0.1392 0.2062 -0.0003 -0.0032 -0.0205 21  HIS   C CA  
1190 C C   . HIS   B 15  ? 0.1660 0.1555 0.2166 -0.0008 -0.0052 -0.0224 21  HIS   C C   
1191 O O   . HIS   B 15  ? 0.1850 0.1733 0.2350 -0.0019 -0.0057 -0.0259 21  HIS   C O   
1192 C CB  . HIS   B 15  ? 0.1505 0.1392 0.2076 -0.0005 -0.0008 -0.0229 21  HIS   C CB  
1193 C CG  . HIS   B 15  ? 0.1592 0.1476 0.2076 -0.0007 0.0001  -0.0233 21  HIS   C CG  
1194 N ND1 . HIS   B 15  ? 0.1590 0.1482 0.2059 0.0000  0.0002  -0.0199 21  HIS   C ND1 
1195 C CD2 . HIS   B 15  ? 0.1814 0.1680 0.2217 -0.0021 0.0008  -0.0265 21  HIS   C CD2 
1196 C CE1 . HIS   B 15  ? 0.1676 0.1559 0.2067 -0.0007 0.0012  -0.0212 21  HIS   C CE1 
1197 N NE2 . HIS   B 15  ? 0.1831 0.1696 0.2175 -0.0021 0.0015  -0.0249 21  HIS   C NE2 
1198 N N   . LEU   B 16  ? 0.1628 0.1532 0.2094 -0.0002 -0.0065 -0.0203 22  LEU   C N   
1199 C CA  . LEU   B 16  ? 0.1721 0.1621 0.2148 -0.0006 -0.0096 -0.0211 22  LEU   C CA  
1200 C C   . LEU   B 16  ? 0.1846 0.1769 0.2340 0.0000  -0.0112 -0.0199 22  LEU   C C   
1201 O O   . LEU   B 16  ? 0.1958 0.1883 0.2449 0.0001  -0.0144 -0.0200 22  LEU   C O   
1202 C CB  . LEU   B 16  ? 0.1756 0.1644 0.2106 -0.0003 -0.0102 -0.0198 22  LEU   C CB  
1203 C CG  . LEU   B 16  ? 0.2013 0.1879 0.2293 -0.0015 -0.0080 -0.0213 22  LEU   C CG  
1204 C CD1 . LEU   B 16  ? 0.2224 0.2075 0.2428 -0.0016 -0.0088 -0.0195 22  LEU   C CD1 
1205 C CD2 . LEU   B 16  ? 0.2123 0.1967 0.2365 -0.0039 -0.0084 -0.0253 22  LEU   C CD2 
1206 N N   . ALA   B 17  ? 0.1640 0.1579 0.2197 0.0001  -0.0091 -0.0186 23  ALA   C N   
1207 C CA  . ALA   B 17  ? 0.1695 0.1657 0.2317 0.0000  -0.0093 -0.0179 23  ALA   C CA  
1208 C C   . ALA   B 17  ? 0.1823 0.1791 0.2492 -0.0005 -0.0123 -0.0201 23  ALA   C C   
1209 O O   . ALA   B 17  ? 0.1890 0.1844 0.2558 -0.0013 -0.0129 -0.0219 23  ALA   C O   
1210 C CB  . ALA   B 17  ? 0.1625 0.1595 0.2287 -0.0010 -0.0064 -0.0160 23  ALA   C CB  
1211 N N   . THR   B 18  ? 0.1811 0.1800 0.2532 -0.0001 -0.0141 -0.0201 24  THR   C N   
1212 C CA  . THR   B 18  ? 0.1883 0.1880 0.2660 -0.0008 -0.0178 -0.0219 24  THR   C CA  
1213 C C   . THR   B 18  ? 0.1894 0.1914 0.2768 -0.0018 -0.0158 -0.0223 24  THR   C C   
1214 O O   . THR   B 18  ? 0.1811 0.1839 0.2701 -0.0022 -0.0116 -0.0208 24  THR   C O   
1215 C CB  . THR   B 18  ? 0.2055 0.2065 0.2867 0.0002  -0.0215 -0.0214 24  THR   C CB  
1216 O OG1 . THR   B 18  ? 0.2145 0.2185 0.3037 0.0010  -0.0179 -0.0208 24  THR   C OG1 
1217 C CG2 . THR   B 18  ? 0.2101 0.2082 0.2818 0.0008  -0.0239 -0.0204 24  THR   C CG2 
1218 N N   . HIS   B 19  ? 0.1845 0.1875 0.2782 -0.0027 -0.0192 -0.0240 25  HIS   C N   
1219 C CA  . HIS   B 19  ? 0.1884 0.1938 0.2923 -0.0039 -0.0173 -0.0244 25  HIS   C CA  
1220 C C   . HIS   B 19  ? 0.1823 0.1911 0.2932 -0.0036 -0.0137 -0.0233 25  HIS   C C   
1221 O O   . HIS   B 19  ? 0.1921 0.2018 0.3062 -0.0052 -0.0092 -0.0225 25  HIS   C O   
1222 C CB  . HIS   B 19  ? 0.2267 0.2330 0.3372 -0.0049 -0.0224 -0.0266 25  HIS   C CB  
1223 C CG  . HIS   B 19  ? 0.3325 0.3354 0.4367 -0.0063 -0.0250 -0.0287 25  HIS   C CG  
1224 N ND1 . HIS   B 19  ? 0.3810 0.3815 0.4827 -0.0070 -0.0215 -0.0293 25  HIS   C ND1 
1225 C CD2 . HIS   B 19  ? 0.3729 0.3741 0.4733 -0.0075 -0.0306 -0.0306 25  HIS   C CD2 
1226 C CE1 . HIS   B 19  ? 0.3911 0.3887 0.4884 -0.0084 -0.0242 -0.0324 25  HIS   C CE1 
1227 N NE2 . HIS   B 19  ? 0.3885 0.3863 0.4835 -0.0092 -0.0297 -0.0333 25  HIS   C NE2 
1228 N N   . ASN   B 20  ? 0.1729 0.1830 0.2856 -0.0020 -0.0155 -0.0234 26  ASN   C N   
1229 C CA  . ASN   B 20  ? 0.1671 0.1803 0.2876 -0.0019 -0.0112 -0.0235 26  ASN   C CA  
1230 C C   . ASN   B 20  ? 0.1692 0.1810 0.2818 -0.0026 -0.0054 -0.0221 26  ASN   C C   
1231 O O   . ASN   B 20  ? 0.1765 0.1901 0.2931 -0.0045 0.0000  -0.0224 26  ASN   C O   
1232 C CB  . ASN   B 20  ? 0.2001 0.2146 0.3263 0.0002  -0.0148 -0.0240 26  ASN   C CB  
1233 C CG  . ASN   B 20  ? 0.2645 0.2825 0.4018 0.0004  -0.0098 -0.0254 26  ASN   C CG  
1234 O OD1 . ASN   B 20  ? 0.2788 0.3003 0.4290 -0.0006 -0.0080 -0.0271 26  ASN   C OD1 
1235 N ND2 . ASN   B 20  ? 0.2870 0.3038 0.4198 0.0013  -0.0069 -0.0251 26  ASN   C ND2 
1236 N N   . ASP   B 21  ? 0.1701 0.1786 0.2709 -0.0018 -0.0063 -0.0206 27  ASP   C N   
1237 C CA  . ASP   B 21  ? 0.1732 0.1802 0.2663 -0.0029 -0.0017 -0.0188 27  ASP   C CA  
1238 C C   . ASP   B 21  ? 0.1763 0.1828 0.2697 -0.0057 0.0011  -0.0174 27  ASP   C C   
1239 O O   . ASP   B 21  ? 0.1881 0.1947 0.2799 -0.0082 0.0056  -0.0163 27  ASP   C O   
1240 C CB  . ASP   B 21  ? 0.1736 0.1775 0.2562 -0.0016 -0.0038 -0.0175 27  ASP   C CB  
1241 C CG  . ASP   B 21  ? 0.1919 0.1952 0.2715 0.0003  -0.0057 -0.0178 27  ASP   C CG  
1242 O OD1 . ASP   B 21  ? 0.1968 0.2016 0.2805 0.0006  -0.0035 -0.0184 27  ASP   C OD1 
1243 O OD2 . ASP   B 21  ? 0.1840 0.1852 0.2575 0.0013  -0.0091 -0.0176 27  ASP   C OD2 
1244 N N   . TRP   B 22  ? 0.1798 0.1853 0.2748 -0.0058 -0.0016 -0.0174 28  TRP   C N   
1245 C CA  . TRP   B 22  ? 0.1876 0.1919 0.2838 -0.0085 0.0003  -0.0156 28  TRP   C CA  
1246 C C   . TRP   B 22  ? 0.2009 0.2078 0.3054 -0.0110 0.0035  -0.0163 28  TRP   C C   
1247 O O   . TRP   B 22  ? 0.2137 0.2195 0.3168 -0.0143 0.0067  -0.0140 28  TRP   C O   
1248 C CB  . TRP   B 22  ? 0.1786 0.1808 0.2760 -0.0078 -0.0031 -0.0162 28  TRP   C CB  
1249 C CG  . TRP   B 22  ? 0.1633 0.1624 0.2537 -0.0068 -0.0039 -0.0149 28  TRP   C CG  
1250 C CD1 . TRP   B 22  ? 0.1846 0.1827 0.2705 -0.0048 -0.0061 -0.0167 28  TRP   C CD1 
1251 C CD2 . TRP   B 22  ? 0.1551 0.1518 0.2433 -0.0082 -0.0028 -0.0115 28  TRP   C CD2 
1252 N NE1 . TRP   B 22  ? 0.1894 0.1852 0.2716 -0.0045 -0.0055 -0.0152 28  TRP   C NE1 
1253 C CE2 . TRP   B 22  ? 0.1736 0.1685 0.2579 -0.0064 -0.0042 -0.0117 28  TRP   C CE2 
1254 C CE3 . TRP   B 22  ? 0.1668 0.1625 0.2558 -0.0113 -0.0011 -0.0079 28  TRP   C CE3 
1255 C CZ2 . TRP   B 22  ? 0.1715 0.1641 0.2553 -0.0070 -0.0043 -0.0086 28  TRP   C CZ2 
1256 C CZ3 . TRP   B 22  ? 0.1724 0.1652 0.2590 -0.0122 -0.0020 -0.0041 28  TRP   C CZ3 
1257 C CH2 . TRP   B 22  ? 0.1676 0.1591 0.2525 -0.0098 -0.0038 -0.0045 28  TRP   C CH2 
1258 N N   . ALA   B 23  ? 0.1816 0.1918 0.2948 -0.0099 0.0025  -0.0191 29  ALA   C N   
1259 C CA  . ALA   B 23  ? 0.1883 0.2017 0.3116 -0.0124 0.0062  -0.0204 29  ALA   C CA  
1260 C C   . ALA   B 23  ? 0.1983 0.2130 0.3203 -0.0143 0.0126  -0.0207 29  ALA   C C   
1261 O O   . ALA   B 23  ? 0.2025 0.2193 0.3308 -0.0175 0.0176  -0.0218 29  ALA   C O   
1262 C CB  . ALA   B 23  ? 0.1705 0.1875 0.3058 -0.0105 0.0025  -0.0234 29  ALA   C CB  
1263 N N   . ASN   B 24  ? 0.1914 0.2049 0.3059 -0.0126 0.0127  -0.0205 30  ASN   C N   
1264 C CA  . ASN   B 24  ? 0.1890 0.2031 0.3012 -0.0146 0.0189  -0.0215 30  ASN   C CA  
1265 C C   . ASN   B 24  ? 0.1932 0.2032 0.2903 -0.0162 0.0196  -0.0183 30  ASN   C C   
1266 O O   . ASN   B 24  ? 0.1868 0.1962 0.2787 -0.0161 0.0219  -0.0190 30  ASN   C O   
1267 C CB  . ASN   B 24  ? 0.2075 0.2240 0.3267 -0.0112 0.0181  -0.0246 30  ASN   C CB  
1268 C CG  . ASN   B 24  ? 0.2521 0.2729 0.3882 -0.0101 0.0172  -0.0276 30  ASN   C CG  
1269 O OD1 . ASN   B 24  ? 0.2682 0.2920 0.4134 -0.0126 0.0232  -0.0302 30  ASN   C OD1 
1270 N ND2 . ASN   B 24  ? 0.2311 0.2524 0.3718 -0.0070 0.0098  -0.0273 30  ASN   C ND2 
1271 N N   . LEU   B 25  ? 0.1978 0.2049 0.2893 -0.0177 0.0175  -0.0148 31  LEU   C N   
1272 C CA  . LEU   B 25  ? 0.2040 0.2074 0.2835 -0.0190 0.0165  -0.0110 31  LEU   C CA  
1273 C C   . LEU   B 25  ? 0.2191 0.2209 0.2901 -0.0241 0.0218  -0.0098 31  LEU   C C   
1274 O O   . LEU   B 25  ? 0.2466 0.2485 0.3186 -0.0286 0.0260  -0.0098 31  LEU   C O   
1275 C CB  . LEU   B 25  ? 0.2083 0.2092 0.2878 -0.0197 0.0129  -0.0076 31  LEU   C CB  
1276 C CG  . LEU   B 25  ? 0.2253 0.2222 0.2957 -0.0207 0.0105  -0.0032 31  LEU   C CG  
1277 C CD1 . LEU   B 25  ? 0.2250 0.2219 0.2923 -0.0166 0.0077  -0.0041 31  LEU   C CD1 
1278 C CD2 . LEU   B 25  ? 0.2272 0.2217 0.3014 -0.0215 0.0073  -0.0001 31  LEU   C CD2 
1279 N N   . VAL   B 26  ? 0.2002 0.2001 0.2619 -0.0241 0.0216  -0.0089 32  VAL   C N   
1280 C CA  . VAL   B 26  ? 0.2164 0.2138 0.2672 -0.0295 0.0256  -0.0075 32  VAL   C CA  
1281 C C   . VAL   B 26  ? 0.2266 0.2199 0.2680 -0.0315 0.0209  -0.0015 32  VAL   C C   
1282 O O   . VAL   B 26  ? 0.2504 0.2407 0.2847 -0.0373 0.0218  0.0021  32  VAL   C O   
1283 C CB  . VAL   B 26  ? 0.2266 0.2247 0.2743 -0.0285 0.0287  -0.0111 32  VAL   C CB  
1284 C CG1 . VAL   B 26  ? 0.2384 0.2331 0.2724 -0.0348 0.0322  -0.0097 32  VAL   C CG1 
1285 C CG2 . VAL   B 26  ? 0.2310 0.2330 0.2905 -0.0270 0.0333  -0.0168 32  VAL   C CG2 
1286 N N   . TRP   B 27  ? 0.1974 0.1903 0.2395 -0.0269 0.0157  -0.0005 33  TRP   C N   
1287 C CA  . TRP   B 27  ? 0.1950 0.1846 0.2316 -0.0280 0.0110  0.0048  33  TRP   C CA  
1288 C C   . TRP   B 27  ? 0.1882 0.1787 0.2306 -0.0222 0.0066  0.0042  33  TRP   C C   
1289 O O   . TRP   B 27  ? 0.1981 0.1908 0.2430 -0.0183 0.0071  0.0005  33  TRP   C O   
1290 C CB  . TRP   B 27  ? 0.2103 0.1977 0.2349 -0.0315 0.0120  0.0061  33  TRP   C CB  
1291 C CG  . TRP   B 27  ? 0.2273 0.2119 0.2473 -0.0319 0.0063  0.0112  33  TRP   C CG  
1292 C CD1 . TRP   B 27  ? 0.2583 0.2393 0.2739 -0.0365 0.0026  0.0173  33  TRP   C CD1 
1293 C CD2 . TRP   B 27  ? 0.2274 0.2126 0.2478 -0.0279 0.0035  0.0106  33  TRP   C CD2 
1294 N NE1 . TRP   B 27  ? 0.2588 0.2385 0.2740 -0.0351 -0.0027 0.0205  33  TRP   C NE1 
1295 C CE2 . TRP   B 27  ? 0.2406 0.2231 0.2585 -0.0300 -0.0017 0.0162  33  TRP   C CE2 
1296 C CE3 . TRP   B 27  ? 0.2247 0.2123 0.2479 -0.0231 0.0046  0.0063  33  TRP   C CE3 
1297 C CZ2 . TRP   B 27  ? 0.2368 0.2195 0.2552 -0.0274 -0.0050 0.0169  33  TRP   C CZ2 
1298 C CZ3 . TRP   B 27  ? 0.2241 0.2114 0.2462 -0.0209 0.0016  0.0072  33  TRP   C CZ3 
1299 C CH2 . TRP   B 27  ? 0.2204 0.2055 0.2407 -0.0229 -0.0028 0.0122  33  TRP   C CH2 
1300 N N   . GLU   B 28  ? 0.1842 0.1726 0.2293 -0.0219 0.0023  0.0078  34  GLU   C N   
1301 C CA  . GLU   B 28  ? 0.1875 0.1765 0.2377 -0.0172 -0.0009 0.0068  34  GLU   C CA  
1302 C C   . GLU   B 28  ? 0.1865 0.1728 0.2369 -0.0184 -0.0051 0.0117  34  GLU   C C   
1303 O O   . GLU   B 28  ? 0.1857 0.1694 0.2352 -0.0223 -0.0068 0.0164  34  GLU   C O   
1304 C CB  . GLU   B 28  ? 0.1949 0.1853 0.2543 -0.0141 -0.0013 0.0036  34  GLU   C CB  
1305 C CG  . GLU   B 28  ? 0.2110 0.2001 0.2761 -0.0164 -0.0018 0.0055  34  GLU   C CG  
1306 C CD  . GLU   B 28  ? 0.2516 0.2377 0.3213 -0.0170 -0.0056 0.0096  34  GLU   C CD  
1307 O OE1 . GLU   B 28  ? 0.2866 0.2703 0.3573 -0.0206 -0.0065 0.0135  34  GLU   C OE1 
1308 O OE2 . GLU   B 28  ? 0.2122 0.1981 0.2852 -0.0140 -0.0076 0.0089  34  GLU   C OE2 
1309 N N   . ASP   B 29  ? 0.1751 0.1619 0.2276 -0.0152 -0.0069 0.0109  35  ASP   C N   
1310 C CA  . ASP   B 29  ? 0.1690 0.1537 0.2251 -0.0157 -0.0112 0.0152  35  ASP   C CA  
1311 C C   . ASP   B 29  ? 0.1565 0.1427 0.2210 -0.0112 -0.0115 0.0117  35  ASP   C C   
1312 O O   . ASP   B 29  ? 0.1603 0.1480 0.2216 -0.0092 -0.0101 0.0089  35  ASP   C O   
1313 C CB  . ASP   B 29  ? 0.1985 0.1821 0.2455 -0.0189 -0.0126 0.0186  35  ASP   C CB  
1314 C CG  . ASP   B 29  ? 0.2609 0.2425 0.3121 -0.0201 -0.0181 0.0240  35  ASP   C CG  
1315 O OD1 . ASP   B 29  ? 0.3044 0.2865 0.3673 -0.0169 -0.0199 0.0234  35  ASP   C OD1 
1316 O OD2 . ASP   B 29  ? 0.2739 0.2535 0.3170 -0.0244 -0.0206 0.0283  35  ASP   C OD2 
1317 N N   . SER   B 30  ? 0.1657 0.1509 0.2408 -0.0100 -0.0129 0.0116  36  SER   C N   
1318 C CA  A SER   B 30  ? 0.1678 0.1539 0.2514 -0.0065 -0.0123 0.0076  36  SER   C CA  
1319 C CA  B SER   B 30  ? 0.1669 0.1531 0.2504 -0.0065 -0.0122 0.0075  36  SER   C CA  
1320 C C   . SER   B 30  ? 0.1719 0.1584 0.2578 -0.0058 -0.0138 0.0089  36  SER   C C   
1321 O O   . SER   B 30  ? 0.1842 0.1722 0.2713 -0.0035 -0.0114 0.0046  36  SER   C O   
1322 C CB  A SER   B 30  ? 0.1920 0.1764 0.2876 -0.0060 -0.0134 0.0073  36  SER   C CB  
1323 C CB  B SER   B 30  ? 0.1888 0.1733 0.2844 -0.0059 -0.0133 0.0071  36  SER   C CB  
1324 O OG  A SER   B 30  ? 0.2240 0.2088 0.3287 -0.0033 -0.0121 0.0030  36  SER   C OG  
1325 O OG  B SER   B 30  ? 0.2170 0.1991 0.3194 -0.0076 -0.0176 0.0131  36  SER   C OG  
1326 N N   . SER   B 31  ? 0.1625 0.1474 0.2488 -0.0083 -0.0179 0.0151  37  SER   C N   
1327 C CA  . SER   B 31  ? 0.1661 0.1516 0.2565 -0.0078 -0.0202 0.0168  37  SER   C CA  
1328 C C   . SER   B 31  ? 0.1741 0.1615 0.2535 -0.0076 -0.0177 0.0145  37  SER   C C   
1329 O O   . SER   B 31  ? 0.1921 0.1807 0.2755 -0.0065 -0.0181 0.0140  37  SER   C O   
1330 C CB  . SER   B 31  ? 0.2169 0.1999 0.3095 -0.0112 -0.0265 0.0245  37  SER   C CB  
1331 O OG  . SER   B 31  ? 0.2905 0.2724 0.3681 -0.0152 -0.0273 0.0279  37  SER   C OG  
1332 N N   . ARG   B 32  ? 0.1509 0.1386 0.2187 -0.0085 -0.0150 0.0130  38  ARG   C N   
1333 C CA  . ARG   B 32  ? 0.1384 0.1273 0.1968 -0.0082 -0.0128 0.0109  38  ARG   C CA  
1334 C C   . ARG   B 32  ? 0.1444 0.1346 0.2007 -0.0053 -0.0088 0.0050  38  ARG   C C   
1335 O O   . ARG   B 32  ? 0.1525 0.1434 0.2022 -0.0048 -0.0071 0.0032  38  ARG   C O   
1336 C CB  . ARG   B 32  ? 0.1505 0.1382 0.1972 -0.0117 -0.0126 0.0132  38  ARG   C CB  
1337 C CG  . ARG   B 32  ? 0.1679 0.1535 0.2125 -0.0158 -0.0171 0.0193  38  ARG   C CG  
1338 C CD  . ARG   B 32  ? 0.1802 0.1640 0.2115 -0.0205 -0.0160 0.0209  38  ARG   C CD  
1339 N NE  . ARG   B 32  ? 0.1672 0.1519 0.1910 -0.0200 -0.0131 0.0176  38  ARG   C NE  
1340 C CZ  . ARG   B 32  ? 0.1990 0.1821 0.2119 -0.0242 -0.0126 0.0186  38  ARG   C CZ  
1341 N NH1 . ARG   B 32  ? 0.2123 0.1925 0.2186 -0.0298 -0.0149 0.0230  38  ARG   C NH1 
1342 N NH2 . ARG   B 32  ? 0.2036 0.1873 0.2115 -0.0232 -0.0100 0.0153  38  ARG   C NH2 
1343 N N   . ASP   B 33  ? 0.1487 0.1390 0.2099 -0.0040 -0.0077 0.0024  39  ASP   C N   
1344 C CA  . ASP   B 33  ? 0.1343 0.1254 0.1925 -0.0022 -0.0051 -0.0024 39  ASP   C CA  
1345 C C   . ASP   B 33  ? 0.1416 0.1330 0.1915 -0.0029 -0.0042 -0.0025 39  ASP   C C   
1346 O O   . ASP   B 33  ? 0.1464 0.1382 0.1922 -0.0016 -0.0030 -0.0053 39  ASP   C O   
1347 C CB  . ASP   B 33  ? 0.1394 0.1309 0.1974 -0.0007 -0.0034 -0.0059 39  ASP   C CB  
1348 C CG  . ASP   B 33  ? 0.1592 0.1505 0.2127 0.0002  -0.0017 -0.0102 39  ASP   C CG  
1349 O OD1 . ASP   B 33  ? 0.1606 0.1517 0.2168 0.0002  -0.0019 -0.0119 39  ASP   C OD1 
1350 O OD2 . ASP   B 33  ? 0.1459 0.1370 0.1930 0.0004  -0.0007 -0.0116 39  ASP   C OD2 
1351 N N   . LEU   B 34  ? 0.1322 0.1233 0.1803 -0.0052 -0.0045 0.0003  40  LEU   C N   
1352 C CA  . LEU   B 34  ? 0.1395 0.1312 0.1820 -0.0060 -0.0026 -0.0008 40  LEU   C CA  
1353 C C   . LEU   B 34  ? 0.1468 0.1389 0.1924 -0.0071 -0.0016 -0.0011 40  LEU   C C   
1354 O O   . LEU   B 34  ? 0.1566 0.1478 0.2055 -0.0088 -0.0027 0.0014  40  LEU   C O   
1355 C CB  . LEU   B 34  ? 0.1505 0.1412 0.1860 -0.0088 -0.0021 0.0017  40  LEU   C CB  
1356 C CG  . LEU   B 34  ? 0.1727 0.1631 0.2040 -0.0081 -0.0025 0.0018  40  LEU   C CG  
1357 C CD1 . LEU   B 34  ? 0.1861 0.1751 0.2099 -0.0118 -0.0022 0.0040  40  LEU   C CD1 
1358 C CD2 . LEU   B 34  ? 0.1743 0.1654 0.2043 -0.0054 -0.0011 -0.0019 40  LEU   C CD2 
1359 N N   . LEU   B 35  ? 0.1391 0.1326 0.1845 -0.0063 0.0001  -0.0039 41  LEU   C N   
1360 C CA  . LEU   B 35  ? 0.1455 0.1399 0.1947 -0.0076 0.0017  -0.0046 41  LEU   C CA  
1361 C C   . LEU   B 35  ? 0.1472 0.1429 0.1947 -0.0080 0.0046  -0.0068 41  LEU   C C   
1362 O O   . LEU   B 35  ? 0.1557 0.1517 0.2020 -0.0058 0.0042  -0.0085 41  LEU   C O   
1363 C CB  . LEU   B 35  ? 0.1498 0.1452 0.2060 -0.0056 0.0001  -0.0070 41  LEU   C CB  
1364 C CG  . LEU   B 35  ? 0.1547 0.1516 0.2167 -0.0071 0.0015  -0.0078 41  LEU   C CG  
1365 C CD1 . LEU   B 35  ? 0.1633 0.1598 0.2317 -0.0065 -0.0005 -0.0085 41  LEU   C CD1 
1366 C CD2 . LEU   B 35  ? 0.1597 0.1590 0.2249 -0.0057 0.0024  -0.0110 41  LEU   C CD2 
1367 N N   . VAL   B 36  ? 0.1412 0.1373 0.1888 -0.0112 0.0078  -0.0066 42  VAL   C N   
1368 C CA  . VAL   B 36  ? 0.1538 0.1511 0.2019 -0.0120 0.0118  -0.0095 42  VAL   C CA  
1369 C C   . VAL   B 36  ? 0.1640 0.1637 0.2209 -0.0127 0.0140  -0.0116 42  VAL   C C   
1370 O O   . VAL   B 36  ? 0.1725 0.1718 0.2299 -0.0155 0.0147  -0.0098 42  VAL   C O   
1371 C CB  . VAL   B 36  ? 0.1760 0.1715 0.2151 -0.0165 0.0153  -0.0084 42  VAL   C CB  
1372 C CG1 . VAL   B 36  ? 0.1939 0.1906 0.2352 -0.0177 0.0209  -0.0126 42  VAL   C CG1 
1373 C CG2 . VAL   B 36  ? 0.1762 0.1695 0.2076 -0.0160 0.0126  -0.0062 42  VAL   C CG2 
1374 N N   . SER   B 37  ? 0.1657 0.1678 0.2305 -0.0100 0.0143  -0.0150 43  SER   C N   
1375 C CA  . SER   B 37  ? 0.1660 0.1710 0.2416 -0.0104 0.0163  -0.0174 43  SER   C CA  
1376 C C   . SER   B 37  ? 0.1798 0.1866 0.2605 -0.0113 0.0216  -0.0211 43  SER   C C   
1377 O O   . SER   B 37  ? 0.1836 0.1891 0.2601 -0.0106 0.0227  -0.0220 43  SER   C O   
1378 C CB  . SER   B 37  ? 0.1725 0.1791 0.2560 -0.0067 0.0110  -0.0183 43  SER   C CB  
1379 O OG  . SER   B 37  ? 0.1905 0.1968 0.2746 -0.0034 0.0079  -0.0192 43  SER   C OG  
1380 N N   . SER   B 38  ? 0.1863 0.1960 0.2767 -0.0131 0.0256  -0.0236 44  SER   C N   
1381 C CA  . SER   B 38  ? 0.2160 0.2276 0.3139 -0.0141 0.0318  -0.0282 44  SER   C CA  
1382 C C   . SER   B 38  ? 0.2309 0.2454 0.3442 -0.0093 0.0284  -0.0307 44  SER   C C   
1383 O O   . SER   B 38  ? 0.2360 0.2519 0.3556 -0.0067 0.0225  -0.0295 44  SER   C O   
1384 C CB  . SER   B 38  ? 0.2379 0.2512 0.3394 -0.0192 0.0388  -0.0300 44  SER   C CB  
1385 O OG  . SER   B 38  ? 0.2817 0.2977 0.3936 -0.0180 0.0357  -0.0296 44  SER   C OG  
1386 N N   . THR   B 39  ? 0.2374 0.2524 0.3567 -0.0084 0.0319  -0.0342 45  THR   C N   
1387 C CA  . THR   B 39  ? 0.2703 0.2874 0.4054 -0.0039 0.0280  -0.0362 45  THR   C CA  
1388 C C   . THR   B 39  ? 0.3066 0.3273 0.4582 -0.0052 0.0357  -0.0419 45  THR   C C   
1389 O O   . THR   B 39  ? 0.3148 0.3351 0.4615 -0.0097 0.0446  -0.0447 45  THR   C O   
1390 C CB  . THR   B 39  ? 0.3008 0.3148 0.4307 -0.0010 0.0245  -0.0351 45  THR   C CB  
1391 O OG1 . THR   B 39  ? 0.3284 0.3409 0.4542 -0.0034 0.0321  -0.0382 45  THR   C OG1 
1392 C CG2 . THR   B 39  ? 0.3127 0.3231 0.4264 -0.0002 0.0186  -0.0303 45  THR   C CG2 
1393 N N   . THR   B 40  ? 0.3275 0.3514 0.4986 -0.0017 0.0323  -0.0437 46  THR   C N   
1394 C CA  . THR   B 40  ? 0.3511 0.3786 0.5416 -0.0023 0.0395  -0.0497 46  THR   C CA  
1395 C C   . THR   B 40  ? 0.3635 0.3890 0.5585 0.0000  0.0410  -0.0523 46  THR   C C   
1396 O O   . THR   B 40  ? 0.3844 0.4113 0.5890 -0.0019 0.0503  -0.0582 46  THR   C O   
1397 C CB  . THR   B 40  ? 0.3822 0.4147 0.5946 0.0001  0.0349  -0.0504 46  THR   C CB  
1398 O OG1 . THR   B 40  ? 0.4144 0.4454 0.6285 0.0047  0.0229  -0.0460 46  THR   C OG1 
1399 C CG2 . THR   B 40  ? 0.3897 0.4244 0.5997 -0.0030 0.0359  -0.0493 46  THR   C CG2 
1400 N N   . ALA   B 41  ? 0.3552 0.3772 0.5436 0.0037  0.0324  -0.0481 47  ALA   C N   
1401 C CA  . ALA   B 41  ? 0.3548 0.3740 0.5469 0.0059  0.0326  -0.0497 47  ALA   C CA  
1402 C C   . ALA   B 41  ? 0.3556 0.3704 0.5270 0.0031  0.0374  -0.0497 47  ALA   C C   
1403 O O   . ALA   B 41  ? 0.3552 0.3681 0.5078 0.0011  0.0358  -0.0458 47  ALA   C O   
1404 C CB  . ALA   B 41  ? 0.3622 0.3794 0.5580 0.0106  0.0206  -0.0448 47  ALA   C CB  
1405 N N   . GLN   B 42  ? 0.3463 0.3593 0.5223 0.0029  0.0430  -0.0540 48  GLN   C N   
1406 C CA  . GLN   B 42  ? 0.3545 0.3632 0.5119 -0.0002 0.0476  -0.0546 48  GLN   C CA  
1407 C C   . GLN   B 42  ? 0.3423 0.3468 0.4881 0.0027  0.0388  -0.0490 48  GLN   C C   
1408 O O   . GLN   B 42  ? 0.3474 0.3509 0.5038 0.0070  0.0324  -0.0475 48  GLN   C O   
1409 C CB  . GLN   B 42  ? 0.3892 0.3974 0.5570 -0.0017 0.0571  -0.0622 48  GLN   C CB  
1410 C CG  . GLN   B 42  ? 0.4631 0.4664 0.6121 -0.0054 0.0619  -0.0635 48  GLN   C CG  
1411 C CD  . GLN   B 42  ? 0.5527 0.5556 0.6843 -0.0127 0.0697  -0.0649 48  GLN   C CD  
1412 O OE1 . GLN   B 42  ? 0.5729 0.5790 0.7067 -0.0152 0.0728  -0.0655 48  GLN   C OE1 
1413 N NE2 . GLN   B 42  ? 0.5802 0.5787 0.6939 -0.0165 0.0725  -0.0652 48  GLN   C NE2 
1414 N N   . GLY   B 43  ? 0.3128 0.3147 0.4373 0.0000  0.0383  -0.0456 49  GLY   C N   
1415 C CA  . GLY   B 43  ? 0.2991 0.2974 0.4113 0.0018  0.0315  -0.0408 49  GLY   C CA  
1416 C C   . GLY   B 43  ? 0.2872 0.2817 0.3933 0.0003  0.0358  -0.0433 49  GLY   C C   
1417 O O   . GLY   B 43  ? 0.2991 0.2933 0.4003 -0.0041 0.0441  -0.0475 49  GLY   C O   
1418 N N   . CYS   B 44  ? 0.2674 0.2587 0.3726 0.0032  0.0303  -0.0408 50  CYS   C N   
1419 C CA  . CYS   B 44  ? 0.2566 0.2441 0.3580 0.0021  0.0337  -0.0433 50  CYS   C CA  
1420 C C   . CYS   B 44  ? 0.2469 0.2310 0.3302 0.0011  0.0302  -0.0390 50  CYS   C C   
1421 O O   . CYS   B 44  ? 0.2612 0.2417 0.3426 0.0009  0.0312  -0.0403 50  CYS   C O   
1422 C CB  . CYS   B 44  ? 0.2791 0.2652 0.3985 0.0061  0.0319  -0.0453 50  CYS   C CB  
1423 S SG  . CYS   B 44  ? 0.3518 0.3423 0.4965 0.0071  0.0376  -0.0518 50  CYS   C SG  
1424 N N   . ASP   B 45  ? 0.2154 0.2004 0.2868 0.0003  0.0263  -0.0343 51  ASP   C N   
1425 C CA  . ASP   B 45  ? 0.2227 0.2049 0.2792 -0.0009 0.0236  -0.0308 51  ASP   C CA  
1426 C C   . ASP   B 45  ? 0.2494 0.2306 0.2952 -0.0061 0.0298  -0.0333 51  ASP   C C   
1427 O O   . ASP   B 45  ? 0.2692 0.2521 0.3147 -0.0093 0.0349  -0.0358 51  ASP   C O   
1428 C CB  . ASP   B 45  ? 0.2273 0.2111 0.2767 -0.0002 0.0182  -0.0257 51  ASP   C CB  
1429 C CG  . ASP   B 45  ? 0.2957 0.2795 0.3512 0.0037  0.0115  -0.0229 51  ASP   C CG  
1430 O OD1 . ASP   B 45  ? 0.3099 0.2912 0.3710 0.0059  0.0091  -0.0229 51  ASP   C OD1 
1431 O OD2 . ASP   B 45  ? 0.2720 0.2576 0.3259 0.0043  0.0082  -0.0205 51  ASP   C OD2 
1432 N N   . THR   B 46  ? 0.2481 0.2261 0.2845 -0.0076 0.0293  -0.0324 52  THR   C N   
1433 C CA  . THR   B 46  ? 0.2520 0.2282 0.2762 -0.0132 0.0336  -0.0340 52  THR   C CA  
1434 C C   . THR   B 46  ? 0.2331 0.2097 0.2457 -0.0145 0.0287  -0.0284 52  THR   C C   
1435 O O   . THR   B 46  ? 0.2446 0.2207 0.2568 -0.0117 0.0237  -0.0250 52  THR   C O   
1436 C CB  . THR   B 46  ? 0.3021 0.2744 0.3247 -0.0141 0.0356  -0.0369 52  THR   C CB  
1437 O OG1 . THR   B 46  ? 0.3367 0.3085 0.3719 -0.0132 0.0409  -0.0429 52  THR   C OG1 
1438 C CG2 . THR   B 46  ? 0.3165 0.2864 0.3240 -0.0205 0.0382  -0.0376 52  THR   C CG2 
1439 N N   . ILE   B 47  ? 0.2240 0.2012 0.2281 -0.0191 0.0302  -0.0273 53  ILE   C N   
1440 C CA  . ILE   B 47  ? 0.2177 0.1951 0.2132 -0.0204 0.0252  -0.0219 53  ILE   C CA  
1441 C C   . ILE   B 47  ? 0.2222 0.1966 0.2072 -0.0245 0.0251  -0.0216 53  ILE   C C   
1442 O O   . ILE   B 47  ? 0.2271 0.1992 0.2059 -0.0294 0.0298  -0.0252 53  ILE   C O   
1443 C CB  . ILE   B 47  ? 0.2272 0.2062 0.2193 -0.0236 0.0256  -0.0199 53  ILE   C CB  
1444 C CG1 . ILE   B 47  ? 0.2531 0.2352 0.2559 -0.0204 0.0266  -0.0210 53  ILE   C CG1 
1445 C CG2 . ILE   B 47  ? 0.2305 0.2097 0.2171 -0.0242 0.0197  -0.0140 53  ILE   C CG2 
1446 C CD1 . ILE   B 47  ? 0.2771 0.2610 0.2875 -0.0143 0.0211  -0.0185 53  ILE   C CD1 
1447 N N   . ALA   B 48  ? 0.2093 0.1835 0.1921 -0.0230 0.0199  -0.0178 54  ALA   C N   
1448 C CA  . ALA   B 48  ? 0.2013 0.1730 0.1751 -0.0269 0.0187  -0.0169 54  ALA   C CA  
1449 C C   . ALA   B 48  ? 0.1941 0.1653 0.1583 -0.0329 0.0174  -0.0142 54  ALA   C C   
1450 O O   . ALA   B 48  ? 0.1971 0.1703 0.1629 -0.0324 0.0149  -0.0107 54  ALA   C O   
1451 C CB  . ALA   B 48  ? 0.1887 0.1612 0.1648 -0.0238 0.0136  -0.0133 54  ALA   C CB  
1452 N N   . ARG   B 49  ? 0.2017 0.1697 0.1555 -0.0389 0.0187  -0.0155 55  ARG   C N   
1453 C CA  . ARG   B 49  ? 0.2033 0.1698 0.1457 -0.0458 0.0164  -0.0121 55  ARG   C CA  
1454 C C   . ARG   B 49  ? 0.2076 0.1722 0.1441 -0.0485 0.0120  -0.0101 55  ARG   C C   
1455 O O   . ARG   B 49  ? 0.2187 0.1799 0.1475 -0.0527 0.0148  -0.0138 55  ARG   C O   
1456 C CB  . ARG   B 49  ? 0.2155 0.1793 0.1491 -0.0522 0.0231  -0.0166 55  ARG   C CB  
1457 C CG  . ARG   B 49  ? 0.2223 0.1885 0.1641 -0.0495 0.0282  -0.0194 55  ARG   C CG  
1458 C CD  . ARG   B 49  ? 0.2414 0.2103 0.1867 -0.0479 0.0240  -0.0138 55  ARG   C CD  
1459 N NE  . ARG   B 49  ? 0.2474 0.2186 0.2010 -0.0455 0.0289  -0.0169 55  ARG   C NE  
1460 C CZ  . ARG   B 49  ? 0.2677 0.2417 0.2286 -0.0422 0.0265  -0.0139 55  ARG   C CZ  
1461 N NH1 . ARG   B 49  ? 0.2421 0.2169 0.2037 -0.0407 0.0195  -0.0079 55  ARG   C NH1 
1462 N NH2 . ARG   B 49  ? 0.2814 0.2575 0.2502 -0.0406 0.0311  -0.0171 55  ARG   C NH2 
1463 N N   . CYS   B 50  ? 0.2099 0.1766 0.1514 -0.0457 0.0055  -0.0048 56  CYS   C N   
1464 C CA  . CYS   B 50  ? 0.2199 0.1859 0.1601 -0.0467 0.0012  -0.0030 56  CYS   C CA  
1465 C C   . CYS   B 50  ? 0.2221 0.1911 0.1692 -0.0447 -0.0059 0.0032  56  CYS   C C   
1466 O O   . CYS   B 50  ? 0.2138 0.1852 0.1672 -0.0419 -0.0071 0.0055  56  CYS   C O   
1467 C CB  . CYS   B 50  ? 0.2305 0.1966 0.1770 -0.0419 0.0043  -0.0070 56  CYS   C CB  
1468 S SG  . CYS   B 50  ? 0.2027 0.1728 0.1631 -0.0333 0.0035  -0.0056 56  CYS   C SG  
1469 N N   . ASP   B 51  ? 0.2189 0.1879 0.1668 -0.0458 -0.0101 0.0050  57  ASP   C N   
1470 C CA  . ASP   B 51  ? 0.2262 0.1984 0.1838 -0.0434 -0.0159 0.0097  57  ASP   C CA  
1471 C C   . ASP   B 51  ? 0.2256 0.1997 0.1916 -0.0387 -0.0147 0.0080  57  ASP   C C   
1472 O O   . ASP   B 51  ? 0.2234 0.1996 0.1961 -0.0384 -0.0188 0.0107  57  ASP   C O   
1473 C CB  . ASP   B 51  ? 0.2605 0.2317 0.2141 -0.0493 -0.0232 0.0149  57  ASP   C CB  
1474 C CG  . ASP   B 51  ? 0.3323 0.3010 0.2786 -0.0540 -0.0247 0.0138  57  ASP   C CG  
1475 O OD1 . ASP   B 51  ? 0.3375 0.3046 0.2806 -0.0530 -0.0192 0.0086  57  ASP   C OD1 
1476 O OD2 . ASP   B 51  ? 0.3952 0.3633 0.3396 -0.0587 -0.0318 0.0184  57  ASP   C OD2 
1477 N N   . CYS   B 52  ? 0.2028 0.1762 0.1693 -0.0351 -0.0091 0.0035  58  CYS   C N   
1478 C CA  . CYS   B 52  ? 0.1847 0.1590 0.1576 -0.0311 -0.0078 0.0022  58  CYS   C CA  
1479 C C   . CYS   B 52  ? 0.1692 0.1474 0.1524 -0.0277 -0.0099 0.0048  58  CYS   C C   
1480 O O   . CYS   B 52  ? 0.1604 0.1405 0.1473 -0.0260 -0.0104 0.0062  58  CYS   C O   
1481 C CB  . CYS   B 52  ? 0.1856 0.1583 0.1584 -0.0277 -0.0027 -0.0018 58  CYS   C CB  
1482 S SG  . CYS   B 52  ? 0.2112 0.1791 0.1761 -0.0310 0.0009  -0.0062 58  CYS   C SG  
1483 N N   . GLN   B 53  ? 0.1657 0.1450 0.1538 -0.0268 -0.0103 0.0050  59  GLN   C N   
1484 C CA  . GLN   B 53  ? 0.1644 0.1472 0.1627 -0.0238 -0.0104 0.0060  59  GLN   C CA  
1485 C C   . GLN   B 53  ? 0.1680 0.1499 0.1667 -0.0214 -0.0066 0.0035  59  GLN   C C   
1486 O O   . GLN   B 53  ? 0.1685 0.1527 0.1742 -0.0201 -0.0058 0.0037  59  GLN   C O   
1487 C CB  . GLN   B 53  ? 0.1747 0.1602 0.1807 -0.0259 -0.0150 0.0091  59  GLN   C CB  
1488 C CG  . GLN   B 53  ? 0.1983 0.1850 0.2071 -0.0273 -0.0196 0.0126  59  GLN   C CG  
1489 C CD  . GLN   B 53  ? 0.2048 0.1942 0.2238 -0.0291 -0.0249 0.0160  59  GLN   C CD  
1490 O OE1 . GLN   B 53  ? 0.2309 0.2190 0.2461 -0.0336 -0.0302 0.0189  59  GLN   C OE1 
1491 N NE2 . GLN   B 53  ? 0.1885 0.1817 0.2212 -0.0259 -0.0234 0.0153  59  GLN   C NE2 
1492 N N   . THR   B 54  ? 0.1695 0.1478 0.1614 -0.0210 -0.0041 0.0013  60  THR   C N   
1493 C CA  . THR   B 54  ? 0.1857 0.1621 0.1774 -0.0190 -0.0013 -0.0002 60  THR   C CA  
1494 C C   . THR   B 54  ? 0.1799 0.1539 0.1682 -0.0168 0.0004  -0.0019 60  THR   C C   
1495 O O   . THR   B 54  ? 0.1789 0.1515 0.1639 -0.0178 0.0007  -0.0031 60  THR   C O   
1496 C CB  . THR   B 54  ? 0.2431 0.2169 0.2326 -0.0211 -0.0010 -0.0006 60  THR   C CB  
1497 O OG1 . THR   B 54  ? 0.2763 0.2467 0.2600 -0.0227 -0.0007 -0.0023 60  THR   C OG1 
1498 C CG2 . THR   B 54  ? 0.2640 0.2404 0.2579 -0.0237 -0.0031 0.0010  60  THR   C CG2 
1499 N N   . GLY   B 55  ? 0.1653 0.1387 0.1546 -0.0143 0.0016  -0.0021 61  GLY   C N   
1500 C CA  . GLY   B 55  ? 0.1725 0.1439 0.1606 -0.0120 0.0022  -0.0033 61  GLY   C CA  
1501 C C   . GLY   B 55  ? 0.1585 0.1286 0.1464 -0.0104 0.0023  -0.0028 61  GLY   C C   
1502 O O   . GLY   B 55  ? 0.1766 0.1464 0.1637 -0.0114 0.0028  -0.0019 61  GLY   C O   
1503 N N   . VAL   B 56  ? 0.1587 0.1277 0.1471 -0.0083 0.0018  -0.0033 62  VAL   C N   
1504 C CA  . VAL   B 56  ? 0.1504 0.1172 0.1370 -0.0074 0.0008  -0.0023 62  VAL   C CA  
1505 C C   . VAL   B 56  ? 0.1594 0.1284 0.1480 -0.0056 0.0001  -0.0028 62  VAL   C C   
1506 O O   . VAL   B 56  ? 0.1560 0.1260 0.1479 -0.0043 -0.0002 -0.0038 62  VAL   C O   
1507 C CB  . VAL   B 56  ? 0.1715 0.1334 0.1578 -0.0067 -0.0006 -0.0019 62  VAL   C CB  
1508 C CG1 . VAL   B 56  ? 0.2027 0.1616 0.1864 -0.0064 -0.0031 0.0000  62  VAL   C CG1 
1509 C CG2 . VAL   B 56  ? 0.1790 0.1383 0.1636 -0.0086 0.0002  -0.0016 62  VAL   C CG2 
1510 N N   . TYR   B 57  ? 0.1600 0.1294 0.1463 -0.0061 0.0000  -0.0024 63  TYR   C N   
1511 C CA  . TYR   B 57  ? 0.1484 0.1193 0.1362 -0.0047 -0.0010 -0.0031 63  TYR   C CA  
1512 C C   . TYR   B 57  ? 0.1681 0.1356 0.1515 -0.0051 -0.0034 -0.0022 63  TYR   C C   
1513 O O   . TYR   B 57  ? 0.1621 0.1263 0.1397 -0.0071 -0.0035 -0.0009 63  TYR   C O   
1514 C CB  . TYR   B 57  ? 0.1496 0.1244 0.1399 -0.0051 0.0009  -0.0043 63  TYR   C CB  
1515 C CG  . TYR   B 57  ? 0.1532 0.1276 0.1402 -0.0070 0.0028  -0.0050 63  TYR   C CG  
1516 C CD1 . TYR   B 57  ? 0.1775 0.1520 0.1640 -0.0089 0.0050  -0.0049 63  TYR   C CD1 
1517 C CD2 . TYR   B 57  ? 0.1627 0.1369 0.1476 -0.0075 0.0029  -0.0064 63  TYR   C CD2 
1518 C CE1 . TYR   B 57  ? 0.1928 0.1671 0.1769 -0.0112 0.0081  -0.0063 63  TYR   C CE1 
1519 C CE2 . TYR   B 57  ? 0.1792 0.1528 0.1605 -0.0100 0.0059  -0.0080 63  TYR   C CE2 
1520 C CZ  . TYR   B 57  ? 0.1952 0.1690 0.1764 -0.0119 0.0089  -0.0080 63  TYR   C CZ  
1521 O OH  . TYR   B 57  ? 0.2230 0.1965 0.2014 -0.0149 0.0130  -0.0103 63  TYR   C OH  
1522 N N   . TYR   B 58  ? 0.1698 0.1377 0.1555 -0.0036 -0.0057 -0.0025 64  TYR   C N   
1523 C CA  . TYR   B 58  ? 0.1706 0.1352 0.1518 -0.0045 -0.0093 -0.0012 64  TYR   C CA  
1524 C C   . TYR   B 58  ? 0.1688 0.1345 0.1455 -0.0063 -0.0079 -0.0027 64  TYR   C C   
1525 O O   . TYR   B 58  ? 0.1736 0.1430 0.1550 -0.0052 -0.0064 -0.0047 64  TYR   C O   
1526 C CB  . TYR   B 58  ? 0.1790 0.1433 0.1664 -0.0022 -0.0131 -0.0007 64  TYR   C CB  
1527 C CG  . TYR   B 58  ? 0.1986 0.1590 0.1811 -0.0036 -0.0182 0.0014  64  TYR   C CG  
1528 C CD1 . TYR   B 58  ? 0.2171 0.1721 0.1934 -0.0056 -0.0211 0.0045  64  TYR   C CD1 
1529 C CD2 . TYR   B 58  ? 0.2256 0.1873 0.2085 -0.0037 -0.0205 0.0006  64  TYR   C CD2 
1530 C CE1 . TYR   B 58  ? 0.2474 0.1980 0.2174 -0.0078 -0.0268 0.0073  64  TYR   C CE1 
1531 C CE2 . TYR   B 58  ? 0.2521 0.2098 0.2290 -0.0059 -0.0260 0.0029  64  TYR   C CE2 
1532 C CZ  . TYR   B 58  ? 0.2768 0.2288 0.2469 -0.0081 -0.0294 0.0064  64  TYR   C CZ  
1533 O OH  . TYR   B 58  ? 0.3226 0.2698 0.2850 -0.0112 -0.0358 0.0094  64  TYR   C OH  
1534 N N   . CYS   B 59  ? 0.1803 0.1422 0.1475 -0.0097 -0.0082 -0.0018 65  CYS   C N   
1535 C CA  . CYS   B 59  ? 0.1960 0.1580 0.1573 -0.0125 -0.0060 -0.0041 65  CYS   C CA  
1536 C C   . CYS   B 59  ? 0.2201 0.1776 0.1734 -0.0147 -0.0111 -0.0025 65  CYS   C C   
1537 O O   . CYS   B 59  ? 0.2442 0.1965 0.1884 -0.0179 -0.0136 0.0003  65  CYS   C O   
1538 C CB  . CYS   B 59  ? 0.2085 0.1696 0.1644 -0.0157 -0.0013 -0.0049 65  CYS   C CB  
1539 S SG  . CYS   B 59  ? 0.2439 0.2043 0.1920 -0.0203 0.0033  -0.0089 65  CYS   C SG  
1540 N N   . SER   B 60  ? 0.2089 0.1682 0.1657 -0.0135 -0.0133 -0.0039 66  SER   C N   
1541 C CA  . SER   B 60  ? 0.2465 0.2019 0.1967 -0.0158 -0.0193 -0.0021 66  SER   C CA  
1542 C C   . SER   B 60  ? 0.2694 0.2204 0.2047 -0.0218 -0.0182 -0.0028 66  SER   C C   
1543 O O   . SER   B 60  ? 0.2949 0.2403 0.2207 -0.0251 -0.0239 0.0005  66  SER   C O   
1544 C CB  . SER   B 60  ? 0.2896 0.2480 0.2472 -0.0136 -0.0218 -0.0037 66  SER   C CB  
1545 O OG  . SER   B 60  ? 0.3477 0.3093 0.3064 -0.0140 -0.0168 -0.0080 66  SER   C OG  
1546 N N   . SER   B 61  ? 0.2561 0.2091 0.1894 -0.0235 -0.0109 -0.0071 67  SER   C N   
1547 C CA  . SER   B 61  ? 0.2569 0.2057 0.1756 -0.0301 -0.0082 -0.0091 67  SER   C CA  
1548 C C   . SER   B 61  ? 0.2818 0.2258 0.1899 -0.0340 -0.0077 -0.0060 67  SER   C C   
1549 O O   . SER   B 61  ? 0.3117 0.2511 0.2053 -0.0406 -0.0055 -0.0072 67  SER   C O   
1550 C CB  . SER   B 61  ? 0.2560 0.2086 0.1783 -0.0308 0.0001  -0.0153 67  SER   C CB  
1551 O OG  . SER   B 61  ? 0.2496 0.2060 0.1807 -0.0284 0.0054  -0.0162 67  SER   C OG  
1552 N N   . ARG   B 62  ? 0.2583 0.2025 0.1727 -0.0308 -0.0095 -0.0024 68  ARG   C N   
1553 C CA  . ARG   B 62  ? 0.2499 0.1890 0.1556 -0.0341 -0.0101 0.0013  68  ARG   C CA  
1554 C C   . ARG   B 62  ? 0.2604 0.1958 0.1685 -0.0319 -0.0188 0.0073  68  ARG   C C   
1555 O O   . ARG   B 62  ? 0.2792 0.2098 0.1818 -0.0342 -0.0205 0.0112  68  ARG   C O   
1556 C CB  . ARG   B 62  ? 0.2652 0.2079 0.1775 -0.0328 -0.0032 -0.0004 68  ARG   C CB  
1557 C CG  . ARG   B 62  ? 0.3001 0.2459 0.2116 -0.0355 0.0056  -0.0062 68  ARG   C CG  
1558 C CD  . ARG   B 62  ? 0.3268 0.2669 0.2217 -0.0434 0.0088  -0.0067 68  ARG   C CD  
1559 N NE  . ARG   B 62  ? 0.3609 0.3042 0.2567 -0.0462 0.0183  -0.0132 68  ARG   C NE  
1560 C CZ  . ARG   B 62  ? 0.4424 0.3862 0.3352 -0.0484 0.0212  -0.0181 68  ARG   C CZ  
1561 N NH1 . ARG   B 62  ? 0.4476 0.3891 0.3355 -0.0483 0.0148  -0.0169 68  ARG   C NH1 
1562 N NH2 . ARG   B 62  ? 0.4596 0.4062 0.3556 -0.0509 0.0305  -0.0246 68  ARG   C NH2 
1563 N N   . ARG   B 63  ? 0.2608 0.1988 0.1795 -0.0272 -0.0238 0.0079  69  ARG   C N   
1564 C CA  . ARG   B 63  ? 0.2808 0.2166 0.2072 -0.0240 -0.0311 0.0124  69  ARG   C CA  
1565 C C   . ARG   B 63  ? 0.2905 0.2259 0.2218 -0.0221 -0.0287 0.0138  69  ARG   C C   
1566 O O   . ARG   B 63  ? 0.3046 0.2345 0.2344 -0.0230 -0.0336 0.0184  69  ARG   C O   
1567 C CB  . ARG   B 63  ? 0.3219 0.2503 0.2385 -0.0281 -0.0400 0.0177  69  ARG   C CB  
1568 C CG  . ARG   B 63  ? 0.3751 0.3036 0.2876 -0.0300 -0.0437 0.0165  69  ARG   C CG  
1569 C CD  . ARG   B 63  ? 0.4480 0.3812 0.3768 -0.0242 -0.0474 0.0159  69  ARG   C CD  
1570 N NE  . ARG   B 63  ? 0.4915 0.4231 0.4168 -0.0265 -0.0541 0.0168  69  ARG   C NE  
1571 C CZ  . ARG   B 63  ? 0.5341 0.4689 0.4570 -0.0276 -0.0513 0.0123  69  ARG   C CZ  
1572 N NH1 . ARG   B 63  ? 0.4995 0.4390 0.4237 -0.0265 -0.0419 0.0069  69  ARG   C NH1 
1573 N NH2 . ARG   B 63  ? 0.5554 0.4884 0.4753 -0.0300 -0.0582 0.0133  69  ARG   C NH2 
1574 N N   . LYS   B 64  ? 0.2696 0.2104 0.2064 -0.0201 -0.0214 0.0100  70  LYS   C N   
1575 C CA  . LYS   B 64  ? 0.2700 0.2104 0.2101 -0.0192 -0.0187 0.0107  70  LYS   C CA  
1576 C C   . LYS   B 64  ? 0.2373 0.1843 0.1890 -0.0150 -0.0144 0.0073  70  LYS   C C   
1577 O O   . LYS   B 64  ? 0.2217 0.1734 0.1765 -0.0139 -0.0116 0.0041  70  LYS   C O   
1578 C CB  . LYS   B 64  ? 0.3250 0.2638 0.2549 -0.0241 -0.0134 0.0101  70  LYS   C CB  
1579 C CG  . LYS   B 64  ? 0.4703 0.4013 0.3878 -0.0292 -0.0165 0.0145  70  LYS   C CG  
1580 C CD  . LYS   B 64  ? 0.5493 0.4801 0.4606 -0.0333 -0.0096 0.0130  70  LYS   C CD  
1581 C CE  . LYS   B 64  ? 0.6379 0.5607 0.5381 -0.0383 -0.0122 0.0179  70  LYS   C CE  
1582 N NZ  . LYS   B 64  ? 0.6821 0.5986 0.5680 -0.0435 -0.0170 0.0209  70  LYS   C NZ  
1583 N N   . HIS   B 65  ? 0.2160 0.1625 0.1730 -0.0133 -0.0139 0.0080  71  HIS   C N   
1584 C CA  . HIS   B 65  ? 0.1968 0.1483 0.1620 -0.0107 -0.0099 0.0053  71  HIS   C CA  
1585 C C   . HIS   B 65  ? 0.2219 0.1740 0.1836 -0.0133 -0.0054 0.0047  71  HIS   C C   
1586 O O   . HIS   B 65  ? 0.2478 0.1954 0.2038 -0.0160 -0.0058 0.0069  71  HIS   C O   
1587 C CB  . HIS   B 65  ? 0.1971 0.1475 0.1702 -0.0079 -0.0117 0.0057  71  HIS   C CB  
1588 C CG  . HIS   B 65  ? 0.2214 0.1720 0.2012 -0.0052 -0.0154 0.0057  71  HIS   C CG  
1589 N ND1 . HIS   B 65  ? 0.2429 0.1983 0.2304 -0.0026 -0.0135 0.0028  71  HIS   C ND1 
1590 C CD2 . HIS   B 65  ? 0.2217 0.1682 0.2024 -0.0049 -0.0211 0.0085  71  HIS   C CD2 
1591 C CE1 . HIS   B 65  ? 0.2235 0.1780 0.2171 -0.0007 -0.0174 0.0034  71  HIS   C CE1 
1592 N NE2 . HIS   B 65  ? 0.2471 0.1964 0.2374 -0.0019 -0.0224 0.0069  71  HIS   C NE2 
1593 N N   . TYR   B 66  ? 0.1879 0.1454 0.1542 -0.0126 -0.0015 0.0020  72  TYR   C N   
1594 C CA  . TYR   B 66  ? 0.1865 0.1455 0.1525 -0.0148 0.0024  0.0012  72  TYR   C CA  
1595 C C   . TYR   B 66  ? 0.1807 0.1431 0.1541 -0.0132 0.0033  0.0003  72  TYR   C C   
1596 O O   . TYR   B 66  ? 0.1731 0.1389 0.1515 -0.0110 0.0029  -0.0009 72  TYR   C O   
1597 C CB  . TYR   B 66  ? 0.1935 0.1558 0.1592 -0.0163 0.0062  -0.0012 72  TYR   C CB  
1598 C CG  . TYR   B 66  ? 0.2075 0.1662 0.1635 -0.0197 0.0067  -0.0011 72  TYR   C CG  
1599 C CD1 . TYR   B 66  ? 0.2307 0.1855 0.1790 -0.0238 0.0084  0.0001  72  TYR   C CD1 
1600 C CD2 . TYR   B 66  ? 0.2287 0.1877 0.1824 -0.0195 0.0057  -0.0024 72  TYR   C CD2 
1601 C CE1 . TYR   B 66  ? 0.2544 0.2053 0.1915 -0.0282 0.0094  0.0001  72  TYR   C CE1 
1602 C CE2 . TYR   B 66  ? 0.2520 0.2071 0.1949 -0.0236 0.0061  -0.0026 72  TYR   C CE2 
1603 C CZ  . TYR   B 66  ? 0.2806 0.2316 0.2146 -0.0282 0.0081  -0.0013 72  TYR   C CZ  
1604 O OH  . TYR   B 66  ? 0.3186 0.2652 0.2397 -0.0334 0.0089  -0.0016 72  TYR   C OH  
1605 N N   . PRO   B 67  ? 0.1854 0.1463 0.1586 -0.0147 0.0041  0.0011  73  PRO   C N   
1606 C CA  . PRO   B 67  ? 0.1687 0.1324 0.1473 -0.0142 0.0046  0.0002  73  PRO   C CA  
1607 C C   . PRO   B 67  ? 0.1840 0.1529 0.1673 -0.0152 0.0070  -0.0009 73  PRO   C C   
1608 O O   . PRO   B 67  ? 0.1967 0.1659 0.1791 -0.0173 0.0096  -0.0013 73  PRO   C O   
1609 C CB  . PRO   B 67  ? 0.1776 0.1374 0.1541 -0.0161 0.0045  0.0014  73  PRO   C CB  
1610 C CG  . PRO   B 67  ? 0.2005 0.1570 0.1711 -0.0184 0.0054  0.0028  73  PRO   C CG  
1611 C CD  . PRO   B 67  ? 0.1903 0.1463 0.1574 -0.0176 0.0044  0.0030  73  PRO   C CD  
1612 N N   . VAL   B 68  ? 0.1789 0.1517 0.1678 -0.0141 0.0061  -0.0015 74  VAL   C N   
1613 C CA  . VAL   B 68  ? 0.1775 0.1550 0.1734 -0.0147 0.0073  -0.0021 74  VAL   C CA  
1614 C C   . VAL   B 68  ? 0.1698 0.1497 0.1702 -0.0152 0.0049  -0.0012 74  VAL   C C   
1615 O O   . VAL   B 68  ? 0.1835 0.1619 0.1809 -0.0147 0.0030  -0.0008 74  VAL   C O   
1616 C CB  . VAL   B 68  ? 0.1926 0.1726 0.1916 -0.0131 0.0079  -0.0032 74  VAL   C CB  
1617 C CG1 . VAL   B 68  ? 0.2130 0.1912 0.2074 -0.0138 0.0106  -0.0046 74  VAL   C CG1 
1618 C CG2 . VAL   B 68  ? 0.1895 0.1694 0.1877 -0.0109 0.0054  -0.0029 74  VAL   C CG2 
1619 N N   . SER   B 69  ? 0.1569 0.1404 0.1652 -0.0164 0.0051  -0.0009 75  SER   C N   
1620 C CA  . SER   B 69  ? 0.1576 0.1438 0.1714 -0.0172 0.0017  0.0006  75  SER   C CA  
1621 C C   . SER   B 69  ? 0.1523 0.1414 0.1723 -0.0153 0.0011  0.0006  75  SER   C C   
1622 O O   . SER   B 69  ? 0.1644 0.1546 0.1878 -0.0140 0.0041  -0.0012 75  SER   C O   
1623 C CB  . SER   B 69  ? 0.1825 0.1715 0.2046 -0.0193 0.0013  0.0012  75  SER   C CB  
1624 O OG  . SER   B 69  ? 0.2642 0.2504 0.2810 -0.0213 0.0016  0.0013  75  SER   C OG  
1625 N N   . PHE   B 70  ? 0.1393 0.1289 0.1596 -0.0155 -0.0025 0.0025  76  PHE   C N   
1626 C CA  . PHE   B 70  ? 0.1393 0.1309 0.1656 -0.0139 -0.0034 0.0029  76  PHE   C CA  
1627 C C   . PHE   B 70  ? 0.1526 0.1459 0.1846 -0.0156 -0.0085 0.0063  76  PHE   C C   
1628 O O   . PHE   B 70  ? 0.1668 0.1588 0.1941 -0.0184 -0.0114 0.0081  76  PHE   C O   
1629 C CB  . PHE   B 70  ? 0.1410 0.1307 0.1606 -0.0121 -0.0024 0.0019  76  PHE   C CB  
1630 C CG  . PHE   B 70  ? 0.1467 0.1335 0.1572 -0.0132 -0.0035 0.0024  76  PHE   C CG  
1631 C CD1 . PHE   B 70  ? 0.1496 0.1334 0.1532 -0.0132 -0.0017 0.0009  76  PHE   C CD1 
1632 C CD2 . PHE   B 70  ? 0.1653 0.1521 0.1746 -0.0146 -0.0061 0.0042  76  PHE   C CD2 
1633 C CE1 . PHE   B 70  ? 0.1568 0.1381 0.1540 -0.0142 -0.0018 0.0004  76  PHE   C CE1 
1634 C CE2 . PHE   B 70  ? 0.1655 0.1497 0.1664 -0.0162 -0.0057 0.0037  76  PHE   C CE2 
1635 C CZ  . PHE   B 70  ? 0.1614 0.1430 0.1570 -0.0158 -0.0033 0.0014  76  PHE   C CZ  
1636 N N   . SER   B 71  ? 0.1384 0.1342 0.1807 -0.0144 -0.0098 0.0071  77  SER   C N   
1637 C CA  . SER   B 71  ? 0.1565 0.1535 0.2060 -0.0162 -0.0157 0.0112  77  SER   C CA  
1638 C C   . SER   B 71  ? 0.1739 0.1683 0.2145 -0.0181 -0.0192 0.0141  77  SER   C C   
1639 O O   . SER   B 71  ? 0.1764 0.1685 0.2064 -0.0177 -0.0165 0.0123  77  SER   C O   
1640 C CB  . SER   B 71  ? 0.1578 0.1580 0.2236 -0.0142 -0.0160 0.0112  77  SER   C CB  
1641 O OG  . SER   B 71  ? 0.1792 0.1787 0.2447 -0.0120 -0.0139 0.0097  77  SER   C OG  
1642 N N   . LYS   B 72  ? 0.1677 0.1623 0.2127 -0.0207 -0.0256 0.0187  78  LYS   C N   
1643 C CA  . LYS   B 72  ? 0.1941 0.1859 0.2301 -0.0236 -0.0289 0.0218  78  LYS   C CA  
1644 C C   . LYS   B 72  ? 0.1833 0.1755 0.2249 -0.0210 -0.0281 0.0219  78  LYS   C C   
1645 O O   . LYS   B 72  ? 0.2050 0.1998 0.2610 -0.0182 -0.0281 0.0216  78  LYS   C O   
1646 C CB  . LYS   B 72  ? 0.2210 0.2123 0.2595 -0.0280 -0.0370 0.0275  78  LYS   C CB  
1647 C CG  . LYS   B 72  ? 0.2867 0.2773 0.3194 -0.0311 -0.0384 0.0274  78  LYS   C CG  
1648 C CD  . LYS   B 72  ? 0.3831 0.3727 0.4168 -0.0364 -0.0477 0.0336  78  LYS   C CD  
1649 C CE  . LYS   B 72  ? 0.4786 0.4672 0.5060 -0.0402 -0.0498 0.0336  78  LYS   C CE  
1650 N NZ  . LYS   B 72  ? 0.5324 0.5204 0.5631 -0.0454 -0.0600 0.0401  78  LYS   C NZ  
1651 N N   . PRO   B 73  ? 0.1818 0.1714 0.2135 -0.0224 -0.0275 0.0224  79  PRO   C N   
1652 C CA  . PRO   B 73  ? 0.1880 0.1780 0.2253 -0.0202 -0.0267 0.0225  79  PRO   C CA  
1653 C C   . PRO   B 73  ? 0.2120 0.2027 0.2627 -0.0206 -0.0327 0.0272  79  PRO   C C   
1654 O O   . PRO   B 73  ? 0.2344 0.2236 0.2841 -0.0247 -0.0393 0.0325  79  PRO   C O   
1655 C CB  . PRO   B 73  ? 0.2087 0.1957 0.2327 -0.0230 -0.0257 0.0230  79  PRO   C CB  
1656 C CG  . PRO   B 73  ? 0.2296 0.2149 0.2413 -0.0256 -0.0238 0.0213  79  PRO   C CG  
1657 C CD  . PRO   B 73  ? 0.1800 0.1665 0.1956 -0.0261 -0.0263 0.0220  79  PRO   C CD  
1658 N N   . SER   B 74  ? 0.1985 0.1912 0.2626 -0.0167 -0.0308 0.0251  80  SER   C N   
1659 C CA  . SER   B 74  ? 0.2244 0.2179 0.3050 -0.0164 -0.0363 0.0290  80  SER   C CA  
1660 C C   . SER   B 74  ? 0.2054 0.1996 0.2969 -0.0129 -0.0335 0.0265  80  SER   C C   
1661 O O   . SER   B 74  ? 0.1925 0.1866 0.2775 -0.0109 -0.0277 0.0219  80  SER   C O   
1662 C CB  . SER   B 74  ? 0.2873 0.2838 0.3801 -0.0158 -0.0377 0.0288  80  SER   C CB  
1663 O OG  . SER   B 74  ? 0.3461 0.3455 0.4467 -0.0119 -0.0308 0.0224  80  SER   C OG  
1664 N N   . LEU   B 75  ? 0.1953 0.1898 0.3036 -0.0125 -0.0384 0.0299  81  LEU   C N   
1665 C CA  . LEU   B 75  ? 0.2099 0.2045 0.3310 -0.0095 -0.0364 0.0277  81  LEU   C CA  
1666 C C   . LEU   B 75  ? 0.2124 0.2106 0.3481 -0.0059 -0.0312 0.0216  81  LEU   C C   
1667 O O   . LEU   B 75  ? 0.2242 0.2245 0.3744 -0.0058 -0.0342 0.0231  81  LEU   C O   
1668 C CB  . LEU   B 75  ? 0.2384 0.2312 0.3730 -0.0110 -0.0450 0.0348  81  LEU   C CB  
1669 C CG  . LEU   B 75  ? 0.3006 0.2894 0.4303 -0.0132 -0.0486 0.0394  81  LEU   C CG  
1670 C CD1 . LEU   B 75  ? 0.3210 0.3083 0.4697 -0.0138 -0.0570 0.0458  81  LEU   C CD1 
1671 C CD2 . LEU   B 75  ? 0.3092 0.2978 0.4362 -0.0105 -0.0417 0.0338  81  LEU   C CD2 
1672 N N   . ILE   B 76  ? 0.1905 0.1893 0.3232 -0.0035 -0.0236 0.0148  82  ILE   C N   
1673 C CA  . ILE   B 76  ? 0.1994 0.2008 0.3417 -0.0012 -0.0170 0.0079  82  ILE   C CA  
1674 C C   . ILE   B 76  ? 0.1918 0.1928 0.3429 0.0010  -0.0125 0.0028  82  ILE   C C   
1675 O O   . ILE   B 76  ? 0.1801 0.1789 0.3216 0.0010  -0.0117 0.0022  82  ILE   C O   
1676 C CB  . ILE   B 76  ? 0.2386 0.2405 0.3639 -0.0017 -0.0117 0.0042  82  ILE   C CB  
1677 C CG1 . ILE   B 76  ? 0.2691 0.2714 0.3880 -0.0040 -0.0158 0.0086  82  ILE   C CG1 
1678 C CG2 . ILE   B 76  ? 0.2577 0.2613 0.3880 -0.0004 -0.0039 -0.0033 82  ILE   C CG2 
1679 C CD1 . ILE   B 76  ? 0.3034 0.3054 0.4067 -0.0047 -0.0118 0.0059  82  ILE   C CD1 
1680 N N   . PHE   B 77  ? 0.1855 0.1884 0.3557 0.0026  -0.0094 -0.0013 83  PHE   C N   
1681 C CA  . PHE   B 77  ? 0.1912 0.1934 0.3710 0.0042  -0.0048 -0.0070 83  PHE   C CA  
1682 C C   . PHE   B 77  ? 0.1955 0.1970 0.3600 0.0040  0.0030  -0.0141 83  PHE   C C   
1683 O O   . PHE   B 77  ? 0.2097 0.2126 0.3675 0.0031  0.0077  -0.0176 83  PHE   C O   
1684 C CB  . PHE   B 77  ? 0.1958 0.2004 0.4018 0.0057  -0.0024 -0.0106 83  PHE   C CB  
1685 C CG  . PHE   B 77  ? 0.2066 0.2099 0.4241 0.0072  0.0023  -0.0167 83  PHE   C CG  
1686 C CD1 . PHE   B 77  ? 0.2230 0.2273 0.4429 0.0071  0.0122  -0.0265 83  PHE   C CD1 
1687 C CD2 . PHE   B 77  ? 0.2154 0.2158 0.4390 0.0079  -0.0028 -0.0129 83  PHE   C CD2 
1688 C CE1 . PHE   B 77  ? 0.2304 0.2330 0.4603 0.0079  0.0169  -0.0328 83  PHE   C CE1 
1689 C CE2 . PHE   B 77  ? 0.2347 0.2335 0.4692 0.0091  0.0016  -0.0189 83  PHE   C CE2 
1690 C CZ  . PHE   B 77  ? 0.2330 0.2330 0.4705 0.0091  0.0115  -0.0291 83  PHE   C CZ  
1691 N N   . VAL   B 78  ? 0.1963 0.1954 0.3555 0.0043  0.0041  -0.0160 84  VAL   C N   
1692 C CA  . VAL   B 78  ? 0.2052 0.2032 0.3503 0.0035  0.0102  -0.0224 84  VAL   C CA  
1693 C C   . VAL   B 78  ? 0.2059 0.2027 0.3621 0.0041  0.0145  -0.0287 84  VAL   C C   
1694 O O   . VAL   B 78  ? 0.2023 0.1976 0.3668 0.0051  0.0109  -0.0264 84  VAL   C O   
1695 C CB  . VAL   B 78  ? 0.2186 0.2148 0.3446 0.0029  0.0071  -0.0189 84  VAL   C CB  
1696 C CG1 . VAL   B 78  ? 0.2287 0.2236 0.3403 0.0018  0.0121  -0.0246 84  VAL   C CG1 
1697 C CG2 . VAL   B 78  ? 0.2270 0.2239 0.3439 0.0021  0.0029  -0.0129 84  VAL   C CG2 
1698 N N   . GLU   B 79  ? 0.2192 0.2162 0.3749 0.0030  0.0223  -0.0368 85  GLU   C N   
1699 C CA  . GLU   B 79  ? 0.2219 0.2174 0.3868 0.0028  0.0278  -0.0444 85  GLU   C CA  
1700 C C   . GLU   B 79  ? 0.2180 0.2105 0.3720 0.0023  0.0262  -0.0449 85  GLU   C C   
1701 O O   . GLU   B 79  ? 0.2103 0.2021 0.3464 0.0016  0.0230  -0.0413 85  GLU   C O   
1702 C CB  . GLU   B 79  ? 0.2577 0.2534 0.4175 0.0002  0.0371  -0.0531 85  GLU   C CB  
1703 C CG  . GLU   B 79  ? 0.3691 0.3679 0.5361 -0.0001 0.0398  -0.0534 85  GLU   C CG  
1704 C CD  . GLU   B 79  ? 0.4653 0.4663 0.6593 0.0010  0.0441  -0.0581 85  GLU   C CD  
1705 O OE1 . GLU   B 79  ? 0.4890 0.4929 0.6904 0.0002  0.0481  -0.0601 85  GLU   C OE1 
1706 O OE2 . GLU   B 79  ? 0.4721 0.4720 0.6815 0.0027  0.0433  -0.0595 85  GLU   C OE2 
1707 N N   . ALA   B 80  ? 0.2111 0.2019 0.3768 0.0026  0.0285  -0.0496 86  ALA   C N   
1708 C CA  . ALA   B 80  ? 0.2135 0.2015 0.3700 0.0019  0.0270  -0.0505 86  ALA   C CA  
1709 C C   . ALA   B 80  ? 0.2287 0.2153 0.3631 -0.0011 0.0303  -0.0548 86  ALA   C C   
1710 O O   . ALA   B 80  ? 0.2377 0.2245 0.3666 -0.0033 0.0362  -0.0600 86  ALA   C O   
1711 C CB  . ALA   B 80  ? 0.2054 0.1913 0.3785 0.0022  0.0302  -0.0565 86  ALA   C CB  
1712 N N   . SER   B 81  ? 0.2118 0.1971 0.3337 -0.0015 0.0261  -0.0519 87  SER   C N   
1713 C CA  . SER   B 81  ? 0.2017 0.1853 0.3042 -0.0043 0.0273  -0.0549 87  SER   C CA  
1714 C C   . SER   B 81  ? 0.2193 0.2008 0.3216 -0.0047 0.0247  -0.0560 87  SER   C C   
1715 O O   . SER   B 81  ? 0.2200 0.2013 0.3367 -0.0028 0.0228  -0.0544 87  SER   C O   
1716 C CB  . SER   B 81  ? 0.2036 0.1884 0.2918 -0.0040 0.0230  -0.0486 87  SER   C CB  
1717 O OG  . SER   B 81  ? 0.1915 0.1772 0.2817 -0.0019 0.0170  -0.0419 87  SER   C OG  
1718 N N   . GLU   B 82  ? 0.2144 0.1941 0.3010 -0.0073 0.0242  -0.0584 88  GLU   C N   
1719 C CA  . GLU   B 82  ? 0.2201 0.1983 0.3064 -0.0078 0.0210  -0.0588 88  GLU   C CA  
1720 C C   . GLU   B 82  ? 0.2153 0.1955 0.3052 -0.0050 0.0148  -0.0506 88  GLU   C C   
1721 O O   . GLU   B 82  ? 0.2210 0.2005 0.3171 -0.0047 0.0125  -0.0499 88  GLU   C O   
1722 C CB  . GLU   B 82  ? 0.2685 0.2444 0.3370 -0.0115 0.0202  -0.0620 88  GLU   C CB  
1723 C CG  . GLU   B 82  ? 0.3304 0.3031 0.3948 -0.0157 0.0265  -0.0712 88  GLU   C CG  
1724 C CD  . GLU   B 82  ? 0.4624 0.4319 0.5082 -0.0206 0.0252  -0.0744 88  GLU   C CD  
1725 O OE1 . GLU   B 82  ? 0.5136 0.4800 0.5519 -0.0251 0.0308  -0.0818 88  GLU   C OE1 
1726 O OE2 . GLU   B 82  ? 0.4403 0.4102 0.4794 -0.0203 0.0184  -0.0698 88  GLU   C OE2 
1727 N N   . TYR   B 83  ? 0.2023 0.1847 0.2880 -0.0036 0.0126  -0.0448 89  TYR   C N   
1728 C CA  . TYR   B 83  ? 0.1986 0.1826 0.2848 -0.0020 0.0077  -0.0378 89  TYR   C CA  
1729 C C   . TYR   B 83  ? 0.2005 0.1851 0.3000 -0.0002 0.0062  -0.0332 89  TYR   C C   
1730 O O   . TYR   B 83  ? 0.2271 0.2121 0.3280 0.0001  0.0028  -0.0283 89  TYR   C O   
1731 C CB  . TYR   B 83  ? 0.1957 0.1812 0.2703 -0.0017 0.0062  -0.0340 89  TYR   C CB  
1732 C CG  . TYR   B 83  ? 0.2147 0.1989 0.2757 -0.0037 0.0063  -0.0370 89  TYR   C CG  
1733 C CD1 . TYR   B 83  ? 0.2366 0.2205 0.2923 -0.0045 0.0030  -0.0367 89  TYR   C CD1 
1734 C CD2 . TYR   B 83  ? 0.2261 0.2095 0.2799 -0.0051 0.0094  -0.0398 89  TYR   C CD2 
1735 C CE1 . TYR   B 83  ? 0.2559 0.2383 0.2993 -0.0065 0.0015  -0.0383 89  TYR   C CE1 
1736 C CE2 . TYR   B 83  ? 0.2579 0.2394 0.2978 -0.0076 0.0086  -0.0413 89  TYR   C CE2 
1737 C CZ  . TYR   B 83  ? 0.2830 0.2638 0.3177 -0.0083 0.0042  -0.0404 89  TYR   C CZ  
1738 O OH  . TYR   B 83  ? 0.3324 0.3109 0.3537 -0.0110 0.0020  -0.0411 89  TYR   C OH  
1739 N N   . TYR   B 84  ? 0.1930 0.1778 0.3022 0.0006  0.0085  -0.0342 90  TYR   C N   
1740 C CA  . TYR   B 84  ? 0.1928 0.1781 0.3147 0.0019  0.0057  -0.0287 90  TYR   C CA  
1741 C C   . TYR   B 84  ? 0.2018 0.1864 0.3403 0.0027  0.0086  -0.0325 90  TYR   C C   
1742 O O   . TYR   B 84  ? 0.2112 0.1962 0.3495 0.0022  0.0137  -0.0387 90  TYR   C O   
1743 C CB  . TYR   B 84  ? 0.1849 0.1721 0.3014 0.0023  0.0039  -0.0236 90  TYR   C CB  
1744 C CG  . TYR   B 84  ? 0.1768 0.1647 0.2797 0.0016  0.0011  -0.0193 90  TYR   C CG  
1745 C CD1 . TYR   B 84  ? 0.1766 0.1655 0.2665 0.0013  0.0025  -0.0206 90  TYR   C CD1 
1746 C CD2 . TYR   B 84  ? 0.1721 0.1596 0.2757 0.0011  -0.0026 -0.0139 90  TYR   C CD2 
1747 C CE1 . TYR   B 84  ? 0.1809 0.1704 0.2609 0.0009  0.0003  -0.0171 90  TYR   C CE1 
1748 C CE2 . TYR   B 84  ? 0.1709 0.1592 0.2633 0.0002  -0.0040 -0.0108 90  TYR   C CE2 
1749 C CZ  . TYR   B 84  ? 0.1745 0.1639 0.2561 0.0004  -0.0025 -0.0126 90  TYR   C CZ  
1750 O OH  . TYR   B 84  ? 0.1782 0.1683 0.2512 -0.0003 -0.0034 -0.0104 90  TYR   C OH  
1751 N N   . PRO   B 85  ? 0.2059 0.1896 0.3596 0.0037  0.0052  -0.0283 91  PRO   C N   
1752 C CA  . PRO   B 85  ? 0.1977 0.1813 0.3704 0.0050  0.0073  -0.0310 91  PRO   C CA  
1753 C C   . PRO   B 85  ? 0.1983 0.1846 0.3720 0.0055  0.0073  -0.0288 91  PRO   C C   
1754 O O   . PRO   B 85  ? 0.1927 0.1803 0.3537 0.0050  0.0042  -0.0236 91  PRO   C O   
1755 C CB  . PRO   B 85  ? 0.2033 0.1848 0.3903 0.0056  0.0013  -0.0244 91  PRO   C CB  
1756 C CG  . PRO   B 85  ? 0.2182 0.1999 0.3910 0.0044  -0.0039 -0.0166 91  PRO   C CG  
1757 C CD  . PRO   B 85  ? 0.2083 0.1911 0.3625 0.0034  -0.0008 -0.0204 91  PRO   C CD  
1758 N N   . ALA   B 86  ? 0.1932 0.1804 0.3841 0.0066  0.0103  -0.0325 92  ALA   C N   
1759 C CA  . ALA   B 86  ? 0.1904 0.1804 0.3867 0.0072  0.0096  -0.0299 92  ALA   C CA  
1760 C C   . ALA   B 86  ? 0.1916 0.1813 0.3902 0.0074  0.0003  -0.0190 92  ALA   C C   
1761 O O   . ALA   B 86  ? 0.1963 0.1836 0.4042 0.0076  -0.0042 -0.0151 92  ALA   C O   
1762 C CB  . ALA   B 86  ? 0.1878 0.1787 0.4077 0.0084  0.0140  -0.0356 92  ALA   C CB  
1763 N N   . ARG   B 87  ? 0.1853 0.1769 0.3726 0.0065  -0.0024 -0.0143 93  ARG   C N   
1764 C CA  . ARG   B 87  ? 0.1828 0.1734 0.3677 0.0054  -0.0107 -0.0044 93  ARG   C CA  
1765 C C   . ARG   B 87  ? 0.1836 0.1763 0.3599 0.0044  -0.0127 -0.0009 93  ARG   C C   
1766 O O   . ARG   B 87  ? 0.2044 0.1993 0.3742 0.0047  -0.0074 -0.0059 93  ARG   C O   
1767 C CB  . ARG   B 87  ? 0.1850 0.1732 0.3534 0.0040  -0.0122 -0.0020 93  ARG   C CB  
1768 C CG  . ARG   B 87  ? 0.1665 0.1562 0.3131 0.0031  -0.0090 -0.0041 93  ARG   C CG  
1769 C CD  . ARG   B 87  ? 0.1835 0.1718 0.3182 0.0024  -0.0078 -0.0055 93  ARG   C CD  
1770 N NE  . ARG   B 87  ? 0.1761 0.1651 0.2931 0.0011  -0.0083 -0.0032 93  ARG   C NE  
1771 C CZ  . ARG   B 87  ? 0.2012 0.1916 0.3073 0.0013  -0.0052 -0.0064 93  ARG   C CZ  
1772 N NH1 . ARG   B 87  ? 0.1847 0.1753 0.2773 0.0003  -0.0059 -0.0043 93  ARG   C NH1 
1773 N NH2 . ARG   B 87  ? 0.1877 0.1791 0.2968 0.0022  -0.0011 -0.0118 93  ARG   C NH2 
1774 N N   . TYR   B 88  ? 0.1826 0.1742 0.3561 0.0026  -0.0202 0.0077  94  TYR   C N   
1775 C CA  . TYR   B 88  ? 0.1976 0.1907 0.3597 0.0010  -0.0222 0.0109  94  TYR   C CA  
1776 C C   . TYR   B 88  ? 0.1812 0.1731 0.3206 -0.0008 -0.0215 0.0121  94  TYR   C C   
1777 O O   . TYR   B 88  ? 0.1858 0.1751 0.3205 -0.0023 -0.0243 0.0157  94  TYR   C O   
1778 C CB  . TYR   B 88  ? 0.2116 0.2039 0.3821 -0.0008 -0.0310 0.0194  94  TYR   C CB  
1779 C CG  . TYR   B 88  ? 0.2474 0.2419 0.4420 0.0012  -0.0319 0.0183  94  TYR   C CG  
1780 C CD1 . TYR   B 88  ? 0.2720 0.2699 0.4698 0.0014  -0.0304 0.0165  94  TYR   C CD1 
1781 C CD2 . TYR   B 88  ? 0.2718 0.2651 0.4874 0.0029  -0.0334 0.0181  94  TYR   C CD2 
1782 C CE1 . TYR   B 88  ? 0.2886 0.2890 0.5107 0.0032  -0.0305 0.0148  94  TYR   C CE1 
1783 C CE2 . TYR   B 88  ? 0.2844 0.2800 0.5251 0.0050  -0.0335 0.0162  94  TYR   C CE2 
1784 C CZ  . TYR   B 88  ? 0.3009 0.3004 0.5450 0.0052  -0.0317 0.0143  94  TYR   C CZ  
1785 O OH  . TYR   B 88  ? 0.3270 0.3294 0.5977 0.0071  -0.0312 0.0119  94  TYR   C OH  
1786 N N   . GLN   B 89  ? 0.1620 0.1555 0.2886 -0.0008 -0.0175 0.0088  95  GLN   C N   
1787 C CA  . GLN   B 89  ? 0.1602 0.1528 0.2678 -0.0024 -0.0167 0.0095  95  GLN   C CA  
1788 C C   . GLN   B 89  ? 0.1579 0.1502 0.2579 -0.0050 -0.0209 0.0149  95  GLN   C C   
1789 O O   . GLN   B 89  ? 0.1746 0.1685 0.2782 -0.0049 -0.0214 0.0149  95  GLN   C O   
1790 C CB  . GLN   B 89  ? 0.1687 0.1624 0.2674 -0.0010 -0.0105 0.0030  95  GLN   C CB  
1791 C CG  . GLN   B 89  ? 0.1764 0.1692 0.2579 -0.0022 -0.0099 0.0037  95  GLN   C CG  
1792 C CD  . GLN   B 89  ? 0.1610 0.1541 0.2351 -0.0009 -0.0054 -0.0018 95  GLN   C CD  
1793 O OE1 . GLN   B 89  ? 0.1684 0.1613 0.2471 0.0002  -0.0029 -0.0059 95  GLN   C OE1 
1794 N NE2 . GLN   B 89  ? 0.1399 0.1328 0.2019 -0.0015 -0.0045 -0.0019 95  GLN   C NE2 
1795 N N   . SER   B 90  ? 0.1551 0.1452 0.2444 -0.0079 -0.0237 0.0191  96  SER   C N   
1796 C CA  . SER   B 90  ? 0.1557 0.1447 0.2359 -0.0116 -0.0277 0.0241  96  SER   C CA  
1797 C C   . SER   B 90  ? 0.1580 0.1473 0.2225 -0.0122 -0.0236 0.0210  96  SER   C C   
1798 O O   . SER   B 90  ? 0.1703 0.1603 0.2305 -0.0101 -0.0187 0.0163  96  SER   C O   
1799 C CB  . SER   B 90  ? 0.1878 0.1735 0.2640 -0.0156 -0.0326 0.0303  96  SER   C CB  
1800 O OG  . SER   B 90  ? 0.2190 0.2037 0.2872 -0.0159 -0.0289 0.0282  96  SER   C OG  
1801 N N   . HIS   B 91  ? 0.1589 0.1475 0.2157 -0.0153 -0.0262 0.0239  97  HIS   C N   
1802 C CA  . HIS   B 91  ? 0.1685 0.1567 0.2110 -0.0165 -0.0227 0.0214  97  HIS   C CA  
1803 C C   . HIS   B 91  ? 0.1705 0.1608 0.2143 -0.0126 -0.0177 0.0157  97  HIS   C C   
1804 O O   . HIS   B 91  ? 0.1751 0.1651 0.2101 -0.0121 -0.0140 0.0126  97  HIS   C O   
1805 C CB  . HIS   B 91  ? 0.1826 0.1690 0.2149 -0.0185 -0.0204 0.0210  97  HIS   C CB  
1806 C CG  . HIS   B 91  ? 0.2021 0.1855 0.2296 -0.0236 -0.0247 0.0266  97  HIS   C CG  
1807 N ND1 . HIS   B 91  ? 0.2352 0.2164 0.2503 -0.0288 -0.0261 0.0288  97  HIS   C ND1 
1808 C CD2 . HIS   B 91  ? 0.2230 0.2051 0.2566 -0.0248 -0.0283 0.0307  97  HIS   C CD2 
1809 C CE1 . HIS   B 91  ? 0.2415 0.2197 0.2534 -0.0335 -0.0303 0.0342  97  HIS   C CE1 
1810 N NE2 . HIS   B 91  ? 0.2538 0.2324 0.2771 -0.0312 -0.0320 0.0359  97  HIS   C NE2 
1811 N N   . LEU   B 92  ? 0.1619 0.1543 0.2171 -0.0103 -0.0177 0.0145  98  LEU   C N   
1812 C CA  . LEU   B 92  ? 0.1581 0.1519 0.2137 -0.0076 -0.0128 0.0093  98  LEU   C CA  
1813 C C   . LEU   B 92  ? 0.1684 0.1631 0.2232 -0.0085 -0.0130 0.0095  98  LEU   C C   
1814 O O   . LEU   B 92  ? 0.1700 0.1655 0.2319 -0.0099 -0.0170 0.0128  98  LEU   C O   
1815 C CB  . LEU   B 92  ? 0.1678 0.1631 0.2366 -0.0051 -0.0111 0.0066  98  LEU   C CB  
1816 C CG  . LEU   B 92  ? 0.1996 0.1957 0.2675 -0.0033 -0.0056 0.0010  98  LEU   C CG  
1817 C CD1 . LEU   B 92  ? 0.1907 0.1852 0.2470 -0.0028 -0.0034 -0.0012 98  LEU   C CD1 
1818 C CD2 . LEU   B 92  ? 0.2341 0.2313 0.3152 -0.0017 -0.0034 -0.0022 98  LEU   C CD2 
1819 N N   . MET   B 93  ? 0.1611 0.1555 0.2078 -0.0079 -0.0094 0.0064  99  MET   C N   
1820 C CA  . MET   B 93  ? 0.1629 0.1577 0.2082 -0.0090 -0.0091 0.0063  99  MET   C CA  
1821 C C   . MET   B 93  ? 0.1733 0.1691 0.2211 -0.0073 -0.0043 0.0020  99  MET   C C   
1822 O O   . MET   B 93  ? 0.1827 0.1773 0.2252 -0.0060 -0.0014 -0.0007 99  MET   C O   
1823 C CB  . MET   B 93  ? 0.1624 0.1548 0.1945 -0.0106 -0.0088 0.0065  99  MET   C CB  
1824 C CG  . MET   B 93  ? 0.2213 0.2122 0.2485 -0.0134 -0.0124 0.0099  99  MET   C CG  
1825 S SD  . MET   B 93  ? 0.2399 0.2279 0.2530 -0.0152 -0.0102 0.0083  99  MET   C SD  
1826 C CE  . MET   B 93  ? 0.2005 0.1883 0.2124 -0.0117 -0.0061 0.0047  99  MET   C CE  
1827 N N   . LEU   B 94  ? 0.1548 0.1524 0.2099 -0.0078 -0.0035 0.0015  100 LEU   C N   
1828 C CA  . LEU   B 94  ? 0.1473 0.1455 0.2037 -0.0072 0.0019  -0.0028 100 LEU   C CA  
1829 C C   . LEU   B 94  ? 0.1443 0.1415 0.1931 -0.0087 0.0035  -0.0031 100 LEU   C C   
1830 O O   . LEU   B 94  ? 0.1374 0.1348 0.1862 -0.0102 0.0005  -0.0005 100 LEU   C O   
1831 C CB  . LEU   B 94  ? 0.1553 0.1568 0.2283 -0.0069 0.0034  -0.0044 100 LEU   C CB  
1832 C CG  . LEU   B 94  ? 0.1921 0.1946 0.2761 -0.0053 0.0024  -0.0047 100 LEU   C CG  
1833 C CD1 . LEU   B 94  ? 0.2258 0.2315 0.3287 -0.0049 0.0048  -0.0071 100 LEU   C CD1 
1834 C CD2 . LEU   B 94  ? 0.2079 0.2084 0.2846 -0.0042 0.0057  -0.0080 100 LEU   C CD2 
1835 N N   . ALA   B 95  ? 0.1502 0.1459 0.1929 -0.0088 0.0079  -0.0063 101 ALA   C N   
1836 C CA  . ALA   B 95  ? 0.1395 0.1336 0.1757 -0.0106 0.0100  -0.0067 101 ALA   C CA  
1837 C C   . ALA   B 95  ? 0.1461 0.1405 0.1838 -0.0117 0.0158  -0.0106 101 ALA   C C   
1838 O O   . ALA   B 95  ? 0.1601 0.1545 0.1987 -0.0112 0.0182  -0.0133 101 ALA   C O   
1839 C CB  . ALA   B 95  ? 0.1569 0.1470 0.1794 -0.0105 0.0089  -0.0057 101 ALA   C CB  
1840 N N   . VAL   B 96  ? 0.1527 0.1469 0.1891 -0.0140 0.0185  -0.0112 102 VAL   C N   
1841 C CA  . VAL   B 96  ? 0.1634 0.1568 0.1975 -0.0163 0.0248  -0.0149 102 VAL   C CA  
1842 C C   . VAL   B 96  ? 0.1838 0.1720 0.2011 -0.0173 0.0247  -0.0145 102 VAL   C C   
1843 O O   . VAL   B 96  ? 0.2031 0.1883 0.2123 -0.0177 0.0220  -0.0117 102 VAL   C O   
1844 C CB  . VAL   B 96  ? 0.1816 0.1768 0.2212 -0.0188 0.0278  -0.0155 102 VAL   C CB  
1845 C CG1 . VAL   B 96  ? 0.1892 0.1830 0.2244 -0.0222 0.0354  -0.0197 102 VAL   C CG1 
1846 C CG2 . VAL   B 96  ? 0.1947 0.1954 0.2534 -0.0177 0.0266  -0.0154 102 VAL   C CG2 
1847 N N   . GLY   B 97  ? 0.1975 0.1843 0.2103 -0.0177 0.0269  -0.0172 103 GLY   C N   
1848 C CA  . GLY   B 97  ? 0.2173 0.1989 0.2149 -0.0188 0.0255  -0.0163 103 GLY   C CA  
1849 C C   . GLY   B 97  ? 0.2256 0.2059 0.2189 -0.0198 0.0277  -0.0196 103 GLY   C C   
1850 O O   . GLY   B 97  ? 0.2270 0.2105 0.2302 -0.0187 0.0299  -0.0227 103 GLY   C O   
1851 N N   . HIS   B 98  ? 0.2172 0.1925 0.1963 -0.0220 0.0263  -0.0187 104 HIS   C N   
1852 C CA  . HIS   B 98  ? 0.2265 0.1997 0.1990 -0.0238 0.0274  -0.0216 104 HIS   C CA  
1853 C C   . HIS   B 98  ? 0.2171 0.1908 0.1917 -0.0202 0.0221  -0.0203 104 HIS   C C   
1854 O O   . HIS   B 98  ? 0.2217 0.1947 0.1957 -0.0177 0.0168  -0.0164 104 HIS   C O   
1855 C CB  . HIS   B 98  ? 0.2523 0.2191 0.2073 -0.0286 0.0269  -0.0203 104 HIS   C CB  
1856 C CG  . HIS   B 98  ? 0.2689 0.2328 0.2149 -0.0313 0.0269  -0.0228 104 HIS   C CG  
1857 N ND1 . HIS   B 98  ? 0.2937 0.2585 0.2402 -0.0345 0.0338  -0.0290 104 HIS   C ND1 
1858 C CD2 . HIS   B 98  ? 0.2901 0.2506 0.2279 -0.0312 0.0206  -0.0204 104 HIS   C CD2 
1859 C CE1 . HIS   B 98  ? 0.3168 0.2782 0.2534 -0.0367 0.0316  -0.0301 104 HIS   C CE1 
1860 N NE2 . HIS   B 98  ? 0.3239 0.2827 0.2554 -0.0347 0.0232  -0.0247 104 HIS   C NE2 
1861 N N   . SER   B 99  ? 0.2175 0.1920 0.1942 -0.0206 0.0241  -0.0241 105 SER   C N   
1862 C CA  . SER   B 99  ? 0.2316 0.2062 0.2091 -0.0182 0.0197  -0.0236 105 SER   C CA  
1863 C C   . SER   B 99  ? 0.2396 0.2128 0.2138 -0.0209 0.0227  -0.0285 105 SER   C C   
1864 O O   . SER   B 99  ? 0.2423 0.2161 0.2184 -0.0235 0.0292  -0.0333 105 SER   C O   
1865 C CB  . SER   B 99  ? 0.2467 0.2256 0.2377 -0.0136 0.0175  -0.0220 105 SER   C CB  
1866 O OG  . SER   B 99  ? 0.2683 0.2505 0.2709 -0.0131 0.0217  -0.0255 105 SER   C OG  
1867 N N   . GLU   B 100 ? 0.2372 0.2086 0.2066 -0.0205 0.0181  -0.0277 106 GLU   C N   
1868 C CA  . GLU   B 100 ? 0.2448 0.2150 0.2116 -0.0226 0.0193  -0.0321 106 GLU   C CA  
1869 C C   . GLU   B 100 ? 0.2408 0.2138 0.2178 -0.0181 0.0151  -0.0307 106 GLU   C C   
1870 O O   . GLU   B 100 ? 0.2288 0.2032 0.2096 -0.0147 0.0106  -0.0262 106 GLU   C O   
1871 C CB  . GLU   B 100 ? 0.2865 0.2509 0.2359 -0.0273 0.0160  -0.0314 106 GLU   C CB  
1872 C CG  . GLU   B 100 ? 0.4270 0.3875 0.3637 -0.0322 0.0187  -0.0308 106 GLU   C CG  
1873 C CD  . GLU   B 100 ? 0.5571 0.5146 0.4836 -0.0388 0.0254  -0.0367 106 GLU   C CD  
1874 O OE1 . GLU   B 100 ? 0.5838 0.5426 0.5150 -0.0393 0.0289  -0.0423 106 GLU   C OE1 
1875 O OE2 . GLU   B 100 ? 0.5907 0.5443 0.5046 -0.0439 0.0276  -0.0361 106 GLU   C OE2 
1876 N N   . PRO   B 101 ? 0.2421 0.2156 0.2233 -0.0184 0.0166  -0.0348 107 PRO   C N   
1877 C CA  . PRO   B 101 ? 0.2359 0.2120 0.2268 -0.0146 0.0127  -0.0333 107 PRO   C CA  
1878 C C   . PRO   B 101 ? 0.2273 0.2023 0.2134 -0.0134 0.0058  -0.0290 107 PRO   C C   
1879 O O   . PRO   B 101 ? 0.2330 0.2106 0.2275 -0.0098 0.0031  -0.0261 107 PRO   C O   
1880 C CB  . PRO   B 101 ? 0.2574 0.2327 0.2505 -0.0164 0.0156  -0.0390 107 PRO   C CB  
1881 C CG  . PRO   B 101 ? 0.2740 0.2486 0.2662 -0.0196 0.0232  -0.0441 107 PRO   C CG  
1882 C CD  . PRO   B 101 ? 0.2606 0.2326 0.2394 -0.0224 0.0227  -0.0415 107 PRO   C CD  
1883 N N   . GLY   B 102 ? 0.2279 0.1987 0.2009 -0.0168 0.0030  -0.0284 108 GLY   C N   
1884 C CA  . GLY   B 102 ? 0.2225 0.1921 0.1928 -0.0158 -0.0041 -0.0242 108 GLY   C CA  
1885 C C   . GLY   B 102 ? 0.2161 0.1868 0.1899 -0.0127 -0.0061 -0.0195 108 GLY   C C   
1886 O O   . GLY   B 102 ? 0.2099 0.1805 0.1857 -0.0110 -0.0113 -0.0164 108 GLY   C O   
1887 N N   . ASP   B 103 ? 0.1941 0.1659 0.1695 -0.0122 -0.0019 -0.0194 109 ASP   C N   
1888 C CA  . ASP   B 103 ? 0.1907 0.1634 0.1692 -0.0098 -0.0031 -0.0157 109 ASP   C CA  
1889 C C   . ASP   B 103 ? 0.1773 0.1542 0.1675 -0.0060 -0.0032 -0.0149 109 ASP   C C   
1890 O O   . ASP   B 103 ? 0.1762 0.1537 0.1690 -0.0042 -0.0043 -0.0123 109 ASP   C O   
1891 C CB  . ASP   B 103 ? 0.1897 0.1621 0.1657 -0.0112 0.0013  -0.0159 109 ASP   C CB  
1892 C CG  . ASP   B 103 ? 0.2315 0.1990 0.1944 -0.0155 0.0011  -0.0155 109 ASP   C CG  
1893 O OD1 . ASP   B 103 ? 0.2502 0.2143 0.2068 -0.0164 -0.0042 -0.0129 109 ASP   C OD1 
1894 O OD2 . ASP   B 103 ? 0.2463 0.2134 0.2058 -0.0183 0.0062  -0.0178 109 ASP   C OD2 
1895 N N   . CYS   B 104 ? 0.1754 0.1548 0.1724 -0.0052 -0.0019 -0.0171 110 CYS   C N   
1896 C CA  . CYS   B 104 ? 0.1697 0.1523 0.1762 -0.0025 -0.0021 -0.0158 110 CYS   C CA  
1897 C C   . CYS   B 104 ? 0.1725 0.1551 0.1801 -0.0011 -0.0056 -0.0137 110 CYS   C C   
1898 O O   . CYS   B 104 ? 0.1863 0.1671 0.1910 -0.0016 -0.0088 -0.0137 110 CYS   C O   
1899 C CB  . CYS   B 104 ? 0.1778 0.1620 0.1908 -0.0023 -0.0012 -0.0181 110 CYS   C CB  
1900 S SG  . CYS   B 104 ? 0.2050 0.1903 0.2237 -0.0029 0.0034  -0.0206 110 CYS   C SG  
1901 N N   . GLY   B 105 ? 0.1638 0.1479 0.1752 0.0002  -0.0049 -0.0119 111 GLY   C N   
1902 C CA  . GLY   B 105 ? 0.1684 0.1528 0.1826 0.0014  -0.0068 -0.0108 111 GLY   C CA  
1903 C C   . GLY   B 105 ? 0.1771 0.1593 0.1877 0.0016  -0.0074 -0.0093 111 GLY   C C   
1904 O O   . GLY   B 105 ? 0.1838 0.1663 0.1983 0.0026  -0.0078 -0.0089 111 GLY   C O   
1905 N N   . GLY   B 106 ? 0.1586 0.1386 0.1626 0.0003  -0.0071 -0.0089 112 GLY   C N   
1906 C CA  . GLY   B 106 ? 0.1650 0.1424 0.1655 0.0001  -0.0076 -0.0073 112 GLY   C CA  
1907 C C   . GLY   B 106 ? 0.1646 0.1437 0.1682 0.0006  -0.0050 -0.0070 112 GLY   C C   
1908 O O   . GLY   B 106 ? 0.1639 0.1451 0.1688 0.0001  -0.0028 -0.0073 112 GLY   C O   
1909 N N   . ILE   B 107 ? 0.1560 0.1336 0.1610 0.0013  -0.0055 -0.0065 113 ILE   C N   
1910 C CA  . ILE   B 107 ? 0.1575 0.1361 0.1641 0.0010  -0.0029 -0.0069 113 ILE   C CA  
1911 C C   . ILE   B 107 ? 0.1541 0.1314 0.1561 -0.0004 -0.0018 -0.0060 113 ILE   C C   
1912 O O   . ILE   B 107 ? 0.1745 0.1488 0.1729 -0.0007 -0.0029 -0.0051 113 ILE   C O   
1913 C CB  . ILE   B 107 ? 0.1924 0.1704 0.2043 0.0021  -0.0028 -0.0079 113 ILE   C CB  
1914 C CG1 . ILE   B 107 ? 0.2136 0.1943 0.2317 0.0029  -0.0025 -0.0093 113 ILE   C CG1 
1915 C CG2 . ILE   B 107 ? 0.2168 0.1940 0.2278 0.0009  0.0001  -0.0088 113 ILE   C CG2 
1916 C CD1 . ILE   B 107 ? 0.2487 0.2292 0.2747 0.0040  -0.0019 -0.0111 113 ILE   C CD1 
1917 N N   . LEU   B 108 ? 0.1452 0.1242 0.1472 -0.0017 0.0000  -0.0059 114 LEU   C N   
1918 C CA  . LEU   B 108 ? 0.1505 0.1287 0.1494 -0.0034 0.0008  -0.0052 114 LEU   C CA  
1919 C C   . LEU   B 108 ? 0.1618 0.1389 0.1605 -0.0042 0.0020  -0.0062 114 LEU   C C   
1920 O O   . LEU   B 108 ? 0.1622 0.1407 0.1623 -0.0049 0.0030  -0.0069 114 LEU   C O   
1921 C CB  . LEU   B 108 ? 0.1462 0.1271 0.1464 -0.0046 0.0010  -0.0042 114 LEU   C CB  
1922 C CG  . LEU   B 108 ? 0.1624 0.1431 0.1611 -0.0067 0.0011  -0.0032 114 LEU   C CG  
1923 C CD1 . LEU   B 108 ? 0.1716 0.1505 0.1680 -0.0070 0.0016  -0.0031 114 LEU   C CD1 
1924 C CD2 . LEU   B 108 ? 0.1688 0.1524 0.1715 -0.0078 0.0001  -0.0017 114 LEU   C CD2 
1925 N N   . ARG   B 109 ? 0.1635 0.1376 0.1603 -0.0046 0.0023  -0.0065 115 ARG   C N   
1926 C CA  . ARG   B 109 ? 0.1820 0.1544 0.1788 -0.0058 0.0042  -0.0085 115 ARG   C CA  
1927 C C   . ARG   B 109 ? 0.1937 0.1645 0.1862 -0.0082 0.0046  -0.0081 115 ARG   C C   
1928 O O   . ARG   B 109 ? 0.2084 0.1781 0.1996 -0.0081 0.0034  -0.0066 115 ARG   C O   
1929 C CB  . ARG   B 109 ? 0.2185 0.1880 0.2194 -0.0038 0.0041  -0.0098 115 ARG   C CB  
1930 C CG  . ARG   B 109 ? 0.3262 0.2965 0.3324 -0.0012 0.0025  -0.0098 115 ARG   C CG  
1931 C CD  . ARG   B 109 ? 0.4029 0.3699 0.4149 0.0005  0.0014  -0.0105 115 ARG   C CD  
1932 N NE  . ARG   B 109 ? 0.4560 0.4226 0.4722 -0.0001 0.0053  -0.0142 115 ARG   C NE  
1933 C CZ  . ARG   B 109 ? 0.4808 0.4495 0.5037 0.0004  0.0076  -0.0169 115 ARG   C CZ  
1934 N NH1 . ARG   B 109 ? 0.5005 0.4717 0.5279 0.0023  0.0054  -0.0159 115 ARG   C NH1 
1935 N NH2 . ARG   B 109 ? 0.4598 0.4280 0.4851 -0.0012 0.0124  -0.0209 115 ARG   C NH2 
1936 N N   . CYS   B 110 ? 0.1759 0.1461 0.1660 -0.0108 0.0064  -0.0098 116 CYS   C N   
1937 C CA  . CYS   B 110 ? 0.1854 0.1534 0.1712 -0.0136 0.0066  -0.0101 116 CYS   C CA  
1938 C C   . CYS   B 110 ? 0.2199 0.1844 0.2064 -0.0142 0.0096  -0.0138 116 CYS   C C   
1939 O O   . CYS   B 110 ? 0.2097 0.1738 0.2014 -0.0120 0.0112  -0.0158 116 CYS   C O   
1940 C CB  . CYS   B 110 ? 0.1887 0.1585 0.1700 -0.0174 0.0057  -0.0088 116 CYS   C CB  
1941 S SG  . CYS   B 110 ? 0.1926 0.1623 0.1702 -0.0204 0.0083  -0.0110 116 CYS   C SG  
1942 N N   . GLN   B 111 ? 0.2446 0.2064 0.2269 -0.0173 0.0104  -0.0151 117 GLN   C N   
1943 C CA  . GLN   B 111 ? 0.2630 0.2212 0.2465 -0.0182 0.0139  -0.0195 117 GLN   C CA  
1944 C C   . GLN   B 111 ? 0.2665 0.2253 0.2496 -0.0200 0.0180  -0.0233 117 GLN   C C   
1945 O O   . GLN   B 111 ? 0.2900 0.2462 0.2771 -0.0201 0.0220  -0.0279 117 GLN   C O   
1946 C CB  . GLN   B 111 ? 0.3074 0.2625 0.2854 -0.0220 0.0141  -0.0205 117 GLN   C CB  
1947 C CG  . GLN   B 111 ? 0.3651 0.3214 0.3344 -0.0273 0.0138  -0.0204 117 GLN   C CG  
1948 C CD  . GLN   B 111 ? 0.4744 0.4277 0.4384 -0.0313 0.0132  -0.0212 117 GLN   C CD  
1949 O OE1 . GLN   B 111 ? 0.4959 0.4507 0.4581 -0.0325 0.0093  -0.0176 117 GLN   C OE1 
1950 N NE2 . GLN   B 111 ? 0.4989 0.4480 0.4613 -0.0336 0.0171  -0.0264 117 GLN   C NE2 
1951 N N   . HIS   B 112 ? 0.2266 0.1885 0.2057 -0.0217 0.0174  -0.0215 118 HIS   C N   
1952 C CA  . HIS   B 112 ? 0.2311 0.1934 0.2081 -0.0246 0.0216  -0.0248 118 HIS   C CA  
1953 C C   . HIS   B 112 ? 0.2445 0.2096 0.2296 -0.0210 0.0226  -0.0251 118 HIS   C C   
1954 O O   . HIS   B 112 ? 0.2712 0.2367 0.2566 -0.0231 0.0270  -0.0284 118 HIS   C O   
1955 C CB  . HIS   B 112 ? 0.2430 0.2061 0.2094 -0.0300 0.0202  -0.0225 118 HIS   C CB  
1956 C CG  . HIS   B 112 ? 0.2569 0.2174 0.2152 -0.0343 0.0183  -0.0220 118 HIS   C CG  
1957 N ND1 . HIS   B 112 ? 0.2641 0.2262 0.2210 -0.0344 0.0126  -0.0169 118 HIS   C ND1 
1958 C CD2 . HIS   B 112 ? 0.2692 0.2258 0.2213 -0.0389 0.0216  -0.0262 118 HIS   C CD2 
1959 C CE1 . HIS   B 112 ? 0.2867 0.2461 0.2372 -0.0386 0.0119  -0.0177 118 HIS   C CE1 
1960 N NE2 . HIS   B 112 ? 0.2898 0.2456 0.2362 -0.0417 0.0171  -0.0233 118 HIS   C NE2 
1961 N N   . GLY   B 113 ? 0.2244 0.1915 0.2155 -0.0163 0.0187  -0.0218 119 GLY   C N   
1962 C CA  . GLY   B 113 ? 0.2096 0.1792 0.2081 -0.0131 0.0187  -0.0217 119 GLY   C CA  
1963 C C   . GLY   B 113 ? 0.1901 0.1626 0.1883 -0.0111 0.0143  -0.0172 119 GLY   C C   
1964 O O   . GLY   B 113 ? 0.1854 0.1577 0.1802 -0.0110 0.0112  -0.0143 119 GLY   C O   
1965 N N   . VAL   B 114 ? 0.1810 0.1561 0.1835 -0.0098 0.0144  -0.0171 120 VAL   C N   
1966 C CA  . VAL   B 114 ? 0.1735 0.1511 0.1766 -0.0081 0.0109  -0.0136 120 VAL   C CA  
1967 C C   . VAL   B 114 ? 0.1621 0.1408 0.1591 -0.0111 0.0097  -0.0110 120 VAL   C C   
1968 O O   . VAL   B 114 ? 0.1845 0.1633 0.1779 -0.0146 0.0116  -0.0114 120 VAL   C O   
1969 C CB  . VAL   B 114 ? 0.1832 0.1631 0.1933 -0.0062 0.0113  -0.0146 120 VAL   C CB  
1970 C CG1 . VAL   B 114 ? 0.1883 0.1704 0.1986 -0.0050 0.0081  -0.0117 120 VAL   C CG1 
1971 C CG2 . VAL   B 114 ? 0.1908 0.1697 0.2090 -0.0029 0.0107  -0.0163 120 VAL   C CG2 
1972 N N   . VAL   B 115 ? 0.1587 0.1381 0.1551 -0.0101 0.0064  -0.0081 121 VAL   C N   
1973 C CA  . VAL   B 115 ? 0.1613 0.1419 0.1552 -0.0124 0.0043  -0.0052 121 VAL   C CA  
1974 C C   . VAL   B 115 ? 0.1618 0.1448 0.1602 -0.0109 0.0028  -0.0036 121 VAL   C C   
1975 O O   . VAL   B 115 ? 0.1620 0.1457 0.1599 -0.0132 0.0016  -0.0015 121 VAL   C O   
1976 C CB  . VAL   B 115 ? 0.1635 0.1437 0.1565 -0.0123 0.0023  -0.0037 121 VAL   C CB  
1977 C CG1 . VAL   B 115 ? 0.1758 0.1577 0.1700 -0.0140 -0.0006 -0.0005 121 VAL   C CG1 
1978 C CG2 . VAL   B 115 ? 0.1692 0.1466 0.1574 -0.0144 0.0036  -0.0051 121 VAL   C CG2 
1979 N N   . GLY   B 116 ? 0.1515 0.1352 0.1542 -0.0076 0.0024  -0.0044 122 GLY   C N   
1980 C CA  . GLY   B 116 ? 0.1571 0.1428 0.1644 -0.0062 0.0013  -0.0037 122 GLY   C CA  
1981 C C   . GLY   B 116 ? 0.1470 0.1327 0.1566 -0.0034 0.0009  -0.0050 122 GLY   C C   
1982 O O   . GLY   B 116 ? 0.1560 0.1400 0.1641 -0.0024 0.0010  -0.0061 122 GLY   C O   
1983 N N   . ILE   B 117 ? 0.1510 0.1380 0.1642 -0.0025 0.0001  -0.0050 123 ILE   C N   
1984 C CA  . ILE   B 117 ? 0.1516 0.1382 0.1654 -0.0008 -0.0005 -0.0065 123 ILE   C CA  
1985 C C   . ILE   B 117 ? 0.1442 0.1313 0.1592 -0.0009 -0.0003 -0.0068 123 ILE   C C   
1986 O O   . ILE   B 117 ? 0.1378 0.1264 0.1571 -0.0014 -0.0002 -0.0060 123 ILE   C O   
1987 C CB  . ILE   B 117 ? 0.1623 0.1498 0.1798 0.0001  -0.0011 -0.0076 123 ILE   C CB  
1988 C CG1 . ILE   B 117 ? 0.1661 0.1553 0.1877 -0.0006 -0.0008 -0.0068 123 ILE   C CG1 
1989 C CG2 . ILE   B 117 ? 0.1846 0.1716 0.2029 0.0006  -0.0008 -0.0083 123 ILE   C CG2 
1990 C CD1 . ILE   B 117 ? 0.1872 0.1775 0.2134 0.0002  -0.0013 -0.0082 123 ILE   C CD1 
1991 N N   . VAL   B 118 ? 0.1337 0.1194 0.1453 -0.0008 -0.0002 -0.0082 124 VAL   C N   
1992 C CA  . VAL   B 118 ? 0.1355 0.1217 0.1485 -0.0014 0.0014  -0.0097 124 VAL   C CA  
1993 C C   . VAL   B 118 ? 0.1403 0.1279 0.1594 -0.0009 0.0014  -0.0110 124 VAL   C C   
1994 O O   . VAL   B 118 ? 0.1490 0.1365 0.1682 -0.0003 0.0000  -0.0114 124 VAL   C O   
1995 C CB  . VAL   B 118 ? 0.1534 0.1369 0.1592 -0.0024 0.0016  -0.0112 124 VAL   C CB  
1996 C CG1 . VAL   B 118 ? 0.1712 0.1549 0.1779 -0.0038 0.0045  -0.0141 124 VAL   C CG1 
1997 C CG2 . VAL   B 118 ? 0.1631 0.1445 0.1632 -0.0032 0.0015  -0.0097 124 VAL   C CG2 
1998 N N   . SER   B 119 ? 0.1386 0.1277 0.1642 -0.0011 0.0028  -0.0115 125 SER   C N   
1999 C CA  . SER   B 119 ? 0.1432 0.1333 0.1763 -0.0006 0.0028  -0.0125 125 SER   C CA  
2000 C C   . SER   B 119 ? 0.1560 0.1465 0.1950 -0.0011 0.0057  -0.0157 125 SER   C C   
2001 O O   . SER   B 119 ? 0.1560 0.1464 0.1992 -0.0009 0.0065  -0.0183 125 SER   C O   
2002 C CB  . SER   B 119 ? 0.1556 0.1469 0.1941 -0.0005 0.0007  -0.0090 125 SER   C CB  
2003 O OG  . SER   B 119 ? 0.1654 0.1572 0.2122 -0.0002 0.0002  -0.0093 125 SER   C OG  
2004 N N   . THR   B 120 ? 0.1463 0.1375 0.1867 -0.0017 0.0076  -0.0160 126 THR   C N   
2005 C CA  . THR   B 120 ? 0.1700 0.1618 0.2178 -0.0024 0.0116  -0.0199 126 THR   C CA  
2006 C C   . THR   B 120 ? 0.1758 0.1670 0.2174 -0.0042 0.0150  -0.0219 126 THR   C C   
2007 O O   . THR   B 120 ? 0.1634 0.1536 0.1967 -0.0047 0.0136  -0.0194 126 THR   C O   
2008 C CB  . THR   B 120 ? 0.1804 0.1746 0.2432 -0.0014 0.0106  -0.0182 126 THR   C CB  
2009 O OG1 . THR   B 120 ? 0.1943 0.1898 0.2576 -0.0018 0.0095  -0.0153 126 THR   C OG1 
2010 C CG2 . THR   B 120 ? 0.1701 0.1645 0.2382 -0.0003 0.0066  -0.0149 126 THR   C CG2 
2011 N N   . GLY   B 121 ? 0.1821 0.1734 0.2277 -0.0057 0.0200  -0.0267 127 GLY   C N   
2012 C CA  . GLY   B 121 ? 0.2014 0.1922 0.2420 -0.0082 0.0243  -0.0288 127 GLY   C CA  
2013 C C   . GLY   B 121 ? 0.2155 0.2071 0.2644 -0.0099 0.0309  -0.0349 127 GLY   C C   
2014 O O   . GLY   B 121 ? 0.2114 0.2030 0.2669 -0.0094 0.0324  -0.0383 127 GLY   C O   
2015 N N   . GLY   B 122 ? 0.2214 0.2135 0.2701 -0.0121 0.0354  -0.0367 128 GLY   C N   
2016 C CA  . GLY   B 122 ? 0.2403 0.2335 0.2974 -0.0144 0.0433  -0.0435 128 GLY   C CA  
2017 C C   . GLY   B 122 ? 0.2383 0.2342 0.3036 -0.0153 0.0465  -0.0435 128 GLY   C C   
2018 O O   . GLY   B 122 ? 0.2321 0.2301 0.3021 -0.0132 0.0416  -0.0382 128 GLY   C O   
2019 N N   . ASN   B 123 ? 0.2506 0.2465 0.3173 -0.0189 0.0550  -0.0499 129 ASN   C N   
2020 C CA  . ASN   B 123 ? 0.2582 0.2571 0.3341 -0.0204 0.0595  -0.0511 129 ASN   C CA  
2021 C C   . ASN   B 123 ? 0.2548 0.2529 0.3198 -0.0210 0.0554  -0.0451 129 ASN   C C   
2022 O O   . ASN   B 123 ? 0.2600 0.2614 0.3364 -0.0203 0.0551  -0.0433 129 ASN   C O   
2023 C CB  . ASN   B 123 ? 0.2822 0.2863 0.3842 -0.0169 0.0584  -0.0510 129 ASN   C CB  
2024 C CG  . ASN   B 123 ? 0.3680 0.3730 0.4843 -0.0167 0.0641  -0.0580 129 ASN   C CG  
2025 O OD1 . ASN   B 123 ? 0.4029 0.4060 0.5134 -0.0206 0.0726  -0.0654 129 ASN   C OD1 
2026 N ND2 . ASN   B 123 ? 0.3891 0.3969 0.5251 -0.0126 0.0595  -0.0559 129 ASN   C ND2 
2027 N N   . GLY   B 124 ? 0.2464 0.2398 0.2906 -0.0224 0.0523  -0.0423 130 GLY   C N   
2028 C CA  . GLY   B 124 ? 0.2297 0.2215 0.2639 -0.0230 0.0487  -0.0370 130 GLY   C CA  
2029 C C   . GLY   B 124 ? 0.2026 0.1963 0.2424 -0.0188 0.0406  -0.0308 130 GLY   C C   
2030 O O   . GLY   B 124 ? 0.1992 0.1925 0.2354 -0.0191 0.0381  -0.0271 130 GLY   C O   
2031 N N   . LEU   B 125 ? 0.1820 0.1772 0.2296 -0.0153 0.0366  -0.0297 131 LEU   C N   
2032 C CA  . LEU   B 125 ? 0.1834 0.1798 0.2344 -0.0122 0.0293  -0.0241 131 LEU   C CA  
2033 C C   . LEU   B 125 ? 0.1914 0.1851 0.2330 -0.0106 0.0253  -0.0225 131 LEU   C C   
2034 O O   . LEU   B 125 ? 0.2135 0.2064 0.2546 -0.0107 0.0272  -0.0258 131 LEU   C O   
2035 C CB  . LEU   B 125 ? 0.2009 0.2016 0.2718 -0.0102 0.0279  -0.0237 131 LEU   C CB  
2036 C CG  . LEU   B 125 ? 0.2279 0.2320 0.3115 -0.0116 0.0313  -0.0252 131 LEU   C CG  
2037 C CD1 . LEU   B 125 ? 0.2507 0.2587 0.3561 -0.0102 0.0326  -0.0276 131 LEU   C CD1 
2038 C CD2 . LEU   B 125 ? 0.2337 0.2385 0.3166 -0.0116 0.0260  -0.0199 131 LEU   C CD2 
2039 N N   . VAL   B 126 ? 0.1631 0.1556 0.1982 -0.0095 0.0201  -0.0180 132 VAL   C N   
2040 C CA  . VAL   B 126 ? 0.1678 0.1585 0.1962 -0.0079 0.0165  -0.0165 132 VAL   C CA  
2041 C C   . VAL   B 126 ? 0.1622 0.1548 0.1975 -0.0060 0.0119  -0.0129 132 VAL   C C   
2042 O O   . VAL   B 126 ? 0.1599 0.1534 0.1975 -0.0063 0.0100  -0.0101 132 VAL   C O   
2043 C CB  . VAL   B 126 ? 0.1793 0.1662 0.1935 -0.0088 0.0150  -0.0149 132 VAL   C CB  
2044 C CG1 . VAL   B 126 ? 0.2167 0.2031 0.2285 -0.0094 0.0138  -0.0122 132 VAL   C CG1 
2045 C CG2 . VAL   B 126 ? 0.1842 0.1698 0.1946 -0.0069 0.0111  -0.0135 132 VAL   C CG2 
2046 N N   . GLY   B 127 ? 0.1588 0.1513 0.1960 -0.0045 0.0102  -0.0128 133 GLY   C N   
2047 C CA  . GLY   B 127 ? 0.1575 0.1512 0.1999 -0.0036 0.0061  -0.0092 133 GLY   C CA  
2048 C C   . GLY   B 127 ? 0.1522 0.1442 0.1862 -0.0031 0.0037  -0.0076 133 GLY   C C   
2049 O O   . GLY   B 127 ? 0.1546 0.1453 0.1842 -0.0026 0.0045  -0.0095 133 GLY   C O   
2050 N N   . PHE   B 128 ? 0.1374 0.1293 0.1693 -0.0036 0.0010  -0.0043 134 PHE   C N   
2051 C CA  . PHE   B 128 ? 0.1405 0.1310 0.1657 -0.0036 -0.0002 -0.0033 134 PHE   C CA  
2052 C C   . PHE   B 128 ? 0.1476 0.1386 0.1761 -0.0044 -0.0026 -0.0007 134 PHE   C C   
2053 O O   . PHE   B 128 ? 0.1525 0.1441 0.1841 -0.0059 -0.0047 0.0020  134 PHE   C O   
2054 C CB  . PHE   B 128 ? 0.1522 0.1411 0.1702 -0.0046 -0.0003 -0.0025 134 PHE   C CB  
2055 C CG  . PHE   B 128 ? 0.1552 0.1429 0.1696 -0.0045 0.0015  -0.0040 134 PHE   C CG  
2056 C CD1 . PHE   B 128 ? 0.1503 0.1359 0.1594 -0.0038 0.0020  -0.0054 134 PHE   C CD1 
2057 C CD2 . PHE   B 128 ? 0.1656 0.1540 0.1824 -0.0057 0.0022  -0.0037 134 PHE   C CD2 
2058 C CE1 . PHE   B 128 ? 0.1649 0.1485 0.1694 -0.0045 0.0032  -0.0061 134 PHE   C CE1 
2059 C CE2 . PHE   B 128 ? 0.1837 0.1706 0.1963 -0.0063 0.0042  -0.0050 134 PHE   C CE2 
2060 C CZ  . PHE   B 128 ? 0.1828 0.1670 0.1886 -0.0059 0.0047  -0.0060 134 PHE   C CZ  
2061 N N   . ALA   B 129 ? 0.1395 0.1301 0.1670 -0.0038 -0.0025 -0.0012 135 ALA   C N   
2062 C CA  . ALA   B 129 ? 0.1295 0.1201 0.1582 -0.0054 -0.0043 0.0014  135 ALA   C CA  
2063 C C   . ALA   B 129 ? 0.1324 0.1217 0.1531 -0.0076 -0.0041 0.0024  135 ALA   C C   
2064 O O   . ALA   B 129 ? 0.1457 0.1344 0.1623 -0.0069 -0.0021 0.0002  135 ALA   C O   
2065 C CB  . ALA   B 129 ? 0.1328 0.1235 0.1634 -0.0043 -0.0035 -0.0001 135 ALA   C CB  
2066 N N   . ASP   B 130 ? 0.1377 0.1265 0.1568 -0.0105 -0.0064 0.0056  136 ASP   C N   
2067 C CA  . ASP   B 130 ? 0.1517 0.1387 0.1619 -0.0136 -0.0058 0.0061  136 ASP   C CA  
2068 C C   . ASP   B 130 ? 0.1631 0.1493 0.1697 -0.0153 -0.0037 0.0054  136 ASP   C C   
2069 O O   . ASP   B 130 ? 0.1668 0.1533 0.1769 -0.0158 -0.0048 0.0071  136 ASP   C O   
2070 C CB  . ASP   B 130 ? 0.1704 0.1566 0.1790 -0.0173 -0.0097 0.0102  136 ASP   C CB  
2071 C CG  . ASP   B 130 ? 0.2459 0.2298 0.2440 -0.0215 -0.0091 0.0102  136 ASP   C CG  
2072 O OD1 . ASP   B 130 ? 0.2357 0.2190 0.2303 -0.0205 -0.0061 0.0070  136 ASP   C OD1 
2073 O OD2 . ASP   B 130 ? 0.2812 0.2634 0.2741 -0.0260 -0.0114 0.0134  136 ASP   C OD2 
2074 N N   . VAL   B 131 ? 0.1541 0.1392 0.1548 -0.0163 -0.0005 0.0027  137 VAL   C N   
2075 C CA  . VAL   B 131 ? 0.1648 0.1493 0.1627 -0.0188 0.0025  0.0015  137 VAL   C CA  
2076 C C   . VAL   B 131 ? 0.1826 0.1646 0.1707 -0.0240 0.0043  0.0013  137 VAL   C C   
2077 O O   . VAL   B 131 ? 0.1896 0.1709 0.1743 -0.0270 0.0079  -0.0004 137 VAL   C O   
2078 C CB  . VAL   B 131 ? 0.1735 0.1592 0.1761 -0.0155 0.0059  -0.0026 137 VAL   C CB  
2079 C CG1 . VAL   B 131 ? 0.1717 0.1593 0.1821 -0.0115 0.0039  -0.0025 137 VAL   C CG1 
2080 C CG2 . VAL   B 131 ? 0.1751 0.1599 0.1765 -0.0140 0.0076  -0.0055 137 VAL   C CG2 
2081 N N   . ARG   B 132 ? 0.1743 0.1550 0.1578 -0.0257 0.0022  0.0025  138 ARG   C N   
2082 C CA  . ARG   B 132 ? 0.1782 0.1561 0.1514 -0.0310 0.0039  0.0015  138 ARG   C CA  
2083 C C   . ARG   B 132 ? 0.2023 0.1780 0.1670 -0.0375 0.0029  0.0045  138 ARG   C C   
2084 O O   . ARG   B 132 ? 0.2220 0.1950 0.1768 -0.0428 0.0063  0.0023  138 ARG   C O   
2085 C CB  . ARG   B 132 ? 0.1812 0.1582 0.1521 -0.0314 0.0010  0.0025  138 ARG   C CB  
2086 C CG  . ARG   B 132 ? 0.1921 0.1700 0.1684 -0.0263 0.0028  -0.0007 138 ARG   C CG  
2087 C CD  . ARG   B 132 ? 0.1733 0.1506 0.1482 -0.0270 -0.0001 0.0006  138 ARG   C CD  
2088 N NE  . ARG   B 132 ? 0.1807 0.1601 0.1615 -0.0258 -0.0049 0.0048  138 ARG   C NE  
2089 C CZ  . ARG   B 132 ? 0.1976 0.1775 0.1806 -0.0258 -0.0077 0.0063  138 ARG   C CZ  
2090 N NH1 . ARG   B 132 ? 0.1929 0.1710 0.1711 -0.0274 -0.0068 0.0046  138 ARG   C NH1 
2091 N NH2 . ARG   B 132 ? 0.1967 0.1790 0.1880 -0.0243 -0.0113 0.0093  138 ARG   C NH2 
2092 N N   . ASP   B 133 ? 0.1959 0.1722 0.1639 -0.0378 -0.0018 0.0095  139 ASP   C N   
2093 C CA  . ASP   B 133 ? 0.2179 0.1914 0.1775 -0.0446 -0.0038 0.0135  139 ASP   C CA  
2094 C C   . ASP   B 133 ? 0.2285 0.2019 0.1870 -0.0462 0.0012  0.0116  139 ASP   C C   
2095 O O   . ASP   B 133 ? 0.2538 0.2242 0.2028 -0.0531 0.0009  0.0144  139 ASP   C O   
2096 C CB  . ASP   B 133 ? 0.2235 0.1971 0.1886 -0.0445 -0.0117 0.0203  139 ASP   C CB  
2097 C CG  . ASP   B 133 ? 0.2593 0.2358 0.2378 -0.0386 -0.0120 0.0205  139 ASP   C CG  
2098 O OD1 . ASP   B 133 ? 0.2405 0.2197 0.2261 -0.0328 -0.0089 0.0161  139 ASP   C OD1 
2099 O OD2 . ASP   B 133 ? 0.2933 0.2688 0.2747 -0.0403 -0.0158 0.0251  139 ASP   C OD2 
2100 N N   . LEU   B 134 ? 0.2103 0.1867 0.1781 -0.0406 0.0056  0.0071  140 LEU   C N   
2101 C CA  . LEU   B 134 ? 0.2156 0.1927 0.1851 -0.0417 0.0103  0.0050  140 LEU   C CA  
2102 C C   . LEU   B 134 ? 0.2312 0.2071 0.1941 -0.0455 0.0177  -0.0005 140 LEU   C C   
2103 O O   . LEU   B 134 ? 0.2329 0.2109 0.2032 -0.0416 0.0224  -0.0059 140 LEU   C O   
2104 C CB  . LEU   B 134 ? 0.2120 0.1928 0.1953 -0.0344 0.0106  0.0030  140 LEU   C CB  
2105 C CG  . LEU   B 134 ? 0.2267 0.2087 0.2176 -0.0306 0.0044  0.0071  140 LEU   C CG  
2106 C CD1 . LEU   B 134 ? 0.2263 0.2114 0.2283 -0.0241 0.0052  0.0040  140 LEU   C CD1 
2107 C CD2 . LEU   B 134 ? 0.2445 0.2247 0.2342 -0.0344 0.0010  0.0124  140 LEU   C CD2 
2108 N N   . LEU   B 135 ? 0.2378 0.2099 0.1867 -0.0537 0.0188  0.0008  141 LEU   C N   
2109 C CA  . LEU   B 135 ? 0.2596 0.2298 0.2008 -0.0584 0.0266  -0.0053 141 LEU   C CA  
2110 C C   . LEU   B 135 ? 0.2723 0.2444 0.2192 -0.0586 0.0345  -0.0103 141 LEU   C C   
2111 O O   . LEU   B 135 ? 0.2964 0.2687 0.2451 -0.0589 0.0418  -0.0172 141 LEU   C O   
2112 C CB  . LEU   B 135 ? 0.2702 0.2353 0.1929 -0.0683 0.0258  -0.0028 141 LEU   C CB  
2113 C CG  . LEU   B 135 ? 0.2818 0.2449 0.1990 -0.0693 0.0168  0.0032  141 LEU   C CG  
2114 C CD1 . LEU   B 135 ? 0.3034 0.2610 0.2010 -0.0803 0.0160  0.0053  141 LEU   C CD1 
2115 C CD2 . LEU   B 135 ? 0.2721 0.2373 0.1967 -0.0629 0.0157  0.0004  141 LEU   C CD2 
2116 N N   . TRP   B 136 ? 0.2678 0.2411 0.2188 -0.0586 0.0331  -0.0071 142 TRP   C N   
2117 C CA  . TRP   B 136 ? 0.2700 0.2455 0.2277 -0.0592 0.0403  -0.0114 142 TRP   C CA  
2118 C C   . TRP   B 136 ? 0.2777 0.2577 0.2526 -0.0508 0.0428  -0.0168 142 TRP   C C   
2119 O O   . TRP   B 136 ? 0.2815 0.2637 0.2640 -0.0511 0.0495  -0.0218 142 TRP   C O   
2120 C CB  . TRP   B 136 ? 0.2712 0.2465 0.2296 -0.0611 0.0374  -0.0061 142 TRP   C CB  
2121 C CG  . TRP   B 136 ? 0.2604 0.2376 0.2281 -0.0544 0.0289  -0.0010 142 TRP   C CG  
2122 C CD1 . TRP   B 136 ? 0.2709 0.2458 0.2343 -0.0549 0.0208  0.0058  142 TRP   C CD1 
2123 C CD2 . TRP   B 136 ? 0.2539 0.2353 0.2374 -0.0465 0.0279  -0.0028 142 TRP   C CD2 
2124 N NE1 . TRP   B 136 ? 0.2710 0.2487 0.2472 -0.0478 0.0160  0.0076  142 TRP   C NE1 
2125 C CE2 . TRP   B 136 ? 0.2618 0.2432 0.2490 -0.0430 0.0202  0.0025  142 TRP   C CE2 
2126 C CE3 . TRP   B 136 ? 0.2618 0.2471 0.2573 -0.0427 0.0328  -0.0083 142 TRP   C CE3 
2127 C CZ2 . TRP   B 136 ? 0.2689 0.2535 0.2690 -0.0361 0.0177  0.0018  142 TRP   C CZ2 
2128 C CZ3 . TRP   B 136 ? 0.2707 0.2591 0.2788 -0.0360 0.0291  -0.0081 142 TRP   C CZ3 
2129 C CH2 . TRP   B 136 ? 0.2682 0.2560 0.2774 -0.0331 0.0219  -0.0033 142 TRP   C CH2 
2130 N N   . LEU   B 137 ? 0.2724 0.2538 0.2537 -0.0438 0.0374  -0.0158 143 LEU   C N   
2131 C CA  . LEU   B 137 ? 0.2709 0.2557 0.2671 -0.0367 0.0385  -0.0200 143 LEU   C CA  
2132 C C   . LEU   B 137 ? 0.3203 0.3049 0.3192 -0.0379 0.0462  -0.0271 143 LEU   C C   
2133 O O   . LEU   B 137 ? 0.3180 0.3056 0.3310 -0.0337 0.0486  -0.0311 143 LEU   C O   
2134 C CB  . LEU   B 137 ? 0.2457 0.2309 0.2449 -0.0306 0.0317  -0.0174 143 LEU   C CB  
2135 C CG  . LEU   B 137 ? 0.2327 0.2193 0.2356 -0.0273 0.0251  -0.0124 143 LEU   C CG  
2136 C CD1 . LEU   B 137 ? 0.2293 0.2158 0.2333 -0.0227 0.0201  -0.0108 143 LEU   C CD1 
2137 C CD2 . LEU   B 137 ? 0.2311 0.2209 0.2461 -0.0238 0.0257  -0.0140 143 LEU   C CD2 
2138 N N   . ASP   B 138 ? 0.3565 0.3374 0.3427 -0.0437 0.0495  -0.0288 144 ASP   C N   
2139 C CA  . ASP   B 138 ? 0.4129 0.3927 0.4002 -0.0458 0.0573  -0.0361 144 ASP   C CA  
2140 C C   . ASP   B 138 ? 0.4607 0.4406 0.4477 -0.0519 0.0670  -0.0416 144 ASP   C C   
2141 O O   . ASP   B 138 ? 0.4728 0.4515 0.4612 -0.0542 0.0746  -0.0486 144 ASP   C O   
2142 C CB  . ASP   B 138 ? 0.4575 0.4327 0.4295 -0.0506 0.0568  -0.0359 144 ASP   C CB  
2143 C CG  . ASP   B 138 ? 0.5327 0.5074 0.5047 -0.0457 0.0491  -0.0322 144 ASP   C CG  
2144 O OD1 . ASP   B 138 ? 0.5561 0.5333 0.5410 -0.0382 0.0460  -0.0320 144 ASP   C OD1 
2145 O OD2 . ASP   B 138 ? 0.5838 0.5553 0.5426 -0.0499 0.0460  -0.0293 144 ASP   C OD2 
2146 N N   . GLU   B 139 ? 0.4829 0.4636 0.4670 -0.0554 0.0675  -0.0387 145 GLU   C N   
2147 C CA  . GLU   B 139 ? 0.5252 0.5060 0.5087 -0.0619 0.0775  -0.0439 145 GLU   C CA  
2148 C C   . GLU   B 139 ? 0.5459 0.5311 0.5432 -0.0590 0.0778  -0.0432 145 GLU   C C   
2149 O O   . GLU   B 139 ? 0.5647 0.5514 0.5670 -0.0629 0.0867  -0.0484 145 GLU   C O   
2150 C CB  . GLU   B 139 ? 0.5776 0.5533 0.5384 -0.0728 0.0796  -0.0416 145 GLU   C CB  
2151 C CG  . GLU   B 139 ? 0.6623 0.6366 0.6144 -0.0743 0.0707  -0.0319 145 GLU   C CG  
2152 C CD  . GLU   B 139 ? 0.7991 0.7677 0.7301 -0.0812 0.0659  -0.0267 145 GLU   C CD  
2153 O OE1 . GLU   B 139 ? 0.8366 0.8021 0.7553 -0.0882 0.0637  -0.0211 145 GLU   C OE1 
2154 O OE2 . GLU   B 139 ? 0.8389 0.8059 0.7661 -0.0799 0.0639  -0.0279 145 GLU   C OE2 
2155 N N1  . A1B4N C .   ? 0.2720 0.2556 0.3228 0.0025  0.0536  0.0298  201 A1B4N A N1  
2156 N N3  . A1B4N C .   ? 0.2141 0.2068 0.2963 -0.0098 0.0318  0.0032  201 A1B4N A N3  
2157 C C4  . A1B4N C .   ? 0.2748 0.2626 0.3121 0.0020  0.0382  0.0220  201 A1B4N A C4  
2158 C C5  . A1B4N C .   ? 0.2748 0.2611 0.3139 0.0036  0.0457  0.0262  201 A1B4N A C5  
2159 C C6  . A1B4N C .   ? 0.2564 0.2344 0.3196 -0.0003 0.0520  0.0309  201 A1B4N A C6  
2160 C C7  . A1B4N C .   ? 0.2609 0.2382 0.3207 -0.0002 0.0457  0.0297  201 A1B4N A C7  
2161 C C8  . A1B4N C .   ? 0.2458 0.2259 0.3194 -0.0047 0.0439  0.0230  201 A1B4N A C8  
2162 C C10 . A1B4N C .   ? 0.2276 0.2170 0.3160 -0.0101 0.0381  0.0082  201 A1B4N A C10 
2163 O O3  . A1B4N C .   ? 0.2193 0.2079 0.3222 -0.0124 0.0421  0.0064  201 A1B4N A O3  
2164 C C9  . A1B4N C .   ? 0.2306 0.2169 0.3072 -0.0070 0.0406  0.0157  201 A1B4N A C9  
2165 C C11 . A1B4N C .   ? 0.2300 0.2179 0.3135 -0.0077 0.0464  0.0162  201 A1B4N A C11 
2166 N N2  . A1B4N C .   ? 0.2422 0.2267 0.3137 -0.0038 0.0500  0.0235  201 A1B4N A N2  
2167 S S   . A1B4N C .   ? 0.2480 0.2349 0.3201 -0.0031 0.0546  0.0240  201 A1B4N A S   
2168 O O1  . A1B4N C .   ? 0.2382 0.2321 0.3156 -0.0055 0.0495  0.0159  201 A1B4N A O1  
2169 O O2  . A1B4N C .   ? 0.2725 0.2559 0.3566 -0.0037 0.0645  0.0285  201 A1B4N A O2  
2170 C C1  . A1B4N C .   ? 0.2829 0.2700 0.3128 0.0064  0.0465  0.0268  201 A1B4N A C1  
2171 O O   . A1B4N C .   ? 0.2994 0.2841 0.3303 0.0086  0.0551  0.0319  201 A1B4N A O   
2172 C C   . A1B4N C .   ? 0.3025 0.2886 0.3261 0.0113  0.0569  0.0320  201 A1B4N A C   
2173 C C3  . A1B4N C .   ? 0.2781 0.2679 0.3058 0.0029  0.0321  0.0188  201 A1B4N A C3  
2174 C C2  . A1B4N C .   ? 0.2812 0.2714 0.3011 0.0053  0.0330  0.0192  201 A1B4N A C2  
2175 N N   . A1B4N C .   ? 0.2781 0.2672 0.2985 0.0072  0.0399  0.0231  201 A1B4N A N   
2181 N N1  . A1B4N F .   ? 0.2208 0.2064 0.2575 -0.0092 0.0245  -0.0390 201 A1B4N C N1  
2182 N N3  . A1B4N F .   ? 0.1705 0.1623 0.2362 0.0007  0.0036  -0.0160 201 A1B4N C N3  
2183 C C4  . A1B4N F .   ? 0.2298 0.2155 0.2559 -0.0066 0.0156  -0.0293 201 A1B4N C C4  
2184 C C5  . A1B4N F .   ? 0.2264 0.2114 0.2531 -0.0091 0.0212  -0.0344 201 A1B4N C C5  
2185 C C6  . A1B4N F .   ? 0.2101 0.1962 0.2605 -0.0053 0.0179  -0.0376 201 A1B4N C C6  
2186 C C7  . A1B4N F .   ? 0.2001 0.1863 0.2481 -0.0039 0.0125  -0.0337 201 A1B4N C C7  
2187 C C8  . A1B4N F .   ? 0.1767 0.1649 0.2361 -0.0015 0.0099  -0.0292 201 A1B4N C C8  
2188 C C10 . A1B4N F .   ? 0.1700 0.1611 0.2411 0.0006  0.0064  -0.0207 201 A1B4N C C10 
2189 O O3  . A1B4N F .   ? 0.1627 0.1539 0.2461 0.0012  0.0064  -0.0213 201 A1B4N C O3  
2190 C C9  . A1B4N F .   ? 0.1647 0.1546 0.2261 -0.0007 0.0096  -0.0256 201 A1B4N C C9  
2191 C C11 . A1B4N F .   ? 0.1726 0.1629 0.2394 -0.0015 0.0142  -0.0293 201 A1B4N C C11 
2192 N N2  . A1B4N F .   ? 0.2021 0.1905 0.2581 -0.0040 0.0180  -0.0342 201 A1B4N C N2  
2193 S S   . A1B4N F .   ? 0.2031 0.1918 0.2585 -0.0059 0.0235  -0.0375 201 A1B4N C S   
2194 O O1  . A1B4N F .   ? 0.1803 0.1713 0.2415 -0.0043 0.0216  -0.0330 201 A1B4N C O1  
2195 O O2  . A1B4N F .   ? 0.2253 0.2137 0.2899 -0.0069 0.0287  -0.0439 201 A1B4N C O2  
2196 C C1  . A1B4N F .   ? 0.2369 0.2203 0.2544 -0.0119 0.0240  -0.0352 201 A1B4N C C1  
2197 O O   . A1B4N F .   ? 0.2490 0.2317 0.2669 -0.0149 0.0305  -0.0409 201 A1B4N C O   
2198 C C   . A1B4N F .   ? 0.2580 0.2394 0.2679 -0.0182 0.0342  -0.0417 201 A1B4N C C   
2199 C C3  . A1B4N F .   ? 0.2401 0.2250 0.2580 -0.0066 0.0132  -0.0255 201 A1B4N C C3  
2200 C C2  . A1B4N F .   ? 0.2341 0.2173 0.2444 -0.0090 0.0157  -0.0263 201 A1B4N C C2  
2201 N N   . A1B4N F .   ? 0.2287 0.2112 0.2381 -0.0118 0.0211  -0.0309 201 A1B4N C N   
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